PMID- 16174741
OWN - NLM
STAT- MEDLINE
DCOM- 20051108
LR  - 20181113
IS  - 0027-8424 (Print)
IS  - 0027-8424 (Linking)
VI  - 102
IP  - 38
DP  - 2005 Sep 20
TI  - Distinct functional units of the Golgi complex in Drosophila cells.
PG  - 13467-72
AB  - A striking variety of glycosylation occur in the Golgi complex in a
      protein-specific manner, but how this diversity and specificity are achieved
      remains unclear. Here we show that stacked fragments (units) of the Golgi complex
      dispersed in Drosophila imaginal disk cells are functionally diverse. The
      UDP-sugar transporter FRINGE-CONNECTION (FRC) is localized to a subset of the
      Golgi units distinct from those harboring SULFATELESS (SFL), which modifies
      glucosaminoglycans (GAGs), and from those harboring the protease RHOMBOID (RHO), 
      which processes the glycoprotein SPITZ (SPI). Whereas the glycosylation and
      function of NOTCH are affected in imaginal disks of frc mutants, those of SPI and
      of GAG core proteins are not, even though FRC transports a broad range of
      glycosylation substrates, suggesting that Golgi units containing FRC and those
      containing SFL or RHO are functionally separable. Distinct Golgi units containing
      FRC and RHO in embryos could also be separated biochemically by immunoisolation
      techniques. We also show that Tn-antigen glycan is localized only in a subset of 
      the Golgi units distributed basally in a polarized cell. We propose that the
      different localizations among distinct Golgi units of molecules involved in
      glycosylation underlie the diversity of glycan modification.
FAU - Yano, Hiroyuki
AU  - Yano H
AD  - Mitsubishi-Kagaku Institute of Life Sciences, 11 Minamiooya, Machida, Tokyo
      194-8511, Japan.
FAU - Yamamoto-Hino, Miki
AU  - Yamamoto-Hino M
FAU - Abe, Masato
AU  - Abe M
FAU - Kuwahara, Reiko
AU  - Kuwahara R
FAU - Haraguchi, Shuka
AU  - Haraguchi S
FAU - Kusaka, Isamu
AU  - Kusaka I
FAU - Awano, Wakae
AU  - Awano W
FAU - Kinoshita-Toyoda, Akiko
AU  - Kinoshita-Toyoda A
FAU - Toyoda, Hidenao
AU  - Toyoda H
FAU - Goto, Satoshi
AU  - Goto S
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20050908
PL  - United States
TA  - Proc Natl Acad Sci U S A
JT  - Proceedings of the National Academy of Sciences of the United States of America
JID - 7505876
RN  - 0 (Drosophila Proteins)
RN  - 0 (Polysaccharides)
SB  - IM
MH  - Animals
MH  - Drosophila/*embryology
MH  - Drosophila Proteins/genetics/*metabolism
MH  - Glycosylation
MH  - Golgi Apparatus/*metabolism
MH  - Polysaccharides/*metabolism
MH  - Protein Processing, Post-Translational/*physiology
MH  - Protein Transport/physiology
PMC - PMC1224666
EDAT- 2005/09/22 09:00
MHDA- 2005/11/09 09:00
CRDT- 2005/09/22 09:00
PHST- 2005/09/22 09:00 [pubmed]
PHST- 2005/11/09 09:00 [medline]
PHST- 2005/09/22 09:00 [entrez]
AID - 0506681102 [pii]
AID - 10.1073/pnas.0506681102 [doi]
PST - ppublish
SO  - Proc Natl Acad Sci U S A. 2005 Sep 20;102(38):13467-72. doi:
      10.1073/pnas.0506681102. Epub 2005 Sep 8.

PMID- 2481651
OWN - NLM
STAT- MEDLINE
DCOM- 19900216
LR  - 20160303
IS  - 0020-7136 (Print)
IS  - 0020-7136 (Linking)
VI  - 44
IP  - 6
DP  - 1989 Dec 15
TI  - Expression of TAG-72 in normal colon, transitional mucosa, and colon cancer.
PG  - 985-9
AB  - Monoclonal antibody (MAb) B72.3 detects an epitope carried by
      high-molecular-weight mucins (tumor-associated glycoprotein, TAG-72) recently
      identified as sialyl-Tn. B72.3 MAb has a restricted pattern of reactivity with
      normal tissues but it reacts with a high proportion of epithelial cancers. To
      determine the possible relationship between neoplastic transformation and
      reactivity with B72.3 MAb, we have analyzed samples of normal colon, colon cancer
      and transitional mucosa (mucosa adjacent to colorectal cancer) or reactive mucosa
      (mucosa adjacent to squamous carcinoma of the anal canal, or mucosa overlying
      lymphoma). B72.3 MAb reacted strongly with 21/21 specimens of transitional mucosa
      and with 17/21 specimens of adjacent colon cancer. Reactivity of B72.3 MAb with
      transitional mucosa was strong and homogeneous, whereas reactivity with cancer
      tissue was weaker and more heterogeneous. Reactive mucosa adjacent to squamous
      carcinoma or lymphoma was also reactive with B72.3 MAb. Our findings show that,
      in the colon, expression of TAG-72 antigen occurs during the process of
      epithelial cell transformation but is also regulated by factors unrelated to the 
      process of carcinogenesis.
FAU - Xu, M
AU  - Xu M
AD  - Memorial Sloan-Kettering Cancer Center, New York, NY 10021.
FAU - Real, F X
AU  - Real FX
FAU - Welt, S
AU  - Welt S
FAU - Schussler, M H
AU  - Schussler MH
FAU - Oettgen, H F
AU  - Oettgen HF
FAU - Old, L J
AU  - Old LJ
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Int J Cancer
JT  - International journal of cancer
JID - 0042124
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Epitopes)
SB  - IM
MH  - Antibodies, Monoclonal
MH  - Antigens, Tumor-Associated, Carbohydrate/*analysis
MH  - Carcinoma, Squamous Cell/*immunology
MH  - Colon/*immunology/pathology
MH  - Colonic Neoplasms/*immunology
MH  - Epitopes
MH  - Humans
MH  - Immunoenzyme Techniques
MH  - Intestinal Mucosa/*immunology/pathology
MH  - Lymphoma/immunology
EDAT- 1989/12/15 00:00
MHDA- 1989/12/15 00:01
CRDT- 1989/12/15 00:00
PHST- 1989/12/15 00:00 [pubmed]
PHST- 1989/12/15 00:01 [medline]
PHST- 1989/12/15 00:00 [entrez]
PST - ppublish
SO  - Int J Cancer. 1989 Dec 15;44(6):985-9.

PMID- 8667623
OWN - NLM
STAT- MEDLINE
DCOM- 19960808
LR  - 20171116
IS  - 0022-4790 (Print)
IS  - 0022-4790 (Linking)
VI  - 62
IP  - 3
DP  - 1996 Jul
TI  - Immunohistochemical expression of sialyl Tn, sialyl Lewis a, sialyl Lewis a-b-,
      and sialyl Lewis x in primary tumor and metastatic lymph nodes in human gastric
      cancer.
PG  - 171-6
AB  - Sialyl Lewis Tn(STN), sialyl Lewis a(CA-9-9), sialyl Lewis a-b-(DU-PAN-2), and
      sialyl Lewis x(SLX) antigens were immunohistochemically examined in the primary
      tumor and metastatic lymph nodes in 35 patients with advanced gastric cancer.
      STN, CA-19-9, DU-PAN-2, and SLX were expressed in 91%, 60%, 31%, and 60% in the
      primary lesion, and 77%, 54%, 22%, and 51% in the metastatic lesion,
      respectively. In only four cases, (11%) were all four antigens expressed in both 
      the primary and metastatic lesions. Three antigens were expressed in 49% of
      primary lesions and in 20% of metastatic lesions. Compared with expression in
      primary lesions, increased, unchanged and decreased expressions in metastatic
      lesions were noted in 23%, 37%, and 40% for STN, 20%, 40%, and 40% for CA-19-9,
      17%, 57%, and 26% for DU-PAN-2, and 26%, 31%, and 43% for SLX, respectively.
      These results indicate that the tumor in the primary and metastatic lesions has a
      heterogeneous expression of sialyl-related antigens. However, metastases cannot
      be predicted based upon the expression of these antigens.
FAU - Ikeda, Y
AU  - Ikeda Y
AD  - Department of Surgery II, Faculty of Medicine, Kyushu University, Fukuoka, Japan.
FAU - Mori, M
AU  - Mori M
FAU - Kajiyama, K
AU  - Kajiyama K
FAU - Haraguchi, Y
AU  - Haraguchi Y
FAU - Sasaki, O
AU  - Sasaki O
FAU - Sugimachi, K
AU  - Sugimachi K
LA  - eng
PT  - Comparative Study
PT  - Journal Article
PL  - United States
TA  - J Surg Oncol
JT  - Journal of surgical oncology
JID - 0222643
RN  - 0
      (5-acetylneuraminyl-(2-3)-galactosyl-(1-4)-(fucopyranosyl-(1-3))-N-acetylglucosam
      ine)
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens, Neoplasm)
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Biomarkers, Tumor)
RN  - 0 (DU-PAN-2 antigen, human)
RN  - 0 (Gangliosides)
RN  - 0 (Lewis Blood-Group System)
RN  - 0 (Lewis X Antigen)
RN  - 0 (Oligosaccharides)
RN  - 0 (sialosyl-Tn antigen)
RN  - 91847-18-6 (sialyl Le(a) ganglioside)
SB  - IM
MH  - Adult
MH  - Aged
MH  - Aged, 80 and over
MH  - Antibodies, Monoclonal
MH  - Antigens, Neoplasm/*metabolism
MH  - Antigens, Tumor-Associated, Carbohydrate/*metabolism
MH  - Biomarkers, Tumor/*metabolism
MH  - Female
MH  - Gangliosides/*metabolism
MH  - Humans
MH  - Immunohistochemistry
MH  - Lewis Blood-Group System/*metabolism
MH  - Lewis X Antigen/*metabolism
MH  - Lymph Nodes/*metabolism
MH  - Lymphatic Metastasis
MH  - Male
MH  - Middle Aged
MH  - Oligosaccharides/metabolism
MH  - Stomach Neoplasms/*metabolism
EDAT- 1996/07/01 00:00
MHDA- 2000/06/20 09:00
CRDT- 1996/07/01 00:00
PHST- 1996/07/01 00:00 [pubmed]
PHST- 2000/06/20 09:00 [medline]
PHST- 1996/07/01 00:00 [entrez]
AID - 10.1002/(SICI)1096-9098(199607)62:3<171::AID-JSO5>3.0.CO;2-4 [pii]
AID - 10.1002/(SICI)1096-9098(199607)62:3<171::AID-JSO5>3.0.CO;2-4 [doi]
PST - ppublish
SO  - J Surg Oncol. 1996 Jul;62(3):171-6. doi:
      10.1002/(SICI)1096-9098(199607)62:3<171::AID-JSO5>3.0.CO;2-4.

PMID- 15182935
OWN - NLM
STAT- MEDLINE
DCOM- 20040726
LR  - 20171116
IS  - 0006-3002 (Print)
IS  - 0006-3002 (Linking)
VI  - 1672
IP  - 3
DP  - 2004 Jun 11
TI  - Expression of cell surface Lewis X and Y antigens and FUT4 mRNA is increased in
      Jurkat cells undergoing apoptosis.
PG  - 157-63
AB  - Cell surface molecules undergo specific changes during apoptosis, including the
      expression of phosphatidylserine (PS) and some proteins and alterations in sugar 
      chains. Among the various sugar chains on the cell surface, Lewis X (Le(X)) and
      Lewis Y (Le(Y)) antigens are key determinants for a variety of biological
      processes. We studied the changes in Le(X) and Le(Y) expression in Jurkat cells, 
      a human T cell line, during apoptosis. Flow cytometry showed that Le(X) and Le(Y)
      antigen expression was enhanced on the cell surface during apoptosis induced by
      anti-Fas antibody. To clarify the mechanism of enhanced Le(X) and Le(Y)
      expression, we assessed the expression levels of fucosyltransferase (FUT1, 2,
      3-5-6, 4, and 9) mRNAs that are predominantly expressed in Jurkat cells and which
      are considered to form Le(X) and Le(Y). The expression of FUT4 mRNA was
      up-regulated after exposing cells to anti-Fas antibody. Moreover, the increase in
      Le(X) and Le(Y) antigen levels was significantly suppressed by caspase 3 or 8
      inhibitors. These results indicated that the induction of FUT (mainly FUT4), the 
      gene expression of which is mediated by signals downstream of caspase 3,
      increases Le(X) and Le(Y) expression in apoptotic cells.
FAU - Azuma, Yutaro
AU  - Azuma Y
AD  - Department of Clinical Chemistry, School of Pharmaceutical Sciences, Toho
      University, 2-2-1 Miyama, Funabashi, Chiba 274-8510, Japan.
      yutaro@phar.toho-u.ac.jp
FAU - Ito, Miyuki
AU  - Ito M
FAU - Taniguchi, Akiyoshi
AU  - Taniguchi A
FAU - Matsumoto, Kojiro
AU  - Matsumoto K
LA  - eng
PT  - Journal Article
PL  - Netherlands
TA  - Biochim Biophys Acta
JT  - Biochimica et biophysica acta
JID - 0217513
RN  - 0 (Antibodies)
RN  - 0 (Caspase Inhibitors)
RN  - 0 (Enzyme Inhibitors)
RN  - 0 (Lewis Blood-Group System)
RN  - 0 (Lewis X Antigen)
RN  - 0 (Lewis Y antigen)
RN  - 0 (RNA, Messenger)
RN  - 0 (fas Receptor)
RN  - 1CC1JFE158 (Dactinomycin)
RN  - EC 2.4.1.- (FUT4 protein, human)
RN  - EC 2.4.1.- (Fucosyltransferases)
RN  - EC 3.4.22.- (Caspases)
SB  - IM
MH  - Antibodies/immunology/pharmacology
MH  - *Apoptosis/drug effects
MH  - Blotting, Northern
MH  - Caspase Inhibitors
MH  - Caspases/metabolism
MH  - Cell Division/drug effects
MH  - Dactinomycin/pharmacology
MH  - Enzyme Inhibitors/pharmacology
MH  - Flow Cytometry
MH  - Fucosyltransferases/*genetics
MH  - Humans
MH  - Jurkat Cells
MH  - Lewis Blood-Group System/*metabolism
MH  - Lewis X Antigen/*metabolism
MH  - RNA, Messenger/genetics/metabolism
MH  - Time Factors
MH  - fas Receptor/immunology
EDAT- 2004/06/09 05:00
MHDA- 2004/07/28 05:00
CRDT- 2004/06/09 05:00
PHST- 2003/09/26 00:00 [received]
PHST- 2004/03/01 00:00 [revised]
PHST- 2004/03/16 00:00 [accepted]
PHST- 2004/06/09 05:00 [pubmed]
PHST- 2004/07/28 05:00 [medline]
PHST- 2004/06/09 05:00 [entrez]
AID - 10.1016/j.bbagen.2004.03.006 [doi]
AID - S0304416504000662 [pii]
PST - ppublish
SO  - Biochim Biophys Acta. 2004 Jun 11;1672(3):157-63. doi:
      10.1016/j.bbagen.2004.03.006.

PMID- 11501845
OWN - NLM
STAT- MEDLINE
DCOM- 20010823
LR  - 20151119
IS  - 0250-7005 (Print)
IS  - 0250-7005 (Linking)
VI  - 21
IP  - 3C
DP  - 2001 May-Jun
TI  - Expression of mucin-associated carbohydrate core antigens in esophageal squamous 
      cell carcinomas.
PG  - 2189-93
AB  - In contrast to gastrointestinal cancer, where a correlation between the
      expression of different mucin-associated core antigens with clinico-pathological 
      parameters and survival probability, has been established, little is known about 
      their importance in esophageal cancer. Therefore, we characterized esophageal
      squamous cell carcinomas from 84 patients immunohistochemically by applying
      monoclonal antibodies (mabs) directed against the Thomsen-Friedenreich (TF)
      antigen MUC1-bound TF antigen and sialyl-Tn. TF was observed in about 40% of the 
      cases and MUC1-TF epitope in about 75%. Sialyl-Tn was detectable in about half of
      the carcinomas under study. None of these mabs showed any correlation between
      binding pattern and clinico-pathological variables, such as TNM stage, lymph node
      metastasis or grading. However, a strong expression of MUC1-TF epitope as well as
      sialyl-Tn antigen predicted a poor survival probability. In conclusion, it is
      suggested that mucin-associated carbohydrate core antigens are involved in the
      biology and clinical course of esophageal squamous carcinomas.
FAU - Flucke, U
AU  - Flucke U
AD  - Institute of Pathology and Department of Visceral and Vascular Surgery,
      University of Cologne, Germany.
FAU - Zirbes, T K
AU  - Zirbes TK
FAU - Schroder, W
AU  - Schroder W
FAU - Monig, S P
AU  - Monig SP
FAU - Koch, V
AU  - Koch V
FAU - Schmitz, K
AU  - Schmitz K
FAU - Thiele, J
AU  - Thiele J
FAU - Dienes, H P
AU  - Dienes HP
FAU - Holscher, A H
AU  - Holscher AH
FAU - Baldus, S E
AU  - Baldus SE
LA  - eng
PT  - Journal Article
PL  - Greece
TA  - Anticancer Res
JT  - Anticancer research
JID - 8102988
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Biomarkers, Tumor)
RN  - 0 (Mucin-1)
RN  - 0 (sialosyl-Tn antigen)
RN  - 3554-90-3 (Thomsen-Friedenreich antigen)
SB  - IM
MH  - Adult
MH  - Aged
MH  - Aged, 80 and over
MH  - Antibodies, Monoclonal
MH  - Antigens, Tumor-Associated, Carbohydrate/*biosynthesis/metabolism
MH  - Biomarkers, Tumor/*biosynthesis
MH  - Carcinoma, Squamous Cell/*immunology/metabolism/pathology
MH  - Esophageal Neoplasms/*immunology/metabolism/pathology
MH  - Female
MH  - Humans
MH  - Immunohistochemistry
MH  - Male
MH  - Middle Aged
MH  - Mucin-1/*immunology/metabolism
MH  - Neoplasm Staging
MH  - Prognosis
EDAT- 2001/08/15 10:00
MHDA- 2001/08/24 10:01
CRDT- 2001/08/15 10:00
PHST- 2001/08/15 10:00 [pubmed]
PHST- 2001/08/24 10:01 [medline]
PHST- 2001/08/15 10:00 [entrez]
PST - ppublish
SO  - Anticancer Res. 2001 May-Jun;21(3C):2189-93.

PMID- 8780713
OWN - NLM
STAT- MEDLINE
DCOM- 19961022
LR  - 20081121
IS  - 0006-291X (Print)
IS  - 0006-291X (Linking)
VI  - 225
IP  - 3
DP  - 1996 Aug 23
TI  - Cloning and expression of cDNA for O-acetylation of GD3 ganglioside.
PG  - 932-8
AB  - O-acetylated sialic acids of glycoproteins and gangliosides show cell
      type-specific and developmentally regulated expression in various systems and
      sometimes reappear as oncofetal antigens. O-acetylation of sialic acids may
      influence cell-cell interactions mediated by the sialic acid-binding lectins.
      Here we describe the molecular cloning and sequencing of a gene that produces
      O-acetyl disialoganglioside (O-acetyl GD3). Expression analysis showed that this 
      gene product participates the O-acetylation of GD3 ganglioside sialic acid. The
      deduced amino acid sequence of the product was found to be similar to the milk
      fat globule membrane glycoprotein.
FAU - Ogura, K
AU  - Ogura K
AD  - Department of Tumor Immunology, Tokyo Metropolitan Institute of Medical Science, 
      Japan.
FAU - Nara, K
AU  - Nara K
FAU - Watanabe, Y
AU  - Watanabe Y
FAU - Kohno, K
AU  - Kohno K
FAU - Tai, T
AU  - Tai T
FAU - Sanai, Y
AU  - Sanai Y
LA  - eng
SI  - GENBANK/D84068
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Biochem Biophys Res Commun
JT  - Biochemical and biophysical research communications
JID - 0372516
RN  - 0 (DNA, Complementary)
RN  - 0 (Gangliosides)
RN  - 0 (Mucin-1)
RN  - 62010-37-1 (ganglioside, GD3)
RN  - 98743-26-1 (9-O-acetyl-GD3 ganglioside)
RN  - EC 2.3.1.- (Acetyltransferases)
RN  - EC 2.3.1.- (ganglioside O-acetyltransferase)
SB  - IM
MH  - Acetylation
MH  - Acetyltransferases/*genetics/*metabolism
MH  - Amino Acid Sequence
MH  - Animals
MH  - Base Sequence
MH  - CHO Cells
MH  - Cloning, Molecular
MH  - Cricetinae
MH  - DNA, Complementary/*genetics
MH  - Gangliosides/*metabolism
MH  - Gene Expression
MH  - Humans
MH  - Molecular Sequence Data
MH  - Mucin-1/genetics
MH  - Rats
MH  - Sequence Homology, Amino Acid
MH  - Transfection
EDAT- 1996/08/23 00:00
MHDA- 1996/08/23 00:01
CRDT- 1996/08/23 00:00
PHST- 1996/08/23 00:00 [pubmed]
PHST- 1996/08/23 00:01 [medline]
PHST- 1996/08/23 00:00 [entrez]
AID - S0006-291X(96)91274-7 [pii]
AID - 10.1006/bbrc.1996.1274 [doi]
PST - ppublish
SO  - Biochem Biophys Res Commun. 1996 Aug 23;225(3):932-8. doi:
      10.1006/bbrc.1996.1274.

PMID- 2159145
OWN - NLM
STAT- MEDLINE
DCOM- 19900606
LR  - 20190501
IS  - 0027-8424 (Print)
IS  - 0027-8424 (Linking)
VI  - 87
IP  - 9
DP  - 1990 May
TI  - Human monoclonal antibody with dual GM2/GD2 specificity derived from an immunized
      melanoma patient.
PG  - 3333-7
AB  - GM2 ganglioside is a common cell surface constituent of human melanoma and other 
      tumors of neuroectodermal origin, and vaccination with GM2 ganglioside results in
      high levels of anti-GM2 antibodies in patients with melanoma. Lymphocytes from a 
      GM2-vaccinated patient (VS) were transformed by Epstein-Barr virus and tested for
      production of antibodies with reactivity for GM2-positive tumor cells. A high
      percentage of antibody-producing B cells was detected, but antibody reactivity
      was generally lost during culture expansion. Two cultures, however, remained
      stable for antibody productivity and one was used to develop a stable hybrid line
      with mouse myeloma. The monoclonal antibody (designated 3-207) derived from
      patient VS has dual specificity for GM2 and GD2, despite the fact that only GM2
      antibody could be detected in the patient's serum. Monoclonal antibody 3-207
      shows high-titered reactivity with a range of melanoma, astrocytoma,
      neuroblastoma, and leukemia cell lines, cells with prominent cell surface
      expression of GM2 and GD2. The cell surface reactivity of monoclonal antibody
      3-207 was not abolished by treatment of target cells with neuraminidase, as the
      enzyme converted GD2 to GM2, which was still detected by monoclonal antibody
      3-207.
FAU - Yamaguchi, H
AU  - Yamaguchi H
AD  - Memorial Sloan-Kettering Cancer Center, New York, NY 10021.
FAU - Furukawa, K
AU  - Furukawa K
FAU - Fortunato, S R
AU  - Fortunato SR
FAU - Livingston, P O
AU  - Livingston PO
FAU - Lloyd, K O
AU  - Lloyd KO
FAU - Oettgen, H F
AU  - Oettgen HF
FAU - Old, L J
AU  - Old LJ
LA  - eng
GR  - CA-08748/CA/NCI NIH HHS/United States
GR  - CA-33049/CA/NCI NIH HHS/United States
GR  - CA-47427/CA/NCI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Proc Natl Acad Sci U S A
JT  - Proceedings of the National Academy of Sciences of the United States of America
JID - 7505876
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (BCG Vaccine)
RN  - 0 (Gangliosides)
RN  - 0 (Vaccines)
RN  - 19600-01-2 (G(M2) Ganglioside)
RN  - 65988-71-8 (ganglioside, GD2)
RN  - EC 3.2.1.18 (Neuraminidase)
SB  - IM
MH  - Animals
MH  - Antibodies, Monoclonal/*isolation & purification
MH  - BCG Vaccine
MH  - Cell Fusion
MH  - Cell Line
MH  - Cell Transformation, Viral
MH  - Chromatography, Thin Layer
MH  - G(M2) Ganglioside/*immunology
MH  - Gangliosides/*immunology/isolation & purification
MH  - Herpesvirus 4, Human/genetics
MH  - Humans
MH  - Melanoma/*immunology
MH  - Mice
MH  - Neuraminidase
MH  - Tumor Cells, Cultured/*immunology
MH  - Vaccines
PMC - PMC53894
EDAT- 1990/05/01 00:00
MHDA- 1990/05/01 00:01
CRDT- 1990/05/01 00:00
PHST- 1990/05/01 00:00 [pubmed]
PHST- 1990/05/01 00:01 [medline]
PHST- 1990/05/01 00:00 [entrez]
AID - 10.1073/pnas.87.9.3333 [doi]
PST - ppublish
SO  - Proc Natl Acad Sci U S A. 1990 May;87(9):3333-7. doi: 10.1073/pnas.87.9.3333.

PMID- 8624728
OWN - NLM
STAT- MEDLINE
DCOM- 19960624
LR  - 20061115
IS  - 0006-8993 (Print)
IS  - 0006-8993 (Linking)
VI  - 700
IP  - 1-2
DP  - 1995 Nov 27
TI  - Developmental changes of ganglioside expressions in postnatal rat cerebellar
      cortex.
PG  - 40-58
AB  - We previously described the differential distribution of gangliosides in adult
      rat brain as detected by specific antibodies. We report here the distribution of 
      gangliosides during the development of postnatal rat cerebellum by an
      immunofluorescence technique with mouse monoclonal antibodies (mAbs). Eleven mAbs
      that specifically recognize each ganglioside were used. Our study revealed that
      the expression of each ganglioside changed dramatically during the development.
      GD3 and O-Ac-GD3 were expressed intensely in the external granular layer at 1, 5,
      and 10 days, whereas GD2 was firstly detected in the internal granular layer at 5
      days and GD1b WAS diffusely detected throughout all layers of the cerebellar
      cortex at early postnatal days. GD2 and GD1b were more intensely expressed in the
      granular layer at 20, 30, and 80 days, suggesting that premature granule cells
      expressed GD3 and its derivative, O-Ac-GD3, whereas mature granule cells express 
      GD2 and GD1B intensely. On the other hand, GM1 was exclusively detected in the
      external granular layer and the molecular layer at 1 and 5 days. The staining
      sites spread gradually from these outer layers into the internal granular layer
      and the white matter after 10 days. The positive cells in the external granular
      layer and the molecular layer appeared to be Bergmann glial cells and their
      radially ascending cytoplasmic processes. The intensity of the staining in these 
      specialized astroglial cells decreased gradually during postnatal days. In
      contrast, the expression of GQ1b was very faint at birth, but gradually increased
      during the development and was detected intensely in the internal granular layer,
      particularly in the cerebellar glomeruli in adulthood, suggesting that GQ1b
      expression may be associated with synapse-related structures. The developmental
      changes of the expression of other gangliosides were also recognized in the
      postnatal rat cerebellum. These results suggest that specific gangliosides may
      play an important role in regulating the early events responsible for the orderly
      formation of the cerebellar cortex.
FAU - Kotani, M
AU  - Kotani M
AD  - Department of Tumor Immunology, Tokyo Metropolitan Institute of Medical Science, 
      Japan.
FAU - Terashima, T
AU  - Terashima T
FAU - Tai, T
AU  - Tai T
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - Netherlands
TA  - Brain Res
JT  - Brain research
JID - 0045503
RN  - 0 (Gangliosides)
RN  - 0 (Nerve Growth Factors)
RN  - 12707-58-3 (ganglioside, GD1a)
RN  - 19553-76-5 (ganglioside, GD1b)
RN  - 37758-47-7 (G(M1) Ganglioside)
RN  - 62010-37-1 (ganglioside, GD3)
RN  - 68652-37-9 (GQ1b ganglioside)
SB  - IM
MH  - Animals
MH  - Carbohydrate Sequence
MH  - Cerebellar Cortex/*chemistry/*growth & development
MH  - Fluorescent Antibody Technique, Indirect
MH  - G(M1) Ganglioside/analysis
MH  - Gangliosides/*analysis
MH  - Molecular Sequence Data
MH  - Morphogenesis
MH  - Nerve Growth Factors/analysis
MH  - Rats
MH  - Rats, Wistar
EDAT- 1995/11/27 00:00
MHDA- 1995/11/27 00:01
CRDT- 1995/11/27 00:00
PHST- 1995/11/27 00:00 [pubmed]
PHST- 1995/11/27 00:01 [medline]
PHST- 1995/11/27 00:00 [entrez]
AID - 0006-8993(95)00923-E [pii]
PST - ppublish
SO  - Brain Res. 1995 Nov 27;700(1-2):40-58.

PMID- 9312075
OWN - NLM
STAT- MEDLINE
DCOM- 19971022
LR  - 20190508
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 272
IP  - 40
DP  - 1997 Oct 3
TI  - Expression cloning of rat cDNA encoding UDP-galactose:GD2
      beta1,3-galactosyltransferase that determines the expression of GD1b/GM1/GA1.
PG  - 24794-9
AB  - Using an anti-GD1b monoclonal antibody, expression cloning of a cDNA for the
      beta1,3-galactosyltransferase gene (EC 2.4.1.62) was performed. KF4C, mouse
      melanoma B16 transfected with polyoma T antigen gene, and GM2/GD2 synthase cDNA
      was used as a recipient cell line for the cDNA library transfection. A cDNA clone
      of GD3 synthase, pD3T-31 was co-transfected with a cDNA library prepared from rat
      brain RNA using the pcDNAI expression vector. The isolated cDNA clone pM1T-9
      predicted a type II membrane protein with 4 amino acids of cytoplasmic domain, 21
      amino acids of transmembrane region, and a large catalytic domain with 346 amino 
      acids. Introduction of the cDNA clone into a mouse melanoma line B16 previously
      transfected with a GM2/GD2 synthase gene resulted in the neo-synthesis of GM1.
      Co-transfection of the cell line with pM1T-9 and a GD3 synthase cDNA resulted in 
      the expression of GD1b as well as GM1. Moreover, introduction of pM1T-9 into L
      cell (lacking GM3 synthase), previously transfected with GM2/GD2 synthase gene,
      resulted in the definite expression of asialo-GM1. These results indicated that
      GD1b/GM1/GA1 synthases were identical, as previously suggested based on
      enzymological analysis. In Northern blots of the beta1, 3-galactosyltransferase
      gene with total RNA from various rat tissues, a 1.6-kilobase mRNA was strongly
      expressed in spleen, thymus, kidney, and testis. However, the expression level of
      the gene in the adult brain tissue was not especially high. On the other hand,
      this gene was expressed at high levels in the rat brain of embryonal day 12, and 
      reached a peak at around birth, then fell to low level in the adult brain.
FAU - Miyazaki, H
AU  - Miyazaki H
AD  - Department of Biochemistry II, Nagoya University School of Medicine, 65 Tsuramai,
      Nagoya 466, Japan.
FAU - Fukumoto, S
AU  - Fukumoto S
FAU - Okada, M
AU  - Okada M
FAU - Hasegawa, T
AU  - Hasegawa T
FAU - Furukawa, K
AU  - Furukawa K
LA  - eng
SI  - GENBANK/AB003478
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (G(A1) ganglioside)
RN  - 0 (Gangliosides)
RN  - 0 (Glycosphingolipids)
RN  - 0 (RNA, Messenger)
RN  - 0 (Recombinant Proteins)
RN  - 19553-76-5 (ganglioside, GD1b)
RN  - 37758-47-7 (G(M1) Ganglioside)
RN  - EC 2.4.1.- (GD2 beta1,3-galactosyltransferase)
RN  - EC 2.4.1.- (Galactosyltransferases)
RN  - EC 2.4.99.- (Sialyltransferases)
RN  - EC 2.4.99.8 (alpha-N-acetylneuraminate alpha-2,8-sialyltransferase)
SB  - IM
MH  - Aging/metabolism
MH  - Amino Acid Sequence
MH  - Animals
MH  - Animals, Newborn
MH  - Base Sequence
MH  - Brain/*enzymology
MH  - Carbohydrate Sequence
MH  - Cloning, Molecular
MH  - Embryonic and Fetal Development
MH  - G(M1) Ganglioside/*biosynthesis/chemistry
MH  - Galactosyltransferases/*biosynthesis/chemistry/metabolism
MH  - Gangliosides/*biosynthesis/chemistry
MH  - Gene Expression Regulation, Developmental
MH  - Gene Expression Regulation, Enzymologic
MH  - Gene Library
MH  - Glycosphingolipids/*biosynthesis/chemistry
MH  - Male
MH  - Melanoma, Experimental
MH  - Mice
MH  - Molecular Sequence Data
MH  - Organ Specificity
MH  - RNA, Messenger/biosynthesis
MH  - Rats
MH  - Recombinant Proteins/biosynthesis/chemistry/metabolism
MH  - Sialyltransferases/biosynthesis/metabolism
MH  - Testis/enzymology
MH  - Transcription, Genetic
MH  - Transfection
MH  - Tumor Cells, Cultured
EDAT- 1997/10/06 00:00
MHDA- 1997/10/06 00:01
CRDT- 1997/10/06 00:00
PHST- 1997/10/06 00:00 [pubmed]
PHST- 1997/10/06 00:01 [medline]
PHST- 1997/10/06 00:00 [entrez]
AID - 10.1074/jbc.272.40.24794 [doi]
PST - ppublish
SO  - J Biol Chem. 1997 Oct 3;272(40):24794-9. doi: 10.1074/jbc.272.40.24794.

PMID- 12460925
OWN - NLM
STAT- MEDLINE
DCOM- 20030107
LR  - 20181130
IS  - 0008-5472 (Print)
IS  - 0008-5472 (Linking)
VI  - 62
IP  - 23
DP  - 2002 Dec 1
TI  - Vascular endothelial growth factor secretion by tumor-infiltrating macrophages
      essentially supports tumor angiogenesis, and IgG immune complexes potentiate the 
      process.
PG  - 7042-9
AB  - Tumor growth requires neoangiogenesis. Members of the vascular endothelial growth
      factor (VEGF) family play an important role as angiogenic promoters in malignant 
      tumors. Tumor cells and stromal cells are sources of VEGF in the tumor. We tested
      the relevance of the tumor-infiltrating macrophage (TIM) contribution as a source
      of VEGF in the tumor environment and the role of the local immune complexes in
      inducing the TIM release of VEGF. Colon and breast carcinoma biopsies were
      studied with immunoperoxidase staining of CD11b, sialyl-Tn (sTn) antigen (Ag),
      and gamma immunoglobulin (IgG). The presence of TIM containing phagosomes
      positive for both IgG and sTn Ag was observed in all tumors, showing that TIMs
      endocytosed local immune complexes. Reverse transcription-PCR analysis of
      macrophage (MO) mRNA showed VEGF-A and -B, but not VEGF-C or -D. That pattern was
      not modified by the presence of tumor cells. In vitro, the interaction of tumor
      cells and MO promoted the secretion of MO VEGF. The MO secretion of VEGF was
      augmented when tumor cells were added to cocultures containing MOs and
      polymorphonuclear cells. Immune complexes formed with tumor sTn Ag and IgG
      induced a 5-fold increase of MO VEGF secretion. In vivo, TIMs and neoangiogenesis
      were associated. In vivo experiments with severe combined immunodeficient and
      athymic nude (nu/nu) mice showed increased number of TIMs, increased tumor
      angiogenesis, and faster tumor growth in mice with significant serum anti-sTn
      IgG. This study demonstrates that VEGF secreted by TIMs represents an essential
      support for tumor angiogenesis and growth, certainly influenced by the humoral
      antitumor immune response.
FAU - Barbera-Guillem, Emilio
AU  - Barbera-Guillem E
AD  - BioCrystal Ltd. Research Laboratories, Westerville, Ohio 43082-8888, USA.
      ebarbera@columbus.rr.com
FAU - Nyhus, Julie K
AU  - Nyhus JK
FAU - Wolford, Chris C
AU  - Wolford CC
FAU - Friece, Chad R
AU  - Friece CR
FAU - Sampsel, James W
AU  - Sampsel JW
LA  - eng
PT  - Journal Article
PL  - United States
TA  - Cancer Res
JT  - Cancer research
JID - 2984705R
RN  - 0 (Antigen-Antibody Complex)
RN  - 0 (Antigens, Neoplasm)
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Endothelial Growth Factors)
RN  - 0 (Immunoglobulin G)
RN  - 0 (Intercellular Signaling Peptides and Proteins)
RN  - 0 (Lymphokines)
RN  - 0 (RNA, Messenger)
RN  - 0 (Vascular Endothelial Growth Factor A)
RN  - 0 (Vascular Endothelial Growth Factors)
RN  - 0 (sialosyl-Tn antigen)
SB  - IM
MH  - Adenocarcinoma/*blood supply/immunology/pathology
MH  - Animals
MH  - Antigen-Antibody Complex/*physiology
MH  - Antigens, Neoplasm/immunology
MH  - Antigens, Tumor-Associated, Carbohydrate/immunology/physiology
MH  - Breast Neoplasms/blood supply/immunology/pathology
MH  - Cell Communication/physiology
MH  - Colonic Neoplasms/blood supply/immunology/pathology
MH  - Endothelial Growth Factors/biosynthesis/genetics/*metabolism
MH  - Female
MH  - Humans
MH  - Immunoglobulin G/immunology/*physiology
MH  - Intercellular Signaling Peptides and Proteins/biosynthesis/genetics/*metabolism
MH  - Lymphokines/biosynthesis/genetics/*metabolism
MH  - Macrophages/immunology/*metabolism
MH  - Mice
MH  - Mice, Inbred C3H
MH  - Mice, SCID
MH  - Neovascularization, Pathologic/immunology/pathology/*physiopathology
MH  - RNA, Messenger/biosynthesis/genetics
MH  - Reverse Transcriptase Polymerase Chain Reaction
MH  - Vascular Endothelial Growth Factor A
MH  - Vascular Endothelial Growth Factors
EDAT- 2002/12/04 04:00
MHDA- 2003/01/08 04:00
CRDT- 2002/12/04 04:00
PHST- 2002/12/04 04:00 [pubmed]
PHST- 2003/01/08 04:00 [medline]
PHST- 2002/12/04 04:00 [entrez]
PST - ppublish
SO  - Cancer Res. 2002 Dec 1;62(23):7042-9.

PMID- 9790295
OWN - NLM
STAT- MEDLINE
DCOM- 19981217
LR  - 20171116
IS  - 1043-3074 (Print)
IS  - 1043-3074 (Linking)
VI  - 20
IP  - 8
DP  - 1998 Dec
TI  - Identification of sialyl Lewis-x in squamous cell carcinoma of the head and neck.
PG  - 726-31
AB  - BACKGROUND: Sialyl Lewis-x (sLx) is a cellular adhesion molecule (CAM) that has
      been implicated in the inflammatory reaction and cancer metastasis. The sLx is
      the carbohydrate ligand of endothelial-selectin (E-selectin), an inducible
      vascular endothelial CAM. The role of sLx has been investigated in several
      cancers, and its presence has been correlated with advanced disease stage,
      decreased disease-free survival, and greater metastatic potential. A recent study
      has found that cultured head and neck (HN) squamous cell carcinoma (SCC) cell
      lines express sLx and that binding of these cells to cytokine activated
      endothelium correlates with the endothelial expression of E-selectin. The purpose
      of this study was to identify sLx in the tumors of patients with HNSCC and to see
      if the presence of sLx correlated with disease status. METHODS: We performed
      immunohistochemical (IHC) staining to detect the sLx antigen using the monoclonal
      antibody (MAb) KM-93. Eighty-two specimens of HNSCC that were obtained at the
      time of resection or biopsy were analyzed for sLx staining patterns and
      intensities. The clinical outcomes of survival, disease-free interval, and
      incidence of distant metastasis were then assessed to determine whether there was
      a correlation with sLx tumor expression. In addition, we analyzed specimens from 
      metastatic HNSCC sites for expression of sLx. RESULTS: The sLx expression was
      identified in 62% of the primary tumor specimens and 87% of the metastatic tumor 
      specimens analyzed by IHC. The staining pattern in the HNSCC tumors differed from
      that seen in normal squamous epithelium but was variable in both intensity and
      distribution. The sLx expression in the metastatic sites was higher than in the
      primary sites in 67% of the specimens (10 of 15). There was no correlation
      between sLx staining and disease status. CONCLUSIONS: The results of this study
      demonstrate that sLx is present in HNSCC and supports the data that show that sLx
      may play a role in the metastasis of HNSCC. Future studies are warranted to
      evaluate the role of sLx, E-selectin, and other CAMs in HNSCC.
FAU - Farmer, R W
AU  - Farmer RW
AD  - Division of Otolaryngology-Head and Neck Surgery, Duke University Medical Center,
      Durham, North Carolina 27710, USA.
FAU - Richtsmeier, W J
AU  - Richtsmeier WJ
FAU - Scher, R L
AU  - Scher RL
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Head Neck
JT  - Head & neck
JID - 8902541
RN  - 0
      (5-acetylneuraminyl-(2-3)-galactosyl-(1-4)-(fucopyranosyl-(1-3))-N-acetylglucosam
      ine)
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Lewis X Antigen)
RN  - 0 (Oligosaccharides)
SB  - IM
MH  - Adolescent
MH  - Aged
MH  - Aged, 80 and over
MH  - Antibodies, Monoclonal
MH  - Carcinoma, Squamous Cell/*metabolism/pathology
MH  - Female
MH  - Head and Neck Neoplasms/*metabolism/pathology
MH  - Humans
MH  - Immunohistochemistry
MH  - Lewis X Antigen/*metabolism
MH  - Male
MH  - Middle Aged
MH  - Neoplasm Metastasis
MH  - Oligosaccharides/*metabolism
EDAT- 1998/10/28 03:03
MHDA- 2000/06/20 09:00
CRDT- 1998/10/28 03:03
PHST- 1998/10/28 03:03 [pubmed]
PHST- 2000/06/20 09:00 [medline]
PHST- 1998/10/28 03:03 [entrez]
AID - 10.1002/(SICI)1097-0347(199812)20:8<726::AID-HED11>3.0.CO;2-C [pii]
PST - ppublish
SO  - Head Neck. 1998 Dec;20(8):726-31.

PMID- 3235849
OWN - NLM
STAT- MEDLINE
DCOM- 19890428
LR  - 20171206
IS  - 0393-6155 (Print)
IS  - 0393-6155 (Linking)
VI  - 3
IP  - 4
DP  - 1988 Oct-Dec
TI  - Molecular profile, tissue distribution and prognostic evaluation of a human
      melanoma-carcinoma antigen recognized by the murine monoclonal antibody B1.1.
PG  - 211-20
AB  - Using the murine monoclonal antibody (MoAb) B1.1 we have analyzed the
      immunochemical profile and the tissue distribution of a human melanoma associated
      antigen (MAA) carrying an epitope shared by the 180 kd CEA. Results of this study
      have demonstrated that the epitope expressed by the MAA is carried by a distinct 
      set of molecules of 110-140 kd. Similarly to the 180 kd CEA molecules synthesized
      by carcinomas, the expression of the melanoma associated CEA like components
      (MA-CEA) is upregulated by IFN-alpha. The tissue distribution of MA-CEA is not
      restricted to malignant primary and metastatic melanocytic lesions but is found
      also at low levels in 64% of benign nevi. No circulating CEA was found in
      patients bearing widespread metastatic disease of MA-CEA positive lesions.
      Preliminary clinical evaluation of stage I melanoma patients bearing MoAb B1.1
      positive lesions has not shown a significative prognostic association of this
      phenotypic marker with clinical course of the disease.
FAU - Natali, P G
AU  - Natali PG
AD  - Regina Elena Cancer Institute, Rome, Italy.
FAU - Nicotra, M R
AU  - Nicotra MR
FAU - Nuti, M
AU  - Nuti M
FAU - Bigotti, G
AU  - Bigotti G
FAU - Calabro, A
AU  - Calabro A
FAU - Schlom, J
AU  - Schlom J
FAU - Giacomini, P
AU  - Giacomini P
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Int J Biol Markers
JT  - The International journal of biological markers
JID - 8712411
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens, Neoplasm)
RN  - 0 (Biomarkers, Tumor)
RN  - 0 (Carcinoembryonic Antigen)
RN  - 0 (Interferon Type I)
RN  - 0 (Melanoma-Specific Antigens)
RN  - 0 (Neoplasm Proteins)
SB  - IM
MH  - Adolescent
MH  - Adult
MH  - Aged
MH  - *Antibodies, Monoclonal
MH  - Antigens, Neoplasm
MH  - Biomarkers, Tumor/*analysis/genetics
MH  - Carcinoembryonic Antigen/analysis
MH  - Cell Line
MH  - Female
MH  - Gene Expression Regulation
MH  - Humans
MH  - Immunohistochemistry
MH  - Interferon Type I/physiology
MH  - Male
MH  - Melanoma/*pathology
MH  - Melanoma-Specific Antigens
MH  - Middle Aged
MH  - Neoplasm Proteins/*analysis/genetics
MH  - Prognosis
MH  - Skin/pathology
MH  - Skin Neoplasms/*pathology
EDAT- 1988/10/01 00:00
MHDA- 1988/10/01 00:01
CRDT- 1988/10/01 00:00
PHST- 1988/10/01 00:00 [pubmed]
PHST- 1988/10/01 00:01 [medline]
PHST- 1988/10/01 00:00 [entrez]
PST - ppublish
SO  - Int J Biol Markers. 1988 Oct-Dec;3(4):211-20.

PMID- 7809154
OWN - NLM
STAT- MEDLINE
DCOM- 19950202
LR  - 20190501
IS  - 0027-8424 (Print)
IS  - 0027-8424 (Linking)
VI  - 91
IP  - 26
DP  - 1994 Dec 20
TI  - Specificity analysis of blood group Lewis-y (Le(y)) antibodies generatedagainst
      synthetic and natural Le(y) determinants.
PG  - 12957-61
AB  - Le(y)-reactive monoclonal antibodies (mAbs) were generated in mice by
      immunization with synthetic Le(y) neoglycoproteins or with Le(y)-expressing
      cells. Serological analysis indicated that mAbs raised against synthetic Le(y)
      (i) reacted strongly with synthetic Le(y) but poorly with natural Le(y), (ii)
      cross-reacted with Le(x) or H-type 2 structures, and (iii) were IgG1, IgG2a, or
      IgG2b. mAbs raised against Le(y)-expressing cells (i) reacted with both synthetic
      Le(y) and natural Le(y), (ii) were of two types: cross-reactive with Le(x) or
      H-type 2 structures or specific for Le(y), and (iii) were IgM or IgG3. One of the
      mAbs raised against natural Le(y), mAb 3S193 (IgG3), showed high specificity for 
      Le(y) in ELISA tests with synthetic Le(y) and Le(y) containing glycoproteins and 
      glycolipids; it also reacted strongly in rosetting assays and cytotoxic tests
      with Le(y)-expressing cells. mAb 3S193 did not lyse O, A, AB, and B human
      erythrocytes in the presence of human complement. In flow cytometry, there was
      weak reactivity with granulocytes, a reactivity also observed with two previously
      described highly specific Le(y) mouse mAbs--BR55-2 (IgG3) and B3 (IgG1). A
      humanized version of mAb 3S193 has been constructed, and the specificity pattern 
      and reactivity for Le(y) remain very similar to mouse mAb 3S193.
FAU - Kitamura, K
AU  - Kitamura K
AD  - Ludwig Institute for Cancer Research, New York Unit, NY.
FAU - Stockert, E
AU  - Stockert E
FAU - Garin-Chesa, P
AU  - Garin-Chesa P
FAU - Welt, S
AU  - Welt S
FAU - Lloyd, K O
AU  - Lloyd KO
FAU - Armour, K L
AU  - Armour KL
FAU - Wallace, T P
AU  - Wallace TP
FAU - Harris, W J
AU  - Harris WJ
FAU - Carr, F J
AU  - Carr FJ
FAU - Old, L J
AU  - Old LJ
LA  - eng
GR  - CA 08748/CA/NCI NIH HHS/United States
GR  - CA 33049/CA/NCI NIH HHS/United States
GR  - CA 52477/CA/NCI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Proc Natl Acad Sci U S A
JT  - Proceedings of the National Academy of Sciences of the United States of America
JID - 7505876
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Biomarkers, Tumor)
RN  - 0 (Glycoconjugates)
RN  - 0 (Glycosphingolipids)
RN  - 0 (Lewis Blood-Group System)
RN  - 0 (Recombinant Fusion Proteins)
SB  - IM
MH  - Animals
MH  - Antibodies, Monoclonal/*immunology
MH  - *Antibody Specificity
MH  - Antibody-Dependent Cell Cytotoxicity
MH  - Antigens, Tumor-Associated, Carbohydrate/*immunology
MH  - Biomarkers, Tumor/immunology
MH  - Carbohydrate Sequence
MH  - Colonic Neoplasms/immunology
MH  - Glycoconjugates/chemical synthesis
MH  - Glycosphingolipids/chemistry/*immunology
MH  - Humans
MH  - Immunity, Cellular
MH  - In Vitro Techniques
MH  - Lewis Blood-Group System/*immunology
MH  - Mice
MH  - Molecular Sequence Data
MH  - Recombinant Fusion Proteins
MH  - Tumor Cells, Cultured
PMC - PMC45559
EDAT- 1994/12/20 00:00
MHDA- 1994/12/20 00:01
CRDT- 1994/12/20 00:00
PHST- 1994/12/20 00:00 [pubmed]
PHST- 1994/12/20 00:01 [medline]
PHST- 1994/12/20 00:00 [entrez]
AID - 10.1073/pnas.91.26.12957 [doi]
PST - ppublish
SO  - Proc Natl Acad Sci U S A. 1994 Dec 20;91(26):12957-61. doi:
      10.1073/pnas.91.26.12957.

PMID- 16476743
OWN - NLM
STAT- MEDLINE
DCOM- 20060605
LR  - 20061115
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 281
IP  - 15
DP  - 2006 Apr 14
TI  - Targeted disruption of Gb3/CD77 synthase gene resulted in the complete deletion
      of globo-series glycosphingolipids and loss of sensitivity to verotoxins.
PG  - 10230-5
AB  - To examine whether globotriaosylceramide (Gb3/CD77) is a receptor for verotoxins 
      (VTs) in vivo, sensitivity of Gb3/CD77 synthase null mutant mice to VT-2 and VT-1
      was analyzed. Although wild-type mice died after administration of 0.02 microg of
      VT-2 or 1.0 microg of VT-1, the mutant mice showed no reaction to doses as much
      as 100 times that administered to wild types. Expression analysis of Gb3/CD77 in 
      mouse tissues with antibody revealed that low, but definite, levels of Gb3/CD77
      were expressed in the microvascular endothelial cells of the brain cortex and pia
      mater and in renal tubular capillaries. Corresponding to the Gb3/CD77 expression,
      tissue damage with edema, congestion, and cytopathic changes was observed,
      indicating that Gb3/CD77 (and its derivatives) exclusively function as a receptor
      for VTs in vivo. The lethal kinetics were similar regardless of
      lipopolysaccharide elimination in VT preparation, suggesting that basal Gb3/CD77 
      levels are sufficient for lethal effects of VTs.
FAU - Okuda, Tetsuya
AU  - Okuda T
AD  - Department of Biochemistry II, Nagoya University School of Medicine, Tsurumai,
      Showa-ku, Nagoya 466-0065, Japan.
FAU - Tokuda, Noriyo
AU  - Tokuda N
FAU - Numata, Shin-ichiro
AU  - Numata S
FAU - Ito, Masafumi
AU  - Ito M
FAU - Ohta, Michio
AU  - Ohta M
FAU - Kawamura, Kumiko
AU  - Kawamura K
FAU - Wiels, Joelle
AU  - Wiels J
FAU - Urano, Takeshi
AU  - Urano T
FAU - Tajima, Orie
AU  - Tajima O
FAU - Furukawa, Keiko
AU  - Furukawa K
FAU - Furukawa, Koichi
AU  - Furukawa K
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20060213
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Cytokines)
RN  - 0 (Glycolipids)
RN  - 0 (Glycosphingolipids)
RN  - 0 (Interleukin-1)
RN  - 0 (Lipopolysaccharides)
RN  - 0 (Shiga Toxins)
RN  - 0 (Tumor Necrosis Factor-alpha)
RN  - EC 2.4.1.- (Galactosyltransferases)
RN  - EC 2.4.1.- (UDP-galactose-lactosylceramide alpha 1-4-galactosyltransferase)
SB  - IM
MH  - Animals
MH  - Blotting, Northern
MH  - Blotting, Southern
MH  - Brain/metabolism
MH  - Chromatography, Thin Layer
MH  - Cytokines/metabolism
MH  - Escherichia coli/pathogenicity
MH  - Female
MH  - Galactosyltransferases/metabolism/*physiology
MH  - *Gene Deletion
MH  - Gene Expression Regulation
MH  - *Gene Expression Regulation, Enzymologic
MH  - Genetic Vectors
MH  - Glycolipids/metabolism
MH  - Glycosphingolipids/*chemistry
MH  - Immunohistochemistry
MH  - Inflammation
MH  - Interleukin-1/metabolism
MH  - Kidney/metabolism
MH  - Kidney Tubules/metabolism
MH  - Kinetics
MH  - Lipopolysaccharides/chemistry/metabolism
MH  - Lymphocytes/metabolism
MH  - Male
MH  - Mice
MH  - Mice, Knockout
MH  - Microcirculation
MH  - Models, Genetic
MH  - Mutation
MH  - Recombination, Genetic
MH  - Reverse Transcriptase Polymerase Chain Reaction
MH  - Shiga Toxins/*chemistry
MH  - Time Factors
MH  - Tumor Necrosis Factor-alpha/metabolism
EDAT- 2006/02/16 09:00
MHDA- 2006/06/06 09:00
CRDT- 2006/02/16 09:00
PHST- 2006/02/16 09:00 [pubmed]
PHST- 2006/06/06 09:00 [medline]
PHST- 2006/02/16 09:00 [entrez]
AID - M600057200 [pii]
AID - 10.1074/jbc.M600057200 [doi]
PST - ppublish
SO  - J Biol Chem. 2006 Apr 14;281(15):10230-5. doi: 10.1074/jbc.M600057200. Epub 2006 
      Feb 13.

PMID- 10200296
OWN - NLM
STAT- MEDLINE
DCOM- 19990517
LR  - 20190501
IS  - 0027-8424 (Print)
IS  - 0027-8424 (Linking)
VI  - 96
IP  - 8
DP  - 1999 Apr 13
TI  - Reconstitution of functional L-selectin ligands on a cultured human endothelial
      cell line by cotransfection of alpha1-->3 fucosyltransferase VII and newly cloned
      GlcNAcbeta:6-sulfotransferase cDNA.
PG  - 4530-5
AB  - Recently, we proposed sialyl 6-sulfo Lewis X as a major carbohydrate-capping
      group of the L-selectin ligands on high endothelial venules in human lymph nodes.
      In this study we succeeded in reconstituting functional L-selectin ligands on a
      cultured human endothelial cell line, ECV304, by transfecting the
      alpha1-->3fucosyltranseferase VII (Fuc-T VII) and newly cloned
      GlcNAcbeta:6-sulfotransferase (6-Sul-T) cDNAs. The ECV304 cells transfected with 
      Fuc-T VII cDNA expressed conventional sialyl Lewis X detected with specific
      antibodies including 2H5, whereas the cells transfected with 6-Sul-T cDNA
      expressed sialyl 6-sulfo lactosamine as well as MECA-79-defined carbohydrate
      determinants, but these singly transfected cells failed to express sialyl 6-sulfo
      Lewis X, as detected with the antisialyl 6-sulfo Lewis X mAb G152. Sialyl 6-sulfo
      Lewis X appeared only on the cells that were cotransfected with both 6-Sul-T and 
      Fuc-T VII cDNAs. Significant adhesion of L-selectin-expressing cells was seen
      only to the doubly transfected ECV304 cells and was inhibited by G152. No
      adhesion was observed to the cells transfected either with 6-Sul-T or with Fuc-T 
      VII cDNA alone. The mRNAs of the two enzymes were expressed or were inducible
      upon interleukin 1 stimulation in human endothelial cells. These results indicate
      that a set of carbohydrate determinants synthesized by the concerted action of
      the two enzymes, as typically represented by the sialyl 6-sulfo Lewis X-capping
      group, serves as an essential component of the ligand for L-selectin and that the
      reagents 2H5 and MECA-79, utilized in earlier studies to detect L-selectin ligand
      on high endothelial venules, recognize two different aspects of the same set of
      synthetic products.
FAU - Kimura, N
AU  - Kimura N
AD  - Program of Experimental Pathology, Aichi Cancer Center, Nagoya 464-8681, Japan.
FAU - Mitsuoka, C
AU  - Mitsuoka C
FAU - Kanamori, A
AU  - Kanamori A
FAU - Hiraiwa, N
AU  - Hiraiwa N
FAU - Uchimura, K
AU  - Uchimura K
FAU - Muramatsu, T
AU  - Muramatsu T
FAU - Tamatani, T
AU  - Tamatani T
FAU - Kansas, G S
AU  - Kansas GS
FAU - Kannagi, R
AU  - Kannagi R
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Proc Natl Acad Sci U S A
JT  - Proceedings of the National Academy of Sciences of the United States of America
JID - 7505876
RN  - 0
      (5-acetylneuraminyl-(2-3)-galactosyl-(1-4)-(fucopyranosyl-(1-3))-N-acetylglucosam
      ine)
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (DNA, Complementary)
RN  - 0 (Oligosaccharides)
RN  - 126880-86-2 (L-Selectin)
RN  - EC 2.4.1.- (Fucosyltransferases)
RN  - EC 2.4.1.152 (galactoside 3-fucosyltransferase)
RN  - EC 2.8.2.- (Sulfotransferases)
RN  - EC 2.8.2.- (carbohydrate sulfotransferases)
SB  - IM
MH  - Antibodies, Monoclonal
MH  - Carbohydrate Sequence
MH  - Cell Line
MH  - Cloning, Molecular
MH  - DNA, Complementary
MH  - Endothelium, Vascular/cytology/*physiology
MH  - Fucosyltransferases/genetics/*metabolism
MH  - Genetic Variation
MH  - Humans
MH  - L-Selectin/*physiology
MH  - Lymph Nodes/immunology
MH  - Molecular Sequence Data
MH  - Oligosaccharides/*biosynthesis/chemistry/genetics
MH  - Sulfotransferases/genetics/*metabolism
MH  - Transfection
MH  - Umbilical Veins
PMC - PMC16366
EDAT- 1999/04/14 00:00
MHDA- 1999/04/14 00:01
CRDT- 1999/04/14 00:00
PHST- 1999/04/14 00:00 [pubmed]
PHST- 1999/04/14 00:01 [medline]
PHST- 1999/04/14 00:00 [entrez]
AID - 10.1073/pnas.96.8.4530 [doi]
PST - ppublish
SO  - Proc Natl Acad Sci U S A. 1999 Apr 13;96(8):4530-5. doi: 10.1073/pnas.96.8.4530.

PMID- 16630548
OWN - NLM
STAT- MEDLINE
DCOM- 20060622
LR  - 20081121
IS  - 0006-291X (Print)
IS  - 0006-291X (Linking)
VI  - 344
IP  - 2
DP  - 2006 Jun 2
TI  - The wbnH gene of Escherichia coli O86:H2 encodes an
      alpha-1,3-N-acetylgalactosaminyl transferase involved in the O-repeating unit
      biosynthesis.
PG  - 631-9
AB  - O-repeating unit biosynthesis is the first committed step in lipopolysaccharide
      (LPS) biosynthesis in a variety of gram-negative bacteria. The wbnH gene was
      previously proposed to encode a glycosyltransferase involved in O-repeating unit 
      synthesis in Escherichia coli O86:H2 strain. In this work, we provide biochemical
      evidence to show that wbnH encodes a N-acetylgalactosaminyl transferase (GalNAcT)
      that catalyzes the transfer of GalNAc from UDP-GalNAc to the
      GalNAc-pyrophosphate-lipid acceptor. WbnH activity was characterized using a
      synthetic acceptor substrate GalNAc alpha-PP-O(CH2)11-OPh. The resulting
      disaccharide product GalNAc-alpha-1,3-GalNAc alpha-PP-O(CH2)11-OPh was analyzed
      by LC-MS and NMR spectroscopy. Substrate specificity study indicates that
      pyrophosphate and hydrophobic lipid moiety are structural requirements for WbnH
      activity. Divalent metal cations are not required for enzyme catalysis,
      suggesting WbnH belongs to glycosyltransferase GT-B superfamily. Our results
      complete the characterization of O86 O-unit assembly pathway, and provide the
      access of chemically defined O-unit substrates for the further investigation of
      O-antigen biosynthetic mechanism.
FAU - Yi, Wen
AU  - Yi W
AD  - Department of Chemistry, The Ohio State University, Columbus, OH 43210, USA.
FAU - Yao, Qingjia
AU  - Yao Q
FAU - Zhang, Yalong
AU  - Zhang Y
FAU - Motari, Edwin
AU  - Motari E
FAU - Lin, Steven
AU  - Lin S
FAU - Wang, Peng George
AU  - Wang PG
LA  - eng
GR  - R01 AI44040/AI/NIAID NIH HHS/United States
PT  - Journal Article
PT  - Research Support, N.I.H., Extramural
PT  - Research Support, Non-U.S. Gov't
DEP - 20060407
PL  - United States
TA  - Biochem Biophys Res Commun
JT  - Biochemical and biophysical research communications
JID - 0372516
RN  - 0 (Escherichia coli Proteins)
RN  - EC 2.4.1.- (N-Acetylgalactosaminyltransferases)
RN  - EC 2.4.1.- (alpha-1,3-N-acetylgalactosaminyl transferase, E coli)
SB  - IM
MH  - Escherichia coli/*genetics
MH  - Escherichia coli Proteins/*genetics
MH  - Gene Expression Regulation, Bacterial/*genetics
MH  - Gene Expression Regulation, Enzymologic/*genetics
MH  - N-Acetylgalactosaminyltransferases/*genetics
MH  - Promoter Regions, Genetic/genetics
MH  - Protein Biosynthesis/*genetics
MH  - Repetitive Sequences, Nucleic Acid/genetics
EDAT- 2006/04/25 09:00
MHDA- 2006/06/23 09:00
CRDT- 2006/04/25 09:00
PHST- 2006/03/22 00:00 [received]
PHST- 2006/03/24 00:00 [accepted]
PHST- 2006/04/25 09:00 [pubmed]
PHST- 2006/06/23 09:00 [medline]
PHST- 2006/04/25 09:00 [entrez]
AID - S0006-291X(06)00708-X [pii]
AID - 10.1016/j.bbrc.2006.03.181 [doi]
PST - ppublish
SO  - Biochem Biophys Res Commun. 2006 Jun 2;344(2):631-9. doi:
      10.1016/j.bbrc.2006.03.181. Epub 2006 Apr 7.

PMID- 16251947
OWN - NLM
STAT- MEDLINE
DCOM- 20051123
LR  - 20070609
IS  - 1476-4687 (Electronic)
IS  - 0028-0836 (Linking)
VI  - 437
IP  - 7063
DP  - 2005 Oct 27
TI  - Protein glycosylation: chaperone mutation in Tn syndrome.
PG  - 1252
AB  - Tn syndrome is a rare autoimmune disease in which subpopulations of blood cells
      in all lineages carry an incompletely glycosylated membrane glycoprotein, known
      as the Tn antigen. This truncated antigen has the sugar N-acetylgalactosamine
      alpha-linked to either a serine or threonine amino-acid residue, whereas the
      correct T antigen has an additional terminal galactose; the defect may be due to 
      a malfunction of the glycosylating enzyme T-synthase. Here we show that Tn
      syndrome is associated with a somatic mutation in Cosmc, a gene on the X
      chromosome that encodes a molecular 'chaperone' that is required for the proper
      folding and hence full activity of T-synthase. The production of the autoimmune
      Tn antigen by a glycosyltransferase enzyme rendered defective by a disabled
      chaperone may have implications for other Tn-related disorders such as IgA
      nephropathy, a condition that can result in renal failure.
FAU - Ju, Tongzhong
AU  - Ju T
AD  - Department of Biochemistry and Molecular Biology, and Oklahoma Center for Medical
      Glycobiology, University of Oklahoma Health Sciences Center, Oklahoma City,
      Oklahoma 73104, USA.
FAU - Cummings, Richard D
AU  - Cummings RD
LA  - eng
PT  - Journal Article
PL  - England
TA  - Nature
JT  - Nature
JID - 0410462
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (C1GALT1C1 protein, human)
RN  - 0 (Molecular Chaperones)
RN  - 0 (Tn antigen)
RN  - EC 2.4.1.- (C1GALT1 protein, human)
RN  - EC 2.4.1.- (Galactosyltransferases)
SB  - IM
MH  - Alleles
MH  - Antigens, Tumor-Associated, Carbohydrate/chemistry/*metabolism
MH  - Autoimmune Diseases/*genetics/*metabolism
MH  - Female
MH  - Galactosyltransferases/chemistry/*metabolism
MH  - Genetic Diseases, X-Linked/genetics
MH  - Glycosylation
MH  - Humans
MH  - Male
MH  - Molecular Chaperones/*genetics/metabolism
MH  - Mutation/*genetics
MH  - Syndrome
EDAT- 2005/10/28 09:00
MHDA- 2005/12/13 09:00
CRDT- 2005/10/28 09:00
PHST- 2005/10/28 09:00 [pubmed]
PHST- 2005/12/13 09:00 [medline]
PHST- 2005/10/28 09:00 [entrez]
AID - 4371252a [pii]
AID - 10.1038/4371252a [doi]
PST - ppublish
SO  - Nature. 2005 Oct 27;437(7063):1252. doi: 10.1038/4371252a.

PMID- 16239572
OWN - NLM
STAT- MEDLINE
DCOM- 20051206
LR  - 20181113
IS  - 0019-9567 (Print)
IS  - 0019-9567 (Linking)
VI  - 73
IP  - 11
DP  - 2005 Nov
TI  - Variations in Helicobacter pylori lipopolysaccharide to evade the innate immune
      component surfactant protein D.
PG  - 7677-86
AB  - Helicobacter pylori is a common and persistent human pathogen of the gastric
      mucosa. Surfactant protein D (SP-D), a component of innate immunity, is expressed
      in the human gastric mucosa and is capable of aggregating H. pylori. Wide
      variation in the SP-D binding affinity to H. pylori has been observed in clinical
      isolates and laboratory-adapted strains. The aim of this study was to reveal
      potential mechanisms responsible for evading SP-D binding and establishing
      persistent infection. An escape variant, J178V, was generated in vitro, and the
      lipopolysaccharide (LPS) structure of the variant was compared to that of the
      parental strain, J178. The genetic basis for structural variation was explored by
      sequencing LPS biosynthesis genes. SP-D binding to clinical isolates was
      demonstrated by fluorescence-activated cell sorter analyses. Here, we show that
      H. pylori evades SP-D binding through phase variation in lipopolysaccharide. This
      phenomenon is linked to changes in the fucosylation of the O chain, which was
      concomitant with slipped-strand mispairing in a poly(C) tract of the
      fucosyltransferase A (fucT1) gene. SP-D binding organisms are predominant in
      mucus in vivo (P = 0.02), suggesting that SP-D facilitates physical elimination. 
      Phase variation to evade SP-D contributes to the persistence of this common
      gastric pathogen.
FAU - Khamri, Wafa
AU  - Khamri W
AD  - Imperial College Faculty of Medicine, St Mary's Campus, Norfolk Place, London, W2
      1PG, United Kingdom. wafa.khamri@imperial.ac.uk
FAU - Moran, Anthony P
AU  - Moran AP
FAU - Worku, Mulugeta L
AU  - Worku ML
FAU - Karim, Q Najma
AU  - Karim QN
FAU - Walker, Marjorie M
AU  - Walker MM
FAU - Annuk, Heidi
AU  - Annuk H
FAU - Ferris, John A
AU  - Ferris JA
FAU - Appelmelk, Ben J
AU  - Appelmelk BJ
FAU - Eggleton, Paul
AU  - Eggleton P
FAU - Reid, Kenneth B M
AU  - Reid KB
FAU - Thursz, Mark R
AU  - Thursz MR
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Infect Immun
JT  - Infection and immunity
JID - 0246127
RN  - 0 (Lipopolysaccharides)
RN  - 0 (Pulmonary Surfactant-Associated Protein D)
SB  - IM
MH  - Carbohydrate Sequence
MH  - Helicobacter Infections/immunology/microbiology
MH  - Helicobacter pylori/chemistry/*immunology
MH  - Humans
MH  - *Immunity, Innate
MH  - Lipopolysaccharides/*chemistry/*immunology
MH  - Molecular Sequence Data
MH  - Polymorphism, Restriction Fragment Length
MH  - Protein Binding
MH  - Pulmonary Surfactant-Associated Protein D/*immunology
PMC - PMC1273859
EDAT- 2005/10/22 09:00
MHDA- 2005/12/13 09:00
CRDT- 2005/10/22 09:00
PHST- 2005/10/22 09:00 [pubmed]
PHST- 2005/12/13 09:00 [medline]
PHST- 2005/10/22 09:00 [entrez]
AID - 73/11/7677 [pii]
AID - 10.1128/IAI.73.11.7677-7686.2005 [doi]
PST - ppublish
SO  - Infect Immun. 2005 Nov;73(11):7677-86. doi: 10.1128/IAI.73.11.7677-7686.2005.

PMID- 8978086
OWN - NLM
STAT- MEDLINE
DCOM- 19970117
LR  - 20181130
IS  - 0378-1097 (Print)
IS  - 0378-1097 (Linking)
VI  - 145
IP  - 3
DP  - 1996 Dec 15
TI  - The identification a novel gene required for lipopolysaccharide biosynthesis by
      Haemophilus influenzae RM7004, using transposon Tn916 mutagenesis.
PG  - 325-31
AB  - Mutagenesis with the transposon Tn916 was used as a strategy to identify genes
      required for synthesis of the Gal alpha (1-4) beta Gal component of Haemophilus
      influenzae strain RM7004 lipopolysaccharide. Insertion of Tn916 into an open
      reading frame (ORF) encoding a protein with 75% homology to the Escherichia coli 
      methionine related protein (Mrp) is described. Mutations in mrp resulted in loss 
      of reactivity with monoclonal antibody (mAb) 4C4, which recognises Gal alpha
      (1-4) beta Gal, and expression of LPS with a different electrophoretic profile to
      that of wild-type RM7004. An unexpected feature of this mutation was that it
      appeared to influence the number of copies of 5'-CAAT-3' present in lic2A, a gene
      which is also required for biosynthesis and phase variable expression of the Gal 
      alpha (1-4) beta Gal LPS epitope.
FAU - High, N J
AU  - High NJ
AD  - Dept. of Paediatrics, University of Oxford, John Radcliffe Hospital, Headington, 
      UK.
FAU - Deadman, M E
AU  - Deadman ME
FAU - Hood, D W
AU  - Hood DW
FAU - Moxon, E R
AU  - Moxon ER
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - FEMS Microbiol Lett
JT  - FEMS microbiology letters
JID - 7705721
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Bacterial Proteins)
RN  - 0 (DNA Transposable Elements)
RN  - 0 (DNA, Bacterial)
RN  - 0 (Lipopolysaccharides)
SB  - IM
MH  - Antibodies, Monoclonal
MH  - Bacterial Proteins/genetics/immunology/metabolism
MH  - Bacteriological Techniques
MH  - Base Sequence
MH  - Blotting, Southern
MH  - Chromosomes, Bacterial/genetics
MH  - DNA Transposable Elements/*genetics
MH  - DNA, Bacterial/genetics
MH  - Enhancer Elements, Genetic/genetics
MH  - Genes, Bacterial/*genetics
MH  - Genetic Testing
MH  - Haemophilus influenzae/cytology/*genetics/metabolism
MH  - Lipopolysaccharides/*biosynthesis
MH  - Molecular Sequence Data
MH  - Mutagenesis/physiology
MH  - Plasmids
MH  - Polymerase Chain Reaction
MH  - Restriction Mapping
MH  - Sequence Analysis, DNA
MH  - Sequence Homology, Amino Acid
EDAT- 1996/12/15 00:00
MHDA- 1996/12/15 00:01
CRDT- 1996/12/15 00:00
PHST- 1996/12/15 00:00 [pubmed]
PHST- 1996/12/15 00:01 [medline]
PHST- 1996/12/15 00:00 [entrez]
AID - S0378109796004223 [pii]
AID - 10.1111/j.1574-6968.1996.tb08596.x [doi]
PST - ppublish
SO  - FEMS Microbiol Lett. 1996 Dec 15;145(3):325-31. doi:
      10.1111/j.1574-6968.1996.tb08596.x.

PMID- 9414130
OWN - NLM
STAT- MEDLINE
DCOM- 19980116
LR  - 20061115
IS  - 0014-5793 (Print)
IS  - 0014-5793 (Linking)
VI  - 418
IP  - 1-2
DP  - 1997 Nov 24
TI  - Preparation of peptides which mimic glycosphingolipids by using phage peptide
      library and their modulation on beta-galactosidase activity.
PG  - 219-23
AB  - We describe the use of a phage-displayed random pentadecamer peptide library for 
      searching glycosphingolipid mimicking peptides. Two phage clones (AD-1 and AD-2) 
      were selected by biopanning using monoclonal antibody AD117m, directed to
      lactotetraosylceramide (Lc4Cer). The amino acid sequences of the selected clones 
      showed high homology (VPPXFXXXY) in 9-mer. Three phage clones were selected by
      using monoclonal antibody H11, directed to neolactotetraosylceramide (nLc4Cer),
      the linkage isomer of Lc4Cer, and the displayed amino acid sequences were
      compared. One of these peptides showed the same amino acid sequence as that of
      AD-2 except for one amino acid substitution. Pentadecamer, 9-mer and point
      mutated 9-mer peptides were synthesized on the basis of the displayed amino acid 
      sequences. Binding activity of the peptides to the monoclonal antibodies or
      Ricinus communis lectin showed that 9-mer peptides are enough to mimic the
      epitope carbohydrate structure. Furthermore, six of the synthesized peptides
      inhibited Jack bean beta-galactosidase activity towards nLc4Cer at a high
      concentration of the enzyme, whereas at lower enzyme concentrations some peptides
      showed potent activation of the enzyme activity. This is the first report of
      carbohydrate mimicking peptides which modulate glycosidase activity.
FAU - Taki, T
AU  - Taki T
AD  - Department of Biochemistry, School of Medicine, Tokyo Medical and Dental
      University, Japan.
FAU - Ishikawa, D
AU  - Ishikawa D
FAU - Hamasaki, H
AU  - Hamasaki H
FAU - Handa, S
AU  - Handa S
LA  - eng
PT  - Comparative Study
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - FEBS Lett
JT  - FEBS letters
JID - 0155157
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Ceramides)
RN  - 0 (Glycosphingolipids)
RN  - 0 (Oligodeoxyribonucleotides)
RN  - 0 (Oligopeptides)
RN  - 0 (Peptide Library)
RN  - 0 (Plant Lectins)
RN  - 9009-86-3 (Ricin)
RN  - EC 3.2.1.23 (beta-Galactosidase)
SB  - IM
MH  - Amino Acid Sequence
MH  - Antibodies, Monoclonal
MH  - Bacteriophages
MH  - Base Sequence
MH  - Carbohydrate Sequence
MH  - Ceramides/*chemistry/pharmacology
MH  - Consensus Sequence
MH  - Fabaceae/enzymology
MH  - Glycosphingolipids/*chemistry/pharmacology
MH  - Kinetics
MH  - Molecular Sequence Data
MH  - Oligodeoxyribonucleotides
MH  - Oligopeptides/*chemistry/*pharmacology
MH  - *Peptide Library
MH  - Plant Lectins
MH  - Plants, Medicinal
MH  - Ricin/chemistry/pharmacology
MH  - Sequence Alignment
MH  - beta-Galactosidase/*antagonists & inhibitors
EDAT- 1997/12/31 00:00
MHDA- 1997/12/31 00:01
CRDT- 1997/12/31 00:00
PHST- 1997/12/31 00:00 [pubmed]
PHST- 1997/12/31 00:01 [medline]
PHST- 1997/12/31 00:00 [entrez]
AID - S0014-5793(97)01386-0 [pii]
PST - ppublish
SO  - FEBS Lett. 1997 Nov 24;418(1-2):219-23.

PMID- 1422133
OWN - NLM
STAT- MEDLINE
DCOM- 19921210
LR  - 20181113
IS  - 0282-0080 (Print)
IS  - 0282-0080 (Linking)
VI  - 9
IP  - 3
DP  - 1992 Jun
TI  - Application of chemically desialylated and degalactosylated human glycophorin for
      induction and characterization of anti-Tn monoclonal antibodies.
PG  - 148-53
AB  - Human erythrocyte glycophorin was desialylated by mild acid hydrolysis and
      degalactosylated by Smith degradation. Two monoclonal antibodies (Tn5 and Tn56)
      obtained by immunization of mice with this 'artificial' Tn antigen were
      characterized and compared in some experiments with two antibodies (BRIC111 and
      LM225) obtained in other laboratories by immunization with Tn erythrocytes. The
      specific binding of the antibodies to glycophorins desialylated and
      degalactosylated on the nitrocellulose blot and to
      asialo-agalactoglycophorin-coated ELISA plates, and reactions with authentic Tn
      antigen served for identification of their anti-Tn specificity. The antibodies
      were further characterized in inhibition assay with various glycoproteins. The
      antibody Tn5 (similar to BRIC111) was shown to be specific for human erythrocyte 
      Tn antigen, whereas Tn56 reacted strongly with different glycoproteins carrying
      O-linked GalNAc alpha- residues, and was strongly bound to the murine
      adenocarcinoma cell line Ta3-Ha. The antibodies Tn5, Tn56 and BRIC111 were
      similarly inhibited by ovine submaxillary mucin (OSM) and asialoOSM, but the
      antibody LM225 showed a distinct preference in reaction with OSM (sialosyl-Tn
      antigen). The results show that Tn antigen, obtained by chemical modifications of
      human glycophorin, enables the preparation and characterization of anti-Tn
      monoclonal antibodies, without using rare Tn erythrocytes.
FAU - Duk, M
AU  - Duk M
AD  - Department of Immunochemistry, Institute of Immunology and Experimental Therapy, 
      Wroclaw, Poland.
FAU - Steuden, I
AU  - Steuden I
FAU - Dus, D
AU  - Dus D
FAU - Radzikowski, C
AU  - Radzikowski C
FAU - Lisowska, E
AU  - Lisowska E
LA  - eng
PT  - Journal Article
PL  - United States
TA  - Glycoconj J
JT  - Glycoconjugate journal
JID - 8603310
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens, Neoplasm)
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Glycophorin)
RN  - 0 (Sialic Acids)
RN  - 0 (Tn antigen)
RN  - GZP2782OP0 (N-Acetylneuraminic Acid)
RN  - X2RN3Q8DNE (Galactose)
SB  - IM
MH  - Antibodies, Monoclonal
MH  - Antigens, Neoplasm/chemistry/*immunology
MH  - *Antigens, Tumor-Associated, Carbohydrate
MH  - Blotting, Western
MH  - Enzyme-Linked Immunosorbent Assay
MH  - Erythrocyte Membrane/*immunology/pathology
MH  - Flow Cytometry
MH  - Galactose/deficiency
MH  - Glycophorin/chemistry/*immunology
MH  - Hemagglutination Tests
MH  - Humans
MH  - N-Acetylneuraminic Acid
MH  - Sialic Acids/deficiency
MH  - Tumor Cells, Cultured
EDAT- 1992/06/01 00:00
MHDA- 1992/06/01 00:01
CRDT- 1992/06/01 00:00
PHST- 1992/06/01 00:00 [pubmed]
PHST- 1992/06/01 00:01 [medline]
PHST- 1992/06/01 00:00 [entrez]
PST - ppublish
SO  - Glycoconj J. 1992 Jun;9(3):148-53.

PMID- 15944793
OWN - NLM
STAT- MEDLINE
DCOM- 20050915
LR  - 20151119
IS  - 1021-335X (Print)
IS  - 1021-335X (Linking)
VI  - 14
IP  - 1
DP  - 2005 Jul
TI  - Simple mucin-type cancer associated antigens are pre-cancerous biomarkers during 
      1,2-dimethylhydrazine-induced rat colon carcinogenesis.
PG  - 219-27
AB  - The simple mucin-type truncated O-glycans Tn (GalNAc-O-Ser/Thr) and sialyl-Tn
      (STn) antigens are useful diagnostic markers for human colon cancer. We herein
      report the characterization of 1,2-dimethylhidrazine (DMH)-induced colon cancer
      in rats as a new model for the study of aberrant O-glycosylation products during 
      carcinogenesis. Evaluated by immunohistochemistry, both anti-Tn and anti-STn MAbs
      revealed no staining of normal colonic mucosa. On the contrary, Tn and STn were
      expressed by the first lesions detected following carcinogen administration
      (aberrant crypt foci), observing the most intense and uniform pattern in crypts
      with severe dysplasia. Adenocarcinomas with non-secreting components showed
      moderately and strong stain, but mucin-secreting carcinomas were mildly stained. 
      The biochemical characterization of soluble Tn glycoproteins from ascitic fluids 
      of rats with colon cancer revealed that Tn is bearing high molecular weight
      glycoproteins (containing sialic acid and/or GlcNAc and GalNAc), which migrated
      as two major components (one of approximately 220 kDa and other>500 kDa).
      Evaluated by CsCl gradient ultracentrifugation and perchloric acid precipitation,
      it was shown that Tn is carried for mucins. These results indicate that Tn and
      STn are pre-cancerous biomarkers in colon of rats treated with DMH. This model of
      rat colon cancer could be useful to study in vivo the temporal sequence of
      molecular events responsible for the deregulation of O-glycosylation pathways
      during colon carcinogenesis, and could contribute to improve the evaluation of
      diagnostic and therapeutic strategies based on the utilization of Tn and STn
      antigens.
FAU - Berriel, Edgardo
AU  - Berriel E
AD  - Clinica Quirurgica F, Hospital de Clinicas, Facultad de Medicina, Universidad de 
      la Republica, Montevideo, Uruguay.
FAU - Hill, Marcelo
AU  - Hill M
FAU - Barcia, Juan J
AU  - Barcia JJ
FAU - Ubillos, Luis
AU  - Ubillos L
FAU - Gonzalez, Mariela
AU  - Gonzalez M
FAU - Detjen, Gisselle
AU  - Detjen G
FAU - Rondan, Mariella
AU  - Rondan M
FAU - Navarrete, Hector
AU  - Navarrete H
FAU - Osinaga, Eduardo
AU  - Osinaga E
LA  - eng
PT  - Journal Article
PL  - Greece
TA  - Oncol Rep
JT  - Oncology reports
JID - 9422756
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Biomarkers, Tumor)
RN  - 0 (Dimethylhydrazines)
RN  - 0 (Glycoproteins)
RN  - 0 (Mucins)
RN  - 0 (Tn antigen)
RN  - 0 (sialosyl-Tn antigen)
SB  - IM
MH  - Animals
MH  - Antigens, Tumor-Associated, Carbohydrate/*analysis
MH  - Biomarkers, Tumor/*analysis
MH  - Colon/chemistry/drug effects/pathology
MH  - Colonic Neoplasms/chemically induced/metabolism/*pathology
MH  - Diagnosis, Differential
MH  - Dimethylhydrazines
MH  - Female
MH  - Glycoproteins/metabolism
MH  - Immunohistochemistry
MH  - Mucins/*analysis
MH  - Precancerous Conditions/metabolism/*pathology
MH  - Rats
MH  - Rats, Wistar
EDAT- 2005/06/10 09:00
MHDA- 2005/09/16 09:00
CRDT- 2005/06/10 09:00
PHST- 2005/06/10 09:00 [pubmed]
PHST- 2005/09/16 09:00 [medline]
PHST- 2005/06/10 09:00 [entrez]
PST - ppublish
SO  - Oncol Rep. 2005 Jul;14(1):219-27.

PMID- 438154
OWN - NLM
STAT- MEDLINE
DCOM- 19790725
LR  - 20061115
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 254
IP  - 10
DP  - 1979 May 25
TI  - Developmental change and genetic defect in the carbohydrate structure of band 3
      glycoprotein of human erythrocyte membrane.
PG  - 3700-3
AB  - The chemical structure of Band 3 glycopeptide prepared from erythrocytes of
      normal adult (blood group OI), umbilical cord vessels (Oi), and an i adult
      variant who fails to develop I antigen (Oi), has been compared. Band 3
      glycopeptide of cord erythrocytes gave, on permethylation analysis, predominantly
      2,4,6-tri-O-methylgalactose and
      3,6-di-O-methyl-2-N-methylacetamido-2-deoxyglucose, whereas the same glycopeptide
      of normal adult erythrocytes gave much higher amounts of
      2,3,4,6-tetra-O-methylgalactose and 2,4-di-O-methylgalactose as compared with
      that of cord erythrocytes. Band 3 glycopeptide from i adult showed the same
      methylation pattern as cord-Band 3 glycopeptide. In accordance with these
      results, Band 3 glycopeptide of cord and i adult erythrocytes were hydrolyzed to 
      mostly small oligosaccharides by endo-beta-galactosidase from Escherichia
      freundii, whereas that of normal adult produced a number of oligosaccharides with
      various sizes which was caused by branched structures. Based on these results and
      structures of released oligosaccharides, the major developmental change of
      carbohydrate structure in the erythrocyte membrane is the conversion of linear
      repeating Galbeta1 leads to 4GlcNAcbeta1 leads to 3Gal to a branched Galbeta 1
      leads to 4GlcNAcbeta 1 leads to 3 (R leads to 6) Gal structure. i individual may 
      result from the lack of the branching enzyme.
FAU - Fukuda, M
AU  - Fukuda M
FAU - Fukuda, M N
AU  - Fukuda MN
FAU - Hakomori, S
AU  - Hakomori S
LA  - eng
PT  - Journal Article
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Carbohydrates)
RN  - 0 (Glycoproteins)
RN  - 0 (Oligosaccharides)
SB  - IM
MH  - Carbohydrates/analysis
MH  - Chromatography, Gas
MH  - Erythrocyte Membrane/*metabolism
MH  - Erythrocytes/*metabolism
MH  - Glycoproteins/*blood/genetics
MH  - Humans
MH  - Oligosaccharides/analysis
EDAT- 1979/05/25 00:00
MHDA- 1979/05/25 00:01
CRDT- 1979/05/25 00:00
PHST- 1979/05/25 00:00 [pubmed]
PHST- 1979/05/25 00:01 [medline]
PHST- 1979/05/25 00:00 [entrez]
PST - ppublish
SO  - J Biol Chem. 1979 May 25;254(10):3700-3.

PMID- 3667566
OWN - NLM
STAT- MEDLINE
DCOM- 19871214
LR  - 20190510
IS  - 0021-924X (Print)
IS  - 0021-924X (Linking)
VI  - 102
IP  - 1
DP  - 1987 Jul
TI  - Application of liposomes to generation of monoclonal antibody to
      glycosphingolipid: production of monoclonal antibody to GgOse4Cer.
PG  - 59-67
AB  - Liposomes were applied to the immunization with GgOse4Cer and screening for
      production of monoclonal antibody to GgOse4Cer. Four-week-old and 22-week-old
      Balb/c mice were immunized with GgOse4Cer and Salmonella minnesota R595
      lipopolysaccharides incorporated liposomes which were composed of
      dipalmitoyl-phosphatidylcholine and cholesterol. Since antibody response to
      GgOse4Cer was higher in 22-week-old than 4-week-old Balb/c mice after
      immunization, 22-week-old Balb/c mice were used for the immunization prior to
      generation of the monoclonal antibodies to GgOse4Cer. The screening of monoclonal
      antibodies was performed by complement-dependent liposome immune lysis assay
      using GgOse4Cer-containing liposomes. Six kinds of monoclonal antibodies, AG-1,
      -2, -3, -4, -5, and -6, of the IgM class were established. The specificities of
      the monoclonal antibodies obtained were defined by complement-dependent liposome 
      immune lysis assay using various glycosphingolipids incorporated in liposomes and
      by thin-layer chromatography (TLC) with immunostaining. All of the monoclonal
      antibodies reacted only with GgOse4Cer in the liposome immune lysis assay. In
      addition, the monoclonal antibodies reacted only with GgOse4Cer in the TLC
      immunostaining. However, none of the monoclonal antibodies obtained was capable
      of removing natural killer activity from C3H/He mice spleen cell suspensions in
      vitro. Liposomes may be useful in the procedures of immunization and screening
      for generation of antiserum and monoclonal antibody to GSLs.
FAU - Watarai, S
AU  - Watarai S
AD  - Laboratory of Biological Products, University of Tokyo.
FAU - Handa, S
AU  - Handa S
FAU - Tadakuma, T
AU  - Tadakuma T
FAU - Yasuda, T
AU  - Yasuda T
LA  - eng
PT  - Journal Article
PL  - England
TA  - J Biochem
JT  - Journal of biochemistry
JID - 0376600
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigen-Antibody Complex)
RN  - 0 (G(A1) ganglioside)
RN  - 0 (Gangliosides)
RN  - 0 (Glycosphingolipids)
RN  - 0 (Immunoglobulin M)
RN  - 0 (Liposomes)
SB  - IM
MH  - Animals
MH  - *Antibodies, Monoclonal
MH  - Antigen-Antibody Complex
MH  - Gangliosides
MH  - Glycosphingolipids/*analysis/*blood/immunology
MH  - Humans
MH  - Immunoglobulin M
MH  - Killer Cells, Natural/immunology
MH  - *Liposomes
MH  - Mice
MH  - Mice, Inbred BALB C
MH  - Mice, Inbred C3H
MH  - Structure-Activity Relationship
EDAT- 1987/07/01 00:00
MHDA- 1987/07/01 00:01
CRDT- 1987/07/01 00:00
PHST- 1987/07/01 00:00 [pubmed]
PHST- 1987/07/01 00:01 [medline]
PHST- 1987/07/01 00:00 [entrez]
AID - 10.1093/oxfordjournals.jbchem.a122041 [doi]
PST - ppublish
SO  - J Biochem. 1987 Jul;102(1):59-67. doi: 10.1093/oxfordjournals.jbchem.a122041.

PMID- 16091596
OWN - NLM
STAT- MEDLINE
DCOM- 20050929
LR  - 20071219
IS  - 0021-924X (Print)
IS  - 0021-924X (Linking)
VI  - 138
IP  - 2
DP  - 2005 Aug
TI  - Characterization of wheat germ agglutinin ligand on soluble glycoproteins in
      Caenorhabditis elegans.
PG  - 209-13
AB  - Some mutants of Caenorhabditis elegans show altered patterns of ectopic binding
      with wheat germ agglutinin (WGA). Some of these mutants also have defects of
      morphogenesis and movement during development. To clarify the structures of
      WGA-ligands in C. elegans that may be involved in developmental events, we have
      analyzed glycan structures capable of binding WGA. We isolated glycoproteins from
      wild-type C. elegans by WGA-affinity chromatography, and analyzed their glycan
      structures by a combination of hydrazine degradation and fluorescent labeling.
      The glycoproteins had oligomannose-type and complex-type N-glycans that included 
      agalacto-biantenna and agalacto-tetraantenna glycans. Although the complex-type
      glycans carried beta-GlcNAc residues at their non-reducing ends, they did not
      bind to the WGA-agarose-resin. Thus, it was suggested that these N-glycans were
      not responsible for WGA-binding of the isolated glycoproteins. Hydrazinolysis of 
      the glycoproteins also released a considerable amount of GalNAc monosaccharide.
      It was surmised that N-acetylgalactosamine was derived from mucin-type O-glycans 
      with the Tn-antigen structure (GalNAcalpha1-O-Ser/Thr). WGA-blotting assay of
      neoglycoproteins revealed that a cluster of Tn-antigens was a good ligand for
      WGA. These results suggested that the WGA-ligand in C. elegans is a cluster of
      alpha-GalNAc monosaccharides linked to mucin-like glycoprotein(s). The
      observations reported in this paper emphasize the possible significance of
      mucin-type O-glycans in the development of a multicellular organism.
FAU - Natsuka, Shunji
AU  - Natsuka S
AD  - Department of Chemistry, Graduate School of Science, Osaka University, Toyonaka.
FAU - Kawaguchi, Masahumi
AU  - Kawaguchi M
FAU - Wada, Yukiko
AU  - Wada Y
FAU - Ichikawa, Akira
AU  - Ichikawa A
FAU - Ikura, Koji
AU  - Ikura K
FAU - Hase, Sumihiro
AU  - Hase S
LA  - eng
PT  - Journal Article
PL  - England
TA  - J Biochem
JT  - Journal of biochemistry
JID - 0376600
RN  - 0 (Caenorhabditis elegans Proteins)
RN  - 0 (Glycoproteins)
RN  - 0 (Ligands)
RN  - 0 (Mucins)
RN  - 0 (Polysaccharides)
RN  - 0 (Wheat Germ Agglutinins)
SB  - IM
MH  - Animals
MH  - Caenorhabditis elegans/*chemistry
MH  - Caenorhabditis elegans Proteins/*chemistry
MH  - Carbohydrate Sequence
MH  - Electrophoresis, Polyacrylamide Gel
MH  - Glycoproteins/*chemistry
MH  - Ligands
MH  - Molecular Sequence Data
MH  - Mucins
MH  - Polysaccharides/*analysis
MH  - Solubility
MH  - Structure-Activity Relationship
MH  - Wheat Germ Agglutinins/*metabolism
EDAT- 2005/08/11 09:00
MHDA- 2005/09/30 09:00
CRDT- 2005/08/11 09:00
PHST- 2005/08/11 09:00 [pubmed]
PHST- 2005/09/30 09:00 [medline]
PHST- 2005/08/11 09:00 [entrez]
AID - 138/2/209 [pii]
AID - 10.1093/jb/mvi117 [doi]
PST - ppublish
SO  - J Biochem. 2005 Aug;138(2):209-13. doi: 10.1093/jb/mvi117.

PMID- 3162916
OWN - NLM
STAT- MEDLINE
DCOM- 19880527
LR  - 20190501
IS  - 0021-9746 (Print)
IS  - 0021-9746 (Linking)
VI  - 41
IP  - 3
DP  - 1988 Mar
TI  - Expression of CEA, CA125, CA19-9 and human milk fat globule membrane antigen in
      ovarian tumours.
PG  - 260-4
AB  - The expression of five different antigens in ovarian tumours was studied by means
      of an immunohistochemical test with anti-CEA, HMFG1 and HMFG2, NS19-9 and OC125
      antibodies. Considerable variation was noted not only between different
      histological types and between tumours of one type but also between areas in a
      single tumour. HMFG1 and HMFG2 were the most reactive of all the antibodies;
      NS19-9 and OC125 were expressed by different populations of cells. It is
      concluded that specific combinations of antibodies are more effective both for
      the monitoring of ovarian cancer as well as for immunodiagnosis and treatment,
      than any single one used.
FAU - Macdonald, F
AU  - Macdonald F
AD  - Surgical Immunology Unit, Queen Elizabeth Hospital, Birmingham.
FAU - Bird, R
AU  - Bird R
FAU - Stokes, H
AU  - Stokes H
FAU - Russell, B
AU  - Russell B
FAU - Crocker, J
AU  - Crocker J
LA  - eng
PT  - Journal Article
PL  - England
TA  - J Clin Pathol
JT  - Journal of clinical pathology
JID - 0376601
RN  - 0 (Antigens, Neoplasm)
RN  - 0 (Antigens, Surface)
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Biomarkers, Tumor)
RN  - 0 (Carcinoembryonic Antigen)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Mucin-1)
SB  - AIM
SB  - IM
MH  - Adenocarcinoma/immunology
MH  - Antigens, Neoplasm/*analysis
MH  - Antigens, Surface/*analysis
MH  - Antigens, Tumor-Associated, Carbohydrate
MH  - Biomarkers, Tumor/*analysis
MH  - Carcinoembryonic Antigen/*analysis
MH  - Cystadenocarcinoma/immunology
MH  - Cystadenoma/immunology
MH  - Endometriosis/immunology
MH  - Female
MH  - Humans
MH  - Membrane Glycoproteins/*analysis
MH  - Mucin-1
MH  - Ovarian Neoplasms/*immunology/secondary
PMC - PMC1141420
EDAT- 1988/03/01 00:00
MHDA- 1988/03/01 00:01
CRDT- 1988/03/01 00:00
PHST- 1988/03/01 00:00 [pubmed]
PHST- 1988/03/01 00:01 [medline]
PHST- 1988/03/01 00:00 [entrez]
AID - 10.1136/jcp.41.3.260 [doi]
PST - ppublish
SO  - J Clin Pathol. 1988 Mar;41(3):260-4. doi: 10.1136/jcp.41.3.260.

PMID- 12146959
OWN - NLM
STAT- MEDLINE
DCOM- 20020905
LR  - 20081121
IS  - 0006-2960 (Print)
IS  - 0006-2960 (Linking)
VI  - 41
IP  - 31
DP  - 2002 Aug 6
TI  - Effect of glycosylation on MUC1 humoral immune recognition: NMR studies of MUC1
      glycopeptide-antibody interactions.
PG  - 9946-61
AB  - MUC1 mucin is a large transmembrane glycoprotein, of which the extracellular
      domain is formed by a repeating 20 amino acid sequence, GVTSAPDTRPAPGSTAPPAH. In 
      normal breast epithelial cells, the extracellular domain is densely covered with 
      highly branched complex carbohydrate structures. However, in neoplastic breast
      tissue, the extracellular domain is underglycosylated, resulting in the exposure 
      of a highly immunogenic core peptide epitope (PDTRP in bold above) as well as the
      normally cryptic core Tn (GalNAc), STn (sialyl alpha2-6 GalNAc), and TF (Gal
      beta1-3 GalNAc) carbohydrates. In the present study, NMR methods were used to
      correlate the effects of cryptic glycosylation outside of the PDTRP core epitope 
      region to the recognition and binding of a monoclonal antibody, Mab B27.29,
      raised against the intact tumor-associated MUC1 mucin. Four peptides were
      studied: a MUC1 16mer peptide of the sequence
      Gly1-Val2-Thr3-Ser4-Ala5-Pro6-Asp7-Thr8-Arg9-Pro10-Ala11-Pro12-Gly13-Ser14-Thr15-
      Ala16, two singly Tn-glycosylated versions of this peptide at either Thr3 or
      Ser4, and a doubly Tn-glycosylated version at both Thr3 and Ser4. The results of 
      these studies showed that the B27.29 MUC1 B-cell epitope maps to two separate
      parts of the glycopeptide, the core peptide epitope spanning the PDTRP sequence
      and a second (carbohydrate) epitope comprised of the Tn moieties attached at Thr3
      and Ser4. The implications of these results are discussed within the framework of
      developing a glycosylated second-generation MUC1 glycopeptide vaccine.
FAU - Grinstead, Jeffrey S
AU  - Grinstead JS
AD  - Department of Medicinal Chemistry, School of Pharmacy, University of Washington, 
      Seattle, WA 98195, USA.
FAU - Koganty, R Rao
AU  - Koganty RR
FAU - Krantz, Mark J
AU  - Krantz MJ
FAU - Longenecker, B Michael
AU  - Longenecker BM
FAU - Campbell, A Patricia
AU  - Campbell AP
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, Non-P.H.S.
PL  - United States
TA  - Biochemistry
JT  - Biochemistry
JID - 0370623
RN  - 0 (Mucin-1)
SB  - IM
MH  - Amino Acid Sequence
MH  - *Antigen-Antibody Reactions
MH  - Glycosylation
MH  - Molecular Sequence Data
MH  - Mucin-1/chemistry/*immunology
MH  - Nuclear Magnetic Resonance, Biomolecular
MH  - Temperature
EDAT- 2002/07/31 10:00
MHDA- 2002/09/06 10:01
CRDT- 2002/07/31 10:00
PHST- 2002/07/31 10:00 [pubmed]
PHST- 2002/09/06 10:01 [medline]
PHST- 2002/07/31 10:00 [entrez]
AID - bi012176z [pii]
PST - ppublish
SO  - Biochemistry. 2002 Aug 6;41(31):9946-61.

PMID- 15623485
OWN - NLM
STAT- MEDLINE
DCOM- 20050225
LR  - 20181113
IS  - 0021-9746 (Print)
IS  - 0021-9746 (Linking)
VI  - 58
IP  - 1
DP  - 2005 Jan
TI  - Distribution of HPV infection and tumour markers in cervical intraepithelial
      neoplasia from cone biopsies of Mozambican women.
PG  - 61-8
AB  - AIMS: To evaluate human papillomavirus (HPV) infection in whole cervical cone
      specimens with cervical intraepithelial neoplasia (CIN). In addition, to evaluate
      the relation between the presence of CIN lesions and HPV infection and the
      expression of Ki-67, p53, cytokeratins, Gp230 glycoprotein, and simple mucin-type
      carbohydrates. METHODS: Cervical cone specimens from five patients with CIN were 
      studied. For each specimen, serial sections encompassing the whole cone were
      collected (52 samples). HPV infection and HPV types were detected by the
      polymerase chain reaction and enzyme immunoassay. The expression of Ki-67, p53,
      cytokeratins, Gp230, and simple mucin-type carbohydrates was examined
      immunohistochemically. RESULTS: All cases showed high risk HPV types, namely
      types 16, 33, 35, and 58. Four of the five patients were infected by multiple
      viral types. HPV-58 was always seen in CIN III, whereas HPV-35 was more frequent 
      in CIN I. The expression of Ki-67 and p53 was higher in CIN III lesions. The
      expression of cytokeratins 8 and 17 showed complete or almost complete overlap
      with CIN III. Altered expression of Gp230, Tn, and sialyl-T was often seen in all
      grades of CIN. CONCLUSIONS: When whole cervical cone specimens are evaluated the 
      rate of multiple HPV infection is very high. The expression of cytokeratins 8 and
      17 is a useful marker of CIN III.
FAU - Carrilho, C
AU  - Carrilho C
AD  - Department of Pathology, Medical School, Eduardo Mondlane University, and Maputo 
      Central Hospital, Maputo, Mozambique.
FAU - Cirnes, L
AU  - Cirnes L
FAU - Alberto, M
AU  - Alberto M
FAU - Buane, L
AU  - Buane L
FAU - Mendes, N
AU  - Mendes N
FAU - David, L
AU  - David L
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - J Clin Pathol
JT  - Journal of clinical pathology
JID - 0376601
RN  - 0 (Biomarkers, Tumor)
RN  - 0 (Ki-67 Antigen)
RN  - 0 (Neoplasm Proteins)
RN  - 0 (Tumor Suppressor Protein p53)
RN  - 68238-35-7 (Keratins)
SB  - AIM
SB  - IM
MH  - Biomarkers, Tumor/*metabolism
MH  - Biopsy
MH  - Cervical Intraepithelial Neoplasia/metabolism/pathology/*virology
MH  - Female
MH  - Humans
MH  - Immunoenzyme Techniques
MH  - Keratins/metabolism
MH  - Ki-67 Antigen/metabolism
MH  - Mozambique
MH  - Neoplasm Proteins/metabolism
MH  - Papillomaviridae/classification/*isolation & purification/pathogenicity
MH  - Papillomavirus Infections/*complications
MH  - Polymerase Chain Reaction/methods
MH  - Tumor Suppressor Protein p53/metabolism
MH  - Uterine Cervical Neoplasms/metabolism/pathology/*virology
PMC - PMC1770547
EDAT- 2004/12/30 09:00
MHDA- 2005/02/26 09:00
CRDT- 2004/12/30 09:00
PHST- 2004/12/30 09:00 [pubmed]
PHST- 2005/02/26 09:00 [medline]
PHST- 2004/12/30 09:00 [entrez]
AID - 58/1/61 [pii]
AID - 10.1136/jcp.2004.020552 [doi]
PST - ppublish
SO  - J Clin Pathol. 2005 Jan;58(1):61-8. doi: 10.1136/jcp.2004.020552.

PMID- 8364861
OWN - NLM
STAT- MEDLINE
DCOM- 19931001
LR  - 20151119
IS  - 0008-543X (Print)
IS  - 0008-543X (Linking)
VI  - 72
IP  - 6
DP  - 1993 Sep 15
TI  - Predictive value of preoperative serum sialyl Tn antigen levels in prognosis of
      patients with gastric cancer.
PG  - 1836-40
AB  - BACKGROUND: Expression of sialyl Tn antigen (STN) or serum STN levels were
      reported to be the independent prognostic factors of colon and ovarian cancers,
      respectively. The clinical significance of serum STN was evaluated as a tumor
      marker in gastric cancer. METHODS: Preoperative STN levels were examined in 350
      patients with gastric cancer, surgically treated in the Department of Surgery II,
      Kyushu University Hospital, and in the National Kyushu Cancer Center, between
      April, 1981 and April, 1986. The patients were divided into two groups: a high
      STN group (n = 304), with over 45 U/ml of STN, and a low STN group (n = 46), with
      less than or equal to 45 U/ml. RESULTS: In the high STN group, the patients were 
      older and the tumors were larger, compared to the low STN group. Histologically, 
      tumors in the high STN group were deeply penetrating and the rates of lymphatic
      involvement, vascular involvement, and lymph node and hepatic metastases were
      higher. Infiltrative growth patterns dominated. Thus, the tumors were in an
      advanced stage. The 5-year survival rate for patients in the high STN group was
      significantly less than that of patients in the low STN group (44.8% +/- 7.9%
      versus 75.1% +/- 2.6%, P < 0.05). CONCLUSIONS: Because a high STN level
      correlates with an advanced tumor stage and a poorer prognosis, close follow-up
      and aggressive therapy are recommended.
FAU - Takahashi, I
AU  - Takahashi I
AD  - Cancer Center, Kyushu University Hospital, Fukuoka, Japan.
FAU - Maehara, Y
AU  - Maehara Y
FAU - Kusumoto, T
AU  - Kusumoto T
FAU - Yoshida, M
AU  - Yoshida M
FAU - Kakeji, Y
AU  - Kakeji Y
FAU - Kusumoto, H
AU  - Kusumoto H
FAU - Furusawa, M
AU  - Furusawa M
FAU - Sugimachi, K
AU  - Sugimachi K
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Cancer
JT  - Cancer
JID - 0374236
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Biomarkers, Tumor)
RN  - 0 (Reagent Kits, Diagnostic)
RN  - 0 (sialosyl-Tn antigen)
SB  - AIM
SB  - IM
MH  - Aged
MH  - Antigens, Tumor-Associated, Carbohydrate/*blood
MH  - *Biomarkers, Tumor
MH  - Female
MH  - Humans
MH  - Male
MH  - Middle Aged
MH  - Prognosis
MH  - Reagent Kits, Diagnostic
MH  - Stomach Neoplasms/*blood/mortality
EDAT- 1993/09/15 00:00
MHDA- 1993/09/15 00:01
CRDT- 1993/09/15 00:00
PHST- 1993/09/15 00:00 [pubmed]
PHST- 1993/09/15 00:01 [medline]
PHST- 1993/09/15 00:00 [entrez]
PST - ppublish
SO  - Cancer. 1993 Sep 15;72(6):1836-40.

PMID- 2479468
OWN - NLM
STAT- MEDLINE
DCOM- 19891227
LR  - 20071114
IS  - 0008-5472 (Print)
IS  - 0008-5472 (Linking)
VI  - 49
IP  - 23
DP  - 1989 Dec 1
TI  - Five new epitope-defined monoclonal antibodies reactive with GM2 and human glioma
      and medulloblastoma cell lines.
PG  - 6645-51
AB  - In order to investigate GM2 expression in gliomas, the GM2-positive human glioma 
      cell line (HGL) D-54 MG, which contains 0.6 nmol GM2/mg protein, representing 77%
      of the total monosialoganglioside fraction, was used as an immunogen for the
      production of anti-GM2 monoclonal antibodies. For ganglioside designations, see
      IUPAC-IUB (Eur. J. Biochem., 79: 11-21, 1977) and Svennerholm (J. Neurochem., 10:
      613-623, 1963). Five IgM monoclonal antibodies (DMAb-1 through DMAb-5)
      specifically recognizing the GalNAc beta1-4(NeuAc alpha 2-3)Gal-terminal epitope 
      common to GM2 and GalNAC-GD1a are reported. The antibodies did not react with
      GM1, GM3, GD2, GD3, GD1a, GD1b, and GQ1b. Purified anti-GM2 MAbs were used to
      define the expression of the "GM2" terminal epitope by cultured human malignant
      and normal cells by radioimmunoassay and membrane immunofluorescence. Among
      neuroectodermal tissue-derived cell lines, DMAb-3, at an optimal concentration of
      5 micrograms/ml, showed high reactivity (radioimmunoassay binding ratios greater 
      than 20) with 9 of 19 HGLs, 3 of 5 medulloblastoma, 4 of 5 neuroblastoma, and 1
      of 3 melanoma lines. Moderate reactivity (binding ratio, 10-20) was exhibited by 
      3 HGL, 2 medulloblastoma, and 1 neuroblastoma lines and low reactivity (binding
      ratio, 3-10) by 5 HGL lines; no reactivity was detected with 2 HGL and 2 melanoma
      lines. Densitometric evaluation of monosialoganglioside extracts from human
      glioma and medulloblastoma cell lines in conjunction with immunostaining on
      thin-layer chromatograms showed that GM2 represents the major
      monosialoganglioside in 8 of 10 HGL and in 3 of 4 Med lines. In these lines the
      amount of GM2 ranged from less than 0.1 to 0.6 nmol/mg protein. These results
      indicate that GM2 represents a proportionally increased ganglioside of most
      glioma, medulloblastoma, and neuroblastoma cells in vitro.
FAU - Vrionis, F D
AU  - Vrionis FD
AD  - Department of Pathology, Duke University Medical Center, Durham, North Carolina
      27710.
FAU - Wikstrand, C J
AU  - Wikstrand CJ
FAU - Fredman, P
AU  - Fredman P
FAU - Mansson, J E
AU  - Mansson JE
FAU - Svennerholm, L
AU  - Svennerholm L
FAU - Bigner, D D
AU  - Bigner DD
LA  - eng
GR  - CA32672/CA/NCI NIH HHS/United States
GR  - NS 20023/NS/NINDS NIH HHS/United States
GR  - R37 CA11898/CA/NCI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Cancer Res
JT  - Cancer research
JID - 2984705R
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antibodies, Neoplasm)
RN  - 0 (Antigens, Neoplasm)
RN  - 0 (Epitopes)
RN  - 0 (Gangliosides)
RN  - 19600-01-2 (G(M2) Ganglioside)
SB  - IM
MH  - Antibodies, Monoclonal/*immunology
MH  - Antibodies, Neoplasm/immunology
MH  - Antibody Specificity
MH  - Antigens, Neoplasm/*immunology
MH  - Dose-Response Relationship, Immunologic
MH  - Epitopes
MH  - G(M2) Ganglioside/*immunology
MH  - Gangliosides/*immunology
MH  - Glioma/*immunology
MH  - Humans
MH  - Medulloblastoma/*immunology
MH  - Melanoma/immunology
MH  - Neuroblastoma/immunology
EDAT- 1989/12/01 00:00
MHDA- 1989/12/01 00:01
CRDT- 1989/12/01 00:00
PHST- 1989/12/01 00:00 [pubmed]
PHST- 1989/12/01 00:01 [medline]
PHST- 1989/12/01 00:00 [entrez]
PST - ppublish
SO  - Cancer Res. 1989 Dec 1;49(23):6645-51.

PMID- 8625173
OWN - NLM
STAT- MEDLINE
DCOM- 19960626
LR  - 20100324
IS  - 0008-543X (Print)
IS  - 0008-543X (Linking)
VI  - 76
IP  - 5
DP  - 1995 Sep 1
TI  - Quantitative lectin-histochemical and immunohistochemical studies on the
      occurrence of alpha(2,3)- and alpha(2,6)-linked sialic acid residues in
      colorectal carcinomas. Relation to clinicopathologic features.
PG  - 727-35
AB  - BACKGROUND: Enhanced sialylation has been considered important for the metastatic
      growth of colorectal carcinomas. Using sequence- and sialic acid-specific lectins
      and a monoclonal antibody, the tumor-associated expression of alpha(2,3)- and
      alpha(2,6)-sialylated oligosaccharides was investigated. The study was designed
      to examine whether a random increase of sialylation or the expression of
      oligosaccharides carrying distinct sialic acid residues affect the biology of
      colorectal carcinomas. METHODS: Using computerized image analysis, formalin fixed
      and paraffin wax embedded specimens from 152 primary colorectal carcinomas were
      subjected to a quantitative analysis of the occurrence of sialoglycoconjugates
      detected by the maackia amurensis agglutinin (MAA: specific for alpha(2,3)-linked
      sialic acid residues), sambucus nigra agglutinin (SNA: specific for
      alpha(2,6)-linked sialic acid residues), and the monoclonal antibody B72.3 (MAB
      B72.3: specific for alpha(2,6)-N-acetyl-galactosamine-1-O-Ser/Thre). The data
      obtained by quantitating lectin/immunohistochemistry were related to morphologic 
      and clinical parameters. RESULTS: Alpha(2,3)-linked sialic acid residues
      increased from Stage I to Stage II tumors but decreased in advanced carcinomas.
      Alpha(2,6)-sialylated glycoconjugates did not show any association with local
      tumor growth (depth of invasion). However, metastatic tumor growth was
      accompanied by a significant increase of alpha(2,6)-sialylated carbohydrate
      sequences. Univariate survival analysis revealed that the expression of SNA- and 
      MAB B72.3-defined reactivity displayed an inverse relation to 5-year survival.
      Although more advanced tumor stage was associated with poor 5-year survival,
      tumors below the cutoff points for SNA- and MAB B72.3-defined reactivity
      indicated a better prognosis than the neoplasms above the cutoff points. In
      contrast, the expression of alpha(2,3)-linked sialic acid residues as detected by
      MAA had no significant effect on survival. Multivariate regression analysis
      revealed that SNA-reactivity, followed by tumor stage and the MAB B72.3-defined
      antigen reactivity were independent prognostic variables predicting overall
      survival, whereas MAA-reactivity, sex, age, histologic differentiation, and tumor
      grade had no independent prognostic value. The simultaneous expression of both
      sialyl-Tn- and SNA-reactivity determined tumors of high risk patients within the 
      different tumor stages. CONCLUSIONS: Sequence-specific sialylation is associated 
      with altered biologic behavior of colorectal carcinomas.
FAU - Vierbuchen, M J
AU  - Vierbuchen MJ
AD  - Department of Pathology, General Hospital St. Georg, Hamburg, Germany.
FAU - Fruechtnicht, W
AU  - Fruechtnicht W
FAU - Brackrock, S
AU  - Brackrock S
FAU - Krause, K T
AU  - Krause KT
FAU - Zienkiewicz, T J
AU  - Zienkiewicz TJ
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Cancer
JT  - Cancer
JID - 0374236
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Lectins)
RN  - 0 (Phytohemagglutinins)
RN  - 0 (Plant Lectins)
RN  - 0 (Sambucus nigra lectins)
RN  - 0 (Sialic Acids)
RN  - 0 (leukoagglutinins, plants)
RN  - EC 3.2.2.22 (Ribosome Inactivating Proteins)
SB  - AIM
SB  - IM
MH  - Antibodies, Monoclonal
MH  - Colorectal Neoplasms/*chemistry/*pathology
MH  - Female
MH  - Histocytochemistry
MH  - Humans
MH  - Image Processing, Computer-Assisted
MH  - Immunohistochemistry
MH  - Lectins
MH  - Male
MH  - Middle Aged
MH  - Phytohemagglutinins
MH  - *Plant Lectins
MH  - Ribosome Inactivating Proteins
MH  - Sialic Acids/*analysis
EDAT- 1995/09/01 00:00
MHDA- 1995/09/01 00:01
CRDT- 1995/09/01 00:00
PHST- 1995/09/01 00:00 [pubmed]
PHST- 1995/09/01 00:01 [medline]
PHST- 1995/09/01 00:00 [entrez]
PST - ppublish
SO  - Cancer. 1995 Sep 1;76(5):727-35.

PMID- 6187397
OWN - NLM
STAT- MEDLINE
DCOM- 19830527
LR  - 20171116
IS  - 0006-4971 (Print)
IS  - 0006-4971 (Linking)
VI  - 61
IP  - 5
DP  - 1983 May
TI  - My-1, the human myeloid-specific antigen detected by mouse monoclonal antibodies,
      is a sugar sequence found in lacto-N-fucopentaose III.
PG  - 1020-3
FAU - Huang, L C
AU  - Huang LC
FAU - Civin, C I
AU  - Civin CI
FAU - Magnani, J L
AU  - Magnani JL
FAU - Shaper, J H
AU  - Shaper JH
FAU - Ginsburg, V
AU  - Ginsburg V
LA  - eng
GR  - 1 KOA-AM-00212/AM/NIADDK NIH HHS/United States
GR  - CA 06973/CA/NCI NIH HHS/United States
GR  - CA 32318/CA/NCI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Blood
JT  - Blood
JID - 7603509
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens, Neoplasm)
RN  - 0 (Epitopes)
RN  - 0 (Lewis X Antigen)
RN  - 0 (Oligosaccharides)
SB  - AIM
SB  - IM
MH  - Adenocarcinoma/immunology
MH  - Animals
MH  - Antibodies, Monoclonal/*immunology
MH  - *Antigens, Neoplasm
MH  - Binding Sites, Antibody
MH  - Bone Marrow/*immunology
MH  - *Epitopes
MH  - Humans
MH  - Lewis X Antigen/*immunology
MH  - Mice
MH  - Oligosaccharides/*immunology
EDAT- 1983/05/01 00:00
MHDA- 1983/05/01 00:01
CRDT- 1983/05/01 00:00
PHST- 1983/05/01 00:00 [pubmed]
PHST- 1983/05/01 00:01 [medline]
PHST- 1983/05/01 00:00 [entrez]
PST - ppublish
SO  - Blood. 1983 May;61(5):1020-3.

PMID- 18316376
OWN - NLM
STAT- MEDLINE
DCOM- 20080619
LR  - 20080421
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 283
IP  - 17
DP  - 2008 Apr 25
TI  - Identification of chondroitin sulfate glucuronyltransferase as chondroitin
      synthase-3 involved in chondroitin polymerization: chondroitin polymerization is 
      achieved by multiple enzyme complexes consisting of chondroitin synthase family
      members.
PG  - 11396-406
LID - 10.1074/jbc.M707549200 [doi]
AB  - Recently, we demonstrated that chondroitin polymerization is achieved by any two 
      combinations of human chondroitin synthase-1 (ChSy-1), ChSy-2 (chondroitin
      sulfate synthase 3, CSS3), and chondroitin-polymerizing factor (ChPF). Although
      an additional ChSy family member, called chondroitin sulfate
      glucuronyltransferase (CSGlcA-T), has been identified, its involvement in
      chondroitin polymerization remains unclear because it possesses only
      glucuronyltransferase II activity responsible for the elongation of chondroitin
      sulfate (CS) chains. Herein, we report that CSGlcA-T exhibits polymerization
      activity on alpha-thrombomodulin bearing the truncated linkage region
      tetrasaccharide through its interaction with ChSy-1, ChSy-2 (CSS3), or ChPF, and 
      the chain length of chondroitin formed by the co-expressed proteins in various
      combinations is different. In addition, ChSy family members co-expressed in
      various combinations exhibited distinct but overlapping acceptor substrate
      specificities toward the two synthetic acceptor substrates,
      GlcUAbeta1-3Galbeta1-O-naphthalenemethanol and
      GlcUAbeta1-3Galbeta1-O-C(2)H(4)NH-benzyloxycarbonyl, both of which share the
      disaccharide sequence with the glycosaminoglycan-protein linkage region
      tetrasaccharide. Moreover, overexpression of CSGlcA-T increased the amount of CS 
      in HeLa cells, whereas the RNA interference of CSGlcA-T resulted in a reduction
      of the amount of CS in the cells. Furthermore, the analysis using the CSGlcA-T
      mutant that lacks any glycosyltransferase activity but interacts with other ChSy 
      family members showed that the glycosyltransferase activity of CSGlcA-T plays an 
      important role in chondroitin polymerization. Overall, these results suggest that
      chondroitin polymerization is achieved by multiple combinations of ChSy-1,
      ChSy-2, CSGlcA-T, and ChPF and that each combination may play a unique role in
      the biosynthesis of CS. Based on these results, we renamed CSGlcA-T chondroitin
      synthase-3 (ChSy-3).
FAU - Izumikawa, Tomomi
AU  - Izumikawa T
AD  - Department of Biochemistry, Kobe Pharmaceutical University, 4-19-1
      Motoyamakita-machi, Higashinada-ku, Kobe 658-8558, Japan.
FAU - Koike, Toshiyasu
AU  - Koike T
FAU - Shiozawa, Shoko
AU  - Shiozawa S
FAU - Sugahara, Kazuyuki
AU  - Sugahara K
FAU - Tamura, Jun-ichi
AU  - Tamura J
FAU - Kitagawa, Hiroshi
AU  - Kitagawa H
LA  - eng
SI  - GENBANK/AB095812
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20080303
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Disaccharides)
RN  - 0 (Glycosaminoglycans)
RN  - 9007-27-6 (Chondroitin)
RN  - EC 2.4.1.- (N-Acetylgalactosaminyltransferases)
RN  - EC 2.4.1.17 (Glucuronosyltransferase)
RN  - EC 2.4.1.17 (chondroitin sulfate glucuronyltransferase)
RN  - EC 2.4.1.175 (chondroitin synthase)
SB  - IM
MH  - Animals
MH  - COS Cells
MH  - Cercopithecus aethiops
MH  - Chondroitin/*chemistry
MH  - Disaccharides/chemistry
MH  - *Gene Expression Regulation, Enzymologic
MH  - Glucuronosyltransferase/chemistry/*physiology
MH  - Glycosaminoglycans/chemistry
MH  - HeLa Cells
MH  - Humans
MH  - Molecular Sequence Data
MH  - Mutagenesis, Site-Directed
MH  - Mutation
MH  - N-Acetylgalactosaminyltransferases/chemistry/*physiology
MH  - Substrate Specificity
EDAT- 2008/03/05 09:00
MHDA- 2008/06/20 09:00
CRDT- 2008/03/05 09:00
PHST- 2008/03/05 09:00 [pubmed]
PHST- 2008/06/20 09:00 [medline]
PHST- 2008/03/05 09:00 [entrez]
AID - M707549200 [pii]
AID - 10.1074/jbc.M707549200 [doi]
PST - ppublish
SO  - J Biol Chem. 2008 Apr 25;283(17):11396-406. doi: 10.1074/jbc.M707549200. Epub
      2008 Mar 3.

PMID- 2318868
OWN - NLM
STAT- MEDLINE
DCOM- 19900502
LR  - 20061115
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 265
IP  - 9
DP  - 1990 Mar 25
TI  - Occurrence of tetra- and pentasaccharides with the sialyl-Le(a) structure in
      human milk.
PG  - 4859-62
AB  - The occurrence of two novel oligosaccharides in human milk was investigated.
      These oligosaccharides were purified by affinity chromatography on a column of an
      immobilized monoclonal antibody, MSW 113. Structural studies, involving 500-MHz
      1H NMR spectroscopy and fast atom bombardment-mass spectrometry, indicated the
      structures of these compounds to be NeuAc alpha 2----3Gal beta 1----3(Fuc alpha
      1----4) GlcNAc and NeuAc alpha 2----3Gal beta 1----3(Fuc alpha 1----4) GlcNac
      beta 1----3Gal. This constitutes the first evidence for the occurrence of
      N-acetylglucosamine or galactose as the reducing-end residue of human milk
      oligosaccharides. These two oligosaccharides bound MSW 113 to nearly the same
      extent as sialyl-Lea hexasaccharide but to another sialyl-Le(a)
      structure-directed monoclonal antibody, NS-19-9, only weakly.
FAU - Kitagawa, H
AU  - Kitagawa H
AD  - Department of Biological Chemistry, Faculty of Pharmaceutical Sciences, Kyoto
      University, Japan.
FAU - Nakada, H
AU  - Nakada H
FAU - Numata, Y
AU  - Numata Y
FAU - Kurosaka, A
AU  - Kurosaka A
FAU - Fukui, S
AU  - Fukui S
FAU - Funakoshi, I
AU  - Funakoshi I
FAU - Kawasaki, T
AU  - Kawasaki T
FAU - Shimada, I
AU  - Shimada I
FAU - Inagaki, F
AU  - Inagaki F
FAU - Yamashina, I
AU  - Yamashina I
LA  - eng
PT  - Comparative Study
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Oligosaccharides)
RN  - 117978-16-2 (sialyl-Le(a) oligosaccharide)
SB  - IM
MH  - Antigens, Tumor-Associated, Carbohydrate
MH  - Carbohydrate Conformation
MH  - Carbohydrate Sequence
MH  - Female
MH  - Humans
MH  - Mass Spectrometry
MH  - Milk, Human/*analysis
MH  - Molecular Sequence Data
MH  - *Oligosaccharides/analysis
MH  - Sequence Homology, Nucleic Acid
EDAT- 1990/03/25 00:00
MHDA- 1990/03/25 00:01
CRDT- 1990/03/25 00:00
PHST- 1990/03/25 00:00 [pubmed]
PHST- 1990/03/25 00:01 [medline]
PHST- 1990/03/25 00:00 [entrez]
PST - ppublish
SO  - J Biol Chem. 1990 Mar 25;265(9):4859-62.

PMID- 8052408
OWN - NLM
STAT- MEDLINE
DCOM- 19940908
LR  - 20171114
IS  - 0306-4522 (Print)
IS  - 0306-4522 (Linking)
VI  - 60
IP  - 1
DP  - 1994 May
TI  - Developmentally regulated expression of a brain specific species of chondroitin
      sulfate proteoglycan, neurocan, identified with a monoclonal antibody IG2 in the 
      rat cerebrum.
PG  - 145-57
AB  - The mammalian brain contains many species of proteoglycan. To identify each
      proteoglycan species, we have raised monoclonal antibodies against soluble
      chondroitin sulfate proteoglycans purified from 10-day-old rat brains. One
      monoclonal antibody, named monoclonal antibody 1G2, recognized two proteoglycan
      species with 220,000 and 150,000 mol. wt core glycoproteins (chondroitin sulfate 
      proteoglycan-220 and chondroitin sulfate proteoglycan-150). Partial amino acid
      sequences of N-termini of their core proteins coincided with those of neurocan, a
      brain-unique chondroitin sulfate proteoglycan species, whose complete coding
      sequence was recently reported [Rauch et al. (1992) J. biol. Chem. 269,
      19,536-19,547]. Western blots revealed that chondroitin sulfate proteoglycan-220 
      became detectable in the rat cerebrum on embryonic day 14, and that it
      disappeared from the brain around postnatal day 30. In contrast, a fairly large
      amount of chondroitin sulfate proteoglycan-150 remained in the mature brain.
      Immunohistochemical studies revealed that 1G2 antigen was first localized in the 
      preplate zone, then both in the marginal zone and in the subplate of the rat
      cerebrum on embryonic day 16, prior to arrival of the first thalamic afferents at
      the cortex. On embryonic day 20, immunolabeling with monoclonal antibody 1G2
      began to spread from the subplate into the developing cortical plate. On
      postnatal day 10, the neuropil of the cerebrum, except for the barrel field, was 
      diffusely stained with the antibody, intensely in the hippocampus and superficial
      layers (I-III) of the cerebral cortex and weakly elsewhere. The barrel hollows
      were stained very weakly compared with the barrel walls at this stage. The
      immunoreactivity in the hippocampus and superficial cortical layers was weakened 
      in the mature brain, so that no particular staining pattern, but weak and diffuse
      staining was observed in the adult rat cerebrum. The 1G2 antigen was
      immunohistochemically associated largely with glial fibrillary acidic
      protein-positive cells in primary cultures of the neonatal rat cerebrum. Both
      chondroitin sulfate proteoglycan-220 and chondroitin sulfate proteoglycan-150
      were detected in the conditioned media not only of highly enriched cultures of
      fetal rat cortical neurons but also of pure cultures of mature astrocytes; more
      (12- to 20-fold) in the astrocyte conditioned media. Astrocytes, in addition to
      neurons, may be a cellular source of neurocan in brain at least under certain
      physiological conditions. The spaciotemporal expression pattern of 1G2
      epitope-bearing proteoglycan, or neurocan, suggests that this proteoglycan
      species plays some roles at least in forming the elongation pathway for early
      cortical afferent fibers as well as the functional barrel structure in the
      somatosensory cortex.
FAU - Oohira, A
AU  - Oohira A
AD  - Department of Perinatology and Neuroglycoscience, Institute for Developmental
      Research, Aichi, Japan.
FAU - Matsui, F
AU  - Matsui F
FAU - Watanabe, E
AU  - Watanabe E
FAU - Kushima, Y
AU  - Kushima Y
FAU - Maeda, N
AU  - Maeda N
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Neuroscience
JT  - Neuroscience
JID - 7605074
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Chondroitin Sulfate Proteoglycans)
RN  - 0 (Culture Media, Conditioned)
RN  - 0 (Lectins, C-Type)
RN  - 0 (Nerve Tissue Proteins)
RN  - 0 (Proteoglycans)
RN  - 148684-98-4 (NCAN protein, human)
RN  - EC 3.2.1.- (Glucosidases)
RN  - EC 4.2.2.- (Chondroitin Lyases)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - *Antibodies, Monoclonal
MH  - Astrocytes/metabolism
MH  - Blotting, Western
MH  - Cells, Cultured
MH  - Cerebral Cortex/cytology/*growth & development/*metabolism
MH  - Chondroitin Lyases/metabolism
MH  - Chondroitin Sulfate Proteoglycans/*biosynthesis/chemistry/immunology
MH  - Culture Media, Conditioned
MH  - Electrophoresis, Polyacrylamide Gel
MH  - Female
MH  - Glucosidases/chemistry
MH  - Hydrolysis
MH  - Immunohistochemistry
MH  - Lectins, C-Type
MH  - Mice
MH  - Mice, Inbred C3H/immunology
MH  - Molecular Sequence Data
MH  - Nerve Tissue Proteins/*biosynthesis/chemistry/immunology
MH  - Pregnancy
MH  - Proteoglycans/biosynthesis/chemistry/immunology
MH  - Rats
MH  - Rats, Sprague-Dawley
EDAT- 1994/05/01 00:00
MHDA- 1994/05/01 00:01
CRDT- 1994/05/01 00:00
PHST- 1994/05/01 00:00 [pubmed]
PHST- 1994/05/01 00:01 [medline]
PHST- 1994/05/01 00:00 [entrez]
AID - 0306-4522(94)90210-0 [pii]
PST - ppublish
SO  - Neuroscience. 1994 May;60(1):145-57.

PMID- 19496993
OWN - NLM
STAT- MEDLINE
DCOM- 20091203
LR  - 20090916
IS  - 0031-8655 (Print)
IS  - 0031-8655 (Linking)
VI  - 85
IP  - 5
DP  - 2009 Sep-Oct
TI  - Specific interaction of the legume lectins, concanavalin a and peanut agglutinin,
      with phycocyanin.
PG  - 1126-33
LID - 10.1111/j.1751-1097.2009.00571.x [doi]
AB  - In a recent study, we found that jacalin, a T-antigen specific lectin could
      interact with phycocyanin (PC) in a carbohydrate-independent manner. We show here
      that concanavalin A and peanut agglutinin too can interact with PC, although the 
      nature of the interaction is distinctly different from that for jacalin. The
      legume lectins bind PC weaker in the presence of their specific carbohydrate
      ligands. Like jacalin, the legume lectins too interact with PC via two distinct
      sites. Higher ionic strengths resulted in a weakening of the interaction at site 
      1 and did not affect the interaction at site 2, clearly indicating that the
      interactions involve charged residues at the former and hydrophobic interactions 
      at the latter site. The implications for the use of these lectin-PC complexes in 
      photodynamic therapy and other clinical applications are discussed.
FAU - Pandey, Gunjan
AU  - Pandey G
AD  - School of Biosciences, Jamia Millia Islamia, New Delhi, India.
FAU - Fatma, Tasneem
AU  - Fatma T
FAU - Komath, Sneha Sudha
AU  - Komath SS
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20090528
PL  - United States
TA  - Photochem Photobiol
JT  - Photochemistry and photobiology
JID - 0376425
RN  - 0 (Lectins)
RN  - 0 (Peanut Agglutinin)
RN  - 11016-15-2 (Phycocyanin)
RN  - 11028-71-0 (Concanavalin A)
SB  - IM
MH  - Concanavalin A/*chemistry
MH  - Fabaceae/*chemistry
MH  - Lectins/*chemistry
MH  - Osmolar Concentration
MH  - Peanut Agglutinin/*chemistry
MH  - Phycocyanin/*chemistry
MH  - Spectrometry, Fluorescence
EDAT- 2009/06/06 09:00
MHDA- 2009/12/16 06:00
CRDT- 2009/06/06 09:00
PHST- 2009/06/06 09:00 [entrez]
PHST- 2009/06/06 09:00 [pubmed]
PHST- 2009/12/16 06:00 [medline]
AID - PHP571 [pii]
AID - 10.1111/j.1751-1097.2009.00571.x [doi]
PST - ppublish
SO  - Photochem Photobiol. 2009 Sep-Oct;85(5):1126-33. doi:
      10.1111/j.1751-1097.2009.00571.x. Epub 2009 May 28.

PMID- 8453646
OWN - NLM
STAT- MEDLINE
DCOM- 19930421
LR  - 20151119
IS  - 0008-5472 (Print)
IS  - 0008-5472 (Linking)
VI  - 53
IP  - 7
DP  - 1993 Apr 1
TI  - Expression of Sialyl-Tn antigens in normal squamous epithelium, dysplasia, and
      squamous cell carcinoma in the esophagus.
PG  - 1706-8
AB  - Two monoclonal antibodies, TKH2 and B72.3, directed toward the Sialyl-Tn antigen 
      (SA 2, 6GalNAc alpha-O-Ser/Thr), were examined immunohistochemically to analyze
      the expression of these antigens in 20 areas of normal squamous epithelium, 12
      lesions of dysplasia, and 86 cases of squamous cell carcinoma including 32 with
      superficial carcinoma in the esophagus. No expression of TKH2 or B72.3 was found 
      in the normal squamous epithelium. Among the 12 lesions of dysplasia only one
      expressed TKH2. In carcinoma the expression of TKH2 and B72.3 was found in 40
      (47%) and 21 (24%) of the 86 carcinomas, respectively; however, the number of
      positive malignant cells with TKH2 and B72.3 totaled less than half that in the
      tissue, and no relationship was found between either prognosis or lymph node
      metastasis and the expression of Sialyl-Tn antigen. These results indicate that
      Sialyl-Tn antigen appears in the process of malignant transformation or tumor
      progression in esophageal squamous cell carcinoma; however, the positive
      expression of Sialyl-Tn antigen was not directly connected to either prognosis or
      lymph node metastasis.
FAU - Ikeda, Y
AU  - Ikeda Y
AD  - Department of Surgery II, Faculty of Medicine, Kyushu University, Fukuoka, Japan.
FAU - Kuwano, H
AU  - Kuwano H
FAU - Baba, K
AU  - Baba K
FAU - Ikebe, M
AU  - Ikebe M
FAU - Matushima, T
AU  - Matushima T
FAU - Adachi, Y
AU  - Adachi Y
FAU - Mori, M
AU  - Mori M
FAU - Sugimachi, K
AU  - Sugimachi K
LA  - eng
PT  - Journal Article
PL  - United States
TA  - Cancer Res
JT  - Cancer research
JID - 2984705R
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Biomarkers, Tumor)
RN  - 0 (sialosyl-Tn antigen)
SB  - IM
MH  - Antibodies, Monoclonal
MH  - Antigens, Tumor-Associated, Carbohydrate/*analysis
MH  - Biomarkers, Tumor/*analysis
MH  - Carcinoma, Squamous Cell/*immunology
MH  - Epithelium/immunology
MH  - Esophageal Neoplasms/*immunology
MH  - Esophagus/*immunology/pathology
MH  - Female
MH  - Humans
MH  - Male
MH  - Middle Aged
EDAT- 1993/04/01 00:00
MHDA- 1993/04/01 00:01
CRDT- 1993/04/01 00:00
PHST- 1993/04/01 00:00 [pubmed]
PHST- 1993/04/01 00:01 [medline]
PHST- 1993/04/01 00:00 [entrez]
PST - ppublish
SO  - Cancer Res. 1993 Apr 1;53(7):1706-8.

PMID- 11406562
OWN - NLM
STAT- MEDLINE
DCOM- 20010712
LR  - 20071205
IS  - 0008-5472 (Print)
IS  - 0008-5472 (Linking)
VI  - 61
IP  - 12
DP  - 2001 Jun 15
TI  - The role of Thomsen-Friedenreich antigen in adhesion of human breast and prostate
      cancer cells to the endothelium.
PG  - 4851-7
AB  - Interactions of metastatic cancer cells with vasculatory endothelium are critical
      during early stages of cancer metastasis. Understanding the molecular
      underpinnings of these interactions is essential for the development of new
      efficacious cancer therapies. Here we demonstrate that cancer-associated
      carbohydrate T antigen plays a leading role in docking breast and prostate cancer
      cells onto endothelium by specifically interacting with endothelium-expressed
      beta-galactoside-binding protein, galectin-3. Importantly, T antigen-bearing
      glycoproteins are also capable of mobilizing galectin-3 to the surface of
      endothelial cells, thus priming them for harboring metastatic cancer cells. The T
      antigen-mediated, tumor-endothelial cell interactions could be efficiently
      disrupted using synthetic compounds either mimicking or masking this carbohydrate
      structure. High efficiency of T antigen-mimicking and T antigen-masking
      inhibitors of tumor cell adhesion warrants their further development into
      antiadhesive cancer therapeutics.
FAU - Glinsky, V V
AU  - Glinsky VV
AD  - Department of Biochemistry, University of Missouri, Columbia, Missouri 65211,
      USA.
FAU - Glinsky, G V
AU  - Glinsky GV
FAU - Rittenhouse-Olson, K
AU  - Rittenhouse-Olson K
FAU - Huflejt, M E
AU  - Huflejt ME
FAU - Glinskii, O V
AU  - Glinskii OV
FAU - Deutscher, S L
AU  - Deutscher SL
FAU - Quinn, T P
AU  - Quinn TP
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, Non-P.H.S.
PL  - United States
TA  - Cancer Res
JT  - Cancer research
JID - 2984705R
RN  - 0 (Antigens, Differentiation)
RN  - 0 (Antigens, Neoplasm)
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Epitopes)
RN  - 0 (Galectin 3)
RN  - 0 (Peptide Fragments)
RN  - 3554-90-3 (Thomsen-Friedenreich antigen)
SB  - IM
MH  - Amino Acid Sequence
MH  - Antigens, Differentiation/metabolism
MH  - Antigens, Neoplasm/*physiology
MH  - Antigens, Tumor-Associated, Carbohydrate/biosynthesis/*physiology
MH  - Bone Marrow/blood supply
MH  - Breast Neoplasms/immunology/*pathology
MH  - Cell Adhesion/physiology
MH  - Endothelium, Vascular/*cytology/metabolism
MH  - Epitopes/immunology
MH  - Female
MH  - Galectin 3
MH  - Humans
MH  - Male
MH  - Microscopy, Confocal
MH  - Molecular Mimicry
MH  - Molecular Sequence Data
MH  - Peptide Fragments/immunology
MH  - Prostatic Neoplasms/immunology/*pathology
EDAT- 2001/06/19 10:00
MHDA- 2001/07/13 10:01
CRDT- 2001/06/19 10:00
PHST- 2001/06/19 10:00 [pubmed]
PHST- 2001/07/13 10:01 [medline]
PHST- 2001/06/19 10:00 [entrez]
PST - ppublish
SO  - Cancer Res. 2001 Jun 15;61(12):4851-7.

PMID- 10506931
OWN - NLM
STAT- MEDLINE
DCOM- 19991126
LR  - 20180607
IS  - 0213-3911 (Print)
IS  - 0213-3911 (Linking)
VI  - 14
IP  - 4
DP  - 1999 Oct
TI  - Immunoreactivity of Thomsen-Friedenreich (TF) antigen in human neoplasms: the
      importance of carrier-specific glycotope expression on MUC1.
PG  - 1153-8
LID - 10.14670/HH-14.1153 [doi]
AB  - On the basis of their known fine specificities we evaluated the
      immunohistochemical marker qualities of two monoclonal antibodies (mabs) defining
      the tumor-associated TF disaccharide Gal beta 1-3 GalNAc. This antigen is
      expressed in certain tumors in correlation with prognosis and metastasis. The
      reactivity of one of these mabs (A78-G/A7) depends on clustered TF disaccharides 
      (glycosylation at vicinal Ser/Thr positions) while the other--mab BW835--has been
      characterized to bind specifically to TF disaccharide linked to a motif within
      the MUC1 repeat. Therefore, mab BW835 represents an interesting tool for the
      identification of tumor-associated glycoforms of MUC1, which are involved in
      tumor progression and metastasis, but also in the recognition of tumor cells by
      cytotoxic T cells. As references the TF-binding lectins from peanut (PNA) and
      Artocarpus integrifolia (jacalin) were applied. The binding patterns of these
      immunoreagents were strikingly distinct. Mab BW835 showed a significantly
      stronger reactivity than mab A78-G/A7, especially in gastric, mammary,
      pancreatic, thyreoideal, renal and bladder carcinomas. PNA and jacalin receptors 
      exhibited an expression in the majority of all cancer types, with the exception
      of seminoma and glioblastoma/sarcoma. These results can be explained by the
      broader fine specificities of the lectins. Furthermore, a strong expression of
      MUC1-bound TF antigen is indicated by the staining pattern of mab BW835. The
      marker qualities of both antigens, TF and MUC1, are combined in the binding
      specificity of BW835, and hence this antibody may have a high impact for the
      immunodetection of these tumor-associated antigens.
FAU - Baldus, S E
AU  - Baldus SE
AD  - Institute of Pathology, University of Cologne, Germany. s-e.baldus@uni-koeln.de
FAU - Hanisch, F G
AU  - Hanisch FG
FAU - Monaca, E
AU  - Monaca E
FAU - Karsten, U R
AU  - Karsten UR
FAU - Zirbes, T K
AU  - Zirbes TK
FAU - Thiele, J
AU  - Thiele J
FAU - Dienes, H P
AU  - Dienes HP
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - Spain
TA  - Histol Histopathol
JT  - Histology and histopathology
JID - 8609357
RN  - 0 (Epitopes, B-Lymphocyte)
RN  - 0 (Glycoproteins)
RN  - 0 (MUC1 tandem repeat peptide)
RN  - 0 (Mucin-1)
RN  - 0 (Peptide Fragments)
RN  - 0 (Thomsen-Friedenreich antigen, cryptic)
RN  - 0 (Trisaccharides)
SB  - IM
MH  - Epitopes, B-Lymphocyte/immunology
MH  - Glycoproteins/immunology
MH  - Humans
MH  - Mucin-1/*immunology
MH  - Neoplasms/*immunology/pathology
MH  - Peptide Fragments/*immunology
MH  - Trisaccharides/*immunology
EDAT- 1999/10/03 00:00
MHDA- 1999/10/03 00:01
CRDT- 1999/10/03 00:00
PHST- 1999/10/03 00:00 [pubmed]
PHST- 1999/10/03 00:01 [medline]
PHST- 1999/10/03 00:00 [entrez]
AID - 10.14670/HH-14.1153 [doi]
PST - ppublish
SO  - Histol Histopathol. 1999 Oct;14(4):1153-8. doi: 10.14670/HH-14.1153.

PMID- 19528665
OWN - NLM
STAT- MEDLINE
DCOM- 20091214
LR  - 20181113
IS  - 1460-2423 (Electronic)
IS  - 0959-6658 (Linking)
VI  - 19
IP  - 10
DP  - 2009 Oct
TI  - A newly generated functional antibody identifies Tn antigen as a novel
      determinant in the cancer cell-lymphatic endothelium interaction.
PG  - 1056-67
LID - 10.1093/glycob/cwp085 [doi]
AB  - Malignant transformation of epithelial cells is frequently associated with the
      alteration of glycosylation pathways. Tn is a common tumor-associated
      carbohydrate antigen present in 90% of human carcinomas and its expression
      correlates with metastatic potential and poor prognosis. Despite its relevance,
      the functional role of Tn in tumor biology has not been firmly established
      probably for the lack of appropriate experimental tools. Our aims were to produce
      highly reactive monoclonal antibodies against Tn making use of synthetically
      produced Tn and to test their usefulness for in vivo imaging as well as to define
      their potential functional activity in tumor cell spread. We immunized mice with 
      Tn clustered on cationized BSA and screened the positive hybridomas with
      Tn-biotinylated alginate. Enzyme-linked immuno sorbent assay and
      immunofluorescence assays revealed that the most reactive anti-Tn IgM mAb
      (2154F12A4) selectively recognized Tn on the MCF7 breast cancer cell line since
      its binding to the cell membrane was completely abolished by preincubation with
      purified Tn. Importantly, QDot 800-conjugated mAb injected in MCF7-tumor bearing 
      mice specifically bound to primary tumor lesions as well as to metastases in
      lymph nodes. In addition, this mAb was able to inhibit cancer cell adhesion to
      lymphatic endothelium suggesting a novel involvement of Tn in the lymphatic
      dissemination of cancer cells and hypothesizing future applications in inhibiting
      lymphatic metastases.
FAU - Danussi, Carla
AU  - Danussi C
AD  - Division of Experimental Oncology 2, Department of Molecular Oncology and
      Translational Research, CRO-IRCCS, 33081 Aviano, Pordenone, Italy.
FAU - Coslovi, Anna
AU  - Coslovi A
FAU - Campa, Cristiana
AU  - Campa C
FAU - Mucignat, Maria T
AU  - Mucignat MT
FAU - Spessotto, Paola
AU  - Spessotto P
FAU - Uggeri, Fulvio
AU  - Uggeri F
FAU - Paoletti, Sergio
AU  - Paoletti S
FAU - Colombatti, Alfonso
AU  - Colombatti A
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20090615
PL  - England
TA  - Glycobiology
JT  - Glycobiology
JID - 9104124
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antibodies, Neoplasm)
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Tn antigen)
SB  - IM
MH  - Animals
MH  - Antibodies, Monoclonal/*immunology
MH  - Antibodies, Neoplasm/*immunology
MH  - Antigens, Tumor-Associated, Carbohydrate/chemistry/*immunology
MH  - Cell Adhesion
MH  - Cell Line, Tumor
MH  - Endothelium/immunology
MH  - Female
MH  - Humans
MH  - Immunohistochemistry
MH  - Lymph Nodes/*immunology
MH  - Lymphatic Metastasis/immunology/pathology
MH  - Mice
MH  - Mice, Inbred BALB C
MH  - Mice, Nude
MH  - Molecular Structure
MH  - Neoplasms/*immunology/pathology
MH  - Xenograft Model Antitumor Assays
PMC - PMC2736043
EDAT- 2009/06/17 09:00
MHDA- 2009/12/16 06:00
CRDT- 2009/06/17 09:00
PHST- 2009/06/17 09:00 [entrez]
PHST- 2009/06/17 09:00 [pubmed]
PHST- 2009/12/16 06:00 [medline]
AID - cwp085 [pii]
AID - 10.1093/glycob/cwp085 [doi]
PST - ppublish
SO  - Glycobiology. 2009 Oct;19(10):1056-67. doi: 10.1093/glycob/cwp085. Epub 2009 Jun 
      15.

PMID- 3167861
OWN - NLM
STAT- MEDLINE
DCOM- 19881115
LR  - 20151119
IS  - 0008-5472 (Print)
IS  - 0008-5472 (Linking)
VI  - 48
IP  - 21
DP  - 1988 Nov 1
TI  - Generation of two murine monoclonal antibodies that can discriminate N-glycolyl
      and N-acetyl neuraminic acid residues of GM2 gangliosides.
PG  - 6154-60
AB  - Since the preliminary analyses of the glycolipids of small cell carcinomas of the
      lung showed an increase of GM2 ganglioside, we generated new murine monoclonal
      antibodies directed to GM2 to identify the molecular species of the glycolipid.
      The monoclonal antibodies MK2-34 and MK1-16 (both IgM), which specifically detect
      N-glycolyl GM2 and N-acetyl GM2, respectively, were generated by immunizing mice 
      with liposomes containing monophosphoryl lipid A, trehalose dimycolate, and the
      antigenic ganglioside. Among the glycolipid preparations extracted from the
      cancer tissues of 39 patients with lung cancer, a significant amount of N-acetyl 
      GM2 was detected with MK1-16 antibody in 70% of the squamous cell carcinoma
      cases, 50% of the lung adenocarcinoma cases, 33% of the large cell carcinoma
      cases, and 100% of the cases of small cell carcinoma of the lung. On the other
      hand, N-glycolyl GM2 which was defined by the monoclonal MK2-34 was not found in 
      any of the glycolipid fractions prepared from the lung cancer tissues examined in
      this study. Immunohistochemical studies of the lung cancer tissues with the
      MK1-16 antibody showed that the N-acetyl GM2 was present not only in small cell
      carcinoma tissues as one of the antigens related to tumors of neuroectodermal
      origin, but also in the squamous cell carcinoma and adenocarcinoma of the lung
      with a comparable frequency. The appearance of the N-acetyl GM2 antigen
      correlated well with the degree of differentiation of the cancer cells in
      patients with squamous cell carcinoma and adenocarcinoma of the lung.
FAU - Miyake, M
AU  - Miyake M
AD  - Department of Laboratory Medicine and Clinical Science, School of Medicine, Kyoto
      University, Japan.
FAU - Ito, M
AU  - Ito M
FAU - Hitomi, S
AU  - Hitomi S
FAU - Ikeda, S
AU  - Ikeda S
FAU - Taki, T
AU  - Taki T
FAU - Kurata, M
AU  - Kurata M
FAU - Hino, A
AU  - Hino A
FAU - Miyake, N
AU  - Miyake N
FAU - Kannagi, R
AU  - Kannagi R
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Cancer Res
JT  - Cancer research
JID - 2984705R
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Gangliosides)
RN  - 0 (Neuraminic Acids)
RN  - 0 (Sialic Acids)
RN  - 1113-83-3 (N-glycolylneuraminic acid)
RN  - 19600-01-2 (G(M2) Ganglioside)
RN  - GZP2782OP0 (N-Acetylneuraminic Acid)
SB  - IM
MH  - Animals
MH  - *Antibodies, Monoclonal/immunology
MH  - Antibody Specificity
MH  - Chromatography, Thin Layer
MH  - G(M2) Ganglioside/*analysis
MH  - Gangliosides/*analysis
MH  - Humans
MH  - Immunohistochemistry
MH  - Lung Neoplasms/*analysis
MH  - Mice
MH  - Mice, Inbred BALB C
MH  - N-Acetylneuraminic Acid
MH  - Neuraminic Acids/*analysis
MH  - Sialic Acids/*analysis
EDAT- 1988/11/01 00:00
MHDA- 1988/11/01 00:01
CRDT- 1988/11/01 00:00
PHST- 1988/11/01 00:00 [pubmed]
PHST- 1988/11/01 00:01 [medline]
PHST- 1988/11/01 00:00 [entrez]
PST - ppublish
SO  - Cancer Res. 1988 Nov 1;48(21):6154-60.

PMID- 7545084
OWN - NLM
STAT- MEDLINE
DCOM- 19951006
LR  - 20131121
IS  - 0008-5472 (Print)
IS  - 0008-5472 (Linking)
VI  - 55
IP  - 18
DP  - 1995 Sep 15
TI  - Monoclonal antibody BW835 defines a site-specific Thomsen-Friedenreich
      disaccharide linked to threonine within the VTSA motif of MUC1 tandem repeats.
PG  - 4036-40
AB  - mAb BW835 (IgG1) has been generated to breast cancer cell lines by alternating
      injections of MCF-7 or SW-613 cells and has been demonstrated to be of value in
      the serodiagnosis of mammary carcinoma. BW835 defines a carbohydrate epitope on
      integrated or secreted MUC1 glycoforms from carcinoma cells and human milk. To
      identify BW835-reactive glycopeptides on MUC1, proteolytic fragments of the mucin
      obtained by digestion with the Gly-C-specific endopeptidase IV from papaya
      corresponding to low molecular mass fragments (< 10 kilodaltons) of the tandem
      repeat domain were screened. A glycosylated fragment (glycopeptide 17) containing
      the mAb HMFG-2-defined epitope was highly reactive to BW835 antibody, while
      nonglycosylated tandem repeat peptide TAP25 or its in vitro-glycosylated
      N-acetylgalactosamine (GalNAc) derivatives were unreactive. Glycopeptide 17 bound
      to peanut agglutinin and to a Thomsen-Friedenreich antigen (TF alpha)-specific
      mAb (A78-G/A7). Binding of BW835 to glycopeptide 17 or to MUC1 was competitively 
      inhibited by peanut agglutinin and by the synthetic glycopeptides TF alpha Ser or
      TF alpha Thr but not by their beta-anomers. Evidence for site specificity of
      binding by BW835 to glycopeptide 17 was revealed by demonstrating nonreactivity
      of the antibody to other TF alpha-expressing glycoproteins with peptide moieties 
      lacking MUC1-specific motifs at putative glycosylation sites. The epitope of
      BW835 was localized to threonine within the VTSA-peptide motif by site-specific
      enzymatic beta-galactosylation of the synthetic tandem repeat peptide
      TAP25-GalNAc1 TAPPAHGVT(-O-alpha GalNAc)SAPDTRPAPGSTAPPA. This is the first
      report on a TF alpha-specific mAb that shows a strict peptide sequence dependency
      of binding.
FAU - Hanisch, F G
AU  - Hanisch FG
AD  - Institute of Immunobiology, University Clinic Cologne, Germany.
FAU - Stadie, T
AU  - Stadie T
FAU - Bosslet, K
AU  - Bosslet K
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Cancer Res
JT  - Cancer research
JID - 2984705R
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens, Neoplasm)
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Epitopes)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Mucin-1)
RN  - 0 (Mucins)
RN  - 2ZD004190S (Threonine)
RN  - 3554-90-3 (Thomsen-Friedenreich antigen)
SB  - IM
MH  - Amino Acid Sequence
MH  - Antibodies, Monoclonal/*immunology
MH  - Antigens, Neoplasm/*analysis
MH  - Antigens, Tumor-Associated, Carbohydrate/*analysis/immunology
MH  - Epitopes
MH  - Female
MH  - Humans
MH  - Membrane Glycoproteins/*analysis/chemistry
MH  - Molecular Sequence Data
MH  - Mucin-1
MH  - Mucins/*analysis/chemistry
MH  - Threonine/chemistry
MH  - Tumor Cells, Cultured
EDAT- 1995/09/15 00:00
MHDA- 1995/09/15 00:01
CRDT- 1995/09/15 00:00
PHST- 1995/09/15 00:00 [pubmed]
PHST- 1995/09/15 00:01 [medline]
PHST- 1995/09/15 00:00 [entrez]
PST - ppublish
SO  - Cancer Res. 1995 Sep 15;55(18):4036-40.

PMID- 11882908
OWN - NLM
STAT- MEDLINE
DCOM- 20020523
LR  - 20181113
IS  - 1219-4956 (Print)
IS  - 1219-4956 (Linking)
VI  - 7
IP  - 4
DP  - 2001
TI  - MUC1 mucin and carbohydrate associated antigens as tumor markers in head and neck
      squamous cell carcinoma.
PG  - 284-91
AB  - UNLABELLED: An immunological analysis to study MUC1 mucin core protein and
      carbohydrate associated antigens as tissue tumor markers in head and neck
      carcinoma was performed. Twenty nine patients with the following tumor
      localizations were included: tongue (n=10), larynx (n=8), oral cavity (n=4),
      maxillary sinus (n=3), tonsillar ring (n=3) and pharynx (n=1); seven samples of
      epithelium obtained from normal organs at the same localizations were studied as 
      controls. Immunohistochemical analysis was performed following standard
      procedures and reaction was graded according to staining intensity and
      distribution. From each tissue section, membrane, cytoplasmic and nuclear
      moieties were obtained by differential centrifugation with subsequent
      fractionation by density gradient centrifugation (6M guanidium chloride-CsCl);
      subcellular moieties and CsCl derived fractions were analyzed by immunoblotting. 
      Monoclonal antibodies (MAbs) reacting with the core protein of MUCI (C595) and
      associated carbohydrate antigens were: Tn, 83D4 MAb; Lewis y antigen (Le y), C14 
      MAb; Lewis x antigen (Le x), KM380 MAb and sialyl Lewis x (sLe x), KM93 MAb.
      Statistical analysis was undertaken by Spearman rank correlation. In tumor
      samples, the immunohistochemical identification of MUCl core protein and
      associated antigens was extended; differences were found in the pattern and
      intensity of expression; results were corroborated by immunoblotting although in 
      a few samples there was not coincidence between both methods. Localization, tumor
      mass or node involvement did not show significant differences for any of the
      antigens studied. CONCLUSIONS: 1) head and neck carcinoma expressed MUCI and
      associated carbohydrate antigens in high levels; 2) no relationship between
      antigenic expression and tumor status was found.
FAU - Croce, M V
AU  - Croce MV
AD  - Facultad de Ciencias Medicas, UNLP, Centro de Investigaciones Inmunologicas
      Basicas y Aplicadas (CINIBA) Calle 60 y 120, La Plata, 1900, Argentina.
FAU - Rabassa, M E
AU  - Rabassa ME
FAU - Price, M R
AU  - Price MR
FAU - Segal-Eiras, A
AU  - Segal-Eiras A
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - Netherlands
TA  - Pathol Oncol Res
JT  - Pathology oncology research : POR
JID - 9706087
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Mucin-1)
SB  - IM
MH  - Adult
MH  - Aged
MH  - Antigens, Tumor-Associated, Carbohydrate/metabolism
MH  - Carcinoma, Squamous Cell/*metabolism/pathology
MH  - Female
MH  - Head and Neck Neoplasms/*metabolism/pathology
MH  - Humans
MH  - Immunoblotting
MH  - Immunoenzyme Techniques
MH  - Male
MH  - Middle Aged
MH  - Mucin-1/*metabolism
EDAT- 2002/03/08 10:00
MHDA- 2002/05/25 10:01
CRDT- 2002/03/08 10:00
PHST- 2002/03/08 10:00 [pubmed]
PHST- 2002/05/25 10:01 [medline]
PHST- 2002/03/08 10:00 [entrez]
AID - PAOR.2001.7.4.0284 [pii]
PST - ppublish
SO  - Pathol Oncol Res. 2001;7(4):284-91.

PMID- 11396208
OWN - NLM
STAT- MEDLINE
DCOM- 20010726
LR  - 20071205
IS  - 0250-7005 (Print)
IS  - 0250-7005 (Linking)
VI  - 21
IP  - 2B
DP  - 2001 Mar-Apr
TI  - Immunohistochemical expression of T, Tn and sialyl-Tn antigens and clinical
      outcome in human breast carcinoma.
PG  - 1327-34
AB  - BACKGROUND: The extent of expression of reactive T (Thomsen-Friedenreich), Tn and
      sialyl-Tn antigens has been assumed to predict carcinoma aggressiveness. We
      studied the expression of T, Tn and sialyl-Tn antigens in a relatively large
      cohort of breast carcinoma patients with known long-term outcome to assess the
      clinical and biological significance of these antigens. MATERIALS AND METHODS: T,
      Tn and sjalyl-Tn antigens were examined in 72 consecutive primary breast
      carcinomas by immunohistochemistry using well defined monoclonal antibodies and
      their semiquantitative values were correlated with established clinicopathologic 
      prognostic parameters of the disease to determine their relationship with
      long-term clinical outcome. RESULTS: Of the 72 carcinomas, 63 (87.5%) each
      expressed T or Tn antigens, while 16 (22%) expressed sialyl-Tn antigens. Most
      carcinomas (81%) expressed more than one of the antigens simultaneously, being
      the most frequent combination T/Tn antigen expression. No significant correlation
      was noted between the expression of T, Tn and sialyl-Tn antigens (whether
      individually or in combination) and the prognostic parameters including patient
      age, disease stage, tumor size, lymph node status, nuclear and histologic grades,
      histologic types, hormone receptor status and menopausal status. Univariate
      survival analyses showed that disease stage, tumour size and lymph node
      metastasis were significant predictors of overall survival. Interestingly, a
      significant inverse correlation was found between the Tn antigen expression (p = 
      0.04), as well as the combined T/Tn (p = 0.03) and Tn/sialyl-Tn (p = 0.02)
      antigen expressions and long-term overall survival. In a multivariate Cox
      proportional hazard model, disease stage and a negative or low Tn antigen
      expression emerged as significant predictors of overall survival. CONCLUSION: Our
      data suggested that the expression of T, Tn and sialyl-Tn antigens does not
      appear to predict the outcome of patients with breast carcinoma in a long-term
      run. Moreover, the findings signified a potential value for a negative or low Tn 
      antigen expression in prognostic stratification of breast carcinomas.
FAU - Imai, J
AU  - Imai J
AD  - Department of Molecular Pathology, Institute of Gerontology, Nippon Medical
      School, 1-396 Kosugi-cho, Nakahara-ky, Kawasaki, Japan. imai@lilac.plala.or.jp
FAU - Ghazizadeh, M
AU  - Ghazizadeh M
FAU - Naito, Z
AU  - Naito Z
FAU - Asano, G
AU  - Asano G
LA  - eng
PT  - Journal Article
PL  - Greece
TA  - Anticancer Res
JT  - Anticancer research
JID - 8102988
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Tn antigen)
RN  - 0 (sialosyl-Tn antigen)
RN  - 3554-90-3 (Thomsen-Friedenreich antigen)
SB  - IM
MH  - Adult
MH  - Aged
MH  - Antigens, Tumor-Associated, Carbohydrate/*biosynthesis
MH  - Breast Neoplasms/*metabolism/pathology
MH  - Carcinoma, Ductal, Breast/*metabolism/pathology
MH  - Carcinoma, Lobular/*metabolism/pathology
MH  - Female
MH  - Humans
MH  - Immunoenzyme Techniques
MH  - Middle Aged
MH  - Predictive Value of Tests
EDAT- 2001/06/09 10:00
MHDA- 2001/07/28 10:01
CRDT- 2001/06/09 10:00
PHST- 2001/06/09 10:00 [pubmed]
PHST- 2001/07/28 10:01 [medline]
PHST- 2001/06/09 10:00 [entrez]
PST - ppublish
SO  - Anticancer Res. 2001 Mar-Apr;21(2B):1327-34.

PMID- 6385004
OWN - NLM
STAT- MEDLINE
DCOM- 19841105
LR  - 20190501
IS  - 0027-8424 (Print)
IS  - 0027-8424 (Linking)
VI  - 81
IP  - 18
DP  - 1984 Sep
TI  - Localization of the gangliosides GD2 and GD3 in adhesion plaques and on the
      surface of human melanoma cells.
PG  - 5767-71
AB  - The predominant gangliosides produced by two cultured human melanoma cell lines
      are GD3 and/or GD2. These gangliosides were found to be cell associated and
      present in substratum-attached material after cell removal by EDTA. Monoclonal
      antibodies directed to GD2 and GD3 specified the cell-surface distribution of
      these gangliosides and localized them in focal adhesion plaques at the interface 
      of cells and their substratum. These attachment sites did not represent
      indiscriminant membrane fragments remaining after removal of cells with EDTA,
      because neither melanoma-associated proteoglycan nor class I histocompatibility
      antigens were detected by their respective antibodies. Our data suggest that the 
      disialogangliosides GD2 and GD3 may be involved in the interaction between human 
      melanoma cells and solid substrata.
FAU - Cheresh, D A
AU  - Cheresh DA
FAU - Harper, J R
AU  - Harper JR
FAU - Schulz, G
AU  - Schulz G
FAU - Reisfeld, R A
AU  - Reisfeld RA
LA  - eng
GR  - CA 07222/CA/NCI NIH HHS/United States
GR  - CA 07544/CA/NCI NIH HHS/United States
GR  - CA 28420/CA/NCI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Proc Natl Acad Sci U S A
JT  - Proceedings of the National Academy of Sciences of the United States of America
JID - 7505876
RN  - 0 (Gangliosides)
RN  - 0 (Membrane Lipids)
RN  - 62010-37-1 (ganglioside, GD3)
RN  - 65988-71-8 (ganglioside, GD2)
SB  - IM
MH  - Cell Adhesion
MH  - Cell Line
MH  - Cell Membrane/analysis
MH  - Chromatography, Thin Layer
MH  - Fluorescent Antibody Technique
MH  - Gangliosides/*analysis
MH  - Humans
MH  - Melanoma/*analysis/pathology
MH  - Membrane Lipids/*analysis
PMC - PMC391792
EDAT- 1984/09/01 00:00
MHDA- 1984/09/01 00:01
CRDT- 1984/09/01 00:00
PHST- 1984/09/01 00:00 [pubmed]
PHST- 1984/09/01 00:01 [medline]
PHST- 1984/09/01 00:00 [entrez]
AID - 10.1073/pnas.81.18.5767 [doi]
PST - ppublish
SO  - Proc Natl Acad Sci U S A. 1984 Sep;81(18):5767-71. doi: 10.1073/pnas.81.18.5767.

PMID- 11479278
OWN - NLM
STAT- MEDLINE
DCOM- 20011011
LR  - 20190513
IS  - 0959-6658 (Print)
IS  - 0959-6658 (Linking)
VI  - 11
IP  - 8
DP  - 2001 Aug
TI  - The fucosylated histo-blood group antigens H type 2 (blood group O, CD173) and
      Lewis Y (CD174) are expressed on CD34+ hematopoietic progenitors but absent on
      mature lymphocytes.
PG  - 677-83
AB  - The expression of LeY, H2, H3, and H4 on a broad variety of human leukemia cell
      lines and native lymphocytes as well as on CD34+ hematopoietic progenitor cells
      was examined by flow cytometry and immunocytochemistry. CD34+ leukemia cell lines
      (KG1, KG1a, and TF1) and native CD34+ hematopoietic progenitor cells expressed H2
      (CD173) and LeY (CD174). In contrast, CD34(-) cell lines (HL-60, U937, JOK-1,
      Raji, Molt-3, Jurkat, and CEM-C7) and mature lymphocytes from peripheral blood
      and tonsils lacked CD173 and CD174. All cell lines and native lymphocytes as well
      as CD34+ precursor cells were negative for H3 and H4. Immunoprecipitation and
      consecutive Western blotting revealed a 170-kDa glycoprotein as the carrier
      molecule for the CD173 and CD174 oligosaccharide sequences on CD34+ hematopoietic
      precursors. The key enzyme for generating CD173 is the beta-D-galactoside
      2-alpha-L-fucosyltransferase (FUT1). As shown by RT-PCR, FUT1 was expressed in
      immature hematopoietic cells but absent in mature lymphocytes, which indicates
      that expression of CD173 within the hematopoietic system is regulated at the
      transcriptional level by FUT1. Due to their exclusive presence on CD34+
      hematopoietic progenitor cells, CD173 and CD174 represent novel markers of early 
      hematopoiesis. The expression of the fucosylated histo-blood group antigens CD173
      and CD174 in CD34+ hematopoietic progenitor cells and down-regulation of FUT1 in 
      mature lymphocytes may be important factors influencing the homing process of
      hematopoietic stem cells to the bone marrow.
FAU - Cao, Y
AU  - Cao Y
AD  - Division of Cellular Immunology, German Cancer Research Centre, Im Neuenheimer
      Feld 280, 69120 Heidelberg, Germany.
FAU - Merling, A
AU  - Merling A
FAU - Karsten, U
AU  - Karsten U
FAU - Schwartz-Albiez, R
AU  - Schwartz-Albiez R
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - Glycobiology
JT  - Glycobiology
JID - 9104124
RN  - 0 (ABO Blood-Group System)
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens, CD)
RN  - 0 (Leukosialin)
RN  - 0 (Lewis Blood-Group System)
RN  - 0 (Lewis Y antigen)
RN  - 0 (Sialoglycoproteins)
RN  - 0 (UN1 sialoglycoprotein, human)
RN  - EC 2.4.1.- (Fucosyltransferases)
RN  - EC 2.4.1.69 (galactoside 2-alpha-L-fucosyltransferase)
SB  - IM
MH  - ABO Blood-Group System/*metabolism
MH  - Antibodies, Monoclonal
MH  - Antigens, CD/biosynthesis
MH  - Carbohydrate Sequence
MH  - Flow Cytometry
MH  - Fucosyltransferases/genetics
MH  - Hematopoietic Stem Cells/enzymology/*metabolism
MH  - Humans
MH  - Leukosialin
MH  - Lewis Blood-Group System/*biosynthesis
MH  - Lymphocytes/enzymology/*metabolism
MH  - Molecular Sequence Data
MH  - Reverse Transcriptase Polymerase Chain Reaction
MH  - Sialoglycoproteins/*biosynthesis
MH  - Tumor Cells, Cultured
EDAT- 2001/08/02 10:00
MHDA- 2001/10/12 10:01
CRDT- 2001/08/02 10:00
PHST- 2001/08/02 10:00 [pubmed]
PHST- 2001/10/12 10:01 [medline]
PHST- 2001/08/02 10:00 [entrez]
AID - 10.1093/glycob/11.8.677 [doi]
PST - ppublish
SO  - Glycobiology. 2001 Aug;11(8):677-83. doi: 10.1093/glycob/11.8.677.

PMID- 19021580
OWN - NLM
STAT- MEDLINE
DCOM- 20090203
LR  - 20081121
IS  - 1470-8752 (Electronic)
IS  - 0300-5127 (Linking)
VI  - 36
IP  - Pt 6
DP  - 2008 Dec
TI  - Lectin-epithelial interactions in the human colon.
PG  - 1482-6
LID - 10.1042/BST0361482 [doi]
AB  - Similar changes in glycosylation occur in the colonic epithelium in inflammatory 
      conditions such as ulcerative colitis and Crohn's disease and also in colon
      cancer and precancerous adenomatous polyps. They include reduced length of
      O-glycans, reduced sulfation, increased sialylation and increased expression of
      oncofetal carbohydrate antigens, such as sialyl-Tn (sialylalpha2-6GalNAc), and
      the TF antigen (Thomsen-Friedenreich antigen) Galbeta1-3GalNAcalpha-Ser/Thr. The 
      changes affect cell surface as well as secreted glycoproteins and mediate altered
      interactions between the epithelium and lectins of dietary, microbial or human
      origin. Different TF-binding lectins cause diverse effects on epithelial cells,
      reflecting subtle differences in binding specificities e.g. for sialylated TF;
      some of these interactions, such as with the TF-binding peanut lectin that
      resists digestion, may be biologically significant. Increased TF expression by
      cancer cells also allows interaction with the human galactose-binding lectin,
      galectin-3. This lectin has increased concentration in the sera of patients with 
      metastatic cancer and binds TF on cancer cell surface MUC1 (mucin 1), causing
      clustering of MUC1 and revealing underlying adhesion molecules which promote
      adhesion to endothelium. This is likely to be an important mechanism in cancer
      metastasis and represents a valid therapeutic target. Tools are now available to 
      allow fast and accurate elucidation of glycosylation changes in epithelial
      disease, characterization of their potential lectin ligands, whether dietary,
      microbial or human, and determination of the functional significance of their
      interactions. This should prove a very fruitful area for future research with
      relevance to infectious, inflammatory and cancerous diseases of the epithelia.
FAU - Rhodes, Jonathan M
AU  - Rhodes JM
AD  - School of Clinical Sciences, University of Liverpool, Duncan Building, Liverpool,
      UK. rhodesjm@liverpool.ac.uk
FAU - Campbell, Barry J
AU  - Campbell BJ
FAU - Yu, Lu-Gang
AU  - Yu LG
LA  - eng
PT  - Journal Article
PT  - Review
PL  - England
TA  - Biochem Soc Trans
JT  - Biochemical Society transactions
JID - 7506897
RN  - 0 (Galectin 3)
RN  - 0 (Lectins)
SB  - IM
MH  - Colon/*metabolism/pathology
MH  - Epithelial Cells/*metabolism
MH  - Galectin 3/metabolism
MH  - Glycosylation
MH  - Humans
MH  - Lectins/*metabolism
MH  - Neoplasm Metastasis
RF  - 46
EDAT- 2008/11/22 09:00
MHDA- 2009/02/04 09:00
CRDT- 2008/11/22 09:00
PHST- 2008/11/22 09:00 [pubmed]
PHST- 2009/02/04 09:00 [medline]
PHST- 2008/11/22 09:00 [entrez]
AID - BST0361482 [pii]
AID - 10.1042/BST0361482 [doi]
PST - ppublish
SO  - Biochem Soc Trans. 2008 Dec;36(Pt 6):1482-6. doi: 10.1042/BST0361482.

PMID- 11291879
OWN - NLM
STAT- MEDLINE
DCOM- 20011205
LR  - 20151119
IS  - 0944-1174 (Print)
IS  - 0944-1174 (Linking)
VI  - 36
IP  - 3
DP  - 2001 Mar
TI  - Circulating sialyl Lewis(x), sialyl Lewis(a), and sialyl Tn antigens in
      colorectal cancer patients: multivariate analysis of predictive factors for serum
      antigen levels.
PG  - 166-72
AB  - Preoperative serum levels of sialyl Lewis(a) (CA 19-9), sialyl Lewis(x) (SLX),
      and sialyl Tn (STN) antigens in colorectal cancer patients were examined to
      establish predictive factors for serum levels of these antigens compared with
      carcinoembryonic antigen (CEA). A total of 308 patients who underwent resection
      for a colorectal cancer were divided into low and high antigen groups (higher or 
      lower than a selected diagnostic-based cutoff value). The cutoff values were 37
      U/ml for CA19-9, 38 U/ml for SLX, 45 U/ml for STN, and 2.5 ng/ml for CEA. The
      American Joint Committee on Cancer Classification and Stage grouping was used to 
      classify the tumors. Statistical tests were conducted using univariate and
      multivariate logistic regression analyses. For CA19-9, 81 patients (26.3%) were
      assigned to the high antigen group: for SLX, 39 (12.7%); for STN, 33 (10.7%); and
      for CEA, 133 (43.2%). Multivariate logistic regression analysis revealed that
      predictive factors associated with high antigen levels were female sex (odds
      ratio [OR], 1.78 vs male sex), T4 (OR, 3.26 vs T1/T2), and M1 (OR, 3.35 vs M0)
      for CA19-9; M1 (OR, 6.40 vs M0) for SLX; mucinous carcinoma (OR, 8.45 vs well
      differentiated adenocarcinoma) and M1 (OR, 8.24 vs M0) for STN; and mucinous
      carcinoma (OR, 7.21 vs well differentiated adenocarcinoma), T3/T4 (OR, 3.84/4.18,
      respectively, vs T1/T2), and M1 (OR, 6.39 vs M0) for CEA. In conclusion, high
      serum levels of CA19-9, SLX, and STN are strongly associated with distant
      metastasis. In addition, high serum levels of CA19-9 may be an independent
      predictor for female gender and T4, and high serum levels of STN may be an
      independent predictor for mucinous carcinoma.
FAU - Nakagoe, T
AU  - Nakagoe T
AD  - First Department of Surgery, Nagasaki University School of Medicine, Japan.
FAU - Sawai, T
AU  - Sawai T
FAU - Tsuji, T
AU  - Tsuji T
FAU - Jibiki, M
AU  - Jibiki M
FAU - Nanashima, A
AU  - Nanashima A
FAU - Yamaguchi, H
AU  - Yamaguchi H
FAU - Kurosaki, N
AU  - Kurosaki N
FAU - Yasutake, T
AU  - Yasutake T
FAU - Ayabe, H
AU  - Ayabe H
LA  - eng
PT  - Journal Article
PL  - Japan
TA  - J Gastroenterol
JT  - Journal of gastroenterology
JID - 9430794
RN  - 0
      (5-acetylneuraminyl-(2-3)-galactosyl-(1-4)-(fucopyranosyl-(1-3))-N-acetylglucosam
      ine)
RN  - 0 (Antigens, Neoplasm)
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Biomarkers, Tumor)
RN  - 0 (Carcinoembryonic Antigen)
RN  - 0 (Gangliosides)
RN  - 0 (Oligosaccharides)
RN  - 0 (sialosyl-Tn antigen)
RN  - 91847-18-6 (sialyl Le(a) ganglioside)
SB  - IM
MH  - Aged
MH  - Antigens, Neoplasm/*blood
MH  - Antigens, Tumor-Associated, Carbohydrate/*blood
MH  - Biomarkers, Tumor/*blood
MH  - Carcinoembryonic Antigen/blood
MH  - Colorectal Neoplasms/*immunology/*pathology
MH  - Female
MH  - Gangliosides/*blood
MH  - Humans
MH  - Logistic Models
MH  - Male
MH  - Middle Aged
MH  - Multivariate Analysis
MH  - Neoplasm Recurrence, Local/immunology/pathology
MH  - Oligosaccharides/*blood
MH  - Predictive Value of Tests
EDAT- 2001/04/09 10:00
MHDA- 2002/01/05 10:01
CRDT- 2001/04/09 10:00
PHST- 2001/04/09 10:00 [pubmed]
PHST- 2002/01/05 10:01 [medline]
PHST- 2001/04/09 10:00 [entrez]
PST - ppublish
SO  - J Gastroenterol. 2001 Mar;36(3):166-72.

PMID- 8260233
OWN - NLM
STAT- MEDLINE
DCOM- 19940125
LR  - 20180113
IS  - 0959-8049 (Print)
IS  - 0959-8049 (Linking)
VI  - 29A
IP  - 13
DP  - 1993
TI  - Expression of sialyl-Tn antigen is correlated with survival time of patients with
      gastric carcinomas.
PG  - 1820-3
AB  - Expression of sialyl-Tn antigen (STN) was examined by an immunohistochemical
      method in 85 primary gastric carcinomas. The STN expression occurred in 53
      (62.4%) cancers, and the positive staining was correlated with degree of gastric 
      wall and lymph vessel invasion, lymph node metastasis, and stage of tumour.
      Five-year survival rates of patients with STN-positive cancers (47.2%) were
      significantly lower than those with STN-negative cancers (84.4%) (P < 0.01), and 
      patients with STN-positive cancers at stage III and stage IV had a worse
      prognosis. In the cancers with serosal invasion, patients with STN-positive
      cancer disclosed a significantly poorer prognosis than those with STN-negative
      cancers (P < 0.01). Therefore, it is suggested that a careful follow-up study and
      intensive postoperative therapy are needed for patients with advanced gastric
      cancers with positive STN expression.
FAU - Ma, X C
AU  - Ma XC
AD  - First Department of Surgery, Shiga University of Medical Science, Otsu, Japan.
FAU - Terata, N
AU  - Terata N
FAU - Kodama, M
AU  - Kodama M
FAU - Jancic, S
AU  - Jancic S
FAU - Hosokawa, Y
AU  - Hosokawa Y
FAU - Hattori, T
AU  - Hattori T
LA  - eng
PT  - Journal Article
PL  - England
TA  - Eur J Cancer
JT  - European journal of cancer (Oxford, England : 1990)
JID - 9005373
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Biomarkers, Tumor)
RN  - 0 (sialosyl-Tn antigen)
SB  - IM
CIN - Eur J Cancer. 1994;30A(9):1398-9. PMID: 7999432
MH  - Antigens, Tumor-Associated, Carbohydrate/*analysis
MH  - Biomarkers, Tumor/*analysis
MH  - Female
MH  - Humans
MH  - Lymphatic Metastasis
MH  - Male
MH  - Middle Aged
MH  - Neoplasm Staging
MH  - Prognosis
MH  - Stomach Neoplasms/immunology/*mortality/pathology
MH  - Survival Rate
EDAT- 1993/01/01 00:00
MHDA- 1993/01/01 00:01
CRDT- 1993/01/01 00:00
PHST- 1993/01/01 00:00 [pubmed]
PHST- 1993/01/01 00:01 [medline]
PHST- 1993/01/01 00:00 [entrez]
AID - 0959-8049(93)90529-O [pii]
PST - ppublish
SO  - Eur J Cancer. 1993;29A(13):1820-3.

PMID- 6270685
OWN - NLM
STAT- MEDLINE
DCOM- 19811221
LR  - 20190501
IS  - 0027-8424 (Print)
IS  - 0027-8424 (Linking)
VI  - 78
IP  - 7
DP  - 1981 Jul
TI  - Monoclonal antibodies that demonstrate specificity for several types of human
      lung cancer.
PG  - 4591-5
AB  - Monoclonal antibodies with selectivity for human lung cancer were produced by
      immunizing BALB/c mice with an established line of human small cell lung cancer
      (NCI-H69) and fusing the mouse spleen cells to mouse myeloma line X63-Ag8.653.
      The resulting hybrid cells were initially screened by immunoautoradiography for
      production of antibodies that would react with NCI-H69 and another small cell
      lung cancer line (NCI-H128) but not its autologous B-lymphoblastoid line
      (NCI-H128BL). Stable monoclonal antibody-producing lines were isolated by
      repeated cloning. Three independently derived monoclonal antibodies, designated
      525A5, 534F8, and 538F12, were found to react with three of the major types of
      human lung cancer (small cell, adenocarcinoma, and squamous carcinoma). They did 
      not react with bronchioloalveolar and large cell lung cancers, myeloma,
      lymphomas, leukemias, osteogeneic sarcoma, mesothelioma, hypernephroma, malignant
      melanoma, simian virus 40-transformed human fetal lung cells, skin fibroblast
      lines, human B-lymphoblastoid lines, human erythrocytes, and rodent cells.
      Interestingly, these antibodies also bound to three out of three human
      neuroblastomas and two out of three breast cancers but failed to react with mouse
      neuroblastoma and rat pheochromocytoma. The monoclonal antibodies reacted with
      human small cell lung cancer tumors obtained at autopsy, but had insignificant
      reactions with normal human lung, liver, spleen, and skeletal muscle. We conclude
      that monoclonal antibodies have been generated that react with common antigenic
      determinants expressed on several human lung cancer types, neuroblastoma, and
      some breast cancers, but are not detectable by our current assays on a variety of
      other human tumors or normal adult human tissues. Such antibodies are of
      potential clinical and biological importance.
FAU - Cuttitta, F
AU  - Cuttitta F
FAU - Rosen, S
AU  - Rosen S
FAU - Gazdar, A F
AU  - Gazdar AF
FAU - Minna, J D
AU  - Minna JD
LA  - eng
PT  - Journal Article
PL  - United States
TA  - Proc Natl Acad Sci U S A
JT  - Proceedings of the National Academy of Sciences of the United States of America
JID - 7505876
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens, Neoplasm)
SB  - IM
MH  - Adenocarcinoma/*immunology
MH  - Animals
MH  - Antibodies, Monoclonal/immunology
MH  - Antigens, Neoplasm/*analysis
MH  - Carcinoma, Small Cell/*immunology
MH  - Carcinoma, Squamous Cell/*immunology
MH  - Cell Line
MH  - Cricetinae
MH  - Cross Reactions
MH  - Hybridomas/immunology
MH  - Lung Neoplasms/*immunology
MH  - Mice
MH  - Neuroblastoma/immunology
MH  - Rats
PMC - PMC319839
EDAT- 1981/07/01 00:00
MHDA- 1981/07/01 00:01
CRDT- 1981/07/01 00:00
PHST- 1981/07/01 00:00 [pubmed]
PHST- 1981/07/01 00:01 [medline]
PHST- 1981/07/01 00:00 [entrez]
AID - 10.1073/pnas.78.7.4591 [doi]
PST - ppublish
SO  - Proc Natl Acad Sci U S A. 1981 Jul;78(7):4591-5. doi: 10.1073/pnas.78.7.4591.

PMID- 6296843
OWN - NLM
STAT- MEDLINE
DCOM- 19830324
LR  - 20190501
IS  - 0027-8424 (Print)
IS  - 0027-8424 (Linking)
VI  - 79
IP  - 24
DP  - 1982 Dec
TI  - Identification of a human neuroectodermal tumor antigen (OFA-I-2) as ganglioside 
      GD2.
PG  - 7629-33
AB  - Two monospecific human antibodies (anti-OFA-I-1 and anti-OFA-I-2) produced in
      vitro by lymphoblast cell lines originating from melanoma patients have been
      shown previously to recognize cell surface antigens (OFA-I-1 and OFA-I-2) on
      human tumors and fetal brain: OFA-I-1 is expressed on a variety of human tumors, 
      while OFA-I-2 has been detected only on tumors of neuroectodermal origin.
      Evidence presented in this report suggests that the two antigens expressed by a
      cultured human melanoma cell line (M14) are chemically distinct and that OFA-I-2 
      is a cell surface glycolipid, ganglioside GD2: GalNAc beta 1 leads to 4 NeuAc
      alpha 2 leads to 8NeuAc alpha 2 leads to 3 Gal beta 1 leads to 4Glc-ceramide.
FAU - Cahan, L D
AU  - Cahan LD
FAU - Irie, R F
AU  - Irie RF
FAU - Singh, R
AU  - Singh R
FAU - Cassidenti, A
AU  - Cassidenti A
FAU - Paulson, J C
AU  - Paulson JC
LA  - eng
GR  - CA12582/CA/NCI NIH HHS/United States
GR  - CA30647/CA/NCI NIH HHS/United States
GR  - NS-00544/NS/NINDS NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Proc Natl Acad Sci U S A
JT  - Proceedings of the National Academy of Sciences of the United States of America
JID - 7505876
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens, Neoplasm)
RN  - 0 (Gangliosides)
RN  - 0 (Sialic Acids)
SB  - IM
MH  - Antibodies, Monoclonal
MH  - Antibody Specificity
MH  - Antigens, Neoplasm/*immunology
MH  - Ectoderm/immunology
MH  - Gangliosides/*immunology
MH  - Humans
MH  - Neoplasms, Nerve Tissue/*immunology
MH  - Sialic Acids/analysis
PMC - PMC347401
EDAT- 1982/12/01 00:00
MHDA- 1982/12/01 00:01
CRDT- 1982/12/01 00:00
PHST- 1982/12/01 00:00 [pubmed]
PHST- 1982/12/01 00:01 [medline]
PHST- 1982/12/01 00:00 [entrez]
AID - 10.1073/pnas.79.24.7629 [doi]
PST - ppublish
SO  - Proc Natl Acad Sci U S A. 1982 Dec;79(24):7629-33. doi: 10.1073/pnas.79.24.7629.

PMID- 3997830
OWN - NLM
STAT- MEDLINE
DCOM- 19850627
LR  - 20071114
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 260
IP  - 10
DP  - 1985 May 25
TI  - Lea-active heptaglycosylceramide, a hybrid of type 1 and type 2 chain, and the
      pattern of glycolipids with Lea, Leb, X (Lex), and Y (Ley) determinants in human 
      blood cell membranes (ghosts). Evidence that type 2 chain can elongate
      repetitively but type 1 chain cannot.
PG  - 6410-5
AB  - Two major glycolipids reactive with the monoclonal anti-Lea antibody have been
      isolated from human blood cell membranes. One component was identified as
      lactofucopentaosyl(II)ceramide and the other as a ceramide heptassaccharide with 
      the structure described below: (formula; see text) The structure includes the Lea
      determinant (type 1 chain) linked to lactoneotetraosylceramide (type 2 chain);
      thus, it is regarded to be a hybrid between type 1 and 2 chain. In addition, a
      minor component having the thin-layer chromatographic mobility of a ceramide
      nonasaccharide, which was reactive to anti-Lea antibody, was detected. No other
      component with a thin-layer chromatographic mobility slower than the above
      components and reactive to the anti-Lea antibody was detected. In contrast, a
      series of slowly migrating glycolipids having X (Lex) determinant (Gal beta
      1----4(Fuc alpha 1----3)GlcNAc) was detected. A similar series of long chain
      glycolipids having Y (Ley) determinant (Fuc alpha 1----2Gal beta
      1----4(Fuc1----3)GlcNAc) was detected in human blood cells; in contrast, only one
      major Leb glycolipid was found with the mobility of a ceramide hexasaccharide. No
      glycolipid with a long carbohydrate chain composed exclusively of type 1 chain
      was detected. Thus, chain elongation may proceed through type 2 chain, but not
      through type 1 chain. Lea and X (Lex) haptens are distributed equally among blood
      group A, B, and O red blood cells, whereas the quantity of Leb and Y (Ley)
      haptens is much lower in A and B blood cells than in O blood cells.
FAU - Kannagi, R
AU  - Kannagi R
FAU - Levery, S B
AU  - Levery SB
FAU - Hakomori, S
AU  - Hakomori S
LA  - eng
GR  - CA19224/CA/NCI NIH HHS/United States
GR  - CA20026/CA/NCI NIH HHS/United States
PT  - Comparative Study
PT  - Journal Article
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (ABO Blood-Group System)
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Glycosphingolipids)
RN  - 0 (Lewis Blood-Group System)
RN  - 0 (Membrane Lipids)
RN  - 97162-56-6 (ceramide heptassaccharide)
SB  - IM
MH  - ABO Blood-Group System/immunology
MH  - Antibodies, Monoclonal/immunology
MH  - Erythrocyte Membrane/analysis/*immunology
MH  - Glycosphingolipids/*blood/immunology/isolation & purification
MH  - Humans
MH  - Lewis Blood-Group System/*immunology
MH  - Membrane Lipids/*blood/immunology/isolation & purification
EDAT- 1985/05/25 00:00
MHDA- 1985/05/25 00:01
CRDT- 1985/05/25 00:00
PHST- 1985/05/25 00:00 [pubmed]
PHST- 1985/05/25 00:01 [medline]
PHST- 1985/05/25 00:00 [entrez]
PST - ppublish
SO  - J Biol Chem. 1985 May 25;260(10):6410-5.

PMID- 7684905
OWN - NLM
STAT- MEDLINE
DCOM- 19930701
LR  - 20171116
IS  - 0006-291X (Print)
IS  - 0006-291X (Linking)
VI  - 193
IP  - 1
DP  - 1993 May 28
TI  - Specific expression of a complex sialyl Lewis X antigen on high endothelial
      venules of human lymph nodes: possible candidate for L-selectin ligand.
PG  - 337-47
AB  - L-selectin is a cell adhesion molecule that mediates homing of lymphocytes to the
      peripheral lymph nodes and is speculated to bind to the carbohydrate determinant 
      which is specifically expressed by the endothelial cells of high endothelial
      venules (HEVs) in the peripheral lymph nodes. One of the murine monoclonal
      antibodies (2H5, IgM, kappa), which was raised against sialyl LeX-active
      glycolipids which have long and complicated carbohydrate structures, was found to
      react strongly to the HEV endothelial cells of the human peripheral lymph nodes, 
      while the typical anti-sialyl LeX antibodies SNH-3, FH-6 and CSLEX-1 failed to
      detect the antigen on HEV under the same condition. This new antibody was
      reactive to essentially all endothelial cells of HEV in the peripheral lymph
      nodes, and moderately to some endothelial cells in Payer's patches and
      appendices, but never reacted with the endothelial cells of post capillary
      venules in the spleen, thymus, or other organs. The 2H5 antibody detected three
      major glycoproteins of 90, 110 and 250 kDa, the most abundant molecular species
      being 110 kDa, in the stroma of human lymph nodes. In Stamper-Woodruff assays
      employing cryostat sections of human lymph nodes, the 2H5 antibody significantly 
      inhibited the adhesion of peripheral lymphocytes to the endothelial cells of HEV.
      These results indicate that the carbohydrate antigens defined by the 2H5
      antibody, most probably sialyl LeX determinants having complex carbohydrate
      structures, serve as the ligand for L-selectin on HEV endothelial cells.
FAU - Sawada, M
AU  - Sawada M
AD  - Department of Experimental Pathology, Aichi Cancer Center, Nagoya, Japan.
FAU - Takada, A
AU  - Takada A
FAU - Ohwaki, I
AU  - Ohwaki I
FAU - Takahashi, N
AU  - Takahashi N
FAU - Tateno, H
AU  - Tateno H
FAU - Sakamoto, J
AU  - Sakamoto J
FAU - Kannagi, R
AU  - Kannagi R
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Biochem Biophys Res Commun
JT  - Biochemical and biophysical research communications
JID - 0372516
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Cell Adhesion Molecules)
RN  - 0 (Lewis X Antigen)
RN  - 0 (Ligands)
RN  - 0 (sialosyl dimeric Le(x) antigen)
RN  - 126880-86-2 (L-Selectin)
SB  - IM
MH  - Antibodies, Monoclonal/immunology
MH  - Antibody Specificity
MH  - Carbohydrate Sequence
MH  - Cell Adhesion/immunology
MH  - Cell Adhesion Molecules/*metabolism
MH  - Endothelium, Vascular/immunology/*metabolism
MH  - Humans
MH  - Immunohistochemistry
MH  - L-Selectin
MH  - Lewis X Antigen/immunology/*metabolism
MH  - Ligands
MH  - Lymph Nodes/*blood supply/immunology
MH  - Lymphocytes/cytology
MH  - Molecular Sequence Data
MH  - Tumor Cells, Cultured
EDAT- 1993/05/28 00:00
MHDA- 1993/05/28 00:01
CRDT- 1993/05/28 00:00
PHST- 1993/05/28 00:00 [pubmed]
PHST- 1993/05/28 00:01 [medline]
PHST- 1993/05/28 00:00 [entrez]
AID - S0006-291X(83)71629-3 [pii]
AID - 10.1006/bbrc.1993.1629 [doi]
PST - ppublish
SO  - Biochem Biophys Res Commun. 1993 May 28;193(1):337-47. doi:
      10.1006/bbrc.1993.1629.

PMID- 7045228
OWN - NLM
STAT- MEDLINE
DCOM- 19820826
LR  - 20111117
IS  - 0022-1767 (Print)
IS  - 0022-1767 (Linking)
VI  - 129
IP  - 2
DP  - 1982 Aug
TI  - Neutral glycolipid antigens as developmental markers of mouse teratocarcinoma and
      early embryos: an immunologic and chemical analysis.
PG  - 603-9
AB  - Purified rabbit antibodies to neutral glycolipids were analyzed for their binding
      to mouse embryonal carcinoma cells (ECC) and preimplantation mouse embryos.
      Antibodies to globotetraosylceramide first bind to 2 to 4-cell embryos and reach 
      a peak of staining intensity with morulae, whereas anti-Forssman antibodies first
      bind to late morulae and then, most intensely, to early blastocysts. We compared 
      the binding of a monoclonal anti-Forssman antibody with that of rabbit
      anti-Forssman antibodies and show that although they react similarly with ECC,
      they do not do so with morulae: The monoclonal antibody stained weakly and
      unevenly, whereas the rabbit antiserum produced a uniformly bright
      immunofluorescent staining. Chemical analyses revealed that
      globotetraosylceramide is the most abundant glycolipid of F9 ECC and that there
      is poor correlation between the concentration of individual glycolipids in these 
      cells and their reactivity with antibodies to glycolipid molecules.
      Interestingly, the 2 Forssman antibody-reactive glycolipids of F9 ECC differ in
      their mobility on TLC plates from the classical Forssman antigen extracted from
      sheep red blood cells. This illustrates the potential problems in extrapolating
      from the coincident binding properties of an anti-glycolipid antibody to the
      chemical structure or abundance of an antigen in different cell types.
FAU - Willison, K R
AU  - Willison KR
FAU - Karol, R A
AU  - Karol RA
FAU - Suzuki, A
AU  - Suzuki A
FAU - Kundu, S K
AU  - Kundu SK
FAU - Marcus, D M
AU  - Marcus DM
LA  - eng
PT  - Journal Article
PL  - United States
TA  - J Immunol
JT  - Journal of immunology (Baltimore, Md. : 1950)
JID - 2985117R
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens, Neoplasm)
RN  - 0 (Globosides)
RN  - 0 (Glycolipids)
RN  - 0 (Lactosylceramides)
RN  - 0 (Trihexosylceramides)
RN  - 71965-57-6 (globotriaosylceramide)
RN  - 9013-60-9 (Forssman Antigen)
SB  - AIM
SB  - IM
MH  - Animals
MH  - Antibodies, Monoclonal/immunology
MH  - Antigens, Neoplasm/*immunology
MH  - Binding Sites, Antibody
MH  - Blastocyst/immunology
MH  - Embryo, Mammalian/*immunology
MH  - Female
MH  - Fluorescent Antibody Technique
MH  - Forssman Antigen/immunology
MH  - Globosides/immunology
MH  - Glycolipids/*immunology
MH  - Lactosylceramides/immunology
MH  - Mice
MH  - Morula/immunology
MH  - Pregnancy
MH  - Rabbits
MH  - Rats
MH  - Teratoma/*immunology
MH  - *Trihexosylceramides
EDAT- 1982/08/01 00:00
MHDA- 1982/08/01 00:01
CRDT- 1982/08/01 00:00
PHST- 1982/08/01 00:00 [pubmed]
PHST- 1982/08/01 00:01 [medline]
PHST- 1982/08/01 00:00 [entrez]
PST - ppublish
SO  - J Immunol. 1982 Aug;129(2):603-9.

PMID- 9873046
OWN - NLM
STAT- MEDLINE
DCOM- 19990205
LR  - 20190508
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 274
IP  - 2
DP  - 1999 Jan 8
TI  - Neisseria gonorrhoeae that infect men have lipooligosaccharides with terminal
      N-acetyllactosamine repeats.
PG  - 1017-25
AB  - Infectious Neisseria gonorrhoeae make relatively large lipooligosaccharides (LOS)
      that structurally resemble human glycosphingolipids. MS11mkC is an LOS variant of
      N. gonorrhoeae strain MS11 which was isolated from men at the onset of dysuria
      (Schneider, H., Griffiss, J. M., Boslego, J. W., Hitchcock, P. J., Zahos, K. M., 
      and Apicella, M. A. (1991) J. Exp. Med. 174, 1601-1605). Delayed extraction
      matrix-assisted laser desorption and ionization and electrospray ionization mass 
      spectrometry of O-deacylated MS11mkC LOS produced ions consistent with known LOS 
      which have lacto-N-neotetraose (Galbeta1-->4GlcNAcbeta1-->3Galbeta1-->4Glc;
      paraglobosyl; monoclonal antibodies (mAbs) 1B2(+) and 06B4(+)) and
      GalNAc-->lacto-N-neotetraose (gangliosyl; mAb 1-1-M+) oligosaccharides. Ion peaks
      for a larger LOS which also bound mAb 1B2 indicated the addition of a hexose
      (+162 Da) to gangliosyl LOS or the addition of a hexose and a N-acetylhexosamine 
      (+365 Da) to paraglobosyl LOS. Analysis of HF-treated and O-deacylated LOS
      revealed three major components present in a phosphoethanolamine (PEA)0 and a
      PEA1 series. Digestion of MS11mkC LOS by beta-N-acetylhexosaminidase and
      beta-galactosidase, alone and sequentially, combined with mAb binding patterns,
      confirmed the presence of a nonreducing terminal repeating LacNAc
      ((Galbeta1-->4GlcNAc)2) on the largest LOS, rather than a parallel
      oligosaccharide structure.
FAU - John, C M
AU  - John CM
AD  - Centre for Immunochemistry, University of California, San Francisco, California
      94121, USA. cjohn@vacom.ucsf.edu.net
FAU - Schneider, H
AU  - Schneider H
FAU - Griffiss, J M
AU  - Griffiss JM
LA  - eng
GR  - AI21620/AI/NIAID NIH HHS/United States
GR  - RR01614/RR/NCRR NIH HHS/United States
PT  - Journal Article
PT  - Research Support, U.S. Gov't, Non-P.H.S.
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Amino Sugars)
RN  - 0 (Lipopolysaccharides)
RN  - 3Y5B2K5OOK (N-acetyllactosamine)
RN  - EC 3.2.1.- (Glycoside Hydrolases)
SB  - IM
MH  - Amino Sugars/*chemistry
MH  - Carbohydrate Sequence
MH  - Glycoside Hydrolases/metabolism
MH  - Humans
MH  - Lipopolysaccharides/chemistry/*metabolism
MH  - Male
MH  - Molecular Sequence Data
MH  - Neisseria gonorrhoeae/*metabolism/pathogenicity
MH  - Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
EDAT- 1999/01/05 00:00
MHDA- 1999/01/05 00:01
CRDT- 1999/01/05 00:00
PHST- 1999/01/05 00:00 [pubmed]
PHST- 1999/01/05 00:01 [medline]
PHST- 1999/01/05 00:00 [entrez]
AID - 10.1074/jbc.274.2.1017 [doi]
PST - ppublish
SO  - J Biol Chem. 1999 Jan 8;274(2):1017-25. doi: 10.1074/jbc.274.2.1017.

PMID- 17038624
OWN - NLM
STAT- MEDLINE
DCOM- 20061025
LR  - 20131121
IS  - 1095-9203 (Electronic)
IS  - 0036-8075 (Linking)
VI  - 314
IP  - 5797
DP  - 2006 Oct 13
TI  - A mutant chaperone converts a wild-type protein into a tumor-specific antigen.
PG  - 304-8
AB  - Monoclonal antibodies have become important therapeutic agents against certain
      cancers. Many tumor-specific antigens are mutant proteins that are predominantly 
      intracellular and thus not readily accessible to monoclonal antibodies. We found 
      that a wild-type transmembrane protein could be transformed into a tumor-specific
      antigen. A somatic mutation in the chaperone gene Cosmc abolished function of a
      glycosyltransferase, disrupting O-glycan Core 1 synthesis and creating a
      tumor-specific glycopeptidic neo-epitope consisting of a monosaccharide and a
      specific wild-type protein sequence. This epitope induced a high-affinity, highly
      specific, syngeneic monoclonal antibody with antitumor activity. Such
      tumor-specific glycopeptidic neo-epitopes represent potential targets for
      monoclonal antibody therapy.
FAU - Schietinger, Andrea
AU  - Schietinger A
AD  - Department of Pathology, Committee on Immunology, Committee on Cancer Biology,
      University of Chicago, Chicago, IL 60637, USA. aschieti@uchicago.edu
FAU - Philip, Mary
AU  - Philip M
FAU - Yoshida, Barbara A
AU  - Yoshida BA
FAU - Azadi, Parastoo
AU  - Azadi P
FAU - Liu, Hui
AU  - Liu H
FAU - Meredith, Stephen C
AU  - Meredith SC
FAU - Schreiber, Hans
AU  - Schreiber H
LA  - eng
GR  - HD 07009/HD/NICHD NIH HHS/United States
GR  - P01-CA97296/CA/NCI NIH HHS/United States
GR  - P41RR018502-01/RR/NCRR NIH HHS/United States
GR  - R01-CA22677/CA/NCI NIH HHS/United States
GR  - R01-CA37516/CA/NCI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, N.I.H., Extramural
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Science
JT  - Science (New York, N.Y.)
JID - 0404511
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens, Neoplasm)
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Cosmc protein, mouse)
RN  - 0 (Epitopes)
RN  - 0 (Gp38 protein, mouse)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Molecular Chaperones)
RN  - 0 (Tn antigen)
RN  - EC 2.4.1.- (Galactosyltransferases)
RN  - KM15WK8O5T (Acetylgalactosamine)
SB  - IM
MH  - Acetylgalactosamine/analysis
MH  - Amino Acid Sequence
MH  - Animals
MH  - Antibodies, Monoclonal/*immunology
MH  - Antibody Affinity
MH  - Antigens, Neoplasm/chemistry/*immunology
MH  - Antigens, Tumor-Associated, Carbohydrate/analysis
MH  - Base Sequence
MH  - Cell Line, Tumor
MH  - Epitopes/immunology
MH  - Galactosyltransferases/metabolism
MH  - Glycosylation
MH  - Membrane Glycoproteins/chemistry/*immunology
MH  - Mice
MH  - Molecular Chaperones/chemistry/*genetics/*metabolism
MH  - Molecular Sequence Data
MH  - *Mutation
EDAT- 2006/10/14 09:00
MHDA- 2006/10/26 09:00
CRDT- 2006/10/14 09:00
PHST- 2006/10/14 09:00 [pubmed]
PHST- 2006/10/26 09:00 [medline]
PHST- 2006/10/14 09:00 [entrez]
AID - 314/5797/304 [pii]
AID - 10.1126/science.1129200 [doi]
PST - ppublish
SO  - Science. 2006 Oct 13;314(5797):304-8. doi: 10.1126/science.1129200.

PMID- 2022659
OWN - NLM
STAT- MEDLINE
DCOM- 19910605
LR  - 20071114
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 266
IP  - 13
DP  - 1991 May 5
TI  - Extended type 1 chain glycosphingolipids: dimeric Lea (III4V4Fuc2Lc6) as human
      tumor-associated antigen.
PG  - 8439-46
AB  - Glycolipid extracts from various human cancer tissues and cell lines showed the
      presence of a slow-migrating glycolipid component which was strongly reactive
      with monoclonal antibody (mAb) NCC-ST-421 (raised against human gastric
      adenocarcinoma) and weakly cross-reactive with anti-Lea mAbs. The slow-migrating 
      glycolipid was isolated from human colonic adenocarcinoma cell line Colo205 grown
      in nude mice, and was purified by high-performance liquid chromatography followed
      by preparative thin-layer chromatography. Its structure was elucidated by
      sequential enzymatic degradation and thin-layer chromatography immunostaining of 
      the degradation products with various mAbs, 1H NMR spectroscopy, positive-ion
      fast atom bombardment mass spectrometry, and methylation analysis. The major
      slow-migrating component reacting with mAb ST-421 was identified as dimeric Lea, 
      with the structure as follows. [formula: see text] Antigens containing this
      structure and various analogous structures (including enzymatically synthesized
      Lea/Lex hybrid antigen) were tested with ST-421. While the mAb was equally
      reactive with dimeric Lea and Lea/Lex, only the former was chemically detectable 
      as the slow-migrating glycolipid from the tumor extract. ST-421 showed less
      reactivity with simple Lea (III4FucLc4) or extended Lea (V4FucLc6, and/or IV3Gal 
      beta 1----3[Fuc alpha 1----4]GlcNAcnLc4), and was not reactive with Lex/Lex
      (dimeric Lex). It was concluded, therefore, that the major tumor-associated
      slow-migrating glycolipid reacting with ST-421 has the dimeric Lea structure
      shown above. Since extension of lacto-series structure has been shown to be
      limited to type 2 chain in normal cells and tissues, extended elongation of type 
      1 chain as shown in this structure represents a novel tumor-associated epitope.
FAU - Stroud, M R
AU  - Stroud MR
AD  - Biomembrane Institute, Seattle, Washington.
FAU - Levery, S B
AU  - Levery SB
FAU - Nudelman, E D
AU  - Nudelman ED
FAU - Salyan, M E
AU  - Salyan ME
FAU - Towell, J A
AU  - Towell JA
FAU - Roberts, C E
AU  - Roberts CE
FAU - Watanabe, M
AU  - Watanabe M
FAU - Hakomori, S
AU  - Hakomori S
LA  - eng
GR  - CA42505/CA/NCI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Glycosphingolipids)
SB  - IM
MH  - Adenocarcinoma/immunology
MH  - Antibodies, Monoclonal
MH  - Antigens, Tumor-Associated, Carbohydrate/*chemistry/immunology/isolation &
      purification
MH  - Carbohydrate Sequence
MH  - Chromatography, High Pressure Liquid
MH  - Colonic Neoplasms/immunology
MH  - Cross Reactions
MH  - Glycosphingolipids/*chemistry/immunology/isolation & purification
MH  - Humans
MH  - Immunoblotting
MH  - Magnetic Resonance Spectroscopy
MH  - Methylation
MH  - Molecular Sequence Data
MH  - Spectrometry, Mass, Fast Atom Bombardment
MH  - Tumor Cells, Cultured
EDAT- 1991/05/05 00:00
MHDA- 1991/05/05 00:01
CRDT- 1991/05/05 00:00
PHST- 1991/05/05 00:00 [pubmed]
PHST- 1991/05/05 00:01 [medline]
PHST- 1991/05/05 00:00 [entrez]
PST - ppublish
SO  - J Biol Chem. 1991 May 5;266(13):8439-46.

PMID- 10436809
OWN - NLM
STAT- MEDLINE
DCOM- 19990909
LR  - 20161017
IS  - 0923-7534 (Print)
IS  - 0923-7534 (Linking)
VI  - 10 Suppl 4
DP  - 1999
TI  - Role of tumour markers, cytogenetics.
PG  - 145-9
AB  - A review is presented on the role of conventional and molecular tumour markers
      (TM) in diagnosis and monitoring of patients with biliopancreatic malignancies.
      For biliopancreatic malignancy, following CEA as more historical and basic TM of 
      gastrointestinal diseases, the mainstay marker is CA 19-9 as
      monosialo-ganglioside/glycolipid and sialyl derivative of lacto-N-fucopentaose II
      (sialyl-Lewis(a), hapten of human Lewis(a) bloodgroup determinant). It is
      detected in serum of healthy individuals at low concentration < 40 U/ml, with
      lower and often transitional elevation in benign hepatobiliary diseases and with 
      highest levels in excretory ductal pancreatic adenocarcinoma (s = 70%-95%, sp =
      72%-90%), biliary (s = 55%-79%), hepatocellular and cholangiocellular cancer (s =
      22%-51%) besides gastric, colorectal and ovarian cancer and occasionally in lung,
      breast and uterine cancer. Physiologically elevated concentrations in healthy
      individuals have to be considered in all sorts of secretions (e.g. sputum,
      saliva, bronchial/gastric secretions, bile juice) of individuals with
      Lewis(a)-positive secretor status in contrast with low or lacking serum levels of
      CA 19-9 in patients with Lewis(a-/b-) status (7%-10% of population). In
      biliopancreatic malignancies, especially pancreatic cancer, CA 19-9 correlates
      well with clinical course of disease following surgical, chemo- or radiotherapy
      by a quick normalisation within 2-4 weeks after complete surgery, a transient
      decrease with successful palliative therapy and an often anticipated increase
      (lead time up to 6 months) before clinical detection in case of relapse or
      progressive disease. From CA 19-9 related TM tests some are detecting in addition
      to sialyl-Lewis(a) (sialyllacto-N-fucopentaose II) also the non-fucosylated
      precursor sialyl-Lewis(c) (sialyllacto-N-tetraose: CA 50, CA 242, Span-1) solely 
      detected by the DUPAN-2 test and independent of the Lewis(a) secretor status.
      Some other markers comprise in addition to sialyl-Lewis(a) partially the
      non-sialylated Lewis(a) antigen (CA 195, CAM 43, CA 494) or are less related (CAM
      17.1). The initial phase of screening and early detection is hoped to be better
      assessed by using molecular markers detecting gene mutations (p53, K-ras), growth
      factors (EGF, TGF-alpha, TGF-beta, HB-EGF, a/bFGFs, KGF) and growth factor
      receptor alterations (EGFr, c-erbB2/3/4). From these, K-ras mutations detected in
      blood, stool and bile juice of patients at risk for pancreatic cancer seem to be 
      more promising than p53 alterations as a more later step in carcinogenesis,
      although they are neither yet well established nor standardised by reliable
      assays. In contrast growth factor and growth factor receptor alterations mainly
      concerning signal transducing systems seem to reflect increased tumour
      aggressiveness, thus shorter survival and poorer prognosis thereby contributing
      in the selection of patients for more aggressive therapy.
FAU - Lamerz, R
AU  - Lamerz R
AD  - Medical Department II, Klinikum Grosshadern, University of Munich, Germany.
      lamerz@med2.med.uni-muenchen.de
LA  - eng
PT  - Journal Article
PT  - Review
PL  - England
TA  - Ann Oncol
JT  - Annals of oncology : official journal of the European Society for Medical
      Oncology
JID - 9007735
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Biomarkers, Tumor)
RN  - 0 (CA 242 antigen)
RN  - 0 (CA-19-9 Antigen)
RN  - 0 (Carcinoembryonic Antigen)
SB  - IM
MH  - Antigens, Tumor-Associated, Carbohydrate/analysis
MH  - Biomarkers, Tumor/*analysis
MH  - CA-19-9 Antigen/analysis
MH  - Carcinoembryonic Antigen/analysis
MH  - *Chromosome Aberrations
MH  - DNA Repair/genetics
MH  - Genes, Tumor Suppressor
MH  - Humans
MH  - Pancreatic Neoplasms/*diagnosis/genetics
RF  - 53
EDAT- 1999/08/07 00:00
MHDA- 1999/08/07 00:01
CRDT- 1999/08/07 00:00
PHST- 1999/08/07 00:00 [pubmed]
PHST- 1999/08/07 00:01 [medline]
PHST- 1999/08/07 00:00 [entrez]
PST - ppublish
SO  - Ann Oncol. 1999;10 Suppl 4:145-9.

PMID- 3469463
OWN - NLM
STAT- MEDLINE
DCOM- 19870402
LR  - 20151119
IS  - 0027-8874 (Print)
IS  - 0027-8874 (Linking)
VI  - 78
IP  - 3
DP  - 1987 Mar
TI  - Monoclonal antibodies and synthetic tumor-associated glycoconjugates in the study
      of the expression of Thomsen-Friedenreich-like and Tn-like antigens on human
      cancers.
PG  - 489-96
AB  - Synthetic carbohydrate haptens, which are conjugated to carrier human serum
      albumin molecules [synthetic tumor-associated glycoconjugates (S-TAGs)], were
      used to immunize mice for monoclonal antibody (MoAb) production. Two of the
      S-TAGs were composed of haptens related to the Thomsen-Friedenreich (TF) antigen,
      and their structures are beta Gal(1----3)-beta GalNAc (TF-beta) and beta
      Gal(1----3) alpha GalNAc (TF-alpha) (Gal = galactose; GaNAc =
      N-acetylgalactosamine). The third S-TAG was made up of Tn hapten groups of the
      structure alpha GalNAc-O-serine. MoAbs specific for TF-alpha and Tn were able to 
      be generated. All MoAbs generated against TF-beta cross-reacted with TF-alpha but
      not with Tn. None of the TF-alpha-specific MoAbs reacted with human carcinomas,
      whereas several TF-beta and Tn MoAbs were found to react with most human lung,
      colon, and breast carcinomas. It is believed that this is the first report of the
      use of synthetic carbohydrate cancer antigens for the production of anticancer
      MoAbs.
FAU - Longenecker, B M
AU  - Longenecker BM
FAU - Willans, D J
AU  - Willans DJ
FAU - MacLean, G D
AU  - MacLean GD
FAU - Selvaraj, S
AU  - Selvaraj S
FAU - Suresh, M R
AU  - Suresh MR
FAU - Noujaim, A A
AU  - Noujaim AA
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - J Natl Cancer Inst
JT  - Journal of the National Cancer Institute
JID - 7503089
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens, Neoplasm)
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Disaccharides)
RN  - 0 (Haptens)
RN  - 0 (Serum Albumin)
RN  - 0 (Tn antigen)
RN  - 3554-90-3 (Thomsen-Friedenreich antigen)
SB  - IM
MH  - *Antibodies, Monoclonal
MH  - Antigens, Neoplasm/*immunology
MH  - *Antigens, Tumor-Associated, Carbohydrate
MH  - Disaccharides/*immunology
MH  - Haptens/immunology
MH  - Humans
MH  - Neoplasms/diagnosis/*immunology
MH  - Serum Albumin/immunology
EDAT- 1987/03/01 00:00
MHDA- 1987/03/01 00:01
CRDT- 1987/03/01 00:00
PHST- 1987/03/01 00:00 [pubmed]
PHST- 1987/03/01 00:01 [medline]
PHST- 1987/03/01 00:00 [entrez]
PST - ppublish
SO  - J Natl Cancer Inst. 1987 Mar;78(3):489-96.

PMID- 14568956
OWN - NLM
STAT- MEDLINE
DCOM- 20040130
LR  - 20190516
IS  - 0022-1767 (Print)
IS  - 0022-1767 (Linking)
VI  - 171
IP  - 9
DP  - 2003 Nov 1
TI  - Complement regulatory protein C1 inhibitor binds to selectins and interferes with
      endothelial-leukocyte adhesion.
PG  - 4786-91
AB  - C1 inhibitor (C1INH), a member of the serine proteinase inhibitor (serpin)
      family, is an inhibitor of proteases in the complement system, the contact system
      of kinin generation, and the intrinsic coagulation pathway. It is the most
      heavily glycosylated plasma protein, containing 13 definitively identified
      glycosylation sites as well as an additional 7 potential glycosylation sites.
      C1INH consists of two distinct domains: a serpin domain and an amino-terminal
      domain. The serpin domain retains all the protease-inhibitory function, while the
      amino-terminal domain bears most of the glycosylation sites. The present studies 
      test the hypothesis that plasma C1INH bears sialyl Lewis(x)-related moieties and 
      therefore binds to selectin adhesion molecules. We demonstrated that plasma C1INH
      does express sialyl Lewis(x)-related moieties on its N-glycan as detected using
      mAb HECA-452 and CSLEX1. The data also show that plasma C1INH can bind to P- and 
      E-selectins by FACS and immunoprecipitation experiments. In a tissue culture
      model of endothelial-leukocyte adhesion, C1INH showed inhibition in a
      dose-dependent manner. Significant inhibition (>50%) was achieved at a
      concentration of 250 micro g/ml or higher. This discovery may suggest that C1INH 
      plays a role in the endothelial-leukocyte interaction during inflammation. It may
      also provide another example of the multifaceted anti-inflammatory effects of
      C1INH in various animal models and human diseases.
FAU - Cai, Shenghe
AU  - Cai S
AD  - Center for Blood Research, Harvard Medical School, Boston, MA 02115, USA.
FAU - Davis, Alvin E 3rd
AU  - Davis AE 3rd
LA  - eng
GR  - HD22082/HD/NICHD NIH HHS/United States
GR  - HD33727/HD/NICHD NIH HHS/United States
PT  - Journal Article
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - J Immunol
JT  - Journal of immunology (Baltimore, Md. : 1950)
JID - 2985117R
RN  - 0 (Complement C1)
RN  - 0 (Complement C1 Inactivator Proteins)
RN  - 0 (Complement C1 Inhibitor Protein)
RN  - 0 (E-Selectin)
RN  - 0 (Lewis X Antigen)
RN  - 0 (P-Selectin)
RN  - 0 (Protease Inhibitors)
RN  - 0 (SERPING1 protein, human)
RN  - 0 (Serpins)
SB  - AIM
SB  - IM
MH  - Animals
MH  - CHO Cells
MH  - Carbohydrate Conformation
MH  - Cell Adhesion/immunology
MH  - Cell Line
MH  - Complement C1/*metabolism
MH  - Complement C1 Inactivator Proteins/biosynthesis/*metabolism/physiology
MH  - Complement C1 Inhibitor Protein
MH  - Cricetinae
MH  - E-Selectin/*metabolism
MH  - Endothelium, Vascular/cytology/immunology/*metabolism
MH  - Humans
MH  - Leukocytes/cytology/immunology/*metabolism
MH  - Lewis X Antigen/biosynthesis/metabolism
MH  - P-Selectin/*metabolism
MH  - Protease Inhibitors/pharmacology
MH  - Protein Binding/immunology
MH  - Serpins/biosynthesis/blood/*metabolism/physiology
MH  - U937 Cells
EDAT- 2003/10/22 05:00
MHDA- 2004/01/31 05:00
CRDT- 2003/10/22 05:00
PHST- 2003/10/22 05:00 [pubmed]
PHST- 2004/01/31 05:00 [medline]
PHST- 2003/10/22 05:00 [entrez]
AID - 10.4049/jimmunol.171.9.4786 [doi]
PST - ppublish
SO  - J Immunol. 2003 Nov 1;171(9):4786-91. doi: 10.4049/jimmunol.171.9.4786.

PMID- 4016748
OWN - NLM
STAT- MEDLINE
DCOM- 19850828
LR  - 20071114
IS  - 0008-5472 (Print)
IS  - 0008-5472 (Linking)
VI  - 45
IP  - 8
DP  - 1985 Aug
TI  - Location and distribution of difucoganglioside (VI3NeuAcV3III3Fuc2nLc6) in normal
      and tumor tissues defined by its monoclonal antibody FH6.
PG  - 3711-7
AB  - The distribution of a novel difucoganglioside (6B ganglioside, NeuAc alpha
      2----3Gal beta 1----4[Fuc alpha 1----3]GlcNAc beta 1----3Gal beta 1----4[Fuc
      alpha 1----3]GlcNAc beta 1----3Gal beta 1----4Glc beta 1----1Cer) in various
      normal adult and fetal tissues, as well as in cancer tissues, has been studied by
      immunoperoxidase staining with a specific monoclonal antibody, FH6, directed to
      this antigen. A large variety of embryonic and fetal tissues (stomach, colon,
      small intestine, pancreas, esophagus, lung, and heart) showed a diffuse, weakly
      positive staining, particularly in the epithelial layer, up to the 70th to 80th
      day of gestation. However, no staining was observed in various normal adult
      tissues, including gastrointestinal and glandular epithelial tissues which were
      stained positively by antibody N-19-9 (directed to sialyl-Lea) or CSLEXI
      (directed to sialyl-Lex). FH6-positive loci were limited to the proximal
      convoluted tubuli in kidney and granulocytes. In contrast, 44 of 76 cases of
      cancer tissue tested, including gastric, colonic, lung, breast, and renal
      cancers, showed clearly positive staining. The intensity of staining in gastric
      and colonic cancer tissues by FH6 antibody was weaker and less frequent, although
      the incidence of positive staining for lung (50%) and breast cancer (86%) was
      significantly higher than that of the antigen stained by monoclonal antibody FH4 
      (Y. Fukushi, S. Hakomori, and T. Shepard, J. Exp. Med., 159: 506-520, 1984),
      which is directed to the asialo core of the FH6 antigen. The antigen levels in
      the serum of patients with various cancers, inflammatory diseases, and normal
      subjects were determined by radioimmunoassay. The antigen level was found to be
      significantly higher in the serum of some patients with cancer, particularly
      lung, liver, and pancreatic cancers, as compared with the serum levels in other
      types of cancer, noncancerous diseases, and normal subjects.
FAU - Fukushi, Y
AU  - Fukushi Y
FAU - Kannagi, R
AU  - Kannagi R
FAU - Hakomori, S
AU  - Hakomori S
FAU - Shepard, T
AU  - Shepard T
FAU - Kulander, B G
AU  - Kulander BG
FAU - Singer, J W
AU  - Singer JW
LA  - eng
GR  - CA19029/CA/NCI NIH HHS/United States
GR  - HD00836/HD/NICHD NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, Non-P.H.S.
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Cancer Res
JT  - Cancer research
JID - 2984705R
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens, Neoplasm)
RN  - 0 (Gangliosides)
RN  - 0 (fucogangliosides)
SB  - IM
MH  - Animals
MH  - Antibodies, Monoclonal/*immunology
MH  - Antigens, Neoplasm/*analysis
MH  - Digestive System/analysis
MH  - Gangliosides/*analysis
MH  - Humans
MH  - Mice
MH  - Neoplasm Staging
MH  - Neoplasms/analysis/*immunology
EDAT- 1985/08/01 00:00
MHDA- 1985/08/01 00:01
CRDT- 1985/08/01 00:00
PHST- 1985/08/01 00:00 [pubmed]
PHST- 1985/08/01 00:01 [medline]
PHST- 1985/08/01 00:00 [entrez]
PST - ppublish
SO  - Cancer Res. 1985 Aug;45(8):3711-7.

PMID- 15536336
OWN - NLM
STAT- MEDLINE
DCOM- 20050401
LR  - 20161020
IS  - 1541-2016 (Print)
IS  - 1533-4058 (Linking)
VI  - 12
IP  - 4
DP  - 2004 Dec
TI  - Expression of cellular adhesion proteins and abnormal glycoproteins in human
      aberrant crypt foci.
PG  - 350-5
AB  - Aberrant crypt foci (ACFs) may be the earliest recognizable histologic precursor 
      lesion for colon cancer. ACF may develop from a complex of events, including the 
      development of cryptal hyperproliferation, defects in the rate of apoptosis, and 
      abnormalities in cellular adhesion. In this study, we hypothesized that human ACF
      would exhibit discrete differences in cell adhesion proteins compared with normal
      mucosa of biologic markers associated with colon cancer. ACFs were isolated from 
      resected colon mucosa from 45 patients undergoing surgery for colon cancer. We
      evaluated the protein expression of 3 biologic markers that may be related to the
      progression of aberrant crypt foci to tumors: carcinoembryonic antigen,
      E-cadherin, and sialyl Tn antigen. In general, ACFs located near cancers in the
      right colon were more often hyperplastic than dysplastic; this was more
      noticeable in the left colon. Carcinoembryonic antigen expression was found to be
      more intense in apical portions of ACF crypts, with sialyl Tn antigen moderately 
      increased, whereas E-cadherin diffusely stained throughout crypts within ACFs.
      There are significant biologic changes in potential tumor markers that accompany 
      the early transformation of the normal glandular epithelium, some of which are
      expressed very early in the colon at the stage of appearance of ACF.
FAU - Wargovich, Michael J
AU  - Wargovich MJ
AD  - Division of Basic Research, South Carolina Cancer Center, University of South
      Carolina School of Medicine, Columbia, SC, USA.
      michael.wargovich@palmettohealth.org
FAU - Chang, Phyllis
AU  - Chang P
FAU - Velasco, Marco
AU  - Velasco M
FAU - Sinicrope, Frank
AU  - Sinicrope F
FAU - Eisenbrodt, Edward
AU  - Eisenbrodt E
FAU - Sellin, Joseph
AU  - Sellin J
LA  - eng
PT  - Journal Article
PL  - United States
TA  - Appl Immunohistochem Mol Morphol
JT  - Applied immunohistochemistry & molecular morphology : AIMM
JID - 100888796
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Biomarkers, Tumor)
RN  - 0 (Cadherins)
RN  - 0 (Carcinoembryonic Antigen)
RN  - 0 (Cell Adhesion Molecules)
RN  - 0 (Glycoproteins)
RN  - 0 (sialosyl-Tn antigen)
SB  - IM
MH  - Antigens, Tumor-Associated, Carbohydrate/analysis/metabolism
MH  - Biomarkers, Tumor/analysis/*metabolism
MH  - Cadherins/analysis/metabolism
MH  - Carcinoembryonic Antigen/analysis/metabolism
MH  - Cell Adhesion Molecules/*metabolism
MH  - Colon/cytology/immunology/metabolism
MH  - Colonic Neoplasms/diagnosis/*metabolism
MH  - Glycoproteins/analysis/*metabolism
MH  - Humans
MH  - Intestinal Mucosa/cytology/immunology/metabolism
MH  - Middle Aged
MH  - Precancerous Conditions/*metabolism
EDAT- 2004/11/13 09:00
MHDA- 2005/04/02 09:00
CRDT- 2004/11/13 09:00
PHST- 2004/11/13 09:00 [pubmed]
PHST- 2005/04/02 09:00 [medline]
PHST- 2004/11/13 09:00 [entrez]
AID - 00129039-200412000-00011 [pii]
PST - ppublish
SO  - Appl Immunohistochem Mol Morphol. 2004 Dec;12(4):350-5.

PMID- 12883744
OWN - NLM
STAT- MEDLINE
DCOM- 20040421
LR  - 20131121
IS  - 1021-335X (Print)
IS  - 1021-335X (Linking)
VI  - 10
IP  - 5
DP  - 2003 Sep-Oct
TI  - Biochemical characterization of soluble Tn glycoproteins from malignant effusions
      of patients with carcinomas.
PG  - 1577-85
AB  - The Tn determinant (GalNAc-O-Ser/Thr) is one of the most specific human tumor
      markers. In normal cells Tn is a cryptic structure in the peptide core of mucin
      type O-glycoproteins, and it is detected in an unmasked form in most human
      carcinomas evaluated by immunohistochemistry. Scarce data are available regarding
      the characteristics of soluble Tn bearing glycoproteins. We herein report the
      first comparative characterization of soluble Tn glycoproteins derived from
      different kinds of human tumors (breast, colon, gastric, ovarian and liver).
      Considerable heterogeneity was observed in the physicochemical properties of Tn
      soluble glycoproteins from all the tumor-associated effusions evaluated. In
      SDS-PAGE analysis Tn glycoproteins from liver and colon effusions migrated as a
      broad single major component (>500 kDa), while several components of >200 kDa
      were identified in samples from breast, ovarian, and gastric cancer. The results 
      of perchloric acid (PCA) treatment and CsCl gradient ultracentrifugation
      indicated that the Tn glycoproteins in effusion fluids correspond predominantly
      to mucin-like glycoproteins. However, in samples from patients with colon and
      liver cancer, a fraction of Tn glycoproteins formed part of the immune complexes 
      that precipitated in PCA, suggesting that the anti-Tn immune response in vivo
      could modify their physicochemical properties. The four apomucins evaluated
      (MUC1, MUC2, MUC5AC and MUC6) carried Tn epitopes in each of the effusions,
      indicating that soluble apomucin detection may reflect the abnormal expression of
      MUC genes inherent to these tumors. Taking together, these results indicate that 
      apomucin expression profile is responsible, at least in part, for the high
      heterogeneity of soluble Tn glycoproteins, and suggest that the identification of
      Tn determinant on the different soluble apomucins could be useful for the
      development of new diagnostic tools as well as to evaluate the anti-tumor immune 
      response in patients with cancer.
FAU - Freire, Teresa
AU  - Freire T
AD  - Depto. de Bioquimica, Laboratorio de Oncologia Basica, Facultad de Medicina,
      Universidad de la Republica, Montevideo, Uruguay.
FAU - Medeiros, Andrea
AU  - Medeiros A
FAU - Reis, Celso A
AU  - Reis CA
FAU - Real, Francisco X
AU  - Real FX
FAU - Osinaga, Eduardo
AU  - Osinaga E
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - Greece
TA  - Oncol Rep
JT  - Oncology reports
JID - 9422756
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Epitopes)
RN  - 0 (Glycoproteins)
RN  - 0 (Perchlorates)
RN  - 0 (Tn antigen)
SB  - IM
MH  - Antibodies, Monoclonal/metabolism
MH  - Antigens, Tumor-Associated, Carbohydrate/*biosynthesis/metabolism
MH  - Blotting, Western
MH  - Breast Neoplasms/metabolism
MH  - Carcinoma/*metabolism
MH  - Centrifugation, Density Gradient
MH  - Colon/metabolism
MH  - Dose-Response Relationship, Drug
MH  - Electrophoresis, Polyacrylamide Gel
MH  - Enzyme-Linked Immunosorbent Assay
MH  - Epitopes
MH  - Female
MH  - Glycoproteins/chemistry
MH  - Humans
MH  - Immunoblotting
MH  - Immunohistochemistry
MH  - Liver/metabolism
MH  - Ovarian Neoplasms/metabolism
MH  - Perchlorates/pharmacology
MH  - Stomach Neoplasms/metabolism
EDAT- 2003/07/29 05:00
MHDA- 2004/04/22 05:00
CRDT- 2003/07/29 05:00
PHST- 2003/07/29 05:00 [pubmed]
PHST- 2004/04/22 05:00 [medline]
PHST- 2003/07/29 05:00 [entrez]
PST - ppublish
SO  - Oncol Rep. 2003 Sep-Oct;10(5):1577-85.

PMID- 9305871
OWN - NLM
STAT- MEDLINE
DCOM- 19971023
LR  - 20190508
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 272
IP  - 39
DP  - 1997 Sep 26
TI  - Oligosaccharides expressed on MUC1 produced by pancreatic and colon tumor cell
      lines.
PG  - 24198-202
AB  - MUC1 is expressed at the apical surface of ductal epithelia of tissues, including
      breast, pancreas, airway, and the gastrointestinal tract, where its functions
      include lubrication and protection of the epithelia. In addition, roles for MUC1 
      have been suggested in both adhesive and antiadhesive properties of tumor cells, 
      and extensive O-glycosylation of the MUC1 tandem repeat domain may contribute to 
      these functions. Little information is available on the specific O-glycosylation 
      of MUC1. One problem in identifying different MUC1 glycoforms has been that
      monoclonal antibodies raised against the MUC1 core protein recognize epitopes in 
      the tandem repeat domain, which is often glycosylated to an extent that obscures 
      these epitopes. We developed an epitope-tagged form of MUC1 that allowed the
      detection of multiple MUC1 glycoforms and established the presence of a number of
      important blood group and tumor-associated carbohydrate antigens on MUC1
      expressed by two pancreatic tumor cell lines (Panc-1 and S2-013) and two colon
      tumor cell lines (Caco-2 and HT-29). Antigens detected include sialyl-Lewisa,
      sialyl-Lewisc, sialyl-Lewisx, and sialyl-Tn.
FAU - Burdick, M D
AU  - Burdick MD
AD  - Eppley Institute for Research in Cancer and Allied Diseases, University of
      Nebraska Medical Center, Omaha, Nebraska 68198-6805, USA.
FAU - Harris, A
AU  - Harris A
FAU - Reid, C J
AU  - Reid CJ
FAU - Iwamura, T
AU  - Iwamura T
FAU - Hollingsworth, M A
AU  - Hollingsworth MA
LA  - eng
GR  - CA57362/CA/NCI NIH HHS/United States
GR  - CA69234/CA/NCI NIH HHS/United States
GR  - DK46589/DK/NIDDK NIH HHS/United States
GR  - etc.
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Antibodies)
RN  - 0 (Epitopes)
RN  - 0 (Mucin-1)
RN  - 0 (Oligosaccharides)
SB  - IM
MH  - Antibodies/immunology
MH  - Colonic Neoplasms/*metabolism/pathology
MH  - Epitopes/metabolism
MH  - Glycosylation
MH  - Humans
MH  - Mucin-1/genetics/immunology/*metabolism
MH  - Oligosaccharides/*metabolism
MH  - Pancreatic Neoplasms/*metabolism/pathology
MH  - Transfection
MH  - Tumor Cells, Cultured
EDAT- 1997/09/26 00:00
MHDA- 1997/09/26 00:01
CRDT- 1997/09/26 00:00
PHST- 1997/09/26 00:00 [pubmed]
PHST- 1997/09/26 00:01 [medline]
PHST- 1997/09/26 00:00 [entrez]
AID - 10.1074/jbc.272.39.24198 [doi]
PST - ppublish
SO  - J Biol Chem. 1997 Sep 26;272(39):24198-202. doi: 10.1074/jbc.272.39.24198.

PMID- 1609521
OWN - NLM
STAT- MEDLINE
DCOM- 19920723
LR  - 20041117
IS  - 0042-9007 (Print)
IS  - 0042-9007 (Linking)
VI  - 62
IP  - 3
DP  - 1992
TI  - Serological and chemical specificities of twelve monoclonal anti-Lea and anti-Leb
      antibodies.
PG  - 180-9
AB  - The serological specificities of twelve hybridomas were compared as to their
      chemical reactivity as determined using direct binding to synthetic carbohydrate 
      structures. All anti-Lea cross-react with type-1-precursor structures and three
      different variants of anti-Lea could be defined by their binding to
      type-3-precursor chains, sialylated compounds and the monosaccharide D-galactose.
      Three major reactivity patterns were also identified among anti-Leb reagents.
      Anti-LebL cross-react with Lea and do not significantly bind to H-related
      structures. Anti-LebH,L had both anti-LebL-like activity (cross-reaction with
      Lea) and anti-LebH-like activity (cross-reaction with H). Finally, anti-LebH
      cross-reacts strongly with H compounds and do not bind to Lea. The binding
      pattern of anti-LebL suggests that these antibodies have lower affinity for ALeb 
      and BLeb pentasaccharides than anti-LebH. All these specificities are not
      absolute, but rather are expressed as members of a quantitative progressive
      varying series, suggesting the existence of a whole range of antibody
      specificities gradually changing from Lea----Lea,b----LebL----LebH,L----LebH. The
      results suggest that anti-LebL will always cross-react with Lea and that
      anti-LebH will always cross-react with H related structures. However, under
      certain well-defined conditions these cross-reactions may not be apparent and
      antibodies might behave as specific anti-Lea or anti-Leb in certain tests.
FAU - Good, A H
AU  - Good AH
AD  - Chembiomed Ltd., Edmonton, Canada.
FAU - Yau, O
AU  - Yau O
FAU - Lamontagne, L R
AU  - Lamontagne LR
FAU - Oriol, R
AU  - Oriol R
LA  - eng
PT  - Journal Article
PL  - England
TA  - Vox Sang
JT  - Vox sanguinis
JID - 0413606
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Lewis Blood-Group System)
RN  - 0 (Oligosaccharides)
SB  - IM
CIN - Vox Sang. 1994;66(4):300. PMID: 8079458
MH  - Antibodies, Monoclonal/*immunology
MH  - Antibody Specificity/immunology
MH  - Carbohydrate Sequence
MH  - Cluster Analysis
MH  - Cross Reactions/immunology
MH  - Enzyme-Linked Immunosorbent Assay
MH  - Hemagglutination Tests
MH  - Humans
MH  - Lewis Blood-Group System/genetics/*immunology
MH  - Molecular Sequence Data
MH  - Oligosaccharides/*immunology
EDAT- 1992/01/01 00:00
MHDA- 1992/01/01 00:01
CRDT- 1992/01/01 00:00
PHST- 1992/01/01 00:00 [pubmed]
PHST- 1992/01/01 00:01 [medline]
PHST- 1992/01/01 00:00 [entrez]
PST - ppublish
SO  - Vox Sang. 1992;62(3):180-9.

PMID- 9023982
OWN - NLM
STAT- MEDLINE
DCOM- 19970307
LR  - 20171116
IS  - 0192-253X (Print)
IS  - 0192-253X (Linking)
VI  - 19
IP  - 4
DP  - 1996
TI  - Origin of primordial germ cells in the prestreak chick embryo.
PG  - 290-301
AB  - The temporal and spatial pattern of segregation of the avian germline from the
      formation of the area pellucida to the beginning of primitive streak formation
      (stages VII-XIV, EG&K) was investigated using the culture of whole embryos and
      central and peripheral embryo fragments on vitelline membranes at stages VII-IX, 
      immunohistological analysis of whole mount embryos and sections with monoclonal
      antibodies MC-480 against stage-specific embryonic antigen-1 (SSEA-1) and EMA-1, 
      and with the culture of dispersed blastoderms at stages IX-XIV with and without
      on STO feeder layer. Whole embryos at intrauterine stages developed up to the
      formation of the primitive streak despite the absence of area pellucida
      expansion. Primordial germ cells (PGCs) appeared in the cultures of whole embryos
      and only in central fragments containing a partially formed area pellucida at
      stages VII-IX. When individual stage IX-XIV embryos were dispersed and cultured
      without a feeder layer, 25-45 PGCs/embryo were detected only with stage X-XIV,
      but not with stage IX blastoderms. However, the culture of dispersed cells from
      the area pellucida of stages IX-XIII on STO feeder layers yielded about 150
      PGCs/embryo. The carbohydrate epitopes recognized by anti-SSEA-1 and EMA-1 first 
      appeared at stage X on cells in association with polyingressing cells on the
      ventral surface of the epiblast and later on the dorsal surface of the hypoblast.
      The SSEA-1-positive hypoblast cells gave rise to chicken PGCs when cultured on a 
      feeder layer of quail blastodermal cells. From these observations, we propose
      that the segregation and development of avian germline is a gradual, epigenetic
      process associated with the translocation of SSEA-1/EMA-1-positive cells from the
      ventral surface of the area pellucida at stage X to the dorsal side of the
      hypoblast at stages XI-XIV.
FAU - Karagenc, L
AU  - Karagenc L
AD  - Department of Poultry Science, North Carolina State University, Raleigh, NC
      27695, USA.
FAU - Cinnamon, Y
AU  - Cinnamon Y
FAU - Ginsburg, M
AU  - Ginsburg M
FAU - Petitte, J N
AU  - Petitte JN
LA  - eng
GR  - N01-HD-2-3144/HD/NICHD NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, Non-P.H.S.
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Dev Genet
JT  - Developmental genetics
JID - 7909963
RN  - 0 (Antigens, Surface)
RN  - 0 (Lewis X Antigen)
SB  - IM
MH  - Animals
MH  - Antigens, Surface/analysis
MH  - *Blastocyst/chemistry/cytology
MH  - Blastoderm/chemistry/cytology
MH  - Cell Culture Techniques
MH  - Chick Embryo
MH  - Coculture Techniques
MH  - *Germ Cells
MH  - Lewis X Antigen/analysis
MH  - Mice
MH  - Quail
MH  - Vitelline Membrane
EDAT- 1996/01/01 00:00
MHDA- 2000/06/20 09:00
CRDT- 1996/01/01 00:00
PHST- 1996/01/01 00:00 [pubmed]
PHST- 2000/06/20 09:00 [medline]
PHST- 1996/01/01 00:00 [entrez]
AID - 10.1002/(SICI)1520-6408(1996)19:4<290::AID-DVG2>3.0.CO;2-4 [pii]
AID - 10.1002/(SICI)1520-6408(1996)19:4<290::AID-DVG2>3.0.CO;2-4 [doi]
PST - ppublish
SO  - Dev Genet. 1996;19(4):290-301. doi:
      10.1002/(SICI)1520-6408(1996)19:4<290::AID-DVG2>3.0.CO;2-4.

PMID- 23747419
OWN - NLM
STAT- MEDLINE
DCOM- 20130909
LR  - 20130708
IS  - 1090-2104 (Electronic)
IS  - 0006-291X (Linking)
VI  - 436
IP  - 3
DP  - 2013 Jul 5
TI  - Influenza virus utilizes N-linked sialoglycans as receptors in A549 cells.
PG  - 394-9
LID - 10.1016/j.bbrc.2013.05.112 [doi]
LID - S0006-291X(13)00919-4 [pii]
AB  - Influenza viruses (IFVs) recognize sialoglycans expressed on the host cell
      surface. To understand the mechanisms underlying tissue and host tropisms of IFV,
      it is essential to elucidate the molecular interaction of the virus with the host
      sialoglycan receptor. We established and applied a new monoclonal antibody, clone
      HYB4, which specifically recognizes the Neu5Acalpha2-3 determinant at the
      non-reducing terminal Gal residue of both glycoproteins and gangliosides to
      investigate the biochemical properties of IFV receptors in A549 cells. HYB4
      significantly blocked virus binding to A549 cells in a dose-dependent manner.
      Virus overlay assay indicated that several glycoproteins with molecular masses of
      80-120 kDa of A549 cells were commonly recognized by different subtypes of IFV,
      such as H1N1 and H3N2. H1N1 virus binding to the glycoproteins was diminished by 
      pretreatment with either sialidase or PNGase F. On TLC-immunostaining experiments
      with HYB4, GM(3) ganglioside was only detected in A549 cells. Interestingly, this
      antibody bound to GM(3) gangliosides on TLC and plastic surfaces, but not on
      lipid bilayers. In comparison with the recognition of Maackia amurensis lectins, 
      HYB4 exclusively recognized Neu5Acalpha2-3Galbeta1-4GlcNAc residues expressed on 
      glycoproteins. These results strongly suggest that N-linked sialoglycans with the
      Neu5Acalpha2-3 determinant on several glycoproteins are receptors for influenza
      virus in A549 cells.
CI  - Copyright (c) 2013 Elsevier Inc. All rights reserved.
FAU - Hidari, Kazuya I P J
AU  - Hidari KI
AD  - Department of Biochemistry, School of Pharmaceutical Sciences, University of
      Shizuoka, 52-1 Yada, Suruga-ku, Shizuoka-shi, Shizuoka 422-8526, Japan.
      hidari@jc.u-aizu.ac.jp
FAU - Yamaguchi, Maho
AU  - Yamaguchi M
FAU - Ueno, Fumihiko
AU  - Ueno F
FAU - Abe, Tomoko
AU  - Abe T
FAU - Yoshida, Kazuhiro
AU  - Yoshida K
FAU - Suzuki, Takashi
AU  - Suzuki T
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20130604
PL  - United States
TA  - Biochem Biophys Res Commun
JT  - Biochemical and biophysical research communications
JID - 0372516
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (G(M3) Ganglioside)
RN  - 0 (Lipid Bilayers)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Phytohemagglutinins)
RN  - 0 (Plant Lectins)
RN  - 0 (Receptors, Cell Surface)
RN  - 0 (Receptors, Virus)
RN  - 0 (Sambucus nigra lectins)
RN  - 0 (leukoagglutinins, plants)
RN  - 0 (sialic acid receptor)
RN  - EC 3.2.1.18 (Neuraminidase)
RN  - EC 3.2.2.22 (Ribosome Inactivating Proteins)
RN  - EC 3.5.1.52 (Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase)
SB  - IM
MH  - Antibodies, Monoclonal/metabolism/pharmacology
MH  - Antibody Specificity
MH  - Cell Line, Tumor
MH  - Dose-Response Relationship, Drug
MH  - G(M3) Ganglioside/metabolism
MH  - Host-Pathogen Interactions
MH  - Humans
MH  - Influenza A Virus, H1N1 Subtype/*metabolism
MH  - Influenza A Virus, H3N2 Subtype/*metabolism
MH  - Lipid Bilayers/metabolism
MH  - Maackia/chemistry
MH  - Membrane Glycoproteins/metabolism
MH  - Molecular Weight
MH  - Neuraminidase/pharmacology
MH  - Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase/pharmacology
MH  - Phytohemagglutinins/metabolism
MH  - Plant Lectins/metabolism
MH  - Receptors, Cell Surface
MH  - Receptors, Virus/*metabolism
MH  - Ribosome Inactivating Proteins/metabolism
MH  - Virus Attachment/drug effects
OTO - NOTNLM
OT  - HA
OT  - IFV
OT  - Influenza virus
OT  - MAH
OT  - MAM
OT  - Maackia amurensis hemagglutinin
OT  - Maackia amurensis mitogen
OT  - Monoclonal antibody
OT  - N-acetylneuraminic acid
OT  - N-glycolylneuraminic acid
OT  - Neu5Ac
OT  - Neu5Gc
OT  - Receptor
OT  - SPR
OT  - SSA
OT  - Sambucus sieboldiana agglutinin
OT  - Sia
OT  - Siaalpha2-3 glycans
OT  - TLC
OT  - hemagglutinin
OT  - influenza virus
OT  - sialic acid
OT  - surface plasmon resonance
OT  - thin-layer chromatography
EDAT- 2013/06/12 06:00
MHDA- 2013/09/10 06:00
CRDT- 2013/06/11 06:00
PHST- 2013/05/18 00:00 [received]
PHST- 2013/05/27 00:00 [accepted]
PHST- 2013/06/11 06:00 [entrez]
PHST- 2013/06/12 06:00 [pubmed]
PHST- 2013/09/10 06:00 [medline]
AID - S0006-291X(13)00919-4 [pii]
AID - 10.1016/j.bbrc.2013.05.112 [doi]
PST - ppublish
SO  - Biochem Biophys Res Commun. 2013 Jul 5;436(3):394-9. doi:
      10.1016/j.bbrc.2013.05.112. Epub 2013 Jun 4.

PMID- 16770733
OWN - NLM
STAT- MEDLINE
DCOM- 20070322
LR  - 20181113
IS  - 0364-3190 (Print)
IS  - 0364-3190 (Linking)
VI  - 31
IP  - 5
DP  - 2006 May
TI  - Differential binding to glycotopes among the layers of three mammalian retinal
      neurons by man-containing N-linked glycan, T(alpha) (Galbeta1-3GalNAcalpha1-), Tn
      (GalNAcalpha1-Ser/Thr) and I (beta)/II (beta) (Galbeta1-3/4GlcNAcbeta-) reactive 
      lectins.
PG  - 619-28
AB  - Carbohydrate structures between retinal neurons and retinal pigment epithelium
      (RPE) play an important role in maintaining the integrity of retinal adhesion to 
      underlying RPE, and in retinal detachment pathogenesis. Since relevant knowledge 
      is still in the primary stage, glycotopes on the adult retina of mongrel canines 
      (dog), micropigs and Sprague-Dawley rats were examined by lectino-histochemistry,
      using a panel of 16 different lectins. Paraffin sections of eyes were stained
      with biotinylated lectins, and visualized by streptavidin-peroxidase and
      diaminobenzidine staining. Mapping the affinity profiles, it is concluded that:
      (i) all sections of the retina reacted well with Morniga M, suggesting that
      N-linked glycans are present in all layers of the retina; (ii) no detectable
      human blood group ABH active glycotopes were found among retinal layers; (iii)
      outer and inner segments contained glycoconjugates rich in ligands reacting with 
      T (alpha) (Galbeta1-3GalNAcalpha1-Ser/Thr) and Tn (GalNAcalpha1-Ser/Thr) specific
      lectins; (iv) cone cells of retina specifically bound peanut agglutinin (PNA),
      which recognizes T (alpha) residues and could be used as a specific marker for
      these photoreceptors; (v) the retinas of rat, dog and pig, had a similar binding 
      profile but with different intensity; (vi) each retinal layer had its own binding
      characteristic. This information may provide useful background knowledge for
      normal retinal physiology and miscellaneous retinal diseases, including retinal
      detachment (RD) and age-related macular degeneration (ARMD).
FAU - Wu, Wei-Chi
AU  - Wu WC
AD  - Department of Ophthalmology, Chang Gung Memorial Hospital, Tao-yuan, Taiwan.
FAU - Lai, Chi-Chun
AU  - Lai CC
FAU - Liu, Jia-Hau
AU  - Liu JH
FAU - Singh, Tanuja
AU  - Singh T
FAU - Li, Lien-Ming
AU  - Li LM
FAU - Peumans, Willy J
AU  - Peumans WJ
FAU - Van Damme, Els J M
AU  - Van Damme EJ
FAU - Wu, Albert M
AU  - Wu AM
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20060523
PL  - United States
TA  - Neurochem Res
JT  - Neurochemical research
JID - 7613461
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Epitopes)
RN  - 0 (Glycoconjugates)
RN  - 0 (Glycoproteins)
RN  - 0 (Lectins)
RN  - 0 (Monosaccharides)
RN  - 0 (Polysaccharides)
RN  - 0 (Tn antigen)
RN  - PHA4727WTP (Mannose)
SB  - IM
MH  - Animals
MH  - Antigens, Tumor-Associated, Carbohydrate/chemistry/*metabolism
MH  - Carbohydrate Conformation
MH  - Carbohydrate Sequence
MH  - Dogs
MH  - *Epitopes
MH  - Glycoconjugates/chemistry/*metabolism
MH  - Glycoproteins/metabolism
MH  - Humans
MH  - Immunohistochemistry
MH  - Lectins/chemistry/*metabolism
MH  - Mannose/*chemistry
MH  - Molecular Sequence Data
MH  - Monosaccharides/chemistry/metabolism
MH  - Pigment Epithelium of Eye/cytology/metabolism
MH  - Polysaccharides/chemistry/*metabolism
MH  - Rats
MH  - Rats, Sprague-Dawley
MH  - Retina/*cytology
MH  - Swine
EDAT- 2006/06/14 09:00
MHDA- 2007/03/23 09:00
CRDT- 2006/06/14 09:00
PHST- 2005/09/23 00:00 [received]
PHST- 2006/02/22 00:00 [accepted]
PHST- 2006/06/14 09:00 [pubmed]
PHST- 2007/03/23 09:00 [medline]
PHST- 2006/06/14 09:00 [entrez]
AID - 10.1007/s11064-006-9060-8 [doi]
PST - ppublish
SO  - Neurochem Res. 2006 May;31(5):619-28. doi: 10.1007/s11064-006-9060-8. Epub 2006
      May 23.

PMID- 3008996
OWN - NLM
STAT- MEDLINE
DCOM- 19860523
LR  - 20151119
IS  - 0008-5472 (Print)
IS  - 0008-5472 (Linking)
VI  - 46
IP  - 5
DP  - 1986 May
TI  - Quantitative and qualitative characterization of human cancer-associated serum
      glycoprotein antigens expressing fucosyl or sialyl-fucosyl type 2 chain
      polylactosamine.
PG  - 2619-26
AB  - The quantity of tumor-associated antigens carrying type 2 chain polylactosamines 
      with four types of fucosyl determinants, LeX (X-hapten), poly-LeX, sialyl LeX,
      and LeY (Y-hapten), present in sera of patients with various malignant and
      non-malignant disorders, as well as the qualitative chemical properties of the
      carrier molecules in sera, have been investigated using four monoclonal
      antibodies, each of which defines one of these determinants. The following
      findings are of particular importance: the serum levels of LeX defined by
      antibody FH2 and poly-LeX defined by ACFH18 in patients with cancer were
      occasionally high (incidence about 10%); however, the majority of patients did
      not show elevated levels; the serum level of the antigen, defined by monoclonal
      antibody FH6 (termed sialyl LeX-i since this determinant is carried by i
      antigen), was significantly high in patients with cancers originating from organs
      from which adenocarcinomas often develop. For example, among various types of
      lung cancer, only adenocarcinoma but not squamous cell carcinoma, small cell
      carcinoma, or large cell carcinoma showed a high level of sialyl LeX-i antigen in
      sera. The incidence of high antigen levels in sera of patients with
      adenocarcinomas of lung was as high as 76% of the observed cases; the serum level
      of Ley (Y-hapten) was frequently high in patients with hepatoma (incidence, 34%);
      sialyl LeX-i antigen was separated on gel filtration as a glycoprotein with an
      average molecular weight greater than 10(6). It was characterized by its
      susceptibility to basehydrolysis, Pronase digestion, and sialidase and
      endo-beta-galactosidase treatment and is assumed to be a high molecular weight
      mucin-type glycoprotein; sialyl LeX-i antigen expressed in sera of patients with 
      cancer was soluble in perchloric acid, while the same antigen in sera of patients
      with noncancerous diseases and normal subjects was mostly insoluble in perchloric
      acid. LeX, a poly-LeX, and essentially all LeY antigens in sera of patients with 
      cancer were perchloric acid-insoluble.
FAU - Kannagi, R
AU  - Kannagi R
FAU - Fukushi, Y
AU  - Fukushi Y
FAU - Tachikawa, T
AU  - Tachikawa T
FAU - Noda, A
AU  - Noda A
FAU - Shin, S
AU  - Shin S
FAU - Shigeta, K
AU  - Shigeta K
FAU - Hiraiwa, N
AU  - Hiraiwa N
FAU - Fukuda, Y
AU  - Fukuda Y
FAU - Inamoto, T
AU  - Inamoto T
FAU - Hakomori, S
AU  - Hakomori S
AU  - et al.
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Cancer Res
JT  - Cancer research
JID - 2984705R
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens, Neoplasm)
RN  - 0 (Glycoproteins)
RN  - 0 (Lewis Blood-Group System)
RN  - 0 (Perchlorates)
RN  - 0 (Sialoglycoproteins)
SB  - IM
MH  - Antibodies, Monoclonal
MH  - Antigens, Neoplasm/*analysis
MH  - Carcinoma, Hepatocellular/blood/immunology
MH  - Glycoproteins/*blood/immunology
MH  - Humans
MH  - Lewis Blood-Group System/*immunology
MH  - Liver Neoplasms
MH  - Lung Neoplasms/blood/immunology
MH  - Neoplasms/blood/*immunology
MH  - Perchlorates
MH  - Sialoglycoproteins/blood/immunology
MH  - Solubility
EDAT- 1986/05/01 00:00
MHDA- 1986/05/01 00:01
CRDT- 1986/05/01 00:00
PHST- 1986/05/01 00:00 [pubmed]
PHST- 1986/05/01 00:01 [medline]
PHST- 1986/05/01 00:00 [entrez]
PST - ppublish
SO  - Cancer Res. 1986 May;46(5):2619-26.

PMID- 3796623
OWN - NLM
STAT- MEDLINE
DCOM- 19870127
LR  - 20151119
IS  - 0161-5890 (Print)
IS  - 0161-5890 (Linking)
VI  - 23
IP  - 7
DP  - 1986 Jul
TI  - A monoclonal antibody defining a binary N-acetyllactosaminyl structure in
      lactoisooctaosylceramide (IV6Gal beta 1----4GlcNAcnLc6): a useful probe for
      determining differential glycosylation patterns between normal and transformed
      human fibroblasts.
PG  - 747-54
AB  - Monoclonal antibodies A5 and C6 have been reported previously to recognize
      developmentally regulated determinants involving N-acetyllactosamine [Fenderson
      B. A., O'Brien D. A., Millette C. F. and Eddy E. M. (1984) Devl Biol. 103,
      117-128]. In the present study, the specificity of these antibodies was
      determined by solid-phase radioimmunoassay and by thin-layer chromatography
      immunostaining using purified glycolipid standards. Antibody A5 recognized
      N-acetyllactosamine (type 2 chain; Gal beta 1----4GlcNAc beta 1----3R),
      irrespective of branching status. In contrast antibody C6 recognized the binary
      N-acetyllactosamine structure carried on lactoisooctaosylceramide. Antibody C6
      did not react with sialosyl or alpha-galactosyl derivatives of the isooctaosyl
      structure, including human G10, G8 and bovine G9. Thus, unlike other anti-I
      antibodies, C6 provides a specific probe for both branching status and absence of
      terminal chain modification. Monoclonal antibodies A5, C6 and anti-I(Ma) were
      used to investigate glycosylation changes associated with oncogenic
      transformation. In contrast to results with lectins, these antibodies
      preferentially labeled the major glycoproteins of SV40-transformed human
      embryonic lung fibroblasts, including GP80, GP180, GP200 and GP250. The results
      suggest that increased expression of unsubstituted polylactosamine core structure
      at the cell surface follows SV40-transformation.
FAU - Fenderson, B A
AU  - Fenderson BA
FAU - Nichols, E J
AU  - Nichols EJ
FAU - Clausen, H
AU  - Clausen H
FAU - Hakomori, S I
AU  - Hakomori SI
LA  - eng
GR  - GM23100/GM/NIGMS NIH HHS/United States
GR  - HD18704/HD/NICHD NIH HHS/United States
GR  - HL31232/HL/NHLBI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - England
TA  - Mol Immunol
JT  - Molecular immunology
JID - 7905289
RN  - 0 (Amino Sugars)
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Glycoproteins)
RN  - 0 (Lactosylceramides)
RN  - 104042-02-6 (lactoisooctaosylceramide)
RN  - 3Y5B2K5OOK (N-acetyllactosamine)
SB  - IM
MH  - Adult
MH  - Amino Sugars/analysis/*immunology
MH  - Antibodies, Monoclonal/*immunology
MH  - Antibody Specificity
MH  - Cell Line
MH  - *Cell Transformation, Neoplastic
MH  - Electrophoresis, Polyacrylamide Gel
MH  - Fibroblasts/immunology
MH  - Glycoproteins/analysis
MH  - Humans
MH  - Lactosylceramides/immunology
EDAT- 1986/07/01 00:00
MHDA- 1986/07/01 00:01
CRDT- 1986/07/01 00:00
PHST- 1986/07/01 00:00 [pubmed]
PHST- 1986/07/01 00:01 [medline]
PHST- 1986/07/01 00:00 [entrez]
PST - ppublish
SO  - Mol Immunol. 1986 Jul;23(7):747-54.

PMID- 7999432
OWN - NLM
STAT- MEDLINE
DCOM- 19950124
LR  - 20180113
IS  - 0959-8049 (Print)
IS  - 0959-8049 (Linking)
VI  - 30A
IP  - 9
DP  - 1994
TI  - Sialyl-Tn expression in gastric carcinoma.
PG  - 1398-9
FAU - Carneiro, F
AU  - Carneiro F
FAU - David, L
AU  - David L
FAU - Sobrinho-Simoes, M
AU  - Sobrinho-Simoes M
LA  - eng
PT  - Comment
PT  - Letter
PL  - England
TA  - Eur J Cancer
JT  - European journal of cancer (Oxford, England : 1990)
JID - 9005373
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Biomarkers, Tumor)
RN  - 0 (sialosyl-Tn antigen)
SB  - IM
CON - Eur J Cancer. 1993;29A(13):1820-3. PMID: 8260233
MH  - Antigens, Tumor-Associated, Carbohydrate/*analysis
MH  - Biomarkers, Tumor/*analysis
MH  - Humans
MH  - Prognosis
MH  - Stomach Neoplasms/*chemistry
EDAT- 1994/01/01 00:00
MHDA- 1994/01/01 00:01
CRDT- 1994/01/01 00:00
PHST- 1994/01/01 00:00 [pubmed]
PHST- 1994/01/01 00:01 [medline]
PHST- 1994/01/01 00:00 [entrez]
AID - 0959-8049(94)90194-5 [pii]
PST - ppublish
SO  - Eur J Cancer. 1994;30A(9):1398-9.

PMID- 6987651
OWN - NLM
STAT- MEDLINE
DCOM- 19800523
LR  - 20190501
IS  - 0027-8424 (Print)
IS  - 0027-8424 (Linking)
VI  - 77
IP  - 1
DP  - 1980 Jan
TI  - I and i antigens of human peripheral blood lymphocytes cocap with receptors for
      concanavalin A.
PG  - 376-80
AB  - Surface immunofluorescence experiments using a human anti-i and two anti-I
      antisera have been performed on human peripheral blood lymphocytes. These are
      known to contain cold-reactive monoclonal IgM antibodies against the carbohydrate
      sequence: (formula: see text). A high proportion of B- and T-type lymphocytes
      express these I and i determinants. In the presence of anti-human immunoglobulin,
      the cold-reactive membrane-associated complexes of I-anti-I and i-anti-i become
      stabilized, and redistribution (with patching and capping) can be elicited at 37 
      degrees C. Dual fluorescence experiments have shown striking concordant staining 
      of I or i (fluorescein) caps and patches with concanavalin A (rhodamine) reactive
      sites on normal and leukemic cells, suggesting that a proportion of I and i
      active structures of lymphocyte membranes are structurally associated or
      physiologically coupled with glycoproteins carrying oligosaccharides with
      branched mannosyl cores.
FAU - Feizi, T
AU  - Feizi T
FAU - Kapadia, A
AU  - Kapadia A
FAU - Yount, W J
AU  - Yount WJ
LA  - eng
PT  - Journal Article
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Proc Natl Acad Sci U S A
JT  - Proceedings of the National Academy of Sciences of the United States of America
JID - 7505876
RN  - 0 (Antigens, Surface)
RN  - 0 (Mannosides)
RN  - 0 (Receptors, Concanavalin A)
SB  - IM
MH  - *Antigens, Surface
MH  - Fluorescent Antibody Technique
MH  - Humans
MH  - *Immunologic Capping
MH  - Lymphocytes/*immunology
MH  - Mannosides
MH  - Receptors, Concanavalin A/*metabolism
PMC - PMC348273
EDAT- 1980/01/01 00:00
MHDA- 1980/01/01 00:01
CRDT- 1980/01/01 00:00
PHST- 1980/01/01 00:00 [pubmed]
PHST- 1980/01/01 00:01 [medline]
PHST- 1980/01/01 00:00 [entrez]
AID - 10.1073/pnas.77.1.376 [doi]
PST - ppublish
SO  - Proc Natl Acad Sci U S A. 1980 Jan;77(1):376-80. doi: 10.1073/pnas.77.1.376.

PMID- 15464996
OWN - NLM
STAT- MEDLINE
DCOM- 20041228
LR  - 20071114
IS  - 0006-291X (Print)
IS  - 0006-291X (Linking)
VI  - 324
IP  - 1
DP  - 2004 Nov 5
TI  - Gangliosides of organ-confined versus metastatic androgen-receptor-negative
      prostate cancer.
PG  - 154-65
AB  - Prior development of a unique androgen-receptor (AR)-negative cell line (HH870)
      from organ-confined (T2b) human prostate cancer (CaP) enabled comparison of the
      gangliosides associated with normal and neoplastic prostate epithelial cells,
      organ-confined versus metastatic (DU 145, PC-3), and AR-negative versus
      AR-positive CaP cell lines. Resorcinol-HCl and specific monoclonal antibodies
      were used to characterize gangliosides on 2D-chromatograms, and to visualize them
      on the cell surface with confocal-fluorescence microscopy. AR-negative cells
      expressed GM1b, GM2, GD2, GD1a, and GM3. GM1a, GD1b, and GT1b were undetectable. 
      GM1b and GD1a were more prominent in AR-negative than in AR-positive cells. PC-3 
      and HH870 cells were unique in the expression of O-acetylGD2 (O-AcGD2) and two
      alpha2,3-sialidase-resistant, alkali-susceptible GMR17-reactive gangliosides.
      Expression of GD1a, GM1b, doublets of GD3, GD2, and O-AcGD2, and the presence of 
      an additional alkali-labile-14.G2a-reactive ganglioside, two alkali-susceptible, 
      and three alkali-resistant GMR17-reactive gangliosides makes HH870 a potential
      component of a polyvalent-vaccine for active-specific immunotherapy of CaP.
FAU - Ravindranath, Mepur H
AU  - Ravindranath MH
AD  - Laboratory of Glycoimmunotherapy, John Wayne Cancer Institute, 2200 Santa Monica 
      Blvd., Santa Monica, CA 90404-2302, USA. Ravindranathm@jwci.org
FAU - Muthugounder, Sakunthala
AU  - Muthugounder S
FAU - Presser, Naftali
AU  - Presser N
FAU - Selvan, Senthamil R
AU  - Selvan SR
FAU - Portoukalian, Jacques
AU  - Portoukalian J
FAU - Brosman, Stanley
AU  - Brosman S
FAU - Morton, Donald L
AU  - Morton DL
LA  - eng
GR  - CA107831-01/CA/NCI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, Non-P.H.S.
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Biochem Biophys Res Commun
JT  - Biochemical and biophysical research communications
JID - 0372516
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Gangliosides)
RN  - 0 (Receptors, Androgen)
SB  - IM
MH  - Animals
MH  - Antibodies, Monoclonal/metabolism
MH  - Cell Line, Tumor
MH  - Epithelial Cells/cytology/metabolism
MH  - Gangliosides/*chemistry/metabolism
MH  - Humans
MH  - Male
MH  - Mice
MH  - Middle Aged
MH  - Prostate/cytology/metabolism
MH  - Prostatic Neoplasms/*chemistry/metabolism/*pathology
MH  - *Receptors, Androgen
EDAT- 2004/10/07 09:00
MHDA- 2004/12/29 09:00
CRDT- 2004/10/07 09:00
PHST- 2004/08/16 00:00 [received]
PHST- 2004/10/07 09:00 [pubmed]
PHST- 2004/12/29 09:00 [medline]
PHST- 2004/10/07 09:00 [entrez]
AID - S0006-291X(04)02017-0 [pii]
AID - 10.1016/j.bbrc.2004.09.029 [doi]
PST - ppublish
SO  - Biochem Biophys Res Commun. 2004 Nov 5;324(1):154-65. doi:
      10.1016/j.bbrc.2004.09.029.

PMID- 9334809
OWN - NLM
STAT- MEDLINE
DCOM- 19971106
LR  - 20160303
IS  - 0020-7136 (Print)
IS  - 0020-7136 (Linking)
VI  - 73
IP  - 1
DP  - 1997 Sep 26
TI  - Selection of tumor antigens as targets for immune attack using
      immunohistochemistry: II. Blood group-related antigens.
PG  - 50-6
AB  - Blood group-related antigens have been attractive targets for immunotherapy of
      cancer since their initial identification as cancer-related antigens. However,
      available information on the relative expression of most of these antigens on
      human malignant and normal tissues has been insufficient for selecting optimal
      antigens and tumors for immune attack. In this study, the distribution of the
      blood group-related antigens TF, Tn, sTn, Le(a), sialyl Le(a), Le(b), Le(x),
      sialyl Le(x), polyfucosyl Le(x) and Le(y) on 13 types of cancer and 16 normal
      tissues was compared. Our results show that sTn is strongly expressed on cancers 
      of breast, colon, stomach, ovary, prostate and uterus; Tn on prostate cancer; TF 
      on cancers of breast, colon, ovary, prostate and uterus; Le(y) on the cancers of 
      colon, lung, pancreas and ovary; Le(a) and Le(x) on gastric cancer; and sialyl
      Le(a) and sialyl Le(x) on colon cancer. The complete absence of these antigens on
      cancers of neuroectodermal or mesodermal origin including melanoma, sarcoma,
      neuroblastoma and B cell lymphoma is as striking as their widespread presence on 
      tumors of epithelial origin. Normal tissues were also tested. Tn and Le(b) were
      only detected on gastric and ovarian epithelia; sTn on Leydig cells of testis in 
      addition to gastric and ovarian epithelia; Le(x) and sialyl Le(x) on
      polymorphonuclear leukocytes; and TF, Le(a), sialyl Le(a), Le(x), sialyl Le(x),
      polyfucosyl Le(x) and Le(y) on epithelia from a variety of tissues.
FAU - Zhang, S
AU  - Zhang S
AD  - Department of Medicine, Memorial Sloan-Kettering Cancer Center, New York, NY
      10021, USA.
FAU - Zhang, H S
AU  - Zhang HS
FAU - Cordon-Cardo, C
AU  - Cordon-Cardo C
FAU - Reuter, V E
AU  - Reuter VE
FAU - Singhal, A K
AU  - Singhal AK
FAU - Lloyd, K O
AU  - Lloyd KO
FAU - Livingston, P O
AU  - Livingston PO
LA  - eng
GR  - CA33049/CA/NCI NIH HHS/United States
GR  - CA61422/CA/NCI NIH HHS/United States
GR  - CA71506/CA/NCI NIH HHS/United States
GR  - etc.
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Int J Cancer
JT  - International journal of cancer
JID - 0042124
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens, Neoplasm)
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Lewis Blood-Group System)
RN  - 0 (Tn antigen)
RN  - 3554-90-3 (Thomsen-Friedenreich antigen)
SB  - IM
MH  - Animals
MH  - Antibodies, Monoclonal/immunology
MH  - Antigens, Neoplasm/*analysis
MH  - Antigens, Tumor-Associated, Carbohydrate/*analysis
MH  - Humans
MH  - Immunohistochemistry
MH  - Lewis Blood-Group System/*analysis
MH  - Mice
MH  - Neoplasms/*immunology
EDAT- 1997/10/23 22:31
MHDA- 2000/06/20 09:00
CRDT- 1997/10/23 22:31
PHST- 1997/10/23 22:31 [pubmed]
PHST- 2000/06/20 09:00 [medline]
PHST- 1997/10/23 22:31 [entrez]
AID - 10.1002/(SICI)1097-0215(19970926)73:1<50::AID-IJC9>3.0.CO;2-0 [pii]
PST - ppublish
SO  - Int J Cancer. 1997 Sep 26;73(1):50-6.

PMID- 10971113
OWN - NLM
STAT- MEDLINE
DCOM- 20001013
LR  - 20171101
IS  - 1018-2438 (Print)
IS  - 1018-2438 (Linking)
VI  - 122
IP  - 4
DP  - 2000 Aug
TI  - Occurrence of IgE antibody-recognizing N-linked glycan moiety of a soybean
      allergen, Gly m Bd 28K.
PG  - 238-45
AB  - BACKGROUND: It has been reported that N-linked glycan moieties of glycoproteins
      function as IgE-reactive determinants. Gly m Bd 28K, a soybean allergen, was a
      glycoprotein with glycan moieties, which are supposed to be the Man(3)GlcNAc(2)
      backbone with the beta1-->2 xylose and alpha1-->3 fucose branches. The purpose of
      the present study was to examine the IgE-binding ability of the glycan moiety of 
      Gly m Bd 28K in the binding reaction with patients' sera. METHODS: A peptide
      containing the glycan moiety was prepared from Gly m Bd 28K by digestion with
      lysyl endopeptidase. The binding site of the glycan moiety was determined by
      amino acid sequence analyses. The glycan moiety of the allergen was characterized
      using anti-horseradish peroxidase antibody (anti-HRP) recognizing the N-linked
      glycan moieties of glycoproteins. The binding of patients' IgE antibodies with
      their glycan moiety was examined by an immunostaining technique using the
      glycopeptide and its deglycosylated peptide derived from Gly m Bd 28K. RESULTS:
      The binding site of the glycan moiety in Gly m Bd 28K was shown to be its Asn20
      residue. Gly m Bd 28K did react with anti-HRP and the sera of soybean-sensitive
      patients, but the binding of IgE antibodies was inhibited by the preincubation
      with anti-HRP. Moreover, the glycopeptide also reacted with the sera of
      soybean-sensitive patients, but its deglycosylated peptide did not react with any
      IgE antibodies of patients' sera. CONCLUSIONS: The specific IgE antibodies
      recognizing the N-linked glycan moieties of Gly m Bd 28K and other glycoproteins 
      with homologous glycan moieties occur in the sera of soybean-sensitive patients. 
      It was indicated that the N-linked glycan moieties such as that of Gly m Bd 28K
      may be one of the common IgE-reactive determinants distributed in various plant
      food proteins.
CI  - Copyright 2000 S. Karger AG, Basel.
FAU - Hiemori, M
AU  - Hiemori M
AD  - Department of Nutrition, School of Medicine, The University of Tokushima,
      Tokushima, Japan.
FAU - Bando, N
AU  - Bando N
FAU - Ogawa, T
AU  - Ogawa T
FAU - Shimada, H
AU  - Shimada H
FAU - Tsuji, H
AU  - Tsuji H
FAU - Yamanishi, R
AU  - Yamanishi R
FAU - Terao, J
AU  - Terao J
LA  - eng
PT  - Journal Article
PL  - Switzerland
TA  - Int Arch Allergy Immunol
JT  - International archives of allergy and immunology
JID - 9211652
RN  - 0 (Allergens)
RN  - 0 (Antigens, Plant)
RN  - 0 (Epitopes)
RN  - 0 (Gly m Bd 28K allergen, Glycine max)
RN  - 0 (Glycopeptides)
RN  - 0 (Glycoproteins)
RN  - 0 (Peptides)
RN  - 0 (Plant Proteins)
RN  - 0 (Polysaccharides)
RN  - 0 (Soybean Proteins)
RN  - 37341-29-0 (Immunoglobulin E)
RN  - EC 1.11.1.- (Horseradish Peroxidase)
SB  - IM
MH  - Allergens/chemistry/*immunology
MH  - Amino Acid Sequence
MH  - Antigens, Plant
MH  - Carbohydrate Conformation
MH  - Carbohydrate Sequence
MH  - Epitopes
MH  - Food Hypersensitivity/etiology
MH  - Glycopeptides/immunology/isolation & purification/metabolism
MH  - Glycoproteins/chemistry/*immunology
MH  - Glycosylation
MH  - Horseradish Peroxidase/metabolism
MH  - Humans
MH  - Immunoglobulin E/blood/*immunology
MH  - Molecular Sequence Data
MH  - Peptides/immunology/isolation & purification/metabolism
MH  - Plant Proteins/adverse effects/chemistry/*immunology
MH  - Polysaccharides/chemistry/*immunology/metabolism
MH  - Soybean Proteins
MH  - Soybeans/*adverse effects/immunology
EDAT- 2000/09/06 11:00
MHDA- 2000/10/21 11:01
CRDT- 2000/09/06 11:00
PHST- 2000/09/06 11:00 [pubmed]
PHST- 2000/10/21 11:01 [medline]
PHST- 2000/09/06 11:00 [entrez]
AID - 24404 [pii]
AID - 10.1159/000024404 [doi]
PST - ppublish
SO  - Int Arch Allergy Immunol. 2000 Aug;122(4):238-45. doi: 10.1159/000024404.

PMID- 17100645
OWN - NLM
STAT- MEDLINE
DCOM- 20070620
LR  - 20081121
IS  - 0929-8665 (Print)
IS  - 0929-8665 (Linking)
VI  - 13
IP  - 9
DP  - 2006
TI  - A novel antiproliferative and antifungal lectin from Amaranthus viridis Linn
      seeds.
PG  - 897-905
AB  - A lectin from the seeds of Amaranthus viridis Linn has been purified by affinity 
      chromatography on asialofetuin-linked amino activated silica. Amaranthus viridis 
      lectin (AVL) has a native molecular mass of 67 kDa. It is a homodimer composed of
      two 36.6 kDa subunits. The lectin gave a single band in non-denaturing PAGE at pH
      4.5 and pH 8.3 and a single peak on HPLC size exclusion and cation exchange
      columns. The purified lectin was specific for both T-antigen and
      N-acetyl-D-lactosamine, markers for various carcinomas, in addition to
      N-acetyl-D-galactosamine, asialofetuin and fetuin. This lectin reacted strongly
      with red blood cells (RBCs) from human ABO blood groups and rat. It also reacted 
      with rabbit, sheep, goat and guinea pig RBCs. The lectin is a glycoprotein having
      no metal ion requirement for its activity. Denaturing agents such as urea,
      thiourea and guanidine-HCl had no effect on its activity when treated for 15
      minutes. AVL showed significant antiproliferative activity towards HB98 and
      P388D1 murine cancer cell lines. It also exerted antifungal activity against
      phytopathogenic fungi Botrytis cincerea and Fusarium oxysporum but not against
      Rhizoctonia solani, Trichoderma reesei, Alternaria solani and Fusarium
      graminearum.
FAU - Kaur, Navjot
AU  - Kaur N
AD  - Department of Molecular Biology and Biochemistry, Guru Nanak Dev University,
      Amritsar 143 005, India. nkaur@buffalo.edu
FAU - Dhuna, Vikram
AU  - Dhuna V
FAU - Kamboj, Sukhdev Singh
AU  - Kamboj SS
FAU - Agrewala, Javed N
AU  - Agrewala JN
FAU - Singh, Jatinder
AU  - Singh J
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - Netherlands
TA  - Protein Pept Lett
JT  - Protein and peptide letters
JID - 9441434
RN  - 0 (Antifungal Agents)
RN  - 0 (Carbohydrates)
RN  - 0 (Metals)
RN  - 0 (Plant Extracts)
RN  - 0 (Plant Lectins)
SB  - IM
MH  - Amaranthus/*chemistry
MH  - Animals
MH  - Antifungal Agents/chemistry/*pharmacology
MH  - Carbohydrates/chemistry
MH  - Cell Line, Tumor
MH  - Cell Proliferation/*drug effects
MH  - Erythrocytes/drug effects
MH  - Fungi/drug effects/metabolism
MH  - Hot Temperature
MH  - Humans
MH  - Metals/chemistry
MH  - Mice
MH  - Plant Extracts/chemistry/*pharmacology
MH  - Plant Lectins/chemistry/*pharmacology
MH  - Seeds/*chemistry
EDAT- 2006/11/15 09:00
MHDA- 2007/06/21 09:00
CRDT- 2006/11/15 09:00
PHST- 2006/11/15 09:00 [pubmed]
PHST- 2007/06/21 09:00 [medline]
PHST- 2006/11/15 09:00 [entrez]
PST - ppublish
SO  - Protein Pept Lett. 2006;13(9):897-905.

PMID- 21551457
OWN - NLM
STAT- MEDLINE
DCOM- 20120423
LR  - 20181211
IS  - 1460-2423 (Electronic)
IS  - 0959-6658 (Linking)
VI  - 21
IP  - 10
DP  - 2011 Oct
TI  - Occurrence of the human tumor-specific antigen structure Galbeta1-3GalNAcalpha-
      (Thomsen-Friedenreich) and related structures on gut bacteria: prevalence,
      immunochemical analysis and structural confirmation.
PG  - 1277-89
LID - 10.1093/glycob/cwr058 [doi]
AB  - The Thomsen-Friedenreich antigen (TF; CD176, Galbeta1-3GalNAcalpha-) is a
      tumor-specific carbohydrate antigen and a promising therapeutic target.
      Antibodies that react with this antigen are frequently found in the sera of
      healthy adults and are assumed to play a role in cancer immunosurveillance. In
      this study, we examined the occurrence of alpha-anomeric TF (TFalpha) on a large 
      variety of gastrointestinal bacteria using a novel panel of well-characterized
      monoclonal antibodies. Reactivity with at least one anti-TF antibody was found in
      13% (16 of 122) of strains analyzed. A more in-depth analysis, using monoclonal
      antibodies specific for alpha- and beta-anomeric TF in combination with periodate
      oxidation, revealed that only two novel Bacteroides ovatus strains (D-6 and F-1),
      isolated from the faeces of healthy persons by TF-immunoaffinity enrichment,
      possessed structures that are immunochemically identical to the true TFalpha
      antigen. The TF-positive capsular polysaccharide structure of strain D-6 was
      characterized by mass spectrometry, monosaccharide composition analysis,
      glycosidase treatments and immunoblot staining with TFalpha- and TFbeta-specific 
      antibodies. The active antigen was identified as Galbeta1-3GalNAc-, which was
      alpha-anomerically linked as a branching structure within a heptasaccharide
      repeating unit. We conclude that structures immunochemically identical to TFalpha
      are extremely rare on the surface of human intestinal bacteria and may only be
      identifiable by binding of both antibodies, NM-TF1 and NM-TF2, which recognize a 
      complete immunomolecular imprint of the TFalpha structure. The two novel B.
      ovatus strains isolated in this study may provide a basis for the development of 
      TF-based anti-tumor vaccines.
FAU - Henderson, Gemma
AU  - Henderson G
AD  - Department of Gastrointestinal Microbiology, German Institute of Human Nutrition,
      Potsdam-Rehbrucke, Arthur-Scheunert-Allee 114-116, D-14558 Nuthetal, Germany.
FAU - Ulsemer, Philippe
AU  - Ulsemer P
FAU - Schober, Ute
AU  - Schober U
FAU - Loffler, Anja
AU  - Loffler A
FAU - Alpert, Carl-Alfred
AU  - Alpert CA
FAU - Zimmermann-Kordmann, Martin
AU  - Zimmermann-Kordmann M
FAU - Reutter, Werner
AU  - Reutter W
FAU - Karsten, Uwe
AU  - Karsten U
FAU - Goletz, Steffen
AU  - Goletz S
FAU - Blaut, Michael
AU  - Blaut M
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20110507
PL  - England
TA  - Glycobiology
JT  - Glycobiology
JID - 9104124
RN  - 0 (Antibodies)
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 3554-90-3 (Thomsen-Friedenreich antigen)
RN  - 3HG052TF3I (Thomsen-Friedenreich antibodies)
SB  - IM
MH  - Antibodies/immunology
MH  - Antigens, Tumor-Associated, Carbohydrate/*chemistry/immunology
MH  - Bacteroidetes/immunology/isolation & purification
MH  - Feces/microbiology
MH  - Gastrointestinal Tract/*microbiology
MH  - Humans
EDAT- 2011/05/10 06:00
MHDA- 2012/04/24 06:00
CRDT- 2011/05/10 06:00
PHST- 2011/05/10 06:00 [entrez]
PHST- 2011/05/10 06:00 [pubmed]
PHST- 2012/04/24 06:00 [medline]
AID - cwr058 [pii]
AID - 10.1093/glycob/cwr058 [doi]
PST - ppublish
SO  - Glycobiology. 2011 Oct;21(10):1277-89. doi: 10.1093/glycob/cwr058. Epub 2011 May 
      7.

PMID- 2471655
OWN - NLM
STAT- MEDLINE
DCOM- 19890714
LR  - 20131121
IS  - 0012-1606 (Print)
IS  - 0012-1606 (Linking)
VI  - 133
IP  - 2
DP  - 1989 Jun
TI  - Transient expression of a chondroitin sulfate-related epitope during cartilage
      histomorphogenesis in the axial skeleton of fetal rats.
PG  - 475-88
AB  - A monoclonal antibody (MC21C), raised in mouse in response to a mixture of bone
      proteins, was found to exhibit a unique reactivity toward native chondroitin
      sulfate chains. Indirect immunofluorescence and immunoperoxidase assays were
      performed on tissue sections at different stages of fetal rat development, in
      order to investigate the distribution of the MC21C epitope during cartilage
      morphogenesis and differentiation. This extracellular marker was present in the
      sclerotome and its distribution subsequently followed the segmentation pattern of
      the precartilaginous vertebral column. In addition, changes in the
      MC21C-immunostaining pattern strongly correlated with the initial growth of the
      vertebrae. In the axial skeleton (spinal column, basis cranii), the
      immunostaining by MC21C was maximum in precartilaginous condensations and then
      rapidly disappeared during the process of chondrification. Also, the
      perinotochordal matrix was intensely immunostained.
FAU - Mark, M P
AU  - Mark MP
AD  - Institut de Biologie Medicale, CNRS LP 6520, Faculte de Medecine, Universite
      Louis Pasteur, Strasbourg, France.
FAU - Butler, W T
AU  - Butler WT
FAU - Ruch, J V
AU  - Ruch JV
LA  - eng
GR  - 5 RO1 AR39273-02/AR/NIAMS NIH HHS/United States
PT  - Comparative Study
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Dev Biol
JT  - Developmental biology
JID - 0372762
RN  - 0 (Epitopes)
RN  - 9007-27-6 (Chondroitin)
RN  - 9007-28-7 (Chondroitin Sulfates)
RN  - EC 4.2.2.- (Chondroitin Lyases)
RN  - P4448TJR7J (Alcian Blue)
SB  - IM
MH  - Alcian Blue
MH  - Animals
MH  - Cartilage/*embryology/metabolism
MH  - Cell Differentiation
MH  - Chondroitin/*analogs & derivatives
MH  - Chondroitin Lyases/metabolism
MH  - Chondroitin Sulfates/*genetics/immunology
MH  - Epitopes/*genetics
MH  - Fluorescent Antibody Technique
MH  - *Gene Expression Regulation
MH  - Gestational Age
MH  - Histocytochemistry
MH  - Immunodiffusion
MH  - Immunoenzyme Techniques
MH  - Mice
MH  - Mice, Inbred BALB C
MH  - Morphogenesis
MH  - Rats
MH  - Rats, Inbred Strains
MH  - Staining and Labeling
EDAT- 1989/06/01 00:00
MHDA- 1989/06/01 00:01
CRDT- 1989/06/01 00:00
PHST- 1989/06/01 00:00 [pubmed]
PHST- 1989/06/01 00:01 [medline]
PHST- 1989/06/01 00:00 [entrez]
AID - 0012-1606(89)90051-1 [pii]
PST - ppublish
SO  - Dev Biol. 1989 Jun;133(2):475-88.

PMID- 8232334
OWN - NLM
STAT- MEDLINE
DCOM- 19931215
LR  - 20061115
IS  - 0161-5890 (Print)
IS  - 0161-5890 (Linking)
VI  - 30
IP  - 16
DP  - 1993 Nov
TI  - Immunoglobulin variable region sequences of two human monoclonal antibodies
      directed to an onco-developmental carbohydrate antigen, lactotetraosylceramide
      (LcOse4Cer).
PG  - 1481-9
AB  - A human monoclonal antibody, 11-50, was generated and was shown to recognize an
      onco-developmental carbohydrate antigen, LcOse4Cer. The isotype of this antibody 
      was IgM, lambda, similar to the previously known human anti-LcOse4 antibodies,
      such as IgMWOO and HMST-1. We raised a murine anti-idiotypic antibody G3 (IgG1,
      kappa) against 11-50, and tested its reactivity towards the affinity purified
      human polyclonal anti-LcOse4 antibodies prepared from pooled human sera using a
      Gal beta 1-->3GlcNAc beta-immobilized column. The results indicated that at least
      a part of the human polyclonal anti-LcOse4 antibodies shared the G3 idiotype with
      11-50. We further analyzed the sequence of variable regions of the two
      anti-LcOse4 antibodies, 11-50 and HMST-1. Sequence analysis of the heavy chain
      variable regions indicated that the VH regions of these two antibodies were
      highly homologous to each other (93.5% at the nucleic acid level), and these
      antibodies utilized the germline genes VH1.9III and hv3005f3 as the VH segments, 
      which are closely related germline genes of the VHIII family. It was noted that
      these germline VH genes are frequently utilized in fetal B cells. The JH region
      of both antibodies was encoded by the JH4 gene. For the light chain, the V lambda
      segments of the two antibodies were 96.3% homologous to each other at the nucleic
      acid level. The V lambda segments of both antibodies showed the highest homology 
      to the rearranged V lambda gene called V lambda II.DS among reported V lambda
      genes, while the exact germline V lambda genes encoding the two antibodies were
      not yet registered in available sequence databanks. The amino acid sequences of
      the J lambda segments of both antibodies were identical. These results indicate
      that the two human antibodies recognizing the onco-developmental carbohydrate
      antigen Lc4 are encoded by the same or very homologous germline genes.
FAU - Yago, K
AU  - Yago K
AD  - Laboratory of Experimental Pathology, Aichi Cancer Center, Japan.
FAU - Zenita, K
AU  - Zenita K
FAU - Ohwaki, I
AU  - Ohwaki I
FAU - Harada, R
AU  - Harada R
FAU - Nozawa, S
AU  - Nozawa S
FAU - Tsukazaki, K
AU  - Tsukazaki K
FAU - Iwamori, M
AU  - Iwamori M
FAU - Endo, N
AU  - Endo N
FAU - Yasuda, N
AU  - Yasuda N
FAU - Okuma, M
AU  - Okuma M
AU  - et al.
LA  - eng
SI  - GENBANK/X72744
SI  - GENBANK/X72745
SI  - GENBANK/X72746
SI  - GENBANK/X72747
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - Mol Immunol
JT  - Molecular immunology
JID - 7905289
RN  - 0 (Antibodies, Anti-Idiotypic)
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens, Neoplasm)
RN  - 0 (Immunoglobulin Heavy Chains)
RN  - 0 (Immunoglobulin Variable Region)
SB  - IM
MH  - Amino Acid Sequence
MH  - Antibodies, Anti-Idiotypic/genetics
MH  - Antibodies, Monoclonal/*genetics
MH  - Antibody Specificity
MH  - Antigens, Neoplasm/genetics/*immunology
MH  - Base Sequence
MH  - Carbohydrate Sequence
MH  - Genes, Immunoglobulin
MH  - Humans
MH  - Immunoglobulin Heavy Chains/*genetics
MH  - Immunoglobulin Variable Region/*genetics
MH  - Molecular Sequence Data
EDAT- 1993/11/01 00:00
MHDA- 1993/11/01 00:01
CRDT- 1993/11/01 00:00
PHST- 1993/11/01 00:00 [pubmed]
PHST- 1993/11/01 00:01 [medline]
PHST- 1993/11/01 00:00 [entrez]
PST - ppublish
SO  - Mol Immunol. 1993 Nov;30(16):1481-9.

PMID- 7887817
OWN - NLM
STAT- MEDLINE
DCOM- 19950413
LR  - 20041117
IS  - 1031-170X (Print)
IS  - 1031-170X (Linking)
VI  - 7
IP  - 4
DP  - 1994 Dec
TI  - Becoming an independent homebirth midwife.
PG  - 27-9
FAU - Smith, S
AU  - Smith S
LA  - eng
PT  - Journal Article
PL  - Australia
TA  - Aust Coll Midwives Inc J
JT  - Australian College of Midwives Incorporated journal
JID - 8903009
SB  - N
MH  - Female
MH  - *Home Childbirth
MH  - Humans
MH  - *Midwifery
MH  - Pregnancy
MH  - *Private Practice
MH  - Tasmania
EDAT- 1994/12/01 00:00
MHDA- 1994/12/01 00:01
CRDT- 1994/12/01 00:00
PHST- 1994/12/01 00:00 [pubmed]
PHST- 1994/12/01 00:01 [medline]
PHST- 1994/12/01 00:00 [entrez]
PST - ppublish
SO  - Aust Coll Midwives Inc J. 1994 Dec;7(4):27-9.

PMID- 2432062
OWN - NLM
STAT- MEDLINE
DCOM- 19870218
LR  - 20171116
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 262
IP  - 1
DP  - 1987 Jan 5
TI  - Y and blood group B type 2 glycolipid antigens accumulate in a human gastric
      carcinoma cell line as detected by monoclonal antibody. Isolation and
      characterization by mass spectrometry and NMR spectroscopy.
PG  - 372-9
AB  - A monoclonal antibody (mAb), BR55-2, was generated from mice immunized with MCF-7
      human breast carcinoma cells. This mAb specifically detected glycolipids with the
      Y determinant Fuc alpha 1----2Gal beta 1----4GlcNAc(3----1 alpha Fuc)-beta
      1----3Gal beta 1----4Glc beta 1----1 Cer and the Y-related B-active difucosylated
      determinant Gal alpha 1----3Gal(2----1 alpha Fuc) beta 1----4GlcNAc(3----1 alpha 
      Fuc) beta 1----3Gal beta 1----4Glc beta 1----1 Cer, but was not reactive with
      related monofucosylated glycolipids of type 2 chain (X-antigen, blood group H),
      type 1 chain (Lea antigen, blood group H and B) or with difucosylated type 2 and 
      type 1 chain structures (A blood group antigen or blood group B and Leb,
      respectively). A series of glycolipids with Y and blood group B type 2
      determinants were detected in human gastric adenocarcinoma cell line KATO III
      with mAb BR55-2 and with a previously characterized anti-blood group B mAb
      PA83-52 (Hansson, G. C., Karlsson, K.-A., Larson, G., McKibbin, J. M., Blaszczyk,
      M., Herlyn, M., Steplewski, Z., and Koprowski, H. (1983) J. Biol. Chem. 258,
      4091-4097). The isolated antigens were structurally characterized by mass
      spectrometry of permethylated and permethylated-reduced derivatives and by proton
      NMR spectroscopy. In a chromatogram binding assay, mAb BR55-2 and mAb PA83-52
      detected minor components with slower mobility than the Y-6 and blood group
      B-7-type 2 structures. The detection of a B type 2 determinant is the first
      chemical evidence for the presence of an autologous difucosyl blood group B type 
      2 antigen in human adenocarcinoma cells.
FAU - Blaszczyk-Thurin, M
AU  - Blaszczyk-Thurin M
FAU - Thurin, J
AU  - Thurin J
FAU - Hindsgaul, O
AU  - Hindsgaul O
FAU - Karlsson, K A
AU  - Karlsson KA
FAU - Steplewski, Z
AU  - Steplewski Z
FAU - Koprowski, H
AU  - Koprowski H
LA  - eng
GR  - CA10815/CA/NCI NIH HHS/United States
GR  - CA21124/CA/NCI NIH HHS/United States
GR  - CA25874/CA/NCI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (ABO Blood-Group System)
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens, Neoplasm)
RN  - 0 (Epitopes)
RN  - 0 (Glycolipids)
RN  - 28RYY2IV3F (Fucose)
SB  - IM
MH  - ABO Blood-Group System/*immunology
MH  - Adenocarcinoma/*immunology
MH  - Animals
MH  - Antibodies, Monoclonal/immunology
MH  - Antibody Specificity
MH  - Antigens, Neoplasm/immunology/*isolation & purification
MH  - Cell Line
MH  - Chemical Phenomena
MH  - Chemistry
MH  - Epitopes/immunology
MH  - Fucose
MH  - Glycolipids/*immunology
MH  - Humans
MH  - Magnetic Resonance Spectroscopy
MH  - Mass Spectrometry
MH  - Mice
MH  - Stomach Neoplasms/*immunology
EDAT- 1987/01/05 00:00
MHDA- 1987/01/05 00:01
CRDT- 1987/01/05 00:00
PHST- 1987/01/05 00:00 [pubmed]
PHST- 1987/01/05 00:01 [medline]
PHST- 1987/01/05 00:00 [entrez]
PST - ppublish
SO  - J Biol Chem. 1987 Jan 5;262(1):372-9.

PMID- 6194834
OWN - NLM
STAT- MEDLINE
DCOM- 19831217
LR  - 20160422
IS  - 0006-4971 (Print)
IS  - 0006-4971 (Linking)
VI  - 62
IP  - 5
DP  - 1983 Nov
TI  - A granulocyte reactive monoclonal antibody, 1G10, identifies the Gal beta 1-4
      (Fuc alpha 1-3)GlcNAc (X determinant) expressed in HL-60 cells on both glycolipid
      and glycoprotein molecules.
PG  - 1022-6
AB  - 1G10, a monoclonal IgM antibody that identifies a differentiation antigen on
      human granulocytes and a subpopulation of monocytes, was found to react
      specifically with glycosphingolipids bearing the Gal beta 1-4(Fuc alpha
      1-3)GlcNAc hapten (X determinant). This carbohydrate determinant was found on
      both glycolipid and glycoprotein molecules isolated from HL-60 cells (a
      promyelocytic leukemia cell line). Thus, this highly conserved
      carbohydrate-defined determinant previously described on mouse embryonic and
      mouse and human carcinoma cells is also expressed as a tissue-specific
      differentiation antigen on normal human granulocytes.
FAU - Urdal, D L
AU  - Urdal DL
FAU - Brentnall, T A
AU  - Brentnall TA
FAU - Bernstein, I D
AU  - Bernstein ID
FAU - Hakomori, S I
AU  - Hakomori SI
LA  - eng
GR  - CA 09351/CA/NCI NIH HHS/United States
GR  - CA 18029/CA/NCI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Blood
JT  - Blood
JID - 7603509
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Epitopes)
RN  - 0 (Glycolipids)
RN  - 0 (Glycoproteins)
RN  - 0 (Haptens)
SB  - AIM
SB  - IM
MH  - Antibodies, Monoclonal/*immunology
MH  - Chromatography, Thin Layer
MH  - Epitopes
MH  - Glycolipids/*immunology
MH  - Glycoproteins/*immunology
MH  - Granulocytes/*immunology
MH  - Haptens/immunology
MH  - Humans
MH  - Leukemia, Myeloid/blood
EDAT- 1983/11/01 00:00
MHDA- 1983/11/01 00:01
CRDT- 1983/11/01 00:00
PHST- 1983/11/01 00:00 [pubmed]
PHST- 1983/11/01 00:01 [medline]
PHST- 1983/11/01 00:00 [entrez]
PST - ppublish
SO  - Blood. 1983 Nov;62(5):1022-6.

PMID- 2435716
OWN - NLM
STAT- MEDLINE
DCOM- 19870515
LR  - 20081121
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 262
IP  - 10
DP  - 1987 Apr 5
TI  - Monoclonal antibody Leo Mel 3, which inhibits killing of human melanoma cells by 
      anomalous killer cells, binds to a sugar sequence in GD2 (II3(NeuAc)2-GgOse3Cer) 
      and several other gangliosides.
PG  - 4800-3
AB  - Human anomalous killer (AK) cells lyse freshly isolated human melanoma cells
      which are insensitive to human natural killer cell-mediated lysis. Monoclonal
      antibody Leo Mel 3, an IgM (k), produced by a hybridoma obtained from a mouse
      immunized with human melanoma cells, binds to melanoma cells and inhibits their
      conjugate formation with AK cells as well as their AK cell-mediated lysis. Other 
      IgM antibodies from the same fusion that bind melanoma cells do not inhibit
      (Werkmeister, J. A., Triglia, T., Andrews, P., and Burns, G. F. (1985) J.
      Immunol. 135, 689-695). Leo Mel 3 binds several different gangliosides from
      melanoma cells, as determined by immunostaining thin layer chromatograms. Binding
      is abolished by treatment of the gangliosides with neuraminidase. In solid-phase 
      radioimmunoassay, Leo Mel 3 binds strongly to ganglioside GD2 and less strongly
      to gangliosides GT3, GD3, and GQ1b. It does not bind to other gangliosides
      including GM1, GM2, GM3, GD1a, GD1b, and GT1b. Thus, the epitope recognized by
      antibody Leo Mel 3 is found in the sugar sequence of ganglioside GD2, GalNAc beta
      1-4[NeuAc alpha 2-8NeuAc alpha 2-3]Gal beta 1-4Glc beta 1 .... This sequence may 
      contain a target in melanoma cells recognized by AK cells.
FAU - Fukuta, S
AU  - Fukuta S
FAU - Werkmeister, J A
AU  - Werkmeister JA
FAU - Burns, G F
AU  - Burns GF
FAU - Ginsburg, V
AU  - Ginsburg V
FAU - Magnani, J L
AU  - Magnani JL
LA  - eng
PT  - Journal Article
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Epitopes)
RN  - 0 (Gangliosides)
RN  - 65988-71-8 (ganglioside, GD2)
SB  - IM
MH  - Antibodies, Monoclonal/*immunology
MH  - Binding Sites
MH  - Carbohydrate Sequence
MH  - Epitopes/immunology
MH  - Gangliosides/*immunology
MH  - Humans
MH  - Killer Cells, Natural/*immunology
MH  - Melanoma/*immunology
EDAT- 1987/04/05 00:00
MHDA- 1987/04/05 00:01
CRDT- 1987/04/05 00:00
PHST- 1987/04/05 00:00 [pubmed]
PHST- 1987/04/05 00:01 [medline]
PHST- 1987/04/05 00:00 [entrez]
PST - ppublish
SO  - J Biol Chem. 1987 Apr 5;262(10):4800-3.

PMID- 6870892
OWN - NLM
STAT- MEDLINE
DCOM- 19830811
LR  - 20170913
IS  - 0006-291X (Print)
IS  - 0006-291X (Linking)
VI  - 113
IP  - 3
DP  - 1983 Jun 29
TI  - Human cancer-associated gangliosides defined by a monoclonal antibody (IB9)
      directed to sialosyl alpha 2 leads to 6 galactosyl residue: a preliminary note.
PG  - 791-8
AB  - A new monoclonal antibody (IB9) was prepared by hybridoma technique directed
      specifically to sialosyl alpha 2 leads to 6 galactosyl residue. With this
      reagent, accumulation of two major gangliosides in human colonic and liver
      adenocarcinoma has been detected, and these gangliosides were isolated and
      characterized as structures A and B (below). Another ganglioside with a ceramide 
      nonasaccharide structure, which reacted to anti-X-hapten antibody after
      desialylation, was also isolated and partially characterized. (formula; see text)
      These gangliosides were absent or present in very small quantity in normal tissue
      and may represent human cancer-associated markers.
FAU - Hakomori, S
AU  - Hakomori S
FAU - Nudelman, E
AU  - Nudelman E
FAU - Levery, S B
AU  - Levery SB
FAU - Patterson, C M
AU  - Patterson CM
LA  - eng
GR  - CA19224/CA/NCI NIH HHS/United States
GR  - CA20026/CA/NCI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Biochem Biophys Res Commun
JT  - Biochemical and biophysical research communications
JID - 0372516
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Gangliosides)
SB  - IM
MH  - Adenocarcinoma/*metabolism
MH  - Antibodies, Monoclonal/*isolation & purification
MH  - Antibody Specificity
MH  - Chemical Phenomena
MH  - Chemistry
MH  - Colonic Neoplasms/*metabolism
MH  - Gangliosides/immunology/*metabolism
MH  - Humans
MH  - Immunochemistry
MH  - Liver Neoplasms/*metabolism
EDAT- 1983/06/29 00:00
MHDA- 1983/06/29 00:01
CRDT- 1983/06/29 00:00
PHST- 1983/06/29 00:00 [pubmed]
PHST- 1983/06/29 00:01 [medline]
PHST- 1983/06/29 00:00 [entrez]
AID - 0006-291X(83)91069-0 [pii]
PST - ppublish
SO  - Biochem Biophys Res Commun. 1983 Jun 29;113(3):791-8.

PMID- 16618943
OWN - NLM
STAT- MEDLINE
DCOM- 20060518
LR  - 20181201
IS  - 0022-1554 (Print)
IS  - 0022-1554 (Linking)
VI  - 54
IP  - 5
DP  - 2006 May
TI  - Terminal alpha1,4-linked N-acetylglucosamine in Helicobacter pylori-associated
      intestinal metaplasia of the human stomach and gastric carcinoma cell lines.
PG  - 585-91
AB  - Helicobacter pylori (Hp) infection is associated with the development of gastric 
      lesions including gastritis, intestinal metaplasia (IM), and gastric carcinoma.
      In humans, Hp is found almost exclusively in the foveolar epithelium of the
      gastric mucosa and rarely colonizes the deeper portions where mucous cells of the
      glands produce mucins with terminal alpha1,4-GlcNAc O-glycans. This structure
      exerts antimicrobial activity against Hp. The development of IM in the stomach is
      characterized by Hp clearance from the metaplastic glands and by major
      alterations in the expression of mucins and mucin-carbohydrates. The present work
      evaluated whether terminal alpha1,4-GlcNAc and sialyl-Tn antigen are implicated
      in the process of Hp clearance from metaplastic glands by analyzing the
      expression of these antigens in different types of IM-complete (n=12) and
      incomplete (n=8)-and in gastric cell lines. Terminal alpha1,4-GlcNAc was not
      detected in IM except in a single foci of one case, indicating that this
      structure is not implicated in the clearance of Hp from IM, in contrast to what
      is observed in normal gastric mucosa. None of the gastric carcinoma cell lines
      studied showed terminal alpha1,4-GlcNAc, suggesting that they do not display a
      gastric gland mucous cell phenotype and therefore are useful models for in vitro 
      Hp studies. Finally, sialyl-Tn antigen colocalizes with MUC2 mucin and is present
      in all cases of complete and incomplete IM, suggesting that either or both can be
      implicated in Hp clearance from IM.
FAU - Ferreira, Bibiana
AU  - Ferreira B
AD  - Institute of Molecular Pathology and Immunology, University of Porto, Portugal.
FAU - Marcos, Nuno T
AU  - Marcos NT
FAU - David, Leonor
AU  - David L
FAU - Nakayama, Jun
AU  - Nakayama J
FAU - Reis, Celso A
AU  - Reis CA
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20060123
PL  - United States
TA  - J Histochem Cytochem
JT  - The journal of histochemistry and cytochemistry : official journal of the
      Histochemistry Society
JID - 9815334
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (MUC2 protein, human)
RN  - 0 (Mucin-2)
RN  - 0 (Mucins)
RN  - 0 (sialosyl-Tn antigen)
RN  - V956696549 (Acetylglucosamine)
SB  - IM
MH  - Acetylglucosamine/*biosynthesis
MH  - Antigens, Tumor-Associated, Carbohydrate/biosynthesis
MH  - Cell Line, Tumor
MH  - Gastric Mucosa/*metabolism/pathology
MH  - *Helicobacter pylori
MH  - Humans
MH  - Immunohistochemistry
MH  - Metaplasia
MH  - Mucin-2
MH  - Mucins/biosynthesis
MH  - Stomach/microbiology/pathology
MH  - Stomach Neoplasms/*metabolism/pathology
EDAT- 2006/04/19 09:00
MHDA- 2006/05/19 09:00
CRDT- 2006/04/19 09:00
PHST- 2006/04/19 09:00 [pubmed]
PHST- 2006/05/19 09:00 [medline]
PHST- 2006/04/19 09:00 [entrez]
AID - jhc.5A6836.2006 [pii]
AID - 10.1369/jhc.5A6836.2006 [doi]
PST - ppublish
SO  - J Histochem Cytochem. 2006 May;54(5):585-91. doi: 10.1369/jhc.5A6836.2006. Epub
      2006 Jan 23.

PMID- 18279843
OWN - NLM
STAT- MEDLINE
DCOM- 20081006
LR  - 20171116
IS  - 0008-6215 (Print)
IS  - 0008-6215 (Linking)
VI  - 343
IP  - 12
DP  - 2008 Aug 11
TI  - Relevance of fucosylation and Lewis antigen expression in the bacterial
      gastroduodenal pathogen Helicobacter pylori.
PG  - 1952-65
LID - 10.1016/j.carres.2007.12.012 [doi]
AB  - Helicobacter pylori is a prevalent bacterial, gastroduodenal pathogen of humans
      that can express Lewis (Le) and related antigens in the O-chains of its surface
      lipopolysaccharide. The O-chains of H. pylori are commonly composed of internal
      Le(x) units with terminal Le(x) or Le(y) units or, in some strains, with
      additional units of Le(a), Le(b), Le(c), sialyl-Le(x) and H-1 antigens, as well
      as blood groups A and B, thereby producing a mosaicism of antigenic units
      expressed. The genetic determination of the Le antigen biosynthetic pathways in
      H. pylori has been studied, and despite striking functional similarity, low
      sequence homology occurs between the bacterial and mammalian alpha(1,3/4)- and
      alpha(1,2)-fucosyltransferases. Factors affecting Le antigen expression in H.
      pylori, that can influence the biological impact of this molecular mimicry,
      include regulation of fucosyltransferase genes through slipped-strand mispairing,
      the activity and expression levels of the functional enzymes, the preferences of 
      the expressed enzyme for distinctive acceptor molecules and the availability of
      activated sugar intermediates. Le mimicry was initially implicated in immune
      evasion and gastric adaptation by the bacterium, but more recent studies show a
      role in gastric colonization and bacterial adhesion with galectin-3 identified as
      the gastric receptor for polymeric Le(x) on the bacterium. From the host defence 
      aspect, innate immune recognition of H. pylori by surfactant protein D is
      influenced by the extent of LPS fucosylation. Furthermore, Le antigen expression 
      affects both the inflammatory response and T-cell polarization that develops
      after infection. Although controversial, evidence suggests that long-term H.
      pylori infection can induce autoreactive anti-Le antibodies cross-reacting with
      the gastric mucosa, in part leading to the development of gastric atrophy. Thus, 
      Le antigen expression and fucosylation in H. pylori have multiple biological
      effects on pathogenesis and disease outcome.
FAU - Moran, Anthony P
AU  - Moran AP
AD  - Department of Microbiology, School of Natural Sciences, National University of
      Ireland, Galway, Ireland. anthony.moran@nuigalway.ie
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Review
DEP - 20071225
PL  - Netherlands
TA  - Carbohydr Res
JT  - Carbohydrate research
JID - 0043535
RN  - 0 (Lewis Blood-Group System)
RN  - 0 (Lewis X Antigen)
RN  - 0 (Lewis Y antigen)
RN  - EC 2.4.1.- (Fucosyltransferases)
SB  - IM
MH  - Animals
MH  - Carbohydrate Sequence
MH  - Fucosyltransferases/*metabolism
MH  - Helicobacter Infections/etiology
MH  - Helicobacter pylori/chemistry/*metabolism/pathogenicity
MH  - Humans
MH  - Lewis Blood-Group System/*biosynthesis
MH  - Lewis X Antigen/*biosynthesis
MH  - Molecular Sequence Data
MH  - Stomach/microbiology
RF  - 137
EDAT- 2008/02/19 09:00
MHDA- 2008/10/07 09:00
CRDT- 2008/02/19 09:00
PHST- 2007/10/12 00:00 [received]
PHST- 2007/11/23 00:00 [revised]
PHST- 2007/12/17 00:00 [accepted]
PHST- 2008/02/19 09:00 [pubmed]
PHST- 2008/10/07 09:00 [medline]
PHST- 2008/02/19 09:00 [entrez]
AID - S0008-6215(07)00547-2 [pii]
AID - 10.1016/j.carres.2007.12.012 [doi]
PST - ppublish
SO  - Carbohydr Res. 2008 Aug 11;343(12):1952-65. doi: 10.1016/j.carres.2007.12.012.
      Epub 2007 Dec 25.

PMID- 12213787
OWN - NLM
STAT- MEDLINE
DCOM- 20030304
LR  - 20190513
IS  - 0959-6658 (Print)
IS  - 0959-6658 (Linking)
VI  - 12
IP  - 9
DP  - 2002 Sep
TI  - Tumor-related expression of alpha1,2fucosylated antigens on colorectal carcinoma 
      cells and its suppression by cell-mediated priming using sugar acceptors for
      alpha1,2fucosyltransferase.
PG  - 545-53
AB  - The accumulation of alpha1,2fucosylated antigens, such as Y
      (Fucalpha1,2Galbeta1,4 [Fucalpha1,3]GlcNAcbeta), Le(b)
      (Fucalpha1,2Galbeta1,3-[Fucalpha1,4]GlcNAcbeta), and H type 2 (Fucalpha1,2
      Galbeta1,4GlcNAcbeta) occurs specifically within human colorectal tumor tissues
      and can be detected by an antifucosylated antigen antibody, such as the YB-2
      antibody. In the present investigation, we found that the expression of these
      antigens bearing an alpha1,2-linked fucose correlated with the resistance of the 
      tumor cells to anticancer treatments. Addition of an exogenous sugar acceptor for
      alpha1,2fucosyltransferase to the cell medium resulted in suppression of
      alpha1,2fucosylated antigen expression on the tumor cells and increased
      susceptibility to anticancer treatment. The increased susceptibility may be
      attributed to cancer cell-mediated priming by sugar acceptors for
      alpha1,2fucosyltransferase added to the medium.
FAU - Yazawa, Shin
AU  - Yazawa S
AD  - Japan Immunoresearch Laboratories, 351-1 Nishiyokote-cho, Takasaki 370-0021,
      Japan. syazawa@po.sphere.ne.jp
FAU - Nishimura, Toyo
AU  - Nishimura T
FAU - Ide, Munenori
AU  - Ide M
FAU - Asao, Takayuki
AU  - Asao T
FAU - Okamura, Akihiko
AU  - Okamura A
FAU - Tanaka, Susumu
AU  - Tanaka S
FAU - Takai, Izumi
AU  - Takai I
FAU - Yagihashi, Yuko
AU  - Yagihashi Y
FAU - Saniabadi, Abby R
AU  - Saniabadi AR
FAU - Kochibe, Naohisa
AU  - Kochibe N
LA  - eng
PT  - Journal Article
PL  - England
TA  - Glycobiology
JT  - Glycobiology
JID - 9104124
RN  - 0 (Antigens, Neoplasm)
RN  - 0 (Antineoplastic Agents)
RN  - 28RYY2IV3F (Fucose)
RN  - EC 2.4.1.- (Fucosyltransferases)
SB  - IM
MH  - Antigens, Neoplasm/*immunology
MH  - Antineoplastic Agents/therapeutic use
MH  - *Carbohydrate Metabolism
MH  - Cell Division
MH  - Colorectal Neoplasms/drug therapy/*immunology/pathology
MH  - Fucose/*metabolism
MH  - Fucosyltransferases/*metabolism
MH  - Humans
MH  - Tumor Cells, Cultured
EDAT- 2002/09/06 10:00
MHDA- 2003/03/05 04:00
CRDT- 2002/09/06 10:00
PHST- 2002/09/06 10:00 [pubmed]
PHST- 2003/03/05 04:00 [medline]
PHST- 2002/09/06 10:00 [entrez]
AID - 10.1093/glycob/cwf070 [doi]
PST - ppublish
SO  - Glycobiology. 2002 Sep;12(9):545-53. doi: 10.1093/glycob/cwf070.

PMID- 9185702
OWN - NLM
STAT- MEDLINE
DCOM- 19970708
LR  - 20160303
IS  - 0020-7136 (Print)
IS  - 0020-7136 (Linking)
VI  - 71
IP  - 6
DP  - 1997 Jun 11
TI  - Influence of spatial configuration on the expression of carcinoembryonic antigen 
      and mucin antigens in human bladder cancer.
PG  - 986-92
AB  - CEA and cellular mucin antigens have been recognized as potential targets for
      specific immunotherapy and are frequently expressed in bladder cancer. We studied
      the coordinated expression of a bladder cancer-associated CEA glycoform and of
      the mucins MUC1, MUC2 and MAUB under various growth conditions in the MGH-U3
      bladder-cancer cell line. CEA and MUC2 mRNAs and proteins were detected in nude
      mouse tumors and spheroids but not in monolayer cultures. Expression of MAUB and 
      bladder-cancer CEA also was induced according to spatial configuration of cells. 
      MUC1 was always expressed under various growth conditions, but its glycosylation 
      was modulated: in spheroids and mostly in tumor cells, the SM3 protein epitope
      was unmasked and sialyl-Tn was induced. The kinetics of modulation of MAUB and
      bladder-cancer CEA were different. The epitope recognized by the monoclonal
      antibody (MAb) 19A211 was rapidly induced in the aggregation phase of spheroid
      formation and rapidly lost upon plating of tumor cells, suggesting a relationship
      with cell contact. By contrast, MAUB induction in spheroids was delayed to the
      compaction phase, when cell aggregates become resistant to disruption, and loss
      of expression upon tumor plating occurred slowly over several culture passages.
      No induction of these 2 antigens was observed in the presence of differentiation 
      agents, endothelial cell products or interferon-gamma, but it occurred when
      MGH-U3 cells were cultured at high density on extracellular matrix. Our results
      suggest that CEA and mucin antigen expression in bladder cancer is modulated by
      the spatial configuration of cells.
FAU - LaRue, H
AU  - LaRue H
AD  - Laboratoire d'Uro-Oncologie Experimentale, Centre de recherche de l'Hotel-Dieu de
      Quebec, Canada.
FAU - Parent-Vaugeois, C
AU  - Parent-Vaugeois C
FAU - Bergeron, A
AU  - Bergeron A
FAU - Champetier, S
AU  - Champetier S
FAU - Fradet, Y
AU  - Fradet Y
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Int J Cancer
JT  - International journal of cancer
JID - 0042124
RN  - 0 (Carcinoembryonic Antigen)
RN  - 0 (Mucins)
RN  - 0 (RNA, Messenger)
SB  - IM
MH  - Animals
MH  - Carcinoembryonic Antigen/*genetics
MH  - Humans
MH  - Kinetics
MH  - Mice
MH  - Mice, Nude
MH  - Mucins/*genetics
MH  - RNA, Messenger/genetics
MH  - Tumor Cells, Cultured
MH  - Urinary Bladder Neoplasms/*immunology
EDAT- 1997/06/11 00:00
MHDA- 2000/06/20 09:00
CRDT- 1997/06/11 00:00
PHST- 1997/06/11 00:00 [pubmed]
PHST- 2000/06/20 09:00 [medline]
PHST- 1997/06/11 00:00 [entrez]
AID - 10.1002/(SICI)1097-0215(19970611)71:6<986::AID-IJC14>3.0.CO;2-4 [pii]
PST - ppublish
SO  - Int J Cancer. 1997 Jun 11;71(6):986-92.

PMID- 11003551
OWN - NLM
STAT- MEDLINE
DCOM- 20001031
LR  - 20181113
IS  - 0282-0080 (Print)
IS  - 0282-0080 (Linking)
VI  - 16
IP  - 11
DP  - 1999 Nov
TI  - A rat experimental model for the design of vaccines against tumor associated
      antigens Tn and Sialyl-Tn.
PG  - 681-4
AB  - Clones either strongly or barely expressing the Tn and Sialyl-Tn antigens were
      isolated from a rat colon carcinoma cell line. Expression of the antigens in
      normal rat tissues was very restricted and vaccination using Ovine Submaxillary
      Mucin as the immunogen could delay growth of the Sialyl-Tn positive cells, but
      not of the Sialyl-Tn negative cells in syngeneic rats. The model should be useful
      for testing new anti-Tn or Sialyl-Tn vaccination protocols.
FAU - Hallouin, F
AU  - Hallouin F
AD  - INSERM U419, Institut de Biologie, Nantes, France.
FAU - Goupille, C
AU  - Goupille C
FAU - Rocher, J
AU  - Rocher J
FAU - Le Pendu, J
AU  - Le Pendu J
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Glycoconj J
JT  - Glycoconjugate journal
JID - 8603310
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Mucins)
RN  - 0 (Tn antigen)
RN  - 0 (sialosyl-Tn antigen)
SB  - IM
MH  - Animals
MH  - Antigens, Tumor-Associated, Carbohydrate/*biosynthesis/immunology
MH  - Cloning, Organism
MH  - Enzyme-Linked Immunosorbent Assay
MH  - Female
MH  - Mice
MH  - Models, Biological
MH  - Mucins/immunology
MH  - Neoplasm Transplantation
MH  - Rats
MH  - Rats, Inbred Strains
MH  - Submandibular Gland/metabolism
MH  - Tissue Distribution
MH  - Tumor Cells, Cultured
MH  - Vaccination
EDAT- 2000/09/26 11:00
MHDA- 2001/02/28 10:01
CRDT- 2000/09/26 11:00
PHST- 2000/09/26 11:00 [pubmed]
PHST- 2001/02/28 10:01 [medline]
PHST- 2000/09/26 11:00 [entrez]
PST - ppublish
SO  - Glycoconj J. 1999 Nov;16(11):681-4.

PMID- 16615117
OWN - NLM
STAT- MEDLINE
DCOM- 20060912
LR  - 20160303
IS  - 0020-7136 (Print)
IS  - 0020-7136 (Linking)
VI  - 119
IP  - 6
DP  - 2006 Sep 15
TI  - Interference with O-glycosylation in RMA lymphoma cells leads to a reduced in
      vivo growth of the tumor.
PG  - 1495-500
AB  - Carbohydrate processing in cancer cells can influence the growth, metastatic
      potential, vascularization and immune recognition of such cells. Interference
      with N-glycosylation has been shown both to reduce the membrane expression of MHC
      class I and to increase the in vitro sensitivity of tumor cells to NK cell
      killing. We investigated the effect of O-glycosylation inhibition on the in vivo 
      growth, phenotype and NK sensitivity of RMA lymphoma cells using benzyl
      N-acetyl-alpha-D-galactosamide (BAG). BAG-treated cells were found to have a
      strongly reduced local growth potential in vivo. However, inhibition of
      O-glycosylation caused this effect without any significant downregulation of
      MHC-I and increase in sensitivity to NK killing as seen after inhibition of
      N-glycosylation using Castanospermine. BAG treatment of RMA cells resulted in the
      removal of larger O-linked glycans and a high expression of the T-antigen
      (GalGalNAc), a target for natural antibodies (NAs) induced by the
      gastrointestinal bacterial flora. Whether the loss of larger O-linked glycans,
      and associated functions, or of biological effects of NA contributed to the
      antitumor effect remains to be established. The results support the idea that
      inhibitors of O- as well as N-linked glycosylation may be useful for the
      treatment of cancer, given that they can be specifically targeted to the tumor
      tissue.
FAU - Chen, Liying
AU  - Chen L
AD  - Microbiology and Tumor Biology Center (MTC), Karolinska Institute, Stockholm,
      Sweden. Liying.Chen@mtc.ki.se
FAU - Sundback, Jonas
AU  - Sundback J
FAU - Olofsson, Sigvard
AU  - Olofsson S
FAU - Jondal, Mikael
AU  - Jondal M
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Int J Cancer
JT  - International journal of cancer
JID - 0042124
RN  - 0 (Anti-Inflammatory Agents, Non-Steroidal)
RN  - 0 (Benzyl Compounds)
RN  - 0 (Enzyme Inhibitors)
RN  - 0 (Indolizines)
RN  - 3554-93-6 (benzyl-alpha-N-acetylgalactosamine)
RN  - EC 3.2.1.45 (Glucosylceramidase)
RN  - KM15WK8O5T (Acetylgalactosamine)
RN  - Q0I3184XM7 (castanospermine)
SB  - IM
MH  - Acetylgalactosamine/analogs & derivatives/metabolism
MH  - Animals
MH  - Anti-Inflammatory Agents, Non-Steroidal/pharmacology
MH  - Benzyl Compounds/metabolism
MH  - Cell Survival
MH  - Enzyme Inhibitors/*pharmacology
MH  - Glucosylceramidase/*antagonists & inhibitors
MH  - Glycosylation
MH  - Humans
MH  - Indolizines/*pharmacology
MH  - Killer Cells, Natural/drug effects/metabolism
MH  - Lymphoma/metabolism/*pathology
MH  - Melanoma, Experimental/metabolism/pathology
MH  - Mice
MH  - Mice, Inbred C57BL
MH  - Tumor Cells, Cultured
EDAT- 2006/04/15 09:00
MHDA- 2006/09/13 09:00
CRDT- 2006/04/15 09:00
PHST- 2006/04/15 09:00 [pubmed]
PHST- 2006/09/13 09:00 [medline]
PHST- 2006/04/15 09:00 [entrez]
AID - 10.1002/ijc.21981 [doi]
PST - ppublish
SO  - Int J Cancer. 2006 Sep 15;119(6):1495-500. doi: 10.1002/ijc.21981.

PMID- 3167827
OWN - NLM
STAT- MEDLINE
DCOM- 19881110
LR  - 20071114
IS  - 0008-5472 (Print)
IS  - 0008-5472 (Linking)
VI  - 48
IP  - 20
DP  - 1988 Oct 15
TI  - An IgG3 monoclonal antibody established after immunization with GM3 lactone:
      immunochemical specificity and inhibition of melanoma cell growth in vitro and in
      vivo.
PG  - 5680-5
AB  - In previous studies, an IgM monoclonal antibody (M2590), established after
      immunization of C57BL/6 mice with syngeneic B16 melanoma cells, was found to
      react with melanoma cells, but not with various normal cells and tissues
      (Taniguchi, M., and Wakabayashi, S., Jpn. J. Cancer Res., 75:418-426, 1984). The 
      structure defined by this antibody was identified as GM3 (Hirabayashi, Y., et
      al., J. Biol. Chem., 260:13328-13333, 1985) organized in membranes at high
      density, although the real immunogen was suggested to be GM3 lactone (Nores, G.
      A., et al., J. Immunol., 139:3171-3176, 1987). Since GM3 lactone was found to be 
      highly immunogenic, we subsequently immunized C57BL/6 mice with GM3 lactone
      coated on Salmonella minnesotae and established hybridoma DH2, secreting an IgG3 
      antibody showing preferential reactivity with GM3 lactone over GM3 under certain 
      conditions. The reactivity of the DH2 antibody was competitively inhibited by
      M2590, and it showed a preferential reactivity with melanoma cells and displayed 
      various immunochemical and immunobiological properties similar to those of M2590.
      However, DH2 antibody inhibited melanoma cell growth in vivo, induced
      antibody-dependent cytotoxicity in vitro, and showed a preferential accumulation 
      in melanoma growth in vivo. These properties are characteristic of the IgG3
      subclass, in striking contrast to IgM antibody M2590, which does not inhibit cell
      growth in vivo or in vitro and does not induce antibody-dependent cytotoxicity.
      Thus, immunization with lactone forms of tumor-associated ganglioside antigens
      might be useful in the production of antibodies and prevention of tumor cell
      growth in vivo (antitumor vaccines).
FAU - Dohi, T
AU  - Dohi T
AD  - Biomembrane Institute, Seattle, Washington 98119.
FAU - Nores, G
AU  - Nores G
FAU - Hakomori, S
AU  - Hakomori S
LA  - eng
GR  - CA42505/CA/NCI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Cancer Res
JT  - Cancer research
JID - 2984705R
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (G(M3) Ganglioside)
RN  - 0 (Gangliosides)
RN  - 0 (Immunoglobulin G)
SB  - IM
MH  - Animals
MH  - *Antibodies, Monoclonal
MH  - Antibody Specificity
MH  - Antibody-Dependent Cell Cytotoxicity
MH  - Cell Division
MH  - Cells, Cultured
MH  - Dogs
MH  - G(M3) Ganglioside/*immunology
MH  - Gangliosides/*immunology
MH  - Immunoglobulin G/*immunology
MH  - Melanoma/immunology/*pathology
MH  - Mice
MH  - Mice, Inbred C57BL
MH  - Rats
EDAT- 1988/10/15 00:00
MHDA- 1988/10/15 00:01
CRDT- 1988/10/15 00:00
PHST- 1988/10/15 00:00 [pubmed]
PHST- 1988/10/15 00:01 [medline]
PHST- 1988/10/15 00:00 [entrez]
PST - ppublish
SO  - Cancer Res. 1988 Oct 15;48(20):5680-5.

PMID- 8625037
OWN - NLM
STAT- MEDLINE
DCOM- 19960627
LR  - 20100324
IS  - 0008-543X (Print)
IS  - 0008-543X (Linking)
VI  - 76
IP  - 10
DP  - 1995 Nov 15
TI  - Expression of Thomsen-Friedenreich-related antigens in primary and metastatic
      colorectal carcinomas. A reevaluation.
PG  - 1700-8
AB  - BACKGROUND: Expression of the pancarcinoma Thomsen-Friedenreich (TF) carbohydrate
      antigen or, more correctly, hapten, in colorectal carcinomas is not generally
      agreed on. Furthermore, its suggested role in liver metastasis so far has not
      been substantiated by direct immunohistochemical evidence. METHODS: Cryostat
      sections from 52 primary tumors (20 with adjacent transitional mucosa), 22 liver 
      metastases of colorectal carcinomas, and 17 samples of normal mucosae were
      examined immunohistologically with a panel of at least two monoclonal antibodies 
      (mAbs) each to TF, to its precursor, Tn, and to sialosyl-Tn, among them two newly
      developed anti-TF mAbs. RESULTS: Of the primary colorectal carcinomas, 60%
      expressed TF. Staining was more intense with TF-alpha/beta-reactive than with
      exclusively TF-alpha- or TF-beta-reactive mAbs. Normal and transitional mucosae
      were negative. Liver metastases were positive for TF in a significantly higher
      percentage of cases (91%) than primary carcinomas. Patients with TF-positive
      primary tumors had a significantly higher risk to develop liver metastases
      compared with patients with TF-negative tumors (57% vs. 14%, respectively). Tn
      and sialosyl-Tn were expressed concomitantly in most primary (85%) and metastatic
      (95%) colorectal carcinomas. These antigens also were detected in transitional
      mucosae (Tn in 25%, sialosyl-Tn in 55% of cases). Normal mucosae were negative.
      CONCLUSIONS: These results prove unequivocally the presence of exposed TF
      epitopes in a majority of colorectal carcinomas in which both anomers of TF are
      expressed. These data further suggest that TF favors liver metastasis and that
      its expression in primary colorectal carcinomas is a significant risk factor for 
      the development of liver metastasis.
FAU - Cao, Y
AU  - Cao Y
AD  - Max Delbruck Centre for Molecular Medicine, Berlin-Buch, Germany.
FAU - Karsten, U R
AU  - Karsten UR
FAU - Liebrich, W
AU  - Liebrich W
FAU - Haensch, W
AU  - Haensch W
FAU - Springer, G F
AU  - Springer GF
FAU - Schlag, P M
AU  - Schlag PM
LA  - eng
GR  - CA 22540/CA/NCI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Cancer
JT  - Cancer
JID - 0374236
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens, Neoplasm)
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 3554-90-3 (Thomsen-Friedenreich antigen)
SB  - AIM
SB  - IM
MH  - Antibodies, Monoclonal/immunology
MH  - Antigens, Neoplasm/*analysis
MH  - Antigens, Tumor-Associated, Carbohydrate/*analysis
MH  - Colorectal Neoplasms/*immunology/pathology
MH  - Humans
MH  - Immunohistochemistry
MH  - Liver Neoplasms/immunology/secondary
MH  - Neoplasm Staging
EDAT- 1995/11/15 00:00
MHDA- 1995/11/15 00:01
CRDT- 1995/11/15 00:00
PHST- 1995/11/15 00:00 [pubmed]
PHST- 1995/11/15 00:01 [medline]
PHST- 1995/11/15 00:00 [entrez]
PST - ppublish
SO  - Cancer. 1995 Nov 15;76(10):1700-8.

PMID- 9404700
OWN - NLM
STAT- MEDLINE
DCOM- 19980102
LR  - 20151119
IS  - 0008-543X (Print)
IS  - 0008-543X (Linking)
VI  - 80
IP  - 12
DP  - 1997 Dec 15
TI  - The prognostic significance of sialyl-Tn antigen in women treated with breast
      carcinoma treated with adjuvant chemotherapy.
PG  - 2240-9
AB  - BACKGROUND: Sialyl-Tn (STn) represents an aberrantly glycosylated mucin epitope
      that is expressed in breast carcinoma and other adenocarcinomas and is an
      important factor in the development of novel immunotherapeutic approaches. The
      primary aim of the current study was to investigate the influence of STn
      expression on the prognoses of patients with breast carcinoma. METHODS: A cohort 
      of 207 women diagnosed with invasive breast carcinoma who were treated with
      anthracycline-containing adjuvant chemotherapy and were enrolled in a randomized 
      clinical trial were studied. Expression of STn was determined by an
      immunohistochemical procedure in which the B72.3 monoclonal antibody was used.
      Kaplan-Meier and Cox proportional regression survival analyses were used to
      compare low STn and high STn patients. RESULTS: Forty-eight (23%) of the 207
      specimens demonstrated high STn staining (>25% cells were immunoreactive). During
      a median follow-up of 5 years, high STn patients had worse disease free survival 
      than low STn patients (55% vs. 74%, respectively; P = 0.03). High STn expression 
      was significantly associated with age (P = 0.04) but not with other conventional 
      prognostic markers. In multivariate analysis using the Cox regression model, high
      STn emerged as an independent prognostic indicator for disease free survival
      (hazard ratio [HR], 2.02; 95% confidence interval [CI], 1.09-3.73) and for
      overall survival (HR, 2.16; 95% CI, 0.95-4.92). CONCLUSIONS: The results of this 
      study suggest that STn may be a valuable marker for identifying women at high
      risk of developing recurrent breast carcinoma who may be candidates for trials
      investigating new therapies in combination with standard adjuvant therapy.
FAU - Kinney, A Y
AU  - Kinney AY
AD  - Department of Breast Medical Oncology, The University of Texas M. D. Anderson
      Cancer Center, Houston 77030, USA.
FAU - Sahin, A
AU  - Sahin A
FAU - Vernon, S W
AU  - Vernon SW
FAU - Frankowski, R F
AU  - Frankowski RF
FAU - Annegers, J F
AU  - Annegers JF
FAU - Hortobagyi, G N
AU  - Hortobagyi GN
FAU - Buzdar, A U
AU  - Buzdar AU
FAU - Frye, D K
AU  - Frye DK
FAU - Dhingra, K
AU  - Dhingra K
LA  - eng
GR  - R25-57730/PHS HHS/United States
PT  - Clinical Trial
PT  - Journal Article
PT  - Randomized Controlled Trial
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Cancer
JT  - Cancer
JID - 0374236
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antibodies, Neoplasm)
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (B72.3 antibody)
RN  - 0 (Biomarkers, Tumor)
RN  - 0 (sialosyl-Tn antigen)
RN  - 5V9KLZ54CY (Vinblastine)
RN  - 80168379AG (Doxorubicin)
RN  - 8N3DW7272P (Cyclophosphamide)
RN  - Q573I9DVLP (Leucovorin)
RN  - U3P01618RT (Fluorouracil)
RN  - YL5FZ2Y5U1 (Methotrexate)
RN  - CAF protocol
RN  - FAC-MV protocol
SB  - AIM
SB  - IM
MH  - Adult
MH  - Aged
MH  - Antibodies, Monoclonal/analysis
MH  - Antibodies, Neoplasm/analysis
MH  - Antigens, Tumor-Associated, Carbohydrate/*biosynthesis
MH  - Antineoplastic Combined Chemotherapy Protocols/*administration & dosage
MH  - Biomarkers, Tumor
MH  - Breast Neoplasms/drug therapy/metabolism/*pathology
MH  - Carcinoma, Ductal, Breast/drug therapy/metabolism/*pathology
MH  - Carcinoma, Lobular/drug therapy/metabolism/*pathology
MH  - Chemotherapy, Adjuvant
MH  - Cohort Studies
MH  - Cyclophosphamide/administration & dosage
MH  - Disease-Free Survival
MH  - Doxorubicin/administration & dosage
MH  - Female
MH  - Fluorouracil/administration & dosage
MH  - Humans
MH  - Immunoenzyme Techniques
MH  - Leucovorin/administration & dosage
MH  - Methotrexate/administration & dosage
MH  - Middle Aged
MH  - Prognosis
MH  - Vinblastine/administration & dosage
EDAT- 1997/12/24 01:15
MHDA- 2000/06/20 09:00
CRDT- 1997/12/24 01:15
PHST- 1997/12/24 01:15 [pubmed]
PHST- 2000/06/20 09:00 [medline]
PHST- 1997/12/24 01:15 [entrez]
AID - 10.1002/(SICI)1097-0142(19971215)80:12<2240::AID-CNCR4>3.0.CO;2-Y [pii]
PST - ppublish
SO  - Cancer. 1997 Dec 15;80(12):2240-9.

PMID- 16477004
OWN - NLM
STAT- MEDLINE
DCOM- 20060613
LR  - 20181113
IS  - 0027-8424 (Print)
IS  - 0027-8424 (Linking)
VI  - 103
IP  - 8
DP  - 2006 Feb 21
TI  - An enzymatic ruler modulates Lewis antigen glycosylation of Helicobacter pylori
      LPS during persistent infection.
PG  - 2863-8
AB  - Helicobacter pylori persistently colonizes about half the human population and
      contributes to the development of peptic ulcer disease and gastric cancer. This
      organism has evolved means to structurally alter its surface characteristics to
      evade innate and adaptive immune responses. H. pylori produces LPS O-antigen
      units that can be posttranslationally fucosylated to generate Lewis antigens,
      structures also found on human epithelial cells. We demonstrate an extensive
      diversity of Lewis x and Lewis y expression in LPS O-antigen units, occurring
      over time and in different regions of the human stomach. Lewis expression
      patterns were correlated with the on/off status of the three fucosyltransferases 
      (FucT), FutA, FutB, and FutC, which are regulated via slipped-strand mispairing
      in intragenic polyC tract regions of the corresponding genes. The alpha1,3-FucT, 
      FutA and FutB, each contain a C-terminal heptad repeat region, consisting of a
      variable number of DD/NLRV/INY tandem repeats. Variations in the number of heptad
      repeats correlated to the sizes of O-antigen polymers to become decorated by
      fucose residues. Our data support a molecular ruler mechanism for how H. pylori
      varies its LPS fucosylation pattern, where one heptad repeat in the enzyme
      corresponds to one N-acetyl-beta-lactosamine unit in the O-antigen
      polysaccharide.
FAU - Nilsson, Christina
AU  - Nilsson C
AD  - Microbiology and Tumor Biology Center, Karolinska Institutet, 171 77 Stockholm,
      Sweden. christina.nilsson@mtc.ki.se
FAU - Skoglund, Anna
AU  - Skoglund A
FAU - Moran, Anthony P
AU  - Moran AP
FAU - Annuk, Heidi
AU  - Annuk H
FAU - Engstrand, Lars
AU  - Engstrand L
FAU - Normark, Staffan
AU  - Normark S
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20060213
PL  - United States
TA  - Proc Natl Acad Sci U S A
JT  - Proceedings of the National Academy of Sciences of the United States of America
JID - 7505876
RN  - 0 (Bacterial Proteins)
RN  - 0 (Lewis Blood-Group System)
RN  - 0 (Lewis Y antigen)
RN  - 0 (Lewis a oligosaccharide)
RN  - 0 (Lipopolysaccharides)
RN  - 0 (O Antigens)
RN  - 0 (Oligosaccharides)
RN  - EC 2.4.1.- (Fucosyltransferases)
SB  - IM
MH  - Amino Acid Sequence
MH  - Bacterial Proteins/chemistry/*genetics
MH  - Dimerization
MH  - Fucosyltransferases/chemistry/*genetics
MH  - Glycosylation
MH  - Helicobacter Infections/*microbiology
MH  - Helicobacter pylori/*enzymology/genetics
MH  - Humans
MH  - Lewis Blood-Group System/analysis/*metabolism
MH  - Lipopolysaccharides/chemistry/metabolism
MH  - Molecular Sequence Data
MH  - O Antigens/chemistry/metabolism
MH  - Oligosaccharides/analysis/*metabolism
MH  - Repetitive Sequences, Amino Acid
MH  - Stomach/microbiology
PMC - PMC1413829
EDAT- 2006/02/16 09:00
MHDA- 2006/06/14 09:00
CRDT- 2006/02/16 09:00
PHST- 2006/02/16 09:00 [pubmed]
PHST- 2006/06/14 09:00 [medline]
PHST- 2006/02/16 09:00 [entrez]
AID - 0511119103 [pii]
AID - 10.1073/pnas.0511119103 [doi]
PST - ppublish
SO  - Proc Natl Acad Sci U S A. 2006 Feb 21;103(8):2863-8. doi:
      10.1073/pnas.0511119103. Epub 2006 Feb 13.

PMID- 1548698
OWN - NLM
STAT- MEDLINE
DCOM- 19920422
LR  - 20131121
IS  - 0022-2836 (Print)
IS  - 0022-2836 (Linking)
VI  - 224
IP  - 1
DP  - 1992 Mar 5
TI  - Refined crystal structure of ascorbate oxidase at 1.9 A resolution.
PG  - 179-205
AB  - The crystal structure of the fully oxidized form of ascorbate oxidase (EC
      1.10.3.3) from Zucchini has been refined at 1.90 A (1 A = 0.1 nm) resolution,
      using an energy-restrained least-squares refinement procedure. The refined model,
      which includes 8764 protein atoms, 9 copper atoms and 970 solvent molecules, has 
      a crystallographic R-factor of 20.3% for 85,252 reflections between 8 and 1.90 A 
      resolution. The root-mean-square deviation in bond lengths and bond angles from
      ideal values is 0.011 A and 2.99 degrees, respectively. The subunits of 552
      residues (70,000 Mr) are arranged as tetramers with D2 symmetry. One of the dyads
      is realized by the crystallographic axis parallel to the c-axis giving one dimer 
      in the asymmetric unit. The dimer related about this crystallographic axis is
      suggested as the dimer present in solution. Asn92 is the attachment site for one 
      of the two N-linked sugar moieties, which has defined electron density for the
      N-linked N-acetyl-glucosamine ring. Each subunit is built up by three domains
      arranged sequentially on the polypeptide chain and tightly associated in space.
      The folding of all three domains is of a similar beta-barrel type and related to 
      plastocyanin and azurin. An analysis of intra- and intertetramer hydrogen bond
      and van der Waals interactions is presented. Each subunit has four copper atoms
      bound as mononuclear and trinuclear species. The mononuclear copper has two
      histidine, a cysteine and a methionine ligand and represents the type-1 copper.
      It is located in domain 3. The bond lengths of the type-1 copper centre are
      comparable to the values for oxidized plastocyanin. The trinuclear cluster has
      eight histidine ligands symmetrically supplied from domain 1 and 3. It may be
      subdivided into a pair of copper atoms with histidine ligands whose ligating
      N-atoms (5 NE2 atoms and one ND1 atom) are arranged trigonal prismatic. The pair 
      is the putative type-3 copper. The remaining copper has two histidine ligands and
      is the putative spectroscopic type-2 copper. Two oxygen atoms are bound to the
      trinuclear species as OH- or O2- and bridging the putative type-3 copper pair and
      as OH- or H2O bound to the putative type-2 copper trans to the copper pair. The
      bond lengths within the trinuclear copper site are similar to comparable
      binuclear model compounds. The putative binding site for the reducing substrate
      is close to the type-1 copper.(ABSTRACT TRUNCATED AT 400 WORDS)
FAU - Messerschmidt, A
AU  - Messerschmidt A
AD  - Max-Planck-Institut fur Biochemie, Martinsried, F.R.G.
FAU - Ladenstein, R
AU  - Ladenstein R
FAU - Huber, R
AU  - Huber R
FAU - Bolognesi, M
AU  - Bolognesi M
FAU - Avigliano, L
AU  - Avigliano L
FAU - Petruzzelli, R
AU  - Petruzzelli R
FAU - Rossi, A
AU  - Rossi A
FAU - Finazzi-Agro, A
AU  - Finazzi-Agro A
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - J Mol Biol
JT  - Journal of molecular biology
JID - 2985088R
RN  - 0 (Solvents)
RN  - 789U1901C5 (Copper)
RN  - EC 1.- (Oxidoreductases)
RN  - EC 1.10.3.2 (Laccase)
RN  - EC 1.10.3.3 (Ascorbate Oxidase)
RN  - S88TT14065 (Oxygen)
SB  - IM
MH  - Amino Acid Sequence
MH  - Ascorbate Oxidase/*chemistry/metabolism
MH  - Binding Sites
MH  - Copper/chemistry/metabolism
MH  - Electron Transport
MH  - Enzyme Activation
MH  - Hydrogen Bonding
MH  - Kinetics
MH  - Laccase
MH  - Models, Molecular
MH  - Molecular Sequence Data
MH  - Oxidoreductases/metabolism
MH  - Oxygen/metabolism
MH  - Plants/enzymology
MH  - Protein Conformation
MH  - Solvents
MH  - Substrate Specificity
MH  - Temperature
MH  - X-Ray Diffraction
EDAT- 1992/03/05 00:00
MHDA- 1992/03/05 00:01
CRDT- 1992/03/05 00:00
PHST- 1992/03/05 00:00 [pubmed]
PHST- 1992/03/05 00:01 [medline]
PHST- 1992/03/05 00:00 [entrez]
AID - 0022-2836(92)90583-6 [pii]
PST - ppublish
SO  - J Mol Biol. 1992 Mar 5;224(1):179-205.

PMID- 10712696
OWN - NLM
STAT- MEDLINE
DCOM- 20000413
LR  - 20031114
IS  - 0950-382X (Print)
IS  - 0950-382X (Linking)
VI  - 35
IP  - 5
DP  - 2000 Mar
TI  - Functional genomics of Helicobacter pylori: identification of a beta-1,4
      galactosyltransferase and generation of mutants with altered lipopolysaccharide.
PG  - 1156-67
AB  - A previously annotated open reading frame (ORF) (HP0826) from Helicobacter pylori
      was cloned and expressed in Escherichia coli cells and determined to be a
      beta-1,4-galactosyltransferase that used GlcNAc as an acceptor. Mutational
      analysis in H. pylori strains demonstrated that this enzyme plays a key role in
      the biosynthesis of the type 2 N-acetyl-lactosamine (LacNAc) polysaccharide
      O-chain backbone, by catalysing the addition of Gal to GlcNAc. To examine the
      potential role of this O-chain structure in bacterial colonization of the host
      stomach, the mutation was introduced into H. pylori strain SS1 which is known to 
      be capable of colonizing the gastric mucosa of mice. Compared with the parental
      strain, mutated SS1 was less efficient at colonizing the murine stomach.
FAU - Logan, S M
AU  - Logan SM
AD  - Institute for Biological Sciences, National Research Council of Canada, Ottawa,
      Ontario, Canada, K1A OR6. susan.logan@nrc.ca
FAU - Conlan, J W
AU  - Conlan JW
FAU - Monteiro, M A
AU  - Monteiro MA
FAU - Wakarchuk, W W
AU  - Wakarchuk WW
FAU - Altman, E
AU  - Altman E
LA  - eng
PT  - Journal Article
PL  - England
TA  - Mol Microbiol
JT  - Molecular microbiology
JID - 8712028
RN  - 0 (DNA Primers)
RN  - 0 (Lipopolysaccharides)
RN  - EC 2.4.1.90 (N-Acetyllactosamine Synthase)
SB  - IM
MH  - Alleles
MH  - Amino Acid Sequence
MH  - Animals
MH  - Base Sequence
MH  - Carbohydrate Sequence
MH  - DNA Primers
MH  - Electrophoresis, Polyacrylamide Gel
MH  - Female
MH  - *Genome, Bacterial
MH  - Helicobacter Infections/enzymology/metabolism/microbiology
MH  - Helicobacter pylori/enzymology/*genetics/metabolism/pathogenicity
MH  - Lipopolysaccharides/chemistry/*metabolism
MH  - Mice
MH  - Molecular Sequence Data
MH  - *Mutagenesis
MH  - N-Acetyllactosamine Synthase/chemistry/*metabolism
MH  - Sequence Homology, Amino Acid
MH  - Spectrometry, Mass, Fast Atom Bombardment
MH  - Stomach/microbiology
EDAT- 2000/03/11 09:00
MHDA- 2000/04/15 09:00
CRDT- 2000/03/11 09:00
PHST- 2000/03/11 09:00 [pubmed]
PHST- 2000/04/15 09:00 [medline]
PHST- 2000/03/11 09:00 [entrez]
AID - mmi1784 [pii]
PST - ppublish
SO  - Mol Microbiol. 2000 Mar;35(5):1156-67.

PMID- 7775461
OWN - NLM
STAT- MEDLINE
DCOM- 19950710
LR  - 20190508
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 270
IP  - 23
DP  - 1995 Jun 9
TI  - Neolactoglycosphingolipids, potential mediators of corneal epithelial cell
      migration.
PG  - 14015-23
AB  - Cell migration is a fundamental process of wound repair in biological systems. In
      an attempt to identify plasma membrane glycoconjugates which mediate cell
      migration, migrating and nonmigrating rabbit corneal epithelia were analyzed for 
      reactivity with monoclonal antibodies (mAbs) specific for unsubstituted
      N-acetyl-lactosamine (mAb 1B2), Le(x) (mAbs 7A and MMA), and sialyl Le(x) (mAb
      CSLEX1) carbohydrate chains of neolactoglycoconjugates. Immunohistochemical
      analysis indicated that regardless of whether the epithelia analyzed were from
      corneas of animals in vivo, corneas in organ culture, or cells in tissue culture,
      migrating cells stained intensely with mAb 1B2, whereas nonmigrating cells either
      did not stain or stained only weakly. mAbs MMA and 7A stained migrating
      epithelium as well as basal and middle cell layers of normal, nonmigrating
      epithelium. mAb CSLEX1 did not stain wounded corneas but stained the superficial 
      cell layer of normal corneal epithelium. Biochemical analyses by TLC
      immunostaining revealed the presence of three mAb 1B2-reactive glycosphingolipids
      (GSL), neolactotetraosyl-(nLc4, paragloboside), neolactohexaosyl- (nLc6), and
      neolacto-octaosylceramide (nLc8) in migrating epithelia. In contrast,
      nonmigrating epithelia contained only trace amounts of these glycolipids.
      Exogenous addition of nLc4, but not various other GSLs including a Le(x)-GSL
      (SSEA-1), stimulated re-epithelialization of wounds in an experimental model of
      corneal epithelial wound healing. Moreover, re-epithelialization of wounds was
      significantly inhibited by mAb 1B2 but not by mAb MMA. The data suggest that
      neolacto-GSLs of corneal epithelium may be among the molecules which mediate
      healing of corneal epithelial wounds by influencing cell migration.
FAU - Panjwani, N
AU  - Panjwani N
AD  - New England Eye Center, Boston, Massachusetts, USA.
FAU - Zhao, Z
AU  - Zhao Z
FAU - Ahmad, S
AU  - Ahmad S
FAU - Yang, Z
AU  - Yang Z
FAU - Jungalwala, F
AU  - Jungalwala F
FAU - Baum, J
AU  - Baum J
LA  - eng
GR  - EY07088/EY/NEI NIH HHS/United States
GR  - EY09349/EY/NEI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Globosides)
RN  - 0 (Glycosphingolipids)
RN  - 0 (Lewis X Antigen)
RN  - 56573-54-7 (paragloboside)
SB  - IM
MH  - Animals
MH  - Antibodies, Monoclonal/immunology
MH  - Cell Communication
MH  - Cell Movement
MH  - Cells, Cultured
MH  - Cornea/*cytology/physiology
MH  - Epithelial Cells
MH  - Globosides/*physiology
MH  - Glycosphingolipids/*physiology
MH  - Immunohistochemistry
MH  - Lewis X Antigen/physiology
MH  - Organ Culture Techniques
MH  - Rabbits
MH  - *Wound Healing
EDAT- 1995/06/09 00:00
MHDA- 1995/06/09 00:01
CRDT- 1995/06/09 00:00
PHST- 1995/06/09 00:00 [pubmed]
PHST- 1995/06/09 00:01 [medline]
PHST- 1995/06/09 00:00 [entrez]
AID - 10.1074/jbc.270.23.14015 [doi]
PST - ppublish
SO  - J Biol Chem. 1995 Jun 9;270(23):14015-23. doi: 10.1074/jbc.270.23.14015.

PMID- 4029397
OWN - NLM
STAT- MEDLINE
DCOM- 19851021
LR  - 20061115
IS  - 0014-5793 (Print)
IS  - 0014-5793 (Linking)
VI  - 189
IP  - 1
DP  - 1985 Sep 9
TI  - A monoclonal antibody reacting specifically with ganglioside GD1b in human brain.
PG  - 23-6
AB  - A mouse monoclonal antibody directed against one of the major human brain
      gangliosides, GD1b, has been produced. The antibody binds specifically to the
      carbohydrate structure of GD1b as it does not react with structurally related
      gangliosides like GM1, GD2, GT1b or Fuc-GM1, or any other ganglioside of human
      brain. The results further indicate that terminal galactose as well as the
      disialosyl group linked to the inner galactose moiety are involved in binding to 
      the antibody.
FAU - Fredman, P
AU  - Fredman P
FAU - Jeansson, S
AU  - Jeansson S
FAU - Lycke, E
AU  - Lycke E
FAU - Svennerholm, L
AU  - Svennerholm L
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - FEBS Lett
JT  - FEBS letters
JID - 0155157
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Carbohydrates)
RN  - 0 (Gangliosides)
RN  - 19553-76-5 (ganglioside, GD1b)
SB  - IM
MH  - Animals
MH  - Antibodies, Monoclonal/*immunology
MH  - Antibody Specificity
MH  - Binding Sites
MH  - *Brain Chemistry
MH  - Carbohydrates/analysis
MH  - Enzyme-Linked Immunosorbent Assay
MH  - Gangliosides/*immunology
MH  - Humans
MH  - Mice
EDAT- 1985/09/09 00:00
MHDA- 1985/09/09 00:01
CRDT- 1985/09/09 00:00
PHST- 1985/09/09 00:00 [pubmed]
PHST- 1985/09/09 00:01 [medline]
PHST- 1985/09/09 00:00 [entrez]
AID - 0014-5793(85)80834-6 [pii]
PST - ppublish
SO  - FEBS Lett. 1985 Sep 9;189(1):23-6.

PMID- 11169215
OWN - NLM
STAT- MEDLINE
DCOM- 20010405
LR  - 20061115
IS  - 0300-9475 (Print)
IS  - 0300-9475 (Linking)
VI  - 53
IP  - 2
DP  - 2001 Feb
TI  - Characterization of Forssman and other antigen/antibody systems in vascularized
      mouse heart to rat xenotransplantation.
PG  - 121-31
AB  - In the present study, the nature of hyperacute xenograft rejection was closely
      studied in a vascularized mouse-to-rat transplantation model. Antibodies against 
      mouse heart, erythrocytes and lymphocytes and against the Forssman antigen were
      raised in the rat. Upon heterotopic heart transplantation the respective antisera
      were intravenously (i.v.) injected. Passive transfer of antiheart,
      antierythrocyte or antilymphocyte serum resulted in hyperacute rejection of the
      transplanted mouse heart. Subfractionation of the antiheart serum showed that the
      capacity to induce hyperacute rejection was carried by the immunoglobulin (Ig)G
      fraction. When antierythrocyte serum adsorbed with mouse erythrocytes was
      administered the cardiac grafts remained beating. To the contrary, antilymphocyte
      serum adsorbed with erythrocytes still had the capacity to induce hyperacute
      rejection. None of the rats that had previously been challenged with the Forssman
      antigen rejected their grafts hyperacutely. Subsequent investigations by electron
      microscopy revealed that the Forssman antigen is expressed on dendritic cells
      (DC) adjacent to the vessels, but not on the vascular endothelium, thus
      explaining the inability of the anti-Forssman serum to induce hyperacute
      rejection. Taken together, we have demonstrated the existence of several
      xenoantigens that can be targets for antibody-mediated rejection, suggesting that
      more than one relevant xenoantigen exists also in more distantly related
      combinations, such as the pig-to-human combination.
FAU - Gustavsson, M L
AU  - Gustavsson ML
AD  - Department of Clinical Chemistry, Sahlgrenska University Hospital and University 
      of Goteborg, Goteborg, Sweden.
FAU - Johnsson, C
AU  - Johnsson C
FAU - Albertsson, P
AU  - Albertsson P
FAU - Lukes, D
AU  - Lukes D
FAU - Steen, L M
AU  - Steen LM
FAU - Johansson, B R
AU  - Johansson BR
FAU - Mjornstedt, L
AU  - Mjornstedt L
FAU - Norrby, J
AU  - Norrby J
FAU - Tufveson, G
AU  - Tufveson G
FAU - Olausson, M
AU  - Olausson M
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - Scand J Immunol
JT  - Scandinavian journal of immunology
JID - 0323767
RN  - 0 (Antibodies, Heterophile)
RN  - 0 (Antigens, Heterophile)
RN  - 0 (Antilymphocyte Serum)
RN  - 0 (Glycolipids)
RN  - 0 (Immunoglobulin G)
RN  - 9013-60-9 (Forssman Antigen)
SB  - IM
MH  - Acute Disease
MH  - Animals
MH  - Antibodies, Heterophile/*immunology
MH  - *Antigen-Antibody Reactions
MH  - Antigens, Heterophile/*immunology
MH  - Antilymphocyte Serum/pharmacology
MH  - Aorta/*immunology/pathology
MH  - Carbohydrate Sequence
MH  - Coronary Vessels/*immunology/pathology
MH  - Dendritic Cells/immunology
MH  - Endothelium, Vascular/*immunology/pathology
MH  - Erythrocytes/immunology
MH  - Forssman Antigen/*immunology
MH  - Glycolipids/immunology
MH  - Graft Rejection/immunology/pathology
MH  - Heart Transplantation/*immunology
MH  - Immunization
MH  - Immunization, Passive
MH  - Immunoglobulin G/immunology
MH  - Mice
MH  - Mice, Inbred BALB C
MH  - Mice, Inbred C57BL
MH  - Microscopy, Electron
MH  - Molecular Sequence Data
MH  - Myocardium/immunology
MH  - Rats
MH  - Rats, Inbred Lew
MH  - Rats, Inbred Strains
MH  - Species Specificity
MH  - Transplantation, Heterologous/*immunology
MH  - Transplantation, Heterotopic
EDAT- 2001/02/13 11:00
MHDA- 2001/04/06 10:01
CRDT- 2001/02/13 11:00
PHST- 2001/02/13 11:00 [pubmed]
PHST- 2001/04/06 10:01 [medline]
PHST- 2001/02/13 11:00 [entrez]
AID - sji840 [pii]
PST - ppublish
SO  - Scand J Immunol. 2001 Feb;53(2):121-31.

PMID- 3170507
OWN - NLM
STAT- MEDLINE
DCOM- 19881108
LR  - 20190510
IS  - 0021-924X (Print)
IS  - 0021-924X (Linking)
VI  - 103
IP  - 4
DP  - 1988 Apr
TI  - Different fine binding specificities of monoclonal antibodies to
      disialosylganglioside GD2.
PG  - 682-7
AB  - The fine structural specificities of six monoclonal antibodies (MAbs) to
      ganglioside GD2, GalNAc beta 1----4(NeuAc alpha 2----8NeuAc alpha 2----3)Gal beta
      1----4Glc-Cer, were studied. The binding specificities of these MAbs were found
      to differ from each other by virtue of their binding to structurally related
      authentic standard glycolipids as revealed by three different assay systems,
      including enzyme immunostaining on thin-layer chromatography, enzyme-linked
      immunosorbent assay, and immune adherence inhibition assay. The MAbs examined
      could be divided into three binding types. MAbs A1-201, A1-410, and A1-425 bound 
      specifically to ganglioside GD2 and none of the other gangliosides tested. Two
      other MAbs (A1-245 and A1-267) reacted not only with GD2, but also with several
      other gangliosides having the sequence NeuAc alpha 2----8NeuAc alpha 2----3Gal
      (GD3, GD1b, GT1a, GT1b, and GQ1b). The reactivities with these gangliosides
      varied to some degree. In addition, these MAbs were found to react with both
      GD3(NeuAc-NeuAc) and GD3(NeuGc-NeuAc), but not with GD3(NeuAc-NeuGc) or
      GD3(NeuGc-NeuGc). The last MAb (A1-287) also reacted with several other
      gangliosides but with lower avidity than A1-245 and A1-267. These findings
      suggest that each MAb to ganglioside GD2 may have an individual binding
      specificity and avidity. These MAbs represent potentially useful reagents for
      analyzing the function of GD2 on cell surface membranes, and provide a system for
      precisely studying the interactions between an anti-ganglioside antibody and the 
      binding epitope of the antigenic determinant.
FAU - Tai, T
AU  - Tai T
AD  - Department of Oncology, Tokyo Metropolitan Institute of Medical Science.
FAU - Kawashima, I
AU  - Kawashima I
FAU - Tada, N
AU  - Tada N
FAU - Dairiki, K
AU  - Dairiki K
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - J Biochem
JT  - Journal of biochemistry
JID - 0376600
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Gangliosides)
RN  - 0 (Glycolipids)
RN  - 65988-71-8 (ganglioside, GD2)
SB  - IM
MH  - Animals
MH  - Antibodies, Monoclonal/*immunology
MH  - Cell Line
MH  - Chromatography, Thin Layer
MH  - Cross Reactions
MH  - Enzyme-Linked Immunosorbent Assay
MH  - Gangliosides/*immunology
MH  - Glycolipids/immunology/isolation & purification
MH  - Humans
MH  - Immune Adherence Reaction
MH  - Immunochemistry
MH  - Mice
EDAT- 1988/04/01 00:00
MHDA- 1988/04/01 00:01
CRDT- 1988/04/01 00:00
PHST- 1988/04/01 00:00 [pubmed]
PHST- 1988/04/01 00:01 [medline]
PHST- 1988/04/01 00:00 [entrez]
AID - 10.1093/oxfordjournals.jbchem.a122329 [doi]
PST - ppublish
SO  - J Biochem. 1988 Apr;103(4):682-7. doi: 10.1093/oxfordjournals.jbchem.a122329.

PMID- 10748143
OWN - NLM
STAT- MEDLINE
DCOM- 20000621
LR  - 20061115
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 275
IP  - 20
DP  - 2000 May 19
TI  - Molecular cloning of globotriaosylceramide/CD77 synthase, a glycosyltransferase
      that initiates the synthesis of globo series glycosphingolipids.
PG  - 15152-6
AB  - The expression cloning of a cDNA for globotriaosylceramide (Gb3)/CD77 synthase
      (alpha1,4-galactosyltransferase) was achieved using an anti-Gb3 antibody and
      mouse L cells as a recipient cell line for the transfection. The isolated cDNA
      clone designated pVTR1 predicted a type II membrane protein with 19 amino acids
      of cytoplasmic domain, 26 amino acids of transmembrane region, and a catalytic
      domain with 308 amino acids. Introduction of the cDNA clone into L cells resulted
      in the neosynthesis of Gb3/CD77, and the extracts of the transfectant cells
      showed alpha1, 4-galactosyltransferase activity only on lactosylceramide and
      galactosylceramide. In Northern blotting, a 2.3-kilobase mRNA was strongly
      expressed in heart, kidney, spleen, and placenta and weakly in colon, small
      intestine, and brain. Transfection of the cDNA into L cells resulted in the
      constitution of sensitivity to the apoptosis with Shiga-like toxins (verotoxins).
      Since Gb3/CD77 synthase initiates the synthesis of globo series glycolipids, the 
      isolation of this cDNA will make possible further investigations into the
      function of its important series of glycolipids.
FAU - Kojima, Y
AU  - Kojima Y
AD  - Department of Biochemistry II, Nagoya University School of Medicine, Tsurumai,
      Nagoya 466-0065, Japan.
FAU - Fukumoto, S
AU  - Fukumoto S
FAU - Furukawa, K
AU  - Furukawa K
FAU - Okajima, T
AU  - Okajima T
FAU - Wiels, J
AU  - Wiels J
FAU - Yokoyama, K
AU  - Yokoyama K
FAU - Suzuki, Y
AU  - Suzuki Y
FAU - Urano, T
AU  - Urano T
FAU - Ohta, M
AU  - Ohta M
FAU - Furukawa, K
AU  - Furukawa K
LA  - eng
SI  - GENBANK/AB037883
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Glycosphingolipids)
RN  - 0 (Recombinant Proteins)
RN  - 0 (Trihexosylceramides)
RN  - 71965-57-6 (globotriaosylceramide)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Base Sequence
MH  - Catalytic Domain
MH  - Cloning, Molecular
MH  - Gene Library
MH  - Glycosphingolipids/*biosynthesis
MH  - Humans
MH  - Kinetics
MH  - L Cells (Cell Line)
MH  - Melanoma
MH  - Mice
MH  - Molecular Sequence Data
MH  - Recombinant Proteins/chemistry/metabolism
MH  - Transfection
MH  - Trihexosylceramides/chemistry/*genetics/*metabolism
MH  - Tumor Cells, Cultured
EDAT- 2000/04/05 09:00
MHDA- 2000/06/24 11:00
CRDT- 2000/04/05 09:00
PHST- 2000/04/05 09:00 [pubmed]
PHST- 2000/06/24 11:00 [medline]
PHST- 2000/04/05 09:00 [entrez]
AID - 10.1074/jbc.M909620199 [doi]
AID - M909620199 [pii]
PST - ppublish
SO  - J Biol Chem. 2000 May 19;275(20):15152-6. doi: 10.1074/jbc.M909620199.

PMID- 8486686
OWN - NLM
STAT- MEDLINE
DCOM- 19930608
LR  - 20131121
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 268
IP  - 14
DP  - 1993 May 15
TI  - Kinetic and spatial interrelationships between ganglioside glycosyltransferases
      and O-acetyltransferase(s) in human melanoma cells.
PG  - 10185-96
AB  - The melanoma-associated disialogangliosides 9(7)-O-acetyl-GD3 and
      9(7)-O-acetyl-GD2 have been structurally well characterized. However, the
      compartmentalization and sequence of action of the biosynthetic activities
      responsible for synthesizing these molecules remain obscure. Here, we have
      studied the spatial and temporal interrelationships among the activities
      responsible for the later stages of ganglioside biosynthesis and those for
      O-acetylation in cultured human melanoma cells. First, brefeldin A treatment was 
      used to separate biosynthetic steps into compartments distal or proximal to the
      transport block imposed by the drug. In keeping with prior reports, GM2/GD2
      synthase was consistently rendered inaccessible to its acceptors GM3 and GD3. In 
      contrast, the effect on GD3 biosynthesis was cell line-specific. Synthesis of GD3
      was nearly abrogated in two lines, while it accumulated in a third line. This
      indicates that the spatial organization of ganglioside processing activities can 
      vary even between similar cell lines. However, in all cell lines studied, the
      ratio of 9(7)-O-acetyl-GD3 to GD3 was not changed by brefeldin A, indicating that
      the majority of ganglioside O-acetyltransferase activity is co-localized with GD3
      biosynthetic activity in the same Golgi subcompartment(s). As an alternative
      approach, Golgi-enriched fractions from melanoma cells were incubated with
      radiolabeled and nonlabeled nucleotide sugars or acetyl-CoA. In these
      preparations, biosynthesis is dependent upon the co-localization of appropriate
      sugar nucleotide transporters, glycosyltransferases, and acceptors that are
      endogenously present within intact topologically correct compartments.
      Incubations with CMP-Neu5Ac and acetyl-CoA corroborated the results with
      brefeldin A, co-localizing ganglioside O-acetyltransferase activity in
      compartments where GD3 biosynthesis takes place. Analyses with CMP-Neu5Ac and
      UDP-GalNAc showed that GD2 and GD3 synthesis occur in partially overlapping
      compartments. Labeling with acetyl-CoA and UDP-GalNAc indicated that although
      labeled acetate can be transferred from acetyl-CoA directly to GD2, ganglioside
      O-acetyltransferase activity does not substantially overlap with the biosynthetic
      compartment(s) for GD2. Instead, O-acetyl-GD3 appears to be co-localized with the
      compartment of GD2 biosynthesis and serves as an acceptor for GD2 synthase. Thus,
      both 9-O-acetyl-GD3 and GD2 can be precursors of 9-O-acetyl-GD2, but apparently
      in distinct compartments.
FAU - Sjoberg, E R
AU  - Sjoberg ER
AD  - Cancer Center, University of California, San Diego, La Jolla 92093-0063.
FAU - Varki, A
AU  - Varki A
LA  - eng
GR  - R01GM32373/GM/NIGMS NIH HHS/United States
PT  - Journal Article
PT  - Research Support, U.S. Gov't, Non-P.H.S.
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Cyclopentanes)
RN  - 0 (Gangliosides)
RN  - 0 (Lipids)
RN  - 20350-15-6 (Brefeldin A)
RN  - 3063-71-6 (Cytidine Monophosphate N-Acetylneuraminic Acid)
RN  - 528-04-1 (Uridine Diphosphate N-Acetylglucosamine)
RN  - EC 2.3.1.- (Acetyltransferases)
RN  - EC 2.4.- (Glycosyltransferases)
RN  - X2RN3Q8DNE (Galactose)
SB  - IM
MH  - Acetyltransferases/*metabolism
MH  - Brefeldin A
MH  - Chromatography, High Pressure Liquid
MH  - Chromatography, Ion Exchange
MH  - Chromatography, Thin Layer
MH  - Cyclopentanes/pharmacology
MH  - Cytidine Monophosphate N-Acetylneuraminic Acid/metabolism
MH  - Galactose/metabolism
MH  - Gangliosides/*biosynthesis/isolation & purification
MH  - Glycosyltransferases/*metabolism
MH  - Golgi Apparatus/metabolism
MH  - Humans
MH  - Kinetics
MH  - Lipid Metabolism
MH  - Lipids/isolation & purification
MH  - Melanoma/*enzymology
MH  - Models, Biological
MH  - Radioisotope Dilution Technique
MH  - Tumor Cells, Cultured
MH  - Uridine Diphosphate N-Acetylglucosamine/metabolism
EDAT- 1993/05/15 00:00
MHDA- 1993/05/15 00:01
CRDT- 1993/05/15 00:00
PHST- 1993/05/15 00:00 [pubmed]
PHST- 1993/05/15 00:01 [medline]
PHST- 1993/05/15 00:00 [entrez]
PST - ppublish
SO  - J Biol Chem. 1993 May 15;268(14):10185-96.

PMID- 18925876
OWN - NLM
STAT- MEDLINE
DCOM- 20090213
LR  - 20121115
IS  - 1470-8728 (Electronic)
IS  - 0264-6021 (Linking)
VI  - 417
IP  - 3
DP  - 2009 Feb 1
TI  - Ligation of tumour-produced mucins to CD22 dramatically impairs splenic marginal 
      zone B-cells.
PG  - 673-83
LID - 10.1042/BJ20081241 [doi]
AB  - CD22 [Siglec-2 (sialic acid-binding, immunoglobulin-like lectin-2)], a negative
      regulator of B-cell signalling, binds to alpha2,6- sialic acid-linked
      glycoconjugates, including a sialyl-Tn antigen that is one of the typical
      tumour-associated carbohydrate antigens expressed on various mucins. Many
      epithelial tumours secrete mucins into tissues and/or the bloodstream. Mouse
      mammary adenocarcinoma cells, TA3-Ha, produce a mucin named epiglycanin, but a
      subline of them, TA3-St, does not. Epiglycanin binds to CD22 and inhibits B-cell 
      signalling in vitro. The in vivo effect of mucins in the tumour-bearing state was
      investigated using these cell lines. It should be noted that splenic MZ (marginal
      zone) B-cells were dramatically reduced in the mice bearing TA3-Ha cells but not 
      in those bearing TA3-St cells, this being consistent with the finding that the
      thymus-independent response was reduced in these mice. When the mucins were
      administered to normal mice, a portion of them was detected in the splenic MZ
      associated with the MZ B-cells. Furthermore, administration of mucins to normal
      mice clearly reduced the splenic MZ B-cells, similar to tumour-bearing mice.
      These results indicate that mucins in the bloodstream interacted with CD22, which
      led to impairment of the splenic MZ B-cells in the tumour-bearing state.
FAU - Toda, Munetoyo
AU  - Toda M
AD  - Department of Biotechnology, Kyoto Sangyo University, Kamigamo-Motoyama, Kita-ku,
      Kyoto 603-8555, Japan.
FAU - Hisano, Risa
AU  - Hisano R
FAU - Yurugi, Hajime
AU  - Yurugi H
FAU - Akita, Kaoru
AU  - Akita K
FAU - Maruyama, Kouji
AU  - Maruyama K
FAU - Inoue, Mizue
AU  - Inoue M
FAU - Adachi, Takahiro
AU  - Adachi T
FAU - Tsubata, Takeshi
AU  - Tsubata T
FAU - Nakada, Hiroshi
AU  - Nakada H
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - Biochem J
JT  - The Biochemical journal
JID - 2984726R
RN  - 0 (Antigens, T-Independent)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Mucins)
RN  - 0 (Receptors, Antigen, B-Cell)
RN  - 0 (Sialic Acid Binding Ig-like Lectin 2)
RN  - 0 (epiglycanin protein, mouse)
SB  - IM
MH  - Adenocarcinoma/immunology/*metabolism
MH  - Animals
MH  - Antigens, T-Independent/immunology/metabolism
MH  - B-Lymphocytes/*immunology/metabolism
MH  - Binding Sites
MH  - CHO Cells
MH  - Cell Line, Tumor
MH  - Cricetinae
MH  - Cricetulus
MH  - Female
MH  - Membrane Glycoproteins/metabolism
MH  - Mice
MH  - Mice, Inbred Strains
MH  - Mucins/*metabolism
MH  - Receptors, Antigen, B-Cell/metabolism
MH  - Sialic Acid Binding Ig-like Lectin 2/immunology/*metabolism
MH  - Signal Transduction
MH  - Spleen/*immunology
EDAT- 2008/10/18 09:00
MHDA- 2009/02/14 09:00
CRDT- 2008/10/18 09:00
PHST- 2008/10/18 09:00 [pubmed]
PHST- 2009/02/14 09:00 [medline]
PHST- 2008/10/18 09:00 [entrez]
AID - BJ20081241 [pii]
AID - 10.1042/BJ20081241 [doi]
PST - ppublish
SO  - Biochem J. 2009 Feb 1;417(3):673-83. doi: 10.1042/BJ20081241.

PMID- 9456440
OWN - NLM
STAT- MEDLINE
DCOM- 19980226
LR  - 20080318
IS  - 1524-9557 (Print)
IS  - 1524-9557 (Linking)
VI  - 21
IP  - 1
DP  - 1998 Jan
TI  - Induction of IgG antibodies by an anti-idiotype antibody mimicking
      disialoganglioside GD2.
PG  - 75-83
AB  - The anti-idiotype (Id) monoclonal antibody (mAb) 1A7 immunoglobulin G1 (IgG1,
      kappa), raised in syngeneic mice against the murine anti-ganglioside GD2 mAb
      14G2a mimics a carbohydrate epitope on GD2 and serves as a surrogate protein
      antigen for this disialoganglioside. Immunization of allogeneic C57BL/6 mice and 
      rabbits with 1A7 induced anti-GD2 antibodies of IgG isotype that recognize
      purified GD2 by enzyme-linked immunosorbent assay (ELISA) and GD2-positive human 
      melanoma cells (M21/P6) by fluorescence-activated cell sorter (FACS) analysis.
      The specificity of the antisera for GD2 was further confirmed by dot-blot
      analysis. These antisera also specifically lyse GD2-positive M21/P6 target cells 
      in an antibody-dependent cellular cytotoxicity assay. Taken together, these
      results suggest that the anti-Id 1A7 can induce GD2-specific IgG antibodies that 
      can recognize cell surface-associated as well as soluble disialoganglioside GD2.
FAU - Sen, G
AU  - Sen G
AD  - Department of Medicine, University of Kentucky, Lexington 40536-0096, USA.
FAU - Chakraborty, M
AU  - Chakraborty M
FAU - Foon, K A
AU  - Foon KA
FAU - Reisfeld, R A
AU  - Reisfeld RA
FAU - Bhattacharya-Chatterjee, M B
AU  - Bhattacharya-Chatterjee MB
LA  - eng
GR  - 5RO1CA72018-01/CA/NCI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - J Immunother
JT  - Journal of immunotherapy (Hagerstown, Md. : 1997)
JID - 9706083
RN  - 0 (Antibodies, Anti-Idiotypic)
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Gangliosides)
RN  - 0 (Immunoglobulin G)
RN  - 65988-71-8 (ganglioside, GD2)
SB  - IM
MH  - Animals
MH  - Antibodies, Anti-Idiotypic/biosynthesis/*immunology
MH  - Antibodies, Monoclonal/immunology
MH  - Antibody-Dependent Cell Cytotoxicity
MH  - Enzyme-Linked Immunosorbent Assay
MH  - Flow Cytometry
MH  - Gangliosides/*immunology
MH  - Humans
MH  - Immunization
MH  - Immunoglobulin G/*biosynthesis/immunology
MH  - Melanoma/immunology
MH  - Mice
MH  - Mice, Inbred BALB C
MH  - Rabbits
EDAT- 1998/02/11 00:00
MHDA- 1998/02/11 00:01
CRDT- 1998/02/11 00:00
PHST- 1998/02/11 00:00 [pubmed]
PHST- 1998/02/11 00:01 [medline]
PHST- 1998/02/11 00:00 [entrez]
PST - ppublish
SO  - J Immunother. 1998 Jan;21(1):75-83.

PMID- 1678888
OWN - NLM
STAT- MEDLINE
DCOM- 19910920
LR  - 20171116
IS  - 0885-3177 (Print)
IS  - 0885-3177 (Linking)
VI  - 6
IP  - 4
DP  - 1991 Jul
TI  - Expression of various sialylated carbohydrate antigens in malignant and
      nonmalignant pancreatic tissues.
PG  - 448-58
AB  - The expression of six sialylated carbohydrate antigens (CA19-9, CA-50, SLEX, SLX,
      DU-PAN-2, ST-439) was examined in malignant and nonmalignant pancreatic tissues
      using an immunohistochemical method to elucidate the characteristics of these
      carbohydrate antigens as tumor markers. All carbohydrate antigens except for
      sialyl SSEA-1 (SLX, 52.4%) were expressed in more than 80% of the pancreatic
      cancer. CA19-9 and CA-50, belonging to type I blood group antigens, and DU-PAN-2 
      and ST-439 were localized predominantly in the cytoplasm of cancer cells, while
      sialyl Lex (SLEX) and SLX, belonging to type II blood group antigens, were
      stained mainly on the apical membranes of malignant glands. Although type I
      antigens were expressed in most nonmalignant pancreatic tissues, the type II
      antigens and ST-439 were absent in almost all of the normal tissues and faintly
      expressed in few chronic pancreatitis tissues, suggesting the high tumor
      specificity of these antigens. Each antigen was expressed on the apical surface
      of ducts in normal pancreas. However, in about 30% of chronic pancreatitis cases,
      type I antigens and DU-PAN-2 were observed in the cytoplasm of ductal cells. All 
      patients showing stromal stain, possibly caused by loss of antigen polar
      expression and shedding into the surrounding stroma adjacent to malignant glands,
      revealed high levels of serum antigen. This finding suggests that the stromal
      appearance of antigens is a significant factor in the elevation of serum antigen 
      levels.
FAU - Satomura, Y
AU  - Satomura Y
AD  - Department of Internal Medicine, Kanazawa University, Japan.
FAU - Sawabu, N
AU  - Sawabu N
FAU - Takemori, Y
AU  - Takemori Y
FAU - Ohta, H
AU  - Ohta H
FAU - Watanabe, H
AU  - Watanabe H
FAU - Okai, T
AU  - Okai T
FAU - Watanabe, K
AU  - Watanabe K
FAU - Matsuno, H
AU  - Matsuno H
FAU - Konishi, F
AU  - Konishi F
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Pancreas
JT  - Pancreas
JID - 8608542
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens, Neoplasm)
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (DU-PAN-2 antigen, human)
RN  - 0 (Lewis X Antigen)
RN  - 0 (ST 439 antigen, human)
SB  - IM
MH  - Antibodies, Monoclonal/immunology
MH  - Antigens, Neoplasm/blood/immunology
MH  - Antigens, Tumor-Associated, Carbohydrate/*blood/immunology
MH  - Humans
MH  - Immunohistochemistry
MH  - Lewis X Antigen/blood/immunology
MH  - Pancreas/immunology/*metabolism
MH  - Pancreatic Neoplasms/*blood/immunology
EDAT- 1991/07/01 00:00
MHDA- 1991/07/01 00:01
CRDT- 1991/07/01 00:00
PHST- 1991/07/01 00:00 [pubmed]
PHST- 1991/07/01 00:01 [medline]
PHST- 1991/07/01 00:00 [entrez]
PST - ppublish
SO  - Pancreas. 1991 Jul;6(4):448-58.

PMID- 17708590
OWN - NLM
STAT- MEDLINE
DCOM- 20071113
LR  - 20070917
IS  - 1615-9853 (Print)
IS  - 1615-9853 (Linking)
VI  - 7
IP  - 18
DP  - 2007 Sep
TI  - A serial lectin approach to the mucin-type O-glycoproteome of Drosophila
      melanogaster S2 cells.
PG  - 3264-77
AB  - Identification of mucin-type O-glycosylated proteins with known functions in
      model organisms like Drosophila could provide keys to elucidate functions of the 
      O-glycan moiety and proteomic analyses of O-glycoproteins in higher eukaryotes
      remain a challenge due to structural heterogeneity and a lack of efficient tools 
      for their specific isolation. Here we report a strategy to evaluate the
      O-glycosylation potential of the embryonal hemocyte-like Drosophila Schneider 2
      (S2) cell line by expression of recombinant glycosylation probes derived from
      tandem repeats of the human mucin MUC1 or of the Drosophila salivary gland
      protein Sgs1. We obtained evidence that mucin-type O-glycosylation in S2 cells
      grown under serum-free conditions is restricted to the Tn-antigen
      (GalNAcalpha-Ser/Thr) and the T-antigen (Galbeta1-3GalNAcalpha-Ser/Thr) and this 
      structural homogeneity enables unique glycoproteomic strategies. We present a
      label-free strategy for the isolation, profiling and analysis of O-glycosylated
      proteins consisting of serial lectin affinity capture, 2-DE-based glycoprotein
      analysis by O-glycan specific mAbs and protein identification by MALDI-MS.
      Protein identity and O-glycosylation was confirmed by ESI-MS/MS with detection of
      diagnostic sugar oxonium-ion fragments. Using this strategy, we established 2-D
      reference maps and identified 21 secreted and intracellular mucin-type
      O-glycoproteins. Our results show that Drosophila S2 cells express
      O-glycoproteins involved in a wide range of biological functions including
      proteins of the extracellular matrix (Laminin gamma-chain, Peroxidasin and
      Glutactin), pathogen recognition proteins (Gnbp1), stress response proteins
      (Glycoprotein 93), secreted proteases (Matrix-metalloprotease 1 and various
      trypsin-like serine proteases), protease inhibitors (Serpin 27 A) and proteins of
      unknown function.
FAU - Schwientek, Tilo
AU  - Schwientek T
AD  - Center for Biochemistry, Medical Faculty, University of Cologne, Koln, Germany.
      akd88@uni-koeln.de
FAU - Mandel, Ulla
AU  - Mandel U
FAU - Roth, Udo
AU  - Roth U
FAU - Muller, Stefan
AU  - Muller S
FAU - Hanisch, Franz-Georg
AU  - Hanisch FG
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - Germany
TA  - Proteomics
JT  - Proteomics
JID - 101092707
RN  - 0 (Carbohydrates)
RN  - 0 (Lectins)
RN  - 0 (Mucins)
RN  - 0 (Proteome)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Carbohydrates/*chemistry
MH  - Chromatography, Affinity
MH  - Drosophila melanogaster/*cytology
MH  - Electrophoresis, Gel, Two-Dimensional
MH  - Gas Chromatography-Mass Spectrometry
MH  - Glycosylation
MH  - Lectins/*chemistry
MH  - Molecular Sequence Data
MH  - Mucins/*chemistry
MH  - *Proteome
EDAT- 2007/08/22 09:00
MHDA- 2007/11/14 09:00
CRDT- 2007/08/22 09:00
PHST- 2007/08/22 09:00 [pubmed]
PHST- 2007/11/14 09:00 [medline]
PHST- 2007/08/22 09:00 [entrez]
AID - 10.1002/pmic.200600793 [doi]
PST - ppublish
SO  - Proteomics. 2007 Sep;7(18):3264-77. doi: 10.1002/pmic.200600793.

PMID- 2551493
OWN - NLM
STAT- MEDLINE
DCOM- 19891115
LR  - 20071114
IS  - 0008-5472 (Print)
IS  - 0008-5472 (Linking)
VI  - 49
IP  - 20
DP  - 1989 Oct 15
TI  - Human IgG3 monoclonal antibody directed to an unbranched repeating type 2 chain
      (Gal beta 1----4GlcNAc beta 1----3Gal beta 1----4GlcNAc beta 1----3Gal beta
      1----R) which is highly expressed in colonic and hepatocellular carcinoma.
PG  - 5689-95
AB  - Previously established human monoclonal antibodies (MAbs) directed to
      carbohydrate antigens are essentially all IgM class, and show relatively low
      affinity and low reactivity at 37 degrees C. We report here the establishment of 
      a human IgG3 MAb displaying high affinity antigen-binding activity at 37 degrees 
      C and efficiently activating cellular cytotoxicity directed to human tumor cell
      lines expressing the polylactosamine antigen. The IgG3 MAb (MH21-134) reacted
      with the repeated unbranched polylactosamine structure Gal beta 1----4GlcNAc beta
      1----3Gal beta 1----4GlcNAc beta 1----3Gal beta 1----R, i.e., nLc6, nLc8, etc.,
      but did not react with sialyl 2----3 or 2----6 substituted derivatives at the
      terminal Gal. This specificity differs from that of several anti-i antibodies, or
      human anti-i-like MAbs which react with sialyl 2----3 substituted structures.
      Directly biotinylated MH21-134 antibody was used in immunohistochemical staining 
      of 154 formalin-fixed, paraffin-embedded tissue sections to study distribution of
      the antigen. High incidence of positive staining was found in colon cancer
      (11/17; 65%) and hepatocellular carcinoma (8/12; 67%), followed by large cell and
      squamous cell carcinoma of lung cancer (10/13; 59%, and 14/26; 54%,
      respectively). TLC immunostaining of glycolipid extracts from a variety of tumor 
      tissues showed the presence of nLc6 and/or nLc8 in over 50% of cases. The
      antigens nLc6 and nLc8 were found to be absent from normal colonic epithelia,
      kidney, and pancreas. Only a weak band corresponding to nLc8 and one
      corresponding to nLc6 were found in liver and spleen, although all these normal
      tissues, including gastrointestinal epithelia, lung, liver, spleen, erythrocytes,
      and lymphocytes, were essentially negative on immunohistology. However, the
      antigen was found to be highly expressed in myelocytes and weakly in bronchial
      glands of lung and pancreatic duct epithelia. Nevertheless, expression of
      unsubstituted, unbranched polylactosamine antigen could be an important basis for
      induction of humoral immune response against certain types of human cancer,
      despite its limited expression in normal cells.
FAU - Miyake, M
AU  - Miyake M
AD  - Biomembrane Institute, Seattle, Washington.
FAU - Kohno, N
AU  - Kohno N
FAU - Nudelman, E D
AU  - Nudelman ED
FAU - Hakomori, S
AU  - Hakomori S
LA  - eng
GR  - CA42505/CA/NCI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Cancer Res
JT  - Cancer research
JID - 2984705R
RN  - 0 (Amino Sugars)
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antibodies, Neoplasm)
RN  - 0 (Glycolipids)
RN  - 0 (I Blood-Group System)
RN  - 0 (Polysaccharides)
SB  - IM
MH  - Amino Sugars/*immunology
MH  - Antibodies, Monoclonal/*immunology
MH  - Antibodies, Neoplasm/*immunology
MH  - Antibody Specificity
MH  - Antibody-Dependent Cell Cytotoxicity
MH  - Carbohydrate Sequence
MH  - Carcinoma, Hepatocellular/*immunology
MH  - Colonic Neoplasms/*immunology
MH  - Cytotoxicity, Immunologic
MH  - Glycolipids/*immunology
MH  - Humans
MH  - I Blood-Group System
MH  - Liver Neoplasms/*immunology
MH  - Molecular Sequence Data
MH  - Polysaccharides/*immunology
EDAT- 1989/10/15 00:00
MHDA- 1989/10/15 00:01
CRDT- 1989/10/15 00:00
PHST- 1989/10/15 00:00 [pubmed]
PHST- 1989/10/15 00:01 [medline]
PHST- 1989/10/15 00:00 [entrez]
PST - ppublish
SO  - Cancer Res. 1989 Oct 15;49(20):5689-95.

PMID- 15313217
OWN - NLM
STAT- MEDLINE
DCOM- 20040923
LR  - 20061115
IS  - 0003-9861 (Print)
IS  - 0003-9861 (Linking)
VI  - 429
IP  - 2
DP  - 2004 Sep 15
TI  - ABH blood group antigens in O-glycans of human glycophorin A.
PG  - 145-53
AB  - The major O-linked oligosaccharide structures attached to human glycophorin A
      (GPA) have been extensively characterized previously. Our own recent findings,
      obtained by immunochemical methods, suggested the presence of blood group A and B
      determinants in O-glycans of human glycophorin originating from blood group A or 
      B erythrocytes, respectively. Here, we elucidate the structure of O-glycans,
      isolated from GPA of blood group A, B, and O individuals by reductive
      beta-elimination, carrying A, B or H blood group epitopes, respectively.
      Structural studies based on nanoflow electrospray-ionization tandem mass
      spectrometry and earlier reported data on the carbohydrate moiety of GPA and ABH 
      antigens allowed us to conclude that these blood group epitopes are elongations
      of the beta-GlcNAc branch attached to C-6 of the reducing GalNAc. The galactose
      linked to C-3 of the reducing GalNAc carries NeuAcalpha2-3 linked residue.
      Identified here O-glycans were found in low amounts, their content estimated at
      about one percent of all GPA O-glycans. These O-glycans with type-2 core,
      carrying the blood group A, B or H determinants, have not been identified in GPA 
      so far. Our results demonstrate the efficacy of nanoESI MS/MS in detecting minor 
      oligosaccharide components present in a mixture with much more abundant
      structures.
FAU - Podbielska, Maria
AU  - Podbielska M
AD  - Ludwik Hirszfeld Institute of Immunology and Experimental Therapy, Polish Academy
      of Sciences, 53-114 Wroclaw, Poland.
FAU - Fredriksson, Sten-Ake
AU  - Fredriksson SA
FAU - Nilsson, Bo
AU  - Nilsson B
FAU - Lisowska, Elwira
AU  - Lisowska E
FAU - Krotkiewski, Hubert
AU  - Krotkiewski H
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Arch Biochem Biophys
JT  - Archives of biochemistry and biophysics
JID - 0372430
RN  - 0 (ABO Blood-Group System)
RN  - 0 (Glycophorin)
RN  - 0 (Polysaccharides)
SB  - IM
MH  - ABO Blood-Group System/*immunology
MH  - Blotting, Western
MH  - Carbohydrate Sequence
MH  - Electrophoresis, Polyacrylamide Gel
MH  - Glycophorin/*immunology
MH  - Methylation
MH  - Molecular Sequence Data
MH  - Polysaccharides/*chemistry/immunology
MH  - Spectrometry, Mass, Electrospray Ionization
EDAT- 2004/08/18 05:00
MHDA- 2004/09/24 05:00
CRDT- 2004/08/18 05:00
PHST- 2004/03/26 00:00 [received]
PHST- 2004/06/03 00:00 [revised]
PHST- 2004/08/18 05:00 [pubmed]
PHST- 2004/09/24 05:00 [medline]
PHST- 2004/08/18 05:00 [entrez]
AID - 10.1016/j.abb.2004.06.018 [doi]
AID - S0003-9861(04)00364-9 [pii]
PST - ppublish
SO  - Arch Biochem Biophys. 2004 Sep 15;429(2):145-53. doi: 10.1016/j.abb.2004.06.018.

PMID- 16177266
OWN - NLM
STAT- MEDLINE
DCOM- 20060301
LR  - 20061115
IS  - 0959-6658 (Print)
IS  - 0959-6658 (Linking)
VI  - 16
IP  - 1
DP  - 2006 Jan
TI  - Elucidation of binding specificity of Jacalin toward O-glycosylated peptides:
      quantitative analysis by frontal affinity chromatography.
PG  - 46-53
AB  - Jacalin, a lectin from the jackfruit Artocarpus integrifolia, has been known as a
      valuable tool for specific capturing of O-glycoproteins such as mucins and IgA1. 
      Though its sugar-binding preference for T/Tn-antigens is well established, its
      detailed specificity has not been elucidated. In this study, we prepared a series
      of mucin-type glycopeptides using human glycosyltransferases, that is,
      ST6GalNAc1, Core1Gal-T1 and -T2, beta3Gn-T6, and Core2GnT1, and investigated
      their binding to immobilized Jacalin by frontal affinity chromatography (FAC). As
      a result, consistent with the previous observation, Jacalin showed high affinity 
      for T-antigen (Core1) and Tn-antigen (alpha N-acetylgalactosamine)-attached
      peptides. Furthermore, we here show as novel findings that (1) Jacalin also
      showed significant affinity for Core3 and sialyl-T (ST)-attached peptides, but
      (2) Jacalin could not bind to Core2, Core6, and sialyl-Tn (STn)-attached
      peptides. The results were also confirmed by FAC using p-nitrophenyl
      (pNP)-derivatized saccharides. In conclusion, Jacalin binds to a
      GalNAcalpha1-peptide, in which C6-OH of alphaGalNAc is free (i.e., Core1, Tn,
      Core3, and ST), whereas it cannot recognize a GalNAcalpha1-peptide with a
      substitution at the C6 position (i.e., Core2, Core6, and STn). These findings
      provide useful information when applying jacalin for functional analysis of
      mucin-type glycoproteins and glycopeptides.
FAU - Tachibana, Kouichi
AU  - Tachibana K
AD  - Glycogene Function Team, National Institute of Advanced Industrial Science and
      Technology (AIST), Central-2, 1-1-1 Umezono, Tsukuba, Ibaraki 305-8568, Japan.
FAU - Nakamura, Sachiko
AU  - Nakamura S
FAU - Wang, Han
AU  - Wang H
FAU - Iwasaki, Hiroko
AU  - Iwasaki H
FAU - Tachibana, Kahori
AU  - Tachibana K
FAU - Maebara, Kanako
AU  - Maebara K
FAU - Cheng, Lamei
AU  - Cheng L
FAU - Hirabayashi, J
AU  - Hirabayashi J
FAU - Narimatsu, H
AU  - Narimatsu H
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20050921
PL  - England
TA  - Glycobiology
JT  - Glycobiology
JID - 9104124
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Mucins)
RN  - 0 (Oligopeptides)
RN  - 0 (Plant Lectins)
RN  - 0 (Tn antigen)
RN  - 0 (jacalin)
RN  - EC 2.4.1.- (Glucosyltransferases)
SB  - IM
MH  - Antigens, Tumor-Associated, Carbohydrate/*chemistry/metabolism
MH  - Chromatography, Affinity
MH  - Glucosyltransferases/*chemistry
MH  - Humans
MH  - Mucins/*chemistry/metabolism
MH  - Oligopeptides/*chemistry/metabolism
MH  - Plant Lectins/*chemistry/metabolism
MH  - Protein Binding
MH  - Substrate Specificity
EDAT- 2005/09/24 09:00
MHDA- 2006/03/02 09:00
CRDT- 2005/09/24 09:00
PHST- 2005/09/24 09:00 [pubmed]
PHST- 2006/03/02 09:00 [medline]
PHST- 2005/09/24 09:00 [entrez]
AID - cwj038 [pii]
AID - 10.1093/glycob/cwj038 [doi]
PST - ppublish
SO  - Glycobiology. 2006 Jan;16(1):46-53. doi: 10.1093/glycob/cwj038. Epub 2005 Sep 21.

PMID- 7061953
OWN - NLM
STAT- MEDLINE
DCOM- 19820521
LR  - 20190508
IS  - 0022-1007 (Print)
IS  - 0022-1007 (Linking)
VI  - 155
IP  - 4
DP  - 1982 Apr 1
TI  - GD3, a prominent ganglioside of human melanoma. Detection and characterisation by
      mouse monoclonal antibody.
PG  - 1133-47
AB  - Mouse monoclonal antibody AbR24 has a high degree of specificity for human
      melanoma cells when tested on viable cultured cells using the protein A mixed
      hemagglutinin serological assay. The antigen detected by this antibody has been
      isolated from melanoma cells and shown to be GD3 ganglioside by compositional and
      partial structural analysis and by comparison with authentic GD3 in thin layer
      chromatography (TLC). AbR24 reacts with authentic GD3, but not with any other
      ganglioside tested. Using TLC and reactivity with AbR24, a wide range of cells
      and tissues was examined for the presence of GD3. A new serological assay, termed
      glycolipid-mediated immune adherence, was devised for assaying the reactivity of 
      AbR24 with gangliosides. Melanomas (cultured cells or tumor tissue) were shown to
      have GD3 and GM3 as major gangliosides. Other cells and tissues examined also
      contained GD3, but usually only in low amounts. Melanomas (and MOLT-4, a T cell
      line) were characterized by a simplified ganglioside profile with GD3 and GM3 as 
      major components. The apparent discrepancy between the ubiquitous presence of GD3
      and the serological specificity of AbR24 for melanoma cells can be explained in
      terms of localization and concentration of GD3 in different cells.
FAU - Pukel, C S
AU  - Pukel CS
FAU - Lloyd, K O
AU  - Lloyd KO
FAU - Travassos, L R
AU  - Travassos LR
FAU - Dippold, W G
AU  - Dippold WG
FAU - Oettgen, H F
AU  - Oettgen HF
FAU - Old, L J
AU  - Old LJ
LA  - eng
GR  - CA-08748/CA/NCI NIH HHS/United States
GR  - CA-19765/CA/NCI NIH HHS/United States
GR  - CA-21445/CA/NCI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - J Exp Med
JT  - The Journal of experimental medicine
JID - 2985109R
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens, Neoplasm)
RN  - 0 (Gangliosides)
RN  - 62010-37-1 (ganglioside, GD3)
RN  - EC 3.2.1.18 (Neuraminidase)
SB  - IM
MH  - Animals
MH  - *Antibodies, Monoclonal
MH  - Antigen-Antibody Reactions
MH  - *Antigens, Neoplasm
MH  - Binding, Competitive
MH  - Chromatography, Thin Layer
MH  - Gangliosides/*immunology/isolation & purification
MH  - Hemagglutination Tests
MH  - Humans
MH  - Kinetics
MH  - Melanoma/analysis/*immunology
MH  - Mice
MH  - Mice, Inbred Strains
MH  - Neuraminidase/pharmacology
PMC - PMC2186649
EDAT- 1982/04/01 00:00
MHDA- 1982/04/01 00:01
CRDT- 1982/04/01 00:00
PHST- 1982/04/01 00:00 [pubmed]
PHST- 1982/04/01 00:01 [medline]
PHST- 1982/04/01 00:00 [entrez]
AID - 10.1084/jem.155.4.1133 [doi]
PST - ppublish
SO  - J Exp Med. 1982 Apr 1;155(4):1133-47. doi: 10.1084/jem.155.4.1133.

PMID- 2447219
OWN - NLM
STAT- MEDLINE
DCOM- 19880209
LR  - 20190508
IS  - 0022-1007 (Print)
IS  - 0022-1007 (Linking)
VI  - 167
IP  - 1
DP  - 1988 Jan 1
TI  - Monoclonal antibodies specific for T cell-associated carbohydrate determinants
      react with human blood group antigens CAD and SDA.
PG  - 119-31
AB  - The CT antigenic determinants have previously been shown to be present on the
      T200 glycoproteins and other proteins of murine cytotoxic T cell clones but not
      of T helper clones or nonactivated lymphocytes (1, 2). Two determinants
      recognized by mAbs CT1 and CT2 are also expressed on thymocytes in a
      developmentally regulated fashion during fetal thymus ontogeny and are found in a
      subset of Lyt-2+ intraepithelial lymphocytes in the intestinal mucosa (3-5).
      Previous studies of the biosynthesis of CT+ proteins suggested that these
      determinants were composed of carbohydrate (8). We now demonstrate that the
      anti-CT mAbs react with a carbohydrate determinant at the nonreducing terminus of
      O-linked oligosaccharides that has the configuration GalNAc beta 1,4[SA alpha
      2,3]-galactose. The CT antibodies detected this determinant not only on CTL
      clones but also in the human blood group antigens Cad and Sda+. Variant CTL
      lines, non-Cad erythrocytes, and Sda- glycoproteins that lacked the GalNAc
      residue did not bind the CT mAb. Sialic acid was essential for CT antigen
      expression since neuraminidase or mild periodate treatment abrogated CT antibody 
      binding. In addition, other carbohydrate structures with terminal GalNAc residues
      such as the A or Tn blood group antigens were not recognized. The CT antibodies
      thus define GalNAc and sialic acid containing carbohydrate antigens that are
      expressed on discrete subsets of T lymphocytes and may also be useful reagents
      for the detection of Cad and Sda+ blood group antigens.
FAU - Conzelmann, A
AU  - Conzelmann A
AD  - Institute of Biochemistry, University of Lausanne, Epalinges, Switzerland.
FAU - Lefrancois, L
AU  - Lefrancois L
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - J Exp Med
JT  - The Journal of experimental medicine
JID - 2985109R
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Blood Group Antigens)
RN  - 0 (Carbohydrates)
RN  - 0 (Epitopes)
RN  - 0 (Sialic Acids)
RN  - GZP2782OP0 (N-Acetylneuraminic Acid)
SB  - IM
MH  - Animals
MH  - Antibodies, Monoclonal/*immunology
MH  - Antibody Specificity
MH  - Blood Group Antigens/*immunology
MH  - Carbohydrates/*immunology
MH  - Cross Reactions
MH  - Epitopes/immunology
MH  - Humans
MH  - Mice
MH  - N-Acetylneuraminic Acid
MH  - Sialic Acids/immunology
MH  - T-Lymphocytes, Cytotoxic/*immunology
PMC - PMC2188809
EDAT- 1988/01/01 00:00
MHDA- 1988/01/01 00:01
CRDT- 1988/01/01 00:00
PHST- 1988/01/01 00:00 [pubmed]
PHST- 1988/01/01 00:01 [medline]
PHST- 1988/01/01 00:00 [entrez]
AID - 10.1084/jem.167.1.119 [doi]
PST - ppublish
SO  - J Exp Med. 1988 Jan 1;167(1):119-31. doi: 10.1084/jem.167.1.119.

PMID- 6156167
OWN - NLM
STAT- MEDLINE
DCOM- 19800928
LR  - 20061115
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 255
IP  - 15
DP  - 1980 Aug 10
TI  - Immunological determinants of proteoglycans. Antibodies against the unsaturated
      oligosaccharide products of chondroitinase ABC-digested cartilage proteoglycans.
PG  - 7102-5
AB  - Bovine nasal cartilage proteoglycan monomer which had been digested with
      chondroitinase ABC to form the keratan sulfate-protein core was injected into
      rabbits. High titer antiserum was obtained as judged by the binding of
      125I-labeled keratan sulfate-protein core. Native proteoglycan did not inhibit
      the interaction of the antiserum with labeled keratan sulfate-protein core.
      However, the disaccharide obtained from chondroitin 4-sulfate by the action of
      chondroitinase ABC, 2-acetamido-2-deoxy-3-O-(beta-D-gluco-4-enepyranosyluronic
      acid)-4-O-sulfo-D-galactose, inhibited the interaction 50% at a concentration of 
      500 microM. The corresponding 6-sulfated and nonsulfated disaccharides at the
      same concentration gave 15% and 10% inhibition, respectively.
      Chondroitinase-digested proteoglycan from Swarm rat chondrosarcoma was strongly
      inhibitory, while the hyaluronidase-digested chondrosarcoma proteoglycan
      exhibited no detectable inhibition. Evidently, the antiserum raised against
      chondroitinase ABC-digested bovine nasal cartilage proteoglycan contains
      antibodies which recognize the unsaturated uronic acid residue linked to
      N-acetylgalactosamine 4-sulfate. These antibodies will be valuable for
      identifying and quantitating chondroitin 4-sulfate-containing proteoglycans in
      tissues.
FAU - Christner, J E
AU  - Christner JE
FAU - Caterson, B
AU  - Caterson B
FAU - Baker, J R
AU  - Baker JR
LA  - eng
PT  - Journal Article
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Antibodies)
RN  - 0 (Epitopes)
RN  - 0 (Oligosaccharides)
RN  - 0 (Proteoglycans)
RN  - EC 4.2.2.- (Chondroitin Lyases)
RN  - EC 4.2.2.- (Chondroitinases and Chondroitin Lyases)
SB  - IM
MH  - Animals
MH  - Antibodies
MH  - Cartilage/analysis
MH  - Cattle
MH  - *Chondroitin Lyases
MH  - *Chondroitinases and Chondroitin Lyases
MH  - *Epitopes
MH  - Immunoassay
MH  - Oligosaccharides/*immunology
MH  - Proteoglycans/*immunology
EDAT- 1980/08/10 00:00
MHDA- 1980/08/10 00:01
CRDT- 1980/08/10 00:00
PHST- 1980/08/10 00:00 [pubmed]
PHST- 1980/08/10 00:01 [medline]
PHST- 1980/08/10 00:00 [entrez]
PST - ppublish
SO  - J Biol Chem. 1980 Aug 10;255(15):7102-5.

PMID- 6833281
OWN - NLM
STAT- MEDLINE
DCOM- 19830527
LR  - 20071114
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 258
IP  - 8
DP  - 1983 Apr 25
TI  - Characterization of monoclonal antibodies specific for the Lewis a human blood
      group determinant.
PG  - 4890-4
AB  - Four hybridoma cell lines were derived from the spleen cells of mice immunized
      with the neutral glycolipids of human meconium. The antibodies secreted by these 
      lines were specific for the Lewis a antigen of the human Lewis blood group system
      as determined by solid phase immunoassay using synthetic carbohydrate antigens
      and by plate binding assay and thin layer chromatography-autoradiography using
      natural glycolipid antigens. Coating protein A-bearing Staphylococcus aureus with
      one of the antibodies yielded a stable reagent that produced rapid agglutination 
      of Lewis a positive human erythrocytes. The fine structural specificity of these 
      antibodies was assessed by competition radioimmunoassay using synthetic
      structural analogs of Lewis a conjugated to bovine serum albumin. One antibody
      was specific for the Lewis a trisaccharide (Gal beta 1 leads to 3(Fuc alpha 1
      leads to 4) beta GlcNAc), while a second recognized the entire Lea (1 leads to 3)
      beta Gal tetrasaccharide. The third and fourth were directed at topography
      largely provided by only the alpha Fuc and beta GlcNAc units. These monoclonal
      antibodies not only represent potentially useful reagents for detecting the Lewis
      a antigen but also provide a system for studying precise relationships between
      anticarbohydrate antibody structure and binding specificity.
FAU - Young, W W Jr
AU  - Young WW Jr
FAU - Johnson, H S
AU  - Johnson HS
FAU - Tamura, Y
AU  - Tamura Y
FAU - Karlsson, K A
AU  - Karlsson KA
FAU - Larson, G
AU  - Larson G
FAU - Parker, J M
AU  - Parker JM
FAU - Khare, D P
AU  - Khare DP
FAU - Spohr, U
AU  - Spohr U
FAU - Baker, D A
AU  - Baker DA
FAU - Hindsgaul, O
AU  - Hindsgaul O
FAU - Lemieux, R U
AU  - Lemieux RU
LA  - eng
GR  - 5 S07 RR05431-19/RR/NCRR NIH HHS/United States
GR  - CA29539/CA/NCI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Lewis Blood-Group System)
SB  - IM
MH  - Animals
MH  - Antibodies, Monoclonal/*immunology
MH  - Cell Line
MH  - Chromatography, Thin Layer
MH  - Humans
MH  - Infant, Newborn
MH  - Lewis Blood-Group System/*immunology
MH  - Mice
MH  - Mice, Inbred BALB C
MH  - Rabbits
EDAT- 1983/04/25 00:00
MHDA- 2001/03/28 10:01
CRDT- 1983/04/25 00:00
PHST- 1983/04/25 00:00 [pubmed]
PHST- 2001/03/28 10:01 [medline]
PHST- 1983/04/25 00:00 [entrez]
PST - ppublish
SO  - J Biol Chem. 1983 Apr 25;258(8):4890-4.

PMID- 16033536
OWN - NLM
STAT- MEDLINE
DCOM- 20050920
LR  - 20180822
IS  - 0818-9641 (Print)
IS  - 0818-9641 (Linking)
VI  - 83
IP  - 4
DP  - 2005 Aug
TI  - Immune response to Thomsen-Friedenreich disaccharide and glycan engineering.
PG  - 405-12
AB  - Cancer-associated mucins show frequent alterations of their oligosaccharide chain
      profile, with a switch to unmask normally cryptic O-glycan backbone and core
      regions. Epithelial tumour cells typically show overexpression of the uncovered
      Gal(beta)1-3GalNAc(alpha)-O-Ser/Thr (Core 1) structure, known as the T antigen or
      the Thomsen-Friedenreich antigen, the oligosaccharide chain of which is called
      the Thomsen-Friedenreich disaccharide (TFD). T antigen expression has been
      associated with immunosuppression, metastasis dissemination, and the
      proliferation of cancer cells. Several different strategies have been used to
      trigger a specific immune response to TFD. Natural T antigen and synthetic TFD
      residues have low immunodominance. In the T antigen, flexibility of the
      glycosidic bond reduces the immunogenicity of the sugar residue. Enhanced
      rigidity should favour certain glycan conformations and thereby improve TFD
      immunotargeting. We propose the term 'glycan engineering' for this approach. Such
      engineering of TFD should reduce the flexibility of its glycan moiety and thereby
      enhance its stability, rigidity and immunogenicity.
FAU - Irazoqui, Fernando J
AU  - Irazoqui FJ
AD  - CIQUIBIC-CONICET/Department of Biological Chemistry, Faculty of Chemical
      Sciences, National University of Cordoba, Ciudad Universitaria, Cordoba,
      Argentina. irazoqui@dqb.fcq.unc.edu.ar
FAU - Sendra, Victor G
AU  - Sendra VG
FAU - Lardone, Ricardo D
AU  - Lardone RD
FAU - Nores, Gustavo A
AU  - Nores GA
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Immunol Cell Biol
JT  - Immunology and cell biology
JID - 8706300
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Disaccharides)
RN  - 0 (Polysaccharides)
RN  - 3554-90-3 (Thomsen-Friedenreich antigen)
SB  - IM
MH  - Animals
MH  - Antigens, Tumor-Associated, Carbohydrate/*chemistry/*immunology
MH  - Carbohydrate Conformation
MH  - Disaccharides/*chemistry/*immunology
MH  - *Drug Design
MH  - Neoplasms/chemistry/immunology
MH  - Polysaccharides/biosynthesis/chemical synthesis/*chemistry/*immunology
EDAT- 2005/07/22 09:00
MHDA- 2005/09/21 09:00
CRDT- 2005/07/22 09:00
PHST- 2005/07/22 09:00 [pubmed]
PHST- 2005/09/21 09:00 [medline]
PHST- 2005/07/22 09:00 [entrez]
AID - ICB1348 [pii]
AID - 10.1111/j.1440-1711.2005.01348.x [doi]
PST - ppublish
SO  - Immunol Cell Biol. 2005 Aug;83(4):405-12. doi: 10.1111/j.1440-1711.2005.01348.x.

PMID- 10528213
OWN - NLM
STAT- MEDLINE
DCOM- 19991119
LR  - 20101118
IS  - 0022-1767 (Print)
IS  - 0022-1767 (Linking)
VI  - 163
IP  - 9
DP  - 1999 Nov 1
TI  - L-selectin ligands expressed by human leukocytes are HECA-452 antibody-defined
      carbohydrate epitopes preferentially displayed by P-selectin glycoprotein
      ligand-1.
PG  - 5070-8
AB  - Leukocytes express L-selectin ligands critical for leukocyte-leukocyte
      interactions at sites of inflammation. The predominant leukocyte L-selectin
      ligand is P-selectin glycoprotein ligand-1 (PSGL-1), which displays appropriate
      sialyl Lewis x (sLex)-like carbohydrate determinants for L-selectin recognition. 
      Among the sLex-like determinants expressed by human leukocytes is a unique
      carbohydrate epitope defined by the HECA-452 mAb. The HECA-452 Ag is a critical
      component of L-selectin ligands expressed by vascular endothelial cells. However,
      HECA-452 Ag expression on human leukocyte L-selectin ligands has not been
      assessed. In this study, the HECA-452 mAb blocked 88-99% of neutrophil rolling
      on, or attachment to, adherent cells expressing L-selectin in multiple
      experimental systems. A function-blocking anti-PSGL-1 mAb also inhibited
      L-selectin binding to neutrophils by 89-98%. In addition, the HECA-452 and
      anti-PSGL-1 mAbs blocked the majority of P-selectin binding to neutrophils.
      Western blot analysis revealed that PSGL-1 immunoprecipitated from neutrophils
      displayed HECA-452 mAb-reactive determinants and that PSGL-1 was the predominant 
      scaffold for HECA-452 Ag display. Leukocyte L-selectin ligands also contained
      sulfated determinants since culturing ligand-bearing cells with NaClO3 abrogated 
      L-selectin binding. Consistent with this, human neutrophils expressed mRNA
      encoding five different sulfotransferases associated with the generation of
      selectin ligands: CHST1, CHST2, CHST3, TPST1, and HEC-GlcNAc6ST. Therefore, the
      HECA-452-defined carbohydrate determinant displayed on PSGL-1 represented the
      predominant L-selectin and P-selectin ligand expressed by neutrophils.
FAU - Tu, L
AU  - Tu L
AD  - Department of Immunology, Duke University Medical Center, Durham, NC 27710, USA.
FAU - Murphy, P G
AU  - Murphy PG
FAU - Li, X
AU  - Li X
FAU - Tedder, T F
AU  - Tedder TF
LA  - eng
GR  - CA54464/CA/NCI NIH HHS/United States
GR  - CA81776/CA/NCI NIH HHS/United States
GR  - HL50985/HL/NHLBI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - J Immunol
JT  - Journal of immunology (Baltimore, Md. : 1950)
JID - 2985117R
RN  - 0 (Antibodies, Blocking)
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens, Differentiation, T-Lymphocyte)
RN  - 0 (Antigens, Neoplasm)
RN  - 0 (CTAGE1 protein, human)
RN  - 0 (Carbohydrates)
RN  - 0 (Epitopes)
RN  - 0 (Ligands)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (P-Selectin)
RN  - 0 (P-selectin ligand protein)
RN  - 126880-86-2 (L-Selectin)
RN  - EC 2.4.1.- (Fucosyltransferases)
RN  - EC 2.4.1.152 (galactoside 3-fucosyltransferase)
RN  - EC 2.8.2.- (Sulfotransferases)
SB  - AIM
SB  - IM
MH  - Animals
MH  - Antibodies, Blocking/pharmacology
MH  - Antibodies, Monoclonal/*metabolism/pharmacology
MH  - Antigens, Differentiation, T-Lymphocyte
MH  - Antigens, Neoplasm
MH  - Blood Circulation/immunology/physiology
MH  - COS Cells
MH  - *Carbohydrate Metabolism
MH  - Carbohydrates/immunology
MH  - Cell Movement/immunology/physiology
MH  - Epitopes/*metabolism
MH  - Fucosyltransferases/genetics
MH  - HL-60 Cells
MH  - Humans
MH  - L-Selectin/*biosynthesis/metabolism
MH  - Leukocytes/*metabolism
MH  - Ligands
MH  - Membrane Glycoproteins/immunology/*metabolism
MH  - Mice
MH  - Neutrophils/immunology/metabolism/physiology
MH  - P-Selectin/immunology/*metabolism
MH  - Sulfotransferases/biosynthesis/genetics
MH  - Transfection
EDAT- 1999/10/21 00:00
MHDA- 1999/10/21 00:01
CRDT- 1999/10/21 00:00
PHST- 1999/10/21 00:00 [pubmed]
PHST- 1999/10/21 00:01 [medline]
PHST- 1999/10/21 00:00 [entrez]
AID - ji_v163n9p5070 [pii]
PST - ppublish
SO  - J Immunol. 1999 Nov 1;163(9):5070-8.

PMID- 6194157
OWN - NLM
STAT- MEDLINE
DCOM- 19831123
LR  - 20071114
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 258
IP  - 19
DP  - 1983 Oct 10
TI  - A monoclonal antibody directed to N-acetylneuraminosyl-alpha 2 leads to
      6-galactosyl residue in gangliosides and glycoproteins.
PG  - 11819-22
AB  - A hybridoma cell line producing a monoclonal antibody directed to
      N-acetylneuraminosyl-alpha 2 leads to 6-galactosyl residue has been established. 
      The antibody is IgG2b and reacts only with lacto-series gangliosides as well as
      with glycoproteins having an N-acetylneuraminosyl-alpha 2 leads to 6-galactosyl
      residue, but does not react with gangliosides or glycoproteins having an
      N-acetylneuraminosyl-alpha 2 leads to 3- or -alpha 2 leads to 4-galactosyl
      residue. The antibody is useful for detecting the specific carbohydrate chain
      having this terminal structure by immunostaining of glycolipids separated on thin
      layer chromatography or glycoproteins separated on gel electrophoresis after
      blotting on nitrocellulose sheet. A remarkable accumulation of a few gangliosides
      having this terminal structure has been detected by this monoclonal antibody in
      some human cancer.
FAU - Hakomori, S
AU  - Hakomori S
FAU - Patterson, C M
AU  - Patterson CM
FAU - Nudelman, E
AU  - Nudelman E
FAU - Sekiguchi, K
AU  - Sekiguchi K
LA  - eng
GR  - CA20026/CA/NCI NIH HHS/United States
GR  - GM23100/GM/NIGMS NIH HHS/United States
PT  - Journal Article
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Epitopes)
RN  - 0 (Gangliosides)
RN  - 0 (Glycoproteins)
RN  - 0 (Oligosaccharides)
SB  - IM
MH  - Adenocarcinoma/analysis
MH  - *Antibodies, Monoclonal
MH  - Carbohydrate Conformation
MH  - Carbohydrate Sequence
MH  - Epitopes/*analysis
MH  - Erythrocytes/analysis
MH  - Gangliosides/*immunology
MH  - Glycoproteins/*immunology
MH  - Humans
MH  - Hybridomas/immunology
MH  - Oligosaccharides
MH  - Radioimmunoassay
EDAT- 1983/10/10 00:00
MHDA- 1983/10/10 00:01
CRDT- 1983/10/10 00:00
PHST- 1983/10/10 00:00 [pubmed]
PHST- 1983/10/10 00:01 [medline]
PHST- 1983/10/10 00:00 [entrez]
PST - ppublish
SO  - J Biol Chem. 1983 Oct 10;258(19):11819-22.

PMID- 6194156
OWN - NLM
STAT- MEDLINE
DCOM- 19831123
LR  - 20171116
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 258
IP  - 19
DP  - 1983 Oct 10
TI  - The monoclonal antibody directed to difucosylated type 2 chain (Fuc alpha 1 leads
      to 2Gal beta 1 leads to 4[Fuc alpha 1 leads to 3]GlcNAc; Y Determinant).
PG  - 11793-7
AB  - One of the monoclonal (AH-6) antibodies prepared by hybridoma technique against
      human gastric cancer cell line MKN74 was found to react with a series of
      glycolipids having the Y determinant (Fuc alpha 1 leads to 2Gal beta 1 leads to
      4[Fuc alpha 1 leads to 3]GlcNAc). The structure of one such glycolipid isolated
      from human colonic cancer and from dog intestine was identified as
      lactodifucohexaosyl-ceramide (Fuc alpha 1 leads to 2Gal beta 1 leads to 4[Fuc
      alpha 1 leads to 3]GlcNAc beta 1 leads to 3Gal beta 1 leads to 4Glc beta 1 leads 
      to 1-ceramide; IV3,III3Fuc2nLc4Cer). The hapten glycolipid did not react with
      monoclonal antibodies directed to Lea, Leb, and X-hapten structures, and the AH-6
      antibody did not react with the X-hapten ceramide pentasaccharide (Gal beta 1
      leads to 4[Fuc alpha 1 leads to 3]GlcNAc beta 1 leads to 3Gal beta 1 leads to
      4Glc beta 1 leads to 1-ceramide), H1 glycolipid (Fuc alpha 1 leads to 2Gal beta 1
      leads to 4GlcNAc beta 1 leads to 3Gal beta 1 leads to 4Glc beta 1 leads to
      1-ceramide), nor with glycolipids having the Leb (Fuc alpha 1 leads to 2Gal beta 
      1 leads to 3[Fuc alpha 1 leads 4]GlcNAc beta 1 leads to R) determinant. The
      antibody reacted with blood group O erythrocytes, but not with A erythrocytes.
      Immunostaining of thin layer chromatography with the monoclonal antibody AH-6
      indicated that a series of glycolipids with the Y determinant is present in
      tumors and in O erythrocytes.
FAU - Abe, K
AU  - Abe K
FAU - McKibbin, J M
AU  - McKibbin JM
FAU - Hakomori, S
AU  - Hakomori S
LA  - eng
GR  - CA 20026/CA/NCI NIH HHS/United States
GR  - CA 29495/CA/NCI NIH HHS/United States
GR  - GM 23100/GM/NIGMS NIH HHS/United States
PT  - Journal Article
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Ceramides)
RN  - 0 (Epitopes)
RN  - 0 (Glycolipids)
RN  - 0 (Oligosaccharides)
RN  - 28RYY2IV3F (Fucose)
SB  - IM
MH  - Animals
MH  - *Antibodies, Monoclonal
MH  - Carbohydrate Conformation
MH  - Carbohydrate Sequence
MH  - Cell Line
MH  - Ceramides/analysis
MH  - Epitopes/*analysis
MH  - Fucose/*analysis
MH  - Glycolipids/analysis
MH  - Humans
MH  - Hybridomas/immunology
MH  - Magnetic Resonance Spectroscopy
MH  - Mice
MH  - Oligosaccharides/analysis
MH  - Radioimmunoassay
MH  - Stomach Neoplasms/analysis
EDAT- 1983/10/10 00:00
MHDA- 1983/10/10 00:01
CRDT- 1983/10/10 00:00
PHST- 1983/10/10 00:00 [pubmed]
PHST- 1983/10/10 00:01 [medline]
PHST- 1983/10/10 00:00 [entrez]
PST - ppublish
SO  - J Biol Chem. 1983 Oct 10;258(19):11793-7.

PMID- 9164959
OWN - NLM
STAT- MEDLINE
DCOM- 19970619
LR  - 20171116
IS  - 0022-1767 (Print)
IS  - 0022-1767 (Linking)
VI  - 158
IP  - 11
DP  - 1997 Jun 1
TI  - Role of a sialyl Lewis(x)-like epitope selectively expressed on vascular
      endothelial cells in local skin inflammation of the rat.
PG  - 5384-92
AB  - The role of the inducible L-selectin ligand was studied in complement-dependent
      acute dermatitis in rats. Although mAbs against typical sialyl Lewis(x) (CSLEX-1 
      and SNH-3) did not react with skin venules, a sialyl Lewis(x)-like epitope
      defined by mAb 2H5 (2H5-Ag) was de novo expressed on the endothelial cells of
      skin venules in the area of inflammation. Expression of 2H5-Ag increased
      concomitantly with the progression of inflammation. 2H5-Ag was identified at the 
      75-, 150-, and 180-kDa bands when inflammatory skin tissue was analyzed by
      Western blotting. In contrast, P- and E-selectins were not detectable. The role
      of 2H5-Ag in this model was studied in in vitro and in vivo methods. First, 2H5
      was i.v. injected 15 min before induction of dermatitis. 2H5 bound to skin
      venules and significantly reduced the neutrophil infiltration and plasma protein 
      leakage. In contrast, CSLEX-1, mAb ARP2-4 (P-selectin blocker), or mAb ARE-5
      (E-selectin blocker) had no effects. Second, adhesion of isolated rat neutrophils
      to the inflammatory skin section was inhibited significantly when the sections,
      but not neutrophils, were preincubated with 2H5. Third, fluorescein-labeled
      normal rat neutrophils were injected into a rat 10 h after induction of
      dermatitis. The number of labeled neutrophils infiltrated into the inflammatory
      site was reduced significantly when they were preincubated with HRL-3 (blocking
      mAb against rat L-selectin), but not with 2H5 or HRL-4 (nonblocking mAb against
      rat L-selectin). These data show that de novo expressed 2H5-Ag/L-selectin
      adhesion pathway contributes to the development of acute complement-dependent
      inflammation in the skin.
FAU - Akahori, T
AU  - Akahori T
AD  - The Third Department of Internal Medicine, Nagoya University School of Medicine, 
      Showa-ku, Japan.
FAU - Yuzawa, Y
AU  - Yuzawa Y
FAU - Nishikawa, K
AU  - Nishikawa K
FAU - Tamatani, T
AU  - Tamatani T
FAU - Kannagi, R
AU  - Kannagi R
FAU - Miyasaka, M
AU  - Miyasaka M
FAU - Okada, H
AU  - Okada H
FAU - Hotta, N
AU  - Hotta N
FAU - Matsuo, S
AU  - Matsuo S
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - J Immunol
JT  - Journal of immunology (Baltimore, Md. : 1950)
JID - 2985117R
RN  - 0 (Epitopes)
RN  - 0 (Lewis X Antigen)
RN  - 126880-86-2 (L-Selectin)
SB  - AIM
SB  - IM
MH  - Animals
MH  - Dermatitis/*immunology/pathology
MH  - Endothelium, Vascular/*immunology
MH  - Epitopes/immunology
MH  - Female
MH  - Inflammation/*immunology/pathology
MH  - L-Selectin/immunology
MH  - Lewis X Antigen/*immunology
MH  - Rats
MH  - Rats, Wistar
MH  - Skin/blood supply/immunology/*pathology
EDAT- 1997/06/01 00:00
MHDA- 1997/06/01 00:01
CRDT- 1997/06/01 00:00
PHST- 1997/06/01 00:00 [pubmed]
PHST- 1997/06/01 00:01 [medline]
PHST- 1997/06/01 00:00 [entrez]
PST - ppublish
SO  - J Immunol. 1997 Jun 1;158(11):5384-92.

PMID- 1997178
OWN - NLM
STAT- MEDLINE
DCOM- 19910329
LR  - 20181130
IS  - 0008-5472 (Print)
IS  - 0008-5472 (Linking)
VI  - 51
IP  - 5
DP  - 1991 Mar 1
TI  - Induction of alpha-N-acetylgalactosamine-O-serine/threonine (Tn) antigen-mediated
      cellular immune response for active immunotherapy in mice.
PG  - 1406-11
AB  - A block in carbohydrate chain elongation of O-glycosylated mucins results in
      accumulation of alpha-GalNAc O linked to serine or threonine (Tn antigen) in a
      large percentage of human adenocarcinomas. Immunization of mice with desialylated
      ovine submaxillary mucin (A-OSM), which contains a large concentration of Tn
      antigen, provided protection against challenge of a highly invasive Tn expressing
      syngeneic mouse mammary tumor, TA3-Ha. A similar protective effect was not
      observed in mice immunized with the deglycosylated mucin or irradiated TA3-Ha
      cells. Immunization with A-OSM but not with deglycosylated mucin resulted in high
      anti-Tn antibody response in mice. A-OSM induced in vitro proliferation of
      T-lymphocytes obtained from mice preimmunized with A-OSM or irradiated TA3-Ha
      cells. This antigen-specific T-cell response was significantly lower if
      lymphocytes were stimulated with either the deglycosylated or sialylated form of 
      mucin. A-OSM stimulation induced primarily a CD4+ T-cell population, and these
      cells secreted interleukin 2 in a dose-dependent fashion. A-OSM was also able to 
      induce delayed-type hypersensitivity in mice in response to footpad injections
      with irradiated TA3-Ha cells. These studies indicate that Tn antigen presented on
      a protein backbone is capable of providing cellular immunity and protection
      against tumor in mice.
FAU - Singhal, A
AU  - Singhal A
AD  - Biomembrane Institute, Seattle, Washington 98119.
FAU - Fohn, M
AU  - Fohn M
FAU - Hakomori, S
AU  - Hakomori S
LA  - eng
GR  - CA42505/CA/NCI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Cancer Res
JT  - Cancer research
JID - 2984705R
RN  - 0 (Antibodies)
RN  - 0 (Antigens, Neoplasm)
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Disaccharides)
RN  - 0 (Interleukin-2)
RN  - 0 (Mucins)
RN  - 0 (Tn antigen)
RN  - 3554-90-3 (Thomsen-Friedenreich antigen)
SB  - IM
MH  - Animals
MH  - Antibodies/analysis
MH  - Antigens, Neoplasm/*immunology
MH  - *Antigens, Tumor-Associated, Carbohydrate
MH  - Disaccharides/immunology
MH  - Female
MH  - Hypersensitivity, Delayed
MH  - Immunization
MH  - Immunotherapy
MH  - Interleukin-2/metabolism
MH  - Lymphocyte Activation
MH  - Mice
MH  - Mucins/*immunology
MH  - Neoplasms, Experimental/*prevention & control
MH  - T-Lymphocytes/immunology
EDAT- 1991/03/01 00:00
MHDA- 1991/03/01 00:01
CRDT- 1991/03/01 00:00
PHST- 1991/03/01 00:00 [pubmed]
PHST- 1991/03/01 00:01 [medline]
PHST- 1991/03/01 00:00 [entrez]
PST - ppublish
SO  - Cancer Res. 1991 Mar 1;51(5):1406-11.

PMID- 2563403
OWN - NLM
STAT- MEDLINE
DCOM- 19890317
LR  - 20190510
IS  - 0027-8874 (Print)
IS  - 0027-8874 (Linking)
VI  - 81
IP  - 5
DP  - 1989 Mar 1
TI  - Expression of lacto series type 2 antigens in human renal cell carcinoma and its 
      clinical significance.
PG  - 352-8
AB  - We performed immunohistochemical examination of serial sections of human fetal
      and adult renal tissue as well as human renal carcinoma tissue, using monoclonal 
      antibodies T5A7, 1B2, FH2, FH4, and FH6. These monoclonal antibodies were
      directed to lacto series type 2 antigens with sugar-chain structures:
      lactosylceramide, lactoneotetraosylceramide (paragloboside), Lex (a chemically
      well-defined fucosyl carbohydrate antigen), difucosyl Lex, and sialosyl-difucosyl
      Lex, respectively. The staining pattern in fetal renal tissue changed
      significantly according to the stage of organogenesis. In addition, expression of
      the antigens, especially paragloboside and sialosyl-difucosyl Lex, was closely
      related to the prognosis of the patient. These results suggest that the
      expression of a series of oncofetal antigens in development or differentiation of
      organs is reflected in the reversion to an immature pattern of antigenic
      expression in tumor tissue. The pattern of antigen expression in renal tumors
      offers a good criterion for ascertaining the degree of tumor differentiation and 
      malignancy and is valuable for determining prognosis.
FAU - Fukushi, Y
AU  - Fukushi Y
AD  - Department of Urology, Tohoku University, School of Medicine, Sendai, Japan.
FAU - Ohtani, H
AU  - Ohtani H
FAU - Orikasa, S
AU  - Orikasa S
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - J Natl Cancer Inst
JT  - Journal of the National Cancer Institute
JID - 7503089
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens, CD)
RN  - 0 (Antigens, Neoplasm)
RN  - 0 (Globosides)
RN  - 0 (Glycolipids)
RN  - 0 (Glycosphingolipids)
RN  - 0 (Lactosylceramides)
RN  - 0 (Lewis X Antigen)
RN  - 4682-48-8 (CDw17 antigen)
RN  - 56573-54-7 (paragloboside)
SB  - IM
MH  - Adult
MH  - Antibodies, Monoclonal
MH  - *Antigens, CD
MH  - Antigens, Neoplasm/*analysis
MH  - Carcinoma, Renal Cell/*analysis/mortality
MH  - Embryo, Mammalian/analysis
MH  - Female
MH  - Fetus/analysis
MH  - Globosides/analysis
MH  - Glycolipids/*analysis/immunology
MH  - Glycosphingolipids/analysis
MH  - Humans
MH  - Immunohistochemistry
MH  - Kidney/analysis/embryology
MH  - Kidney Neoplasms/*analysis/mortality
MH  - *Lactosylceramides
MH  - Lewis X Antigen
MH  - Neoplasm Staging
MH  - Pregnancy
MH  - Prognosis
EDAT- 1989/03/01 00:00
MHDA- 1989/03/01 00:01
CRDT- 1989/03/01 00:00
PHST- 1989/03/01 00:00 [pubmed]
PHST- 1989/03/01 00:01 [medline]
PHST- 1989/03/01 00:00 [entrez]
AID - 10.1093/jnci/81.5.352 [doi]
PST - ppublish
SO  - J Natl Cancer Inst. 1989 Mar 1;81(5):352-8. doi: 10.1093/jnci/81.5.352.

PMID- 8262898
OWN - NLM
STAT- MEDLINE
DCOM- 19940126
LR  - 20190512
IS  - 0021-924X (Print)
IS  - 0021-924X (Linking)
VI  - 114
IP  - 2
DP  - 1993 Aug
TI  - Characterization of ganglioside expression in human melanoma cells: immunological
      and biochemical analysis.
PG  - 186-93
AB  - The expression of N-glycolylneuraminic acid (NeuGc)-containing gangliosides in
      human melanoma cells grown both in culture and as xenografts in athymic (nu/nu)
      mice was analyzed extensively with specific mouse monoclonal antibodies (MAbs).
      Three MAbs (GMR8, GMR14, and GMR3) specific for GM3(NeuGc), GM2(NeuGc), and
      GD3(NeuGc-NeuGc-), respectively, were used. Significant differences were observed
      in the ganglioside compositions between the cultured cells in vitro and the
      tumors grown in vivo. The major difference was that the cells cultured in
      serum-free medium did not express any NeuGc-containing gangliosides, whereas
      those grown in nude mice expressed a number of NeuGc-containing gangliosides,
      namely GM3(NeuGc), GM2(NeuGc), GD3(NeuAc-NeuGc-), GD3(NeuGc-NeuAc-), and
      GD3(NeuGc-NeuGc-). The structures of these gangliosides were also determined
      chemically. No activity of CMP-NeuAc hydroxylase was demonstrated either in the
      melanoma cells cultured in vitro or in those grown in nude mice, suggesting that 
      these cells incorporated NeuGc-containing glycoconjugates from the mouse sera and
      converted them to other NeuGc-containing gangliosides. The mouse sera contained
      only GM2(NeuGc), but not the other NeuGc-containing gangliosides or any
      NeuAc-containing gangliosides.
FAU - Kawashima, I
AU  - Kawashima I
AD  - Department of Tumor Immunology, Tokyo Metropolitan Institute of Medical Science, 
      Tokyo.
FAU - Ozawa, H
AU  - Ozawa H
FAU - Kotani, M
AU  - Kotani M
FAU - Suzuki, M
AU  - Suzuki M
FAU - Kawano, T
AU  - Kawano T
FAU - Gomibuchi, M
AU  - Gomibuchi M
FAU - Tai, T
AU  - Tai T
LA  - eng
PT  - Comparative Study
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - J Biochem
JT  - Journal of biochemistry
JID - 0376600
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Gangliosides)
RN  - 0 (Neuraminic Acids)
RN  - 1113-83-3 (N-glycolylneuraminic acid)
RN  - EC 1.- (Mixed Function Oxygenases)
RN  - EC 1.14.18.2 (CMPacetylneuraminate monooxygenase)
SB  - IM
MH  - Animals
MH  - Antibodies, Monoclonal
MH  - Antibody Specificity
MH  - Cell Line
MH  - Chromatography, Thin Layer
MH  - Flow Cytometry
MH  - Fluorescent Antibody Technique
MH  - Gangliosides/analysis/chemistry/immunology/*metabolism
MH  - Humans
MH  - Melanoma/*metabolism
MH  - Mice
MH  - Mice, Nude
MH  - Mixed Function Oxygenases/metabolism
MH  - Neuraminic Acids/*analysis
MH  - Tumor Cells, Cultured
EDAT- 1993/08/01 00:00
MHDA- 1993/08/01 00:01
CRDT- 1993/08/01 00:00
PHST- 1993/08/01 00:00 [pubmed]
PHST- 1993/08/01 00:01 [medline]
PHST- 1993/08/01 00:00 [entrez]
AID - 10.1093/oxfordjournals.jbchem.a124153 [doi]
PST - ppublish
SO  - J Biochem. 1993 Aug;114(2):186-93. doi: 10.1093/oxfordjournals.jbchem.a124153.

PMID- 7537175
OWN - NLM
STAT- MEDLINE
DCOM- 19950530
LR  - 20071114
IS  - 0008-5472 (Print)
IS  - 0008-5472 (Linking)
VI  - 55
IP  - 9
DP  - 1995 May 1
TI  - Tumor-associated sialylated antigens are constitutively expressed in normal human
      colonic mucosa.
PG  - 1869-74
AB  - Immunohistochemical studies have indicated that sialylated carbohydrate antigens 
      such as sialyl-Tn, sialyl-Le(a), and sialyl-Le(x) are expressed in a
      tumor-associated fashion in human colon. Since sialic acid residues are
      O-acetylated more extensively in normal colonic epithelium than in colon cancer
      cells, we examined whether deacetylation of colonic tissues might enable
      monoclonal antibodies to recognize these tumor-associated sialylated antigens. In
      normal colon, deacetylation turned most cases (82%) positive with anti-sialyl-Tn 
      mAb TKH2; and in colon cancers, it increased the number of TKH2-positive cells.
      Sialyl-Le(a) and sialyl-Le(x) detection was also increased after deacetylation of
      normal and malignant colonic tissues so that the frequency of positive cases in
      normal tissues was similar to that in the cancers. However, in the stomach and
      pancreas, the same treatment rarely increased the detection of the sialylated
      epitopes in normal or cancerous tissues. Thus, the same sialylated epitopes can
      be expressed in a tumor-associated fashion by different mechanisms in different
      gastrointestinal organs; in the colon, these antigens are constitutively
      expressed and O-acetylated, whereas in the upper gastrointestinal tract, they are
      rarely O-acetylated, suggesting that other mechanisms such as differences in
      glycosylation account for the cancer-associated expression.
FAU - Ogata, S
AU  - Ogata S
AD  - Department of Medicine, Mount Sinai School of Medicine, New York, New York 10029,
      USA.
FAU - Ho, I
AU  - Ho I
FAU - Chen, A
AU  - Chen A
FAU - Dubois, D
AU  - Dubois D
FAU - Maklansky, J
AU  - Maklansky J
FAU - Singhal, A
AU  - Singhal A
FAU - Hakomori, S
AU  - Hakomori S
FAU - Itzkowitz, S H
AU  - Itzkowitz SH
LA  - eng
GR  - CA52491/CA/NCI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Cancer Res
JT  - Cancer research
JID - 2984705R
RN  - 0
      (5-acetylneuraminyl-(2-3)-galactosyl-(1-4)-(fucopyranosyl-(1-3))-N-acetylglucosam
      ine)
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Epitopes)
RN  - 0 (Gangliosides)
RN  - 0 (Oligosaccharides)
RN  - 0 (di-sialyl Le(a))
RN  - 0 (sialosyl-Tn antigen)
RN  - 91847-18-6 (sialyl Le(a) ganglioside)
SB  - IM
MH  - Adenocarcinoma/chemistry
MH  - Antibodies, Monoclonal
MH  - Antigens, Tumor-Associated, Carbohydrate/*analysis/immunology
MH  - Carbohydrate Sequence
MH  - Colon/*chemistry
MH  - Colonic Neoplasms/chemistry
MH  - Epitopes
MH  - Gangliosides/analysis
MH  - Humans
MH  - Immunohistochemistry
MH  - Intestinal Mucosa/*chemistry
MH  - Molecular Sequence Data
MH  - Oligosaccharides/analysis
MH  - Pancreas/chemistry
MH  - Stomach/chemistry
EDAT- 1995/05/01 00:00
MHDA- 1995/05/01 00:01
CRDT- 1995/05/01 00:00
PHST- 1995/05/01 00:00 [pubmed]
PHST- 1995/05/01 00:01 [medline]
PHST- 1995/05/01 00:00 [entrez]
PST - ppublish
SO  - Cancer Res. 1995 May 1;55(9):1869-74.

PMID- 1726779
OWN - NLM
STAT- MEDLINE
DCOM- 19921201
LR  - 20181113
IS  - 0282-0080 (Print)
IS  - 0282-0080 (Linking)
VI  - 8
IP  - 4
DP  - 1991 Aug
TI  - Concanavalin A-stimulated expression of gangliosides with GalNAc beta 1-4(NeuAc
      alpha 2-3)Gal beta structure in murine thymocytes.
PG  - 354-60
AB  - We analysed the glycolipids of mouse thymocytes before and after Concanavalin A
      (Con A) or recombinant interleukin-2 (rIL-2) stimulation by TLC-immunostaining
      with carbohydrate-specific antiglycolipid antibodies. The thymocytes were
      cultured in serum-free medium in the presence of 500 ng ml-1 Con A, 10 U ml-1
      rIL-2 or Con A plus rIL-2 for 6, 12, 24, 48, and 72 h, and were found to start
      proliferating 24 h after cultivation in the presence of Con A or Con A plus
      rIL-2, the maximum levels being reached at 72 h and 48 h, respectively, in a
      thymidine uptake experiment. The concentrations of II3Neu-Gg4Cer, Gg4Cer and
      IV3GalNAc alpha-Gb4Cer after 48 h Con A stimulation were found to be at almost
      the original levels. Conversely, II3Neu-Gg3Cer, which was not detected in the
      thymocytes at the start, began to appear after 48 h stimulation with Con A and
      Con A plus rIL-2, and IV3Neu-Gg5Cer in the cells 48 h after stimulation with Con 
      A and Con A plus rIL-2 has increased to 41 and 44 times higher than in the
      original cells, respectively, as judged on TLC-immunostaining with monoclonal
      antibody YHD-06, which detects the GalNAc beta 1-4(NeuAc or NeuGc alpha 2-3)Gal
      beta-structure. These results indicate that the increased synthesis of both
      gangliosides, in other words, the activation of
      N-acetylgalactosaminyltransferase, is associated with the mitogen-induced
      proliferation.(ABSTRACT TRUNCATED AT 250 WORDS)
FAU - Horikawa, K
AU  - Horikawa K
AD  - Department of Biochemistry, Faculty of Medicine, University of Tokyo, Japan.
FAU - Yamasaki, M
AU  - Yamasaki M
FAU - Iwamori, M
AU  - Iwamori M
FAU - Nakakuma, H
AU  - Nakakuma H
FAU - Takatsuki, K
AU  - Takatsuki K
FAU - Nagai, Y
AU  - Nagai Y
LA  - eng
PT  - Journal Article
PL  - United States
TA  - Glycoconj J
JT  - Glycoconjugate journal
JID - 8603310
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Epitopes)
RN  - 0 (Gangliosides)
RN  - 0 (Interleukin-2)
RN  - 0 (Recombinant Proteins)
RN  - 11028-71-0 (Concanavalin A)
SB  - IM
MH  - Animals
MH  - Antibodies, Monoclonal
MH  - Antibody Specificity
MH  - Carbohydrate Conformation
MH  - Carbohydrate Sequence
MH  - Cell Division
MH  - Cells, Cultured
MH  - Concanavalin A/*pharmacology
MH  - Epitopes/immunology
MH  - Female
MH  - Flow Cytometry
MH  - Gangliosides/chemistry/immunology/*metabolism
MH  - Immunoenzyme Techniques
MH  - Interleukin-2/pharmacology
MH  - Mice
MH  - Mice, Inbred BALB C
MH  - Molecular Sequence Data
MH  - Molecular Structure
MH  - Recombinant Proteins/pharmacology
MH  - Thymus Gland/cytology/*metabolism
EDAT- 1991/08/01 00:00
MHDA- 1991/08/01 00:01
CRDT- 1991/08/01 00:00
PHST- 1991/08/01 00:00 [pubmed]
PHST- 1991/08/01 00:01 [medline]
PHST- 1991/08/01 00:00 [entrez]
PST - ppublish
SO  - Glycoconj J. 1991 Aug;8(4):354-60.

PMID- 10571017
OWN - NLM
STAT- MEDLINE
DCOM- 19991208
LR  - 20161126
IS  - 0006-3002 (Print)
IS  - 0006-3002 (Linking)
VI  - 1455
IP  - 2-3
DP  - 1999 Oct 8
TI  - Tn-syndrome.
PG  - 255-68
AB  - The idiopathic Tn-syndrome, formerly called 'permanent mixed-field
      polyagglutinability', is a rare hematological disorder characterized by the
      expression of the Tn-antigen on all blood cell lineages. The immunodominant
      epitope of the Tn-antigen is terminal alpha-N-acetylgalactosamine,
      O-glycosidically linked to protein. Normally this residue is 3'-substituted by
      5-galactose thereby forming the core 1 structure known as the
      Thomsen-Friedenreich (TF) antigen (Galbeta1 ==> 3GalNAcalpha1 ==> Thr/Ser). The
      cause of the exposure of the Tn-antigen appears to be due to the silencing of the
      gene expression of beta1,3galactosyltransferase, since treatment of deficient
      Tn(+) lymphocyte T clones with 5'azacytidine or Na butyrate leads to reexpression
      of enzyme activity and the sialylated TF-antigen. The Tn-syndrome is acquired and
      permanent and affects both sexes at any age. Its origin is unknown. Pluripotent
      stem cells are affected since all lineages are involved but each one to a
      variable extent. Therefore, normal cells co-exist with Tn-transformed cells.
      Clinically, patients suffering from the Tn-syndrome appear healthy. Laboratory
      findings usually reveal moderate thrombocyto- and leukopenia and some signs of
      hemolytic anemia not warranting any treatment.
FAU - Berger, E G
AU  - Berger EG
AD  - Institute of Physiology, University of Zurich, Switzerland.
      egberger@physiol.unizh.ch
LA  - eng
PT  - Journal Article
PT  - Review
PL  - Netherlands
TA  - Biochim Biophys Acta
JT  - Biochimica et biophysica acta
JID - 0217513
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens, Neoplasm)
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Lectins)
RN  - 0 (Tn antigen)
RN  - 0 (sialosyl-Tn antigen)
RN  - 3554-90-3 (Thomsen-Friedenreich antigen)
RN  - EC 2.4.1.- (Galactosyltransferases)
RN  - EC 2.4.1.122 (glycoprotein-N-acetylgalactosamine 3-beta-galactosyltransferase)
RN  - M801H13NRU (Azacitidine)
SB  - IM
MH  - Anemia, Hemolytic/immunology
MH  - Antibodies, Monoclonal
MH  - Antigens, Neoplasm/chemistry/immunology
MH  - Antigens, Tumor-Associated, Carbohydrate/chemistry/*immunology
MH  - Azacitidine
MH  - Blood Cells/*immunology
MH  - Erythrocyte Membrane/immunology
MH  - Galactosyltransferases/deficiency
MH  - Hematologic Diseases/enzymology/*immunology/pathology
MH  - Humans
MH  - Lectins
MH  - Leukopenia/immunology
MH  - Molecular Structure
MH  - Syndrome
MH  - Thrombocytopenia/immunology
RF  - 58
EDAT- 1999/11/26 00:00
MHDA- 1999/11/26 00:01
CRDT- 1999/11/26 00:00
PHST- 1999/11/26 00:00 [pubmed]
PHST- 1999/11/26 00:01 [medline]
PHST- 1999/11/26 00:00 [entrez]
AID - S0925-4439(99)00069-1 [pii]
PST - ppublish
SO  - Biochim Biophys Acta. 1999 Oct 8;1455(2-3):255-68.

PMID- 3364985
OWN - NLM
STAT- MEDLINE
DCOM- 19880602
LR  - 20180126
IS  - 0003-9861 (Print)
IS  - 0003-9861 (Linking)
VI  - 262
IP  - 2
DP  - 1988 May 1
TI  - Monoclonal antibodies that bind to galactosylgloboside (SSEA-3 antigen).
PG  - 620-5
AB  - The 3-fucosyllactosamine (3-FL) antigenic determinant, Gal(beta 1-4)[Fuc(alpha
      1-3)]-GlcNAc-R, is very immunogenic in BALB/c mice. A panel of monoclonal
      antibodies was raised against a novel glycosphingolipid that contains a terminal 
      3-FL structure (structure 1): (formula: see text) Surprisingly, most of these
      antibodies reacted with the internal galactosylgloboside structure rather than
      with the terminal 3-FL epitope. The specificities of two of these antibodies, 5A3
      and 8A7, were analyzed by enzyme-linked immunosorbent assay and immunostaining
      procedures, and compared with MC631 (anti-SSEA-3), the only other monoclonal
      antibody known to bind to galactosylgloboside. 5A3 and 8A7 bound equally well to 
      structure 1 and to galactosylgloboside. These antibodies also bound to structure 
      1 from which the terminal galactose, or the galactose and fucose, had been
      removed, but not to globoside or sialylated galactosylgloboside. In contrast,
      MC631 did not bind to structure 1 but, as described previously, did bind to
      globoside and sialylated galactosylgloboside. Galactosylgloboside is a
      developmentally regulated antigen of mouse embryos, human teratocarcinomas, and
      mouse embryonic brain. Antibodies 5A3 and 8A7 will complement MC631 in the
      analysis of the distribution and regulation of galactosylgloboside.
FAU - Marcus, D M
AU  - Marcus DM
AD  - Department of Medicine, Baylor College of Medicine, Houston, Texas 77030.
FAU - Gilbert, S
AU  - Gilbert S
FAU - Sekine, M
AU  - Sekine M
FAU - Suzuki, A
AU  - Suzuki A
LA  - eng
GR  - AI 17712/AI/NIAID NIH HHS/United States
PT  - Comparative Study
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Arch Biochem Biophys
JT  - Archives of biochemistry and biophysics
JID - 0372430
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Carbohydrates)
RN  - 0 (Globosides)
RN  - 0 (Glycosphingolipids)
RN  - 0 (Stage-Specific Embryonic Antigens)
RN  - 0 (stage-specific embryonic antigen-3)
SB  - IM
MH  - Antibodies, Monoclonal/*immunology
MH  - Antibody Specificity
MH  - Antigens, Tumor-Associated, Carbohydrate
MH  - Carbohydrates/analysis
MH  - Globosides/*immunology
MH  - Glycosphingolipids/*immunology
MH  - Stage-Specific Embryonic Antigens
EDAT- 1988/05/01 00:00
MHDA- 1988/05/01 00:01
CRDT- 1988/05/01 00:00
PHST- 1988/05/01 00:00 [pubmed]
PHST- 1988/05/01 00:01 [medline]
PHST- 1988/05/01 00:00 [entrez]
AID - 0003-9861(88)90414-6 [pii]
PST - ppublish
SO  - Arch Biochem Biophys. 1988 May 1;262(2):620-5.

PMID- 7532228
OWN - NLM
STAT- MEDLINE
DCOM- 19950322
LR  - 20190512
IS  - 0027-8874 (Print)
IS  - 0027-8874 (Linking)
VI  - 87
IP  - 6
DP  - 1995 Mar 15
TI  - Alterations in gastric mucin with malignant transformation: novel pathway for
      mucin synthesis.
PG  - 441-6
AB  - BACKGROUND: Mucins are high-molecular-weight glycoproteins produced by both
      normal and cancer cells. However, in cancer cells, abnormal mucins are
      synthesized and potentially can be used as markers for the development and
      progression of certain malignancies. In a previous study, we reported the
      production of a new monoclonal antibody directed against a mucin antigen termed
      F1 alpha, an O-linked oligosaccharide similar to sialyl Tn and
      Thomsen-Friedenreich (T) antigens, that has not been previously detected in human
      cancers. F1 alpha is expressed in a high percentage (80.2%; 89/111) of gastric
      cancers. PURPOSE: In the present study, we compared the expression of F1 alpha
      with that of sialyl Tn and T antigens in human gastric cancer tissues to
      determine how differences in the expression of these cancer-associated antigens
      correlated with the biological properties of cancer cells. METHODS: A total of
      141 cases of gastric cancer were studied. Sections of formalin-fixed,
      paraffin-embedded tissue were immunostained for F1 alpha, sialyl Tn, and T
      antigens. The relationship between the expression of these antigens and the
      patient's clinicopathologic characteristics was studied. The chi-square test
      (two-sided) was used for statistical analyses. RESULTS: F1 alpha was expressed in
      a high percentage of the cases of early to advanced cancers, irrespective of the 
      degree of malignant progression. The rate of expression of sialyl Tn antigen in
      early carcinoma was low, but it increased significantly as depth of invasion
      increased (P < .05) and was significantly higher in patients with hepatic or
      lymph node metastasis than in those without such metastasis (P < .01). Expression
      of T antigen significantly increased with depth of invasion (P < .01) and was
      significantly higher in patients with hepatic metastasis (P < .05), lymph node
      metastasis (P < .05), or peritoneal dissemination (P < .01) than in those without
      such metastasis or dissemination. In consecutive sections of the same specimen,
      the sites of staining for F1 alpha and sialyl Tn antigens seldom coincided. In
      many cases, F1 alpha staining was predominant, but the sialyl Tn-dominant region 
      tended to increase as gastric cancer progressed. Regions of T-antigen staining
      were usually circumscribed by those of F1 alpha staining. CONCLUSION: Our
      findings indicate that the expression of F1 alpha begins almost at the same time 
      as does carcinogenesis in gastric epithelial cells. Moreover, in association with
      progression of gastric carcinoma, synthetic pathways for sialyl Tn antigen and T 
      antigen probably are activated independently.
FAU - Yamashita, Y
AU  - Yamashita Y
AD  - First Department of Surgery, Osaka City University Medical School, Japan.
FAU - Chung, Y S
AU  - Chung YS
FAU - Horie, R
AU  - Horie R
FAU - Kannagi, R
AU  - Kannagi R
FAU - Sowa, M
AU  - Sowa M
LA  - eng
PT  - Comparative Study
PT  - Journal Article
PL  - United States
TA  - J Natl Cancer Inst
JT  - Journal of the National Cancer Institute
JID - 7503089
RN  - 0 (Antigens, Surface)
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Biomarkers, Tumor)
RN  - 0 (F1alpha antigen)
RN  - 0 (Gastric Mucins)
RN  - 0 (Glycoproteins)
RN  - 0 (Mucins)
RN  - 0 (sialosyl-T antigen)
RN  - 0 (sialosyl-Tn antigen)
SB  - IM
MH  - Antigens, Surface/metabolism
MH  - Antigens, Tumor-Associated, Carbohydrate/*metabolism
MH  - Biomarkers, Tumor/metabolism
MH  - Cell Transformation, Neoplastic
MH  - Gastric Mucins/biosynthesis/*metabolism
MH  - Gene Expression Regulation, Neoplastic
MH  - Glycoproteins/*metabolism
MH  - Humans
MH  - Immunohistochemistry
MH  - Liver Neoplasms/secondary
MH  - Lymphatic Metastasis
MH  - Mucins/*metabolism
MH  - Peritoneal Neoplasms/secondary
MH  - Stomach Neoplasms/immunology/*metabolism/pathology
EDAT- 1995/03/15 00:00
MHDA- 1995/03/15 00:01
CRDT- 1995/03/15 00:00
PHST- 1995/03/15 00:00 [pubmed]
PHST- 1995/03/15 00:01 [medline]
PHST- 1995/03/15 00:00 [entrez]
AID - 10.1093/jnci/87.6.441 [doi]
PST - ppublish
SO  - J Natl Cancer Inst. 1995 Mar 15;87(6):441-6. doi: 10.1093/jnci/87.6.441.

PMID- 12946359
OWN - NLM
STAT- MEDLINE
DCOM- 20031010
LR  - 20061115
IS  - 0022-2836 (Print)
IS  - 0022-2836 (Linking)
VI  - 332
IP  - 1
DP  - 2003 Sep 5
TI  - Structural basis of the carbohydrate specificities of jacalin: an X-ray and
      modeling study.
PG  - 217-28
AB  - The structures of the complexes of tetrameric jacalin with Gal, Me-alpha-GalNAc, 
      Me-alpha-T-antigen, GalNAcbeta1-3Gal-alpha-O-Me and Galalpha1-6Glc (mellibiose)
      show that the sugar-binding site of jacalin has three components: the primary
      site, secondary site A, and secondary site B. In these structures and in the two 
      structures reported earlier, Gal or GalNAc occupy the primary site with the
      anomeric carbon pointing towards secondary site A. The alpha-substituents, when
      present, interact, primarily hydrophobically, with secondary site A which has
      variable geometry. O-H..., centered pi and C-H...pi hydrogen bonds involving this
      site also exist. On the other hand, beta-substitution leads to severe steric
      clashes. Therefore, in complexes involving beta-linked disaccharides, the
      reducing sugar binds at the primary site with the non-reducing end located at
      secondary site B. The interactions at secondary site B are primarily through
      water bridges. Thus, the nature of the linkage determines the mode of the
      association of the sugar with jacalin. The interactions observed in the crystal
      structures and modeling based on them provide a satisfactory qualitative
      explanation of the available thermodynamic data on jacalin-carbohydrate
      interactions. They also lead to fresh insights into the nature of the binding of 
      glycoproteins by jacalin.
FAU - Jeyaprakash, A Arockia
AU  - Jeyaprakash AA
AD  - Molecular Biophysics Unit, UGC Centre of Advanced Study, Indian Institute of
      Science, Bangalore 560 012, India.
FAU - Katiyar, S
AU  - Katiyar S
FAU - Swaminathan, C P
AU  - Swaminathan CP
FAU - Sekar, K
AU  - Sekar K
FAU - Surolia, A
AU  - Surolia A
FAU - Vijayan, M
AU  - Vijayan M
LA  - eng
SI  - PDB/1UGW
SI  - PDB/1UGX
SI  - PDB/1UGY
SI  - PDB/1UH0
SI  - PDB/1UH1
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - J Mol Biol
JT  - Journal of molecular biology
JID - 2985088R
RN  - 0 (Adjuvants, Immunologic)
RN  - 0 (Carbohydrates)
RN  - 0 (Plant Lectins)
RN  - 0 (jacalin)
SB  - IM
MH  - Adjuvants, Immunologic/*chemistry/metabolism
MH  - Artocarpus/chemistry
MH  - Binding Sites
MH  - Carbohydrate Metabolism
MH  - Carbohydrates/*chemistry
MH  - Crystallography, X-Ray
MH  - Humans
MH  - Models, Molecular
MH  - Plant Lectins/*chemistry/metabolism
MH  - Protein Binding
MH  - Protein Structure, Secondary
EDAT- 2003/08/30 05:00
MHDA- 2003/10/11 05:00
CRDT- 2003/08/30 05:00
PHST- 2003/08/30 05:00 [pubmed]
PHST- 2003/10/11 05:00 [medline]
PHST- 2003/08/30 05:00 [entrez]
AID - S002228360300901X [pii]
PST - ppublish
SO  - J Mol Biol. 2003 Sep 5;332(1):217-28.

PMID- 7640454
OWN - NLM
STAT- MEDLINE
DCOM- 19950915
LR  - 20181113
IS  - 0941-1291 (Print)
IS  - 0941-1291 (Linking)
VI  - 25
IP  - 3
DP  - 1995
TI  - Characterization of cell surface antigens expressed in the HMA-1 breast cancer
      cell line.
PG  - 244-50
AB  - This report describes the characterization of an estrogen receptor-positive
      breast cancer cell line, HMA-1, established from a breast cancer patient, based
      on the expression of tumor-associated antigens (TAAs), the HLA-DR antigen, and
      the c-erbB-2 proto-oncogene product. In flow cytometric and immunohistochemical
      analyses, HMA-1 was found to express increased levels of several TAAs including
      MUC1, TAG-72 (sialyl Tn), Tn, T, sialyl Le(a), Le(x), and Le(y). HMA-1 also
      expressed enhanced levels of the HLA-DR antigen and c-erbB-2 protein. These
      results indicate that HMA-1 is a unique cell line with abundant TAAs which may
      serve as an appropriate breast cancer cell line for application in the
      multidisciplinary research of breast cancer.
FAU - Ohuchi, N
AU  - Ohuchi N
AD  - Second Department of Surgery, Tohoku University School of Medicine, Sendai,
      Japan.
FAU - Harada, Y
AU  - Harada Y
FAU - Masuko, T
AU  - Masuko T
FAU - Matano, S
AU  - Matano S
FAU - Mori, S
AU  - Mori S
LA  - eng
PT  - Journal Article
PL  - Japan
TA  - Surg Today
JT  - Surgery today
JID - 9204360
RN  - 0 (Antigens, Neoplasm)
RN  - 0 (Antigens, Surface)
RN  - 0 (HLA-DR Antigens)
RN  - 0 (Receptors, Estrogen)
RN  - EC 2.7.10.1 (Receptor, ErbB-2)
SB  - IM
MH  - Amino Acid Sequence
MH  - Antigens, Neoplasm/*analysis
MH  - Antigens, Surface/*analysis
MH  - Breast Neoplasms/*immunology
MH  - Cell Line
MH  - Female
MH  - Flow Cytometry
MH  - HLA-DR Antigens/analysis
MH  - Humans
MH  - Immunohistochemistry
MH  - Middle Aged
MH  - Molecular Sequence Data
MH  - Receptor, ErbB-2/analysis
MH  - Receptors, Estrogen/analysis
MH  - Tumor Cells, Cultured
EDAT- 1995/01/01 00:00
MHDA- 1995/01/01 00:01
CRDT- 1995/01/01 00:00
PHST- 1995/01/01 00:00 [pubmed]
PHST- 1995/01/01 00:01 [medline]
PHST- 1995/01/01 00:00 [entrez]
PST - ppublish
SO  - Surg Today. 1995;25(3):244-50.

PMID- 9857245
OWN - NLM
STAT- MEDLINE
DCOM- 19990323
LR  - 20151119
IS  - 1121-760X (Print)
IS  - 1121-760X (Linking)
VI  - 42
IP  - 3
DP  - 1998
TI  - Immunohistochemical study of Tn, sialosyl-Tn and T antigens in human meningiomas.
PG  - 197-203
AB  - Since an aberrant glycosylation associated with abnormal expression of cell
      surface carbohydrates has been described in many human tumours, we have
      investigated the expression of simple mucintype carbohydrate antigens (Tn,
      sialosyl-Tn and T) in 30 formalin-fixed paraffin-embedded surgical specimens of
      primary meningiomas, subdivided according to the WHO classification as follows:
      18 meningotheliomatous, 7 transitional, 2 angiomatous and 3 anaplastic; in
      addition, 5 meningeal samples taken at autopsy were tested as control. Specific
      monoclonal antibodies (HB-Tn1, HB-STn1 and HB-T1, Dako) were utilized with ABC
      method; the percentage of immunostained cells was graded as follows: O (no
      staining); 1 (> 0 to 5%); 2 (> 5 to 50%); 3 (> 50%). Tn antigen was not expressed
      in any case. Sialosyl-Tn antigen was demonstrated only in cases of anaplastic
      meningiomas (score 1-3). The immunoreactivity for T antigen was found in 2 cases 
      of meningotheliomatous (score 1) and in all the anaplastic meningiomas (score
      1-2). Negative results were obtained with antisera in the control meningeal
      samples. Our results thus document a peculiar expression of sialosyl-Tn and T
      antigens in anaplastic meningiomas, suggesting a block of glycosylation as an
      immunophenotypic finding of malignant transformation. The sporadic immunostaining
      for T antigen encountered in the meningotheliomatous variety may be interpreted
      as an intermediate step of malignant changes.
FAU - Giuffre, G
AU  - Giuffre G
AD  - Department of Human Pathology, University of Messina, Italy.
FAU - Vitarelli, E
AU  - Vitarelli E
FAU - Tuccari, G
AU  - Tuccari G
FAU - Barresi, G
AU  - Barresi G
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - Italy
TA  - Eur J Histochem
JT  - European journal of histochemistry : EJH
JID - 9207930
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Antigens, Viral, Tumor)
RN  - 0 (Biomarkers, Tumor)
RN  - 0 (Mucins)
RN  - 0 (sialosyl-Tn antigen)
RN  - 3554-90-3 (Thomsen-Friedenreich antigen)
SB  - IM
MH  - Antigens, Tumor-Associated, Carbohydrate/*immunology
MH  - Antigens, Viral, Tumor/*immunology
MH  - Biomarkers, Tumor/*immunology
MH  - Humans
MH  - Meningeal Neoplasms/*immunology/pathology
MH  - Meningioma/*immunology/pathology
MH  - Mucins/*immunology
EDAT- 1998/12/19 00:00
MHDA- 1998/12/19 00:01
CRDT- 1998/12/19 00:00
PHST- 1998/12/19 00:00 [pubmed]
PHST- 1998/12/19 00:01 [medline]
PHST- 1998/12/19 00:00 [entrez]
PST - ppublish
SO  - Eur J Histochem. 1998;42(3):197-203.

PMID- 2908846
OWN - NLM
STAT- MEDLINE
DCOM- 19890125
LR  - 20151119
IS  - 0008-5472 (Print)
IS  - 0008-5472 (Linking)
VI  - 49
IP  - 1
DP  - 1989 Jan 1
TI  - Expression of Tn, sialosyl-Tn, and T antigens in human colon cancer.
PG  - 197-204
AB  - Mucin glycoproteins are major secretory products of the colon and contain
      O-linked oligosaccharides synthesized on a polypeptide backbone. The initial step
      in the synthesis of O-linked oligosaccharides is the addition of
      N-acetylgalactosamine to serine or threonine residues forming the Tn antigen.
      This substance can then receive additional carbohydrate residues such as sialic
      acid to form sialosyl-Tn antigen, or galactose to form T antigen. In the colon,
      the T antigen is an oncodevelopmental cancer-associated antigen but little is
      known about Tn and sialosyl-Tn expression. The present comparative
      immunohistochemical study was performed to analyze the expression of these
      antigens in fetal, normal adult, and malignant colorectal tissues with an aim
      toward elucidating whether Tn and sialosyl-Tn are also oncodevelopmental colon
      cancer-associated antigens and to gain insight into the earliest steps of mucin
      glycosylation in colonocytes. We used three reagents to detect Tn antigen (two
      monoclonal antibodies ETn1.01 and CU-1, and one lectin Vicia villosa), two
      reagents to detect sialosyl-Tn (monoclonal antibodies TKH2 and B72.3) and one to 
      detect T antigen (monoclonal antibody AH9-16). Except for occasional reactivity
      with VVA and CU-1, cells of normal colonic mucosa did not express Tn,
      sialosyl-Tn, or T antigens. However, in the transitional mucosa immediately
      adjacent to cancer, all three antigens were expressed (ranging from 35 to 67% of 
      cases depending upon the reagent). In colon cancers, the percentage of cases
      expressing each antigen were as follows: Tn 72-81%, sialosyl-Tn 93-96%, and T
      71%. Unlike T antigen, which was preferentially expressed by moderately well- and
      well-differentiated adenocarcinomas, both Tn and sialosyl-Tn antigens were
      expressed by most histological subsets of colon cancers, including poorly
      differentiated adenocarcinomas and mucinous (colloid and signet ring cell type)
      carcinomas. The majority of cancers expressed both Tn and sialosyl-Tn, usually in
      association with T antigen. Only one cancer lacked all three antigens. Fetal
      colonic mucosal cells expressed all three antigens, particularly in goblet cell
      mucin. These results indicate that like T antigen, Tn and sialosyl-Tn are
      oncodevelopmental cancer-associated antigens in the colon. Moreover, Tn and
      sialosyl-Tn antigens appear to be useful markers of poorly differentiated
      adenocarcinomas and mucinous carcinomas: two histological subsets that often fail
      to express other cancer-associated antigens and that are often associated with a 
      poor clinical outcome.(ABSTRACT TRUNCATED AT 400 WORDS)
FAU - Itzkowitz, S H
AU  - Itzkowitz SH
AD  - Gastrointestinal Research Laboratory, Veterans Administration Medical Center, San
      Francisco, California 94121.
FAU - Yuan, M
AU  - Yuan M
FAU - Montgomery, C K
AU  - Montgomery CK
FAU - Kjeldsen, T
AU  - Kjeldsen T
FAU - Takahashi, H K
AU  - Takahashi HK
FAU - Bigbee, W L
AU  - Bigbee WL
FAU - Kim, Y S
AU  - Kim YS
LA  - eng
GR  - CA42981/CA/NCI NIH HHS/United States
GR  - CA47551/CA/NCI NIH HHS/United States
GR  - FOS TW03783/TW/FIC NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, Non-P.H.S.
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Cancer Res
JT  - Cancer research
JID - 2984705R
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens, Neoplasm)
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Antigens, Viral, Tumor)
RN  - 0 (Tn antigen)
RN  - 0 (sialosyl-Tn antigen)
SB  - IM
MH  - Antibodies, Monoclonal
MH  - Antigens, Neoplasm/*analysis
MH  - *Antigens, Tumor-Associated, Carbohydrate
MH  - Antigens, Viral, Tumor/*analysis
MH  - Colon/immunology
MH  - Colonic Neoplasms/*immunology
MH  - Fetus/immunology
MH  - Glycosylation
MH  - Humans
MH  - Intestinal Mucosa/immunology
EDAT- 1989/01/01 00:00
MHDA- 1989/01/01 00:01
CRDT- 1989/01/01 00:00
PHST- 1989/01/01 00:00 [pubmed]
PHST- 1989/01/01 00:01 [medline]
PHST- 1989/01/01 00:00 [entrez]
PST - ppublish
SO  - Cancer Res. 1989 Jan 1;49(1):197-204.

PMID- 2908845
OWN - NLM
STAT- MEDLINE
DCOM- 19890125
LR  - 20151119
IS  - 0008-5472 (Print)
IS  - 0008-5472 (Linking)
VI  - 49
IP  - 1
DP  - 1989 Jan 1
TI  - Two human monoclonal antibodies reacting with the major gangliosides of human
      melanomas and comparison with corresponding mouse monoclonal antibodies.
PG  - 191-6
AB  - The fine specificity analysis of two human monoclonal antibodies (AbFCM1 and
      AbHJM1) reacting with gangliosides is described and their specificities are
      compared with analogous mouse monoclonal antibodies (mAbs). These two antibodies 
      were generated from lymphocytes of melanoma patients by Epstein-Barr virus
      transformation followed by fusion with mouse myeloma NS-1. Using a wide variety
      of gangliosides, including N-glycolylneuraminic acid (NeuGc)-containing
      compounds, the precise structures recognized by these two antibodies were
      elucidated by enzyme-linked immunosorbent assay and immunostaining of thin-layer 
      chromatograms. AbFCM1 reacted with N-acetylneuraminic acid (NeuAc)-type GM3,
      GD1a, sialylparagloboside, and GT1b in decreasing order of intensity. This
      antibody also reacted with (NeuAc-NeuGc-)-GD3 and -disialylparagloboside, but did
      not react with NeuGc-type GM3, GM2, sialylparagloboside, (NeuGc)2-GD3 and
      -disialylparagloboside. The main epitope structures recognized by AbFCM1 are,
      therefore, NeuAc alpha 2----3Gal beta 1- and NeuAc alpha 2----8NeuGc alpha
      2----Gal beta 1-. These results are similar to the specificity of mouse mAb
      M2590. AbHJM1 reacted with NeuAc-type GD3 and disialylparagloboside, GD2, GD1b,
      GM3, and GT1b, in decreasing order of intensity. Among NeuGc-type gangliosides,
      this antibody reacts with (NeuAc-NeuGc-)-GD3 and -disialylparagloboside, but did 
      not react with gangliosides containing only NeuGc. Consequently the epitope
      structure recognized by AbHJM1 is probably (R)-(NeuAc alpha 2----8Sialic acid
      alpha 2----3)Gal beta 1-. Mouse anti-GD3 mAbR24, in contrast, showed strong
      reactivity only with GD3 and -disialylparagloboside among NeuAc-type
      gangliosides, but showed a similar pattern to AbHJM1 in its reactivity with
      NeuGc-containing gangliosides. Although these two human monoclonal antibodies are
      not highly restricted in their specificities, they reacted best with the major
      gangliosides, GM3 and GD3, present in the majority of human melanomas.
FAU - Furukawa, K
AU  - Furukawa K
AD  - Memorial Sloan-Kettering Cancer Center, New York, New York 10021.
FAU - Yamaguchi, H
AU  - Yamaguchi H
FAU - Oettgen, H F
AU  - Oettgen HF
FAU - Old, L J
AU  - Old LJ
FAU - Lloyd, K O
AU  - Lloyd KO
LA  - eng
GR  - CA 08478/CA/NCI NIH HHS/United States
GR  - CA 47427/CA/NCI NIH HHS/United States
PT  - Comparative Study
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Cancer Res
JT  - Cancer research
JID - 2984705R
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Gangliosides)
SB  - IM
MH  - Animals
MH  - *Antibodies, Monoclonal/immunology
MH  - Antibody Specificity
MH  - Erythrocytes/analysis
MH  - Gangliosides/*analysis/immunology
MH  - Humans
MH  - Melanoma/*analysis
MH  - Mice
MH  - Tumor Cells, Cultured
EDAT- 1989/01/01 00:00
MHDA- 1989/01/01 00:01
CRDT- 1989/01/01 00:00
PHST- 1989/01/01 00:00 [pubmed]
PHST- 1989/01/01 00:01 [medline]
PHST- 1989/01/01 00:00 [entrez]
PST - ppublish
SO  - Cancer Res. 1989 Jan 1;49(1):191-6.

PMID- 242969
OWN - NLM
STAT- MEDLINE
DCOM- 19771229
LR  - 20091111
IS  - 0019-9605 (Print)
IS  - 0019-9605 (Linking)
VI  - 19
IP  - 11
DP  - 1977 Nov
TI  - [Perspective of an expanded role: the abdomen. II].
PG  - 12-7
FAU - Viens, F
AU  - Viens F
FAU - Delisle, C
AU  - Delisle C
LA  - fre
PT  - Journal Article
TT  - Une vision du role elargi: l'abdomen. Deuxieme partie.
PL  - Canada
TA  - Infirm Can
JT  - L' Infirmiere canadienne
JID - 0042116
SB  - N
MH  - *Abdomen
MH  - Auscultation
MH  - Humans
MH  - Nursing Assessment
MH  - Palpation
MH  - Percussion
MH  - *Physical Examination
EDAT- 1977/11/01 00:00
MHDA- 1977/11/01 00:01
CRDT- 1977/11/01 00:00
PHST- 1977/11/01 00:00 [pubmed]
PHST- 1977/11/01 00:01 [medline]
PHST- 1977/11/01 00:00 [entrez]
PST - ppublish
SO  - Infirm Can. 1977 Nov;19(11):12-7.

PMID- 10536039
OWN - NLM
STAT- MEDLINE
DCOM- 20000119
LR  - 20190513
IS  - 0959-6658 (Print)
IS  - 0959-6658 (Linking)
VI  - 9
IP  - 11
DP  - 1999 Nov
TI  - A structural comparison of lipopolysaccharides from two strains of Helicobacter
      pylori, of which one strain (442) does and the other strain (471) does not
      stimulate pepsinogen secretion.
PG  - 1235-45
AB  - Lipopolysaccharides (LPSs) from strains of Helicobacter pylori (442 and 471),
      which differed in stimulation of pepsinogen secretion, were isolated as
      water-soluble material of high-M(r), and as water-insoluble gels of low-M(r).
      Chemical and spectroscopic analyses of soluble LPS and oligosaccharides liberated
      from the gels led to proposed structures with Lewis (Le) antigen termini
      connected to N -acetyllacto-saminoglycans of alternating 3-linked beta-D-Gal and 
      4-linked beta-D-GlcNAc residues with various laterally attached glycosyl
      substituents. The LPS of H.pylori 442 was similar to previously examined strains 
      (NCTC 11637 and P466) in having partially glycosylated chains with alpha-L-Fuc
      units attached to O-3 of the majority of GlcNAc residues in Le(x)units, and in
      chain termination with Le(x)or Le(y)determinants. In contrast, terminal
      Le(y)units occurred in LPS of H.pylori 471 and glycosaminoglycan chains carried a
      smaller proportion of alpha-L-Fuc units, but at O-6 of a majority of
      nonfucosylated GlcNAc residues, there was a novel type of branching with
      alpha-D-Gal substituents. Evidence for the branched regions was obtained
      from(1)H-NMR spectra and from characterization of oligosaccharides formed by the 
      action of endo-beta-galactosidase. Examination of oligosaccharides liberated from
      water-insoluble LPS gels of H.pylori 442 and 471 provided evidence for similar
      core OS structures to those from other H.pylori strains but interesting
      differences were observed.
FAU - Aspinall, G O
AU  - Aspinall GO
AD  - Department of Chemistry, York University, North York, ON M3J 1P3, Canada.
FAU - Mainkar, A S
AU  - Mainkar AS
FAU - Moran, A P
AU  - Moran AP
LA  - eng
PT  - Comparative Study
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - Glycobiology
JT  - Glycobiology
JID - 9104124
RN  - 0 (Antigens, Bacterial)
RN  - 0 (Lewis Blood-Group System)
RN  - 0 (Lipopolysaccharides)
RN  - 0 (O Antigens)
RN  - 0 (Oligosaccharides)
RN  - 9001-10-9 (Pepsinogen A)
SB  - IM
MH  - Antigens, Bacterial/*chemistry/immunology
MH  - Carbohydrate Conformation
MH  - Carbohydrate Sequence
MH  - Duodenal Ulcer/microbiology
MH  - Glycosylation
MH  - Helicobacter Infections/microbiology
MH  - Helicobacter pylori/*chemistry/immunology/isolation & purification
MH  - Humans
MH  - Lewis Blood-Group System/*chemistry
MH  - Lipopolysaccharides/*chemistry/immunology
MH  - Magnetic Resonance Spectroscopy
MH  - Molecular Sequence Data
MH  - Molecular Weight
MH  - O Antigens/*chemistry/immunology
MH  - Oligosaccharides/analysis
MH  - Pepsinogen A/*metabolism
MH  - Secretory Rate/drug effects
MH  - Solubility
MH  - Species Specificity
MH  - Stimulation, Chemical
EDAT- 1999/10/27 00:00
MHDA- 1999/10/27 00:01
CRDT- 1999/10/27 00:00
PHST- 1999/10/27 00:00 [pubmed]
PHST- 1999/10/27 00:01 [medline]
PHST- 1999/10/27 00:00 [entrez]
AID - cwc119 [pii]
AID - 10.1093/glycob/9.11.1235 [doi]
PST - ppublish
SO  - Glycobiology. 1999 Nov;9(11):1235-45. doi: 10.1093/glycob/9.11.1235.

PMID- 7590936
OWN - NLM
STAT- MEDLINE
DCOM- 19951207
LR  - 20180220
IS  - 0165-2478 (Print)
IS  - 0165-2478 (Linking)
VI  - 46
IP  - 1-2
DP  - 1995 May
TI  - Production of human monoclonal antibodies to i blood group by EBV-induced
      transformation: possible presence of a new glycolipid in cord red cell membranes 
      and human hematopoietic cell lines.
PG  - 93-100
AB  - To study the differentiation-associated glycolipid two anti-i mAb producers, GL-1
      and GL-2, were established from the combination of EBV-induced transformation of 
      normal PBL and immune lysis of fluorescent dye-trapped liposome-containing bovine
      i-active glycolipid. The mAb GL-1 reacted with both sialosylparagloboside and
      pentahexosyl ceramide and the bovine i-active glycolipid whereas mAb GL-2 reacted
      only with the bovine i-active glycolipid in LILA. Both mAbs cold-agglutinate
      human cord red cells but not adult red cells. However, unexpectedly, the majority
      of the reactivity of these mAbs in human cord red cells on TLC was not identical 
      to the i-active glycolipid. The GL-1 antigenic substance is considered to be a
      glycolipid distinct from the i-active glycolipid because the immunoreactivity was
      canceled with endoglycoceramidase which cleaves a linkage between the
      oligosaccharide and ceramide. Based on complement cytolysis with the mAb, 15
      hematopoietic cell lines and normal peripheral lymphocytes were screened for
      susceptibility to the mAbs. A Burkitt lymphoma cell line, Ramos, was most
      sensitive among those tested, and BJA-B, Daudi, Namalwa in the B cell lines,
      TALL-1, Jurkatt in the T-cell lines and HL-60 in the non-lymphoid cell lines were
      sensitive whereas normal lymphocytes or other 8 cell lines were not. An
      immunoreactive spot with the same Rf with cord red cells was also detected in
      sensitive cell lines. The possible presence of a new glycolipid antigen
      determined from the mAb and related to the differentiation of hematopoietic cells
      was speculated.
FAU - Nagatsuka, Y
AU  - Nagatsuka Y
AD  - Department of Microbiology, Nihon University School of Medicine, Tokyo, Japan.
FAU - Watarai, S
AU  - Watarai S
FAU - Yasuda, T
AU  - Yasuda T
FAU - Higashi, H
AU  - Higashi H
FAU - Yamagata, T
AU  - Yamagata T
FAU - Ono, Y
AU  - Ono Y
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - Netherlands
TA  - Immunol Lett
JT  - Immunology letters
JID - 7910006
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Glycolipids)
RN  - 0 (I Blood-Group System)
SB  - IM
MH  - Antibodies, Monoclonal/*biosynthesis
MH  - Antibody-Dependent Cell Cytotoxicity
MH  - Carbohydrate Sequence
MH  - Cell Line, Transformed
MH  - Chromatography, Thin Layer
MH  - Erythrocytes/*immunology
MH  - Fetal Blood/*immunology
MH  - Glycolipids/*blood/immunology
MH  - Hematopoietic Stem Cells/*immunology
MH  - Herpesvirus 4, Human/immunology
MH  - Humans
MH  - I Blood-Group System/*immunology
MH  - Molecular Sequence Data
EDAT- 1995/05/01 00:00
MHDA- 1995/05/01 00:01
CRDT- 1995/05/01 00:00
PHST- 1995/05/01 00:00 [pubmed]
PHST- 1995/05/01 00:01 [medline]
PHST- 1995/05/01 00:00 [entrez]
AID - 0165-2478(95)00028-4 [pii]
PST - ppublish
SO  - Immunol Lett. 1995 May;46(1-2):93-100.

PMID- 3566745
OWN - NLM
STAT- MEDLINE
DCOM- 19870427
LR  - 20170913
IS  - 0006-291X (Print)
IS  - 0006-291X (Linking)
VI  - 143
IP  - 2
DP  - 1987 Mar 13
TI  - Predefined gene transfer for expression of a glycosphingolipid antigen by
      transfection with a cosmid genomic library prepared from a cell line in which the
      specific glycosphingolipid is highly expressed.
PG  - 716-22
AB  - The deliberate transfer of globotriaosylceramide (Gb3) expression in mouse
      lymphoma L5178 cells was achieved by transfection with a cosmid DNA library
      prepared from human Burkitt lymphoma Ramos cells in which Gb3 was highly
      expressed. The recipient mouse lymphoma cells did not contain Gb3 but did contain
      its direct precursor, lactosylceramide. The transfected cells expressed Gb3,
      detected both chemically and immunologically, and contained human DNA detected by
      an Alu sequence probe. This model demonstrates a general method for studying
      glycosyltransferase genes and other factors necessary for the expression of
      glycosphingolipid antigens.
FAU - Kojima, H
AU  - Kojima H
FAU - Tsuchiya, S
AU  - Tsuchiya S
FAU - Sekiguchi, K
AU  - Sekiguchi K
FAU - Gelinas, R
AU  - Gelinas R
FAU - Hakomori, S
AU  - Hakomori S
LA  - eng
GR  - AMHL 31232/AM/NIADDK NIH HHS/United States
GR  - OIG CA42505/CA/NCI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Biochem Biophys Res Commun
JT  - Biochemical and biophysical research communications
JID - 0372516
RN  - 0 (Globosides)
RN  - 0 (Glycosphingolipids)
RN  - 0 (Trihexosylceramides)
RN  - 71965-57-6 (globotriaosylceramide)
RN  - EC 2.4.1.- (Hexosyltransferases)
SB  - IM
MH  - Animals
MH  - Burkitt Lymphoma/physiopathology
MH  - Cell Line
MH  - Cloning, Molecular
MH  - Gene Expression Regulation
MH  - Globosides/immunology/*physiology
MH  - Glycosphingolipids/*physiology
MH  - Hexosyltransferases/genetics
MH  - Leukemia L5178/physiopathology
MH  - Mice
MH  - Transfection
MH  - *Trihexosylceramides
EDAT- 1987/03/13 00:00
MHDA- 1987/03/13 00:01
CRDT- 1987/03/13 00:00
PHST- 1987/03/13 00:00 [pubmed]
PHST- 1987/03/13 00:01 [medline]
PHST- 1987/03/13 00:00 [entrez]
AID - 0006-291X(87)91413-6 [pii]
PST - ppublish
SO  - Biochem Biophys Res Commun. 1987 Mar 13;143(2):716-22.

PMID- 3294333
OWN - NLM
STAT- MEDLINE
DCOM- 19880902
LR  - 20190508
IS  - 0022-1007 (Print)
IS  - 0022-1007 (Linking)
VI  - 168
IP  - 1
DP  - 1988 Jul 1
TI  - Human sperm carbohydrate antigens defined by an antisperm human monoclonal
      antibody derived from an infertile woman bearing antisperm antibodies in her
      serum.
PG  - 343-56
AB  - The epitope structure of the human sperm antigen reacting with antibodies present
      in sera of infertile women has been studied using mAb H6-3C4, which produces
      immobilization of human sperm in the presence of complement. Another antibody,
      NUH2, which also induces human sperm immobilization, was used to substantiate the
      presence of a receptor on sperm involved in susceptibility to immobilization.
      Both antibodies defined type 2 chain polylactosamine structure. H6-3C4 is
      directed to internally located repetitive N-acetyllactosamine, i.e., sialyl-i, i,
      or fucosyl-i. NUH2 defines binary alpha 2----3 sialyl type 2 chain, i.e.,
      sialyl-I. Thus, the presence of antibodies in the sera of infertile women
      directed to sperm lactosaminoglycan or lactosaminolipid could be the basis for
      infertility in these cases.
FAU - Tsuji, Y
AU  - Tsuji Y
AD  - Biomembrane Institute, University of Washington, Seattle 98119.
FAU - Clausen, H
AU  - Clausen H
FAU - Nudelman, E
AU  - Nudelman E
FAU - Kaizu, T
AU  - Kaizu T
FAU - Hakomori, S
AU  - Hakomori S
FAU - Isojima, S
AU  - Isojima S
LA  - eng
PT  - Comparative Study
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - J Exp Med
JT  - The Journal of experimental medicine
JID - 2985109R
RN  - 0 (Amino Sugars)
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens)
RN  - 0 (Carbohydrates)
RN  - 3Y5B2K5OOK (N-acetyllactosamine)
RN  - 9007-36-7 (Complement System Proteins)
SB  - IM
MH  - Amino Sugars/immunology
MH  - Antibodies, Monoclonal/*immunology
MH  - Antibody Specificity
MH  - Antigens/*immunology
MH  - Carbohydrate Sequence
MH  - Carbohydrates/*immunology
MH  - Chromatography, Thin Layer
MH  - Complement System Proteins/immunology
MH  - Female
MH  - Fluorescent Antibody Technique
MH  - Hemagglutination
MH  - Humans
MH  - Immunoassay
MH  - Infertility, Female/*immunology
MH  - Male
MH  - Molecular Sequence Data
MH  - Radioimmunoassay
MH  - Sperm Motility
MH  - Spermatozoa/*immunology
PMC - PMC2188971
EDAT- 1988/07/01 00:00
MHDA- 1988/07/01 00:01
CRDT- 1988/07/01 00:00
PHST- 1988/07/01 00:00 [pubmed]
PHST- 1988/07/01 00:01 [medline]
PHST- 1988/07/01 00:00 [entrez]
AID - 10.1084/jem.168.1.343 [doi]
PST - ppublish
SO  - J Exp Med. 1988 Jul 1;168(1):343-56. doi: 10.1084/jem.168.1.343.

PMID- 3169804
OWN - NLM
STAT- MEDLINE
DCOM- 19881123
LR  - 20061115
IS  - 0272-457X (Print)
IS  - 0272-457X (Linking)
VI  - 7
IP  - 4
DP  - 1988 Aug
TI  - Production and characterization of a mouse monoclonal antibody to the glycolipid 
      asialo-GM1.
PG  - 323-31
AB  - The glycosphingolipid asialo-GM1 (aGM1) is a true differentiation antigen of
      murine lymphoid cells. This glycolipid is highly immunogenic in the rabbit, but
      the antisera produced shows some cross reactivity with GM1, the naturally
      occurring sialylated derivative of aGM1. In the present study we examined the
      ability to raise anti-aGM1 antisera in the mouse. We compared the efficiency of
      several immunization methods in various strains of mice. The most effective
      procedure involved repeated intraperitoneal injections of aGM1-cholesterol rich
      particles in the NZB mouse. Hybrid B cell lines were generated by fusion of mouse
      myeloma cells with the splenocytes of an NZB mouse immunized with aGM1. The
      specificity of the antisera produced and of the monoclonal antibody secreted by
      one of these hybridomas (103HT30) was defined by ELISA and by immunostaining on
      thin layer chromatograms. The monoclonal antibody 103HT30 is an IgM. It reacted
      with aGM1 but not with any of the structurally-related ganglioside or neutral
      glycolipids tested. In particular, 103HT30 monoclonal antibody did not present
      any detectable cross-reactivity with GM1.
FAU - Jacquemart, F
AU  - Jacquemart F
AD  - Unite de neurobiologie cellulaire, moleculaire et clinique, INSERM U-134, Hopital
      de la Salpetriere, Paris, France.
FAU - Millot, G
AU  - Millot G
FAU - Goujet-Zalc, C
AU  - Goujet-Zalc C
FAU - Mahouy, G
AU  - Mahouy G
FAU - Zalc, B
AU  - Zalc B
LA  - eng
PT  - Comparative Study
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Hybridoma
JT  - Hybridoma
JID - 8202424
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Glycosphingolipids)
RN  - 37758-47-7 (G(M1) Ganglioside)
RN  - 71012-19-6 (asialo GM1 ganglioside)
SB  - IM
MH  - Animals
MH  - Antibodies, Monoclonal/*biosynthesis
MH  - Cross Reactions
MH  - G(M1) Ganglioside/immunology
MH  - Glycosphingolipids/*immunology
MH  - Immunization/methods
MH  - Kinetics
MH  - Mice
MH  - Mice, Inbred Strains
MH  - Rabbits
MH  - Species Specificity
EDAT- 1988/08/01 00:00
MHDA- 1988/08/01 00:01
CRDT- 1988/08/01 00:00
PHST- 1988/08/01 00:00 [pubmed]
PHST- 1988/08/01 00:01 [medline]
PHST- 1988/08/01 00:00 [entrez]
AID - 10.1089/hyb.1988.7.323 [doi]
PST - ppublish
SO  - Hybridoma. 1988 Aug;7(4):323-31. doi: 10.1089/hyb.1988.7.323.

PMID- 15330211
OWN - NLM
STAT- MEDLINE
DCOM- 20040923
LR  - 20151119
IS  - 0250-7005 (Print)
IS  - 0250-7005 (Linking)
VI  - 24
IP  - 4
DP  - 2004 Jul-Aug
TI  - Differences in prognosis of colorectal cancer patients based on the expression of
      sialyl Lewisa, sialyl Lewisx and sialyl Tn antigens in serum and tumor tissue.
PG  - 2541-6
AB  - PURPOSE: To clarify the differences in prognosis of colorectal cancer patients
      based on the expression of sialyl Lewisaa sialyl Lewisx and sialyl Tn antigens in
      serum and tumor tissue. PATIENTS AND METHODS: Preoperative serum levels (by
      radioimmunoassay) and tumor tissue expression (by immunohistochemistry) of these 
      antigens were simultaneously determined in 52 patients. For each antigen,
      patients were classified into one of four groups: Group S-/T-, S-/T+, S+/T- and
      S+/T+. (S denotes serum, T denotes tumor tissue, and negative and positive
      represent expression). RESULTS: For sialyl Lewisa antigen, the survival time of
      Group S+/T+ was significantly shorter than Group S-/T- or Group S-/T+ (p=0.027 or
      p=0.032, respectively). For sialyl Lewisx antigen, the survival time of Group
      S-/T+ was significantly shorter than Group S-/T- (p=0.048). CONCLUSION: Increased
      expressions of sialyl Lewisa antigen in serum and sialyl Lewisx antigen in tumor 
      tissue may be associated with poor prognosis in colorectal cancer patients.
FAU - Akamine, Shinji
AU  - Akamine S
AD  - First Department of Surgery, Nagasaki University School of Medicine, Nagasaki,
      Japan. shinji@net.nagasaki-u.ac.jp
FAU - Nakagoe, Tohru
AU  - Nakagoe T
FAU - Sawai, Terumitsu
AU  - Sawai T
FAU - Tsuji, Takashi
AU  - Tsuji T
FAU - Tanaka, Kenji
AU  - Tanaka K
FAU - Hidaka, Shigekazu
AU  - Hidaka S
FAU - Shibasaki, Shin-Ichi
AU  - Shibasaki S
FAU - Nanashima, Atsushi
AU  - Nanashima A
FAU - Yamaguchi, Hiroyuki
AU  - Yamaguchi H
FAU - Nagayasu, Takeshi
AU  - Nagayasu T
FAU - Yasutake, Toru
AU  - Yasutake T
LA  - eng
PT  - Comparative Study
PT  - Journal Article
PL  - Greece
TA  - Anticancer Res
JT  - Anticancer research
JID - 8102988
RN  - 0
      (5-acetylneuraminyl-(2-3)-galactosyl-(1-4)-(fucopyranosyl-(1-3))-N-acetylglucosam
      ine)
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Biomarkers, Tumor)
RN  - 0 (Gangliosides)
RN  - 0 (Oligosaccharides)
RN  - 0 (sialosyl-Tn antigen)
RN  - 91847-18-6 (sialyl Le(a) ganglioside)
SB  - IM
MH  - Aged
MH  - Antigens, Tumor-Associated, Carbohydrate/*biosynthesis/blood
MH  - Biomarkers, Tumor/*biosynthesis/blood
MH  - Colorectal Neoplasms/blood/*immunology/pathology/surgery
MH  - Female
MH  - Gangliosides/biosynthesis/blood
MH  - Humans
MH  - Immunohistochemistry
MH  - Male
MH  - Middle Aged
MH  - Oligosaccharides/biosynthesis/blood
MH  - Prognosis
MH  - Radioimmunoassay
MH  - Survival Rate
EDAT- 2004/08/28 05:00
MHDA- 2004/09/24 05:00
CRDT- 2004/08/28 05:00
PHST- 2004/08/28 05:00 [pubmed]
PHST- 2004/09/24 05:00 [medline]
PHST- 2004/08/28 05:00 [entrez]
PST - ppublish
SO  - Anticancer Res. 2004 Jul-Aug;24(4):2541-6.

PMID- 7531419
OWN - NLM
STAT- MEDLINE
DCOM- 19950307
LR  - 20061115
IS  - 0364-5134 (Print)
IS  - 0364-5134 (Linking)
VI  - 37
IP  - 2
DP  - 1995 Feb
TI  - Serum anti-GQ1b IgG antibodies recognize surface epitopes on Campylobacter jejuni
      from patients with Miller Fisher syndrome.
PG  - 260-4
AB  - Three patients who had diarrhea prior to the development of Miller Fisher
      syndrome are presented. Campylobacter jejuni was isolated from stool specimens
      from all patients. High titers of anti-GQ1b IgG antibodies were demonstrated in
      the serum of these patients by enzyme-linked immunosorbent assay and thin-layer
      chromatography overlay. In enzyme-linked immunosorbent assay inhibition studies
      the anti-GQ1b IgG antibodies bound specifically to whole bacteria of the Miller
      Fisher syndrome-associated C. jejuni strains. The presence of anti-GQ1b IgG
      binding epitopes on the surface of the C. jejuni from the patients was not
      exclusively associated with a specific Penner serotype. It is suggested that
      anti-GQ1b antibodies are formed during the initial infection that elicits Miller 
      Fisher syndrome. The cross-reactivity of anti-GQ1b IgG antibodies with surface
      epitopes on Miller Fisher syndrome-associated C. jejuni strains supports the
      hypothesis of molecular mimicry between bacteria and neural tissue.
FAU - Jacobs, B C
AU  - Jacobs BC
AD  - Department of Neurology, University Hospital Dijkzigt, The Netherlands.
FAU - Endtz, H
AU  - Endtz H
FAU - van der Meche, F G
AU  - van der Meche FG
FAU - Hazenberg, M P
AU  - Hazenberg MP
FAU - Achtereekte, H A
AU  - Achtereekte HA
FAU - van Doorn, P A
AU  - van Doorn PA
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Ann Neurol
JT  - Annals of neurology
JID - 7707449
RN  - 0 (Epitopes)
RN  - 0 (Gangliosides)
RN  - 0 (Immunoglobulin G)
RN  - 68652-37-9 (GQ1b ganglioside)
SB  - IM
MH  - Adult
MH  - Ataxia/immunology/*microbiology
MH  - Campylobacter Infections/immunology
MH  - Campylobacter jejuni/*immunology
MH  - Diarrhea/immunology/*microbiology
MH  - Epitopes
MH  - Gangliosides/*immunology
MH  - Humans
MH  - Immunoglobulin G/*blood
MH  - Male
MH  - Molecular Mimicry
MH  - Ophthalmoplegia/immunology/*microbiology
MH  - Syndrome
EDAT- 1995/02/01 00:00
MHDA- 1995/02/01 00:01
CRDT- 1995/02/01 00:00
PHST- 1995/02/01 00:00 [pubmed]
PHST- 1995/02/01 00:01 [medline]
PHST- 1995/02/01 00:00 [entrez]
AID - 10.1002/ana.410370218 [doi]
PST - ppublish
SO  - Ann Neurol. 1995 Feb;37(2):260-4. doi: 10.1002/ana.410370218.

PMID- 15121843
OWN - NLM
STAT- MEDLINE
DCOM- 20040617
LR  - 20190509
IS  - 0270-7306 (Print)
IS  - 0270-7306 (Linking)
VI  - 24
IP  - 10
DP  - 2004 May
TI  - Normal embryonic and germ cell development in mice lacking alpha
      1,3-fucosyltransferase IX (Fut9) which show disappearance of stage-specific
      embryonic antigen 1.
PG  - 4221-8
AB  - Stage-specific embryonic antigen 1 (SSEA-1), an antigenic epitope defined as a
      Lewis x carbohydrate structure, is expressed during the 8-cell to blastocyst
      stages in mouse embryos and in primordial germ cells, undifferentiated embryonic 
      stem cells, and embryonic carcinoma cells. For many years, SSEA-1 has been
      implicated in the development of mouse embryos as a functional carbohydrate
      epitope in cell-to-cell interaction during morula compaction. In a previous
      study, alpha 1,3-fucosyltransferase IX (Fut9) exhibited very strong activity for 
      the synthesis of Lewis x compared to other alpha 1,3-fucosyltransferases in an in
      vitro substrate specificity assay. Fut4 and Fut9 transcripts were expressed in
      mouse embryos. The Fut9 transcript was detected in embryonic-day-13.5 gonads
      containing primordial germ cells, but the Fut4 transcript was not. In order to
      identify the role of SSEA-1 and determine the key enzyme for SSEA-1 synthesis in 
      vivo, we have generated Fut9-deficient (Fut9(-/-)) mice. Fut9(-/-) mice develop
      normally, with no gross phenotypic abnormalities, and are fertile.
      Immunohistochemical analysis revealed an absence of SSEA-1 expression in early
      embryos and primordial germ cells of Fut9(-/-) mice. Therefore, we conclude that 
      expression of the SSEA-1 epitope in the developing mouse embryo is not essential 
      for embryogenesis in vivo.
FAU - Kudo, Takashi
AU  - Kudo T
AD  - Glycogene Function Team, Research Center for Glycoscience, National Institute of 
      Advanced Industrial Science and Technology, Open Space Laboratory, Tsukuba,
      Ibaraki 305-8568, Japan.
FAU - Kaneko, Mika
AU  - Kaneko M
FAU - Iwasaki, Hiroko
AU  - Iwasaki H
FAU - Togayachi, Akira
AU  - Togayachi A
FAU - Nishihara, Shoko
AU  - Nishihara S
FAU - Abe, Kuniya
AU  - Abe K
FAU - Narimatsu, Hisashi
AU  - Narimatsu H
LA  - eng
SI  - GENBANK/AB015426
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Mol Cell Biol
JT  - Molecular and cellular biology
JID - 8109087
RN  - 0 (DNA, Complementary)
RN  - 0 (Isoenzymes)
RN  - 0 (Lewis X Antigen)
RN  - EC 2.4.1.- (Fucosyltransferases)
RN  - EC 2.4.1.152 (galactoside 3-fucosyltransferase)
SB  - IM
MH  - Animals
MH  - Base Sequence
MH  - Blastocyst/immunology
MH  - Chromosome Mapping
MH  - DNA, Complementary/genetics
MH  - Embryonic and Fetal Development
MH  - Female
MH  - Fucosyltransferases/*deficiency/genetics
MH  - Gene Expression Regulation, Developmental
MH  - Gene Expression Regulation, Enzymologic
MH  - Germ Cells/enzymology/immunology
MH  - In Vitro Techniques
MH  - Isoenzymes/deficiency/genetics
MH  - Lewis X Antigen/*metabolism
MH  - Mice
MH  - Mice, Inbred C57BL
MH  - Mice, Knockout
MH  - Molecular Sequence Data
MH  - Pregnancy
PMC - PMC400454
EDAT- 2004/05/04 05:00
MHDA- 2004/06/18 05:00
CRDT- 2004/05/04 05:00
PHST- 2004/05/04 05:00 [pubmed]
PHST- 2004/06/18 05:00 [medline]
PHST- 2004/05/04 05:00 [entrez]
AID - 10.1128/mcb.24.10.4221-4228.2004 [doi]
PST - ppublish
SO  - Mol Cell Biol. 2004 May;24(10):4221-8. doi: 10.1128/mcb.24.10.4221-4228.2004.

PMID- 8883420
OWN - NLM
STAT- MEDLINE
DCOM- 19961122
LR  - 20190515
IS  - 0007-0920 (Print)
IS  - 0007-0920 (Linking)
VI  - 74
IP  - 8
DP  - 1996 Oct
TI  - A randomised phase II study of sialyl-Tn and DETOX-B adjuvant with or without
      cyclophosphamide pretreatment for the active specific immunotherapy of breast
      cancer.
PG  - 1292-6
AB  - Studies in animal models of mouse mammary carcinoma have shown that ovine
      submaxillary mucin, which carries multiple sialyl-Tn (STn) epitopes, is effective
      in stimulating an immune response and inhibiting tumour growth. In similar
      studies using carbohydrate antigens, pretreatment with low-dose cyclophosphamide 
      has been shown to be important in modulating the immune response to antigen
      possibly by inhibiting suppresser T-cell activity. In a clinical trial assessing 
      the efficacy and toxicity of synthetic STn, patients with metastatic breast
      cancer were randomised to receive 100 micrograms STn linked to keyhole limpet
      haemocyanin (KLH) with DETOX-B adjuvant given by subcutaneous injection at weeks 
      0, 2, 5 and 9 with or without low-dose cyclophosphamide (CTX, 300 mg m-2)
      pretreatment, 3 days before the start of immunotherapy. Patients with responding 
      or stable disease after the first four injections were eligible to receive
      STn-KLH at 4 week intervals. The main toxicity noted was the development of
      subcutaneous granulomata at injection sites. Of 23 patients randomised, 18
      received four injections, 5 patients having developed progressive disease during 
      the initial 12 week period. Two minor responses were noted in the 18 patients who
      received four active specific immunotherapy (ASI) injections and a further five
      patients had stable disease. Six patients continued ASI at 4 week intervals and a
      partial response was noted in a patient who had previously had stable disease.
      All patients developed IgG and IgM responses to sialyl-Tn and levels of IgM
      antibodies were significantly higher in those patients who were pretreated with
      CTX. Measurable tumour responses have been recorded following ASI with STn-KLH
      plus DETOX and the immunomodulatory properties of low-dose CTX have been
      confirmed.
FAU - Miles, D W
AU  - Miles DW
AD  - ICRF Clinical Oncology Unit, Guy's Hospital, London.
FAU - Towlson, K E
AU  - Towlson KE
FAU - Graham, R
AU  - Graham R
FAU - Reddish, M
AU  - Reddish M
FAU - Longenecker, B M
AU  - Longenecker BM
FAU - Taylor-Papadimitriou, J
AU  - Taylor-Papadimitriou J
FAU - Rubens, R D
AU  - Rubens RD
LA  - eng
PT  - Clinical Trial
PT  - Clinical Trial, Phase II
PT  - Journal Article
PT  - Randomized Controlled Trial
PL  - England
TA  - Br J Cancer
JT  - British journal of cancer
JID - 0370635
RN  - 0 (Adjuvants, Immunologic)
RN  - 0 (Antibodies, Neoplasm)
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Immunoconjugates)
RN  - 0 (Immunoglobulin G)
RN  - 0 (Immunoglobulin M)
RN  - 0 (sialosyl-Tn antigen)
RN  - 8N3DW7272P (Cyclophosphamide)
RN  - 9013-72-3 (Hemocyanins)
RN  - FV4Y0JO2CX (keyhole-limpet hemocyanin)
SB  - IM
MH  - Adjuvants, Immunologic/*therapeutic use
MH  - Adult
MH  - Aged
MH  - Antibodies, Neoplasm/biosynthesis/blood
MH  - Antigens, Tumor-Associated, Carbohydrate/*therapeutic use
MH  - Breast Neoplasms/blood/drug therapy/*therapy
MH  - Chemotherapy, Adjuvant
MH  - Combined Modality Therapy
MH  - Cyclophosphamide/*therapeutic use
MH  - Dose-Response Relationship, Drug
MH  - Female
MH  - Hemocyanins/*therapeutic use
MH  - Humans
MH  - Immunoconjugates/*therapeutic use
MH  - Immunoglobulin G/biosynthesis/blood
MH  - Immunoglobulin M/biosynthesis/blood
MH  - *Immunotherapy, Active
MH  - Middle Aged
MH  - Sensitivity and Specificity
PMC - PMC2075933
EDAT- 1996/10/01 00:00
MHDA- 1996/10/01 00:01
CRDT- 1996/10/01 00:00
PHST- 1996/10/01 00:00 [pubmed]
PHST- 1996/10/01 00:01 [medline]
PHST- 1996/10/01 00:00 [entrez]
AID - 10.1038/bjc.1996.532 [doi]
PST - ppublish
SO  - Br J Cancer. 1996 Oct;74(8):1292-6. doi: 10.1038/bjc.1996.532.

PMID- 16525726
OWN - NLM
STAT- MEDLINE
DCOM- 20060807
LR  - 20131121
IS  - 1107-3756 (Print)
IS  - 1107-3756 (Linking)
VI  - 17
IP  - 4
DP  - 2006 Apr
TI  - The influence of N- and O-glycosylation inhibitors on the glycosylation profile
      of cellular membrane proteins and adhesive properties of carcinoma cell lines.
PG  - 669-74
AB  - The effects of N- and O-glycosylation inhibitors on the expression of membrane
      proteins (MUC1 and some integrins) were evaluated in human endometrial (Ishikawa)
      and breast (MCF-7) cancer cells. Subconfluent cells were treated with 1-3 mg%
      concentration of tunicamycin and 2-10 mM of benzyl-N-acetyl-alpha-galactosaminide
      for 1-2 days, and used for flow cytometry, immunohistochemical staining, adhesion
      test and Western blotting. Benzyl-N-acetyl-alpha-galactosaminide inhibits MUC1
      expression on the surface of breast more than endometrial cancer cells.
      Tunicamycin reduces MUC1 concentration on the cellular surface more than
      benzylglycoside, and greatly reduces glycosylation of glycoproteins, causing an
      increase in cell adhesion in both types of cancer cells. The expression of
      alpha2beta1 integrins on the surface of these cells was weak and decreased after 
      treatment with inhibitors. Two different glycoforms of MUC1 proteins in
      endometrial cells and three in breast cancer cells were expressed and their
      molecular weights were reduced after treatment with glycosylation inhibitors. It 
      was confirmed with lectin detection of carbohydrate epitopes (Tn and T) in MUC1
      proteins. These observations show that glycosylation inhibitors altered the N-
      and O-glycan patterns in a sufficient manner, and positively modified the
      biological features of cancer cells.
FAU - Paszkiewicz-Gadek, Anna
AU  - Paszkiewicz-Gadek A
AD  - Department of Medical Chemistry, Medical University of Bialystok, 15-230
      Bialystok, Poland. zachemog@amb.edu.pl
FAU - Porowska, Halina
AU  - Porowska H
FAU - Lemancewicz, Dorota
AU  - Lemancewicz D
FAU - Wolczynski, Slawomir
AU  - Wolczynski S
FAU - Gindzienski, Andrzej
AU  - Gindzienski A
LA  - eng
PT  - Journal Article
PL  - Greece
TA  - Int J Mol Med
JT  - International journal of molecular medicine
JID - 9810955
RN  - 0 (1-benzyl-2-acetamido-2-galactopyranoside)
RN  - 0 (Antigens, Neoplasm)
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Collagen Type I)
RN  - 0 (Integrin alpha2beta1)
RN  - 0 (MUC1 protein, human)
RN  - 0 (Membrane Proteins)
RN  - 0 (Mucin-1)
RN  - 0 (Mucins)
RN  - 0 (Tn antigen)
RN  - 11089-65-9 (Tunicamycin)
RN  - 3554-90-3 (Thomsen-Friedenreich antigen)
RN  - X2RN3Q8DNE (Galactose)
SB  - IM
MH  - Antigens, Neoplasm/metabolism
MH  - Antigens, Tumor-Associated, Carbohydrate/metabolism
MH  - Blotting, Western
MH  - Breast Neoplasms/*metabolism/pathology
MH  - Cell Adhesion/drug effects
MH  - Cell Line, Tumor
MH  - Collagen Type I/metabolism
MH  - Endometrial Neoplasms/*metabolism/pathology
MH  - Female
MH  - Flow Cytometry
MH  - Galactose/analogs & derivatives/pharmacology
MH  - Glycosylation/drug effects
MH  - Humans
MH  - Integrin alpha2beta1/metabolism
MH  - Membrane Proteins/*metabolism
MH  - Mucin-1
MH  - Mucins/metabolism
MH  - Protein Binding/drug effects
MH  - Tunicamycin/pharmacology
EDAT- 2006/03/10 09:00
MHDA- 2006/08/08 09:00
CRDT- 2006/03/10 09:00
PHST- 2006/03/10 09:00 [pubmed]
PHST- 2006/08/08 09:00 [medline]
PHST- 2006/03/10 09:00 [entrez]
PST - ppublish
SO  - Int J Mol Med. 2006 Apr;17(4):669-74.

PMID- 7526777
OWN - NLM
STAT- MEDLINE
DCOM- 19941213
LR  - 20061115
IS  - 0364-5134 (Print)
IS  - 0364-5134 (Linking)
VI  - 36
IP  - 5
DP  - 1994 Nov
TI  - Molecular mimicry between GQ1b ganglioside and lipopolysaccharides of
      Campylobacter jejuni isolated from patients with Fisher's syndrome.
PG  - 791-3
AB  - We isolated Campylobacter jejuni from 2 patients with Fisher's syndrome
      subsequent to enteritis. Crude lipopolysaccharide fractions were extracted from
      the bacteria and separated by thin-layer chromatography. Monoclonal antibodies to
      GQ1b ganglioside (GMR13 and 7F5) reacted with both lipopolysaccharide fractions, 
      indicating that the lipopolysaccharides bear the GQ1b epitope. This is the first 
      report of molecular mimicry between neural tissue components and the antecedent
      infectious agents of Fisher's syndrome.
FAU - Yuki, N
AU  - Yuki N
AD  - Department of Neurology, Tokyo Medical and Dental University, Japan.
FAU - Taki, T
AU  - Taki T
FAU - Takahashi, M
AU  - Takahashi M
FAU - Saito, K
AU  - Saito K
FAU - Yoshino, H
AU  - Yoshino H
FAU - Tai, T
AU  - Tai T
FAU - Handa, S
AU  - Handa S
FAU - Miyatake, T
AU  - Miyatake T
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Ann Neurol
JT  - Annals of neurology
JID - 7707449
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Epitopes)
RN  - 0 (Gangliosides)
RN  - 0 (Lipopolysaccharides)
RN  - 68652-37-9 (GQ1b ganglioside)
SB  - IM
MH  - Antibodies, Monoclonal
MH  - Campylobacter Infections/*immunology
MH  - Campylobacter jejuni/*immunology/isolation & purification
MH  - Cerebellar Ataxia/*immunology/microbiology
MH  - Chromatography, Thin Layer
MH  - Epitopes
MH  - Gangliosides/*immunology
MH  - Humans
MH  - Lipopolysaccharides/*immunology
MH  - Male
MH  - *Molecular Mimicry
MH  - Ophthalmoplegia/immunology/microbiology
MH  - Syndrome
EDAT- 1994/11/01 00:00
MHDA- 1994/11/01 00:01
CRDT- 1994/11/01 00:00
PHST- 1994/11/01 00:00 [pubmed]
PHST- 1994/11/01 00:01 [medline]
PHST- 1994/11/01 00:00 [entrez]
AID - 10.1002/ana.410360517 [doi]
PST - ppublish
SO  - Ann Neurol. 1994 Nov;36(5):791-3. doi: 10.1002/ana.410360517.

PMID- 17892882
OWN - NLM
STAT- MEDLINE
DCOM- 20080819
LR  - 20080215
IS  - 0020-7519 (Print)
IS  - 0020-7519 (Linking)
VI  - 38
IP  - 3-4
DP  - 2008 Mar
TI  - Mucin-type O-glycosylation in Mesocestoides vogae (syn. corti).
PG  - 265-76
AB  - Protein glycosylation is an important post-translational modification underlying 
      host-parasite interactions, which may determine the outcome of infection.
      Although Mesocestoides vogae represents an important model for investigating the 
      various aspects of cestode biology, virtually no information is available about
      the structure and synthesis of glycans in this parasite. In this work, focused on
      the initiation pathway of mucin-type O-glycosylation in M. vogae, we
      characterized O-glycoproteins bearing the simple mucin-type cancer-associated Tn 
      and sialyl-Tn antigens, and the expression and activity of ppGalNAc-T, the key
      enzyme responsible for the first step of mucin-type O-glycosylation. Using
      immunohistochemistry, Tn and sialyl-Tn antigens were detected mainly in the
      tegument (microtriches) and in parenchymal cells. Tn expression was also observed
      in lateral nerve cords. Both Tn and sialyl-Tn antigens were detected in in vitro 
      cultured parasites. Based on their electrophoretic mobility, Tn- and
      sialyl-Tn-bearing glycoproteins from M. vogae were separated into several
      components of 22 to 60 kDa. The observation that Tn and sialyl-Tn glycoproteins
      remained in the 0.6N perchloric acid-soluble fraction suggested that they could
      be good candidates for characterizing mucin-type glycosylation in this parasite. 
      O-glycoproteins were purified and initially characterized using a proteomic
      approach. Immunohistochemical analysis of the tissue distribution of ppGalNAc-T
      revealed that this enzyme is expressed in the sub-tegumental region and in the
      parenchyma of the parasite. In M. vogae cultured in vitro, ppGalNAc-T was mainly 
      detected in the suckers. Using a panel of 8 acceptor substrate synthetic
      peptides, we found that M. vogae ppGalNAc-T preferentially glycosylate threonine 
      residues, the best substrates being peptides derived from human mucin MUC1 and
      from Trypanosoma cruzi mucin. These results suggest that M. vogae might represent
      a useful model to study O-glycosylation, and provide new research avenues for
      future studies on the glycopathobiology of helminth parasites.
FAU - Medeiros, Andrea
AU  - Medeiros A
AD  - Departamento de Bioquimica, Facultad de Medicina, Universidad de la Republica,
      Montevideo, Uruguay.
FAU - Chiribao, Maria Laura
AU  - Chiribao ML
FAU - Ubillos, Luis
AU  - Ubillos L
FAU - Festari, Maria Florencia
AU  - Festari MF
FAU - Saldana, Jenny
AU  - Saldana J
FAU - Robello, Carlos
AU  - Robello C
FAU - Dominguez, Laura
AU  - Dominguez L
FAU - Calvete, Juan Jose
AU  - Calvete JJ
FAU - Osinaga, Eduardo
AU  - Osinaga E
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20070814
PL  - England
TA  - Int J Parasitol
JT  - International journal for parasitology
JID - 0314024
RN  - 0 (Antigens, Helminth)
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Mucins)
RN  - 0 (Tn antigen)
RN  - 0 (sialosyl-Tn antigen)
RN  - EC 2.4.1.- (N-Acetylgalactosaminyltransferases)
RN  - EC 2.4.1.41 (polypeptide N-acetylgalactosaminyltransferase)
SB  - IM
MH  - Animals
MH  - Antigens, Helminth/analysis/*metabolism
MH  - Antigens, Tumor-Associated, Carbohydrate/metabolism
MH  - Blotting, Western
MH  - Carbohydrate Sequence
MH  - Cestode Infections/metabolism
MH  - Electrophoresis, Polyacrylamide Gel
MH  - Glycosylation
MH  - Host-Parasite Interactions
MH  - Immunohistochemistry
MH  - Mesocestoides/chemistry/*metabolism
MH  - Mice
MH  - Mice, Inbred Strains
MH  - Mucins/metabolism
MH  - N-Acetylgalactosaminyltransferases/analysis
MH  - Parasitology/methods
EDAT- 2007/09/26 09:00
MHDA- 2008/08/20 09:00
CRDT- 2007/09/26 09:00
PHST- 2007/06/03 00:00 [received]
PHST- 2007/07/13 00:00 [revised]
PHST- 2007/07/27 00:00 [accepted]
PHST- 2007/09/26 09:00 [pubmed]
PHST- 2008/08/20 09:00 [medline]
PHST- 2007/09/26 09:00 [entrez]
AID - S0020-7519(07)00288-3 [pii]
AID - 10.1016/j.ijpara.2007.07.015 [doi]
PST - ppublish
SO  - Int J Parasitol. 2008 Mar;38(3-4):265-76. doi: 10.1016/j.ijpara.2007.07.015. Epub
      2007 Aug 14.

PMID- 8161226
OWN - NLM
STAT- MEDLINE
DCOM- 19940518
LR  - 20061115
IS  - 0003-9861 (Print)
IS  - 0003-9861 (Linking)
VI  - 310
IP  - 1
DP  - 1994 Apr
TI  - Generation of one set of murine monoclonal antibodies specific for globo-series
      glycolipids: evidence for differential distribution of the glycolipids in rat
      small intestine.
PG  - 89-96
AB  - We generated four murine monoclonal antibodies (MAbs) specific for globo-series
      glycolipids by immunizing C3H/HeN mice with these purified glycolipids adsorbed
      to Salmonella minnesota followed by fusion with mouse myeloma cells. By use of a 
      wide variety of glycolipids, the precise structures recognized by these MAbs were
      elucidated through an enzyme-linked immunosorbent assay and an immunostaining on 
      thin-layer chromatography. These four MAbs, designated as BGR23, BGR47, BMR26,
      and BGR27, exhibited highly restricted binding specificities, reacting only with 
      the globo-series glycolipids Gb3Cer, III3Gal alpha-Gb3Cer, Gb4Cer, and IV3GalNAc 
      alpha-Gb4Cer, respectively, which were used for immunization. None of the other
      various glycolipids or gangliosides were recognized. We determined the
      localization of these globo-series glycolipids in adult rat small intestine by
      means of an immunofluorescence technique with these MAbs. Our study revealed that
      there is a differential distribution of these glycolipids in the rat tissue.
      III3Gal alpha-Gb3Cer was demonstrated on the cryptic cells and circular muscle,
      whereas Gb4Cer was localized on both the circular and longitudinal muscles. The
      expression of Gb3Cer was associated with the epithelium and the capillary
      endothelial cells in the lamina propria mucosae as well as with the tunica
      submucosa, whereas IV3GalNAc alpha-Gb4Cer was detected on the epithelium,
      capillary endothelial cells in the lamina propria mucosae, and both the muscle
      layers.
FAU - Kotani, M
AU  - Kotani M
AD  - Department of Tumor Immunology, Tokyo Metropolitan Institute of Medical Science, 
      Japan.
FAU - Kawashima, I
AU  - Kawashima I
FAU - Ozawa, H
AU  - Ozawa H
FAU - Ogura, K
AU  - Ogura K
FAU - Ariga, T
AU  - Ariga T
FAU - Tai, T
AU  - Tai T
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Arch Biochem Biophys
JT  - Archives of biochemistry and biophysics
JID - 0372430
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Globosides)
RN  - 0 (Trihexosylceramides)
RN  - 11034-93-8 (globotetraosylceramide)
RN  - 71965-57-6 (globotriaosylceramide)
SB  - IM
MH  - Animals
MH  - *Antibodies, Monoclonal
MH  - Antibody Specificity
MH  - Carbohydrate Sequence
MH  - Chromatography, Thin Layer
MH  - Enzyme-Linked Immunosorbent Assay
MH  - Globosides/*immunology/*isolation & purification
MH  - Immunohistochemistry
MH  - Intestine, Small/*chemistry/cytology
MH  - Mice
MH  - Mice, Inbred C3H
MH  - Molecular Sequence Data
MH  - Rats
MH  - Trihexosylceramides/immunology
EDAT- 1994/04/01 00:00
MHDA- 1994/04/01 00:01
CRDT- 1994/04/01 00:00
PHST- 1994/04/01 00:00 [pubmed]
PHST- 1994/04/01 00:01 [medline]
PHST- 1994/04/01 00:00 [entrez]
AID - S0003-9861(84)71144-1 [pii]
AID - 10.1006/abbi.1994.1144 [doi]
PST - ppublish
SO  - Arch Biochem Biophys. 1994 Apr;310(1):89-96. doi: 10.1006/abbi.1994.1144.

PMID- 9182286
OWN - NLM
STAT- MEDLINE
DCOM- 19970611
LR  - 20151119
IS  - 0344-0338 (Print)
IS  - 0344-0338 (Linking)
VI  - 192
IP  - 12
DP  - 1996 Dec
TI  - Expression of sialyl-Tn in breast cancer. Correlation with prognostic parameters.
PG  - 1181-6
AB  - To investigate the expression of a simple mucin-type carbohydrate antigen
      (Sialyl-Tn/STn) and its putative relationship with established or potentially
      useful clinico-pathologic prognostic parameters in breast cancer, we studied
      forty-six cases of invasive breast carcinoma in formalin-fixed, paraffin-embedded
      tissue sections. STn antigen was detected by the HB-STn antibody using an
      avidin-biotin-peroxidase method. The parameters studied were tumour size,
      histologic grade, nodal status, proliferative index (with MIB-1), ER expression, 
      ploidy, c-erbB-2 and p53 expression. STn expression was observed in 18 cases
      (39%) of breast cancer. The expression of STn was associated with axillary node
      metastasis, ER negativity and c-erbB-2 expression. A tendency towards an
      association between STn immunoreactivity and high histologic grade was also
      found. No correlation was observed between STn immunoreactivity and age, tumour
      size, proliferative index, ploidy and p53 expression. We conclude that the
      detection of STn immunoreactivity may be useful for predicting the likelihood of 
      lymph node metastasis and that the outcome of patients with breast cancer should 
      be further investigated in order to find whether or not the data of the present
      study are confirmed in larger series.
FAU - Soares, R
AU  - Soares R
AD  - Unit of Molecular Pathology, IPATIMUP, Porto Medical School, Portugal.
FAU - Marinho, A
AU  - Marinho A
FAU - Schmitt, F
AU  - Schmitt F
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - Germany
TA  - Pathol Res Pract
JT  - Pathology, research and practice
JID - 7806109
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Biomarkers, Tumor)
RN  - 0 (Receptors, Estrogen)
RN  - 0 (sialosyl-Tn antigen)
SB  - IM
MH  - Adult
MH  - Aged
MH  - Antigens, Tumor-Associated, Carbohydrate/*metabolism
MH  - Biomarkers, Tumor/*metabolism
MH  - Breast Neoplasms/diagnosis/*metabolism
MH  - Carcinoma, Ductal, Breast/diagnosis/metabolism
MH  - Genes, erbB-2/physiology
MH  - Humans
MH  - Immunohistochemistry
MH  - Middle Aged
MH  - Prognosis
MH  - Receptors, Estrogen/metabolism
EDAT- 1996/12/01 00:00
MHDA- 1996/12/01 00:01
CRDT- 1996/12/01 00:00
PHST- 1996/12/01 00:00 [pubmed]
PHST- 1996/12/01 00:01 [medline]
PHST- 1996/12/01 00:00 [entrez]
AID - S0344-0338(96)80148-8 [pii]
AID - 10.1016/S0344-0338(96)80148-8 [doi]
PST - ppublish
SO  - Pathol Res Pract. 1996 Dec;192(12):1181-6. doi: 10.1016/S0344-0338(96)80148-8.

PMID- 16239964
OWN - NLM
STAT- MEDLINE
DCOM- 20060203
LR  - 20181113
IS  - 0021-9738 (Print)
IS  - 0021-9738 (Linking)
VI  - 115
IP  - 11
DP  - 2005 Nov
TI  - Lewis X component in human milk binds DC-SIGN and inhibits HIV-1 transfer to CD4+
      T lymphocytes.
PG  - 3256-64
AB  - DC-specific ICAM3-grabbing non-integrin (DC-SIGN), which is expressed on DCs, can
      interact with a variety of pathogens such as HIV-1, hepatitis C, Ebola,
      cytomegalovirus, Dengue virus, Mycobacterium, Leishmania, and Candida albicans.
      We demonstrate that human milk can inhibit the DC-SIGN-mediated transfer of HIV-1
      to CD4+ T lymphocytes as well as viral transfer by both immature and mature DCs. 
      The inhibitory factor directly interacted with DC-SIGN and prevented the HIV-1
      gp120 envelope protein from binding to the receptor. The human milk proteins
      lactoferrin, alpha-lactalbumin, lysozyme, beta-casein, and secretory leukocyte
      protease inhibitor did not bind DC-SIGN or demonstrate inhibition of viral
      transfer. The inhibitory effect could be fully alleviated with an Ab recognizing 
      the Lewis X (LeX) sugar epitope, commonly found in human milk. LeX in polymeric
      form or conjugated to protein could mimic the inhibitory activity, whereas free
      LeX sugar epitopes could not. We reveal that a LeX motif present in human milk
      can bind to DC-SIGN and thereby prevent the capture and subsequent transfer of
      HIV-1 to CD4+ T lymphocytes. The presence of such a DC-SIGN-binding molecule in
      human milk may both influence antigenic presentation and interfere with pathogen 
      transfer in breastfed infants.
FAU - Naarding, Marloes A
AU  - Naarding MA
AD  - Department of Human Retrovirology, Academic Medical Center, University of
      Amsterdam, Amsterdam, The Netherlands.
FAU - Ludwig, Irene S
AU  - Ludwig IS
FAU - Groot, Fedde
AU  - Groot F
FAU - Berkhout, Ben
AU  - Berkhout B
FAU - Geijtenbeek, Teunis B H
AU  - Geijtenbeek TB
FAU - Pollakis, Georgios
AU  - Pollakis G
FAU - Paxton, William A
AU  - Paxton WA
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20051020
PL  - United States
TA  - J Clin Invest
JT  - The Journal of clinical investigation
JID - 7802877
RN  - 0 (Cell Adhesion Molecules)
RN  - 0 (DC-specific ICAM-3 grabbing nonintegrin)
RN  - 0 (Lectins, C-Type)
RN  - 0 (Lewis X Antigen)
RN  - 0 (Receptors, Cell Surface)
RN  - 0 (Trisaccharides)
RN  - 0 (galactosyl-(1,4)-fucopyranosyl-(1,3)-N-acetylglucosamine)
SB  - AIM
SB  - IM
MH  - CD4-Positive T-Lymphocytes/immunology/*virology
MH  - Cell Adhesion Molecules/*metabolism/physiology
MH  - Cell Line, Tumor
MH  - Cells, Cultured
MH  - Dendritic Cells/immunology/virology
MH  - Female
MH  - HIV Infections/*immunology/*prevention & control/transmission
MH  - HIV-1/*immunology
MH  - Humans
MH  - Infectious Disease Transmission, Vertical
MH  - Lectins, C-Type/*metabolism/physiology
MH  - Lewis X Antigen/*metabolism/physiology
MH  - Milk, Human/*immunology/*metabolism
MH  - Protein Binding/immunology
MH  - Receptors, Cell Surface/*metabolism/physiology
MH  - Trisaccharides/*metabolism/physiology
PMC - PMC1257537
EDAT- 2005/10/22 09:00
MHDA- 2006/02/04 09:00
CRDT- 2005/10/22 09:00
PHST- 2005/03/22 00:00 [received]
PHST- 2005/08/23 00:00 [accepted]
PHST- 2005/10/22 09:00 [pubmed]
PHST- 2006/02/04 09:00 [medline]
PHST- 2005/10/22 09:00 [entrez]
AID - 10.1172/JCI25105 [doi]
PST - ppublish
SO  - J Clin Invest. 2005 Nov;115(11):3256-64. doi: 10.1172/JCI25105. Epub 2005 Oct 20.

PMID- 10993897
OWN - NLM
STAT- MEDLINE
DCOM- 20010201
LR  - 20161025
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 275
IP  - 51
DP  - 2000 Dec 22
TI  - Expression cloning of human globoside synthase cDNAs. Identification of beta
      3Gal-T3 as UDP-N-acetylgalactosamine:globotriaosylceramide beta
      1,3-N-acetylgalactosaminyltransferase.
PG  - 40498-503
AB  - By using a eukaryocytic cell expression cloning system, we have isolated cDNAs of
      the globoside synthase (beta1, 3-N-acetylgalactosaminyltransferase) gene. Mouse
      fibroblast L cells transfected with SV40 large T antigen and previously cloned
      Gb3/CD77 synthase cDNAs were co-transfected with a cDNA library prepared from
      mRNA from human kidney together with Forssman synthase cDNA, and Forssman
      antigen-positive cells were panned using an anti-Forssman monoclonal antibody.
      The isolated cDNAs contained a single open reading frame predicting a type II
      membrane protein with 351 amino acids. Surprisingly, the cDNA clones turned out
      to be identical with previously reported beta3Gal-T3, which had been cloned by
      sequence homology with other galactosyltransferases. Substrate specificity
      analysis with extracts from cDNA-transfected L cells confirmed that the gene
      product was actually beta1, 3-N-acetylgalactosaminyltransferase that specifically
      catalyzes the transfer of N-acetylgalactosamine onto globotriaosylceramide.
      Results of TLC immunostaining of neutral glycolipids from the cDNA-transfected
      cells also supported the identity of the newly synthesized component as
      globoside. The results show that glycosyltransferases apparently belonging to a
      single glycosyltransferase family do not necessarily catalyze reactions utilizing
      the same acceptor or even the same sugar donor. The globoside synthase gene was
      expressed in many tissues, such as heart, brain, testis, etc. We propose the
      designation beta3GalNAc-T1 for the cloned globoside synthase gene.
FAU - Okajima, T
AU  - Okajima T
AD  - Department of Biochemistry II, Nagoya University School of Medicine, 65 Tsurumai,
      Nagoya 466-0065, the Japanese Red Cross Central Blood Center, Hiroo 4-1-31,
      Shibuya-ku, Tokyo 150, Japan.
FAU - Nakamura, Y
AU  - Nakamura Y
FAU - Uchikawa, M
AU  - Uchikawa M
FAU - Haslam, D B
AU  - Haslam DB
FAU - Numata, S I
AU  - Numata SI
FAU - Furukawa, K
AU  - Furukawa K
FAU - Urano, T
AU  - Urano T
FAU - Furukawa, K
AU  - Furukawa K
LA  - eng
GR  - R29 AI042817/AI/NIAID NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (DNA, Complementary)
RN  - EC 2.4.1.- (N-Acetylgalactosaminyltransferases)
RN  - EC 2.4.1.41 (polypeptide N-acetylgalactosaminyltransferase)
SB  - IM
MH  - Amino Acid Sequence
MH  - Carbohydrate Sequence
MH  - Cloning, Molecular
MH  - DNA, Complementary
MH  - Molecular Sequence Data
MH  - N-Acetylgalactosaminyltransferases/chemistry/*genetics/metabolism
MH  - Sequence Homology, Amino Acid
MH  - Transfection
EDAT- 2000/09/20 11:00
MHDA- 2001/02/28 10:01
CRDT- 2000/09/20 11:00
PHST- 2000/09/20 11:00 [pubmed]
PHST- 2001/02/28 10:01 [medline]
PHST- 2000/09/20 11:00 [entrez]
AID - 10.1074/jbc.M006902200 [doi]
AID - M006902200 [pii]
PST - ppublish
SO  - J Biol Chem. 2000 Dec 22;275(51):40498-503. doi: 10.1074/jbc.M006902200.

PMID- 12851687
OWN - NLM
STAT- MEDLINE
DCOM- 20040304
LR  - 20081121
IS  - 1019-6439 (Print)
IS  - 1019-6439 (Linking)
VI  - 23
IP  - 2
DP  - 2003 Aug
TI  - Expansion of natural killer cells in mice transgenic for IgM antibody to
      ganglioside GD2: demonstration of prolonged survival after challenge with
      syngeneic tumor cells.
PG  - 381-8
AB  - IgM antibodies to gangliosides, sialic acid-containing glycosphingolipids, have
      been shown to mediate anti-tumor effects in cancer patients with melanoma and
      neuroblastoma and to correlate with survival. Mechanisms by which the antibodies 
      induce tumor suppression, however, have not been systematically studied. To
      investigate this point, we produced and characterized C57BL/6 mice transgenic for
      IgM antibody to ganglioside GD2. The transgenic (TG) mice showed high IgM, but
      not IgG antibody titers against GD2 in their sera. No significant clinical
      symptoms were observed. When EL4 cells, syngeneic T lymphoma that express
      ganglioside GD2, were injected into TG mice, prolonged survival was observed.
      Complement-dependent cytotoxicity (CDC) of EL4 cells was mediated with TG mice
      sera. Neither antibody-dependent cellular cytotoxicity with their sera nor
      cytotoxic T lymphocyte activity to EL4 cells was shown in TG mice. Spleen
      lymphocytes from TG mice had increased numbers of natural killer (NK) cells, but 
      not T cells, B cells, or macrophages compared with wild-type mice. Depletion of
      NK cells with anti-asialo GM1 rabbit serum reduced or abrogated the observed
      anti-tumor effects, suggesting that NK cells play a major role in tumor
      eradication or suppression. NK cell activity in TG mice was much higher than
      wild-type mice. Moreover, TG mice showed prolonged survival after injection with 
      syngeneic B16 melanoma cells, which express GM3, but not GD2 or GD3. Taking these
      results together, our studies demonstrate that the TG mice have significant
      anti-tumor characteristics, probably due to CDC and NK cell expansion and
      activation with anti-ganglioside GD2 antibody.
FAU - Kawashima, Ikuo
AU  - Kawashima I
AD  - Department of Tumor Immunology, Tokyo Metropolitan Organization for Medical
      Research, The Tokyo Metropolitan Institute of Medical Science, Tokyo 113-8613,
      Japan.
FAU - Yoshida, Yukiko
AU  - Yoshida Y
FAU - Taya, Chouji
AU  - Taya C
FAU - Shitara, Hiroshi
AU  - Shitara H
FAU - Yonekawa, Hiromichi
AU  - Yonekawa H
FAU - Karasuyama, Hajime
AU  - Karasuyama H
FAU - Tada, Nobuhiko
AU  - Tada N
FAU - Furukawa, Koichi
AU  - Furukawa K
FAU - Tai, Tadashi
AU  - Tai T
LA  - eng
PT  - Comparative Study
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - Greece
TA  - Int J Oncol
JT  - International journal of oncology
JID - 9306042
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Gangliosides)
RN  - 0 (Immunoglobulin M)
RN  - 65988-71-8 (ganglioside, GD2)
RN  - 82115-62-6 (Interferon-gamma)
RN  - 9007-36-7 (Complement System Proteins)
SB  - IM
MH  - Animals
MH  - Antibodies, Monoclonal/immunology
MH  - Antibody-Dependent Cell Cytotoxicity
MH  - Complement System Proteins/immunology
MH  - Female
MH  - Gangliosides/*immunology
MH  - Humans
MH  - Immunoglobulin M/*immunology
MH  - Interferon-gamma/blood/pharmacology
MH  - Killer Cells, Natural/*immunology
MH  - Lymphocyte Depletion
MH  - Lymphoma, T-Cell/*immunology/mortality/therapy
MH  - Macrophages/immunology/metabolism
MH  - Melanoma, Experimental/*immunology/mortality/therapy
MH  - Mice
MH  - Mice, Inbred C57BL
MH  - Mice, Transgenic
MH  - Spleen/immunology/metabolism
MH  - Survival Rate
MH  - T-Lymphocytes, Cytotoxic/immunology
MH  - Tumor Cells, Cultured/immunology
EDAT- 2003/07/10 05:00
MHDA- 2004/03/05 05:00
CRDT- 2003/07/10 05:00
PHST- 2003/07/10 05:00 [pubmed]
PHST- 2004/03/05 05:00 [medline]
PHST- 2003/07/10 05:00 [entrez]
PST - ppublish
SO  - Int J Oncol. 2003 Aug;23(2):381-8.

PMID- 8407875
OWN - NLM
STAT- MEDLINE
DCOM- 19931112
LR  - 20190512
IS  - 0021-924X (Print)
IS  - 0021-924X (Linking)
VI  - 114
IP  - 1
DP  - 1993 Jul
TI  - Generation of a monoclonal antibody specific for ganglioside GM4: evidence for
      GM4 expression on astrocytes in chicken cerebellum.
PG  - 5-8
AB  - We established a murine monoclonal antibody (MAb) specific for ganglioside GM4 by
      immunizing C3H/HeN mice with chemically synthesized GM4 adsorbed to Salmonella
      minnesota, followed by fusion with mouse myeloma cells. The MAb, designated as
      AMR10, was shown to exhibit high binding specificity, reacting only with the
      ganglioside GM4 used for immunization and native GM4 from human brain. We
      determined the distribution of GM4 in adult chicken cerebellum by means of the
      immunofluorescence technique with the MAb. Our study revealed that GM4 expression
      was associated with astrocytes in the granular layer and the white matter, but
      not with myelin in any layers of the chicken cerebellar cortex.
FAU - Ozawa, H
AU  - Ozawa H
AD  - Department of Tumor Immunology, Tokyo Metropolitan Institute of Medical Science.
FAU - Kotani, M
AU  - Kotani M
FAU - Kawashima, I
AU  - Kawashima I
FAU - Numata, M
AU  - Numata M
FAU - Ogawa, T
AU  - Ogawa T
FAU - Terashima, T
AU  - Terashima T
FAU - Tai, T
AU  - Tai T
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - J Biochem
JT  - Journal of biochemistry
JID - 0376600
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Gangliosides)
RN  - 0 (Glycolipids)
RN  - 66456-69-7 (ganglioside, GM4)
SB  - IM
MH  - Animals
MH  - Antibodies, Monoclonal/*immunology
MH  - Antibody Specificity
MH  - Astrocytes/*chemistry
MH  - Carbohydrate Sequence
MH  - Cerebellar Cortex/chemistry
MH  - Cerebellum/*chemistry
MH  - Chickens
MH  - Fluorescent Antibody Technique
MH  - Gangliosides/*analysis/immunology
MH  - Glycolipids/immunology
MH  - Humans
MH  - Mice
MH  - Molecular Sequence Data
MH  - Stereoisomerism
MH  - Tissue Distribution
EDAT- 1993/07/01 00:00
MHDA- 1993/07/01 00:01
CRDT- 1993/07/01 00:00
PHST- 1993/07/01 00:00 [pubmed]
PHST- 1993/07/01 00:01 [medline]
PHST- 1993/07/01 00:00 [entrez]
AID - 10.1093/oxfordjournals.jbchem.a124138 [doi]
PST - ppublish
SO  - J Biochem. 1993 Jul;114(1):5-8. doi: 10.1093/oxfordjournals.jbchem.a124138.

PMID- 15539921
OWN - NLM
STAT- MEDLINE
DCOM- 20041129
LR  - 20151119
IS  - 0030-2414 (Print)
IS  - 0030-2414 (Linking)
VI  - 67
IP  - 2
DP  - 2004
TI  - Correlation analysis between tumor-associated antigen sialyl-Tn expression and
      ST6GalNAc I activity in human colon adenocarcinoma.
PG  - 159-65
AB  - OBJECTIVES: Sialyl-Tn (sTn) is a mucin carbohydrate-associated antigen that is
      strongly expressed in a large number of colorectal carcinomas. In this study, we 
      combined immunohistochemical and enzymatic techniques in order to find the
      correlation between sTn tissue expression and the sialyltransferase activity
      (ST6GalNAc I) responsible for its synthesis in colorectal cancer (CRC) patients. 
      METHODS: We compared sTn expression in healthy (n = 46), tumorous (n = 60) and
      transitional tissue (n = 46) from CRC patients, and correlated sTn altered
      expression with clinicopathologic variables of the patient. Furthermore, we
      determined ST6GalNAc I tissue activity employing asialo-ovine submaxillary mucin 
      (asialo-OSM) as glycoprotein acceptor (n = 27). RESULTS: The rates of sTn
      positive expression obtained for healthy, tumorous and transitional tissues were 
      15, 67 and 63%, respectively. These rates led to statistically significant
      differences between healthy and tumorous or transitional tissue (p = 0.001); sTn 
      expression was related to the first stages of the tumor invasion in transitional 
      tissue. As regards ST6GalNAc I activity, we found an enhancement in transitional 
      tissue. Statistical correlation analysis did not reveal association between sTn
      expression and ST6GalNAc I activity. CONCLUSIONS: Our findings indicated that sTn
      antigen tissue expression and ST6GalNAc I activity levels were not correlated in 
      CRC, in spite of the overexpression of the antigen in tumorous and transitional
      tissue.
CI  - 2004 S. Karger AG, Basel.
FAU - Vazquez-Martin, C
AU  - Vazquez-Martin C
AD  - Department of Biochemistry, Genetics and Immunology, Faculty of Sciences,
      University of Vigo, Vigo, Spain.
FAU - Cuevas, E
AU  - Cuevas E
FAU - Gil-Martin, E
AU  - Gil-Martin E
FAU - Fernandez-Briera, A
AU  - Fernandez-Briera A
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - Switzerland
TA  - Oncology
JT  - Oncology
JID - 0135054
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Biomarkers, Tumor)
RN  - 0 (sialosyl-Tn antigen)
RN  - EC 2.4.99.- (Sialyltransferases)
RN  - EC 2.4.99.1 (beta-D-galactoside alpha 2-6-sialyltransferase)
SB  - IM
MH  - Adenocarcinoma/enzymology/immunology/*metabolism/pathology
MH  - Aged
MH  - Antigens, Tumor-Associated, Carbohydrate/analysis/*metabolism
MH  - Biomarkers, Tumor/*metabolism
MH  - Colonic Neoplasms/enzymology/immunology/*metabolism/pathology
MH  - Female
MH  - Gene Expression Regulation, Enzymologic
MH  - Gene Expression Regulation, Neoplastic
MH  - Humans
MH  - Immunohistochemistry
MH  - Male
MH  - Sialyltransferases/analysis/*metabolism
MH  - Up-Regulation
EDAT- 2004/11/13 09:00
MHDA- 2004/12/16 09:00
CRDT- 2004/11/13 09:00
PHST- 2003/10/23 00:00 [received]
PHST- 2004/02/18 00:00 [accepted]
PHST- 2004/11/13 09:00 [pubmed]
PHST- 2004/12/16 09:00 [medline]
PHST- 2004/11/13 09:00 [entrez]
AID - 81003 [pii]
AID - 10.1159/000081003 [doi]
PST - ppublish
SO  - Oncology. 2004;67(2):159-65. doi: 10.1159/000081003.

PMID- 8490832
OWN - NLM
STAT- MEDLINE
DCOM- 19930615
LR  - 20151119
IS  - 0008-543X (Print)
IS  - 0008-543X (Linking)
VI  - 71
IP  - 10
DP  - 1993 May 15
TI  - Association of expression of blood group-related carbohydrate antigens with
      prognosis in breast cancer.
PG  - 3044-53
AB  - BACKGROUND: It has been thought that carbohydrate antigens, especially Lewis (Le)
      blood group antigens, are cancer-related antigens. METHODS: The authors conducted
      immunohistochemical studies to investigate the expression of seven different
      types of Le carbohydrate antigens in breast cancer tissue and their usefulness as
      an indicator of the degree of malignancy and as a prognostic factor. RESULTS:
      When this expression was compared in the cancerous portion of 300 breast cancers 
      and noncancerous mammary ductal epithelium in each of the patients, reduced
      expression of type 1 carbohydrate antigens and increased expression of type 2
      carbohydrate antigens were found in the cancerous portions. No correlation was
      detected between the antigen expression and clinicopathologic factors. The
      prognosis of patients in whom type 2 carbohydrate antigens were increased in the 
      cancerous portion, especially Lex (19.7% of patients) and sialyl Lex-i (20.3% of 
      patients), was poorer than in patients in whom they were not increased (P <
      0.01). CONCLUSIONS: The relative expression of type 2 carbohydrate antigens in
      breast cancer tissue seems capable of serving as a prognostic factor.
FAU - Narita, T
AU  - Narita T
AD  - Department of Surgery II, Nagoya University School of Medicine, Japan.
FAU - Funahashi, H
AU  - Funahashi H
FAU - Satoh, Y
AU  - Satoh Y
FAU - Watanabe, T
AU  - Watanabe T
FAU - Sakamoto, J
AU  - Sakamoto J
FAU - Takagi, H
AU  - Takagi H
LA  - eng
PT  - Journal Article
PL  - United States
TA  - Cancer
JT  - Cancer
JID - 0374236
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Lewis Blood-Group System)
SB  - AIM
SB  - IM
MH  - Antibodies, Monoclonal
MH  - Antigens, Tumor-Associated, Carbohydrate/*immunology
MH  - Breast Diseases/immunology
MH  - Breast Neoplasms/diagnosis/*immunology
MH  - Carbohydrate Sequence
MH  - Female
MH  - Humans
MH  - Immunoenzyme Techniques
MH  - *Lewis Blood-Group System
MH  - Molecular Sequence Data
MH  - Prognosis
MH  - Survival Analysis
EDAT- 1993/05/15 00:00
MHDA- 1993/05/15 00:01
CRDT- 1993/05/15 00:00
PHST- 1993/05/15 00:00 [pubmed]
PHST- 1993/05/15 00:01 [medline]
PHST- 1993/05/15 00:00 [entrez]
PST - ppublish
SO  - Cancer. 1993 May 15;71(10):3044-53.

PMID- 9887355
OWN - NLM
STAT- MEDLINE
DCOM- 19990329
LR  - 20181113
IS  - 1219-4956 (Print)
IS  - 1219-4956 (Linking)
VI  - 4
IP  - 4
DP  - 1998
TI  - Immunohistopathological characterizatin of spontaneous metastases in a human lung
      mucoepidermoid adenocarcinoma (HLMC) xenograft.
PG  - 259-66
AB  - The most common clinical form of lung cancer is a disseminated disease with
      distant metastases; several years of cancer progression precede presentation, and
      this ultimately limits the efficacy of curative therapy. In this
      immunohistochemical study, we examined a mucinous adenocarcinoma cell line,
      maintained by xenogeneic transplantation, and a spontaneous metastatic variant
      which produces distant tumors (in liver, spleen and kidney). The aim was to
      investigate possible parameters which characterize the metastatic process.
      Histopathological comparison between the two subcutaneous transplanted tumor
      lines showed that both lines presented a similar cellular morphology, a different
      pattern of cellular growth and an increased vascularization in the metastatic
      line with respect to its parent. All the tumor sections expressed differential
      immune reactivity with monoclonal antibodies against Lewis y (MAb C14),
      sialyl-Lewis x (MAb SNH3) and Lewis x (MAb FH2) determinants. Neither expressed
      MUC 1 mucins detectable with monoclonal antibodies reactive with the mucin
      protein core (MAbs C595 and SM3) nor was carcinoembryonic antigen (MAb C365)
      expressed. Neoplastic cells were reactive with an anti-pan cytokeratin monoclonal
      antibody confirming their epithelial histogenesis. Our findings have been
      evaluated with respect to defining metastatic phenotypes in lung cancer by
      examination of distinct histopathological and immunological parameters.
FAU - Croce, M V
AU  - Croce MV
AD  - Centro de Investigaciones Inmunologicas Basicas y Aplicadas (CIMBA), National
      University of La Plata, Argentina.
FAU - Colussi, A G
AU  - Colussi AG
FAU - De Bravo, M G
AU  - De Bravo MG
FAU - Price, M R
AU  - Price MR
FAU - Segal-Eiras, A
AU  - Segal-Eiras A
LA  - eng
PT  - Comparative Study
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - Netherlands
TA  - Pathol Oncol Res
JT  - Pathology oncology research : POR
JID - 9706087
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Biomarkers, Tumor)
RN  - 0 (Carcinoembryonic Antigen)
RN  - 0 (Gangliosides)
RN  - 0 (Lewis Blood-Group System)
RN  - 0 (Lewis X Antigen)
RN  - 0 (Lewis Y antigen)
RN  - 0 (MUC1 tandem repeat peptide)
RN  - 0 (Mucin-1)
RN  - 0 (Mucins)
RN  - 0 (Neoplasm Proteins)
RN  - 0 (Oligopeptides)
RN  - 0 (Peptide Fragments)
RN  - 0 (sialyl Lewis(x) ganglioside)
SB  - IM
MH  - Adenocarcinoma, Mucinous/blood supply/chemistry/pathology/*secondary
MH  - Animals
MH  - Antibodies, Monoclonal/immunology
MH  - Apoptosis
MH  - Biomarkers, Tumor/analysis
MH  - Carcinoembryonic Antigen/analysis
MH  - Cell Nucleus/ultrastructure
MH  - Cytoplasm/ultrastructure
MH  - Gangliosides/analysis
MH  - Humans
MH  - Image Processing, Computer-Assisted
MH  - Immunoenzyme Techniques
MH  - Injections, Subcutaneous
MH  - Kidney Neoplasms/blood supply/chemistry/pathology/*secondary
MH  - Lewis Blood-Group System/analysis
MH  - Lewis X Antigen/analysis
MH  - Liver Neoplasms, Experimental/blood supply/chemistry/pathology/*secondary
MH  - Lung Neoplasms/chemistry/*pathology
MH  - Mice
MH  - Mice, Nude
MH  - *Mucin-1
MH  - Mucins/analysis
MH  - Neoplasm Proteins/analysis
MH  - Neoplasm Transplantation
MH  - Neoplastic Stem Cells/chemistry/ultrastructure
MH  - Oligopeptides/analysis
MH  - *Peptide Fragments
MH  - Phenotype
MH  - Splenic Neoplasms/blood supply/chemistry/pathology/*secondary
MH  - Transplantation, Heterologous
MH  - Tumor Cells, Cultured/pathology/transplantation
EDAT- 1999/01/15 00:00
MHDA- 1999/01/15 00:01
CRDT- 1999/01/15 00:00
PHST- 1999/01/15 00:00 [pubmed]
PHST- 1999/01/15 00:01 [medline]
PHST- 1999/01/15 00:00 [entrez]
PST - ppublish
SO  - Pathol Oncol Res. 1998;4(4):259-66.

PMID- 4055789
OWN - NLM
STAT- MEDLINE
DCOM- 19851220
LR  - 20071114
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 260
IP  - 27
DP  - 1985 Nov 25
TI  - Proton NMR and fast-atom bombardment mass spectrometry analysis of the
      melanoma-associated ganglioside 9-O-acetyl-GD3.
PG  - 14556-63
AB  - A glycolipid antigen, detected by a monoclonal antibody (ME 311) obtained by
      immunizing mice with a human metastatic melanoma cell line (WM 46), was isolated 
      and structurally characterized. Using immunostaining on thin-layer chromatograms 
      for monitoring, 1.0 mg of a pure alkali-labile disialoganglioside was obtained
      from 23 g of packed melanoma cells (WM 164). Fractionation of the lipid extract
      was done on DEAE-Sepharose columns into total disialogangliosides which were
      repeatedly separated by high-pressure liquid chromatography. On mild alkaline
      treatment, the ganglioside was converted to a slower migrating species identical 
      with a ganglioside GD3 isolated from the same source (Neu5Ac alpha 2----8Neu5Ac
      alpha 2----3Gal beta 1----4Glc beta 1----1-cer-amide) and specifically detected
      by monoclonal antibody R24. Comparison of the two gangliosides by fast-atom
      bombardment mass spectrometry (revealing an acetyl group on the terminal sialic
      acid on the alkali-labile species) and by 1H NMR (indicating the position of the 
      acetyl group) suggested the following structure: Neu5,9Ac2 alpha 2----8Neu5Ac
      alpha 2----3Gal beta 1----4Glc beta 1----1-ceramide. This is identical with a
      ganglioside proposed earlier to exist in melanoma cells (Cheresh, D. A., Varki,
      A. P., Varki, N. M., Stallcup, W. B., Levine, J., and Reisfeld, R. A. (1984) J.
      Biol. Chem. 259, 7453-7459). Immunostaining with ME 311 antibody of cell extracts
      on thin-layer chromatography chromatograms revealed only this ganglioside in the 
      melanoma cells, while normal human brain was negative. However, in one of the
      total ganglioside extracts tested for presence of binding with antibody ME 311,
      three gangliosides were found to bind. No evidence was obtained for the presence 
      of the antigenic epitope in mucins or glycoproteins of the melanoma cells.
FAU - Thurin, J
AU  - Thurin J
FAU - Herlyn, M
AU  - Herlyn M
FAU - Hindsgaul, O
AU  - Hindsgaul O
FAU - Stromberg, N
AU  - Stromberg N
FAU - Karlsson, K A
AU  - Karlsson KA
FAU - Elder, D
AU  - Elder D
FAU - Steplewski, Z
AU  - Steplewski Z
FAU - Koprowski, H
AU  - Koprowski H
LA  - eng
GR  - CA-10815/CA/NCI NIH HHS/United States
GR  - CA-21124/CA/NCI NIH HHS/United States
GR  - CA-25874/CA/NCI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigen-Antibody Complex)
RN  - 0 (Gangliosides)
RN  - 0 (Glycolipids)
RN  - 98743-26-1 (9-O-acetyl-GD3 ganglioside)
SB  - IM
MH  - Antibodies, Monoclonal
MH  - Antigen-Antibody Complex
MH  - Cell Line
MH  - Chromatography, Thin Layer
MH  - Gangliosides/*analysis
MH  - Gas Chromatography-Mass Spectrometry/methods
MH  - Glycolipids/*analysis
MH  - Humans
MH  - Magnetic Resonance Spectroscopy/methods
MH  - Melanoma/*analysis
MH  - Nevus/analysis
EDAT- 1985/11/25 00:00
MHDA- 1985/11/25 00:01
CRDT- 1985/11/25 00:00
PHST- 1985/11/25 00:00 [pubmed]
PHST- 1985/11/25 00:01 [medline]
PHST- 1985/11/25 00:00 [entrez]
PST - ppublish
SO  - J Biol Chem. 1985 Nov 25;260(27):14556-63.

PMID- 2470757
OWN - NLM
STAT- MEDLINE
DCOM- 19890705
LR  - 20171116
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 264
IP  - 16
DP  - 1989 Jun 5
TI  - Specific interaction between Lex and Lex determinants. A possible basis for cell 
      recognition in preimplantation embryos and in embryonal carcinoma cells.
PG  - 9476-84
AB  - The Lex determinant (Gal beta 1----4[Fuc alpha 1----3]GlcNAc-beta 1----R) has
      been implicated as having a role in mediating compaction of the mouse embryo at
      the morula stage (Fenderson, B., Zehavi, U., and Hakomori, S. (1984) J. Exp. Med.
      160, 1591-1596). Here, we present evidence suggesting a role for Lex in F9
      embryonal carcinoma cell adhesion and a mechanism for Lex recognition based on
      carbohydrate-carbohydrate interaction. Homotypic aggregation of F9 cells was
      inhibited by lacto-N-fucopentaose III, and F9 cells showed a preferential
      interaction with Lex liposomes. The following observations suggest that the
      structure capable of recognizing Lex per se on F9 cells is Lex: (i) Cell
      surface-labeled components solubilized in octylglucoside, affinity-bound on an
      Lex-octyl-Sepharose column, contained glycoproteins reactive with anti-Lex
      antibody. (ii) Liposomes containing Lex showed significant interaction with Lex
      glycolipid, but not other glycolipids, coated on a plastic surface. (iii)
      Liposomes containing Lex glycolipid were found to self-aggregate, whereas
      liposomes containing paragloboside (nLc4) or sialylparagloboside (IV3NeuAcnLc4)
      did not. (iv) The diffusibility of 3H-labeled lacto-N-fucopentaitol III (but not 
      I or II), incubated with Lex liposome, from the lower to the upper Boyden chamber
      through a semipermeable membrane was inhibited. In all these experiments (i-iv), 
      the interaction of Lex to Lex (or Lex to lacto-N-fucopentaose III) was clearly
      observed only in the presence of Ca2+ and Mg2+ and was enhanced by the presence
      of Mn2+. These interactions were inhibited by EDTA. The results suggest the novel
      hypothesis that carbohydrate-carbohydrate interactions may play an important role
      in controlling cell recognition during F9 cell aggregation and during embryonic
      development.
FAU - Eggens, I
AU  - Eggens I
AD  - Biomembrane Institute, Seattle, Washington 98119.
FAU - Fenderson, B
AU  - Fenderson B
FAU - Toyokuni, T
AU  - Toyokuni T
FAU - Dean, B
AU  - Dean B
FAU - Stroud, M
AU  - Stroud M
FAU - Hakomori, S
AU  - Hakomori S
LA  - eng
GR  - CA42505/CA/NCI NIH HHS/United States
GR  - GM23100/GM/NIGMS NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Epitopes)
RN  - 0 (Glycolipids)
RN  - 0 (Lewis Blood-Group System)
RN  - 0 (Lewis X Antigen)
RN  - 0 (Liposomes)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Oligosaccharides)
RN  - 0 (Solutions)
SB  - IM
MH  - Animals
MH  - Antigen-Antibody Reactions
MH  - Cell Aggregation/drug effects
MH  - *Cell Communication
MH  - Cell Line
MH  - Chromatography, Affinity
MH  - Diffusion Chambers, Culture
MH  - Embryonal Carcinoma Stem Cells
MH  - *Embryonic Development
MH  - Epitopes/immunology
MH  - Female
MH  - Glycolipids/physiology
MH  - Humans
MH  - *Lewis Blood-Group System/immunology
MH  - Lewis X Antigen/analysis/immunology/*physiology
MH  - Liposomes
MH  - Membrane Glycoproteins/immunology
MH  - Mice
MH  - Neoplastic Stem Cells/pathology
MH  - Oligosaccharides/analysis/immunology
MH  - Pregnancy
MH  - Solutions
EDAT- 1989/06/05 00:00
MHDA- 1989/06/05 00:01
CRDT- 1989/06/05 00:00
PHST- 1989/06/05 00:00 [pubmed]
PHST- 1989/06/05 00:01 [medline]
PHST- 1989/06/05 00:00 [entrez]
PST - ppublish
SO  - J Biol Chem. 1989 Jun 5;264(16):9476-84.

PMID- 18282768
OWN - NLM
STAT- MEDLINE
DCOM- 20080730
LR  - 20080310
IS  - 1050-4648 (Print)
IS  - 1050-4648 (Linking)
VI  - 24
IP  - 4
DP  - 2008 Apr
TI  - Purification and characterization of a T-antigen specific lectin from the
      coelomic fluid of a marine invertebrate, sea cucumber (Holothuria scabra).
PG  - 450-8
LID - 10.1016/j.fsi.2008.01.002 [doi]
AB  - A novel lectin was purified from the coelomic fluid of the sea cucumber
      Holothuria scabra (HSL), subjected to bacterial challenge. HSL is a monomeric
      glycoprotein of molecular mass 182 kDa. The lectin is highly thermostable as it
      retains full activity for 1 h at 80 degrees C. Further, the hemagglutination
      activity of HSL is unaffected by pH in the range 2-11. Unlike other lectins
      purified from marine invertebrates, the hemagglutination activity of HSL does not
      require any divalent metal ions. The affinity profile of HSL was studied by a
      combination of hemagglutination inhibition and fluorescence spectroscopy. HSL
      binds to desialylated glycoproteins, MealphaGal, T-antigen and T
      (alpha-ser)-antigen with a distinction between beta1-4 and beta1-3 linkages.
      Mealpha-T-antigen was a potent ligand having highest affinity (Ka 8.32 x
      10(7)M(-1)). Monosaccharide binding is enthalphically driven while disaccharide
      binding involves both entropic and enthalpic contributions.
FAU - Gowda, Nagaraj M
AU  - Gowda NM
AD  - Gene Laboratory, National Institute of Oceanography, Dona Paula, Goa 403 004,
      India.
FAU - Goswami, Usha
AU  - Goswami U
FAU - Khan, M Islam
AU  - Khan MI
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20080111
PL  - England
TA  - Fish Shellfish Immunol
JT  - Fish & shellfish immunology
JID - 9505220
RN  - 0 (Amino Acids)
RN  - 0 (Antigens)
RN  - 0 (Carbohydrates)
RN  - 0 (Cations, Divalent)
RN  - 0 (Lectins)
SB  - IM
MH  - Amino Acids/analysis
MH  - Animals
MH  - Antigens/immunology/*metabolism
MH  - Body Fluids/*chemistry
MH  - Carbohydrates/analysis
MH  - Cations, Divalent/pharmacology
MH  - Circular Dichroism
MH  - Fluorescence
MH  - Hemagglutination Inhibition Tests
MH  - Holothuria/*chemistry/immunology
MH  - Hydrogen-Ion Concentration
MH  - Lectins/*chemistry/immunology/*isolation & purification/metabolism
MH  - Mass Spectrometry
MH  - Molecular Weight
MH  - Sensitivity and Specificity
MH  - Temperature
EDAT- 2008/02/20 09:00
MHDA- 2008/07/31 09:00
CRDT- 2008/02/20 09:00
PHST- 2007/11/23 00:00 [received]
PHST- 2007/12/24 00:00 [revised]
PHST- 2008/01/03 00:00 [accepted]
PHST- 2008/02/20 09:00 [pubmed]
PHST- 2008/07/31 09:00 [medline]
PHST- 2008/02/20 09:00 [entrez]
AID - S1050-4648(08)00007-7 [pii]
AID - 10.1016/j.fsi.2008.01.002 [doi]
PST - ppublish
SO  - Fish Shellfish Immunol. 2008 Apr;24(4):450-8. doi: 10.1016/j.fsi.2008.01.002.
      Epub 2008 Jan 11.

PMID- 8052660
OWN - NLM
STAT- MEDLINE
DCOM- 19940902
LR  - 20190501
IS  - 0027-8424 (Print)
IS  - 0027-8424 (Linking)
VI  - 91
IP  - 16
DP  - 1994 Aug 2
TI  - 9-O-acetylated sialic acids have widespread but selective expression: analysis
      using a chimeric dual-function probe derived from influenza C
      hemagglutinin-esterase.
PG  - 7782-6
AB  - While 9-O-acetylation of sialic acids has been reported in some mammalian
      tissues, the distribution of this modification on specific cell types and
      molecules is largely unknown. The influenza C virus hemagglutinin-esterase is a
      membrane-bound glycoprotein that binds specifically to 9-O-acetylated sialic
      acids (hemagglutinin activity) and then hydrolyzes the O-acetyl group
      (receptor-destroying activity). A recombinant soluble form of influenza C virus
      hemagglutinin-esterase wherein the C-terminal transmembrane and cytoplasmic
      domains are replaced by the Fc portion of human IgG retains both its recognition 
      and enzymatic functions. The latter activity can selectively remove 9-O-acetyl
      groups from bound or free sialic acids and, under specific conditions, 7-O-acetyl
      groups as well. Irreversible inactivation of the esterase unmasks stable
      recognition activity, giving a molecule that binds specifically to 9-O-acetylated
      sialic acids. These probes demonstrate widespread but selective expression of
      9-O-acetylated sialic acids in certain cell types of rat tissues. Patterns of
      polarized or gradient expression further demonstrate the regulated nature of this
      modification. Direct probing of blots and thin-layer plates shows selective
      expression of 9-O-acetylation on certain glycoproteins and glycolipids in such
      tissues. Thus, 9-O-acetylation is more widespread than previously thought and
      occurs on specific molecules and cell types.
FAU - Klein, A
AU  - Klein A
AD  - Glycobiology Program, Cancer Center, University of California, San Diego, La
      Jolla 92093.
FAU - Krishna, M
AU  - Krishna M
FAU - Varki, N M
AU  - Varki NM
FAU - Varki, A
AU  - Varki A
LA  - eng
GR  - R01GM32373/GM/NIGMS NIH HHS/United States
PT  - Journal Article
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Proc Natl Acad Sci U S A
JT  - Proceedings of the National Academy of Sciences of the United States of America
JID - 7505876
RN  - 0 (Glycolipids)
RN  - 0 (Glycoproteins)
RN  - 0 (Hemagglutinins, Viral)
RN  - 0 (Molecular Probes)
RN  - 0 (Recombinant Fusion Proteins)
RN  - 0 (Sialic Acids)
RN  - 0 (Viral Fusion Proteins)
RN  - 0 (Viral Proteins)
RN  - 0 (hemagglutinin esterase)
RN  - 55717-54-9 (9-O-acetyl-N-acetylneuraminic acid)
RN  - EC 3.1.- (Esterases)
SB  - IM
MH  - Animals
MH  - Esterases/genetics/metabolism
MH  - Glycolipids/chemistry/isolation & purification
MH  - Glycoproteins/chemistry/isolation & purification
MH  - Hemagglutinins, Viral/genetics/metabolism
MH  - Histocytochemistry
MH  - Influenzavirus C/enzymology/genetics
MH  - Molecular Probes
MH  - Rats
MH  - Rats, Sprague-Dawley
MH  - Recombinant Fusion Proteins/metabolism
MH  - Sialic Acids/*isolation & purification
MH  - Tissue Distribution
MH  - *Viral Fusion Proteins
MH  - Viral Proteins/genetics/metabolism
PMC - PMC44486
EDAT- 1994/08/02 00:00
MHDA- 1994/08/02 00:01
CRDT- 1994/08/02 00:00
PHST- 1994/08/02 00:00 [pubmed]
PHST- 1994/08/02 00:01 [medline]
PHST- 1994/08/02 00:00 [entrez]
AID - 10.1073/pnas.91.16.7782 [doi]
PST - ppublish
SO  - Proc Natl Acad Sci U S A. 1994 Aug 2;91(16):7782-6. doi: 10.1073/pnas.91.16.7782.

PMID- 12017332
OWN - NLM
STAT- MEDLINE
DCOM- 20020625
LR  - 20041117
IS  - 0250-7005 (Print)
IS  - 0250-7005 (Linking)
VI  - 22
IP  - 1A
DP  - 2002 Jan-Feb
TI  - Predictive factors for preoperative serum levels of sialy Lewis(x), sialyl
      Lewis(a) and sialyl Tn antigens in gastric cancer patients.
PG  - 451-8
AB  - Preoperative serum levels of sialyl Lewis(a) (CA19-9), sialyl Lewis(x) (SLX) and 
      sialyl Tn (STN) antigens in 180 patients with gastric cancer were examined to
      establish predictive factors for serum levels of these antigens compared with
      carcinoembryonic antigen (CEA). The patients were divided into low and high
      antigen groups. Multivariate logistic regression analysis revealed the following 
      independent predictive factors for high antigen levels [odds ratio]: liver
      metastasis for CA19-9 [4.40], SLX [9.90], STN [39.65] and CEA [5.14]; peritoneal 
      dissemination for SLX [4.78] or STN [13.01]; venous invasion for CEA [3.56];
      lymph node metastasis for CA19-9 [4.51]. In addition, high CA19-9 levels were
      independently related to lymph node metastasis in patients with stage I or II
      tumors. In conclusion, high serum levels of CA19-9, SLX and STN are associated
      with liver metastasis, while high serum levels of SLX and STN are associated with
      peritoneal dissemination. In addition, high serum CA19-9 levels may represent an 
      independent predictor for lymph node metastasis.
FAU - Nakagoe, Tohru
AU  - Nakagoe T
AD  - First Department of Surgery, Nagasaki University School of Medicine, Japan.
      nakagoe@net.nagasaki-u.ac.jp
FAU - Sawai, Terumitsu
AU  - Sawai T
FAU - Tsuji, Takashi
AU  - Tsuji T
FAU - Jibiki, Masa-Aki
AU  - Jibiki MA
FAU - Nanashima, Atsushi
AU  - Nanashima A
FAU - Yamaguchi, Hiroyuki
AU  - Yamaguchi H
FAU - Yasutake, Toru
AU  - Yasutake T
FAU - Ayabe, Hiroyoshi
AU  - Ayabe H
FAU - Arisawa, Kokichi
AU  - Arisawa K
FAU - Ishikawa, Hiroshi
AU  - Ishikawa H
LA  - eng
PT  - Journal Article
PL  - Greece
TA  - Anticancer Res
JT  - Anticancer research
JID - 8102988
RN  - 0
      (5-acetylneuraminyl-(2-3)-galactosyl-(1-4)-(fucopyranosyl-(1-3))-N-acetylglucosam
      ine)
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (CA-19-9 Antigen)
RN  - 0 (Carcinoembryonic Antigen)
RN  - 0 (Gangliosides)
RN  - 0 (Oligosaccharides)
RN  - 0 (sialosyl-Tn antigen)
RN  - 91847-18-6 (sialyl Le(a) ganglioside)
SB  - IM
MH  - Adult
MH  - Aged
MH  - Aged, 80 and over
MH  - Antigens, Tumor-Associated, Carbohydrate/*blood
MH  - CA-19-9 Antigen/blood
MH  - Carcinoembryonic Antigen/blood
MH  - Female
MH  - Gangliosides/*blood
MH  - Humans
MH  - Logistic Models
MH  - Male
MH  - Middle Aged
MH  - Oligosaccharides/*blood
MH  - Predictive Value of Tests
MH  - Preoperative Care
MH  - Stomach Neoplasms/*blood/pathology/surgery
EDAT- 2002/05/23 10:00
MHDA- 2002/06/26 10:01
CRDT- 2002/05/23 10:00
PHST- 2002/05/23 10:00 [pubmed]
PHST- 2002/06/26 10:01 [medline]
PHST- 2002/05/23 10:00 [entrez]
PST - ppublish
SO  - Anticancer Res. 2002 Jan-Feb;22(1A):451-8.

PMID- 3592664
OWN - NLM
STAT- MEDLINE
DCOM- 19870702
LR  - 20151119
IS  - 0003-9861 (Print)
IS  - 0003-9861 (Linking)
VI  - 255
IP  - 1
DP  - 1987 May 15
TI  - Monoclonal antibody CC3C195, which detects cancer-associated antigens in serum,
      binds to the human Lea blood group antigen and to its sialylated derivative.
PG  - 214-6
AB  - Mouse monoclonal antibody CC3C195, which detects elevated levels of its antigen
      in sera from many patients with colon and pancreatic cancer, binds with high
      affinity to the sialylated human Lea blood group antigen NeuAc alpha 2-3Gal beta 
      1-3 [Fuc alpha 1-4]GlcNac . . . and with lower affinity to the Lea blood group
      antigen itself.
FAU - Fukuta, S
AU  - Fukuta S
FAU - Magnani, J L
AU  - Magnani JL
FAU - Gaur, P K
AU  - Gaur PK
FAU - Ginsburg, V
AU  - Ginsburg V
LA  - eng
PT  - Journal Article
PL  - United States
TA  - Arch Biochem Biophys
JT  - Archives of biochemistry and biophysics
JID - 0372430
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens, Neoplasm)
RN  - 0 (Isoantigens)
RN  - 0 (Lewis Blood-Group System)
SB  - IM
MH  - Animals
MH  - *Antibodies, Monoclonal
MH  - Antibody Specificity
MH  - *Antigen-Antibody Reactions
MH  - Antigens, Neoplasm/immunology
MH  - Humans
MH  - Isoantigens/*immunology
MH  - Lewis Blood-Group System/*immunology
MH  - Mice
MH  - Mice, Inbred BALB C
EDAT- 1987/05/15 00:00
MHDA- 1987/05/15 00:01
CRDT- 1987/05/15 00:00
PHST- 1987/05/15 00:00 [pubmed]
PHST- 1987/05/15 00:01 [medline]
PHST- 1987/05/15 00:00 [entrez]
AID - 0003-9861(87)90314-6 [pii]
PST - ppublish
SO  - Arch Biochem Biophys. 1987 May 15;255(1):214-6.

PMID- 8445257
OWN - NLM
STAT- MEDLINE
DCOM- 19930402
LR  - 20180602
IS  - 0022-1759 (Print)
IS  - 0022-1759 (Linking)
VI  - 159
IP  - 1-2
DP  - 1993 Feb 26
TI  - Immunochemical characterization of anti-H monoclonal antibodies obtained from a
      mouse immunized with human saliva.
PG  - 261-7
AB  - Three IgM class anti-H monoclonal antibodies (1E3, 1E5 and 3H1) were obtained
      from a BALB/c mouse immunized with human O type saliva. These antibodies were
      found to agglutinate red cells from O group and A and B subgroups but not from
      Bombay and para-Bombay individuals whose H antigen was barely detected by anti-H 
      reagents. The agglutination reactions of these antibodies were inhibited by H
      antigens from human tissues. It was also demonstrated that both 1E3 and 3H1
      reacted with H disaccharide (Fuc alpha 1-->2Gal beta), H type 1 (Fuc alpha
      1-->2Gal beta 1-->3GlcNAc beta), H type 2 (Fuc alpha 1-->2Gal beta 1-->4GlcNAc
      beta), H type 3 (Fuc alpha 1-->2Gal beta 1-->3GalNAc alpha) and H type 4 (Fuc
      alpha 1-->2Gal beta 1-->3GalNAc beta) but not with Lea (Gal beta 1-->3[Fuc alpha 
      1-->4]GlcNAc beta), Leb (Fuc alpha 1-->2Gal beta 1-->3[Fuc alpha 1-->4]GlcNAc
      beta), X (Gal beta 1-->4[Fuc alpha-->3]GlcNAc beta) or Y (Fuc alpha 1-->2Gal beta
      1-->4[Fuc alpha 1-->3]GlcNAc beta). On the other hand, 1E5 was found to react
      with H type 1, H type 2, Leb and Y. Because of the unique reactivities against
      various fucosyl linkages these monoclonal antibodies could be useful not only as 
      anti-H reagents but also as reagents for the structural analysis of fucosylated
      glycoconjugates.
FAU - Nakajima, T
AU  - Nakajima T
AD  - Department of Legal Medicine, School of Medicine, Gunma University, Maebashi,
      Japan.
FAU - Yazawa, S
AU  - Yazawa S
FAU - Miyazaki, S
AU  - Miyazaki S
FAU - Furukawa, K
AU  - Furukawa K
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - Netherlands
TA  - J Immunol Methods
JT  - Journal of immunological methods
JID - 1305440
RN  - 0 (ABO Blood-Group System)
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Carbohydrates)
SB  - IM
MH  - ABO Blood-Group System/*immunology
MH  - Adsorption
MH  - Animals
MH  - Antibodies, Monoclonal/*immunology
MH  - Carbohydrate Sequence
MH  - Carbohydrates/immunology
MH  - Hemagglutination
MH  - Humans
MH  - Immunization
MH  - Male
MH  - Mice
MH  - Mice, Inbred BALB C
MH  - Molecular Sequence Data
MH  - Saliva/*immunology
EDAT- 1993/02/26 00:00
MHDA- 1993/02/26 00:01
CRDT- 1993/02/26 00:00
PHST- 1993/02/26 00:00 [pubmed]
PHST- 1993/02/26 00:01 [medline]
PHST- 1993/02/26 00:00 [entrez]
AID - 0022-1759(93)90165-4 [pii]
PST - ppublish
SO  - J Immunol Methods. 1993 Feb 26;159(1-2):261-7.

PMID- 1696162
OWN - NLM
STAT- MEDLINE
DCOM- 19900912
LR  - 20151119
IS  - 0008-5472 (Print)
IS  - 0008-5472 (Linking)
VI  - 50
IP  - 16
DP  - 1990 Aug 15
TI  - Serological mapping of the TAG-72 tumor-associated antigen using 19 distinct
      monoclonal antibodies.
PG  - 4872-9
AB  - Monoclonal antibody (MAb) B72.3 has been shown to be of potential utility in the 
      management of human carcinoma via its use in (a) the targeting of carcinoma
      lesions in colorectal and ovarian cancer patients, (b) immunohistochemical
      analyses of biopsies and effusions, and (c) serum assays to help define the
      presence of carcinoma. The B72.3-reactive antigen, designated tumor-associated
      glycoprotein 72 (TAG-72), has been characterized as a high molecular weight
      glycoprotein with the properties of a mucin. We report here the utilization of
      MAb B72.3 and 18 second generation MAbs (generated using purified TAG-72 obtained
      from a colon carcinoma xenograft as immunogen) to construct a serological map of 
      the TAG-72 molecule. The generation and initial characterization of 10 of the
      second generation MAbs have been described previously; in addition, eight
      previously unreported MAbs were used. All 19 MAbs produced immune precipitate
      lines against purified TAG-72 in double immunodiffusion, indicating that each
      epitope recognized by a single MAb is present at least twice on the TAG-72
      molecule. Immunodepletion analyses utilizing 11 of the anti-TAG-72 MAbs indicated
      that each recognizes the same molecule or population of molecules. Nineteen
      competition radioimmunoassays were developed and 19 purified competitor
      immunoglobulins were used in each assay. The patterns of cross-competition
      indicated the presence of a complex array of tumor-associated epitopes on the
      TAG-72 molecule. Some of the MAbs recognized epitopes that were structurally or
      spatially related to one another, but none appeared to recognize identical
      epitopes. The spectrum of inhibitory reactivities of these MAbs for TAG-72
      binding varied from extremely restricted to more broad inhibition. The
      serological mapping studies reported here provide information as to the range and
      nature of the epitopes expressed on the TAG-72 molecule, help form the basis for 
      selecting alternative anti-TAG-72 MAbs for use in potential clinical
      applications, and further define the nature of this oncofetal antigen.
FAU - Kuroki, M
AU  - Kuroki M
AD  - Laboratory of Tumor Immunology and Biology, National Cancer Institute, National
      Institutes of Health, Bethesda, Maryland 20892.
FAU - Fernsten, P D
AU  - Fernsten PD
FAU - Wunderlich, D
AU  - Wunderlich D
FAU - Colcher, D
AU  - Colcher D
FAU - Simpson, J F
AU  - Simpson JF
FAU - Poole, D J
AU  - Poole DJ
FAU - Schlom, J
AU  - Schlom J
LA  - eng
PT  - Journal Article
PL  - United States
TA  - Cancer Res
JT  - Cancer research
JID - 2984705R
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens, Neoplasm)
RN  - 0 (Carcinoembryonic Antigen)
RN  - 0 (Epitopes)
RN  - 0 (Glycoproteins)
RN  - 0 (tumor-associated antigen 72)
SB  - IM
MH  - *Antibodies, Monoclonal/isolation & purification
MH  - Antigens, Neoplasm/*analysis/immunology/isolation & purification
MH  - Blotting, Western
MH  - Carcinoembryonic Antigen/isolation & purification
MH  - Cell Line
MH  - Colonic Neoplasms/analysis/*pathology
MH  - Enzyme-Linked Immunosorbent Assay
MH  - Epitopes/analysis
MH  - Female
MH  - Glycoproteins/*analysis/immunology/isolation & purification
MH  - Humans
MH  - Immunoenzyme Techniques
MH  - Ovarian Neoplasms/analysis/*pathology
MH  - Radioimmunoassay
EDAT- 1990/08/15 00:00
MHDA- 1990/08/15 00:01
CRDT- 1990/08/15 00:00
PHST- 1990/08/15 00:00 [pubmed]
PHST- 1990/08/15 00:01 [medline]
PHST- 1990/08/15 00:00 [entrez]
PST - ppublish
SO  - Cancer Res. 1990 Aug 15;50(16):4872-9.

PMID- 2153431
OWN - NLM
STAT- MEDLINE
DCOM- 19900314
LR  - 20151119
IS  - 0008-543X (Print)
IS  - 0008-543X (Linking)
VI  - 65
IP  - 3
DP  - 1990 Feb 1
TI  - The abnormal occurrence and the differentiation-dependent distribution of
      N-acetyl and N-glycolyl species of the ganglioside GM2 in human germ cell tumors.
      A study with specific monoclonal antibodies.
PG  - 499-505
AB  - Human primary germ cell tumors were analyzed for the presence of the ganglioside 
      GM2 using three specific monoclonal antibodies which can distinguish the
      molecular species of the sialic acid moiety: the antibody MK1-16 is specific for 
      N-acetyl GM2, MK2-34 is specific for N-glycolyl GM2, and MK1-17 detects both
      N-acetyl and N-glycolyl GM2. When the occurrence of the GM2 antigen was tested in
      107 cases of human germ cell tumors by the immunohistochemical technique using
      these antibodies, seminoma was characterized as having the highest frequency of
      N-acetyl GM2 (89.4%, 42 of 47 cases) among germ cell tumors, followed by
      embryonal carcinoma (40.0%), and teratocarcinoma (26.6%). Compared with this,
      yolk sac tumors and choriocarcinoma had a much lower positive incidence of the
      N-acetyl GM2 antigen. On the other hand, the N-glycolyl GM2 antigen was not found
      at all in 47 cases of seminoma (0%), and the positive incidence was very low in
      embryonal carcinoma (6.6%), although considerably higher incidences were obtained
      with choriocarcinoma (25.0%), yolk sac tumor (22.2%), and teratocarcinoma
      (13.3%). The presence and molecular species of the GM2 antigens in these human
      germ cell tumors were also ascertained chemically by the thin-layer
      chromatography (TLC) immunostaining of the ganglioside fractions prepared from
      primary germ cell tumors. These results indicate that seminoma specifically
      contains N-acetyl GM2 and no N-glycolyl GM2, suggesting that N-acetyl GM2 could
      be a good marker for seminoma. On the other hand, non-seminomatous germ cell
      tumors were characterized by the presence of N-glycolyl GM2, one of the
      Hanganutziu-Deicher antigens (H-D antigens). Moreover, the positive occurrence of
      N-glycolyl GM2 correlated very well with the degree of differentiation of
      non-seminomatous germ cell tumors, i.e., the differentiated tumors such as yolk
      sac tumors, choriocarcinoma, and teratocarcinoma had a higher positive incidence 
      of N-glycolyl GM2 type H-D antigen but a lower positive incidence of N-acetyl GM2
      when compared with embryonal carcinoma, the most undifferentiated tumors among
      non-seminomatous germ cell tumors.
FAU - Miyake, M
AU  - Miyake M
AD  - Department of Laboratory Medicine and Clinical Science, School of Medicine, Kyoto
      University, Japan.
FAU - Hashimoto, K
AU  - Hashimoto K
FAU - Ito, M
AU  - Ito M
FAU - Ogawa, O
AU  - Ogawa O
FAU - Arai, E
AU  - Arai E
FAU - Hitomi, S
AU  - Hitomi S
FAU - Kannagi, R
AU  - Kannagi R
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Cancer
JT  - Cancer
JID - 0374236
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Gangliosides)
RN  - 19600-01-2 (G(M2) Ganglioside)
SB  - AIM
SB  - IM
MH  - Antibodies, Monoclonal
MH  - Carbohydrate Sequence
MH  - Choriocarcinoma/analysis
MH  - Dysgerminoma/analysis
MH  - G(M2) Ganglioside/*analysis
MH  - Gangliosides/*analysis
MH  - Humans
MH  - Immunohistochemistry
MH  - Mesonephroma/analysis
MH  - Molecular Sequence Data
MH  - Neoplasms, Germ Cell and Embryonal/*analysis
MH  - Teratoma/analysis
EDAT- 1990/02/01 00:00
MHDA- 1990/02/01 00:01
CRDT- 1990/02/01 00:00
PHST- 1990/02/01 00:00 [pubmed]
PHST- 1990/02/01 00:01 [medline]
PHST- 1990/02/01 00:00 [entrez]
PST - ppublish
SO  - Cancer. 1990 Feb 1;65(3):499-505.

PMID- 11279053
OWN - NLM
STAT- MEDLINE
DCOM- 20010712
LR  - 20131121
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 276
IP  - 23
DP  - 2001 Jun 8
TI  - Myelin-associated glycoprotein interacts with ganglioside GT1b. A mechanism for
      neurite outgrowth inhibition.
PG  - 20280-5
AB  - Myelin-associated glycoprotein (MAG) is expressed on myelinating glia and
      inhibits neurite outgrowth from post-natal neurons. MAG has a sialic acid binding
      site in its N-terminal domain and binds to specific sialylated glycans and
      gangliosides present on the surface of neurons, but the significance of these
      interactions in the effect of MAG on neurite outgrowth is unclear. Here we
      present evidence to suggest that recognition of sialylated glycans is essential
      for inhibition of neurite outgrowth by MAG. Arginine 118 on MAG is known to make 
      a key contact with sialic acid. We show that mutation of this residue reduces the
      potency of MAG inhibitory activity but that residual activity is also a result of
      carbohydrate recognition. We then go on to investigate gangliosides GT1b and GD1a
      as candidate MAG receptors. We show that MAG specifically binds both gangliosides
      and that both are expressed on the surface of MAG-responsive neurons.
      Furthermore, antibody cross-linking of cell surface GT1b, but not GD1a, mimics
      the effect of MAG, in that neurite outgrowth is inhibited through activation of
      Rho kinase. These data strongly suggest that interaction with GT1b on the
      neuronal cell surface is a potential mechanism for inhibition of neurite
      outgrowth by MAG.
FAU - Vinson, M
AU  - Vinson M
AD  - Neurology Centre of Excellence for Drug Discovery, GlaxoSmithKline, New Frontiers
      Science Park North, Third Ave., Harlow, Essex CM19 5AW, United Kingdom.
FAU - Strijbos, P J
AU  - Strijbos PJ
FAU - Rowles, A
AU  - Rowles A
FAU - Facci, L
AU  - Facci L
FAU - Moore, S E
AU  - Moore SE
FAU - Simmons, D L
AU  - Simmons DL
FAU - Walsh, F S
AU  - Walsh FS
LA  - eng
PT  - Journal Article
DEP - 20010306
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Enzyme Inhibitors)
RN  - 0 (Gangliosides)
RN  - 0 (Myelin-Associated Glycoprotein)
RN  - 59247-13-1 (trisialoganglioside GT1)
RN  - 94ZLA3W45F (Arginine)
RN  - EC 3.6.1.- (GTP Phosphohydrolases)
SB  - IM
MH  - Animals
MH  - Arginine/metabolism
MH  - Cells, Cultured
MH  - Enzyme Inhibitors/pharmacology
MH  - Enzyme-Linked Immunosorbent Assay
MH  - GTP Phosphohydrolases/metabolism
MH  - Gangliosides/*metabolism
MH  - Immunohistochemistry
MH  - Myelin-Associated Glycoprotein/chemistry/*metabolism
MH  - *Neurites
MH  - Protein Binding
MH  - Rats
EDAT- 2001/03/30 10:00
MHDA- 2001/07/13 10:01
CRDT- 2001/03/30 10:00
PHST- 2001/03/30 10:00 [pubmed]
PHST- 2001/07/13 10:01 [medline]
PHST- 2001/03/30 10:00 [entrez]
AID - 10.1074/jbc.M100345200 [doi]
AID - M100345200 [pii]
PST - ppublish
SO  - J Biol Chem. 2001 Jun 8;276(23):20280-5. doi: 10.1074/jbc.M100345200. Epub 2001
      Mar 6.

PMID- 6200583
OWN - NLM
STAT- MEDLINE
DCOM- 19840504
LR  - 20071114
IS  - 0270-6474 (Print)
IS  - 0270-6474 (Linking)
VI  - 4
IP  - 3
DP  - 1984 Mar
TI  - The D1.1 antigen: a cell surface marker for germinal cells of the central nervous
      system.
PG  - 820-31
AB  - A monoclonal antibody against a cell surface ganglioside present on
      neuroepithelial cells was produced by immunizing mice with the B49 cell line, a
      clonal line with properties of both neurons and glial cells. The expression of
      this antigen, designated as D1.1, was analyzed in the developing rat cerebellum. 
      The D1.1 antigen was localized by the immunofluorescent staining method to
      germinal cells of the external granule layer (EGL). Fluorescent labeling of cells
      comprising the EGL was apparent on embryonic day 18 when the EGL first forms, and
      the labeling was present throughout the period of postnatal cerebellar
      development. No cells within the adult cerebellum were labeled with the anti-D1.1
      antibody. The D1.1-labeled cells of the EGL synthesize DNA, as demonstrated by
      [3H] thymidine autoradiography. However, within 48 hr after their final mitosis, 
      nascent cerebellar cells that had migrated away from the external granule layer
      were no longer labeled with antibody. Some of the neurons and some of the
      astrocytes in cerebellar cell cultures were fluorescently labeled with the
      anti-D1.1 antibody. The number of anti-D1.1-labeled neurons in the cultures
      decreased over the first 10 days in vitro in agreement with the findings that in 
      vivo the fluorescent labeling of the D1.1 antigen disappears from postmitotic
      cells. The antibody recognizes a ganglioside that in thin layer chromatographic
      experiments has a mobility between that of the GM1 and GM2 ganglioside. These
      data suggest that the D1.1 ganglioside antigen is a cell surface marker for
      germinal cells and that the acquisition and subsequent loss of this antigen is an
      aspect of the biochemical maturation of neurons and glial cells.
FAU - Levine, J M
AU  - Levine JM
FAU - Beasley, L
AU  - Beasley L
FAU - Stallcup, W B
AU  - Stallcup WB
LA  - eng
GR  - NS 16112/NS/NINDS NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - J Neurosci
JT  - The Journal of neuroscience : the official journal of the Society for
      Neuroscience
JID - 8102140
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens, Surface)
RN  - 0 (Epitopes)
RN  - 0 (Gangliosides)
SB  - IM
MH  - Animals
MH  - Antibodies, Monoclonal
MH  - Antigens, Surface/*analysis
MH  - Brain/cytology/embryology/*growth & development
MH  - Cell Differentiation
MH  - Cell Line
MH  - Cerebellum/*cytology
MH  - Epitopes/immunology
MH  - Fluorescent Antibody Technique
MH  - Gangliosides/immunology
MH  - Hybridomas/immunology
MH  - Mice
MH  - Neurons/*immunology
MH  - Rats
EDAT- 1984/03/01 00:00
MHDA- 1984/03/01 00:01
CRDT- 1984/03/01 00:00
PHST- 1984/03/01 00:00 [pubmed]
PHST- 1984/03/01 00:01 [medline]
PHST- 1984/03/01 00:00 [entrez]
PST - ppublish
SO  - J Neurosci. 1984 Mar;4(3):820-31.

PMID- 8253783
OWN - NLM
STAT- MEDLINE
DCOM- 19940113
LR  - 20061115
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 268
IP  - 35
DP  - 1993 Dec 15
TI  - Novel gangliosides containing the sialyl-Le(a) structure from a human rectal
      adenocarcinoma.
PG  - 26541-5
AB  - Oligosaccharides were released from the gangliosides of a human rectal
      adenocarcinoma with endoglycoceramidase (Rhodococcus sp. G-74-2) and then
      purified by affinity chromatography on a column of an immobilized monoclonal
      antibody, MSW 113. Structural studies, involving 600-MHz 1H NMR spectrometry,
      indicated the structures of these compounds to be as follows. [formula: see text]
      Three of these oligosaccharides, 2, 3, and 4, are novel as to ganglioside sugar
      chains and contain both lacto series types 1 and 2 chains. Oligosaccharides 3 and
      4 are unique in that they contain the sialyl-Le(a)-X structure in linear and
      branched structures. Gangliosides with the oligosaccharide structures presented
      above might be new potential tumor markers.
FAU - Kitagawa, H
AU  - Kitagawa H
AD  - Department of Biological Chemistry, Faculty of Pharmaceutical Sciences, Kyoto
      University, Japan.
FAU - Nakada, H
AU  - Nakada H
FAU - Fukui, S
AU  - Fukui S
FAU - Funakoshi, I
AU  - Funakoshi I
FAU - Kawasaki, T
AU  - Kawasaki T
FAU - Tate, S
AU  - Tate S
FAU - Inagaki, F
AU  - Inagaki F
FAU - Yamashina, I
AU  - Yamashina I
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Gangliosides)
RN  - 91847-18-6 (sialyl Le(a) ganglioside)
SB  - IM
MH  - Adenocarcinoma/*chemistry
MH  - Antigens, Tumor-Associated, Carbohydrate/chemistry/*isolation & purification
MH  - Carbohydrate Conformation
MH  - Carbohydrate Sequence
MH  - Chromatography, Affinity
MH  - Chromatography, High Pressure Liquid
MH  - Chromatography, Thin Layer
MH  - Gangliosides/*isolation & purification
MH  - Humans
MH  - Magnetic Resonance Spectroscopy
MH  - Molecular Sequence Data
MH  - Rectal Neoplasms/*chemistry
MH  - Spectrometry, Mass, Fast Atom Bombardment
EDAT- 1993/12/15 00:00
MHDA- 1993/12/15 00:01
CRDT- 1993/12/15 00:00
PHST- 1993/12/15 00:00 [pubmed]
PHST- 1993/12/15 00:01 [medline]
PHST- 1993/12/15 00:00 [entrez]
PST - ppublish
SO  - J Biol Chem. 1993 Dec 15;268(35):26541-5.

id: 9398638 Error occurred: The following PMID is not available: 9398638

PMID- 2747606
OWN - NLM
STAT- MEDLINE
DCOM- 19890817
LR  - 20151119
IS  - 0301-4894 (Print)
IS  - 0301-4894 (Linking)
VI  - 90
IP  - 2
DP  - 1989 Feb
TI  - [Monoclonal antibody NCC-ST-439 in gastric cancer tissue].
PG  - 222-7
AB  - An immunohistochemical study revealed that NCC-ST-439 positive tumor were
      detected in 33% of the 244 gastric carcinomas. The incidence of NCC-ST-439
      immunoactivity in well differentiated adenocarcinomas (papillary and tubular
      adenocarcinoma) was significantly higher than in poorly differentiated
      adenocarcinomas (including signet-ring cell and mucinous adenocarcinoma).
      Moreover, NCC-ST-439 immunoreactive tumors showed more frequent vessel invasion
      and higher DNA content than non-reactive tumors. The recurrence rates of
      NCC-ST-439 immunoreactive tumors in the liver and lymph nodes were significantly 
      higher than those of non-reactive tumors. Patients with NCC-ST-439 immunoreactive
      carcinoma had much worse prognosis than those with NCC-ST-439 non-reactive
      carcinoma. These results suggest that NCC-ST-439 antigen produced by tumor cells 
      plays an important role in the invasive growth and vessel invasion and also
      serves as a biological marker of malignancy in patients with gastric cancer.
FAU - Kamata, T
AU  - Kamata T
AD  - Second Department of Surgery, Kanazawa University School, Japan.
FAU - Yoneumura, Y
AU  - Yoneumura Y
FAU - Sugiyama, K
AU  - Sugiyama K
FAU - Yamaguchi, A
AU  - Yamaguchi A
FAU - Miwa, K
AU  - Miwa K
FAU - Miyazaki, I
AU  - Miyazaki I
LA  - jpn
PT  - English Abstract
PT  - Journal Article
PL  - Japan
TA  - Nihon Geka Gakkai Zasshi
JT  - Nihon Geka Gakkai zasshi
JID - 0405405
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens, Neoplasm)
RN  - 0 (Biomarkers, Tumor)
RN  - 0 (DNA, Neoplasm)
SB  - IM
MH  - Adenocarcinoma/immunology/secondary
MH  - *Antibodies, Monoclonal
MH  - Antigens, Neoplasm/analysis
MH  - Biomarkers, Tumor/analysis
MH  - Cell Nucleus/analysis
MH  - DNA, Neoplasm/analysis
MH  - Humans
MH  - Immunohistochemistry
MH  - Liver Neoplasms/secondary
MH  - Lymphatic Metastasis
MH  - Neoplasm Invasiveness
MH  - Neoplasm Staging
MH  - Prognosis
MH  - Stomach Neoplasms/*immunology/mortality/pathology
EDAT- 1989/02/01 00:00
MHDA- 1989/02/01 00:01
CRDT- 1989/02/01 00:00
PHST- 1989/02/01 00:00 [pubmed]
PHST- 1989/02/01 00:01 [medline]
PHST- 1989/02/01 00:00 [entrez]
PST - ppublish
SO  - Nihon Geka Gakkai Zasshi. 1989 Feb;90(2):222-7.

PMID- 3891385
OWN - NLM
STAT- MEDLINE
DCOM- 19850813
LR  - 20101118
IS  - 0014-4827 (Print)
IS  - 0014-4827 (Linking)
VI  - 158
IP  - 2
DP  - 1985 Jun
TI  - Spatial interrelationships between proteoglycans and extracellular matrix
      proteins in cell cultures.
PG  - 321-32
AB  - Immunolabelling of cultured cells for chondroitin-sulfate proteoglycan (CSPG), in
      conjunction with antibodies to fibronectin, collagen and laminin, revealed the
      spatial interrelationships between the different matrix components. CSPG was
      organized in two major forms. Fibronectin-independent dotted patterns of CSPG
      were detected on the substrate and cell surfaces at early stages after plating.
      At later stages, however, significant overlapping was found between the two
      extracellular matrix components. Immunoelectron microscopic examination indicated
      that the CSPG was organized as granules of varying sizes which were associated
      with the cell surface, the substrate, or with the periphery of the fibronectin
      network.
FAU - Avnur, Z
AU  - Avnur Z
FAU - Geiger, B
AU  - Geiger B
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Exp Cell Res
JT  - Experimental cell research
JID - 0373226
RN  - 0 (Chondroitin Sulfate Proteoglycans)
RN  - 0 (Fibronectins)
RN  - 0 (Laminin)
RN  - 0 (Proteins)
RN  - 0 (Proteoglycans)
RN  - 9007-34-5 (Collagen)
SB  - IM
MH  - Animals
MH  - Cells, Cultured
MH  - Chick Embryo
MH  - Chondroitin Sulfate Proteoglycans/metabolism
MH  - Collagen/metabolism
MH  - Extracellular Matrix/metabolism/*ultrastructure
MH  - Fibronectins/metabolism
MH  - Fluorescent Antibody Technique
MH  - Laminin/metabolism
MH  - Microscopy, Electron
MH  - Proteins/*metabolism
MH  - Proteoglycans/*metabolism
MH  - Tissue Distribution
EDAT- 1985/06/01 00:00
MHDA- 1985/06/01 00:01
CRDT- 1985/06/01 00:00
PHST- 1985/06/01 00:00 [pubmed]
PHST- 1985/06/01 00:01 [medline]
PHST- 1985/06/01 00:00 [entrez]
PST - ppublish
SO  - Exp Cell Res. 1985 Jun;158(2):321-32.

PMID- 3143700
OWN - NLM
STAT- MEDLINE
DCOM- 19890123
LR  - 20190510
IS  - 0910-5050 (Print)
IS  - 0910-5050 (Linking)
VI  - 79
IP  - 10
DP  - 1988 Oct
TI  - Production of monoclonal antibodies directed against carbohydrate moieties of
      cell surface glycoproteins.
PG  - 1119-29
AB  - Through the use of a technique for raising monoclonal antibodies, coupled with a 
      solid-phase radioimmunoassay utilizing immobilized glycopeptides prepared from
      the surface membranes of the colorectal cancer cells (LS 180) used for the
      immunization, carbohydrate-directed monoclonal antibodies were obtained. One of
      the monoclonal antibodies, MLS 102, reacted immunohistochemically intensely with 
      the colorectal cancer cell surface and the mucinous glycoproteins secreted by the
      cancer cells, but only weakly with normal colon tissue. The antigenic determinant
      recognized by MLS 102 was the carbohydrate moiety of glycoproteins with terminal 
      sialic acid. The antigens defined by other monoclonal antibodies, MLS 103 and
      104, were immunohistochemically detected in both normal colonic epithelial and
      cancer cells. These antibodies seemed to recognize the carbohydrate moieties of
      both glycoproteins and glycolipids. The method described in this report can be
      generally applied to raise cell surface carbohydrate-directed antibodies.
FAU - Fukui, S
AU  - Fukui S
AD  - Department of Biological Chemistry, Faculty of Pharmaceutical Sciences, Kyoto
      University.
FAU - Numata, Y
AU  - Numata Y
FAU - Kurosaka, A
AU  - Kurosaka A
FAU - Kitagawa, H
AU  - Kitagawa H
FAU - Nakada, H
AU  - Nakada H
FAU - Funakoshi, I
AU  - Funakoshi I
FAU - Kawasaki, T
AU  - Kawasaki T
FAU - Takahashi, Y
AU  - Takahashi Y
FAU - Hayashi, K
AU  - Hayashi K
FAU - Yamashina, I
AU  - Yamashina I
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - Japan
TA  - Jpn J Cancer Res
JT  - Japanese journal of cancer research : Gann
JID - 8509412
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens, Neoplasm)
RN  - 0 (Carbohydrates)
RN  - 0 (Glycolipids)
RN  - 0 (Glycoproteins)
SB  - IM
MH  - Animals
MH  - *Antibodies, Monoclonal/biosynthesis
MH  - Antigens, Neoplasm/analysis
MH  - Carbohydrates/*analysis/immunology
MH  - Cell Fusion
MH  - Glycolipids/analysis
MH  - Glycoproteins/*analysis/immunology
MH  - Humans
MH  - Hybridomas
MH  - Immunohistochemistry
MH  - Male
MH  - Mice
MH  - Mice, Inbred BALB C
PMC - PMC5917637
EDAT- 1988/10/01 00:00
MHDA- 1988/10/01 00:01
CRDT- 1988/10/01 00:00
PHST- 1988/10/01 00:00 [pubmed]
PHST- 1988/10/01 00:01 [medline]
PHST- 1988/10/01 00:00 [entrez]
AID - 10.1111/j.1349-7006.1988.tb01535.x [doi]
PST - ppublish
SO  - Jpn J Cancer Res. 1988 Oct;79(10):1119-29. doi:
      10.1111/j.1349-7006.1988.tb01535.x.

PMID- 16965854
OWN - NLM
STAT- MEDLINE
DCOM- 20070604
LR  - 20081121
IS  - 0304-3835 (Print)
IS  - 0304-3835 (Linking)
VI  - 249
IP  - 2
DP  - 2007 May 8
TI  - Biological significance of cancer-associated sialyl-Tn antigen: modulation of
      malignant phenotype in gastric carcinoma cells.
PG  - 157-70
AB  - The activation of an abnormal glycosylation pathway in cancer cells leads to the 
      formation of the sialyl-Tn antigen, blocking regular carbohydrate chain
      elongation. Sialyl-Tn antigen is rarely expressed in normal tissues but is
      aberrantly expressed in a variety of carcinomas, where it constitutes a marker of
      poor prognosis. Although the clinical significance of sialyl-Tn is well
      characterized, a functional role for this glycan and its contribution to cancer
      progression remain to be elucidated. This study evaluates the capability of
      sialyl-Tn to modify processes like cell cycle, apoptosis, actin cytoskeleton
      dynamics, adhesion and motility on ECM components, cell-cell aggregation and
      invasion. De-novo expression of sialyl-Tn leads to major morphological and cell
      behavior alterations in gastric carcinoma cells which were reverted by specific
      antibody blockage. Sialyl-Tn antigen is able to modulate a malignant phenotype
      inducing a more aggressive cell behavior, such as decreased cell-cell aggregation
      and increased ECM adhesion, migration and invasion.
FAU - Pinho, Sandra
AU  - Pinho S
AD  - Institute of Molecular Pathology and Immunology of the University of Porto
      (IPATIMUP), Rua Dr. Roberto Frias, s/n 4200-465 Porto, Portugal.
FAU - Marcos, Nuno T
AU  - Marcos NT
FAU - Ferreira, Bibiana
AU  - Ferreira B
FAU - Carvalho, Ana S
AU  - Carvalho AS
FAU - Oliveira, Maria J
AU  - Oliveira MJ
FAU - Santos-Silva, Filipe
AU  - Santos-Silva F
FAU - Harduin-Lepers, Anne
AU  - Harduin-Lepers A
FAU - Reis, Celso A
AU  - Reis CA
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20060911
PL  - Ireland
TA  - Cancer Lett
JT  - Cancer letters
JID - 7600053
RN  - 0 (Antigens, Neoplasm)
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (MUC1 protein, human)
RN  - 0 (Mucin-1)
RN  - 0 (Mucins)
RN  - 0 (sialosyl-Tn antigen)
RN  - EC 2.4.99.- (Sialyltransferases)
RN  - EC 2.4.99.- (galactosyl-1-3-N-acetylgalactosaminyl-specific
      2,6-sialyltransferase)
RN  - EC 2.4.99.3 (CMP-N-acetylneuraminate-alpha-N-acetylgalactosaminide
      alpha-2,6-sialyltransferase)
SB  - IM
MH  - Antigens, Neoplasm/metabolism
MH  - Antigens, Tumor-Associated, Carbohydrate/*metabolism
MH  - Apoptosis
MH  - Carcinoma/*metabolism/pathology
MH  - Cell Adhesion
MH  - Cell Aggregation
MH  - Cell Line, Tumor
MH  - Cell Movement
MH  - Cell Proliferation
MH  - Humans
MH  - Mucin-1
MH  - Mucins/metabolism
MH  - Neoplasm Invasiveness
MH  - Phenotype
MH  - Sialyltransferases/genetics
MH  - Stomach Neoplasms/*metabolism/pathology
EDAT- 2006/09/13 09:00
MHDA- 2007/06/05 09:00
CRDT- 2006/09/13 09:00
PHST- 2006/06/27 00:00 [received]
PHST- 2006/08/07 00:00 [revised]
PHST- 2006/08/09 00:00 [accepted]
PHST- 2006/09/13 09:00 [pubmed]
PHST- 2007/06/05 09:00 [medline]
PHST- 2006/09/13 09:00 [entrez]
AID - S0304-3835(06)00506-4 [pii]
AID - 10.1016/j.canlet.2006.08.010 [doi]
PST - ppublish
SO  - Cancer Lett. 2007 May 8;249(2):157-70. doi: 10.1016/j.canlet.2006.08.010. Epub
      2006 Sep 11.

PMID- 10644674
OWN - NLM
STAT- MEDLINE
DCOM- 20000229
LR  - 20190508
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 275
IP  - 4
DP  - 2000 Jan 28
TI  - Structural analysis of glycosaminoglycans in Drosophila and Caenorhabditis
      elegans and demonstration that tout-velu, a Drosophila gene related to EXT tumor 
      suppressors, affects heparan sulfate in vivo.
PG  - 2269-75
AB  - We have devised a sensitive method for the isolation and structural analysis of
      glycosaminoglycans from two genetically tractable model organisms, the fruit fly,
      Drosophila melanogaster, and the nematode, Caenorhabditis elegans. We detected
      chondroitin/chondroitin sulfate- and heparan sulfate-derived disaccharides in
      both organisms. Chondroitinase digestion of glycosaminoglycans from adult
      Drosophila produced both nonsulfated and 4-O-sulfated unsaturated disaccharides, 
      whereas only unsulfated forms were detected in C. elegans. Heparin lyases
      released disaccharides bearing N-, 2-O-, and 6-O-sulfated species, including
      mono-, di-, and trisulfated forms. We observed tissue- and stage-specific
      differences in both chondroitin sulfate and heparan sulfate composition in
      Drosophila. We have also applied these methods toward the analysis of tout-velu, 
      an EXT-related gene in Drosophila that controls the tissue distribution of the
      growth factor Hedgehog. The proteins encoded by the vertebrate tumor suppressor
      genes EXT1 and 2, show heparan sulfate co-polymerase activity, and it has been
      proposed that tout-velu affects Hedgehog activity via its role in heparan sulfate
      biosynthesis. Analysis of total glycosaminoglycans from tout-velu mutant larvae
      show marked reductions in heparan sulfate but not chondroitin sulfate, consistent
      with its proposed function as a heparan sulfate co-polymerase.
FAU - Toyoda, H
AU  - Toyoda H
AD  - Department of Molecular Biology, University of Arizona, Tucson, Arizona 85721,
      USA.
FAU - Kinoshita-Toyoda, A
AU  - Kinoshita-Toyoda A
FAU - Selleck, S B
AU  - Selleck SB
LA  - eng
GR  - GM-25243/GM/NIGMS NIH HHS/United States
GR  - GM-54832/GM/NIGMS NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Drosophila Proteins)
RN  - 0 (Membrane Proteins)
RN  - 0 (tout-velu protein, Drosophila)
RN  - 9050-30-0 (Heparitin Sulfate)
SB  - IM
MH  - Animals
MH  - Caenorhabditis elegans/*metabolism
MH  - Carbohydrate Conformation
MH  - Cattle
MH  - Chromatography, High Pressure Liquid
MH  - Drosophila/genetics/growth & development/*metabolism
MH  - *Drosophila Proteins
MH  - *Genes, Tumor Suppressor
MH  - Heparitin Sulfate/*metabolism
MH  - Membrane Proteins/*genetics
EDAT- 2000/01/25 09:00
MHDA- 2000/03/04 09:00
CRDT- 2000/01/25 09:00
PHST- 2000/01/25 09:00 [pubmed]
PHST- 2000/03/04 09:00 [medline]
PHST- 2000/01/25 09:00 [entrez]
AID - 10.1074/jbc.275.4.2269 [doi]
PST - ppublish
SO  - J Biol Chem. 2000 Jan 28;275(4):2269-75. doi: 10.1074/jbc.275.4.2269.

PMID- 1698709
OWN - NLM
STAT- MEDLINE
DCOM- 19901115
LR  - 20151119
IS  - 0272-457X (Print)
IS  - 0272-457X (Linking)
VI  - 9
IP  - 4
DP  - 1990 Aug
TI  - Characterization of an antigen defined by monoclonal antibody KMO1.
PG  - 363-75
AB  - We have isolated an antigen defined by the monoclonal antibody KMO1 from tissue
      culture supernatant as a glycoprotein and from cancer cells as a glycolipid. The 
      antigenic determinant was a carbohydrate. Antibody KMO1 inhibited the binding
      activity of 19-9 to CA19-9, but 19-9 antibody did not inhibited the binding
      activity of KMO1 to KMO1 antigen. The glycolipid antigen of KMO1 was a
      monosialoganglioside and was separated into 3 components on thin layer
      chromatography. The 19-9 antibody reacted with one of the components. These
      results suggest that the KMO1 antigen is similar to but not identical to CA19-9.
FAU - Kano, Y
AU  - Kano Y
AD  - Research Division, Green Cross Corporation, Hirakata, Japan.
FAU - Taniguchi, T
AU  - Taniguchi T
FAU - Uemura, Y
AU  - Uemura Y
FAU - Yokoyama, K
AU  - Yokoyama K
FAU - Uesaka, K
AU  - Uesaka K
FAU - Yamamoto, M
AU  - Yamamoto M
FAU - Ohyanagi, H
AU  - Ohyanagi H
FAU - Saitoh, Y
AU  - Saitoh Y
LA  - eng
PT  - Journal Article
PL  - United States
TA  - Hybridoma
JT  - Hybridoma
JID - 8202424
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens, Neoplasm)
RN  - 0 (Biomarkers, Tumor)
RN  - 0 (Carbohydrates)
RN  - 0 (Epitopes)
RN  - 0 (Gangliosides)
RN  - 0 (Glycolipids)
RN  - 0 (Glycoproteins)
SB  - IM
MH  - Animals
MH  - Antibodies, Monoclonal
MH  - Antigens, Neoplasm/blood/*isolation & purification
MH  - Biomarkers, Tumor/immunology/*isolation & purification
MH  - Carbohydrates/immunology
MH  - Chromatography, Affinity
MH  - Epitopes/immunology
MH  - Gangliosides/immunology/isolation & purification
MH  - Glycolipids/immunology/isolation & purification
MH  - Glycoproteins/immunology/isolation & purification
MH  - Humans
MH  - Mice
MH  - Mice, Inbred BALB C
MH  - Molecular Weight
MH  - Tumor Cells, Cultured/immunology
EDAT- 1990/08/01 00:00
MHDA- 1990/08/01 00:01
CRDT- 1990/08/01 00:00
PHST- 1990/08/01 00:00 [pubmed]
PHST- 1990/08/01 00:01 [medline]
PHST- 1990/08/01 00:00 [entrez]
AID - 10.1089/hyb.1990.9.363 [doi]
PST - ppublish
SO  - Hybridoma. 1990 Aug;9(4):363-75. doi: 10.1089/hyb.1990.9.363.

PMID- 7174794
OWN - NLM
STAT- MEDLINE
DCOM- 19830214
LR  - 20181113
IS  - 0021-9738 (Print)
IS  - 0021-9738 (Linking)
VI  - 70
IP  - 6
DP  - 1982 Dec
TI  - Surface modifications in the platelets of a patient with
      alpha-N-acetyl-D-galactosamine residues, the Tn-syndrome.
PG  - 1281-91
AB  - The Tn-syndrome is an acquired disorder characterized by the polyagglutination of
      blood cells and the pathological exposure of alpha-N-acetyl-D-galactosamine
      residues (Tn-antigen) at the cell surface. We now report studies on the platelet 
      of a patient (Ba.) of which 81% reacted positively with a fluorescein conjugate
      of Helix pomatia agglutinin (HPA). The surface proteins of Ba. platelets were
      labeled with 125I by the lactoperoxidase-catalyzed procedure; single and
      two-dimensional electrophoresis on sodium dodecyl sulfate (SDS)-polyacrylamide
      gels was followed by autoradiography that revealed normal 125I-labeling of the
      major membrane glycoproteins (GP) but that GP Ib had a faster than normal
      migration. the abnormal GP Ib of Ba. platelets was strongly labeled when platelet
      suspensions were treated sequentially with neuraminidase, galactose oxidase, and 
      sodium [3H]borohydride. Unlike the GP Ib of normal human platelets, it was also
      strongly labeled when Ba. platelets were treated with galactose oxidase and
      sodium [3H]borohydride alone. Both the alloantigen, PlA1, and quinidine-dependent
      antibody receptor activity were normally expressed by Ba. platelets, which also
      bound a monoclonal antibody (AN51) to GP Ib. Analysis of Ba. platelets by crossed
      immunoelectrophoresis using a rabbit anti-human platelet antibody preparation
      revealed the presence of an immunoprecipitate in the GP Ib position that had an
      abnormal appearance and migration in the second dimension. An altered position of
      the precipitate given by Factor VIIIR:Ag was also noted. Incorporation of HPA
      into the agarose gel during the first dimension electrophoresis resulted in the
      specific precipitation of the abnormal GP Ib of Ba. platelets. Our studies show
      that circulating Tn-platelets contain GP Ib with a modified oligosaccharide chain
      structure responsible for the platelet expression of Tn-antigen activity.
FAU - Nurden, A T
AU  - Nurden AT
FAU - Dupuis, D
AU  - Dupuis D
FAU - Pidard, D
AU  - Pidard D
FAU - Kieffer, N
AU  - Kieffer N
FAU - Kunicki, T J
AU  - Kunicki TJ
FAU - Cartron, J P
AU  - Cartron JP
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - J Clin Invest
JT  - The Journal of clinical investigation
JID - 7802877
RN  - 0 (Antigens, Surface)
RN  - 0 (Glycoproteins)
RN  - 0 (Lectins)
RN  - 0 (Membrane Proteins)
RN  - 7535-00-4 (Galactosamine)
RN  - KM15WK8O5T (Acetylgalactosamine)
SB  - AIM
SB  - IM
MH  - Acetylgalactosamine/*immunology
MH  - Antigens, Surface/analysis
MH  - Blood Platelet Disorders/*blood/immunology
MH  - Blood Platelets/analysis/*immunology
MH  - Galactosamine/*analogs & derivatives
MH  - Glycoproteins/*blood/immunology
MH  - Helix (Snails)
MH  - Humans
MH  - Isoelectric Point
MH  - Lectins
MH  - Membrane Proteins/analysis
MH  - Molecular Weight
MH  - Syndrome
PMC - PMC370345
EDAT- 1982/12/01 00:00
MHDA- 1982/12/01 00:01
CRDT- 1982/12/01 00:00
PHST- 1982/12/01 00:00 [pubmed]
PHST- 1982/12/01 00:01 [medline]
PHST- 1982/12/01 00:00 [entrez]
PST - ppublish
SO  - J Clin Invest. 1982 Dec;70(6):1281-91.

PMID- 16144911
OWN - NLM
STAT- MEDLINE
DCOM- 20051101
LR  - 20061115
IS  - 1078-0432 (Print)
IS  - 1078-0432 (Linking)
VI  - 11
IP  - 17
DP  - 2005 Sep 1
TI  - Enhanced production of interleukin 6 in peripheral blood monocytes stimulated
      with mucins secreted into the bloodstream.
PG  - 6127-32
AB  - PURPOSE: It has been reported that tumor progression is correlated with the serum
      level of interleukin 6 (IL-6). The purpose of this study was to investigate by
      what mechanism, other than production from tumor cell, the serum level of IL-6 is
      elevated in the tumor-bearing state. EXPERIMENTAL DESIGN: Monocytes from healthy 
      donors were cultured in the presence of sera from colon cancer patients, and the 
      activity to elevate IL-6 production was estimated. This activity of serum was
      also examined after various biochemical treatments. RESULTS: When monocytes from 
      healthy donors were cultured in the presence of sera from patients with colon
      cancer, secretion of IL-6 from the cells was markedly elevated. Serum proteins
      were fractionated on Sepharose 4B and the activity to elevate IL-6 production was
      found in the excluded fractions. Sialyl Tn antigen was detected in these same
      fractions. By excluding some mucins from the serum, the inducing activity was
      reduced to 40% of the original level. Furthermore, we purified mucins from the
      conditioned medium of colon cancer cells. Production of IL-6 was effectively
      elevated by a small amount of purified mucins in a dose-dependent manner. When
      the inducing activity was examined in the presence of binding or competitive
      inhibitors to the scavenger receptor, the effect was remarkably reduced.
      CONCLUSIONS: Mucins secreted from colon cancer cells into the bloodstream induce 
      production of IL-6 in peripheral blood monocytes through the scavenger receptor, 
      which may be responsible for the high level of serum IL-6 in colon cancer
      patients.
FAU - Yokoigawa, Norio
AU  - Yokoigawa N
AD  - Department of Surgery, Kansai Medical University, Moriguchi, Osaka, Japan.
FAU - Takeuchi, Noriko
AU  - Takeuchi N
FAU - Toda, Munetoyo
AU  - Toda M
FAU - Inoue, Mizue
AU  - Inoue M
FAU - Kaibori, Masaki
AU  - Kaibori M
FAU - Yanagida, Hidesuke
AU  - Yanagida H
FAU - Tanaka, Hironori
AU  - Tanaka H
FAU - Ogura, Tokuhiro
AU  - Ogura T
FAU - Takada, Hideho
AU  - Takada H
FAU - Okumura, Tadayoshi
AU  - Okumura T
FAU - Kwon, A-H
AU  - Kwon AH
FAU - Kamiyama, Yasuo
AU  - Kamiyama Y
FAU - Nakada, Hiroshi
AU  - Nakada H
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Clin Cancer Res
JT  - Clinical cancer research : an official journal of the American Association for
      Cancer Research
JID - 9502500
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Culture Media, Conditioned)
RN  - 0 (Interleukin-6)
RN  - 0 (Mucins)
RN  - 0 (Peptide Fragments)
RN  - 0 (Receptors, Immunologic)
RN  - 0 (Receptors, Scavenger)
RN  - 0 (sialosyl-Tn antigen)
SB  - IM
MH  - Aged
MH  - Aged, 80 and over
MH  - Antigens, Tumor-Associated, Carbohydrate/*metabolism
MH  - Cell Culture Techniques
MH  - Colonic Neoplasms/*blood
MH  - Culture Media, Conditioned/pharmacology
MH  - Female
MH  - Humans
MH  - Interleukin-6/*metabolism
MH  - Male
MH  - Middle Aged
MH  - Monocytes/*metabolism
MH  - Mucins/*pharmacology
MH  - Peptide Fragments/pharmacology
MH  - Receptors, Immunologic/antagonists & inhibitors/*metabolism
MH  - Receptors, Scavenger
MH  - Up-Regulation
EDAT- 2005/09/08 09:00
MHDA- 2005/11/03 09:00
CRDT- 2005/09/08 09:00
PHST- 2005/09/08 09:00 [pubmed]
PHST- 2005/11/03 09:00 [medline]
PHST- 2005/09/08 09:00 [entrez]
AID - 11/17/6127 [pii]
AID - 10.1158/1078-0432.CCR-05-0292 [doi]
PST - ppublish
SO  - Clin Cancer Res. 2005 Sep 1;11(17):6127-32. doi: 10.1158/1078-0432.CCR-05-0292.

PMID- 1471247
OWN - NLM
STAT- MEDLINE
DCOM- 19930122
LR  - 20041117
IS  - 0041-1132 (Print)
IS  - 0041-1132 (Linking)
VI  - 32
IP  - 9
DP  - 1992 Nov-Dec
TI  - Expression of the Tn antigen in myelodysplasia, lymphoma, and leukemia.
PG  - 834-8
AB  - Expression of the normally cryptic blood group antigen Tn has occasionally been
      reported in hematologic disease, but the true frequency of this change is not
      known. A mouse monoclonal antibody (FBT3) and immunohistochemistry were used to
      examine expression of the Tn antigen. Expression was not detected in 35 normal
      bone marrow aspirates examined, but it was detected in 5 of 725 abnormal bone
      marrow aspirates, including 2 (3.6%) of 55 cases of de novo acute nonlymphocytic 
      leukemia and 2 cases that terminated in acute nonlymphocytic leukemia. In two
      patients, one with acute myeloblastic leukemia and the other in blast
      transformation of chronic myeloid leukemia, the Tn antigen was expressed on 2
      percent of blast cells. In one case of non-Hodgkin's lymphoma, 4 percent of
      normal myeloid cells expressed the antigen. In the other two cases, one of acute 
      myelomonocytic leukemia and the other of myelodysplasia, only 2 to 8 percent of
      myeloid and erythroid cells initially were Tn positive. Subsequent serial
      immunohistochemical studies of bone marrow aspirates and peripheral blood in
      these two cases showed increasing numbers of Tn-positive erythroid and myeloid
      cells 8 to 12 months before polyagglutination was detected serologically.
      Tn-positive cells increased to > 90 percent in the terminal phase in both cases
      of both diseases. The results suggest that Tn expression in these two patients
      may have conferred a growth advantage to the cells and could be related to
      disease progression.
FAU - Roxby, D J
AU  - Roxby DJ
AD  - Hematology Department, Flinders Medical Centre, Bedford Park, Australia.
FAU - Pfeiffer, M B
AU  - Pfeiffer MB
FAU - Morley, A A
AU  - Morley AA
FAU - Kirkland, M A
AU  - Kirkland MA
LA  - eng
PT  - Case Reports
PT  - Journal Article
PL  - United States
TA  - Transfusion
JT  - Transfusion
JID - 0417360
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens, Neoplasm)
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Blood Group Antigens)
RN  - 0 (Tn antigen)
SB  - IM
MH  - Adult
MH  - Aged
MH  - Antibodies, Monoclonal
MH  - Antigens, Neoplasm/*analysis
MH  - *Antigens, Tumor-Associated, Carbohydrate
MH  - Blood Group Antigens/immunology
MH  - Female
MH  - Hematopoietic System/cytology/immunology
MH  - Humans
MH  - Leukemia/*immunology
MH  - Lymphoma/*immunology
MH  - Male
MH  - Middle Aged
MH  - Myelodysplastic Syndromes/*immunology
EDAT- 1992/11/01 00:00
MHDA- 1992/11/01 00:01
CRDT- 1992/11/01 00:00
PHST- 1992/11/01 00:00 [pubmed]
PHST- 1992/11/01 00:01 [medline]
PHST- 1992/11/01 00:00 [entrez]
PST - ppublish
SO  - Transfusion. 1992 Nov-Dec;32(9):834-8.

PMID- 2111348
OWN - NLM
STAT- MEDLINE
DCOM- 19900628
LR  - 20131121
IS  - 0022-1767 (Print)
IS  - 0022-1767 (Linking)
VI  - 144
IP  - 11
DP  - 1990 Jun 1
TI  - Northern hybridization analysis of VH gene expression in murine monoclonal
      antibodies directed to cancer-associated ganglioside antigens having various
      sialic acid linkages.
PG  - 4442-51
AB  - The expression of the VH genes in 46 murine hybridoma cells that secrete mAb
      directed to the cancer-associated carbohydrate Ag, especially acidic glycolipids 
      such as gangliosides and sulfated glycoplipids, was analyzed by Northern
      hybridization of poly(A)+ RNA of hybridoma with cDNA probes for nine VH gene
      families. Different hybridomas tended to express VH genes of the same family when
      the cognate Ag had the same or similar carbohydrate structures; i.e., the VH
      genes of the J558 family (group 1) were preferentially expressed in the mAb
      directed to various gangliosides that have NeuAc alpha (or NeuGc alpha) 2-3
      and/or 2-8 linkage (71%), the most common linkage of sialic acid residues in the 
      gangliosides of higher animals, and the hybridomas directed to sulfated
      glycolipids also expressed mainly the VH genes of the J558 family (80%). In
      contrast, the five mAb directed to various gangliosides with NeuAc alpha 2-6
      linkage were exclusively encoded by the VH genes of Q52 family (group 2, 100%),
      and three antibodies directed to gangliosides with a NeuAc alpha 2-9 linkage all 
      expressed genes of J606 family (group 6, 100%). The VH family usage was largely
      correlated with the linkage of sialic acid residues in the cognate carbohydrate
      Ag, but was not correlated at all with the difference in the fine specificities
      toward the core neutral carbohydrate chain, to which the sialic acid residues
      were attached. These findings suggest that the VH gene family in these
      anticarbohydrate antibodies is selected, depending primarily on the linkage of
      the sialic acid residues in carbohydrate Ag; these residues form the
      immunodominant sugar residue in the respective antigenic determinant.
FAU - Zenita, K
AU  - Zenita K
AD  - Department of Clinical Science and Laboratory Medicine, Kyoto University, School 
      of Medicine, Japan.
FAU - Hirashima, K
AU  - Hirashima K
FAU - Shigeta, K
AU  - Shigeta K
FAU - Hiraiwa, N
AU  - Hiraiwa N
FAU - Takada, A
AU  - Takada A
FAU - Hashimoto, K
AU  - Hashimoto K
FAU - Fujimoto, E
AU  - Fujimoto E
FAU - Yago, K
AU  - Yago K
FAU - Kannagi, R
AU  - Kannagi R
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - J Immunol
JT  - Journal of immunology (Baltimore, Md. : 1950)
JID - 2985117R
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antibodies, Neoplasm)
RN  - 0 (Gangliosides)
RN  - 0 (Glycolipids)
RN  - 0 (Immunoglobulin Heavy Chains)
RN  - 0 (Immunoglobulin Variable Region)
RN  - 0 (Sialic Acids)
RN  - 0 (Sulfates)
RN  - GZP2782OP0 (N-Acetylneuraminic Acid)
SB  - AIM
SB  - IM
MH  - Animals
MH  - Antibodies, Monoclonal/*genetics
MH  - Antibodies, Neoplasm/*genetics
MH  - Antibody Specificity
MH  - Blotting, Northern
MH  - Carbohydrate Sequence
MH  - Gangliosides/*immunology
MH  - Gene Expression
MH  - *Genes, Immunoglobulin
MH  - Glycolipids/immunology
MH  - Hybridomas/physiology
MH  - Immunoglobulin Heavy Chains/*genetics
MH  - Immunoglobulin Variable Region/*genetics
MH  - Mice
MH  - Molecular Sequence Data
MH  - N-Acetylneuraminic Acid
MH  - Sialic Acids/immunology
MH  - Structure-Activity Relationship
MH  - Sulfates/*immunology
EDAT- 1990/06/01 00:00
MHDA- 1990/06/01 00:01
CRDT- 1990/06/01 00:00
PHST- 1990/06/01 00:00 [pubmed]
PHST- 1990/06/01 00:01 [medline]
PHST- 1990/06/01 00:00 [entrez]
PST - ppublish
SO  - J Immunol. 1990 Jun 1;144(11):4442-51.

PMID- 15864747
OWN - NLM
STAT- MEDLINE
DCOM- 20051027
LR  - 20061115
IS  - 1021-7770 (Print)
IS  - 1021-7770 (Linking)
VI  - 12
IP  - 1
DP  - 2005
TI  - Further characterization of the binding properties of two monoclonal antibodies
      recognizing human Tn red blood cells.
PG  - 153-66
AB  - The terminal alpha anomeric Ga1NAc residue is an essential sugar for the Tn
      glycotope, human blood group A determinant, and Forssman antigen. In a previous
      study [King M.J., Parson S.F., Wu A,M., Jones N., Transfusion 31: 142-149, 1991] 
      we defined two monoclonal antibodies (MoAbs, BRIC66 and BRIC111) reacting with
      human Tn red blood cells. However, more advanced studies of these two MoAbs were 
      hampered by the lack of availability of Gal/GalNAc related glycotopes. In order
      to use these antibodies as powerful probes to elucidate structural changes during
      life processes, we have characterized in detail the combining sites of these two 
      MoAbs using enzyme-linked immunosorbent (ELISA) and inhibition assays with an
      extended glycan/ligand collection. From the results, it has been established that
      BRIC66 demonstrated multiple specificities and its reactivity towards glycotopes 
      was defined as: Ga1NAc alpha1-->Ser/Thr (Tn) > or = Ga1NAc alpha1-->3(LFuc
      alpha1-->2)Gal (Ah) > Ga1NAcalpha1-->3Galbeta1-->4Glc (AL) > Ga1NAalpha1-->3Gal
      (A) GalNAc alpha1-->3GalNAc >> Gal or Glc. Another MoAb, BRIC111, mainly bound
      Tn-glycophorin. The best ligand for this MoAb was Tn-containing glycopeptides
      (M.W. < 3.0 x 10(3) Da) from asialo ovine salivary mucin (OSM), which was
      approximately 70 and 58 times more active than Ga1NAc and monomeric Ga1NAc
      alpha1-->Ser/Thr (Tn), respectively, suggesting that the active glycotopes
      present in glycophorin for BRIC111 binding also exist in OSM. The N-acetyl group 
      at carbon-2 and configuration at carbon-2 and carbon-4 of the alpha anomeric
      Ga1NAc are required for the binding of either MoAb. Identification of these
      binding properties should aid in the selection of these MoAbs and the conditions 
      required for biological studies and clinical applications.
FAU - Wua, Albert M
AU  - Wua AM
AD  - Glyco-Immunochemistry Research Laboratory, Institute of Molecular and Cellular
      Biology, Taiwan. amwu@mail.cgu.edu.tw
FAU - Wub, June H
AU  - Wub JH
FAU - Kuoa, Hsiang-Wei
AU  - Kuoa HW
FAU - Herpa, Anthony
AU  - Herpa A
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - J Biomed Sci
JT  - Journal of biomedical science
JID - 9421567
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Glycoproteins)
RN  - 0 (Oligosaccharides)
RN  - 0 (Tn antigen)
SB  - IM
MH  - Animals
MH  - Antibodies, Monoclonal/*metabolism
MH  - Antigens, Tumor-Associated, Carbohydrate/*metabolism
MH  - Binding Sites
MH  - Erythrocytes/chemistry/*metabolism
MH  - Glycoproteins/chemistry/metabolism
MH  - Humans
MH  - Oligosaccharides/chemistry/metabolism
MH  - Protein Binding
MH  - Substrate Specificity
EDAT- 2005/05/03 09:00
MHDA- 2005/10/28 09:00
CRDT- 2005/05/03 09:00
PHST- 2004/07/01 00:00 [received]
PHST- 2004/10/01 00:00 [accepted]
PHST- 2005/05/03 09:00 [pubmed]
PHST- 2005/10/28 09:00 [medline]
PHST- 2005/05/03 09:00 [entrez]
AID - 10.1007/s11373-004-8179-3 [doi]
PST - ppublish
SO  - J Biomed Sci. 2005;12(1):153-66. doi: 10.1007/s11373-004-8179-3.

PMID- 15864746
OWN - NLM
STAT- MEDLINE
DCOM- 20051027
LR  - 20121115
IS  - 1021-7770 (Print)
IS  - 1021-7770 (Linking)
VI  - 12
IP  - 1
DP  - 2005
TI  - Polyvalent GalNAcalpha1-->Ser/Thr (Tn) and Galbeta1-->3GalNAcalpha1-->Ser/Thr (T 
      alpha) as the most potent recognition factors involved in Maclura pomifera
      agglutinin-glycan interactions.
PG  - 135-52
AB  - The agglutinin isolated from the seeds of Maclura pomifera (MPA) recognizes a
      mucin-type disaccharide sequence, Galbeta1-->3GalNAc (T) on a human erythrocyte
      membrane. We have utilized the enzyme-linked lectinosorbent assay (ELLSA) and
      inhibition assay to more systematically analyze the carbohydrate specificity of
      MPA with glyco-recognition factors and mammalian Gal/GalNAc structural units in
      lectin-glycoform interactions. From the results, it is concluded that the high
      densities of polyvalent GalNAcalpha1-->Ser/Thr (Tn) and
      Galbeta1-->3GalNAcalpha1-->Ser/Thr (T(alpha)) glycotopes in macromolecules are
      the most critical factors for MPA binding, being on a nanogram basis 2.0 x 10(5),
      4.6 x 10(4) and 3.9 x 10(4) more active than monovalent Gal, monomeric T and Tn
      glycotope, respectively. Other carbohydrate structural units in mammalian
      glycoconjugates, such as human blood group Sd (a+) related disaccharide
      (GalNAcbeta1-->4Gal) and Pk/P1 active disaccharide (Galalpha1-->4Gal) were
      inactive. These results demonstrate that the configurations of carbon-4 and
      carbon-2 are essential for MPA binding and establish the importance of affinity
      enhancement by high-density polyvalencies of Tn/T glycotopes in MPA-glycan
      interactions. The overall binding profile of MPA can be defined in decreasing
      order as high density of polyvalent Tn/T(alpha) (M.W. > 4.0 x 10(4)) >>
      Tn-containing glycopeptides (M.W. < 3.0 x 10(3)) > monomeric T/Tn and P
      (GalNAcbeta1-->3Gal) > GalNAc > Gal >> Man, L: ARA: , D: Fuc and Glc (inactive). 
      Our findings should aid in the selection of this lectin for elucidating functions
      of carbohydrate chains in life processes and for applications in the biomedical
      sciences.
FAU - Wu, Albert M
AU  - Wu AM
AD  - Glyco-Immunochemistry Research Laboratory, Institute of Molecular and Cellular
      Biology, College of Medicine, Chang-Gung University, Kweishan, Taoyuan 333,
      Taiwan. amwu@mail.cgu.edu.tw
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - J Biomed Sci
JT  - Journal of biomedical science
JID - 9421567
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Blood Group Antigens)
RN  - 0 (Glycoproteins)
RN  - 0 (Lectins)
RN  - 0 (Oligosaccharides)
RN  - 0 (Plant Lectins)
RN  - 0 (Tn antigen)
RN  - 27KFF3PMTU (maclurin)
RN  - 3554-90-3 (Thomsen-Friedenreich antigen)
SB  - IM
MH  - Animals
MH  - Antigens, Tumor-Associated, Carbohydrate/*metabolism
MH  - Blood Group Antigens/chemistry/metabolism
MH  - Carbohydrate Sequence
MH  - Erythrocytes/chemistry/cytology
MH  - Glycoproteins/*metabolism
MH  - Humans
MH  - Lectins/metabolism
MH  - Molecular Sequence Data
MH  - Oligosaccharides/chemistry/metabolism
MH  - Plant Lectins/*metabolism
EDAT- 2005/05/03 09:00
MHDA- 2005/10/28 09:00
CRDT- 2005/05/03 09:00
PHST- 2004/07/01 00:00 [received]
PHST- 2004/10/12 00:00 [accepted]
PHST- 2005/05/03 09:00 [pubmed]
PHST- 2005/10/28 09:00 [medline]
PHST- 2005/05/03 09:00 [entrez]
AID - 10.1007/s11373-004-8178-4 [doi]
PST - ppublish
SO  - J Biomed Sci. 2005;12(1):135-52. doi: 10.1007/s11373-004-8178-4.

PMID- 10852523
OWN - NLM
STAT- MEDLINE
DCOM- 20000713
LR  - 20171116
IS  - 0023-852X (Print)
IS  - 0023-852X (Linking)
VI  - 110
IP  - 6
DP  - 2000 Jun
TI  - Ki-67 (MIB1), p53, and Lewis-X (LeuM1) as prognostic factors of recurrence in T1 
      and T2 laryngeal carcinoma.
PG  - 1012-7
AB  - OBJECTIVES: Recently published data suggest a prognostic value of
      immunohistochemical proliferation markers for limited laryngeal carcinoma.
      Previous studies have reported contrasting findings on this issue. In this
      context, different treatment modalities may be responsible for contradictory
      findings. To study the relationship between proliferative activity--expressed by 
      the immunohistochemical labeling index of proliferation-associated markers Ki-67 
      (MIB1), Lewis-X (LeuM1), and proliferating cell nuclear antigen (PCNA) and by p53
      status--and treatment failure in a matched-pair study on recurrent and
      nonrecurrent T1 and T2 glottic carcinoma having received primary transoral laser 
      surgery. METHODS: Twenty-one patients with tumor recurrence were randomly
      selected and matched with 26 patients with nonrecurrent disease regarding
      histopathological grading and age. MIB1 staining was used to determine the Ki-67 
      labeling index, and LeuM1 staining for detecting the Lewis-X antigen;
      immunohistochemistry determined the p53 status and PCNA labeling index. RESULTS: 
      The Ki-67 labeling index was significantly (P = .001) higher in tumors from
      patients who had treatment failure (mean = 20.02%) than in patients who did not
      fail treatment ("nonfailures") (mean = 9.95%). Carcinoma with a Ki-67 (MIB1)
      labeling index above the median (15%) of the general study population showed a
      mean time to relapse of 23 months (n = 21), compared with 50 months for cases (n 
      = 26) below the median (P = .016). PCNA labeling index correlated less
      impressively with tumor recurrence (mean = 28.59% for treatment failures, mean = 
      21.75% for nonfailures, P = .022). Positive detection of the Lewis-X antigen was 
      significantly associated with recurrence (P = .015) and time to relapse (P =
      .006). Status of p53 was not a significant prognostic factor. CONCLUSION: The
      Ki-67 (MIB1) labeling index may be associated with early relapse of limited
      laryngeal carcinoma treated with transoral laser surgery. Since the prognostic
      relevance of Ki-67 seems to be different for radiological and surgical concepts
      of treatment, Ki-67 might become useful as criterion of therapy selection. The
      Lewis-X antigen, for the first time used on laryngeal carcinoma, seems to be a
      strong prognostic marker deserving further investigations.
FAU - Sittel, C
AU  - Sittel C
AD  - Department of Otorhinolaryngology--Head and Neck Surgery, University of Cologne, 
      Germany.
FAU - Eckel, H E
AU  - Eckel HE
FAU - Damm, M
AU  - Damm M
FAU - von Pritzbuer, E
AU  - von Pritzbuer E
FAU - Kvasnicka, H M
AU  - Kvasnicka HM
LA  - eng
PT  - Journal Article
PL  - United States
TA  - Laryngoscope
JT  - The Laryngoscope
JID - 8607378
RN  - 0 (Antigens, Neoplasm)
RN  - 0 (Antigens, Surface)
RN  - 0 (Ki-67 Antigen)
RN  - 0 (Leu-M1 antigen)
RN  - 0 (Lewis X Antigen)
RN  - 0 (Proliferating Cell Nuclear Antigen)
SB  - IM
MH  - Adult
MH  - Aged
MH  - Aged, 80 and over
MH  - Antigens, Neoplasm/metabolism
MH  - Antigens, Surface/*metabolism
MH  - Carcinoma, Squamous Cell/genetics/*metabolism
MH  - Female
MH  - Follow-Up Studies
MH  - *Genes, p53
MH  - Humans
MH  - Immunohistochemistry
MH  - Ki-67 Antigen/*metabolism
MH  - Laryngeal Neoplasms/genetics/*metabolism
MH  - Lewis X Antigen
MH  - Male
MH  - Middle Aged
MH  - Neoplasm Recurrence, Local/genetics/*metabolism
MH  - Neoplasm Staging
MH  - Prognosis
MH  - Proliferating Cell Nuclear Antigen/genetics/metabolism
EDAT- 2000/06/14 09:00
MHDA- 2000/07/15 11:00
CRDT- 2000/06/14 09:00
PHST- 2000/06/14 09:00 [pubmed]
PHST- 2000/07/15 11:00 [medline]
PHST- 2000/06/14 09:00 [entrez]
AID - 10.1097/00005537-200006000-00024 [doi]
PST - ppublish
SO  - Laryngoscope. 2000 Jun;110(6):1012-7. doi: 10.1097/00005537-200006000-00024.

PMID- 3258005
OWN - NLM
STAT- MEDLINE
DCOM- 19880413
LR  - 20190508
IS  - 0022-1007 (Print)
IS  - 0022-1007 (Linking)
VI  - 167
IP  - 2
DP  - 1988 Feb 1
TI  - Expression of Ley antigen in human immunodeficiency virus-infected human T cell
      lines and in peripheral lymphocytes of patients with acquired immune deficiency
      syndrome (AIDS) and AIDS-related complex (ARC).
PG  - 323-31
AB  - Ley determinant (Fuc alpha 1----2Gal beta 1----4[Fuc alpha 1----3]GlcNAc beta
      1----R) defined by mAb BM-1 is highly expressed in human immunodeficiency virus
      (HIV)-infected T cell lines and in CD3+ peripheral mature T cells of patients
      with acquired immune deficiency syndrome (AIDS) or with AIDS-related complex
      (ARC). Ley expression increased greatly in the CD3+ population in the advanced
      stage of AIDS when the CD4+ population decreased greatly. Six other carbohydrate 
      antigens tested by their respective mAbs were not detected in these same cells.
      None of the carbohydrate antigens tested by the seven mAbs used in this study
      were found in noninfected T cell lines and in normal peripheral blood
      lymphocytes.
FAU - Adachi, M
AU  - Adachi M
AD  - Japan Immunoresearch Laboratories, Takasaki.
FAU - Hayami, M
AU  - Hayami M
FAU - Kashiwagi, N
AU  - Kashiwagi N
FAU - Mizuta, T
AU  - Mizuta T
FAU - Ohta, Y
AU  - Ohta Y
FAU - Gill, M J
AU  - Gill MJ
FAU - Matheson, D S
AU  - Matheson DS
FAU - Tamaoki, T
AU  - Tamaoki T
FAU - Shiozawa, C
AU  - Shiozawa C
FAU - Hakomori, S
AU  - Hakomori S
LA  - eng
GR  - CA-42505/CA/NCI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - J Exp Med
JT  - The Journal of experimental medicine
JID - 2985109R
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Glycosphingolipids)
RN  - 0 (Lewis Blood-Group System)
RN  - 104200-12-6 (Le(y)-active trifucosylnonaosylceramide)
SB  - IM
SB  - X
MH  - AIDS-Related Complex/*immunology
MH  - Acquired Immunodeficiency Syndrome/*immunology
MH  - Antibodies, Monoclonal/immunology
MH  - Antigen-Antibody Reactions
MH  - Cell Line
MH  - Glycosphingolipids/*analysis
MH  - HIV/*immunology
MH  - Humans
MH  - Lewis Blood-Group System/immunology
MH  - T-Lymphocytes/analysis/*immunology
PMC - PMC2188859
EDAT- 1988/02/01 00:00
MHDA- 1988/02/01 00:01
CRDT- 1988/02/01 00:00
PHST- 1988/02/01 00:00 [pubmed]
PHST- 1988/02/01 00:01 [medline]
PHST- 1988/02/01 00:00 [entrez]
AID - 10.1084/jem.167.2.323 [doi]
PST - ppublish
SO  - J Exp Med. 1988 Feb 1;167(2):323-31. doi: 10.1084/jem.167.2.323.

PMID- 16800635
OWN - NLM
STAT- MEDLINE
DCOM- 20060823
LR  - 20061115
IS  - 0006-2960 (Print)
IS  - 0006-2960 (Linking)
VI  - 45
IP  - 26
DP  - 2006 Jul 4
TI  - Carboxyl terminus of Helicobacter pylori alpha1,3-fucosyltransferase determines
      the structure and stability.
PG  - 8108-16
AB  - Helicobacter pylori is well known as the primary cause of gastritis, duodenal
      ulcers, and gastric cancer. The pathogenic bacteria produces Lewis x and Lewis y 
      epitopes in the O-antigens of lipopolysaccharides to mimic the carbohydrate
      antigens of gastric epithelial cells to avoid detection by the host's immune
      system. The enzyme alpha1,3-fucosyltransferase from H. pylori catalyzes the
      glycosyl addition of fucose from the donor GDP-fucose to the acceptor
      N-acetyllactosamine. The poor solubility of the enzyme was resolved by systematic
      deletion of the C-terminus. We report here the first structural analysis using CD
      spectroscopy and analytical ultracentrifugation. The results indicate that up to 
      80 residues, including the tail rich in hydrophobic and positively charged
      residues (sequence 434-478) and 5 of the 10 tandem repeats of 7 amino acids each 
      (399-433), can be removed without significant change in structure and catalysis. 
      Half of the heptad repeats are required to maintain both the secondary and native
      quaternary structures. Removal of more residues in the C-terminus led to major
      structural alteration, which was correlated with the loss of enzymatic activity. 
      In accordance with the thermal denaturation studies, the results support the idea
      that a higher number of tandem repeats functioning to facilitate a dimeric
      structure helps to prevent the protein from unfolding during incubation at higher
      temperatures.
FAU - Lin, Sheng-Wei
AU  - Lin SW
AD  - Institute of Biological Chemistry and Genomics Research Center, Academia Sinica, 
      No. 128 Academia Road Section 2, Nan-Kang, Taipei 11529, Taiwan.
FAU - Yuan, Tsui-Min
AU  - Yuan TM
FAU - Li, Jei-Ru
AU  - Li JR
FAU - Lin, Chun-Hung
AU  - Lin CH
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Biochemistry
JT  - Biochemistry
JID - 0370623
RN  - 0 (Bacterial Proteins)
RN  - 0 (DNA Primers)
RN  - 0 (Recombinant Proteins)
RN  - EC 2.4.1.- (Fucosyltransferases)
RN  - EC 2.4.1.152 (galactoside 3-fucosyltransferase)
SB  - IM
MH  - Amino Acid Sequence
MH  - Bacterial Proteins/chemistry
MH  - Base Sequence
MH  - Circular Dichroism
MH  - DNA Primers
MH  - Enzyme Stability
MH  - Fucosyltransferases/*chemistry
MH  - Helicobacter pylori/*enzymology
MH  - Kinetics
MH  - Molecular Sequence Data
MH  - Polymerase Chain Reaction
MH  - Protein Conformation
MH  - Recombinant Proteins/chemistry
MH  - Ultracentrifugation
EDAT- 2006/06/28 09:00
MHDA- 2006/08/24 09:00
CRDT- 2006/06/28 09:00
PHST- 2006/06/28 09:00 [pubmed]
PHST- 2006/08/24 09:00 [medline]
PHST- 2006/06/28 09:00 [entrez]
AID - 10.1021/bi0601297 [doi]
PST - ppublish
SO  - Biochemistry. 2006 Jul 4;45(26):8108-16. doi: 10.1021/bi0601297.

PMID- 11903928
OWN - NLM
STAT- MEDLINE
DCOM- 20020501
LR  - 20061115
IS  - 0305-1846 (Print)
IS  - 0305-1846 (Linking)
VI  - 27
IP  - 6
DP  - 2001 Dec
TI  - The glioma-associated gangliosides 3'-isoLM1, GD3 and GM2 show selective area
      expression in human glioblastoma xenografts in nude rat brains.
PG  - 451-64
AB  - This work describes the in vivo expression and distribution of glioma-associated 
      gangliosides (GD3, GM2, 3'-isoLM1) in a novel human brain tumour nude rat
      xenograft model. In this model, the tumours, which are established directly from 
      human glioblastoma biopsies, show extensive infiltrative growth within the rat
      brain. This model therefore provides an opportunity to study ganglioside
      expression not only within the macroscopic tumour, but also in brain areas with
      tumour cell infiltration. The ganglioside expression was studied by confocal
      microscopy of immunostained brain sections using antiganglioside monoclonal
      antibodies. Xenografts from four human glioblastoma multiformes were established 
      in rats and the brains removed after 3-4 months. Ganglioside GD3 was expressed in
      the tumour parenchyma while ganglioside 3'-isoLM1 was more abundantly expressed
      in the periphery of the tumour associated with areas of tumour cell invasion. GM2
      expression was only seen in one tumour, where it was located within the main
      tumour mass. Double staining with a pan antihuman monoclonal antibody (3B4) and
      the antiganglioside monoclonal antibodies confirmed that the ganglioside
      expression was associated with tumour cells. This work supports the concept of
      different biological roles for individual gangliosides and indicates that
      antibodies or ligands directed against GD3 and 3'-isoLM1 might be complementary
      when applied in the treatment of human glioblastomas.
FAU - Hedberg, K M
AU  - Hedberg KM
AD  - Institute of Clinical Neuroscience, Experimental Neuroscience Section, Goteborg
      University, Sahlgrenska University Hospital/Molndal, Molndal, Sweden.
      kristina.hedberg@neuro.gu.se
FAU - Mahesparan, R
AU  - Mahesparan R
FAU - Read, T A
AU  - Read TA
FAU - Tysnes, B B
AU  - Tysnes BB
FAU - Thorsen, F
AU  - Thorsen F
FAU - Visted, T
AU  - Visted T
FAU - Bjerkvig, R
AU  - Bjerkvig R
FAU - Fredman, P
AU  - Fredman P
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - Neuropathol Appl Neurobiol
JT  - Neuropathology and applied neurobiology
JID - 7609829
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Gangliosides)
RN  - 103842-51-9 (IV(3)-NeuAc-LcOse4Cer)
RN  - 62010-37-1 (ganglioside, GD3)
RN  - 65988-71-8 (ganglioside, GD2)
SB  - IM
MH  - Animals
MH  - Antibodies, Monoclonal
MH  - Antigens, Tumor-Associated, Carbohydrate/analysis/biosynthesis
MH  - Brain Injuries/metabolism
MH  - Brain Neoplasms/chemistry/*metabolism
MH  - Disease Models, Animal
MH  - Fluorescent Antibody Technique
MH  - Gangliosides/*analysis/biosynthesis/immunology
MH  - Glioblastoma/chemistry/*metabolism
MH  - Humans
MH  - Microscopy, Confocal
MH  - Neoplasm Transplantation
MH  - Rats
MH  - Rats, Nude
MH  - Transplantation, Heterologous
MH  - Wounds, Stab/metabolism
EDAT- 2002/03/21 10:00
MHDA- 2002/05/02 10:01
CRDT- 2002/03/21 10:00
PHST- 2002/03/21 10:00 [pubmed]
PHST- 2002/05/02 10:01 [medline]
PHST- 2002/03/21 10:00 [entrez]
AID - 353 [pii]
PST - ppublish
SO  - Neuropathol Appl Neurobiol. 2001 Dec;27(6):451-64.

PMID- 7901202
OWN - NLM
STAT- MEDLINE
DCOM- 19931201
LR  - 20171116
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 268
IP  - 30
DP  - 1993 Oct 25
TI  - Expression cloning of a novel Gal beta (1-3/1-4) GlcNAc alpha
      2,3-sialyltransferase using lectin resistance selection.
PG  - 22782-7
AB  - This report describes the isolation of a cDNA encoding a novel human Gal beta
      (1-3/1-4)GlcNac alpha 2,3-sialyl-transferase involved in the biosynthesis of the 
      sialyl Lewis x determinant (NeuAc alpha 2-3 Gal beta 1-4(Fuc alpha 1-3)GlcNAc). A
      cDNA library of the human melanoma cell line WM266-4 was constructed in an
      Epstein-Barr virus-based cloning vector. Selection of the B-cell line Namalwa
      expressing transfected cDNAs in the presence of the cytotoxic lectin Ricinus
      communis agglutinin 120 gave a cDNA encoding a protein with type II transmembrane
      topology, as found for mammalian glycosyltransferases. The use of this lectin,
      which is specific to galactose residues (especially the Gal beta 1-4GlcNAc
      structure), originates from our prediction that the modification of the Gal beta 
      1-4GlcNAc structure (a backbone of the sialyl Lewis x structure) by
      glycosyltransferases may increase the levels of resistance to this lectin.
      Comparison of this cDNA sequence with those of three other cloned
      sialyltransferases revealed two conserved regions shared by all four enzymes.
      Expression of the COOH-terminal catalytic domain of this protein showed alpha
      2,3-sialyltransferase activity with substrate specificity different from that of 
      CMP-N-acetylneuraminate:N-acetyllactosaminide alpha-2,3-sialyltransferase
      (Gal-beta 1-3(4)GlcNAc alpha 2,3-sialyltransferase, EC 2.4.99.6). Furthermore,
      expression of this cDNA in Namalwa cells increased the level of sialyl Lewis x
      antigens. The cloning approach based on lectin resistance may be useful for the
      isolation of cDNAs encoding other mammalian glycosyltransferases.
FAU - Sasaki, K
AU  - Sasaki K
AD  - Tokyo Research Laboratories, Kyowa Hakko Kogyo Co., Ltd., Japan.
FAU - Watanabe, E
AU  - Watanabe E
FAU - Kawashima, K
AU  - Kawashima K
FAU - Sekine, S
AU  - Sekine S
FAU - Dohi, T
AU  - Dohi T
FAU - Oshima, M
AU  - Oshima M
FAU - Hanai, N
AU  - Hanai N
FAU - Nishi, T
AU  - Nishi T
FAU - Hasegawa, M
AU  - Hasegawa M
LA  - eng
SI  - GENBANK/X74570
PT  - Comparative Study
PT  - Journal Article
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (DNA Primers)
RN  - 0 (DNA, Complementary)
RN  - 0 (Lewis X Antigen)
RN  - 9009-86-3 (Ricin)
RN  - EC 2.4.99.- (Sialyltransferases)
RN  - EC 2.4.99.4 (beta-galactoside alpha-2,3-sialyltransferase)
RN  - EC 2.4.99.6 (N-acetyllactosaminide alpha-2,3-sialyltransferase)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Base Sequence
MH  - Blotting, Northern
MH  - Carbohydrate Sequence
MH  - Cloning, Molecular
MH  - Conserved Sequence
MH  - DNA Primers
MH  - DNA, Complementary/chemistry/genetics/isolation & purification/metabolism
MH  - Drug Resistance
MH  - Gene Expression
MH  - Gene Library
MH  - Genetic Vectors
MH  - Humans
MH  - Lewis X Antigen/biosynthesis
MH  - Melanoma
MH  - Molecular Sequence Data
MH  - Polymerase Chain Reaction
MH  - Rats
MH  - Restriction Mapping
MH  - Ricin/*toxicity
MH  - Sequence Homology, Amino Acid
MH  - Sialyltransferases/*biosynthesis
MH  - Transcription, Genetic
MH  - Transfection
MH  - Tumor Cells, Cultured
EDAT- 1993/10/25 00:00
MHDA- 1993/10/25 00:01
CRDT- 1993/10/25 00:00
PHST- 1993/10/25 00:00 [pubmed]
PHST- 1993/10/25 00:01 [medline]
PHST- 1993/10/25 00:00 [entrez]
PST - ppublish
SO  - J Biol Chem. 1993 Oct 25;268(30):22782-7.

PMID- 2119368
OWN - NLM
STAT- MEDLINE
DCOM- 19901019
LR  - 20190510
IS  - 0910-5050 (Print)
IS  - 0910-5050 (Linking)
VI  - 81
IP  - 6-7
DP  - 1990 Jun-Jul
TI  - Immunohistological and biochemical detection of fucosylated polylactosamine
      antigen with monoclonal antibody ACFH18 in gastric cancer and normal gastric
      mucosa.
PG  - 676-81
AB  - A mouse monoclonal antibody ACFH18, produced by immunizing with human gastric
      cell line MKN-74, recognizes a novel glycolipid antigen,
      fucosyl-lactoneodecaosylceramide. In the present study, we investigated the
      immunohistological localization of this antigen and its biochemical detection in 
      glycolipid fraction in normal and malignant human gastric tissue, compared with
      other tumor-associated type-2 chain glycolipid antigens such as sialyl Lex,
      sialyl Lex-i and Ley. Reactivity with ACFH18 was detected immunohistologically in
      the proliferation zone of normal fundic gland region as well as in 38 of 54 cases
      of gastric cancer, with preferential binding to undifferentiated type cancer.
      Glycolipids reacting with ACFH18, especially slow-migrating glycolipids on
      thin-layer chromatography, were accumulated in all of four cancer specimens
      compared with normal mucosa obtained from the same patients. Many glycolipids
      with sialyl Lex or sialyl Lex-i epitope were detected in normal mucosa and almost
      all of these glycolipids were accumulated in cancer specimens. Sialyl LeX-i
      antigen was increased more specifically in cancer than sialyl LeX was. A Ley
      antigenic glycolipid was considerably decreased in three of four cancer cases and
      increased in one case. From these results, glycolipid detected by ACFH18 appeared
      to be a tumor-associated antigen comparable to sialyl LeX and sialyl Lex-i
      antigens, but with a unique character as an undifferentiated-type
      tumor-associated antigen.
FAU - Dohi, T
AU  - Dohi T
AD  - Division of Clinical Biochemistry, Clinical Research Institute, National Medical 
      Center, Tokyo.
FAU - Abe, K
AU  - Abe K
FAU - Ohshiba, S
AU  - Ohshiba S
FAU - Yamaguchi, K
AU  - Yamaguchi K
FAU - Oshima, M
AU  - Oshima M
LA  - eng
PT  - Comparative Study
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - Japan
TA  - Jpn J Cancer Res
JT  - Japanese journal of cancer research : Gann
JID - 8509412
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Glycolipids)
SB  - IM
MH  - *Antibodies, Monoclonal
MH  - Antigens, Tumor-Associated, Carbohydrate/*immunology
MH  - Chromatography, Thin Layer
MH  - Glycolipids/immunology
MH  - Humans
MH  - Immunohistochemistry
MH  - Mucous Membrane/immunology
MH  - Stomach/*immunology
MH  - Stomach Neoplasms/*immunology
EDAT- 1990/06/01 00:00
MHDA- 1990/06/01 00:01
CRDT- 1990/06/01 00:00
PHST- 1990/06/01 00:00 [pubmed]
PHST- 1990/06/01 00:01 [medline]
PHST- 1990/06/01 00:00 [entrez]
AID - 10.1111/j.1349-7006.1990.tb02626.x [doi]
PST - ppublish
SO  - Jpn J Cancer Res. 1990 Jun-Jul;81(6-7):676-81. doi:
      10.1111/j.1349-7006.1990.tb02626.x.

PMID- 3476183
OWN - NLM
STAT- MEDLINE
DCOM- 19871022
LR  - 20071114
IS  - 0008-543X (Print)
IS  - 0008-543X (Linking)
VI  - 60
IP  - 7
DP  - 1987 Oct 1
TI  - The detection of human pancreatic cancer-associated antigen in the serum of
      cancer patients.
PG  - 1636-43
AB  - A radioimmunoassay (RIA) test for human pancreatic cancer-associated antigen
      (Span-1) was developed to evaluate the diagnosis of various gastrointestinal
      disorders. Serum Span-1 in normal subjects ranged from 5 to 275 U/ml, with a mean
      of 58.8 U/ml (+/- 58.7, standard deviation). All control subjects had levels of
      less than 400 U/ml. Study subjects, 93% with pancreatic cancer, 59% with
      hepatobiliary cancers, 23% with gastric cancers, and 13% with colonic cancers had
      serum Span-1 levels greater than 400 U/ml. Sensitivities of Span-1, CA 19-9, and 
      Dupan-2 for pancreatic cancer were 94%, 85%, and 38% respectively. Span-1 in
      patients with Stage I pancreatic cancer showed a 50% positive rating but CA 19-9 
      and Dupan-2 showed only 0% and 25%. Although a positive rating of these three
      antibodies increased in advanced cases, Span-1 showed the highest positive
      rating. Span-1 reacted with colonic cancer tissues with Lewisa-b- phenotype.
      However, none of these tissues did not react against CA 19-9. From these results,
      Span-1 has a good predictive value for detecting pancreatic cancer compared with 
      CA 19-9 and Dupan-2.
FAU - Chung, Y S
AU  - Chung YS
FAU - Ho, J J
AU  - Ho JJ
FAU - Kim, Y S
AU  - Kim YS
FAU - Tanaka, H
AU  - Tanaka H
FAU - Nakata, B
AU  - Nakata B
FAU - Hiura, A
AU  - Hiura A
FAU - Motoyoshi, H
AU  - Motoyoshi H
FAU - Satake, K
AU  - Satake K
FAU - Umeyama, K
AU  - Umeyama K
LA  - eng
GR  - CA-24321/CA/NCI NIH HHS/United States
PT  - Comparative Study
PT  - Journal Article
PT  - Research Support, U.S. Gov't, Non-P.H.S.
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Cancer
JT  - Cancer
JID - 0374236
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens, Neoplasm)
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (DU-PAN-2 antigen, human)
RN  - 0 (pancreas-specific antigen)
SB  - AIM
SB  - IM
MH  - Antibodies, Monoclonal
MH  - Antigens, Neoplasm/analysis/*blood
MH  - Antigens, Tumor-Associated, Carbohydrate
MH  - Cell Line
MH  - Gastrointestinal Diseases/blood
MH  - Humans
MH  - Pancreatic Diseases/blood
MH  - Radioimmunoassay
EDAT- 1987/10/01 00:00
MHDA- 1987/10/01 00:01
CRDT- 1987/10/01 00:00
PHST- 1987/10/01 00:00 [pubmed]
PHST- 1987/10/01 00:01 [medline]
PHST- 1987/10/01 00:00 [entrez]
PST - ppublish
SO  - Cancer. 1987 Oct 1;60(7):1636-43.

PMID- 3699929
OWN - NLM
STAT- MEDLINE
DCOM- 19860612
LR  - 20160303
IS  - 0020-7136 (Print)
IS  - 0020-7136 (Linking)
VI  - 37
IP  - 5
DP  - 1986 May 15
TI  - A radioimmunoassay for the detection of a human tumor-associated glycoprotein
      (TAG-72) using monoclonal antibody B72.3.
PG  - 659-66
AB  - Monoclonal antibody (MAb) B72.3 was generated against a carcinoma metastasis and 
      has been shown to bind with a high degree of selectivity to a tumor-associated
      glycoprotein (TAG-72) found in human colon and breast carcinomas, while showing
      minimal reactivity to any normal adult tissues. Competition radioimmunoassays
      have been developed for the detection of TAG-72 in tumors and sera from both
      athymic mice bearing human carcinoma xenografts and patients with colon, breast
      and other carcinomas. The distribution of TAG-72 in human tumor xenografts was
      restricted to tumors originating from the LS-174T human colon carcinoma, with no 
      significant reactivity being detected in human tumor xenografts from a different 
      colon carcinoma, a human breast carcinoma, or a human melanoma. The levels of
      TAG-72 in clinical material obtained from surgery were examined; high levels were
      found in colon carcinomas and to a lesser extent in breast carcinomas, while no
      detectable levels were found in normal tissues. Sera from apparently normal
      patients contained a mean level of 2.2 units per ml of TAG-72. A level of 3
      standard deviations above the mean level of TAG-72 found in normals was employed 
      as a cut-off value to indicate a positive test result in subsequent studies. No
      patient with inflammatory disease or other benign colon disease exhibited
      elevated levels of TAG-72. Seven out of 20 patients with other carcinomas had
      elevated serum levels of TAG-72. The serum TAG-72 levels were compared with the
      serum levels of antigens recognized by the MAbs currently used to screen sera of 
      carcinoma patients (CEA, GICA, and OC125). It was clearly demonstrated that
      TAG-72 is different from these antigens and can be found in some sera in which no
      antigen is detected by otherwise available MAb RIAs.
FAU - Paterson, A J
AU  - Paterson AJ
FAU - Schlom, J
AU  - Schlom J
FAU - Sears, H F
AU  - Sears HF
FAU - Bennett, J
AU  - Bennett J
FAU - Colcher, D
AU  - Colcher D
LA  - eng
PT  - Journal Article
PL  - United States
TA  - Int J Cancer
JT  - International journal of cancer
JID - 0042124
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens, Neoplasm)
RN  - 0 (Glycoproteins)
RN  - 0 (tumor-associated antigen 72)
SB  - IM
MH  - Animals
MH  - Antibodies, Monoclonal
MH  - Antigens, Neoplasm/*analysis
MH  - Binding, Competitive
MH  - Breast Neoplasms/immunology
MH  - Carcinoma/*immunology
MH  - Colonic Diseases/immunology
MH  - Colonic Neoplasms/*immunology
MH  - Glycoproteins/*analysis
MH  - Humans
MH  - Mice
MH  - Neoplasm Transplantation
MH  - Neoplasms, Experimental/*analysis
MH  - Radioimmunoassay
MH  - Rectal Neoplasms/*immunology
EDAT- 1986/05/15 00:00
MHDA- 1986/05/15 00:01
CRDT- 1986/05/15 00:00
PHST- 1986/05/15 00:00 [pubmed]
PHST- 1986/05/15 00:01 [medline]
PHST- 1986/05/15 00:00 [entrez]
PST - ppublish
SO  - Int J Cancer. 1986 May 15;37(5):659-66.

PMID- 7309759
OWN - NLM
STAT- MEDLINE
DCOM- 19820222
LR  - 20071114
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 256
IP  - 24
DP  - 1981 Dec 25
TI  - Monoclonal antibodies directed against the human Leb blood group antigen.
PG  - 13223-5
AB  - Four monoclonal antibodies produced by hybridomas obtained from a mouse immunized
      with a human adenocarcinoma cell line SW1116 (Koprowski, H., Steplewski, Z.,
      Mitchell, K., Herlyn, M., Herlyn, D., and Fuhrer, P. (1979) Somatic Cell Genet.
      5, 957-972) are directed against the Leb antigen of the human Lewis blood group
      system. Their specificities were established by binding studies using purified
      Leb-active ceramide hexasaccharide and by hapten inhibition studies involving
      oligosaccharides obtained from human milk.
FAU - Brockhaus, M
AU  - Brockhaus M
FAU - Magnani, J L
AU  - Magnani JL
FAU - Blaszczyk, M
AU  - Blaszczyk M
FAU - Steplewski, Z
AU  - Steplewski Z
FAU - Koprowski, H
AU  - Koprowski H
FAU - Karlsson, K A
AU  - Karlsson KA
FAU - Larson, G
AU  - Larson G
FAU - Ginsburg, V
AU  - Ginsburg V
LA  - eng
GR  - CA-10815/CA/NCI NIH HHS/United States
GR  - CA-21124/CA/NCI NIH HHS/United States
GR  - RR-05540/RR/NCRR NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigen-Antibody Complex)
RN  - 0 (Glycosphingolipids)
RN  - 0 (Lewis Blood-Group System)
RN  - 0 (Oligosaccharides)
SB  - IM
MH  - *Antibodies, Monoclonal
MH  - Antigen-Antibody Complex
MH  - Carbohydrate Conformation
MH  - Carbohydrate Sequence
MH  - Cell Line
MH  - Colonic Neoplasms/immunology
MH  - Glycosphingolipids/immunology
MH  - Humans
MH  - Kinetics
MH  - Lewis Blood-Group System/*immunology
MH  - Melanoma/immunology
MH  - Oligosaccharides
EDAT- 1981/12/25 00:00
MHDA- 1981/12/25 00:01
CRDT- 1981/12/25 00:00
PHST- 1981/12/25 00:00 [pubmed]
PHST- 1981/12/25 00:01 [medline]
PHST- 1981/12/25 00:00 [entrez]
PST - ppublish
SO  - J Biol Chem. 1981 Dec 25;256(24):13223-5.

PMID- 19436292
OWN - NLM
STAT- MEDLINE
DCOM- 20090617
LR  - 20181113
IS  - 1532-1827 (Electronic)
IS  - 0007-0920 (Linking)
VI  - 100
IP  - 11
DP  - 2009 Jun 2
TI  - Sialyl-Tn vaccine induces antibody-mediated tumour protection in a relevant
      murine model.
PG  - 1746-54
LID - 10.1038/sj.bjc.6605083 [doi]
AB  - Changes in the composition of glycans added to glycoproteins and glycolipids are 
      characteristic of the change to malignancy. Sialyl-Tn (STn) is expressed by
      25-30% of breast carcinomas but its expression on normal tissue is highly
      restricted. Sialyl-Tn is an O-linked disaccharide that can be carried on various 
      glycoproteins. One such glycoprotein MUC1 is expressed by the vast majority of
      breast carcinomas. Both STn and MUC1 have been considered as targets for
      immunotherapy of breast cancer patients. Here we used different immunogens to
      target STn in an MUC1 transgenic mouse model of tumour challenge. We show that
      synthetic STn coupled to keyhole limpet haemocyanin (Theratope), induced
      antibodies to STn that recognised the glycan carried on a number of glycoproteins
      and in these mice a significant delay in tumour growth was observed. The
      protection was dependent on STn being expressed by the tumour and was antibody
      mediated. Affinity chromatography of the STn-expressing tumour cell line,
      followed by mass spectrometry, identified osteopontin as a novel STn-carrying
      glycoprotein which was highly expressed by the tumours. These results suggest
      that if antibodies can be induced to a number of targets expressed by the tumour 
      cells, a humoral response can be effective in controlling tumour growth.
FAU - Julien, S
AU  - Julien S
AD  - Breast Cancer Biology Group, King's College London, London SE1 9RT, UK.
FAU - Picco, G
AU  - Picco G
FAU - Sewell, R
AU  - Sewell R
FAU - Vercoutter-Edouart, A-S
AU  - Vercoutter-Edouart AS
FAU - Tarp, M
AU  - Tarp M
FAU - Miles, D
AU  - Miles D
FAU - Clausen, H
AU  - Clausen H
FAU - Taylor-Papadimitriou, J
AU  - Taylor-Papadimitriou J
FAU - Burchell, J M
AU  - Burchell JM
LA  - eng
GR  - Cancer Research UK/United Kingdom
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20090512
PL  - England
TA  - Br J Cancer
JT  - British journal of cancer
JID - 0370635
RN  - 0 (Antibodies)
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Biomarkers, Tumor)
RN  - 0 (Mucin-1)
RN  - 0 (Vaccines)
RN  - 0 (sialosyl-Tn antigen)
RN  - 9013-72-3 (Hemocyanins)
RN  - FV4Y0JO2CX (keyhole-limpet hemocyanin)
SB  - IM
MH  - Animals
MH  - Antibodies/*immunology
MH  - Antigens, Tumor-Associated, Carbohydrate/*immunology/*metabolism
MH  - Biomarkers, Tumor/*immunology/*metabolism
MH  - Cell Line, Tumor
MH  - Disease Models, Animal
MH  - Hemocyanins/immunology
MH  - Immunotherapy
MH  - Mice
MH  - Mice, Inbred BALB C
MH  - Mucin-1/immunology
MH  - Neoplasms/*immunology/metabolism/pathology
MH  - Survival Rate
MH  - Vaccines/*immunology
PMC - PMC2695689
EDAT- 2009/05/14 09:00
MHDA- 2009/06/18 09:00
CRDT- 2009/05/14 09:00
PHST- 2009/05/14 09:00 [entrez]
PHST- 2009/05/14 09:00 [pubmed]
PHST- 2009/06/18 09:00 [medline]
AID - 6605083 [pii]
AID - 10.1038/sj.bjc.6605083 [doi]
PST - ppublish
SO  - Br J Cancer. 2009 Jun 2;100(11):1746-54. doi: 10.1038/sj.bjc.6605083. Epub 2009
      May 12.

PMID- 14652017
OWN - NLM
STAT- MEDLINE
DCOM- 20040318
LR  - 20131121
IS  - 0006-291X (Print)
IS  - 0006-291X (Linking)
VI  - 312
IP  - 4
DP  - 2003 Dec 26
TI  - Sialyl-Tn antigen expression and O-linked GalNAc-Thr synthesis by Trypanosoma
      cruzi.
PG  - 1309-16
AB  - Most Trypanosoma cruzi O-glycans are linked to Thr/Ser residues via
      N-acetylglucosamine. We report that the mucin-type carcinoma-associated sialyl-Tn
      antigen (NeuAc-GalNAc-O-Ser/Thr) is expressed by T. cruzi. A specific MAb allowed
      us to localize the antigen on the surface of epimastigotes and to identify
      reactive components in parasite lysates (32, 60, and 94kDa). In addition,
      ppGalNAc-T activity was characterized in epimastigotes, and direct evidence was
      obtained for the in vitro incorporation of GalNAc to a synthetic peptide derived 
      from a T. cruzi mucin. These results add an as yet unknown complexity to the
      pathways of O-glycan biosynthesis in this protozoan parasite.
FAU - Freire, Teresa
AU  - Freire T
AD  - Depto. de Bioquimica, Facultad de Medicina, Universidad de la Republica,
      Montevideo, Uruguay.
FAU - Robello, Carlos
AU  - Robello C
FAU - Soule, Silvia
AU  - Soule S
FAU - Ferreira, Fernando
AU  - Ferreira F
FAU - Osinaga, Eduardo
AU  - Osinaga E
LA  - eng
PT  - Comparative Study
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Biochem Biophys Res Commun
JT  - Biochemical and biophysical research communications
JID - 0372516
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Mucins)
RN  - 0 (Tn antigen)
RN  - 0 (sialosyl-Tn antigen)
RN  - EC 2.4.1.- (N-Acetylgalactosaminyltransferases)
RN  - EC 2.4.1.- (UDP-GalNAc polypeptide N-acetylgalactosaminyltransferase 9)
RN  - EC 3.4.24.- (Metalloendopeptidases)
RN  - EC 3.4.24.- (molecule metalloprotease-related protein-1, human)
RN  - KM15WK8O5T (Acetylgalactosamine)
SB  - IM
MH  - Acetylgalactosamine/chemistry/*metabolism
MH  - Amino Acid Sequence
MH  - Animals
MH  - Antigens, Tumor-Associated, Carbohydrate/chemistry/*metabolism
MH  - Enzyme Activation
MH  - Fluorescent Antibody Technique, Direct/methods
MH  - Hydrogen-Ion Concentration
MH  - Metalloendopeptidases
MH  - Molecular Sequence Data
MH  - Mucins/chemistry/*metabolism
MH  - N-Acetylgalactosaminyltransferases/chemistry/*metabolism
MH  - Trypanosoma cruzi/chemistry/*metabolism
EDAT- 2003/12/04 05:00
MHDA- 2004/03/19 05:00
CRDT- 2003/12/04 05:00
PHST- 2003/12/04 05:00 [pubmed]
PHST- 2004/03/19 05:00 [medline]
PHST- 2003/12/04 05:00 [entrez]
AID - S0006291X03024185 [pii]
PST - ppublish
SO  - Biochem Biophys Res Commun. 2003 Dec 26;312(4):1309-16.

PMID- 1773918
OWN - NLM
STAT- MEDLINE
DCOM- 19920303
LR  - 20171128
IS  - 0301-4681 (Print)
IS  - 0301-4681 (Linking)
VI  - 48
IP  - 2
DP  - 1991 Nov
TI  - Immunohistochemical localization of the carbohydrate antigen 4C9 in the mouse
      embryo: a reliable marker of mouse primordial germ cells.
PG  - 75-82
AB  - Expression of 4C9, a Lex[Gal beta 1----4(Fuc alpha 1----3)GlcNAc] antigen, during
      mouse embryogenesis was studied by immunohistochemical methods. Distribution of
      4C9 was similar to, but not identical with that of SSEA-1 (stage-specific
      embryonic antigen-1). Notably, 4C9 was detected in some of the inner cell mass
      cells of late blastocysts, ectoderm cells migrating from the primitive streak to 
      the mesoderm space and primordial germ cells just formed from the migrating
      cells. Thus, 4C9 was considered to be continuously expressed in the cell lineage 
      starting at the totipotent 8 cell stage and leading to primordial germ cells.
      While 4C9 gradually decreased from the surface of primordial germ cells after
      they have settled in the gonad, the antigen remained in cytoplasmic granules for 
      some period in a sex determined manner. In male gonads, cytoplasmic granules
      positive for 4C9 tended to be polarized to one side of cytoplasm. The 4C9
      reactive material completely disappeared from male germ cells by day 16 of
      gestation. In female gonads, granules scattered throughout the cytoplasm and cell
      surface were positive for 4C9. On day 16 of gestation the cell surface
      antigenicity was lost, but some cytoplasmic antigenicity still remained. As
      above, 4C9 is a reliable marker to study the origin, migration and
      differentiation of primordial germ cells, and to distinguish male and female germ
      cells. By immunoelectron microscopy, 4C9 was detected at the plasma membrane, the
      Golgi apparatus, and dense-cored vesicles in primordial germ cells on 10-11 days 
      of gestation.
FAU - Yoshinaga, K
AU  - Yoshinaga K
AD  - Department of Anatomy, Kumamoto University Medical School, Japan.
FAU - Muramatsu, H
AU  - Muramatsu H
FAU - Muramatsu, T
AU  - Muramatsu T
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - Differentiation
JT  - Differentiation; research in biological diversity
JID - 0401650
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Biomarkers)
RN  - 0 (Lewis Blood-Group System)
SB  - IM
MH  - Animals
MH  - Antibodies, Monoclonal
MH  - Antibody Specificity
MH  - Biomarkers
MH  - Carbohydrate Sequence
MH  - Cell Membrane/chemistry/immunology/ultrastructure
MH  - Cytoplasmic Granules/chemistry/immunology/ultrastructure
MH  - Ectoderm/chemistry/cytology/immunology
MH  - Embryo, Mammalian/chemistry/*immunology
MH  - Female
MH  - Germ Cells/chemistry/*immunology
MH  - Golgi Apparatus/chemistry/immunology/ultrastructure
MH  - Immunohistochemistry
MH  - Lewis Blood-Group System/*analysis
MH  - Male
MH  - Mesoderm/chemistry/cytology/immunology
MH  - Mice
MH  - Mice, Inbred C57BL
MH  - Mice, Inbred ICR
MH  - Microscopy, Electron
MH  - Molecular Sequence Data
MH  - Ovary/cytology/embryology/immunology
MH  - Precipitin Tests
MH  - Testis/cytology/embryology/immunology
EDAT- 1991/11/01 00:00
MHDA- 1991/11/01 00:01
CRDT- 1991/11/01 00:00
PHST- 1991/11/01 00:00 [pubmed]
PHST- 1991/11/01 00:01 [medline]
PHST- 1991/11/01 00:00 [entrez]
AID - S0301-4681(11)60283-1 [pii]
PST - ppublish
SO  - Differentiation. 1991 Nov;48(2):75-82.

PMID- 15466199
OWN - NLM
STAT- MEDLINE
DCOM- 20041116
LR  - 20061115
IS  - 0008-5472 (Print)
IS  - 0008-5472 (Linking)
VI  - 64
IP  - 19
DP  - 2004 Oct 1
TI  - Role of the human ST6GalNAc-I and ST6GalNAc-II in the synthesis of the
      cancer-associated sialyl-Tn antigen.
PG  - 7050-7
AB  - The Sialyl-Tn antigen (Neu5Acalpha2-6GalNAc-O-Ser/Thr) is highly expressed in
      several human carcinomas and is associated with carcinoma aggressiveness and poor
      prognosis. We characterized two human sialyltransferases, CMP-Neu5Ac:GalNAc-R
      alpha2,6-sialyltransferase (ST6GalNAc)-I and ST6GalNAc-II, that are candidate
      enzymes for Sialyl-Tn synthases. We expressed soluble recombinant hST6GalNAc-I
      and hST6GalNAc-II and characterized the substrate specificity of both enzymes
      toward a panel of glycopeptides, glycoproteins, and other synthetic
      glycoconjugates. The recombinant ST6GalNAc-I and ST6GalNAc-II showed similar
      substrate specificity toward glycoproteins and GalNAcalpha-O-Ser/Thr
      glycopeptides, such as glycopeptides derived from the MUC2 mucin and the
      HIVgp120. We also observed that the amino acid sequence of the acceptor
      glycopeptide contributes to the in vitro substrate specificity of both enzymes.
      We additionally established a gastric cell line, MKN45, stably transfected with
      the full length of either ST6GalNAc-I or ST6GalNAc-II and evaluated the
      carbohydrate antigens expression profile induced by each enzyme. MKN45
      transfected with ST6GalNAc-I showed high expression of Sialyl-Tn, whereas MKN45
      transfected with ST6GalNAc-II showed the biosynthesis of the Sialyl-6T structure 
      [Galbeta1-3 (Neu5Acalpha2-6)GalNAc-O-Ser/Thr]. In conclusion, although both
      enzymes show similar in vitro activities when Tn antigen alone is available,
      whenever both Tn and T antigens are present, ST6GalNAc-I acts preferentially on
      Tn antigen, whereas the ST6GalNAc-II acts preferentially on T antigen. Our
      results show that ST6GalNAc-I is the major Sialyl-Tn synthase and strongly
      support the hypothesis that the expression of the Sialyl-Tn antigen in cancer
      cells is due to ST6GalNAc-I activity.
FAU - Marcos, Nuno T
AU  - Marcos NT
AD  - Institute of Molecular Pathology and Immunology of the University of Porto,
      Porto, Portugal.
FAU - Pinho, Sandra
AU  - Pinho S
FAU - Grandela, Catarina
AU  - Grandela C
FAU - Cruz, Andrea
AU  - Cruz A
FAU - Samyn-Petit, Benedicte
AU  - Samyn-Petit B
FAU - Harduin-Lepers, Anne
AU  - Harduin-Lepers A
FAU - Almeida, Raquel
AU  - Almeida R
FAU - Silva, Filipe
AU  - Silva F
FAU - Morais, Vanessa
AU  - Morais V
FAU - Costa, Julia
AU  - Costa J
FAU - Kihlberg, Jan
AU  - Kihlberg J
FAU - Clausen, Henrik
AU  - Clausen H
FAU - Reis, Celso A
AU  - Reis CA
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Cancer Res
JT  - Cancer research
JID - 2984705R
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Glycopeptides)
RN  - 0 (Recombinant Proteins)
RN  - 0 (sialosyl-Tn antigen)
RN  - EC 2.4.99.- (Sialyltransferases)
RN  - EC 2.4.99.- (galactosyl-1-3-N-acetylgalactosaminyl-specific
      2,6-sialyltransferase)
RN  - EC 2.4.99.3 (CMP-N-acetylneuraminate-alpha-N-acetylgalactosaminide
      alpha-2,6-sialyltransferase)
SB  - IM
MH  - Antigens, Tumor-Associated, Carbohydrate/*biosynthesis
MH  - Carbohydrate Sequence
MH  - Cell Line, Tumor
MH  - Enzyme-Linked Immunosorbent Assay
MH  - Glycopeptides/metabolism
MH  - Humans
MH  - Molecular Sequence Data
MH  - Recombinant Proteins/biosynthesis/genetics/isolation & purification/metabolism
MH  - Sialyltransferases/biosynthesis/genetics/isolation & purification/*metabolism
MH  - Stomach Neoplasms/enzymology/genetics/*metabolism
MH  - Substrate Specificity
MH  - Transfection
EDAT- 2004/10/07 09:00
MHDA- 2004/11/17 09:00
CRDT- 2004/10/07 09:00
PHST- 2004/10/07 09:00 [pubmed]
PHST- 2004/11/17 09:00 [medline]
PHST- 2004/10/07 09:00 [entrez]
AID - 64/19/7050 [pii]
AID - 10.1158/0008-5472.CAN-04-1921 [doi]
PST - ppublish
SO  - Cancer Res. 2004 Oct 1;64(19):7050-7. doi: 10.1158/0008-5472.CAN-04-1921.

PMID- 18798567
OWN - NLM
STAT- MEDLINE
DCOM- 20090512
LR  - 20131121
IS  - 1097-0134 (Electronic)
IS  - 0887-3585 (Linking)
VI  - 75
IP  - 1
DP  - 2009 Apr
TI  - Structural basis for sugar recognition, including the Tn carcinoma antigen, by
      the lectin SNA-II from Sambucus nigra.
PG  - 89-103
LID - 10.1002/prot.22222 [doi]
AB  - Bark of elderberry (Sambucus nigra) contains a galactose
      (Gal)/N-acetylgalactosamine (GalNAc)-specific lectin (SNA-II) corresponding to
      slightly truncated B-chains of a genuine Type-II ribosome-inactivating protein
      (Type-II RIPs, SNA-V), found in the same species. The three-dimensional X-ray
      structure of SNA-II has been determined in two distinct crystal forms, hexagonal 
      and tetragonal, at 1.90 A and 1.35 A, respectively. In both crystal forms, the
      SNA-II molecule folds into two linked beta-trefoil domains, with an overall
      conformation similar to that of the B-chains of ricin and other Type-II RIPs.
      Glycosylation is observed at four sites along the polypeptide chain, accounting
      for 14 saccharide units. The high-resolution structures of SNA-II in complex with
      Gal and five Gal-related saccharides (GalNAc, lactose, alpha1-methylgalactose,
      fucose, and the carcinoma-specific Tn antigen) were determined at 1.55 A
      resolution or better. Binding is observed in two saccharide-binding sites for
      most of the sugars: a conserved aspartate residue interacts simultaneously with
      the O3 and O4 atoms of saccharides. In one of the binding sites, additional
      interactions with the protein involve the O6 atom. Analytical gel filtration,
      small angle X-ray scattering studies and crystal packing analysis indicate that, 
      although some oligomeric species are present, the monomeric species predominate
      in solution.
CI  - (c) 2008 Wiley-Liss, Inc.
FAU - Maveyraud, Laurent
AU  - Maveyraud L
AD  - Institut de Pharmacologie et de Biologie Structurale (IPBS), UMR 5089, Universite
      Paul Sabatier Toulouse III/CNRS, Toulouse, France. laurent.maveyraud@ipbs.fr
FAU - Niwa, Hideaki
AU  - Niwa H
FAU - Guillet, Valerie
AU  - Guillet V
FAU - Svergun, Dmitri I
AU  - Svergun DI
FAU - Konarev, Peter V
AU  - Konarev PV
FAU - Palmer, Rex A
AU  - Palmer RA
FAU - Peumans, Willy J
AU  - Peumans WJ
FAU - Rouge, Pierre
AU  - Rouge P
FAU - Van Damme, Els J M
AU  - Van Damme EJ
FAU - Reynolds, Colin D
AU  - Reynolds CD
FAU - Mourey, Lionel
AU  - Mourey L
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Proteins
JT  - Proteins
JID - 8700181
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Plant Lectins)
RN  - 0 (Polysaccharides)
RN  - 0 (Sambucus nigra lectins)
RN  - 0 (Tn antigen)
RN  - EC 3.2.2.22 (Ribosome Inactivating Proteins)
RN  - X2RN3Q8DNE (Galactose)
SB  - IM
MH  - Antigens, Tumor-Associated, Carbohydrate/chemistry/*metabolism
MH  - Binding Sites
MH  - Crystallography, X-Ray
MH  - Galactose/analysis/chemistry/*metabolism
MH  - Plant Lectins/*chemistry/isolation & purification/*metabolism
MH  - Polysaccharides/chemistry
MH  - Protein Binding
MH  - Protein Conformation
MH  - Protein Multimerization
MH  - Ribosome Inactivating Proteins/*chemistry/isolation & purification/*metabolism
MH  - Sambucus nigra/*chemistry/metabolism
MH  - Scattering, Small Angle
MH  - Wood/chemistry
EDAT- 2008/09/19 09:00
MHDA- 2009/05/13 09:00
CRDT- 2008/09/19 09:00
PHST- 2008/09/19 09:00 [pubmed]
PHST- 2009/05/13 09:00 [medline]
PHST- 2008/09/19 09:00 [entrez]
AID - 10.1002/prot.22222 [doi]
PST - ppublish
SO  - Proteins. 2009 Apr;75(1):89-103. doi: 10.1002/prot.22222.

PMID- 2460087
OWN - NLM
STAT- MEDLINE
DCOM- 19881122
LR  - 20190501
IS  - 0264-6021 (Print)
IS  - 0264-6021 (Linking)
VI  - 254
IP  - 1
DP  - 1988 Aug 15
TI  - Immunochemical characterization of mucins. Polypeptide (M1) and polysaccharide (A
      and Leb) antigens.
PG  - 185-93
AB  - Seven monoclonal antibodies (MAbs) reacting with high-molecular-mass components
      (greater than 20,000 kDa) isolated from an ovarian mucinous cyst of an A Le(a-b+)
      patient are described. By the use of immunoradiometric methods, these MAbs
      characterized seven different epitopes associated with components having a
      density of 1.45 g/ml by CsCl-density-gradient ultracentrifugation, like mucins.
      Two MAbs reacted with A and Lewis blood-group antigens respectively
      (polysaccharide epitopes). The five other MAbs characterized five M1 epitopes
      (called a, b, c, d and e), mainly associated with components of more than 20,000 
      kDa and 2000 kDa. They were completely destroyed by papain and 2-mercaptoethanol 
      treatment (polypeptide epitopes). Moreover, timed trypsin digestion of native
      mucin resulted in a progressive loss of M1 activity and degraded these mucins
      into smaller M1-positive fragments. The a and c epitopes were partially degraded 
      from relatively high-molecular-mass fragments (2000 kDa to 500 kDa) into a 100
      kDa fragment. The b and d epitopes were completely degraded into smaller
      fragments ranging from 100 kDa to 40 kDa. The e epitope was completely destroyed 
      by trypsin. These different pathways of M1 antigen degradation suggest the
      occurrence of different epitopes located in separate regions of the mucin
      molecules.
FAU - Bara, J
AU  - Bara J
AD  - Institut de Recherches sur le Cancer, C.N.R.S., Villejuif, France.
FAU - Gautier, R
AU  - Gautier R
FAU - Le Pendu, J
AU  - Le Pendu J
FAU - Oriol, R
AU  - Oriol R
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - Biochem J
JT  - The Biochemical journal
JID - 2984726R
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens)
RN  - 0 (Epitopes)
RN  - 0 (Mucins)
RN  - 0 (Peptides)
RN  - 0 (Polysaccharides)
RN  - 60-24-2 (Mercaptoethanol)
RN  - EC 3.4.21.4 (Trypsin)
RN  - EC 3.4.22.2 (Papain)
SB  - IM
MH  - Antibodies, Monoclonal
MH  - Antigens/*analysis
MH  - Centrifugation, Isopycnic
MH  - Electrophoresis, Polyacrylamide Gel
MH  - Epitopes/analysis
MH  - Humans
MH  - Mercaptoethanol/pharmacology
MH  - Mucins/*immunology
MH  - Papain/pharmacology
MH  - Peptides/*immunology
MH  - Polysaccharides/*immunology
MH  - Radioimmunoassay
MH  - Trypsin/pharmacology
PMC - PMC1135055
EDAT- 1988/08/15 00:00
MHDA- 1988/08/15 00:01
CRDT- 1988/08/15 00:00
PHST- 1988/08/15 00:00 [pubmed]
PHST- 1988/08/15 00:01 [medline]
PHST- 1988/08/15 00:00 [entrez]
AID - 10.1042/bj2540185 [doi]
PST - ppublish
SO  - Biochem J. 1988 Aug 15;254(1):185-93. doi: 10.1042/bj2540185.

PMID- 2449247
OWN - NLM
STAT- MEDLINE
DCOM- 19880401
LR  - 20170915
IS  - 0006-3002 (Print)
IS  - 0006-3002 (Linking)
VI  - 958
IP  - 3
DP  - 1988 Feb 19
TI  - Monoclonal antibody directed to a Hanganutziu-Deicher active ganglioside, GM2
      (NeuGc).
PG  - 368-74
AB  - Spleen cells from NZB mouse immunized with a membrane fraction of rabbit thymus
      tissue were fused with BALB/c 6-thioguanine-resistant myeloma cells,
      P3-X63-Ag8.653. One hybridoma clone (Y-2-HD-1) produced IgM immunoglobulin that
      bound to an N-glycolylneuraminic acid-containing GM2 ganglioside, GM2(NeuGc),
      which is known to be a Hanganutziu-Deicher antigen. The specificity of the
      Y-2-HD-1 monoclonal antibody was examined, using authentic glycosphingolipids
      structurally related to GM2(NeuGc), by means of an enzyme-linked immunosorbent
      assay and thin-layer chromatography/enzyme immunostaining, respectively. The
      monoclonal antibody was found to be highly specific to GM2(NeuGc) and the epitope
      was a non-reducing terminal GalNAc beta 1-4[NeuGc alpha 2-3]Gal structure. This
      monoclonal antibody (Y-2-HD-1) bound to native mouse erythrocytes, in which
      GM2(NeuGc) is a major ganglioside. These results indicate that GM2(NeuGc) is
      located on the surface of mouse erythrocytes.
FAU - Sanai, Y
AU  - Sanai Y
AD  - Department of Biochemistry, Faculty of Medicine, University of Tokyo, Japan.
FAU - Yamasaki, M
AU  - Yamasaki M
FAU - Nagai, Y
AU  - Nagai Y
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - Netherlands
TA  - Biochim Biophys Acta
JT  - Biochimica et biophysica acta
JID - 0217513
RN  - 0 (12-keto-5,8,11,13-eicosatetraenoic acid)
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens, Heterophile)
RN  - 0 (Arachidonic Acids)
RN  - 0 (Epitopes)
RN  - 0 (Fatty Acids, Unsaturated)
RN  - 0 (Gangliosides)
RN  - 0 (Immunoglobulin M)
RN  - 19600-01-2 (G(M2) Ganglioside)
RN  - 81416-72-0 (15-keto-5,8,11,13-eicosatetraenoic acid)
RN  - 88528-32-9 (GM2 N-glycolylneuraminic acid ganglioside)
SB  - IM
MH  - Animals
MH  - Antibodies, Monoclonal/*immunology
MH  - Antibody Specificity
MH  - Antigens, Heterophile/*immunology
MH  - Arachidonic Acids/biosynthesis
MH  - Chromatography, Thin Layer
MH  - Enzyme-Linked Immunosorbent Assay
MH  - Epitopes/immunology
MH  - Erythrocytes/immunology
MH  - Fatty Acids, Unsaturated/biosynthesis
MH  - Female
MH  - G(M2) Ganglioside/analogs & derivatives/*immunology
MH  - Gangliosides/*immunology
MH  - Hybridomas/immunology
MH  - Immunoenzyme Techniques
MH  - Immunoglobulin M/immunology
MH  - Mice
MH  - Mice, Inbred BALB C
MH  - Mice, Inbred C3H
MH  - Mice, Inbred C57BL
MH  - Mice, Inbred NZB
MH  - Rabbits
EDAT- 1988/02/19 00:00
MHDA- 1988/02/19 00:01
CRDT- 1988/02/19 00:00
PHST- 1988/02/19 00:00 [pubmed]
PHST- 1988/02/19 00:01 [medline]
PHST- 1988/02/19 00:00 [entrez]
AID - 0005-2760(88)90222-6 [pii]
PST - ppublish
SO  - Biochim Biophys Acta. 1988 Feb 19;958(3):368-74.

PMID- 17674202
OWN - NLM
STAT- MEDLINE
DCOM- 20080715
LR  - 20181113
IS  - 0282-0080 (Print)
IS  - 0282-0080 (Linking)
VI  - 25
IP  - 2
DP  - 2008 Feb
TI  - Temporal changes in the carbohydrates expressed on BG01 human embryonic stem
      cells during differentiation as embryoid bodies.
PG  - 121-36
AB  - Cell surface carbohydrates present on BG01 human embryonic stem cells after 28
      days of differentiation were examined using two classes of carbohydrate binding
      proteins: lectins and antibodies specific for carbohydrate epitopes. Specificity 
      of lectin staining was verified using carbohydrate ligands to block lectin
      interaction, glycohydrolases to cleave specific sugar residues that are receptors
      for these proteins, and periodate oxidation to destroy susceptible sugar
      residues. Specific antibodies were used to identify various tissue types and germ
      layers present in the 12- and 28-day differentiating embryoid bodies. Results
      from 12 and 28-day differentiated embryoid bodies were compared to determine
      changes over time. A slight increase in the sialylation of alpha-GalNAc was seen 
      between 12 and 28 days of differentiation due to the presence of sialyl Tn and/or
      other sialylated alpha-GalNAc residues. Increases were also observed in GalNAc,
      the T antigen (Gal beta1,3 GalNAc), and difucosylated LacNAc residues during this
      time interval. Additionally, some distinct differences in the pattern of lectin
      staining between 12 and 28 days were observed. Not unexpectedly, the presence of 
      most differentiated cell-types increased during this time period with the
      exception of neural progenitors, which decreased. Undifferentiated cells, which
      were prevalent in the 12-day EBs, were undetectable after 28 days. We conclude
      that several changes in glycosylation occurred during the differentiation of
      embryonic stem cells, and that these changes may play a role in embryonic
      development.
FAU - Wearne, Kimberly A
AU  - Wearne KA
AD  - Department of Biological Chemistry, University of Michigan, 1150 West Medical
      Center Drive, 3220E MSRBIII, Ann Arbor, MI 48109, USA.
FAU - Winter, Harry C
AU  - Winter HC
FAU - Goldstein, Irwin J
AU  - Goldstein IJ
LA  - eng
GR  - 5 P30 CA46592/CA/NCI NIH HHS/United States
GR  - GM-069985/GM/NIGMS NIH HHS/United States
GR  - GM-29470/GM/NIGMS NIH HHS/United States
PT  - Journal Article
PT  - Research Support, N.I.H., Extramural
PT  - Research Support, Non-U.S. Gov't
DEP - 20070803
PL  - United States
TA  - Glycoconj J
JT  - Glycoconjugate journal
JID - 8603310
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Carbohydrates)
RN  - 0 (Immune Sera)
RN  - 0 (Lectins)
SB  - IM
MH  - Antibodies, Monoclonal/metabolism
MH  - *Carbohydrate Metabolism/genetics
MH  - Carbohydrate Sequence
MH  - Carbohydrates/*biosynthesis/*genetics/immunology
MH  - Cell Differentiation/*physiology
MH  - Cell Line
MH  - Cell Membrane/chemistry/metabolism
MH  - Embryonic Stem Cells/chemistry/*cytology/*metabolism
MH  - Female
MH  - Humans
MH  - Immune Sera/metabolism
MH  - Lectins/metabolism
MH  - Molecular Sequence Data
MH  - Pregnancy
MH  - Staining and Labeling
MH  - Time Factors
EDAT- 2007/08/04 09:00
MHDA- 2008/07/17 09:00
CRDT- 2007/08/04 09:00
PHST- 2007/04/25 00:00 [received]
PHST- 2007/07/02 00:00 [accepted]
PHST- 2007/06/27 00:00 [revised]
PHST- 2007/08/04 09:00 [pubmed]
PHST- 2008/07/17 09:00 [medline]
PHST- 2007/08/04 09:00 [entrez]
AID - 10.1007/s10719-007-9064-x [doi]
PST - ppublish
SO  - Glycoconj J. 2008 Feb;25(2):121-36. doi: 10.1007/s10719-007-9064-x. Epub 2007 Aug
      3.

PMID- 7693048
OWN - NLM
STAT- MEDLINE
DCOM- 19931126
LR  - 20171116
IS  - 0006-4971 (Print)
IS  - 0006-4971 (Linking)
VI  - 82
IP  - 9
DP  - 1993 Nov 1
TI  - A distinct type of sialyl Lewis X antigen defined by a novel monoclonal antibody 
      is selectively expressed on helper memory T cells.
PG  - 2797-805
AB  - A subset of human helper memory T cells is known to adhere to E-selectin
      expressed on cytokine-activated endothelial cells. However, sialyl Lex antigen,
      the carbohydrate ligand for E-selectin, has been hardly detectable on these
      cells, at least when typical anti-sialyl Lex antibodies were used for detection. 
      One of the MoAbs (2F3, IgM), which we raised against a chemically synthesized
      sialyl Lex glycolipid preparation, is found to react selectively to CD4+
      CD45RObright+ CD45RA- helper memory T cells among peripheral lymphocytes in
      healthy individuals. The specificity of the antibody is in clear contrast to that
      of the hitherto reported typical anti-sialyl Lex antibodies FH-6 and SNH-3. These
      classical anti-sialyl Lex antibodies were known to react to a subset of natural
      killer (NK) cells, but were not reactive with any particular subset of resting
      peripheral T or B cells of healthy individuals if the cells were not activated.
      On the other hand, the newly generated 2F3 antibody specifically reacted to
      helper memory T cells, and did not react to NK cells, B cells, or any T cells
      other than helper memory T cells. When tested against the sialyl Lex-active
      glycolipid antigen, the reactivity of 2F3 was not significantly different from
      that of the classical anti-sialyl Lex antibodies. But when tested against
      oligosaccharides prepared from cellular glycoproteins, 2F3 detected a distinct
      set of O-linked oligosaccharides, which were not reactive to the classical
      anti-sialyl Lex antibodies. Our results suggest that various molecular species of
      sialyl Lex antigens are present on carbohydrate side chains of cellular
      glycoproteins, and that helper memory T cells express a distinct type of sialyl
      Lex antigen that is defined by 2F3 but is not efficiently detected by other
      typical anti-sialyl Lex antibodies. Among cultured lymphocytic leukemia cells,
      the adult T-cell leukemia (ATL) cells preferentially expressed the 2F3-defined
      antigen, and acute lymphocytic leukemia cells rarely expressed the antigen. The
      cultured ATL cells expressing the 2F3-defined antigen showed a clear
      E-selectin-dependent adhesion to cytokin-activated endothelial cells, and the
      2F3-defined sialyl Lex antigen served as a ligand for E-selectin as ascertained
      by the clear inhibition of adhesion with the 2F3 antibody.(ABSTRACT TRUNCATED AT 
      400 WORDS)
FAU - Ohmori, K
AU  - Ohmori K
AD  - Department of Laboratory Medicine, Kyoto University, School of Medicine, Japan.
FAU - Takada, A
AU  - Takada A
FAU - Ohwaki, I
AU  - Ohwaki I
FAU - Takahashi, N
AU  - Takahashi N
FAU - Furukawa, Y
AU  - Furukawa Y
FAU - Maeda, M
AU  - Maeda M
FAU - Kiso, M
AU  - Kiso M
FAU - Hasegawa, A
AU  - Hasegawa A
FAU - Kannagi, M
AU  - Kannagi M
FAU - Kannagi, R
AU  - Kannagi R
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Blood
JT  - Blood
JID - 7603509
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Cell Adhesion Molecules)
RN  - 0 (E-Selectin)
RN  - 0 (Lewis X Antigen)
RN  - EC 3.1.3.48 (Leukocyte Common Antigens)
SB  - AIM
SB  - IM
MH  - Antibodies, Monoclonal/*immunology
MH  - Cell Adhesion Molecules/metabolism
MH  - Cells, Cultured
MH  - E-Selectin
MH  - Humans
MH  - *Immunologic Memory
MH  - Leukemia, T-Cell/immunology
MH  - Leukemic Infiltration
MH  - Leukocyte Common Antigens/analysis
MH  - Lewis X Antigen/*analysis/immunology/physiology
MH  - Skin/pathology
MH  - T-Lymphocytes, Helper-Inducer/*immunology
EDAT- 1993/11/01 00:00
MHDA- 1993/11/01 00:01
CRDT- 1993/11/01 00:00
PHST- 1993/11/01 00:00 [pubmed]
PHST- 1993/11/01 00:01 [medline]
PHST- 1993/11/01 00:00 [entrez]
PST - ppublish
SO  - Blood. 1993 Nov 1;82(9):2797-805.

PMID- 1567198
OWN - NLM
STAT- MEDLINE
DCOM- 19920515
LR  - 20180126
IS  - 0003-9861 (Print)
IS  - 0003-9861 (Linking)
VI  - 294
IP  - 2
DP  - 1992 May 1
TI  - Generation of murine monoclonal antibodies specific for N-glycolylneuraminic
      acid-containing gangliosides.
PG  - 427-33
AB  - We generated two murine monoclonal antibodies (MAbs) specific for mono- and
      disialylgangliosides having N-glycolylneuraminic acid (NeuGc) as their sialic
      acid moiety, respectively, by immunizing C3H/HeN mice with these purified
      gangliosides adsorbed to Salmonella minnesota followed by fusion with mouse
      myeloma cells. By use of a wide variety of glycolipids, including
      NeuGc-containing gangliosides, the precise structures recognized by these two
      antibodies were elucidated through enzyme-linked immunosorbent assay and
      immunostaining on thin-layer chromatography. One MAb, GMR8, which was generated
      by immunizing the mice with purified GM3(NeuGc), reacted specifically with
      gangliosides having NeuGc alpha 2----3Gal- terminal structures, such as
      GM3(NeuGc), IV3NeuGc alpha-Gg4Cer, IV3NeuGc alpha-nLc4Cer, V3NeuGc alpha-Gb5Cer, 
      and GD1a(NeuGc, NeuGc). None of the other gangliosides having internal NeuGc
      alpha2----3Gal- sequences, such as GM2(NeuGc) and GM1(NeuGc), nor corresponding
      gangliosides having NeuAc alpha 2----3Gal- sequences, nor neutral glycolipids
      were recognized. Thus, the epitope structures recognized by the MAb were found to
      be strictly NeuGc alpha 2----3Gal- terminal structures. In contrast, the other
      MAb, GMR3, which was generated by immunizing the mice with purified
      GD3(NeuGc-NeuGc-) adsorbed to the bacteria, reacted specifically with
      gangliosides having NeuGc alpha 2----8NeuGc alpha 2----3Gal- terminal sequences, 
      such as GD3(NeuGc-NeuGc-), IV3NeuGc alpha 2-Gg4Cer, IV3NeuGc alpha 2-nLc4Cer, and
      V3NeuGc alpha 2-Gb5Cer, but did not react with corresponding gangliosides having 
      NeuAc as their sialic acid moiety or with the neutral glycolipids tested. The
      epitope structures recognized by the MAb were suggested to be NeuGc alpha
      2----8NeuGc alpha 2----3Gal- terminal structures. Using these MAbs, we determined
      the distribution of such gangliosides in the spleen, kidney, and liver of several
      mice strains. Novel gangliosides reactive with these MAbs were detected in these 
      tissues.
FAU - Ozawa, H
AU  - Ozawa H
AD  - Department of Tumor Immunology, Tokyo Metropolitan Institute of Medical Science, 
      Honkomagome, Japan.
FAU - Kawashima, I
AU  - Kawashima I
FAU - Tai, T
AU  - Tai T
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Arch Biochem Biophys
JT  - Archives of biochemistry and biophysics
JID - 0372430
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigen-Antibody Complex)
RN  - 0 (Gangliosides)
RN  - 0 (Glycosphingolipids)
RN  - 0 (Neuraminic Acids)
RN  - 1113-83-3 (N-glycolylneuraminic acid)
SB  - IM
MH  - Animals
MH  - *Antibodies, Monoclonal
MH  - Antibody Specificity
MH  - Antigen-Antibody Complex
MH  - Carbohydrate Conformation
MH  - Carbohydrate Sequence
MH  - Chromatography, Thin Layer
MH  - Enzyme-Linked Immunosorbent Assay
MH  - Gangliosides/*analysis/chemistry/immunology
MH  - Glycosphingolipids/analysis/immunology
MH  - Mice
MH  - Mice, Inbred C3H/immunology
MH  - Molecular Sequence Data
MH  - Neuraminic Acids/*analysis/immunology
EDAT- 1992/05/01 00:00
MHDA- 1992/05/01 00:01
CRDT- 1992/05/01 00:00
PHST- 1992/05/01 00:00 [pubmed]
PHST- 1992/05/01 00:01 [medline]
PHST- 1992/05/01 00:00 [entrez]
AID - 0003-9861(92)90707-4 [pii]
PST - ppublish
SO  - Arch Biochem Biophys. 1992 May 1;294(2):427-33.

PMID- 9516847
OWN - NLM
STAT- MEDLINE
DCOM- 19980331
LR  - 20061115
IS  - 0959-8049 (Print)
IS  - 0959-8049 (Linking)
VI  - 33
IP  - 12
DP  - 1997 Oct
TI  - Detection of neuroblastoma cells in CD34+ selected peripheral stem cells using a 
      combination of tyrosine hydroxylase nested RT-PCR and anti-ganglioside GD2
      immunocytochemistry.
PG  - 2024-30
AB  - A sensitive assay was developed for the detection of neuroblastoma cell
      contamination in CD34+ selected and unseparated peripheral blood stem cells
      (PBSC) used for autologous transplantation in stage 4 neuroblastoma patients.
      Specifically, we established a non-radioactive nested cDNA-PCR (nPCR) for
      detection of tyrosine hydroxylase (TH) gene expression combined with
      anti-disialoganglioside GD2 immunocytochemistry with the murine monoclonal
      antibody (MAb) 14G2a. Sensitivities of TH nPCR determined with a number of
      neuroblastoma cell lines and PBSCs correlated to cell line dependent basal TH
      gene expression levels and ranged from 1:10(4) to 1:10(6). The sensitivity
      obtained by immunocytochemistry was 1:10(5). We observed the highest PBSC
      contamination rate of 47% (18/38) among 38 PBSC specimens exclusively obtained
      from stage 4 neuroblastoma patients by using TH nPCR and GD2 immunocytochemistry 
      in combination. Furthermore, a clinically applied purging method, CD34+ selection
      by immunoabsorption (CD34+ purity 42.4%), was used on 16 PBSCs. 10/16 (63%)
      preparations were contaminated prior to CD34+ selection and 56% (9/16) remained
      contaminated. A significant reduction of neuroblastoma cell contamination by
      CD34+ selection was not detectable, but the absolute amount of re-infused tumour 
      cells was decreased due to 100-fold smaller cell counts of CD34+ selected grafts 
      used for transplantation. 22 PBSC preparations were used for transplantation. A
      Kaplan-Meier analysis showed an event-free survival probability of 0.56 +/- 0.22 
      (n = 9) in the group with contaminated PBSCs versus 0.88 +/- 0.12 (n = 8) with no
      detectable neuroblastoma-cell contamination. Our data suggest that the combined
      use of TH nPCR and GD2 immunocytochemistry is optimal to detect contamination and
      monitor purging strategies.
FAU - Lode, H N
AU  - Lode HN
AD  - Department of Haematology Oncology, University Children's Hospital, Tuebingen,
      Germany.
FAU - Handgretinger, R
AU  - Handgretinger R
FAU - Schuermann, U
AU  - Schuermann U
FAU - Seitz, G
AU  - Seitz G
FAU - Klingebiel, T
AU  - Klingebiel T
FAU - Niethammer, D
AU  - Niethammer D
FAU - Beck, J
AU  - Beck J
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - Eur J Cancer
JT  - European journal of cancer (Oxford, England : 1990)
JID - 9005373
RN  - 0 (Antigens, CD34)
RN  - 0 (Antigens, Neoplasm)
RN  - 0 (Neoplasm Proteins)
RN  - EC 1.14.16.2 (Tyrosine 3-Monooxygenase)
SB  - IM
MH  - Antigens, CD34/analysis
MH  - Antigens, Neoplasm/analysis
MH  - Bone Marrow Purging/*methods
MH  - Cell Separation/methods
MH  - Disease-Free Survival
MH  - Hematopoietic Stem Cells/*pathology
MH  - Humans
MH  - Immunohistochemistry/methods
MH  - Neoplasm Proteins/*analysis/genetics
MH  - Neuroblastoma/enzymology/immunology/*pathology/therapy
MH  - Polymerase Chain Reaction/methods
MH  - Sensitivity and Specificity
MH  - Transplantation, Autologous
MH  - Tyrosine 3-Monooxygenase/*analysis/genetics
EDAT- 1998/03/28 00:00
MHDA- 1998/03/28 00:01
CRDT- 1998/03/28 00:00
PHST- 1998/03/28 00:00 [pubmed]
PHST- 1998/03/28 00:01 [medline]
PHST- 1998/03/28 00:00 [entrez]
AID - S0959-8049(97)00243-8 [pii]
PST - ppublish
SO  - Eur J Cancer. 1997 Oct;33(12):2024-30.

PMID- 9845419
OWN - NLM
STAT- MEDLINE
DCOM- 19990216
LR  - 20171116
IS  - 0882-0139 (Print)
IS  - 0882-0139 (Linking)
VI  - 27
IP  - 6
DP  - 1998 Dec
TI  - Expression of the sialosyl-Tn epitope on CD45 derived from activated peripheral
      blood T cells.
PG  - 323-38
AB  - The cell surface protein tyrosine phosphatase CD45 is a major target of IgM
      anti-T cell autoantibodies in systemic lupus erythematosus (SLE). The
      autoreactive determinants on CD45 are O-linked glycans expressed on activated T
      cells and certain T cell lines, rather than linear or conformational polypeptide 
      epitopes or N-linked glycans. To identify oligosaccharide structures that may
      play a role in the functional interactions of CD45 or are candidate target
      epitopes of SLE anti-CD45 autoantibodies, autoreactive CD45 purified from Jurkat 
      T cells and non-autoreactive CD45 purified from CLL B cells were tested by ELISA 
      for expression of mucin-type O-glycan structures. Monoclonal antibodies (mAbs)
      directed against blood group A, type 1 H chains, type 2 H chains, T, Le(a),
      sialylated-Le(a), Le(b), sialylated-Le(c), Le(x), sialylated-Le(x),
      multi-fucosylated Le(x), Le(y), and sialylated-extended Le(v) failed to react
      with CD45 from either B cells or T cells. However, mAbs directed against Tn
      (galNAcalpha1-->O-ser/thr) or sialosyl-Tn
      (neuNAcalpha2-6gaINAcalpha1-->O-ser/thr) structures reacted with CD45 derived
      from Jurkat T cells, but not from CLL B cells. Anti-Tn mAbs also reacted in
      western blotting procedures with CD45 isolated from Jurkat T cells, but did not
      react with CD45 isolated from CEM, MOLT-3, or PEER T cells; Daudi, Raji, or CLL B
      cells; or resting or Con A-activated PBL. However, anti-sialosyl-Tn mAbs stained 
      blots of CD45 isolated from Jurkat and CEM T cells and Con A-activated PBL, a
      pattern of reactivity similar to that of the anti-CD45 autoantibodies. Flow
      cytometric analyses demonstrated that the sialosyl-Tn epitopes are expressed on a
      subpopulation of CD4 +/CD8- T cells.
FAU - Fernsten, P
AU  - Fernsten P
AD  - Division of Rheumatology and Immunology, Thurston Arthritis Research Center, The 
      University of North Carolina at Chapel Hill, 27599, USA.
FAU - Shaw, M
AU  - Shaw M
FAU - Hocker, S
AU  - Hocker S
FAU - Fulghum, R
AU  - Fulghum R
FAU - Winfield, J
AU  - Winfield J
LA  - eng
GR  - AR3070/AR/NIAMS NIH HHS/United States
GR  - AR30863/AR/NIAMS NIH HHS/United States
GR  - AR7416/AR/NIAMS NIH HHS/United States
PT  - Journal Article
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - England
TA  - Immunol Invest
JT  - Immunological investigations
JID - 8504629
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Autoantibodies)
RN  - 0 (Carbohydrates)
RN  - 0 (Epitopes)
RN  - 0 (Immunoglobulin M)
RN  - 0 (Sialic Acids)
RN  - 11028-71-0 (Concanavalin A)
RN  - EC 3.1.3.48 (Leukocyte Common Antigens)
RN  - EC 3.1.3.48 (Protein Tyrosine Phosphatase, Non-Receptor Type 1)
SB  - IM
MH  - Antibodies, Monoclonal
MH  - Autoantibodies/blood
MH  - B-Lymphocytes/immunology
MH  - Carbohydrates/chemistry
MH  - Cell Line
MH  - Concanavalin A/pharmacology
MH  - Epitopes/chemistry
MH  - Humans
MH  - Immunoglobulin M/blood
MH  - In Vitro Techniques
MH  - Jurkat Cells
MH  - Leukocyte Common Antigens/*chemistry
MH  - Lupus Erythematosus, Systemic/immunology
MH  - Lymphocyte Activation
MH  - Protein Tyrosine Phosphatase, Non-Receptor Type 1
MH  - Sialic Acids/chemistry
MH  - T-Lymphocyte Subsets/immunology
MH  - T-Lymphocytes/*immunology
EDAT- 1998/12/09 00:00
MHDA- 1998/12/09 00:01
CRDT- 1998/12/09 00:00
PHST- 1998/12/09 00:00 [pubmed]
PHST- 1998/12/09 00:01 [medline]
PHST- 1998/12/09 00:00 [entrez]
PST - ppublish
SO  - Immunol Invest. 1998 Dec;27(6):323-38.

PMID- 8958810
OWN - NLM
STAT- MEDLINE
DCOM- 19970106
LR  - 20061115
IS  - 0022-3417 (Print)
IS  - 0022-3417 (Linking)
VI  - 180
IP  - 3
DP  - 1996 Nov
TI  - Expression of sialyl Lewis(X) in rat heart with ischaemia/reperfusion and
      reduction of myocardial reperfusion injury by a monoclonal antibody against
      sialyl Lewis(X)
PG  - 305-10
AB  - Neutrophils which infiltrate into the myocardial tissue subjected to ischaemia,
      followed by reperfusion, play a major role in myocardial reperfusion injury. It
      is known that early rolling attachment of neutrophils is mainly mediated by the
      selection family of cell-adhesion molecules and that this adhesion is then
      strengthened through the interaction of integrins and intercellular adhesion
      molecule-1. To investigate the role of sialyl Lewis(X) (SLe(X)), which is a
      ligand of all three members of the selections, in myocardial reperfusion injury, 
      the expression of SLe(X) was examined in rat hearts subjected to 30 min of
      ischaemia followed by reperfusion. The effects were also analysed of in vivo
      administration of an anti-SLe(X) monoclonal antibody (MAb) on myocardial necrosis
      in a rat model of myocardial reperfusion injury. Reperfusion of ischaemic
      myocardial tissue resulted in enhanced expression of SLe(X) on the luminal
      surface of vascular endothelial cells (VECs), as well as cardiac myocytes.
      Furthermore, the in vivo administration of an anti-SLe(X) MAb significantly
      reduced the extent of the myocardial infarction developed after 30 min of
      ischaemia followed by 48 h of reperfusion. These findings indicate that SLe(X)
      plays a critical role in the development of myocardial reperfusion injury and
      offer a potentially useful immune therapy to protect against this injury.
FAU - Seko, Y
AU  - Seko Y
AD  - Third Department of Internal Medicine, Faculty of Medicine, University of Tokyo, 
      Japan.
FAU - Enokawa, Y
AU  - Enokawa Y
FAU - Tamatani, T
AU  - Tamatani T
FAU - Kannagi, R
AU  - Kannagi R
FAU - Yagita, H
AU  - Yagita H
FAU - Okumura, K
AU  - Okumura K
FAU - Yazaki, Y
AU  - Yazaki Y
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - J Pathol
JT  - The Journal of pathology
JID - 0204634
RN  - 0
      (5-acetylneuraminyl-(2-3)-galactosyl-(1-4)-(fucopyranosyl-(1-3))-N-acetylglucosam
      ine)
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Oligosaccharides)
SB  - IM
CIN - J Pathol. 1997 Sep;183(1):124-5. PMID: 9370958
MH  - Animals
MH  - Antibodies, Monoclonal/*therapeutic use
MH  - Endothelium, Vascular/*metabolism
MH  - Immunoenzyme Techniques
MH  - Male
MH  - Myocardial Ischemia/metabolism
MH  - Myocardial Reperfusion
MH  - Myocardial Reperfusion Injury/*metabolism/pathology/prevention & control
MH  - Myocardium/*metabolism
MH  - Oligosaccharides/immunology/*metabolism
MH  - Rats
MH  - Rats, Wistar
EDAT- 1996/11/01 00:00
MHDA- 2000/06/20 09:00
CRDT- 1996/11/01 00:00
PHST- 1996/11/01 00:00 [pubmed]
PHST- 2000/06/20 09:00 [medline]
PHST- 1996/11/01 00:00 [entrez]
AID - 10.1002/(SICI)1096-9896(199611)180:3<305::AID-PATH651>3.0.CO;2-S [pii]
AID - 10.1002/(SICI)1096-9896(199611)180:3<305::AID-PATH651>3.0.CO;2-S [doi]
PST - ppublish
SO  - J Pathol. 1996 Nov;180(3):305-10. doi:
      10.1002/(SICI)1096-9896(199611)180:3<305::AID-PATH651>3.0.CO;2-S.

PMID- 19609959
OWN - NLM
STAT- MEDLINE
DCOM- 20090929
LR  - 20090723
IS  - 1615-9861 (Electronic)
IS  - 1615-9853 (Linking)
VI  - 9
IP  - 13
DP  - 2009 Jul
TI  - Identification of blood group A/A-Leb/y and B/B-Leb/y active glycotopes
      co-expressed on the O-glycans isolated from two distinct human ovarian cyst
      fluids.
PG  - 3445-62
LID - 10.1002/pmic.200800870 [doi]
AB  - Although the individual human blood group A and B determinants are well defined, 
      their co-expression pattern on a particular glycan carrier in individuals of
      blood group AB status has not been delineated. To address this issue, complex
      O-glycans were isolated from two distinct sources of human ovarian cyst
      glycoproteins (HOC 89 and Cyst 19) and profiled by advanced MS analyses, in
      conjunction with defining their binding characteristics against a panel of
      lectins and monoclonal antibodies. The major O-glycans of HOC 89 were found to
      correspond to sialyl Tn, mono- and di-sialyl T structures, whereas those of Cyst 
      19 were apparently more heterogeneous and extended to larger sizes. A minimal
      structure that carries both A and B determinants on the same molecule was
      identified, in which the A epitope is attached directly to the core GalNAc,
      whereas the B epitope is preferentially located on the six arms of a core 2
      structure. Both arms can be further extended with internal fucosylation that
      appears to be restricted to those non-sialylated chains already carrying the
      terminal ABH determinants, thus giving rise to rather prominent A/B-Le(b/y)
      glycotopes on larger O-glycans.
FAU - Yu, Shin-Yi
AU  - Yu SY
AD  - Institute of Biochemical Sciences, National Taiwan University, Taipei, Taiwan.
FAU - Yang, Zhangung
AU  - Yang Z
FAU - Khoo, Kay-Hooi
AU  - Khoo KH
FAU - Wu, Albert M
AU  - Wu AM
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - Germany
TA  - Proteomics
JT  - Proteomics
JID - 101092707
RN  - 0 (ABO Blood-Group System)
RN  - 0 (Epitopes)
RN  - 0 (Glycoproteins)
RN  - 0 (Lectins)
RN  - 0 (Polysaccharides)
SB  - IM
MH  - ABO Blood-Group System/immunology/*isolation & purification
MH  - Carbohydrate Sequence
MH  - Cyst Fluid/*chemistry
MH  - Epitopes/immunology
MH  - Female
MH  - Glycoproteins/chemistry/isolation & purification
MH  - Glycosylation
MH  - Humans
MH  - Lectins/chemistry/isolation & purification
MH  - Ovarian Cysts/*chemistry
MH  - Polysaccharides/chemistry/*immunology/*isolation & purification
MH  - Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
EDAT- 2009/07/18 09:00
MHDA- 2009/09/30 06:00
CRDT- 2009/07/18 09:00
PHST- 2009/07/18 09:00 [entrez]
PHST- 2009/07/18 09:00 [pubmed]
PHST- 2009/09/30 06:00 [medline]
AID - 10.1002/pmic.200800870 [doi]
PST - ppublish
SO  - Proteomics. 2009 Jul;9(13):3445-62. doi: 10.1002/pmic.200800870.

PMID- 8702594
OWN - NLM
STAT- MEDLINE
DCOM- 19960916
LR  - 20190508
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 271
IP  - 32
DP  - 1996 Aug 9
TI  - Functional relationships of the genetic locus encoding the glycosyltransferase
      enzymes involved in expression of the lacto-N-neotetraose terminal
      lipopolysaccharide structure in Neisseria meningitidis.
PG  - 19166-73
AB  - The biosynthetic function of the lgtABE genetic locus of Neisseria meningitidis
      was determined by structural analysis of lipopolysaccharide (LPS) derived from
      mutant strains and enzymic assay for glycosyltransferase activity. LPS was
      obtained from mutants generated by insertion of antibiotic resistance cassets in 
      each of the three genes lgtA, lgtB, lgtE of the N. meningitidis immunotype L3
      strain phi3 MC58. LPS from the parent strain expresses the terminal
      lacto-N-neotetraose structure, Galbeta1-->4GlcNAcbeta1-->3Galbeta1-->4Glc. Mild
      hydrazine treatment of the LPS afforded O-deacylated samples that were analyzed
      directly by electrospray ionization mass spectrometry (ESI-MS) in the negative
      ion mode. In conjunction with results from sugar analysis, ESI-MS revealed
      successive loss of the sugars Gal, GlcNAc, and Gal in lgt B, lgt A, and lgt E
      LPS, respectively. The structure of a sample of O- and N-deacylated LPS derived
      by aqueous KOH treatment of lgt B LPS was determined in detail by two-dimensional
      homo- and heteronuclear NMR methods. Using a synthetic beta-GlcNAc acceptor and a
      beta-lactose acceptor, the glycosyltransferase activities encoded by the lgtB and
      lgtA genes were unambiguously established. These data provide the first
      definitive evidence that the three genes encode the respective
      glycosyltransferases required for biosynthesis of the terminal trisaccharide
      moiety of the lacto-N-neotetraose structure in Neisseria LPS. From ESI-MS data,
      it was also determined that the Gal-deficient LPS expressed by the lgt E mutant
      is identical to that of the major component expressed by immunotype L3
      galE-deficient strains. The galE gene which encodes for UDP-glucose-4-epimerase
      plays an essential role in the incorporation of Gal into meningococcal LPS.
FAU - Wakarchuk, W
AU  - Wakarchuk W
AD  - Institute for Biological Sciences, National Research Council of Canada, Ottawa,
      Ontario, K1A 0R6, Canada.
FAU - Martin, A
AU  - Martin A
FAU - Jennings, M P
AU  - Jennings MP
FAU - Moxon, E R
AU  - Moxon ER
FAU - Richards, J C
AU  - Richards JC
LA  - eng
GR  - Wellcome Trust/United Kingdom
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Lipopolysaccharides)
RN  - 0 (Oligosaccharides)
RN  - BY63N40B1L (lacto-N-neotetraose)
RN  - EC 2.4.- (Glycosyltransferases)
SB  - IM
MH  - Carbohydrate Conformation
MH  - Carbohydrate Sequence
MH  - Glycosyltransferases/*genetics/metabolism
MH  - Lipopolysaccharides/chemistry/*metabolism
MH  - Magnetic Resonance Spectroscopy
MH  - Mass Spectrometry/methods
MH  - Molecular Sequence Data
MH  - Neisseria meningitidis/enzymology/*genetics
MH  - Oligosaccharides/*chemistry
EDAT- 1996/08/09 00:00
MHDA- 1996/08/09 00:01
CRDT- 1996/08/09 00:00
PHST- 1996/08/09 00:00 [pubmed]
PHST- 1996/08/09 00:01 [medline]
PHST- 1996/08/09 00:00 [entrez]
AID - 10.1074/jbc.271.32.19166 [doi]
PST - ppublish
SO  - J Biol Chem. 1996 Aug 9;271(32):19166-73. doi: 10.1074/jbc.271.32.19166.

PMID- 9052758
OWN - NLM
STAT- MEDLINE
DCOM- 19970320
LR  - 20160303
IS  - 0020-7136 (Print)
IS  - 0020-7136 (Linking)
VI  - 70
IP  - 5
DP  - 1997 Mar 4
TI  - Colon carcinoma glycoproteins carrying alpha 2,6-linked sialic acid reactive with
      Sambucus nigra agglutinin are not constitutively expressed in normal human colon 
      mucosa and are distinct from sialyl-Tn antigen.
PG  - 575-81
AB  - In human colon carcinoma, increased amounts of sialic acids have been found and
      correlated with tumor progression. Further, the degree of O-acetylation of sialic
      acid residues in normal mucosa is higher than in colon carcinoma. Thus,
      tumor-associated sialylated antigens may be constitutively expressed in
      O-acetylated form in normal mucosa unreactive with the respective monoclonal
      antibodies. We have earlier demonstrated a colon carcinoma-associated expression 
      of alpha 2,6-linked sialic acid residues with the Sambucus nigra agglutinin
      (SNA). We report now that de-acetylation of normal and transitional colonic
      mucosa, in contrast to sialyl-Tn antigen, does not result in SNA binding.
      Further, the alpha 2,6-linked sialic acid recognized by SNA is distinct from that
      of sialyl-Tn antigen. This is confirmed by Northern blotting detecting
      transcripts for alpha 2,6 sialyltransferase of N-glycoproteins and measurement of
      activity for this sialyltransferase. Blot analysis by SNA of colon carcinoma
      cells revealed few reactive glycoproteins. Quantitative differences in lectin
      labeling and sialyltransferase activity were found in HCT116 colon carcinoma cell
      sub-lines. Our data suggest that SNA binding in human colon carcinoma is due to
      de novo expression of a specific sialic acid present on selected glycoproteins.
FAU - Murayama, T
AU  - Murayama T
AD  - Department of Pathology, University of Zurich, Switzerland.
FAU - Zuber, C
AU  - Zuber C
FAU - Seelentag, W K
AU  - Seelentag WK
FAU - Li, W P
AU  - Li WP
FAU - Kemmner, W
AU  - Kemmner W
FAU - Heitz, P U
AU  - Heitz PU
FAU - Roth, J
AU  - Roth J
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Int J Cancer
JT  - International journal of cancer
JID - 0042124
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Glycoproteins)
RN  - 0 (Lectins)
RN  - 0 (Neoplasm Proteins)
RN  - 0 (Plant Lectins)
RN  - 0 (Sambucus nigra lectins)
RN  - 0 (sialosyl-Tn antigen)
RN  - EC 2.4.99.- (Sialyltransferases)
RN  - EC 2.4.99.1 (beta-D-galactoside alpha 2-6-sialyltransferase)
RN  - EC 3.2.2.22 (Ribosome Inactivating Proteins)
RN  - GZP2782OP0 (N-Acetylneuraminic Acid)
SB  - IM
MH  - Acetylation
MH  - Antigens, Tumor-Associated, Carbohydrate/metabolism
MH  - Blotting, Northern
MH  - Carcinoma/*metabolism
MH  - Colonic Neoplasms/*metabolism
MH  - Glycoproteins/*metabolism
MH  - Humans
MH  - Intestinal Mucosa/*metabolism
MH  - Lectins/*metabolism
MH  - N-Acetylneuraminic Acid/*metabolism
MH  - Neoplasm Proteins/*metabolism
MH  - *Plant Lectins
MH  - Ribosome Inactivating Proteins
MH  - Sialyltransferases/*metabolism
EDAT- 1997/03/04 00:00
MHDA- 2000/06/20 09:00
CRDT- 1997/03/04 00:00
PHST- 1997/03/04 00:00 [pubmed]
PHST- 2000/06/20 09:00 [medline]
PHST- 1997/03/04 00:00 [entrez]
AID - 10.1002/(SICI)1097-0215(19970304)70:5<575::AID-IJC14>3.0.CO;2-C [pii]
PST - ppublish
SO  - Int J Cancer. 1997 Mar 4;70(5):575-81.

PMID- 2659167
OWN - NLM
STAT- MEDLINE
DCOM- 19890727
LR  - 20071114
IS  - 0008-5472 (Print)
IS  - 0008-5472 (Linking)
VI  - 49
IP  - 13
DP  - 1989 Jul 1
TI  - Mosaicism in the expression of tumor-associated carbohydrate antigens in human
      colonic and gastric cancers.
PG  - 3662-9
AB  - Serial sequential sections from a single tumor were examined by
      immunohistological staining with several monoclonal antibodies directed,
      respectively, to different tumor-associated carbohydrate epitopes. Staining
      patterns were compared with those of conventional staining with hematoxylin-eosin
      or periodate/Schiff's reagent. Each tumor showed different areas of staining with
      different antibodies, and the combined staining map shows a clear mosaicism of
      antigen expression within the same tumor. For example, some areas of a given
      tumor were stained by FH4 (defining dimeric Le(x)), while other complementary
      areas were strongly stained, in a mutually exclusive manner, by SH1 (defining
      Le(x)), AH6 (defining Le(y)), FH6 (defining sialosyl dimeric (Le(x)), or TKH2
      (defining sialosyl-Tn). Some areas were stained by two or three of these
      antibodies. Comparisons of the mosaic-staining patterns with cytohistological
      properties of tumor cells within specific areas suggested that the pattern of
      antigen expression is correlated with degree of differentiation; e.g.,
      poorly-differentiated cells with severe dysplasia did not express high levels of 
      Le(x) or Le(y) but did express sialyl-Le(x) or dimeric Le(x); on the other hand, 
      moderately or well-differentiated tumor cells in some areas expressed high levels
      of Le(x) or Le(y) but lower levels of sialyl-Le(x). Areas showing strong
      expression of sialyl-Tn in their secretions were consistently correlated with
      presence of well-differentiated tumor cells, whereas secretions from normal
      mucosae were consistently characterized by lack of sialyl-Tn expression. It is
      postulated that the original in situ tumors (which had homogeneous glycosylation 
      patterns) evolved into several spatially discrete cell populations displaying
      different degrees of glycosylation, reflecting stages of tumor cell
      differentiation and progression.
FAU - Nakasaki, H
AU  - Nakasaki H
AD  - Biomembrane Institute, Seattle, Washington 98119.
FAU - Mitomi, T
AU  - Mitomi T
FAU - Noto, T
AU  - Noto T
FAU - Ogoshi, K
AU  - Ogoshi K
FAU - Hanaue, H
AU  - Hanaue H
FAU - Tanaka, Y
AU  - Tanaka Y
FAU - Makuuchi, H
AU  - Makuuchi H
FAU - Clausen, H
AU  - Clausen H
FAU - Hakomori, S
AU  - Hakomori S
LA  - eng
GR  - CA42505/CA/NCI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Cancer Res
JT  - Cancer research
JID - 2984705R
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens, Neoplasm)
RN  - 0 (Carbohydrates)
SB  - IM
MH  - Antibodies, Monoclonal/immunology
MH  - Antigens, Neoplasm/*immunology
MH  - Carbohydrate Sequence
MH  - Carbohydrates/*immunology
MH  - Cell Differentiation
MH  - Colonic Neoplasms/*immunology/pathology
MH  - Female
MH  - Glycosylation
MH  - Humans
MH  - Immunoenzyme Techniques
MH  - Male
MH  - Middle Aged
MH  - Molecular Sequence Data
MH  - Stomach Neoplasms/*immunology/pathology
EDAT- 1989/07/01 00:00
MHDA- 1989/07/01 00:01
CRDT- 1989/07/01 00:00
PHST- 1989/07/01 00:00 [pubmed]
PHST- 1989/07/01 00:01 [medline]
PHST- 1989/07/01 00:00 [entrez]
PST - ppublish
SO  - Cancer Res. 1989 Jul 1;49(13):3662-9.

PMID- 12556292
OWN - NLM
STAT- MEDLINE
DCOM- 20030911
LR  - 20151119
IS  - 1522-7952 (Print)
IS  - 1522-7952 (Linking)
VI  - 22
IP  - 2
DP  - 2003 Mar-Apr
TI  - SIALYL-Tn antigen distribution in Helicobacter pylori chronic gastritis in
      children: an immunohistochemical study.
PG  - 117-29
AB  - Sialyl-Tn antigen (STn) is a mucin-type carbohydrate normally present in goblet
      cells of small and large bowel. STn expression has been demonstrated to occur in 
      complete and incomplete intestinal metaplasia as well as in many carcinomas but
      in no normal gastric cell. The aim of our present study was to evaluate the
      distribution of STn in Helicobacter pylori chronic gastritis (HpCG) of pediatric 
      patients. Eighteen gastric biopsies from 15 children (mean age: 11.5 years) with 
      HpCG, 9 gastric biopsies from 9 children without H. pylori infection, and 1
      heterotopic gastric mucosa in Meckel's diverticulum were immunostained using the 
      anti-STn antibody STn1 (18/18), NCL-MUC-1 (7/18), and NCL-MUC-2 (18/18)
      antibodies. Also, sulfated mucosubstances were investigated with the Alcian
      Blue-Periodic Acid Schiff (AB-PAS), pH 1.0 stain. Although with different
      intensity (weak in 5/18, moderate 9/18, and intense 4/18) all cases with HpCG
      exhibited STn immunoreactivity. The expression of STn was found to be located
      mainly to the supranuclear region of the epithelial cells at the foveolae and
      glandular necks, with occasional cells showing diffuse cytoplasmic staining. When
      reactivity was intense, it was for the most part found in the cells at the neck
      of the glands. The mucus out of the luminal border above the positive cells was
      usually also stained. MUC-1 was negative (2/7) or weakly positive (5/7) in a few 
      surface mucous cells. MUC-2 was negative (16/18) or occasionally detected in some
      foveolar and surface cells (2/18). AB-PAS pH 1.0 revealed the presence of
      sulfomucins in the cytoplasm of isolated cells of gastric pits and glands of most
      cases (11/15). None of these findings was observed in the control group. We
      conclude that STn can be identified in gastric cells of pediatric patients with
      HpCG and that this does not correlate with other mucosubtances markers. The
      findings could indicate that minimal intestinal metaplasia takes place in
      children with HpCG.
FAU - Cohen, Marta
AU  - Cohen M
AD  - Department of Pathology, Hospital de Ninos Superiora Sor Maria Ludovica, La
      Plata, Argentina.
FAU - Drut, Ricardo
AU  - Drut R
FAU - Cueto Rua, Eduardo
AU  - Cueto Rua E
LA  - eng
PT  - Journal Article
PL  - United States
TA  - Pediatr Pathol Mol Med
JT  - Pediatric pathology & molecular medicine
JID - 100885435
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Biomarkers, Tumor)
RN  - 0 (sialosyl-Tn antigen)
SB  - IM
MH  - Adolescent
MH  - Antigens, Tumor-Associated, Carbohydrate/*biosynthesis
MH  - Biomarkers, Tumor/*biosynthesis
MH  - Child
MH  - Female
MH  - Gastric Mucosa/metabolism/pathology
MH  - Gastritis/*microbiology
MH  - Helicobacter Infections/metabolism
MH  - Helicobacter pylori/*immunology
MH  - Humans
MH  - Immunohistochemistry
MH  - Male
MH  - Metaplasia
MH  - Stomach/pathology
EDAT- 2003/01/31 04:00
MHDA- 2003/09/13 05:00
CRDT- 2003/01/31 04:00
PHST- 2003/01/31 04:00 [pubmed]
PHST- 2003/09/13 05:00 [medline]
PHST- 2003/01/31 04:00 [entrez]
AID - DMVLTMPX5KKBJ12M [pii]
PST - ppublish
SO  - Pediatr Pathol Mol Med. 2003 Mar-Apr;22(2):117-29.

PMID- 17057347
OWN - NLM
STAT- MEDLINE
DCOM- 20070116
LR  - 20070724
IS  - 0907-4449 (Print)
IS  - 0907-4449 (Linking)
VI  - 62
IP  - Pt 11
DP  - 2006 Nov
TI  - Structural studies on peanut lectin complexed with disaccharides involving
      different linkages: further insights into the structure and interactions of the
      lectin.
PG  - 1413-21
AB  - Crystal structures of peanut lectin complexed with Galbeta1-3Gal,
      methyl-T-antigen, Galbeta1-6GalNAc, Galalpha1-3Gal and Galalpha1-6Glc and that of
      a crystal grown in the presence of Galalpha1-3Galbeta1-4Gal have been determined 
      using data collected at 100 K. The use of water bridges as a strategy for
      generating carbohydrate specificity was previously deduced from the complexes of 
      the lectin with lactose (Galbeta1-4Glc) and T-antigen (Galbeta1-3GalNAc). This
      has been confirmed by the analysis of the complexes with Galbeta1-3Gal and
      methyl-T-antigen (Galbeta1-3GalNAc-alpha-OMe). A detailed analysis of
      lectin-sugar interactions in the complexes shows that they are more extensive
      when the beta-anomer is involved in the linkage. As expected, the second sugar
      residue is ill-defined when the linkage is 1-->6. There are more than two dozen
      water molecules which occur in the hydration shells of all structures determined 
      at resolutions better than 2.5 A. Most of them are involved in stabilizing the
      structure, particularly loops. Water molecules involved in lectin-sugar
      interactions are also substantially conserved. The lectin molecule is fairly
      rigid and does not appear to be affected by changes in temperature.
FAU - Natchiar, S Kundhavai
AU  - Natchiar SK
AD  - Molecular Biophysics Unit, Indian Institute of Science, Bangalore 560012, India.
FAU - Srinivas, O
AU  - Srinivas O
FAU - Mitra, Nivedita
AU  - Mitra N
FAU - Surolia, A
AU  - Surolia A
FAU - Jayaraman, N
AU  - Jayaraman N
FAU - Vijayan, M
AU  - Vijayan M
LA  - eng
PT  - Comparative Study
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20061018
PL  - United States
TA  - Acta Crystallogr D Biol Crystallogr
JT  - Acta crystallographica. Section D, Biological crystallography
JID - 9305878
RN  - 0 (Disaccharides)
RN  - 0 (Peanut Agglutinin)
SB  - IM
MH  - Disaccharides/*chemistry/metabolism
MH  - *Models, Molecular
MH  - Peanut Agglutinin/*chemistry/metabolism
MH  - Protein Binding
MH  - Protein Structure, Quaternary
MH  - Protein Structure, Secondary
MH  - Structure-Activity Relationship
EDAT- 2006/10/24 09:00
MHDA- 2007/01/17 09:00
CRDT- 2006/10/24 09:00
PHST- 2006/06/27 00:00 [received]
PHST- 2006/09/04 00:00 [accepted]
PHST- 2006/10/24 09:00 [pubmed]
PHST- 2007/01/17 09:00 [medline]
PHST- 2006/10/24 09:00 [entrez]
AID - S0907444906035712 [pii]
AID - 10.1107/S0907444906035712 [doi]
PST - ppublish
SO  - Acta Crystallogr D Biol Crystallogr. 2006 Nov;62(Pt 11):1413-21. doi:
      10.1107/S0907444906035712. Epub 2006 Oct 18.

PMID- 8286201
OWN - NLM
STAT- MEDLINE
DCOM- 19940218
LR  - 20190515
IS  - 0007-0920 (Print)
IS  - 0007-0920 (Linking)
VI  - 69
IP  - 1
DP  - 1994 Jan
TI  - Combined evaluation of preoperative serum sialyl-Tn antigen and carcinoembryonic 
      antigen levels is prognostic for gastric cancer patients.
PG  - 163-6
AB  - We have found that elevation of preoperative serum sialyl-Tn antigen (STN) levels
      is associated with a poor prognosis for gastric cancer patients, and these high
      levels remain in the advanced stage of the disease. We have now examined findings
      with the combined assay of STN and carcinoembryonic antigen (CEA) levels with
      regard to prediction of the prognosis of gastric cancer patients. Serum CEA
      levels and STN levels were determined preoperatively in 349 Japanese patients
      with gastric cancer. The patients were divided into four groups: (A) the CEA (-) 
      STN (-) group (CEA < or = 5 ng ml-1, STN < or = 45 U ml-1, n = 286); (B) the CEA 
      (-) STN (+) group (CEA < or = 5 ng ml-1, STN > 45 U ml-1, n = 31); (C) the CEA
      (+) STN (-) group (CEA > 5 ng ml-1, STN < or = 45 U ml-1, n = 17); and (D) the
      CEA (+) STN (+) group (CEA > 5 ng ml-1, STN > 45 U ml-1, n = 15).
      Clinicopathological features and the prognosis of these groups were examined. The
      distribution of two markers showed no significant correlation. The patients in
      the CEA (+) STN (+) group (group D) had more advanced disease than the patients
      in CEA (-) STN (-) group (group A); tumour size was larger, serosal invasion was 
      prominent, lymphatic and vascular involvement was frequent and the tumour was
      more infiltrative. Lymph node metastasis and hepatic metastasis were more common.
      Total gastrectomy was usually performed, and the non-curative rate was higher.
      The 5-year survival of patients in the CEA (+) STN (+) (group D) was 14.5 +/-
      9.5%, that is lower than that of patients in any other group [CEA (+) STN (-)
      (group C) 44.1 +/- 12.7% (P < 0.05); CEA (-) STN (+) (group B) 60.1 +/- 9.5% (P >
      0.05); CEA (-) STN (-) (group A) 77.6 +/- 9.5% (P < 0.05)]. This combined assay
      of these markers will aid in estimating the prognosis and selecting appropriate
      drugs and care for gastric cancer patients.
FAU - Takahashi, I
AU  - Takahashi I
AD  - Cancer Center of Kyushu University Hospital, Fukuoka, Japan.
FAU - Maehara, Y
AU  - Maehara Y
FAU - Kusumoto, T
AU  - Kusumoto T
FAU - Kohnoe, S
AU  - Kohnoe S
FAU - Kakeji, Y
AU  - Kakeji Y
FAU - Baba, H
AU  - Baba H
FAU - Sugimachi, K
AU  - Sugimachi K
LA  - eng
PT  - Clinical Trial
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - Br J Cancer
JT  - British journal of cancer
JID - 0370635
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Biomarkers, Tumor)
RN  - 0 (Carcinoembryonic Antigen)
RN  - 0 (sialosyl-Tn antigen)
SB  - IM
MH  - Aged
MH  - Antigens, Tumor-Associated, Carbohydrate/*blood
MH  - Biomarkers, Tumor/*blood
MH  - Carcinoembryonic Antigen/*blood
MH  - Evaluation Studies as Topic
MH  - Female
MH  - Follow-Up Studies
MH  - Humans
MH  - Male
MH  - Middle Aged
MH  - Predictive Value of Tests
MH  - Prognosis
MH  - Stomach Neoplasms/*blood/metabolism/pathology
PMC - PMC1968791
EDAT- 1994/01/01 00:00
MHDA- 1994/01/01 00:01
CRDT- 1994/01/01 00:00
PHST- 1994/01/01 00:00 [pubmed]
PHST- 1994/01/01 00:01 [medline]
PHST- 1994/01/01 00:00 [entrez]
AID - 10.1038/bjc.1994.27 [doi]
PST - ppublish
SO  - Br J Cancer. 1994 Jan;69(1):163-6. doi: 10.1038/bjc.1994.27.

PMID- 3940648
OWN - NLM
STAT- MEDLINE
DCOM- 19860220
LR  - 20151119
IS  - 0008-5472 (Print)
IS  - 0008-5472 (Linking)
VI  - 46
IP  - 2
DP  - 1986 Feb
TI  - Analysis of a human tumor-associated glycoprotein (TAG-72) identified by
      monoclonal antibody B72.3.
PG  - 850-7
AB  - Monoclonal antibody B72.3 binds a high-molecular-weight tumor-associated
      glycoprotein identified as TAG-72. This study reports the partial purification
      and characterization of TAG-72 from a xenograft of a human carcinoma cell line,
      LS-174T, which expresses high levels of this antigen. The tumor homogenate was
      initially fractionated by Sepharose CL-4B chromatography. The
      high-molecular-weight TAG-72, found in the exclusion volume, was then subjected
      to two sequential passages through B72.3 antibody affinity columns. At each step 
      of the procedure, TAG-72 content was quantitated using a competition
      radioimmunoassay, and the degree of purification was expressed as the ratio of
      antigen in units to total protein. The three-step procedure produced a
      purification of TAG-72 with minimal contamination by other proteins as shown by
      polyacrylamide gel electrophoresis, followed by staining with Coomassie Blue or
      periodic acid/Schiff reagent. The density of affinity-purified TAG-72, as
      determined by cesium chloride gradient ultracentrifugation, was found to be 1.45 
      g/ml. This density determination, together with the high molecular weight of
      TAG-72, its resistance to Chondroitinase digestion, the presence of blood
      group-related oligosaccharides, and sensitivity to shearing into
      lower-molecular-weight forms suggest that TAG-72 is a mucin-like molecule.
FAU - Johnson, V G
AU  - Johnson VG
FAU - Schlom, J
AU  - Schlom J
FAU - Paterson, A J
AU  - Paterson AJ
FAU - Bennett, J
AU  - Bennett J
FAU - Magnani, J L
AU  - Magnani JL
FAU - Colcher, D
AU  - Colcher D
LA  - eng
PT  - Journal Article
PL  - United States
TA  - Cancer Res
JT  - Cancer research
JID - 2984705R
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens, Neoplasm)
RN  - 0 (Blood Group Antigens)
RN  - 0 (Glycoproteins)
RN  - 0 (Mucins)
RN  - 0 (Neoplasm Proteins)
SB  - IM
MH  - Antibodies, Monoclonal
MH  - Antigens, Neoplasm/immunology/*isolation & purification
MH  - Blood Group Antigens
MH  - Carbohydrate Sequence
MH  - Cytoplasm/immunology
MH  - Electrophoresis, Polyacrylamide Gel
MH  - Glycoproteins/immunology/*isolation & purification
MH  - Humans
MH  - Molecular Weight
MH  - Mucins/immunology/*isolation & purification
MH  - Neoplasm Proteins/immunology/*isolation & purification
MH  - Ultracentrifugation
EDAT- 1986/02/01 00:00
MHDA- 1986/02/01 00:01
CRDT- 1986/02/01 00:00
PHST- 1986/02/01 00:00 [pubmed]
PHST- 1986/02/01 00:01 [medline]
PHST- 1986/02/01 00:00 [entrez]
PST - ppublish
SO  - Cancer Res. 1986 Feb;46(2):850-7.

PMID- 16563047
OWN - NLM
STAT- MEDLINE
DCOM- 20060518
LR  - 20161021
IS  - 0894-203X (Print)
IS  - 0894-203X (Linking)
VI  - 22
IP  - 1
DP  - 2006
TI  - H-deficient Bombay and para-Bombay red blood cells are most strongly agglutinated
      by the galactophilic lectins of Aplysia and Pseudomonas aeruginosa that detect I 
      and P1 antigens.
PG  - 15-22
AB  - The galactophilic lectins Aplysia gonad lectin (AGL) and Pseudomonas aeruginosa
      lectin (PA-IL), which detect human I and P1 RBC antigens, were examined for
      hemagglutination of H+ (group O and B) and H-deficient (Bombay and para-Bombay
      phenotype) RBCs. The results were compared with those obtained using two other
      galactophilic lectins, Maclura pomifera lectin (MPL) and Arachis hypogaea
      (peanut) agglutinin (PNA), which share T-antigen affinity, and two fucose-binding
      H-specific lectins, Ulex europaeus (UEA-I) and Pseudomonas aeruginosa lectin
      (PA-IIL), as well as with those achieved with anti-I serum. The results revealed 
      that, in contrast to UEA-I and PA-IIL, which preferentially agglutinated H+ RBCs,
      and to MPL and PNA, which similarly agglutinated all examined RBCs, AGL, PA-IL,
      and the anti-I serum agglutinated the H-deficient RBCs more strongly than did the
      H+ RBCs. These findings could be attributed to increased levels of I and P1
      antigens on those RBCs resulting from the use of the free common H-type 2
      precursor for their synthesis. Since both PA-IL and PA-IIL are regarded as
      potential pathogen adhesins, it would be interesting to statistically compare the
      sensitivities of individuals of H+ and H-deficient RBC populations to P.
      aeruginosa infections.
FAU - Gilboa-Garber, N
AU  - Gilboa-Garber N
AD  - Faculty of Life Sciences, Bar-Ilan University, Ramat-Gan 52900, Israel.
FAU - Sudakevitz, D
AU  - Sudakevitz D
FAU - Levene, C
AU  - Levene C
FAU - Rahimi-Levene, N
AU  - Rahimi-Levene N
FAU - Yahalom, V
AU  - Yahalom V
LA  - eng
PT  - Journal Article
PL  - United States
TA  - Immunohematology
JT  - Immunohematology
JID - 8806387
RN  - 0 (ABO Blood-Group System)
RN  - 0 (Adhesins, Bacterial)
RN  - 0 (Galectins)
RN  - 0 (Globosides)
RN  - 0 (I Blood-Group System)
RN  - 0 (Lectins)
RN  - 0 (adhesin, Pseudomonas)
RN  - 0 (galactopyranosyl-1-4-paragloboside)
SB  - IM
MH  - ABO Blood-Group System/*analysis
MH  - Adhesins, Bacterial/blood/*chemistry
MH  - Animals
MH  - Aplysia/*chemistry
MH  - Blood Grouping and Crossmatching/methods
MH  - Erythrocytes/chemistry/microbiology
MH  - Galectins/blood/*chemistry
MH  - Globosides/*analysis/blood
MH  - Hemagglutination
MH  - Humans
MH  - I Blood-Group System/*analysis
MH  - Lectins/blood/*chemistry
MH  - Pseudomonas Infections/blood
EDAT- 2006/03/28 09:00
MHDA- 2006/05/19 09:00
CRDT- 2006/03/28 09:00
PHST- 2006/03/28 09:00 [pubmed]
PHST- 2006/05/19 09:00 [medline]
PHST- 2006/03/28 09:00 [entrez]
PST - ppublish
SO  - Immunohematology. 2006;22(1):15-22.

PMID- 2418872
OWN - NLM
STAT- MEDLINE
DCOM- 19860403
LR  - 20071114
IS  - 0006-2960 (Print)
IS  - 0006-2960 (Linking)
VI  - 24
IP  - 26
DP  - 1985 Dec 17
TI  - Analysis of the specificity of five murine anti-blood group A monoclonal
      antibodies, including one that identifies type 3 and type 4 A determinants.
PG  - 7820-6
AB  - The specificity of five mouse monoclonal anti-A blood group antibodies (Ab), four
      of which were produced by immunization with cultured human cancer cells and one
      with a synthetic antigen, has been determined by examining their reactivity with 
      purified A glycolipids, erythrocyte glycolipids, oligosaccharides, ovarian cyst
      glycoproteins, and salivary glycoproteins. Two of the antibodies (HT29-36 and CB)
      reacted with all A variant structures tested and have a broad anti-A reactivity. 
      Ab CLH6 did not agglutinate A erythrocytes and reacted preferentially with the
      type 1A structure. Ab S12 agglutinated all A1 erythrocytes and reacted best with 
      simple, monofucosyl type 2 A structures, such as Aa-2, Ab-2, and A
      tetrasaccharide. Ab M2 has a novel, but complex, spectrum of reactivity. It
      reacts with type 3 and type 4 A chains and not with type 1 and type 2 A chains.
      It appears to recognize both an external A structure (formula; see text) (I)
      (found) in type 3 and type 4 chains) and also an internal structure (II) found in
      type 3 chains. Ab M2 agglutinates all A and AB erythrocytes but does not react
      with salivary glycoproteins.
FAU - Furukawa, K
AU  - Furukawa K
FAU - Clausen, H
AU  - Clausen H
FAU - Hakomori, S
AU  - Hakomori S
FAU - Sakamoto, J
AU  - Sakamoto J
FAU - Look, K
AU  - Look K
FAU - Lundblad, A
AU  - Lundblad A
FAU - Mattes, M J
AU  - Mattes MJ
FAU - Lloyd, K O
AU  - Lloyd KO
LA  - eng
GR  - CA-08748/CA/NCI NIH HHS/United States
GR  - CA-19224/CA/NCI NIH HHS/United States
GR  - CA-34039/CA/NCI NIH HHS/United States
GR  - etc.
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Biochemistry
JT  - Biochemistry
JID - 0370623
RN  - 0 (ABO Blood-Group System)
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Epitopes)
RN  - 0 (Glycolipids)
RN  - 0 (Glycoproteins)
RN  - 0 (Oligosaccharides)
SB  - IM
MH  - ABO Blood-Group System/*immunology
MH  - Animals
MH  - Antibodies, Monoclonal/*immunology
MH  - Antibody Specificity
MH  - Cell Line
MH  - Epitopes/immunology
MH  - Erythrocytes/immunology
MH  - Glycolipids/immunology
MH  - Glycoproteins/immunology
MH  - Hemagglutination
MH  - Humans
MH  - Mice
MH  - Neoplasms/immunology
MH  - Oligosaccharides/immunology
EDAT- 1985/12/17 00:00
MHDA- 1985/12/17 00:01
CRDT- 1985/12/17 00:00
PHST- 1985/12/17 00:00 [pubmed]
PHST- 1985/12/17 00:01 [medline]
PHST- 1985/12/17 00:00 [entrez]
PST - ppublish
SO  - Biochemistry. 1985 Dec 17;24(26):7820-6.

PMID- 6203895
OWN - NLM
STAT- MEDLINE
DCOM- 19840730
LR  - 20101118
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 259
IP  - 12
DP  - 1984 Jun 25
TI  - A monoclonal antibody recognizes an O-acylated sialic acid in a human
      melanoma-associated ganglioside.
PG  - 7453-9
AB  - Monoclonal antibody D1.1 originally prepared against the B49 cell line derived
      from a rat brain tumor was shown to react with a ganglioside present in fetal rat
      brain. We have found that this antigen is also present in human malignant
      melanoma tumors as well as many melanoma cell lines. The ganglioside from human
      melanoma cell lines migrates between GM1 and GM2 on one-dimensional thin layer
      chromatography. Analysis by two-dimensional thin layer chromatography with
      intermediate ammonia treatment suggests that the ganglioside contains one or more
      base-labile O-acyl esters. Mild base hydrolysis under conditions known to remove 
      O-acyl esters results in complete loss of antigenic reactivity. Thus, the
      alkali-labile moiety is a critical component of the epitope recognized by the
      antibody. Analysis of the sialic acids of total gangliosides from
      [6-3H]glucosamine-labeled melanoma cells showed that approximately 10% of these
      molecules are O-acylated. Similar analysis of the purified ganglioside showed
      that greater than 30% of the sialic acids comigrated with authentic
      9-O-acetyl-N-acetylneuraminic acid. The antibody did not cross-react with normal 
      human skin melanocytes nor with any of a large number of normal human adult and
      fetal tissues. The antibody also did not react with numerous other malignant cell
      lines studied. These findings suggest that the antigenic epitope defined by
      antibody D1.1 contains an O-acylated sialic acid and may arise from aberrant
      O-acetylation occurring in human malignant melanoma cells.
FAU - Cheresh, D A
AU  - Cheresh DA
FAU - Varki, A P
AU  - Varki AP
FAU - Varki, N M
AU  - Varki NM
FAU - Stallcup, W B
AU  - Stallcup WB
FAU - Levine, J
AU  - Levine J
FAU - Reisfeld, R A
AU  - Reisfeld RA
LA  - eng
GR  - CA28420/CA/NCI NIH HHS/United States
GR  - GM32373/GM/NIGMS NIH HHS/United States
GR  - NS16112/NS/NINDS NIH HHS/United States
GR  - etc.
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens, Neoplasm)
RN  - 0 (Epitopes)
RN  - 0 (Gangliosides)
RN  - 0 (Melanoma-Specific Antigens)
RN  - 0 (Neoplasm Proteins)
RN  - 0 (Sialic Acids)
SB  - IM
MH  - Animals
MH  - Antibodies, Monoclonal/*immunology
MH  - Antigens, Neoplasm
MH  - Brain Neoplasms/immunology
MH  - Cell Line
MH  - Chromatography, Paper
MH  - Epitopes/*analysis
MH  - Gangliosides/*immunology
MH  - Humans
MH  - Hydrogen-Ion Concentration
MH  - Melanoma/immunology
MH  - Melanoma-Specific Antigens
MH  - Neoplasm Proteins/*immunology
MH  - Rats
MH  - Sialic Acids/*immunology
EDAT- 1984/06/25 00:00
MHDA- 1984/06/25 00:01
CRDT- 1984/06/25 00:00
PHST- 1984/06/25 00:00 [pubmed]
PHST- 1984/06/25 00:01 [medline]
PHST- 1984/06/25 00:00 [entrez]
PST - ppublish
SO  - J Biol Chem. 1984 Jun 25;259(12):7453-9.

PMID- 16140958
OWN - NLM
STAT- MEDLINE
DCOM- 20051115
LR  - 20081121
IS  - 0008-5472 (Print)
IS  - 0008-5472 (Linking)
VI  - 65
IP  - 17
DP  - 2005 Sep 1
TI  - Molecular basis of incomplete O-glycan synthesis in MCF-7 breast cancer cells:
      putative role of MUC6 in Tn antigen expression.
PG  - 7880-7
AB  - An incomplete elongation of O-glycan saccharide chains in mucins have been found 
      in epithelial cancers, leading to the expression of shorter carbohydrate
      structures, such as the Tn antigen (GalNAc-O-Ser/Thr). This antigen is one of the
      most specific human cancer-associated structures and is capable of inducing
      effective immune responses against cancer cells. We aimed to investigate the
      causes of the expression of Tn antigen in the Tn-rich MCF-7 breast cancer cell
      line focusing on the first step of the O-glycosylation process. Interestingly,
      amino acid sequences derived from "non-mammary" apomucins (MUC5B and MUC6) were
      very good acceptor substrates for ppGalNAc-Ts, which are the enzymes catalyzing
      the Tn antigen synthesis. MUC6 peptide glycosylation with MCF-7 microsome
      extracts as source of ppGalNAc-T activity yielded 95% conversion of the peptide
      into MUC6-Tn. In addition, the MUC6-Tn glycopeptide was a poor acceptor substrate
      for core 1 beta3Gal-T, the next enzyme involved in the saccharide chain
      biosynthesis, yielding only 5% conversion of MUC6-Tn into MUC6-TF. These results 
      indicate that non-mammary apomucin expression could be responsible, at least in
      part, for Tn antigen expression in MCF-7 breast cancer cells due to a combined
      action on glycosyltransferases: an increase of ppGalNAc-T activity and a decrease
      of core 1 beta3Gal-T activity. Our hypothesis is supported by experiments in vivo
      showing that (a) native MUC6 glycoproteins express the Tn antigen in MCF-7 cells 
      and (b) Tn antigen expression is increased after transfection with a construct
      encoding for a MUC6 recombinant protein into the low Tn-expressing breast cancer 
      cell T47D. These results open new horizons in breast cancer glycoimmunology,
      stressing the potential role of non-mammary apomucins.
FAU - Freire, Teresa
AU  - Freire T
AD  - Laboratorio de Oncologia Basica y Biologia Molecular, Departamento de Bioquimica,
      Facultad de Medicina, Universidad de la Republica, Montevideo, Uruguay.
FAU - Bay, Sylvie
AU  - Bay S
FAU - von Mensdorff-Pouilly, Silvia
AU  - von Mensdorff-Pouilly S
FAU - Osinaga, Eduardo
AU  - Osinaga E
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Cancer Res
JT  - Cancer research
JID - 2984705R
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Glycopeptides)
RN  - 0 (MUC6 protein, human)
RN  - 0 (Mucin-6)
RN  - 0 (Mucins)
RN  - 0 (Polysaccharides)
RN  - 0 (Tn antigen)
SB  - IM
MH  - Amino Acid Sequence
MH  - Antigens, Tumor-Associated, Carbohydrate/*biosynthesis/immunology
MH  - Breast Neoplasms/genetics/immunology/*metabolism
MH  - Cell Line, Tumor
MH  - Glycopeptides/immunology/metabolism
MH  - Glycosylation
MH  - Humans
MH  - Molecular Sequence Data
MH  - Mucin-6
MH  - Mucins/genetics/immunology/*metabolism
MH  - Polysaccharides/*biosynthesis
MH  - Transfection
EDAT- 2005/09/06 09:00
MHDA- 2005/11/16 09:00
CRDT- 2005/09/06 09:00
PHST- 2005/09/06 09:00 [pubmed]
PHST- 2005/11/16 09:00 [medline]
PHST- 2005/09/06 09:00 [entrez]
AID - 65/17/7880 [pii]
AID - 10.1158/0008-5472.CAN-04-3746 [doi]
PST - ppublish
SO  - Cancer Res. 2005 Sep 1;65(17):7880-7. doi: 10.1158/0008-5472.CAN-04-3746.

PMID- 12547345
OWN - NLM
STAT- MEDLINE
DCOM- 20030606
LR  - 20061115
IS  - 0020-7519 (Print)
IS  - 0020-7519 (Linking)
VI  - 33
IP  - 1
DP  - 2003 Jan
TI  - Mucin-type O-glycosylation in Fasciola hepatica: characterisation of
      carcinoma-associated Tn and sialyl-Tn antigens and evaluation of
      UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase activity.
PG  - 47-56
AB  - Simple mucin-type cancer-associated O-glycan structures, such as the Tn antigen
      (GalNAc-O-Ser/Thr), are expressed by certain helminth parasites. These antigens
      are involved in several types of receptor-ligand interactions, and they are
      potential targets for immunotherapy. The aim of this work was to study the
      initiation pathway of mucin-type O-glycosylation in Fasciola hepatica, performing
      a biochemical and immunohistochemical characterisation of Tn and sialyl-Tn
      antigens, and evaluating the ppGaNTase activity, which catalyses the first step
      in O-glycan biosynthesis. Using ELISA, both Tn and sialyl-Tn antigens were
      detected predominantly in the somatic and deoxycholate extracts.
      Immunofluorescence analysis revealed that Tn antigen is preferentially expressed 
      in testis, while sialyl-Tn glycoproteins were more widely distributed, being
      present in parenchymal cells, basal membrane of the tegument, and apical surface 
      of epithelial cells lining the caeca. On the basis of their electrophoretic
      mobility, Tn glycoproteins were resolved as six components of 10, 37, 76, 125,
      170 and 205 kDa, and sialyl-Tn components showed an apparent molecular mass of 28
      and 32 kDa, and two broad bands of 90-110 and 170-190 kDa. The observation that
      only the 76 kDa Tn-glycoprotein remained in the 0.6 N perchloric acid-soluble
      fraction suggests that it could be a good candidate for mucin characterisation in
      this parasite. The ppGaNTase activity showed its maximal activity at pH 7-7.5 and
      37 degrees C, showing that Mn(2+) was the best divalent cation activator. Using a
      panel of nine synthetic peptides as acceptor substrates, we found that F.
      hepatica ppGaNTase was able to glycosylate both threonines and serines, the best 
      substrates being the peptides derived from the tandem repeat region of human
      mucins (MUC2 and MUC6), and from Trypanosoma cruzi and Trypanosoma brucei
      glycoproteins. The results reported here constitute the first evidence on
      O-glycosylation pathways in F. hepatica, and may help to identify new biological 
      characteristics of this parasite as well as of the host-parasite relationship.
FAU - Freire, Teresa
AU  - Freire T
AD  - Departamento de Bioqui;mica, Facultad de Medicina, Universidad de la Republica,
      Montevideo, Uruguay.
FAU - Casaravilla, Cecilia
AU  - Casaravilla C
FAU - Carmona, Carlos
AU  - Carmona C
FAU - Osinaga, Eduardo
AU  - Osinaga E
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - Int J Parasitol
JT  - International journal for parasitology
JID - 0314024
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens, Helminth)
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Tn antigen)
RN  - 0 (sialosyl-Tn antigen)
RN  - EC 2.4.1.- (N-Acetylgalactosaminyltransferases)
RN  - EC 2.4.1.41 (polypeptide N-acetylgalactosaminyltransferase)
SB  - IM
MH  - Animals
MH  - Antibodies, Monoclonal/immunology
MH  - Antigens, Helminth/*metabolism
MH  - Antigens, Tumor-Associated, Carbohydrate/genetics/immunology/*metabolism
MH  - Electrophoresis, Polyacrylamide Gel
MH  - Enzyme-Linked Immunosorbent Assay
MH  - Fasciola hepatica/enzymology/*immunology
MH  - Glycosylation
MH  - Hydrogen-Ion Concentration
MH  - Male
MH  - N-Acetylgalactosaminyltransferases/*metabolism
MH  - Testis/immunology
EDAT- 2003/01/28 04:00
MHDA- 2003/06/07 05:00
CRDT- 2003/01/28 04:00
PHST- 2003/01/28 04:00 [pubmed]
PHST- 2003/06/07 05:00 [medline]
PHST- 2003/01/28 04:00 [entrez]
AID - S002075190200231X [pii]
PST - ppublish
SO  - Int J Parasitol. 2003 Jan;33(1):47-56.

PMID- 20103942
OWN - NLM
STAT- MEDLINE
DCOM- 20100518
LR  - 20100127
IS  - 1881-7823 (Electronic)
IS  - 1881-7815 (Linking)
VI  - 3
IP  - 1
DP  - 2009 Feb
TI  - Inhibition of cancer cell growth by anti-Tn monoclonal antibody MLS128.
PG  - 32-7
AB  - Tn-antigens are generally masked by covalently linked carbohydrates but are
      exposed in most primary and metastatic epithelial malignant tumors, providing
      sensitive markers for detection of carcinoma. Here, therapeutic potentials of
      tumor-associated carbohydrate antigen-specific antibodies were investigated.
      MLS128, an anti-Tn monoclonal antibody, binds to a carbohydrate epitope
      consisting of three consecutive Tn-antigens (GalNAcalpha-Ser/Thr). MLS128
      treatment significantly inhibited colon and breast cancer cell growth. MLS128
      bound to 110-210 kDa glycoproteins on the cell surface. MLS128 treatment caused
      down-regulation of insulin-like growth factor-I receptor and epidermal growth
      factor receptor in LS180 colon cancer cells, suggesting that MLS128-inhibited
      cancer cell growth is in part mediated by down-regulation of growth factor
      receptors. This study provides the first insights into the potential use of this 
      particular type of anti-Tn antigen antibodies as a cancer therapeutic.
FAU - Morita, Noriyuki
AU  - Morita N
AD  - Department of Applied Biochemistry, Tokai University School of Engineering,
      Hiratsuka, Kanagawa, Japan.
FAU - Yajima, Yukiko
AU  - Yajima Y
FAU - Asanuma, Hideki
AU  - Asanuma H
FAU - Nakada, Hiroshi
AU  - Nakada H
FAU - Fujita-Yamaguchi, Yoko
AU  - Fujita-Yamaguchi Y
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - Japan
TA  - Biosci Trends
JT  - Bioscience trends
JID - 101502754
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Tn antigen)
SB  - IM
MH  - Antibodies, Monoclonal/immunology/pharmacology/*therapeutic use
MH  - Antigens, Tumor-Associated, Carbohydrate/*immunology
MH  - Blotting, Western
MH  - Cell Line, Tumor
MH  - Cell Proliferation/drug effects
MH  - Humans
MH  - Neoplasms/*drug therapy/metabolism
EDAT- 2010/01/28 06:00
MHDA- 2010/05/19 06:00
CRDT- 2010/01/28 06:00
PHST- 2010/01/28 06:00 [entrez]
PHST- 2010/01/28 06:00 [pubmed]
PHST- 2010/05/19 06:00 [medline]
PST - ppublish
SO  - Biosci Trends. 2009 Feb;3(1):32-7.

PMID- 9261149
OWN - NLM
STAT- MEDLINE
DCOM- 19970915
LR  - 20190508
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 272
IP  - 34
DP  - 1997 Aug 22
TI  - Cloning and heterologous expression of an alpha1,3-fucosyltransferase gene from
      the gastric pathogen Helicobacter pylori.
PG  - 21357-63
AB  - Helicobacter pylori is an important human pathogen which causes both gastric and 
      duodenal ulcers and is also associated with gastric cancer and lymphoma. This
      microorganism has been shown to express cell surface glycoconjugates including
      Lewis X (Lex) and Lewis Y. These bacterial oligosaccharides are structurally
      similar to tumor-associated carbohydrate antigens found in mammals. In this
      study, we report the cloning of a novel alpha1,3-fucosyltransferase gene (HpfucT)
      involved in the biosynthesis of Lex within H. pylori. The deduced amino acid
      sequence of HpfucT consists of 478 residues with the calculated molecular mass of
      56,194 daltons, which is approximately 100 amino acids longer than known
      mammalian alpha1,3/1,4-fucosyltransferases. The approximately 52-kDa protein
      encoded by HpfucT was expressed in Escherichia coli CSRDE3 cells and gave rise to
      alpha1,3-fucosyltransferase activity but neither alpha1,4-fucosyltransferase nor 
      alpha1,2-fucosyltransferase activity as characterized by radiochemical assays and
      capillary zone electrophoresis. Truncation of the C-terminal 100 amino acids of
      HpFuc-T abolished the enzyme activity. An approximately 72-amino acid region of
      HpFuc-T exhibits significant sequence identity (40-45%) with the highly conserved
      C-terminal catalytic domain among known mammalian and chicken
      alpha1,3-fucosyltransferases. These lines of evidence indicate that the HpFuc-T
      represents the bacterial alpha1,3-fucosyltransferase. In addition, several
      structural features unique to HpFuc-T, including 10 direct repeats of seven amino
      acids and the lack of the transmembrane segment typical for known eukaryotic
      alpha1,3-fucosyltransferases, were revealed. Notably, the repeat region contains 
      a leucine zipper motif previously demonstrated to be responsible for dimerization
      of various basic region-leucine zipper proteins, suggesting that the HpFuc-T
      protein could form dimers.
FAU - Ge, Z
AU  - Ge Z
AD  - Department of Medical Microbiology and Immunology, University of Alberta,
      Edmonton, Alberta, Canada T6G 2H7.
FAU - Chan, N W
AU  - Chan NW
FAU - Palcic, M M
AU  - Palcic MM
FAU - Taylor, D E
AU  - Taylor DE
LA  - eng
SI  - GENBANK/AF008596
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Bacterial Proteins)
RN  - 0 (Lewis X Antigen)
RN  - 0 (Recombinant Proteins)
RN  - EC 2.4.1.- (Fucosyltransferases)
RN  - EC 2.4.1.152 (galactoside 3-fucosyltransferase)
SB  - IM
MH  - Amino Acid Sequence
MH  - Bacterial Proteins/chemistry/genetics
MH  - Base Sequence
MH  - Cloning, Molecular
MH  - Escherichia coli
MH  - Fucosyltransferases/*genetics/metabolism
MH  - *Genes, Bacterial
MH  - Helicobacter pylori/*enzymology/genetics
MH  - Lewis X Antigen/*biosynthesis
MH  - Molecular Sequence Data
MH  - Recombinant Proteins
MH  - Regulatory Sequences, Nucleic Acid
MH  - Sequence Alignment
MH  - Sequence Homology, Amino Acid
MH  - Solubility
EDAT- 1997/08/22 00:00
MHDA- 1997/08/22 00:01
CRDT- 1997/08/22 00:00
PHST- 1997/08/22 00:00 [pubmed]
PHST- 1997/08/22 00:01 [medline]
PHST- 1997/08/22 00:00 [entrez]
AID - 10.1074/jbc.272.34.21357 [doi]
PST - ppublish
SO  - J Biol Chem. 1997 Aug 22;272(34):21357-63. doi: 10.1074/jbc.272.34.21357.

PMID- 8654583
OWN - NLM
STAT- MEDLINE
DCOM- 19960801
LR  - 20031114
IS  - 0014-5793 (Print)
IS  - 0014-5793 (Linking)
VI  - 388
IP  - 1
DP  - 1996 Jun 10
TI  - Antigen binding of antiganglioside antibodies in vitro is strongly influenced by 
      the ganglioside composition of the sample.
PG  - 29-33
AB  - The ability of antiganglioside antibodies to detect their respective antigens in 
      various environments was studied. In contrast to sensitive detection of pure
      ganglioside standards by ELISA, antibody binding to mixtures of gangliosides was 
      drastically reduced. This loss of sensitivity also occurred with immunostaining
      of gangliosides absorbed to silica gel. Moreover, absorption of antibodies to
      antigen-containing lipid vesicles failed, if the vesicles were prepared together 
      with other gangliosides. These data indicate that antigen accessibility is
      strongly influenced by surrounding gangliosides. This should be considered
      whenever gangliosides are traced by antibodies. The ELISA procedure appears
      useful to test for such properties.
FAU - Hildebrandt, H
AU  - Hildebrandt H
AD  - Institut fur Zoologie, Universitat Hohenheim, Stuttgart, Germany.
LA  - eng
PT  - Journal Article
PL  - England
TA  - FEBS Lett
JT  - FEBS letters
JID - 0155157
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Gangliosides)
SB  - IM
MH  - Animals
MH  - *Antibodies, Monoclonal
MH  - Antibody Specificity
MH  - *Antigen-Antibody Reactions
MH  - Brain
MH  - Enzyme-Linked Immunosorbent Assay/*methods
MH  - Gangliosides/*analysis/chemistry/immunology
MH  - Osmolar Concentration
MH  - Rats
MH  - Sensitivity and Specificity
EDAT- 1996/06/10 00:00
MHDA- 1996/06/10 00:01
CRDT- 1996/06/10 00:00
PHST- 1996/06/10 00:00 [pubmed]
PHST- 1996/06/10 00:01 [medline]
PHST- 1996/06/10 00:00 [entrez]
AID - 0014-5793(96)00503-0 [pii]
PST - ppublish
SO  - FEBS Lett. 1996 Jun 10;388(1):29-33.

PMID- 8575847
OWN - NLM
STAT- MEDLINE
DCOM- 19960313
LR  - 20160303
IS  - 0020-7136 (Print)
IS  - 0020-7136 (Linking)
VI  - 65
IP  - 3
DP  - 1996 Jan 26
TI  - Sialyl Tn antigen is an independent predictor of outcome in patients with gastric
      cancer.
PG  - 295-300
AB  - The prognostic value of the immunohistochemical expression of Sialyl Tn antigen
      (STn) was evaluated in 242 patients with gastric carcinoma. Formalin-fixed,
      paraffin-embedded specimens of gastric adenocarcinomas were stained with the
      monoclonal antibody C1282, produced by immunization with ovine submaxillary mucin
      (OSM). Positive immunoreactivity for STn was observed in 149 (62%) patients. The 
      expression of STn did not correlate with stage of disease (TNM), tumour location,
      presence of lymph-node or distant metastases, histological type, age or gender.
      STn immunoreactivity correlated strongly with overall survival in univariate
      analysis. The median survival in the STn-positive group was 21 months, in
      comparison to 38 months in the STn-negative group. The difference in survival
      between STn-negative and STn-positive tumours was significant in patients with
      stage-I cancer, but not in patients with stage-II -III or -IV disease. STn
      immunoreactivity emerged as an independent prognostic factor in Cox multivariate 
      analysis. It is concluded that the immunohistochemical expression of STn is a
      good marker in the prediction of survival in patients with stage-I gastric
      carcinoma.
FAU - Victorzon, M
AU  - Victorzon M
AD  - Fourth Department of Surgery, University of Helsinki, Finland.
FAU - Nordling, S
AU  - Nordling S
FAU - Nilsson, O
AU  - Nilsson O
FAU - Roberts, P J
AU  - Roberts PJ
FAU - Haglund, C
AU  - Haglund C
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Int J Cancer
JT  - International journal of cancer
JID - 0042124
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Biomarkers, Tumor)
RN  - 0 (Tn antigen)
SB  - IM
MH  - Adenocarcinoma/*metabolism/physiopathology
MH  - Adult
MH  - Aged
MH  - Aged, 80 and over
MH  - Antigens, Tumor-Associated, Carbohydrate/*analysis
MH  - Biomarkers, Tumor/*analysis
MH  - Female
MH  - Humans
MH  - Immunohistochemistry
MH  - Male
MH  - Middle Aged
MH  - Predictive Value of Tests
MH  - Prognosis
MH  - Stomach Neoplasms/*metabolism/physiopathology
EDAT- 1996/01/26 00:00
MHDA- 2000/06/20 09:00
CRDT- 1996/01/26 00:00
PHST- 1996/01/26 00:00 [pubmed]
PHST- 2000/06/20 09:00 [medline]
PHST- 1996/01/26 00:00 [entrez]
AID - 10.1002/(SICI)1097-0215(19960126)65:3<295::AID-IJC3>3.0.CO;2-V [pii]
AID - 10.1002/(SICI)1097-0215(19960126)65:3<295::AID-IJC3>3.0.CO;2-V [doi]
PST - ppublish
SO  - Int J Cancer. 1996 Jan 26;65(3):295-300. doi:
      10.1002/(SICI)1097-0215(19960126)65:3<295::AID-IJC3>3.0.CO;2-V.

PMID- 208994
OWN - NLM
STAT- MEDLINE
DCOM- 19780915
LR  - 20131121
IS  - 0074-7696 (Print)
IS  - 0074-7696 (Linking)
VI  - 53
DP  - 1978
TI  - Cellular adhesiveness and extracellular substrata.
PG  - 65-144
FAU - Grinnell, F
AU  - Grinnell F
LA  - eng
PT  - Journal Article
PT  - Research Support, U.S. Gov't, P.H.S.
PT  - Review
PL  - United States
TA  - Int Rev Cytol
JT  - International review of cytology
JID - 2985180R
RN  - 0 (Culture Media)
RN  - 0 (Proteins)
RN  - E0399OZS9N (Cyclic AMP)
SB  - IM
MH  - Animals
MH  - *Cell Adhesion
MH  - Cell Movement
MH  - Chemotaxis
MH  - Culture Media
MH  - Cyclic AMP/physiology
MH  - Erythrocytes/physiology
MH  - Fibroblasts/physiology
MH  - Foreign-Body Reaction/pathology
MH  - Humans
MH  - Lymphocytes/physiology
MH  - Macrophages/physiology
MH  - Morphogenesis
MH  - Neoplasm Metastasis
MH  - Neoplasms/pathology
MH  - Platelet Adhesiveness
MH  - Proteins/physiology
MH  - Wound Healing
RF  - 627
EDAT- 1978/01/01 00:00
MHDA- 1978/01/01 00:01
CRDT- 1978/01/01 00:00
PHST- 1978/01/01 00:00 [pubmed]
PHST- 1978/01/01 00:01 [medline]
PHST- 1978/01/01 00:00 [entrez]
PST - ppublish
SO  - Int Rev Cytol. 1978;53:65-144.

PMID- 6926850
OWN - NLM
STAT- MEDLINE
DCOM- 19841128
LR  - 20151119
IS  - 0272-457X (Print)
IS  - 0272-457X (Linking)
VI  - 1
IP  - 1
DP  - 1981
TI  - Detection of monoclonal antibody-defined colorectal carcinoma antigen by
      solid-phase binding inhibition radioimmunoassay.
PG  - 37-45
AB  - We have established a solid-phase binding inhibition radioimmunoassay for the
      detection of colorectal carcinoma-specific antigens in tissue culture
      supernatants of human colorectal carcinoma cell lines and in serum and urine of
      colorectal carcinoma patients. Using the [3H]glucosamine-labeled cell membrane
      glycolipid antigen and colorectal carcinoma-specific monoclonal antibodies in
      this assay, we have been able to detect several human colorectal carcinoma
      membrane-specific antigens that are released from the cell membrane into tissue
      culture supernatants, and an antigen detected by antibodies 1116-NS-19-9 and
      1116-NS-52a that is found only in the serum and urine of cancer patients.
FAU - Chang, T H
AU  - Chang TH
FAU - Steplewski, Z
AU  - Steplewski Z
FAU - Sears, H F
AU  - Sears HF
FAU - Koprowski, H
AU  - Koprowski H
LA  - eng
GR  - CA-10815/CA/NCI NIH HHS/United States
GR  - CA-21124/CA/NCI NIH HHS/United States
GR  - RR-05540/RR/NCRR NIH HHS/United States
PT  - Journal Article
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Hybridoma
JT  - Hybridoma
JID - 8202424
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens, Neoplasm)
RN  - 0 (Gangliosides)
RN  - 0 (colon carcinoma monosialoganglioside antigen)
SB  - IM
MH  - *Antibodies, Monoclonal
MH  - Antibody Specificity
MH  - Antigens, Neoplasm/*analysis/immunology/urine
MH  - Cell Line
MH  - Colonic Neoplasms/*immunology/urine
MH  - Gangliosides/*analysis/immunology/urine
MH  - Humans
MH  - Hybridomas
MH  - Radioimmunoassay
MH  - Rectal Neoplasms/*immunology/urine
EDAT- 1981/01/01 00:00
MHDA- 1981/01/01 00:01
CRDT- 1981/01/01 00:00
PHST- 1981/01/01 00:00 [pubmed]
PHST- 1981/01/01 00:01 [medline]
PHST- 1981/01/01 00:00 [entrez]
AID - 10.1089/hyb.1.1981.1.37 [doi]
PST - ppublish
SO  - Hybridoma. 1981;1(1):37-45. doi: 10.1089/hyb.1.1981.1.37.

PMID- 2422108
OWN - NLM
STAT- MEDLINE
DCOM- 19860613
LR  - 20180203
IS  - 0046-8177 (Print)
IS  - 0046-8177 (Linking)
VI  - 17
IP  - 5
DP  - 1986 May
TI  - Use of a monoclonal antibody (B72.3) as a novel immunohistochemical adjunct for
      the diagnosis of carcinomas in fine needle aspiration biopsy specimens.
PG  - 501-13
AB  - Monoclonal antibody B72.3 has been shown to be reactive with a
      high-molecular-weight glycoprotein complex termed TAG(tumor-associated
      glycoprotein)-72. By the avidin-biotin immunoperoxidase method, fine needle
      aspirates and corresponding surgically excised tumor tissues from both malignant 
      and benign tissues were analyzed for TAG-72 expression. Staining (range, 1 to 100
      per cent of tumor cells) with monoclonal antibody B72.3 was observed in needle
      aspirates from 18 of 18 adenocarcinomas and adenosquamous carcinomas of the lung,
      17 of 21 adenocarcinomas of the breast, and six of six adenocarcinomas of the
      colon, as well as adenocarcinomas from other body sites. In contrast, small cell 
      carcinomas of the lung, malignant melanomas, lymphomas, and sarcomas did not
      stain with the antibody. Benign lesions from the breast, lung, pancreas, parotid,
      and thyroid also failed to stain. In 66 patients, tumor-bearing tissue had also
      been resected and was available for comparative examination with monoclonal
      antibody B72.3. In 62 of these 66 patients, the staining patterns in the
      aspirates were found to be predictive of the patterns of antibody reactivity in
      the comparable surgically resected tissues. From these studies it is concluded
      that monoclonal antibody B72.3 defines a tumor-associated antigen that is
      expressed in neoplastic cells but not in benign cells and is most selectively
      expressed in adenocarcinomas. This monoclonal antibody may be used as a novel
      adjunct for the diagnosis of carcinoma in fine needle aspiration biopsy
      specimens.
FAU - Johnston, W W
AU  - Johnston WW
FAU - Szpak, C A
AU  - Szpak CA
FAU - Lottich, S C
AU  - Lottich SC
FAU - Thor, A
AU  - Thor A
FAU - Schlom, J
AU  - Schlom J
LA  - eng
PT  - Journal Article
PL  - United States
TA  - Hum Pathol
JT  - Human pathology
JID - 9421547
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens, Neoplasm)
RN  - 0 (Glycoproteins)
RN  - 0 (tumor-associated antigen 72)
SB  - IM
MH  - *Antibodies, Monoclonal
MH  - Antigens, Neoplasm/metabolism
MH  - Biopsy, Needle
MH  - Breast Neoplasms/metabolism/secondary
MH  - Carcinoma/*diagnosis/pathology
MH  - Glycoproteins/metabolism
MH  - Histocytochemistry/methods
MH  - Humans
MH  - Immunochemistry/methods
MH  - Immunoenzyme Techniques
MH  - Lung Neoplasms/metabolism/secondary
MH  - Staining and Labeling
EDAT- 1986/05/01 00:00
MHDA- 1986/05/01 00:01
CRDT- 1986/05/01 00:00
PHST- 1986/05/01 00:00 [pubmed]
PHST- 1986/05/01 00:01 [medline]
PHST- 1986/05/01 00:00 [entrez]
AID - S0046-8177(86)80041-7 [pii]
PST - ppublish
SO  - Hum Pathol. 1986 May;17(5):501-13.

PMID- 17607374
OWN - NLM
STAT- MEDLINE
DCOM- 20071002
LR  - 20181113
IS  - 1219-4956 (Print)
IS  - 1219-4956 (Linking)
VI  - 13
IP  - 2
DP  - 2007
TI  - Lewis x is highly expressed in normal tissues: a comparative immunohistochemical 
      study and literature revision.
PG  - 130-8
AB  - An immunohistochemical analysis was employed to determine the expression of
      carbohydrate antigens associated to mucins in normal epithelia. Tissue samples
      were obtained as biopsies from normal breast (18), colon (35) and oral cavity
      mucosa (8). The following carbohydrate epitopes were studied: sialyl-Lewis x,
      Lewis x, Lewis y, Tn hapten, sialyl-Tn and Thomsen-Friedenreich antigen. Mucins
      were also studied employing antibodies against MUC1, MUC2, MUC4, MUC5AC, MUC6 and
      also normal colonic glycolipid. Statistical analysis was performed and Kendall
      correlations were obtained. Lewis x showed an apical pattern mainly at plasma
      membrane, although cytoplasmic staining was also found in most samples. TF, Tn
      and sTn haptens were detected in few specimens, while sLewis x was found in oral 
      mucosa and breast tissue. Also, normal breast expressed MUC1 at a high
      percentage, whereas MUC4 was observed in a small number of samples. Colon
      specimens mainly expressed MUC2 and MUC1, while most oral mucosa samples
      expressed MUC4 and MUC1. A positive correlation between MUC1VNTR and TF epitope
      (r=0.396) was found in breast samples, while in colon specimens MUC2 and colonic 
      glycolipid versus Lewis x were statistically significantly correlated (r=0.28 and
      r=0.29, respectively). As a conclusion, a defined carbohydrate epitope expression
      is not exclusive of normal tissue or a determined localization, and it is
      possible to assume that different glycoproteins and glycolipids may be carriers
      of carbohydrate antigens depending on the tissue localization considered.
FAU - Croce, Maria V
AU  - Croce MV
AD  - Centre of Basic and Applied Immunological Research (CINIBA), Faculty of Medical
      Sciences, UNLP, La Plata, Argentina.
FAU - Isla-Larrain, Marina
AU  - Isla-Larrain M
FAU - Rabassa, Martin E
AU  - Rabassa ME
FAU - Demichelis, Sandra
AU  - Demichelis S
FAU - Colussi, Andrea G
AU  - Colussi AG
FAU - Crespo, Marina
AU  - Crespo M
FAU - Lacunza, Ezequiel
AU  - Lacunza E
FAU - Segal-Eiras, Amada
AU  - Segal-Eiras A
LA  - eng
PT  - Comparative Study
PT  - Journal Article
PT  - Review
DEP - 20070703
PL  - Netherlands
TA  - Pathol Oncol Res
JT  - Pathology oncology research : POR
JID - 9706087
RN  - 0 (Antigens, Neoplasm)
RN  - 0 (Lewis X Antigen)
RN  - 0 (MUC1 protein, human)
RN  - 0 (MUC2 protein, human)
RN  - 0 (MUC4 protein, human)
RN  - 0 (Mucin-1)
RN  - 0 (Mucin-2)
RN  - 0 (Mucin-4)
RN  - 0 (Mucins)
SB  - IM
MH  - Antigens, Neoplasm/metabolism
MH  - Biopsy
MH  - Breast/*metabolism/pathology
MH  - Cell Membrane/metabolism/pathology
MH  - Colon/*metabolism/pathology
MH  - Female
MH  - Gene Expression Regulation
MH  - Humans
MH  - Intestinal Mucosa/metabolism/pathology
MH  - Lewis X Antigen/genetics/*metabolism
MH  - Mouth/*metabolism/pathology
MH  - Mouth Mucosa/metabolism/pathology
MH  - Mucin-1
MH  - Mucin-2
MH  - Mucin-4
MH  - Mucins/metabolism
MH  - Mucous Membrane/metabolism/pathology
RF  - 83
EDAT- 2007/07/04 09:00
MHDA- 2007/10/03 09:00
CRDT- 2007/07/04 09:00
PHST- 2006/10/26 00:00 [received]
PHST- 2007/05/10 00:00 [accepted]
PHST- 2007/07/04 09:00 [pubmed]
PHST- 2007/10/03 09:00 [medline]
PHST- 2007/07/04 09:00 [entrez]
AID - PAOR.2007.13.2.0130 [doi]
PST - ppublish
SO  - Pathol Oncol Res. 2007;13(2):130-8. doi: PAOR.2007.13.2.0130. Epub 2007 Jul 3.

PMID- 11326683
OWN - NLM
STAT- MEDLINE
DCOM- 20010524
LR  - 20071205
IS  - 0250-7005 (Print)
IS  - 0250-7005 (Linking)
VI  - 20
IP  - 6D
DP  - 2000 Nov-Dec
TI  - Expression of the Thomsen-Friedenreich (TF) antigen in the human placenta.
PG  - 5129-33
AB  - The Thomsen-Friedenreich (TF) antigen (or, more precisely, epitope; Gal beta
      1-3GalNAc-) has been known for a long time as a pancarcinoma antigen. Here we
      report the immunohistochemical identification of this carbohydrate antigen in the
      human placenta. Paraffin-embedded placental and decidual tissues of the first,
      second and third trimester were incubated with different monoclonal antibodies
      (A78-G/A7 and HH8) directed against the TF-epitope and stained with an
      immunohistochemistry system. We found a strong expression of the TF-epitope in
      the first trimester of pregnancy. In addition, we identified an expression of the
      TF-antigen in the second trimester of pregnancy but only in a few cases a
      positive staining in the third trimester of pregnancy.
FAU - Richter, D U
AU  - Richter DU
AD  - University of Rostock, Department of Obstetrics and Gynaecology, Doberaner Str.
      142, D-18055 Rostock, Germany.
FAU - Jeschke, U
AU  - Jeschke U
FAU - Makovitzky, J
AU  - Makovitzky J
FAU - Goletz, S
AU  - Goletz S
FAU - Karsten, U
AU  - Karsten U
FAU - Briese, V
AU  - Briese V
FAU - Friese, K
AU  - Friese K
LA  - eng
PT  - Journal Article
PL  - Greece
TA  - Anticancer Res
JT  - Anticancer research
JID - 8102988
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 3554-90-3 (Thomsen-Friedenreich antigen)
SB  - IM
MH  - Antigens, Tumor-Associated, Carbohydrate/*biosynthesis
MH  - Female
MH  - Gestational Age
MH  - Humans
MH  - Immunohistochemistry
MH  - Placenta/cytology/*metabolism
EDAT- 2001/05/01 10:00
MHDA- 2001/05/26 10:01
CRDT- 2001/05/01 10:00
PHST- 2001/05/01 10:00 [pubmed]
PHST- 2001/05/26 10:01 [medline]
PHST- 2001/05/01 10:00 [entrez]
PST - ppublish
SO  - Anticancer Res. 2000 Nov-Dec;20(6D):5129-33.

PMID- 2097812
OWN - NLM
STAT- MEDLINE
DCOM- 19910722
LR  - 20151119
IS  - 0040-8727 (Print)
IS  - 0040-8727 (Linking)
VI  - 162
IP  - 2
DP  - 1990 Oct
TI  - Selection of monoclonal antibodies detecting KM01 antigen.
PG  - 127-36
AB  - Monoclonal antibodies (MoAbs) were selected for specific binding inhibition of
      KM01 to the KM01 antigen, which was detected in the serum of colorectal and other
      gastrointestinal carcinoma patients. Out of 91 MoAbs tested, 8 were found to have
      the inhibiting activity. The reactivity of these MoAbs with glycolipid antigen,
      which was isolated from cancer cell line, corresponded well with that of cancer
      patients sera. These monoclonal antibodies are thought to be useful in
      combination with KM01 for the construction of the second generation of the KM01
      antigen-detecting system.
FAU - Kano, Y
AU  - Kano Y
AD  - Research Division, Green Cross Corporation, Hirakata.
FAU - Taniguchi, T
AU  - Taniguchi T
FAU - Uemura, Y
AU  - Uemura Y
FAU - Yokoyama, K
AU  - Yokoyama K
FAU - Ohyanagi, H
AU  - Ohyanagi H
FAU - Saitoh, Y
AU  - Saitoh Y
LA  - eng
PT  - Journal Article
PL  - Japan
TA  - Tohoku J Exp Med
JT  - The Tohoku journal of experimental medicine
JID - 0417355
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Glycolipids)
SB  - IM
MH  - *Antibodies, Monoclonal
MH  - Antigens, Tumor-Associated, Carbohydrate/*analysis
MH  - Bile Duct Neoplasms/blood
MH  - Cell Line
MH  - Enzyme-Linked Immunosorbent Assay
MH  - Gastrointestinal Neoplasms/blood
MH  - Glycolipids/analysis
MH  - Humans
MH  - Liver Neoplasms/blood
MH  - Neoplasms/*blood
MH  - Pancreatic Neoplasms/blood
MH  - Reference Values
EDAT- 1990/10/01 00:00
MHDA- 1990/10/01 00:01
CRDT- 1990/10/01 00:00
PHST- 1990/10/01 00:00 [pubmed]
PHST- 1990/10/01 00:01 [medline]
PHST- 1990/10/01 00:00 [entrez]
PST - ppublish
SO  - Tohoku J Exp Med. 1990 Oct;162(2):127-36.

PMID- 12031100
OWN - NLM
STAT- MEDLINE
DCOM- 20021220
LR  - 20061115
IS  - 1536-8599 (Print)
IS  - 1536-8599 (Linking)
VI  - 21
IP  - 2
DP  - 2002 Apr
TI  - SA-Lea and tumor metastasis: the old prediction and recent findings.
PG  - 111-6
AB  - Several in vivo studies demonstrated that tumor metastasis depend on the
      expression of carbohydrate Lewis structures. Lewis antigens and their derivatives
      such as Lewis b (Leb), Lewis X (LeX), sialyl Lewis X (SA-LeX), sialyl Lewis a
      (SA-Lea), and Lewis Y (LeY) were identified as tumor-associated structures
      approximately 20 years ago by Koprowski et al. using hybridoma technology and
      showed that upregulation and/or de novo expression of these determinants on the
      tumor cell surface is associated with a poor prognosis. LeX and SA-LeX are
      ligands for selectin adhesion molecules; E- and P-selectins are vascular
      receptors expressed on activated endothelial cells (ECs) and L-selectin is
      expressed on leukocytes. Leukocytes also express on their surface LeX and SA-LeX 
      determinants, which are involved in the initial steps of extravasation, that is, 
      rolling, which is alpha step mediated by interaction with E-selectin on ECs. We
      hypothesized that the tumor cells transmigration from the bloodstream to
      metastatic sites is similar to lymphocyte extravasation and that adhesion of
      cancer cells in analogy with the lymphocyte rolling is mediated by interaction of
      carbohydrate determinants on tumor cells with selectins on ECs. To assess the
      role of interaction of carbohydrate structures with E-selectin in metastatic
      process in vivo, we demonstrated that the peptides mimicking SA-Lea blocked
      colonization of tumor cells in experimental model of lung metastasis in vivo.
      Furthermore, the metastases formation was completely attenuated in
      E-selectin-knock out (KO) mice demonstrating the importance of selectin-mediated 
      interaction in this process. We also showed that a peptide mimicking SA-Lea
      E-selectin ligand has an ability to significantly reduce neutrophil recruitment
      into peritoneal cavity in acute inflammatory conditions. These studies support
      the hypothesis that the interaction of tumor cells via the carbohydrate SA-Lea
      determinant and E-selectin constitutes the important step in the metastatic
      process in analogy with lymphocyte extravasation and that carbohydrate antigen
      mimics have a potential as anti-inflammatories and anti-adhesive tumor
      therapeutics.
FAU - Thurin, Magdalena
AU  - Thurin M
AD  - Cancer Diagnosis Program, NCI, NIH, Rockville, Maryland 20852, USA.
      thurinm@mail.nih.gov
FAU - Kieber-Emmons, Thomas
AU  - Kieber-Emmons T
LA  - eng
PT  - Journal Article
PT  - Research Support, U.S. Gov't, Non-P.H.S.
PT  - Research Support, U.S. Gov't, P.H.S.
PT  - Review
PL  - United States
TA  - Hybrid Hybridomics
JT  - Hybridoma and hybridomics
JID - 101131136
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (E-Selectin)
RN  - 0 (Gangliosides)
RN  - 0 (Peptides)
RN  - 91847-18-6 (sialyl Le(a) ganglioside)
SB  - IM
MH  - Animals
MH  - Antigens, Tumor-Associated, Carbohydrate/*metabolism
MH  - Carcinoma, Small Cell/metabolism
MH  - Cell Adhesion
MH  - E-Selectin/genetics/metabolism
MH  - Gangliosides/*metabolism
MH  - Humans
MH  - Inflammation/metabolism
MH  - *Neoplasm Metastasis
MH  - Peptides/metabolism
MH  - Risk Factors
RF  - 49
EDAT- 2002/05/29 10:00
MHDA- 2002/12/21 04:00
CRDT- 2002/05/29 10:00
PHST- 2002/05/29 10:00 [pubmed]
PHST- 2002/12/21 04:00 [medline]
PHST- 2002/05/29 10:00 [entrez]
AID - 10.1089/153685902317401708 [doi]
PST - ppublish
SO  - Hybrid Hybridomics. 2002 Apr;21(2):111-6. doi: 10.1089/153685902317401708.

PMID- 9406719
OWN - NLM
STAT- MEDLINE
DCOM- 19980102
LR  - 20071114
IS  - 0008-543X (Print)
IS  - 0008-543X (Linking)
VI  - 80
IP  - 12 Suppl
DP  - 1997 Dec 15
TI  - Preclinical analysis of radiolabeled anti-GD2 immunoglobulin G.
PG  - 2642-9
AB  - BACKGROUND: Unlabeled murine monoclonal anti-GD2 immunoglobulin (Ig)G (14G2a)
      reactive with nervous system diganglioside and neuroblastoma, melanoma, and small
      cell lung carcinoma produces tumor regression. However, serious acute abdominal
      pain, paresthesia, hypotension and hypertension, syndrome of inappropriate
      secretion of antidiuretic hormone (SIADH), and occasional motor weakness occur.
      Studies in preclinical animal models can elucidate the mechanism of the observed 
      neurotoxicity and lead to anti-GD2 antibody treatment with a higher therapeutic
      ratio. METHODS: One mg of 14G2a or control IgG was labeled with 1-2 mCi of
      indium-111 and administered intravenously to beagles (n = 8). In 2 dogs,
      additional high dose (200 mg) unlabeled 14G2a was given over 5 days. Whole body
      gamma camera images and SPECT scans were obtained repeatedly over 7 days. On Day 
      7, sciatic nerve conduction studies were performed, and after euthanasia
      radioactivity was determined in major organs. RESULTS: Unlabeled high dose 14G2a 
      administered to mice, rats, or rabbits did not cause neurotoxicity within 3
      weeks. GD2 antigens were shown by immunochemistry to be present in brain and
      peripheral nerve tissues of rodents and beagles. After in vivo administration of 
      radiolabeled 14G2a, canine lymph nodes showed specific uptake, but only minimal
      radioactivity was found in the nervous system. Dogs that received additional high
      dose unlabeled 14G2a showed much higher lymph node uptake and follicular lymph
      node hyperplasia. Low motor response amplitudes on nerve conduction studies were 
      noted. CONCLUSIONS: A radioisotope label on IgG and its visualization in a large 
      series of animal models indicate that a low protein dose of anti-GD2 IgG will not
      cause neurologic side effects in patients. High protein dose anti-GD2 IgG may
      enhance antineoplastic effects and contribute to neurotoxicity through
      stimulation of normal lymphocytes with subsequent release of cytokines.
FAU - Vriesendorp, F J
AU  - Vriesendorp FJ
AD  - Department of Neurology, University of Texas Health Science Center, Houston
      77030, USA.
FAU - Quadri, S M
AU  - Quadri SM
FAU - Flynn, R E
AU  - Flynn RE
FAU - Malone, M R
AU  - Malone MR
FAU - Cromeens, D M
AU  - Cromeens DM
FAU - Stephens, L C
AU  - Stephens LC
FAU - Vriesendorp, H M
AU  - Vriesendorp HM
LA  - eng
GR  - 5 KO8 NS01530/NS/NINDS NIH HHS/United States
GR  - CA 16672/CA/NCI NIH HHS/United States
GR  - CA 51161/CA/NCI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Cancer
JT  - Cancer
JID - 0374236
RN  - 0 (Gangliosides)
RN  - 0 (Immunoglobulin G)
RN  - 65988-71-8 (ganglioside, GD2)
SB  - AIM
SB  - IM
MH  - Animals
MH  - Dogs
MH  - Female
MH  - Gangliosides/*immunology
MH  - Immunoglobulin G/metabolism/*therapeutic use
MH  - Immunohistochemistry
MH  - Lymph Nodes/pathology
MH  - Male
MH  - Mice
MH  - Neural Conduction
MH  - Rabbits
MH  - *Radioimmunotherapy
MH  - Rats
MH  - Rats, Inbred Lew
MH  - Tissue Distribution
EDAT- 1997/12/24 01:20
MHDA- 2000/06/20 09:00
CRDT- 1997/12/24 01:20
PHST- 1997/12/24 01:20 [pubmed]
PHST- 2000/06/20 09:00 [medline]
PHST- 1997/12/24 01:20 [entrez]
AID - 10.1002/(SICI)1097-0142(19971215)80:12+<2642::AID-CNCR40>3.0.CO;2-9 [pii]
PST - ppublish
SO  - Cancer. 1997 Dec 15;80(12 Suppl):2642-9.

PMID- 9873990
OWN - NLM
STAT- MEDLINE
DCOM- 19990225
LR  - 20171116
IS  - 0272-457X (Print)
IS  - 0272-457X (Linking)
VI  - 17
IP  - 5
DP  - 1998 Oct
TI  - Novel monoclonal antibodies to putative selectin carbohydrate ligands that
      inhibit selectin binding to myeloid cells.
PG  - 445-56
AB  - Four newly developed monoclonal antibodies (MAbs) are characterized using
      flowcytometry, enzyme-linked immunoadsorbent assay (ELISA), immunoprecipitation
      and Western blots, carbohydrate epitope mapping, glycosidase cleavage, and
      competition binding assays. Their effects on selectin binding to myeloid cells
      was tested. These MAbs react only with myeloid cells. MAbs CI-1, BU60, and HIM95 
      recognize epitopes expressed by CD11/CD18 (beta2) integrins, while HI247 and
      CSLEX1 do not. The epitopes require Lewis x [Galbeta1-4 (Fucalpha1-3)GlcNAc]
      based on reactivity with oligosaccharide-polyacrylamide-biotin or
      oligosaccharide-BSA conjugates. MAb HI247 recognizes a related structure,
      sialyl-Lewis x, NeuAcalpha2-3GaLbeta1-4(Fucalpha1-3)GlcNAc. The three MAbs
      against Lewis x show some minor differences in their reactivity such as
      recognizing their antigens on CD11/CD18 integrins after endo-beta-galactosidase
      treatment and recognizing free Lewis x. The hydroxyl group on C-3 of the terminal
      galactose is important for recognition by MAb CI-1, BU60, and HIM95 as its
      substitution with sulfo group of sialic acid abolishes the binding of these MAbs.
      The C-3 sialic acid is crucial for the binding of MAb HI247. Its replacement by
      sulphate or its cleavage by sialidase eliminates recognition by this MAb. MAbs
      HI247 and CSLEX-1 did not react in ELISA with immobilized CD11/CD18, suggesting
      that the majority of sialyl Lewis x on CD11/CD18 molecules may have sialic acid
      6-linked rather than 3-linked to galactose. Unexpectedly, MAb BU60 inhibited
      binding of P-selectin mu chain chimera to HL-60 or U937 cells, while CI-1, HIM95 
      and three other defined anti-Lewis x MAbs (6C7, M6-1 and LeuM1) did not. MAb
      HI247 inhibited binding of both E- and P-selectin chimeras to these cell lines
      more effectively than several characterized MAbs (CSLEX-1, FH6, HECA-452) to
      sialyl Lewis x and related oligosaccharides. Certain combinations of these
      anticarbohydrate MAbs had additive inhibitory effects on selectin binding,
      suggesting a potential application of these new MAbs in cell adhesion/migration
      and tumor metastasis studies.
FAU - Zhang, K
AU  - Zhang K
AD  - Department of Pediatrics, Dalhousie University, Halifax, Nova Scotia, Canada.
FAU - Chuluyan, H E
AU  - Chuluyan HE
FAU - Hardie, D
AU  - Hardie D
FAU - Shen, D C
AU  - Shen DC
FAU - Larsen, R
AU  - Larsen R
FAU - Issekutz, A
AU  - Issekutz A
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Hybridoma
JT  - Hybridoma
JID - 8202424
RN  - 0
      (5-acetylneuraminyl-(2-3)-galactosyl-(1-4)-(fucopyranosyl-(1-3))-N-acetylglucosam
      ine)
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (CD18 Antigens)
RN  - 0 (E-Selectin)
RN  - 0 (Oligosaccharides)
RN  - 0 (P-Selectin)
RN  - 0 (Selectins)
SB  - IM
MH  - Animals
MH  - Antibodies, Monoclonal/*biosynthesis
MH  - Binding, Competitive
MH  - CD18 Antigens/immunology
MH  - Cell Line
MH  - E-Selectin/immunology/metabolism
MH  - HL-60 Cells
MH  - Humans
MH  - In Vitro Techniques
MH  - Melanoma/immunology
MH  - Mice
MH  - Oligosaccharides/*immunology/metabolism
MH  - P-Selectin/immunology/metabolism
MH  - Selectins/blood/immunology/*metabolism
EDAT- 1999/01/05 00:00
MHDA- 1999/01/05 00:01
CRDT- 1999/01/05 00:00
PHST- 1999/01/05 00:00 [pubmed]
PHST- 1999/01/05 00:01 [medline]
PHST- 1999/01/05 00:00 [entrez]
AID - 10.1089/hyb.1998.17.445 [doi]
PST - ppublish
SO  - Hybridoma. 1998 Oct;17(5):445-56. doi: 10.1089/hyb.1998.17.445.

PMID- 7462199
OWN - NLM
STAT- MEDLINE
DCOM- 19810424
LR  - 20190512
IS  - 0021-924X (Print)
IS  - 0021-924X (Linking)
VI  - 88
IP  - 6
DP  - 1980 Dec
TI  - Structural studies of the sugar chains of cold-insoluble globulin isolated from
      human plasma.
PG  - 1587-94
AB  - The asparagine-linked sugar chains of cold-insoluble globulin isolated from human
      plasma were released as oligosaccharides from the polypeptide moiety by
      hydrazinolysis. These oligosaccharides were N-acetylated and could be labeled by 
      reduction with NaB[3H]4. The yield of radioactive oligosaccharides indicated that
      the glycoprotein has four asparagine-linked sugar chains in one molecule. More
      than 90% of the radioactive oligosaccharides contain N-acetylneuraminic acid, and
      could be separated into two acidic oligosaccharides, A-1 and A-2. By sequential
      exoglycosidase digestion in combination with methylation studies, their
      structures were elucidated as Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man
      alpha 1 leads to 6(NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1
      leads to 2Man alpha 1 leads to 3) Man beta 1 leads to 4GlcNAc beta 1 leads to
      4GlcNAc and NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to
      2Man alpha 1 leads to 6 (NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta
      1 leads to 2 Man alpha 1 leads to 3)-Man beta 1 leads to 4GlcNAc beta 1 leads to 
      4GlcNAc.
FAU - Takasaki, S
AU  - Takasaki S
FAU - Yamashita, K
AU  - Yamashita K
FAU - Suzuki, K
AU  - Suzuki K
FAU - Kobata, A
AU  - Kobata A
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - J Biochem
JT  - Journal of biochemistry
JID - 0376600
RN  - 0 (Fibronectins)
RN  - 0 (Hydrazines)
RN  - 0 (Oligosaccharides)
RN  - 0 (Sialic Acids)
SB  - IM
MH  - Carbohydrate Sequence
MH  - Chemical Phenomena
MH  - Chemistry
MH  - Electrophoresis, Paper
MH  - Fibronectins/*blood
MH  - Humans
MH  - Hydrazines
MH  - Hydrogen-Ion Concentration
MH  - Methylation
MH  - Oligosaccharides/analysis
MH  - Sialic Acids/analysis
EDAT- 1980/12/01 00:00
MHDA- 1980/12/01 00:01
CRDT- 1980/12/01 00:00
PHST- 1980/12/01 00:00 [pubmed]
PHST- 1980/12/01 00:01 [medline]
PHST- 1980/12/01 00:00 [entrez]
AID - 10.1093/oxfordjournals.jbchem.a133133 [doi]
PST - ppublish
SO  - J Biochem. 1980 Dec;88(6):1587-94. doi: 10.1093/oxfordjournals.jbchem.a133133.

PMID- 10447878
OWN - NLM
STAT- MEDLINE
DCOM- 19991214
LR  - 20131121
IS  - 0950-382X (Print)
IS  - 0950-382X (Linking)
VI  - 33
IP  - 4
DP  - 1999 Aug
TI  - Sialic acid in the lipopolysaccharide of Haemophilus influenzae: strain
      distribution, influence on serum resistance and structural characterization.
PG  - 679-92
AB  - A survey of Haemophilus influenzae strains indicated that around one-third of
      capsular strains and over two-thirds of non-typeable strains included sialic acid
      in their lipopolysaccharides (LPS). Mutation of the CMP-Neu5Ac synthetase gene
      (siaB) resulted in a sialylation-deficient phenotype. Isogenic pairs, wild type
      and siaB mutant of two non-typeable strains were used to demonstrate that sialic 
      acid influences resistance to the killing effect of normal human serum but has
      little effect on attachment to, or invasion of, cultured human epithelial cells
      or neutrophils. We determine for the first time the site of attachment of sialic 
      acid in the LPS of a non-typeable strain and report that a small proportion of
      glycoforms include two sialic acid residues in a disaccharide unit.
FAU - Hood, D W
AU  - Hood DW
AD  - Molecular Infectious Diseases Group, University of Oxford Department of
      Paediatrics, Institute of Molecular Medicine, John Radcliffe Hospital,
      Headington, Oxford OX3 9DS, UK. dhood@molbiol.ox.ac.uk
FAU - Makepeace, K
AU  - Makepeace K
FAU - Deadman, M E
AU  - Deadman ME
FAU - Rest, R F
AU  - Rest RF
FAU - Thibault, P
AU  - Thibault P
FAU - Martin, A
AU  - Martin A
FAU - Richards, J C
AU  - Richards JC
FAU - Moxon, E R
AU  - Moxon ER
LA  - eng
GR  - AI20897/AI/NIAID NIH HHS/United States
GR  - AI33505/AI/NIAID NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - England
TA  - Mol Microbiol
JT  - Molecular microbiology
JID - 8712028
RN  - 0 (Bacterial Proteins)
RN  - 0 (Disaccharides)
RN  - 0 (Lipopolysaccharides)
RN  - 0 (Oligosaccharides)
RN  - EC 2.7.7.43 (N-Acylneuraminate Cytidylyltransferase)
RN  - EC 2.7.7.43 (SiaB protein, Neisseria meningitidis)
RN  - GZP2782OP0 (N-Acetylneuraminic Acid)
SB  - IM
MH  - Bacterial Adhesion/genetics
MH  - Bacterial Proteins/genetics
MH  - Carbohydrate Sequence
MH  - Cell Line
MH  - Disaccharides/chemistry
MH  - Drug Resistance/genetics
MH  - Haemophilus influenzae/enzymology/*genetics
MH  - Lipopolysaccharides/*chemistry
MH  - Molecular Sequence Data
MH  - Mutation
MH  - N-Acetylneuraminic Acid/analysis
MH  - *N-Acylneuraminate Cytidylyltransferase
MH  - Neutrophils
MH  - Oligosaccharides/chemistry
EDAT- 1999/08/14 00:00
MHDA- 1999/08/14 00:01
CRDT- 1999/08/14 00:00
PHST- 1999/08/14 00:00 [pubmed]
PHST- 1999/08/14 00:01 [medline]
PHST- 1999/08/14 00:00 [entrez]
AID - mmi1509 [pii]
PST - ppublish
SO  - Mol Microbiol. 1999 Aug;33(4):679-92.

PMID- 6760897
OWN - NLM
STAT- MEDLINE
DCOM- 19830415
LR  - 20161126
IS  - 0006-3002 (Print)
IS  - 0006-3002 (Linking)
VI  - 694
IP  - 4
DP  - 1982 Dec
TI  - Complex carbohydrates of the extracellular matrix structures, interactions and
      biological roles.
PG  - 375-418
FAU - Aplin, J D
AU  - Aplin JD
FAU - Hughes, R C
AU  - Hughes RC
LA  - eng
PT  - Journal Article
PT  - Review
PL  - Netherlands
TA  - Biochim Biophys Acta
JT  - Biochimica et biophysica acta
JID - 0217513
RN  - 0 (Blood Proteins)
RN  - 0 (Fibronectins)
RN  - 0 (Glycoproteins)
RN  - 0 (Laminin)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Membrane Proteins)
RN  - 0 (Neoplasm Proteins)
RN  - 0 (Proteins)
RN  - 0 (Proteoglycans)
RN  - 0 (chondronectin protein, human)
RN  - 0 (nidogen)
RN  - 9007-34-5 (Collagen)
RN  - 9007-58-3 (Elastin)
SB  - IM
MH  - Animals
MH  - Basement Membrane/metabolism
MH  - Blood Proteins/metabolism
MH  - *Carbohydrate Metabolism
MH  - Cell Adhesion
MH  - Cell Membrane/*physiology
MH  - Collagen/metabolism
MH  - Elastin/metabolism
MH  - Fibronectins/metabolism
MH  - Glycoproteins/*metabolism
MH  - Humans
MH  - Laminin
MH  - *Membrane Glycoproteins
MH  - Membrane Proteins/*metabolism
MH  - Neoplasm Proteins/metabolism
MH  - Proteins/metabolism
MH  - Proteoglycans/metabolism
RF  - 536
EDAT- 1982/12/01 00:00
MHDA- 1982/12/01 00:01
CRDT- 1982/12/01 00:00
PHST- 1982/12/01 00:00 [pubmed]
PHST- 1982/12/01 00:01 [medline]
PHST- 1982/12/01 00:00 [entrez]
PST - ppublish
SO  - Biochim Biophys Acta. 1982 Dec;694(4):375-418.

PMID- 15221966
OWN - NLM
STAT- MEDLINE
DCOM- 20040827
LR  - 20160303
IS  - 0020-7136 (Print)
IS  - 0020-7136 (Linking)
VI  - 111
IP  - 3
DP  - 2004 Sep 1
TI  - Thomsen-Friedenreich (T) antigen expression increases sensitivity of natural
      killer cell lysis of cancer cells.
PG  - 388-97
AB  - In this study, we demonstrate a correlation between T antigen expression on a
      panel of human carcinoma cell lines and their sensitivity to porcine NK cell
      lysis. Specifically, the more T antigen is expressed, the more sensitive the
      cancer cells are to porcine NK cell lysis. Furthermore, this correlation also
      exists for these cells and their ability to induce tumors in vivo. In this
      porcine animal model, the less T antigen is expressed, the more prolific the
      tumor growth in vivo and vice versa. Using the human colorectal adenocarcinoma
      cell line SW-48, we used limiting dilution to clone 2 populations of cells, one
      expressing high and the other low levels of T antigen, clones 143 and 111,
      respectively. In these cloned cells, the clone that expressed more T antigen was 
      more NK-sensitive in vitro and weakly induced tumor growth in vivo. Inversely,
      the clone that expressed less T antigen clone was more NK-resistant in vitro and 
      grew more prolific tumors in vivo. Using soluble T antigen in a competitive
      inhibition assay, there was a decrease in porcine NK cell killing of the T
      antigen+ human cell line Colo 320HSR. Taken together, these findings suggest a
      novel role for T antigen in the NK cell recognition of cancer cells, specifically
      as markers for NK sensitivity in carcinoma cell lines. The significance of T
      antigens as targets for NK cell-mediated lysis is novel and identifies NK cell-T 
      antigen interactions as potentially significant in the immunotherapy of cancer
      and its associated metastases.
CI  - Copyright 2004 Wiley-Liss, Inc.
FAU - Sotiriadis, John
AU  - Sotiriadis J
AD  - Department of Microbiology and Immunology, Finch University of Health
      Sciences/Chicago Medical School, North Chicago, IL 60064, USA.
FAU - Shin, Soon-Cheon
AU  - Shin SC
FAU - Yim, Daesong
AU  - Yim D
FAU - Sieber, David
AU  - Sieber D
FAU - Kim, Yoon Berm
AU  - Kim YB
LA  - eng
PT  - Journal Article
PL  - United States
TA  - Int J Cancer
JT  - International journal of cancer
JID - 0042124
RN  - 0 (Antigens, Neoplasm)
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 3554-90-3 (Thomsen-Friedenreich antigen)
SB  - IM
MH  - Adenocarcinoma
MH  - Animals
MH  - Antigens, Neoplasm/*genetics/immunology
MH  - Antigens, Tumor-Associated, Carbohydrate/*genetics/immunology
MH  - Cell Division
MH  - Cell Line, Tumor
MH  - Clone Cells
MH  - Colorectal Neoplasms
MH  - Humans
MH  - Killer Cells, Natural/*immunology
MH  - Swine
EDAT- 2004/06/29 05:00
MHDA- 2004/08/28 05:00
CRDT- 2004/06/29 05:00
PHST- 2004/06/29 05:00 [pubmed]
PHST- 2004/08/28 05:00 [medline]
PHST- 2004/06/29 05:00 [entrez]
AID - 10.1002/ijc.20274 [doi]
PST - ppublish
SO  - Int J Cancer. 2004 Sep 1;111(3):388-97. doi: 10.1002/ijc.20274.

PMID- 6693758
OWN - NLM
STAT- MEDLINE
DCOM- 19840322
LR  - 20170214
IS  - 0022-1554 (Print)
IS  - 0022-1554 (Linking)
VI  - 32
IP  - 3
DP  - 1984 Mar
TI  - Immunohistochemical and biochemical demonstration of the change in glycolipid
      composition of the intestinal epithelial cell surface in mice in relation to
      epithelial cell differentiation and bacterial association.
PG  - 299-304
AB  - We have previously demonstrated the appearance of fucosyl asialo-GM1 (FGA1) in
      the small-intestinal epithelial cells of germ-free mice via the induction of
      GDP-fucose: asialo-GM1 (GA1) alpha(1 leads to 2) fucosyltransferase (FT) after
      the conventionalization of these animals (Umesaki Y, Sakata T, Yajima T: Biochem 
      Biophys Res Commun 105:439, 1982). The present study, based on this earlier work,
      demonstrates the changes in the glycolipid antigens of the small-intestinal
      epithelial-cell membrane as shown immunohistochemically with specific antibodies 
      raised against asialo GM1 (GA1) and FGA1. In germ-free mice, GA1 was localized
      both in the villus cells and in the crypt cells. In the process of
      conventionalization, FGA1 appeared in the villus cells while the GA1 content of
      these cells was decreased. Four to 5 days after the conventionalization
      procedure, the fluorescence produced by anti-FGA1 was strongest in the villus
      cells, while that produced by anti-GA1 was detected only in the crypt cells. At
      this same time the FT activity of the small-intestinal mucosa was highest, with
      most of the GA1 apparently being converted into FGA1, as shown in the paper cited
      above. Thereafter, the GA1 content of both the villus and crypt cells again
      increased greatly. On the other hand, the fluorescence produced with anti-FGA1
      decreased, and could no longer be detected 14 days after conventionalization. The
      activity of FT, measured biochemically in epithelial cells differentially
      isolated from the villus tip to the crypt, was greater in the villus than in the 
      crypt region. This confirmed the intense staining with anti-FGA1 that was seen in
      villus cells. The fluorescence produced by the two anti-glycolipid antibodies
      used in the study distributed not only in the microvillus membrane but also to
      some extent in the basolateral membrane. The localization of the respective
      glycolipids contrasted with that of the glycoprotein sucrase--isomaltase enzyme
      complex, the fluorescence of which was exclusively confined to the
      microvillus-membrane side of the villus cells.
FAU - Umesaki, Y
AU  - Umesaki Y
LA  - eng
PT  - Journal Article
PL  - United States
TA  - J Histochem Cytochem
JT  - The journal of histochemistry and cytochemistry : official journal of the
      Histochemistry Society
JID - 9815334
RN  - 0 (Antibodies)
RN  - 0 (G(A1) ganglioside)
RN  - 0 (Gangliosides)
RN  - 0 (Glycolipids)
RN  - 0 (Glycosphingolipids)
RN  - 0 (Membrane Lipids)
RN  - EC 2.4.1.- (Fucosyltransferases)
RN  - EC 3.2.1.- (Sucrase-Isomaltase Complex)
SB  - IM
MH  - Animals
MH  - Antibodies/immunology
MH  - *Cell Differentiation
MH  - Enzyme-Linked Immunosorbent Assay
MH  - Epithelium/metabolism
MH  - Female
MH  - Fucosyltransferases/metabolism
MH  - Gangliosides
MH  - Glycolipids/analysis/*metabolism
MH  - Glycosphingolipids/analysis/immunology
MH  - Histocytochemistry
MH  - Immunochemistry
MH  - Intestine, Small/*metabolism/microbiology
MH  - Membrane Lipids/*metabolism
MH  - Mice
MH  - Subcellular Fractions/analysis
MH  - Sucrase-Isomaltase Complex/metabolism
EDAT- 1984/03/01 00:00
MHDA- 1984/03/01 00:01
CRDT- 1984/03/01 00:00
PHST- 1984/03/01 00:00 [pubmed]
PHST- 1984/03/01 00:01 [medline]
PHST- 1984/03/01 00:00 [entrez]
AID - 10.1177/32.3.6693758 [doi]
PST - ppublish
SO  - J Histochem Cytochem. 1984 Mar;32(3):299-304. doi: 10.1177/32.3.6693758.

PMID- 8038519
OWN - NLM
STAT- MEDLINE
DCOM- 19940819
LR  - 20181113
IS  - 0941-1291 (Print)
IS  - 0941-1291 (Linking)
VI  - 24
IP  - 4
DP  - 1994
TI  - The recognition of cancer-associated fucosylated antigens in colorectal cancer by
      a novel monoclonal antibody, YB-2.
PG  - 382-4
AB  - A monoclonal antibody, YB-2, which has a novel epitope for fucosylated antigens
      and shows cross-reactivity with Y/Leb/H type 2 antigens, was used in an
      immunohistochemical study of human neoplastic and normal colorectal tissues. Of
      64 colorectal cancers, 59 (92.2%) were stained by the YB-2 antibody; however,
      only 3 (12.0%) of 25 samples of normal colon mucosa and 13 (50.0%) of 26 adenomas
      expressed the antigens recognized by YB-2. Clinicopathologically, the
      YB-2-negative colon cancers were exclusively in Dukes stage A. These results
      indicate that the monoclonal antibody, YB-2, could detect cancer-associated
      antigens, and the degree of YB-2-reacted antigen expression might be correlated
      with the progression of colorectal carcinogenesis.
FAU - Naitoh, H
AU  - Naitoh H
AD  - First Department of Surgery, Gunma University School of Medicine, Japan.
FAU - Yazawa, S
AU  - Yazawa S
FAU - Asao, T
AU  - Asao T
FAU - Nakajima, T
AU  - Nakajima T
FAU - Nakamura, J
AU  - Nakamura J
FAU - Takenoshita, S
AU  - Takenoshita S
FAU - Nagamachi, Y
AU  - Nagamachi Y
LA  - eng
PT  - Journal Article
PL  - Japan
TA  - Surg Today
JT  - Surgery today
JID - 9204360
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens, Neoplasm)
SB  - IM
MH  - Adenoma/immunology/pathology
MH  - Antibodies, Monoclonal/*immunology
MH  - Antigens, Neoplasm/*analysis
MH  - Carcinoma/immunology/pathology
MH  - Colorectal Neoplasms/*immunology/pathology
MH  - Humans
MH  - Neoplasm Staging
EDAT- 1994/01/01 00:00
MHDA- 1994/01/01 00:01
CRDT- 1994/01/01 00:00
PHST- 1994/01/01 00:00 [pubmed]
PHST- 1994/01/01 00:01 [medline]
PHST- 1994/01/01 00:00 [entrez]
PST - ppublish
SO  - Surg Today. 1994;24(4):382-4.

PMID- 16384952
OWN - NLM
STAT- MEDLINE
DCOM- 20060209
LR  - 20181113
IS  - 0146-0404 (Print)
IS  - 0146-0404 (Linking)
VI  - 47
IP  - 1
DP  - 2006 Jan
TI  - Mucin characteristics of human corneal-limbal epithelial cells that exclude the
      rose bengal anionic dye.
PG  - 113-9
AB  - PURPOSE: Rose bengal is an organic anionic dye used to assess damage of the
      ocular surface epithelium in ocular surface disease. It has been proposed that
      mucins have a protective role, preventing rose bengal staining of normal ocular
      surface epithelial cells. The current study was undertaken to evaluate rose
      bengal staining in a human corneal-limbal epithelial (HCLE) cell line known to
      produce and glycosylate membrane-associated mucins. METHODS: HCLE cells were
      grown to confluence in serum-free medium and switched to DMEM/F12 with 10% serum 
      to promote differentiation. Immunolocalization of the membrane-associated mucins 
      MUC1 and MUC16 and the T-antigen carbohydrate epitope was performed with the
      monoclonal antibodies HMFG-2 and OC125 and jacalin lectin, respectively. To
      assess dye uptake, cultures were incubated for 5 minutes with 0.1% rose bengal
      and photographed. To determine whether exclusion of negatively charged rose
      bengal requires a negative charge at the cell surface, cells were incubated with 
      fluoresceinated cationized ferritin. The effect of hyperosmotic stress on rose
      bengal staining in vitro was evaluated by increasing the ion concentration (Ca+2 
      and Mg+2) in the rose bengal uptake assay. RESULTS: The cytoplasm and nucleus of 
      confluent HCLE cells cultured in media without serum, lacking the expression of
      MUC16 but not MUC1, as well as human corneal fibroblasts, which do not express
      mucins, stained with rose bengal. Culture of HCLE cells in medium containing
      serum resulted in the formation of islands of stratified cells that excluded rose
      bengal. Apical cells of the stratified islands produced MUC16 and the T-antigen
      carbohydrate epitope on their apical surfaces. Colocalization experiments
      demonstrated that fluoresceinated cationized ferritin did not bind to these
      stratified cells, indicating that rose bengal is excluded from cells that lack
      negative charges. Increasing the amounts of divalent cations in the media reduced
      the cellular area protected against rose bengal uptake. CONCLUSIONS: These
      results indicate that stratification and differentiation of corneal epithelial
      cells, as measured by the capacity to produce the membrane-associated mucin MUC16
      and the mucin-associated T-antigen carbohydrate on their apical surfaces provide 
      protection against rose bengal penetrance in vitro and suggest a role for
      membrane-associated mucins and their oligosaccharides in the protection of ocular
      surface epithelia.
FAU - Argueso, Pablo
AU  - Argueso P
AD  - Schepens Eye Research Institute and Department of Ophthalmology, Harvard Medical 
      School, Boston, Massachusetts 02114, USA. argueso@vision.eri.harvard.edu
FAU - Tisdale, Ann
AU  - Tisdale A
FAU - Spurr-Michaud, Sandra
AU  - Spurr-Michaud S
FAU - Sumiyoshi, Mika
AU  - Sumiyoshi M
FAU - Gipson, Ilene K
AU  - Gipson IK
LA  - eng
GR  - R01 EY003306/EY/NEI NIH HHS/United States
GR  - R01 EY014847/EY/NEI NIH HHS/United States
GR  - R01EY014847/EY/NEI NIH HHS/United States
GR  - R01EY03306/EY/NEI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, N.I.H., Extramural
PL  - United States
TA  - Invest Ophthalmol Vis Sci
JT  - Investigative ophthalmology & visual science
JID - 7703701
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (CA-125 Antigen)
RN  - 0 (Fluorescent Dyes)
RN  - 0 (MUC16 protein, human)
RN  - 0 (MUC4 protein, human)
RN  - 0 (Membrane Proteins)
RN  - 0 (Mucin-1)
RN  - 0 (Mucin-4)
RN  - 0 (Mucins)
RN  - 0 (polycationic ferritin)
RN  - 02F3473H9O (Magnesium Chloride)
RN  - 1ZPG1ELY14 (Rose Bengal)
RN  - 9007-73-2 (Ferritins)
RN  - M4I0D6VV5M (Calcium Chloride)
SB  - IM
MH  - Antibodies, Monoclonal
MH  - CA-125 Antigen/*metabolism
MH  - Calcium Chloride/pharmacology
MH  - Cell Differentiation
MH  - Cell Nucleus/metabolism
MH  - Cells, Cultured
MH  - Cytoplasm/metabolism
MH  - Epithelial Cells/drug effects/*metabolism
MH  - Epithelium, Corneal/cytology
MH  - Ferritins/metabolism
MH  - Fluorescent Dyes/*metabolism
MH  - Humans
MH  - Limbus Corneae/*cytology
MH  - Magnesium Chloride/pharmacology
MH  - Membrane Proteins
MH  - Microscopy, Fluorescence
MH  - Mucin-1/*metabolism
MH  - Mucin-4
MH  - Mucins/*metabolism
MH  - Oxidative Stress
MH  - Rose Bengal/*metabolism
MH  - Staining and Labeling
PMC - PMC1351157
MID - NIHMS7216
EDAT- 2005/12/31 09:00
MHDA- 2006/02/10 09:00
CRDT- 2005/12/31 09:00
PHST- 2005/12/31 09:00 [pubmed]
PHST- 2006/02/10 09:00 [medline]
PHST- 2005/12/31 09:00 [entrez]
AID - 47/1/113 [pii]
AID - 10.1167/iovs.05-0735 [doi]
PST - ppublish
SO  - Invest Ophthalmol Vis Sci. 2006 Jan;47(1):113-9. doi: 10.1167/iovs.05-0735.

PMID- 1701275
OWN - NLM
STAT- MEDLINE
DCOM- 19910111
LR  - 20171116
IS  - 0036-8075 (Print)
IS  - 0036-8075 (Linking)
VI  - 250
IP  - 4984
DP  - 1990 Nov 23
TI  - Recognition by ELAM-1 of the sialyl-Lex determinant on myeloid and tumor cells.
PG  - 1132-5
AB  - Endothelial leukocyte adhesion molecule-1 (ELAM-1) is an endothelial cell
      adhesion molecule that allows myeloid cells to attach to the walls of blood
      vessels adjacent to sites of inflammation. ELAM-1 recognizes the sialyl-Lewis X
      (sialyl-Lex) determinant, NeuAc alpha 2-3Gal beta 1-4(Fuc alpha 1-3)GlcNAc-, a
      granulocyte carbohydrate also found on the surface of some tumor cell lines.
      Binding of myeloid cells to soluble ELAM-1 is inhibited by a monoclonal antibody 
      recognizing sialyl-Lex or by proteins bearing sialyl-Lex, some of which may
      participate in humoral regulation of myeloid cell adhesion. Stimulated
      granulocytes also release an inhibitor of ELAM-1 binding that can be selectively 
      adsorbed by monoclonal antibody to sialyl-Lex.
FAU - Walz, G
AU  - Walz G
AD  - Department of Genetics, Harvard Medical School, Boston, MA 02114.
FAU - Aruffo, A
AU  - Aruffo A
FAU - Kolanus, W
AU  - Kolanus W
FAU - Bevilacqua, M
AU  - Bevilacqua M
FAU - Seed, B
AU  - Seed B
LA  - eng
GR  - AI27849/AI/NIAID NIH HHS/United States
GR  - DK43031/DK/NIDDK NIH HHS/United States
GR  - HL36028/HL/NHLBI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Science
JT  - Science (New York, N.Y.)
JID - 0404511
RN  - 0
      (5-acetylneuraminyl-(2-3)-galactosyl-(1-4)-(fucopyranosyl-(1-3))-N-acetylglucosam
      ine)
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Cell Adhesion Molecules)
RN  - 0 (E-Selectin)
RN  - 0 (Interleukin-1)
RN  - 0 (Interleukin-8)
RN  - 0 (Lewis X Antigen)
RN  - 0 (Oligosaccharides)
RN  - 0 (Orosomucoid)
RN  - 28RYY2IV3F (Fucose)
RN  - EC 2.4.1.- (Fucosyltransferases)
RN  - EC 3.2.1.18 (Neuraminidase)
SB  - IM
MH  - Amniotic Fluid/chemistry
MH  - Antibodies, Monoclonal/pharmacology
MH  - Carbohydrate Sequence
MH  - Cell Adhesion/physiology
MH  - Cell Adhesion Molecules/immunology/*metabolism
MH  - Cell Membrane/metabolism
MH  - E-Selectin
MH  - Endothelium, Vascular/metabolism
MH  - Fucose/metabolism
MH  - Fucosyltransferases/metabolism
MH  - Granulocytes/*metabolism
MH  - Immunosorbent Techniques
MH  - Interleukin-1/pharmacology
MH  - Interleukin-8/pharmacology
MH  - Lewis X Antigen/chemistry/*metabolism
MH  - Molecular Sequence Data
MH  - Neoplasms/*metabolism
MH  - Neuraminidase/metabolism
MH  - Oligosaccharides/chemistry
MH  - Orosomucoid/metabolism
MH  - Tumor Cells, Cultured
EDAT- 1990/11/23 00:00
MHDA- 1990/11/23 00:01
CRDT- 1990/11/23 00:00
PHST- 1990/11/23 00:00 [pubmed]
PHST- 1990/11/23 00:01 [medline]
PHST- 1990/11/23 00:00 [entrez]
PST - ppublish
SO  - Science. 1990 Nov 23;250(4984):1132-5.

PMID- 1701274
OWN - NLM
STAT- MEDLINE
DCOM- 19910111
LR  - 20171116
IS  - 0036-8075 (Print)
IS  - 0036-8075 (Linking)
VI  - 250
IP  - 4984
DP  - 1990 Nov 23
TI  - ELAM-1 mediates cell adhesion by recognition of a carbohydrate ligand,
      sialyl-Lex.
PG  - 1130-2
AB  - Recruitment of neutrophils to sites of inflammation is mediated in part by
      endothelial leukocyte adhesion molecule-1 (ELAM-1), which is expressed on
      activated endothelial cells of the blood vessel walls. ELAM-1 is a member of the 
      LEC-CAM or selectin family of adhesion molecules that contain a lectin motif
      thought to recognize carbohydrate ligands. In this report, cell adhesion by
      ELAM-1 is shown to be mediated by a carbohydrate ligand, sialyl-Lewis X (SLex;
      NeuAc alpha 2,3Gal beta 1,4(Fuc alpha 1,3)-GlcNAc-), a terminal structure found
      on cell-surface glycoprotein and glycolipid carbohydrate groups of neutrophils.
FAU - Phillips, M L
AU  - Phillips ML
AD  - Cytel Corp., La Jolla, CA 92037.
FAU - Nudelman, E
AU  - Nudelman E
FAU - Gaeta, F C
AU  - Gaeta FC
FAU - Perez, M
AU  - Perez M
FAU - Singhal, A K
AU  - Singhal AK
FAU - Hakomori, S
AU  - Hakomori S
FAU - Paulson, J C
AU  - Paulson JC
LA  - eng
PT  - Journal Article
PL  - United States
TA  - Science
JT  - Science (New York, N.Y.)
JID - 0404511
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Cell Adhesion Molecules)
RN  - 0 (E-Selectin)
RN  - 0 (Lewis X Antigen)
RN  - 0 (Ligands)
RN  - EC 3.2.1.18 (Neuraminidase)
SB  - IM
MH  - Animals
MH  - Antibodies, Monoclonal/pharmacology
MH  - Carbohydrate Conformation
MH  - Carbohydrate Sequence
MH  - Cell Adhesion/*physiology
MH  - Cell Adhesion Molecules/immunology/*physiology
MH  - Cell Line
MH  - Cricetinae
MH  - E-Selectin
MH  - Glycosylation
MH  - Humans
MH  - Lewis X Antigen/chemistry/*physiology
MH  - Ligands
MH  - Molecular Sequence Data
MH  - Neuraminidase/pharmacology
MH  - Neutrophils/*physiology
EDAT- 1990/11/23 00:00
MHDA- 1990/11/23 00:01
CRDT- 1990/11/23 00:00
PHST- 1990/11/23 00:00 [pubmed]
PHST- 1990/11/23 00:01 [medline]
PHST- 1990/11/23 00:00 [entrez]
PST - ppublish
SO  - Science. 1990 Nov 23;250(4984):1130-2.

PMID- 1370643
OWN - NLM
STAT- MEDLINE
DCOM- 19920227
LR  - 20171116
IS  - 0006-4971 (Print)
IS  - 0006-4971 (Linking)
VI  - 79
IP  - 3
DP  - 1992 Feb 1
TI  - Reactivity profiles of leukemic myeloblasts with monoclonal antibodies directed
      to sialosyl-Le(x) and other lacto-series type 2 chain antigens:absence of
      reactivity with normal hematopoietic progenitor cells.
PG  - 713-9
AB  - We investigated the expression profiles of lacto-series type 2 antigens in
      hematopoietic cells and their progenitors, in comparison with leukemic
      leukocytes. Reactivity profiles of various anti-type 2 chain monoclonal
      antibodies (MoAbs) with leukemic blasts from 12 patients with acute myeloblastic 
      leukemia (AML) and those from two patients with acute unclassified leukemia (AUL)
      show that anti-sialosyl-Le(x) MoAb SNH3 reacted strongly with greater than 95% of
      leukemic blast leukocyte populations from all patients (14 of 14). Another
      anti-sialosyl-Le(x) MoAb, FH6, showed less reactivity than SNH3 (12 of 14
      patients), while anti-Le(y) MoAb AH6 showed reactivity with only 8 of 14
      patients. On the other hand, none of the anti-type 2 chain MoAbs reacted with
      CD34+ normal adult bone marrow (BM) mononuclear cells obtained independently from
      three healthy volunteers. MoAb SNH3, but not FH6 or AH6, showed
      complement-mediated cytotoxicity to leukemic blasts from these patients, as well 
      as to myelogenous leukemia cell line HL60. Colony-forming unit
      granulocyte-macrophage (CFU-GM), but not burst-forming unit-erythroid (BFU-E),
      was incompletely inhibited by treatment of normal BM mononuclear cells with SNH3 
      and complement. The absence of type 2 chain antigen expression in hematopoietic
      progenitor cells and in in vitro hematopoietic colonies (CFU-GM and BFU-E)
      strongly suggests that application of anti-carbohydrate MoAbs, particularly
      anti-sialosyl-Le(x) could be useful for elimination of leukemic myeloblasts
      infiltrating in BM, for purging of leukemic blasts in BM, and for facilitation of
      autologous BM transplantation.
FAU - Muroi, K
AU  - Muroi K
AD  - Department of Medicine, Jichi Medical School, Tochigi-ken, Japan.
FAU - Suda, T
AU  - Suda T
FAU - Nojiri, H
AU  - Nojiri H
FAU - Ema, H
AU  - Ema H
FAU - Amemiya, Y
AU  - Amemiya Y
FAU - Miura, Y
AU  - Miura Y
FAU - Nakauchi, H
AU  - Nakauchi H
FAU - Singhal, A
AU  - Singhal A
FAU - Hakomori, S
AU  - Hakomori S
LA  - eng
GR  - CA42505/CA/NCI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Blood
JT  - Blood
JID - 7603509
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antibodies, Neoplasm)
RN  - 0 (Antigens, CD)
RN  - 0 (Antigens, CD34)
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Lewis Blood-Group System)
RN  - 0 (Lewis X Antigen)
RN  - 0 (Sialic Acids)
SB  - AIM
SB  - IM
MH  - Antibodies, Monoclonal/*immunology
MH  - Antibodies, Neoplasm/immunology
MH  - Antibody-Dependent Cell Cytotoxicity
MH  - Antigens, CD/analysis/immunology
MH  - Antigens, CD34
MH  - Antigens, Tumor-Associated, Carbohydrate/chemistry/*immunology
MH  - Carbohydrate Sequence
MH  - Cytotoxicity, Immunologic
MH  - Flow Cytometry
MH  - Hematopoietic Stem Cells/*immunology
MH  - Humans
MH  - In Vitro Techniques
MH  - Leukemia/*immunology
MH  - Lewis Blood-Group System/chemistry/immunology
MH  - Lewis X Antigen/chemistry/immunology
MH  - Molecular Sequence Data
MH  - Sialic Acids/immunology
MH  - Tumor Cells, Cultured
EDAT- 1992/02/01 00:00
MHDA- 1992/02/01 00:01
CRDT- 1992/02/01 00:00
PHST- 1992/02/01 00:00 [pubmed]
PHST- 1992/02/01 00:01 [medline]
PHST- 1992/02/01 00:00 [entrez]
PST - ppublish
SO  - Blood. 1992 Feb 1;79(3):713-9.

PMID- 10894166
OWN - NLM
STAT- MEDLINE
DCOM- 20000731
LR  - 20071114
IS  - 1074-7613 (Print)
IS  - 1074-7613 (Linking)
VI  - 12
IP  - 6
DP  - 2000 Jun
TI  - Specialized contributions by alpha(1,3)-fucosyltransferase-IV and FucT-VII during
      leukocyte rolling in dermal microvessels.
PG  - 665-76
AB  - Noninflamed skin venules support constitutive leukocyte rolling. P-selectin
      controls the rolling frequency, whereas E-selectin dictates rolling velocity
      (Vroll). Fucosylated selectin ligands are essential for all interactions, as
      rolling was absent in mice doubly deficient in alpha1,3-fucosyltransferase
      (FucT)-IV and FucT-VII. The rolling fraction was reduced in FucT-VII-/- animals
      but normal in FucT-IV-/- mice. However, Vroll was markedly increased in both
      strains. P-selectin ligands generated by FucT-VII are crucial for initial
      leukocyte tethering, whereas E-selectin ligands that permit maximum slowing of
      Vroll require simultaneous expression of FucT-IV and FucT-VII. These results
      demonstrate a role for FucT-IV in selectin-dependent adhesion and suggest that
      the endothelial selectins and FucTs have distinct but overlapping functions in
      the immunosurveillance of the skin.
FAU - Weninger, W
AU  - Weninger W
AD  - The Center for Blood Research and Department of Pathology, Children's Hospital,
      Harvard Medical School, Boston, Massachusetts 02115, USA.
FAU - Ulfman, L H
AU  - Ulfman LH
FAU - Cheng, G
AU  - Cheng G
FAU - Souchkova, N
AU  - Souchkova N
FAU - Quackenbush, E J
AU  - Quackenbush EJ
FAU - Lowe, J B
AU  - Lowe JB
FAU - von Andrian, U H
AU  - von Andrian UH
LA  - eng
GR  - HL48675/HL/NHLBI NIH HHS/United States
GR  - HL54936/HL/NHLBI NIH HHS/United States
GR  - HL56949/HL/NHLBI NIH HHS/United States
GR  - etc.
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Immunity
JT  - Immunity
JID - 9432918
RN  - 0 (E-Selectin)
RN  - 0 (Ligands)
RN  - 0 (P-Selectin)
RN  - 126880-86-2 (L-Selectin)
RN  - EC 2.4.1.- (Fucosyltransferases)
RN  - EC 2.4.1.152 (galactoside 3-fucosyltransferase)
SB  - IM
MH  - Animals
MH  - Cell Movement/genetics/*immunology
MH  - E-Selectin/biosynthesis/metabolism/physiology
MH  - Ear/blood supply
MH  - Female
MH  - Fucosyltransferases/metabolism/*physiology
MH  - Inflammation/enzymology/immunology
MH  - L-Selectin/genetics/physiology
MH  - Leukocytes/*enzymology/*immunology/metabolism
MH  - Ligands
MH  - Male
MH  - Mice
MH  - Mice, Inbred C57BL
MH  - Mice, Knockout
MH  - Microcirculation/enzymology/immunology/metabolism
MH  - P-Selectin/genetics/metabolism/physiology
MH  - Skin/*blood supply/enzymology/immunology/pathology
MH  - Venules/enzymology/immunology/metabolism
EDAT- 2000/07/14 11:00
MHDA- 2000/08/06 11:00
CRDT- 2000/07/14 11:00
PHST- 2000/07/14 11:00 [pubmed]
PHST- 2000/08/06 11:00 [medline]
PHST- 2000/07/14 11:00 [entrez]
AID - S1074-7613(00)80217-4 [pii]
PST - ppublish
SO  - Immunity. 2000 Jun;12(6):665-76.

PMID- 7004456
OWN - NLM
STAT- MEDLINE
DCOM- 19810327
LR  - 20071115
IS  - 0014-4827 (Print)
IS  - 0014-4827 (Linking)
VI  - 131
IP  - 1
DP  - 1981 Jan
TI  - Changes in the expression and polarization of blood group I and i antigens in
      post-implantation embryos and teratocarcinomas of mouse associated with cell
      differentiation.
PG  - 185-95
FAU - Kapadia, A
AU  - Kapadia A
FAU - Feizi, T
AU  - Feizi T
FAU - Evans, M J
AU  - Evans MJ
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Exp Cell Res
JT  - Experimental cell research
JID - 0373226
RN  - 0 (Blood Group Antigens)
RN  - 0 (I Blood-Group System)
SB  - IM
MH  - Animals
MH  - *Blood Group Antigens
MH  - *Cell Differentiation
MH  - Cell Line
MH  - Cell Membrane/immunology
MH  - Cytoplasm/immunology
MH  - Embryo, Mammalian/*immunology
MH  - Endoderm/immunology
MH  - Fluorescent Antibody Technique
MH  - *I Blood-Group System
MH  - Mice
MH  - Teratoma
EDAT- 1981/01/01 00:00
MHDA- 1981/01/01 00:01
CRDT- 1981/01/01 00:00
PHST- 1981/01/01 00:00 [pubmed]
PHST- 1981/01/01 00:01 [medline]
PHST- 1981/01/01 00:00 [entrez]
AID - 0014-4827(81)90418-3 [pii]
PST - ppublish
SO  - Exp Cell Res. 1981 Jan;131(1):185-95.

PMID- 10394128
OWN - NLM
STAT- MEDLINE
DCOM- 19990805
LR  - 20171101
IS  - 0030-2414 (Print)
IS  - 0030-2414 (Linking)
VI  - 57
IP  - 1
DP  - 1999 Jul
TI  - Sialyl Tn is a frequently expressed antigen in colorectal cancer: No correlation 
      with patient prognosis.
PG  - 70-6
AB  - Immunohistochemical expression of sialyl Tn antigen (STn), previously claimed to 
      be a prognostic factor in colorectal cancer, was evaluated in 239 patients with
      colorectal adenocarcinoma. Formalin-fixed, paraffin-embedded specimens were
      stained with the monoclonal antibody C1282. STn immunoreactivity was seen in 189 
      of 239 tumors (79%). There was no significant correlation between STn
      immunoreactivity and Dukes stage, tumor location, histological type or gender.
      However, STn was significantly more often expressed in younger patients. There
      was so significant difference in survival between STn-negative patients (median
      survival 68 months) and STn-positive patients (median survival 79 months). In a
      Cox multivariate analysis, Dukes stage was the strongest predictor of outcome,
      followed by the age of the patient, whereas STn did not provide any prognostic
      information.
FAU - Lundin, M
AU  - Lundin M
AD  - Second Department of Surgery, University of Helsinki, Finland.
FAU - Nordling, S
AU  - Nordling S
FAU - Roberts, P J
AU  - Roberts PJ
FAU - Lundin, J
AU  - Lundin J
FAU - Carpelan-Holmstrom, M
AU  - Carpelan-Holmstrom M
FAU - von Boguslawsky, K
AU  - von Boguslawsky K
FAU - Haglund, C
AU  - Haglund C
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - Switzerland
TA  - Oncology
JT  - Oncology
JID - 0135054
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Biomarkers, Tumor)
RN  - 0 (sialosyl-Tn antigen)
SB  - IM
MH  - Adenocarcinoma/*immunology/pathology
MH  - Adult
MH  - Age Factors
MH  - Aged
MH  - Aged, 80 and over
MH  - Antigens, Tumor-Associated, Carbohydrate/*analysis
MH  - Biomarkers, Tumor/*analysis
MH  - Colorectal Neoplasms/*immunology/pathology
MH  - Female
MH  - Humans
MH  - Immunohistochemistry
MH  - Male
MH  - Middle Aged
MH  - Neoplasm Staging
MH  - Predictive Value of Tests
MH  - Prognosis
MH  - Proportional Hazards Models
MH  - Survival Analysis
EDAT- 1999/07/08 00:00
MHDA- 1999/07/08 00:01
CRDT- 1999/07/08 00:00
PHST- 1999/07/08 00:00 [pubmed]
PHST- 1999/07/08 00:01 [medline]
PHST- 1999/07/08 00:00 [entrez]
AID - 12003 [pii]
AID - 10.1159/000012003 [doi]
PST - ppublish
SO  - Oncology. 1999 Jul;57(1):70-6. doi: 10.1159/000012003.

PMID- 7697593
OWN - NLM
STAT- MEDLINE
DCOM- 19950504
LR  - 20151119
IS  - 0008-543X (Print)
IS  - 0008-543X (Linking)
VI  - 75
IP  - 8
DP  - 1995 Apr 15
TI  - Expression of sialyl Lewis(a) as a new prognostic factor for patients with
      advanced colorectal carcinoma.
PG  - 2051-6
AB  - BACKGROUND: Sialyl Lewis(a) antigen (SLA) is considered to be a cancer-associated
      carbohydrate antigen. METHODS: A total of 309 surgically resected primary
      colorectal cancer specimens and 501 associated metastases to regional lymph nodes
      were analyzed immunohistochemically using a monoclonal antibody (NS19-9)
      recognizing SLA. The specimens were obtained from 1981 to 1988 at the Department 
      of Surgery, Keio University School of Medicine (Tokyo, Japan). RESULTS: Sialyl
      Lewis(a) antigen expression was detected in 75.4% (233/309) of the primary tumors
      and in 78.5% (99/126) of the metastases to regional lymph nodes. Significantly
      stronger expression was noted in the regional lymph node metastases than in the
      primary lesions (P = 4.5E-7). Sialyl Lewis(a) antigen expression in the primary
      tumors correlated significantly with regional lymph node metastasis (P < 0.005), 
      recurrence (P < 0.005), and postoperative survival (P < 0.001) as determined by
      univariate analysis. Sialyl Lewis(a) antigen expression in the regional lymph
      node metastases also correlated strongly with recurrence (P < 0.005) and survival
      (P < 0.01). As determined by multivariate analysis, SLA expression in the primary
      tumor correlated strongly with recurrence (P = 3.0E-6) and survival (P = 6.9E-3).
      CONCLUSIONS: Sialyl Lewis(a) antigen expression in primary tumors and metastases 
      to regional lymph nodes is a useful marker for evaluating tumor aggressiveness
      and prognosis in patients with advanced colorectal cancer.
FAU - Nakayama, T
AU  - Nakayama T
AD  - Department of Surgery, School of Medicine, Keio University, Tokyo, Japan.
FAU - Watanabe, M
AU  - Watanabe M
FAU - Katsumata, T
AU  - Katsumata T
FAU - Teramoto, T
AU  - Teramoto T
FAU - Kitajima, M
AU  - Kitajima M
LA  - eng
PT  - Journal Article
PL  - United States
TA  - Cancer
JT  - Cancer
JID - 0374236
RN  - 0 (Biomarkers, Tumor)
RN  - 0 (Lewis Blood-Group System)
SB  - AIM
SB  - IM
MH  - Aged
MH  - Biomarkers, Tumor/*analysis
MH  - Colorectal Neoplasms/*immunology/mortality/pathology/surgery
MH  - Humans
MH  - Immunoenzyme Techniques
MH  - Lewis Blood-Group System/*analysis
MH  - Middle Aged
MH  - Multivariate Analysis
MH  - Prognosis
EDAT- 1995/04/15 00:00
MHDA- 1995/04/15 00:01
CRDT- 1995/04/15 00:00
PHST- 1995/04/15 00:00 [pubmed]
PHST- 1995/04/15 00:01 [medline]
PHST- 1995/04/15 00:00 [entrez]
PST - ppublish
SO  - Cancer. 1995 Apr 15;75(8):2051-6.

PMID- 16752227
OWN - NLM
STAT- MEDLINE
DCOM- 20070111
LR  - 20081121
IS  - 0167-6806 (Print)
IS  - 0167-6806 (Linking)
VI  - 98
IP  - 1
DP  - 2006 Jul
TI  - Expression of Vicia villosa agglutinin (VVA)-binding glycoprotein in primary
      breast cancer cells in relation to lymphatic metastasis: is atypical MUC1 bearing
      Tn antigen a receptor of VVA?
PG  - 31-43
AB  - Aberrant carbohydrate expression frequently occurs in breast cancer and may endow
      cells with metastatic potential. Here we first studied the relationship between
      expression of Vicia villosa agglutinin (lectin) (VVA)-binding carbohydrates and
      aggressive breast cancer. We then investigated the molecular characteristics of
      these glycoproteins and compared them with those of glycoproteins recognized by
      the mouse anti-Tn monoclonal antibody (MAb) HB-Tn1. Histochemical studies of
      samples from 322 cases of invasive ductal carcinoma demonstrated that VVA-binding
      carbohydrate expression correlated with tumor stage, lymphatic invasion, and
      lymph node metastasis (p=0.0385, p=0.0019, and p=0.0430. respectively). Western
      blotting analysis of frozen materials from 39 cases, under denaturing and
      reducing conditions, revealed that the major cancer cell-specific VVA-binding
      proteins were molecules of about 30, 33, and >200 kDa. Cases expressing the
      approximately 33 kDa molecule had significant lymphatic invasion more frequently 
      than did cases not expressing this molecule (p=0.0076). Binding of VVA to the
      approximately 30 and approximately 33 kDa molecules was completely lost by
      preincubation of VVA with 1 mM Tn antigen (N-acetylgalactosamine
      alpha1-O-serine). The VVA-binding molecules appeared to react with VU-3C6
      anti-MUC1 MAb. Expression of HB-Tn1 in breast cancer cells showed significant
      correlation with expression of VVA-binding carbohydrate(s) (p<0.0001) but HB-Tn1 
      reactivity was not clearly related to breast cancer aggressiveness. Because
      anti-Tn MAbs bound to Tn antigen clusters, we concluded that atypical MUC1
      bearing the noncluster form of Tn antigen is implicated in aggressive growth of
      primary breast cancer cells, particularly in lymphatic metastasis.
FAU - Kawaguchi, Takanori
AU  - Kawaguchi T
AD  - Second Department of Pathology, School of Medicine, Fukushima Medical University,
      Fukushima, and Department of Pathology, Chiba National Hospital, Japan.
      t-kawa@fmu.ac.jp
FAU - Takazawa, Hiroshi
AU  - Takazawa H
FAU - Imai, Shunsuke
AU  - Imai S
FAU - Morimoto, Junji
AU  - Morimoto J
FAU - Watanabe, Takanori
AU  - Watanabe T
FAU - Kanno, Masahiko
AU  - Kanno M
FAU - Igarashi, Seiji
AU  - Igarashi S
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20060605
PL  - Netherlands
TA  - Breast Cancer Res Treat
JT  - Breast cancer research and treatment
JID - 8111104
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Carbohydrates)
RN  - 0 (Epitopes)
RN  - 0 (Glycoproteins)
RN  - 0 (Mucin-1)
RN  - 0 (Plant Lectins)
RN  - 0 (Tn antigen)
RN  - 0 (Vicia lectins)
SB  - IM
MH  - Adult
MH  - Aged
MH  - Antibodies, Monoclonal/chemistry
MH  - Antigens, Tumor-Associated, Carbohydrate/*biosynthesis
MH  - Breast Neoplasms/*metabolism
MH  - Carbohydrates/chemistry
MH  - Cell Proliferation
MH  - Epitopes/chemistry
MH  - Female
MH  - Glycoproteins/*metabolism
MH  - Humans
MH  - Lymphatic Metastasis
MH  - Middle Aged
MH  - Mucin-1/*biosynthesis
MH  - Plant Lectins/*chemistry/metabolism
EDAT- 2006/06/06 09:00
MHDA- 2007/01/12 09:00
CRDT- 2006/06/06 09:00
PHST- 2005/11/01 00:00 [received]
PHST- 2005/11/01 00:00 [accepted]
PHST- 2006/06/06 09:00 [pubmed]
PHST- 2007/01/12 09:00 [medline]
PHST- 2006/06/06 09:00 [entrez]
AID - 10.1007/s10549-005-9115-6 [doi]
PST - ppublish
SO  - Breast Cancer Res Treat. 2006 Jul;98(1):31-43. doi: 10.1007/s10549-005-9115-6.
      Epub 2006 Jun 5.

PMID- 19863951
OWN - NLM
STAT- MEDLINE
DCOM- 20100126
LR  - 20091117
IS  - 1873-426X (Electronic)
IS  - 0008-6215 (Linking)
VI  - 344
IP  - 18
DP  - 2009 Dec 14
TI  - Studies on the interactions between glycosylated beta3-peptides and the lectin
      Vicia villosa by saturation transfer difference NMR spectroscopy.
PG  - 2577-80
LID - 10.1016/j.carres.2009.06.040 [doi]
AB  - Saturation transfer difference (STD) NMR spectroscopy was used to study the
      interaction of the lectin Vicia villosa (VVLB(4)) with alpha-D-GalNAc
      glycosylated beta(3)-peptides. The data were compared to those obtained with the 
      monosaccharides D-Gal, D-GalNAc, and D-Glc as well as with those obtained with
      the Tn antigen alpha-glycopeptide (D-GalNAc-alpha-O-Ser/Thr), molecule naturally 
      recognized by V. villosa. Evidence that the lectin also recognizes glycosylated
      beta(3)-peptides and has close contact with both the sugar and amino acid
      moieties was obtained.
FAU - Kaszowska, Marta
AU  - Kaszowska M
AD  - Department of Chemistry, Swedish University of Agricultural Sciences, PO Box
      7015, SE-750 07 Uppsala, Sweden.
FAU - Norgren, Anna S
AU  - Norgren AS
FAU - Arvidson, Per I
AU  - Arvidson PI
FAU - Sandstrom, Corine
AU  - Sandstrom C
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20090704
PL  - Netherlands
TA  - Carbohydr Res
JT  - Carbohydrate research
JID - 0043535
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Glycopeptides)
RN  - 0 (Monosaccharides)
RN  - 0 (Plant Lectins)
RN  - 0 (Tn antigen)
RN  - 0 (Vicia lectins)
SB  - IM
MH  - Antigens, Tumor-Associated, Carbohydrate
MH  - Glycopeptides/*chemistry
MH  - Magnetic Resonance Spectroscopy/*methods
MH  - Molecular Conformation
MH  - Monosaccharides
MH  - Plant Lectins/*chemistry
MH  - Protein Binding
EDAT- 2009/10/30 06:00
MHDA- 2010/01/27 06:00
CRDT- 2009/10/30 06:00
PHST- 2009/04/27 00:00 [received]
PHST- 2009/06/24 00:00 [revised]
PHST- 2009/06/30 00:00 [accepted]
PHST- 2009/10/30 06:00 [entrez]
PHST- 2009/10/30 06:00 [pubmed]
PHST- 2010/01/27 06:00 [medline]
AID - S0008-6215(09)00307-3 [pii]
AID - 10.1016/j.carres.2009.06.040 [doi]
PST - ppublish
SO  - Carbohydr Res. 2009 Dec 14;344(18):2577-80. doi: 10.1016/j.carres.2009.06.040.
      Epub 2009 Jul 4.

PMID- 2212003
OWN - NLM
STAT- MEDLINE
DCOM- 19901121
LR  - 20181113
IS  - 0021-9738 (Print)
IS  - 0021-9738 (Linking)
VI  - 86
IP  - 4
DP  - 1990 Oct
TI  - Activation pathways of synovial T lymphocytes. Expression and function of the
      UM4D4/CDw60 antigen.
PG  - 1124-36
AB  - Accumulating evidence implicates a central role for synovial T cells in the
      pathogenesis of rheumatoid arthritis, but the activation pathways that drive
      proliferation and effector function of these cells are not known. We have
      recently generated a novel monoclonal antibody against a rheumatoid synovial T
      cell line that recognizes an antigen termed UM4D4 (CDw60). This antigen is
      expressed on a minority of peripheral blood T cells, and represents the surface
      component of a distinct pathway of human T cell activation. The current studies
      were performed to examine the expression and function of UM4D4 on T cells
      obtained from synovial fluid and synovial membranes of patients with rheumatoid
      arthritis and other forms of inflammatory joint disease. The UM4D4 antigen is
      expressed at high surface density on about three-fourths of synovial fluid T
      cells and on a small subset of synovial fluid natural killer cells; in synovial
      tissue it is present on more than 90% of T cells in lymphoid aggregates, and on
      approximately 50% of T cells in stromal infiltrates In addition, UM4D4 is
      expressed in synovial tissue on a previously undescribed population of
      HLA-DR/DP-negative non-T cells with a dendritic morphology. Anti-UM4D4 was
      co-mitogenic for both RA and non-RA synovial fluid mononuclear cells, and induced
      IL-2 receptor expression. The UM4D4/CDw60 antigen may represent a functional
      activation pathway for synovial compartment T cells, which could play an
      important role in the pathogenesis of inflammatory arthritis.
FAU - Fox, D A
AU  - Fox DA
AD  - Department of Internal Medicine, University of Michigan Medical Center, Ann Arbor
      48109.
FAU - Millard, J A
AU  - Millard JA
FAU - Kan, L
AU  - Kan L
FAU - Zeldes, W S
AU  - Zeldes WS
FAU - Davis, W
AU  - Davis W
FAU - Higgs, J
AU  - Higgs J
FAU - Emmrich, F
AU  - Emmrich F
FAU - Kinne, R W
AU  - Kinne RW
LA  - eng
GR  - AR38477/AR/NIAMS NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - J Clin Invest
JT  - The Journal of clinical investigation
JID - 7802877
RN  - 0 (Antigens, CD)
RN  - 0 (Antigens, Differentiation, T-Lymphocyte)
RN  - 0 (Antigens, Surface)
RN  - 0 (CDw60 antigen)
RN  - 0 (Receptors, Interleukin-2)
RN  - NI40JAQ945 (Tetradecanoylphorbol Acetate)
SB  - AIM
SB  - IM
MH  - Adult
MH  - Aged
MH  - Aged, 80 and over
MH  - Antigens, CD/*analysis
MH  - Antigens, Differentiation, T-Lymphocyte/*analysis/physiology
MH  - Antigens, Surface/analysis
MH  - Arthritis, Rheumatoid/*immunology
MH  - Female
MH  - Humans
MH  - *Lymphocyte Activation
MH  - Male
MH  - Middle Aged
MH  - Receptors, Interleukin-2/analysis
MH  - Synovial Fluid/*immunology
MH  - T-Lymphocytes/*immunology
MH  - Tetradecanoylphorbol Acetate/pharmacology
PMC - PMC296841
EDAT- 1990/10/01 00:00
MHDA- 1990/10/01 00:01
CRDT- 1990/10/01 00:00
PHST- 1990/10/01 00:00 [pubmed]
PHST- 1990/10/01 00:01 [medline]
PHST- 1990/10/01 00:00 [entrez]
AID - 10.1172/JCI114817 [doi]
PST - ppublish
SO  - J Clin Invest. 1990 Oct;86(4):1124-36. doi: 10.1172/JCI114817.

PMID- 7678075
OWN - NLM
STAT- MEDLINE
DCOM- 19930203
LR  - 20141120
IS  - 0008-5472 (Print)
IS  - 0008-5472 (Linking)
VI  - 53
IP  - 2
DP  - 1993 Jan 15
TI  - Contribution of carbohydrate antigens sialyl Lewis A and sialyl Lewis X to
      adhesion of human cancer cells to vascular endothelium.
PG  - 354-61
AB  - The carbohydrate antigen, sialyl Lex, is known to be a ligand for the cell
      adhesion molecule called ELAM-1 (E-selectin, endothelial cell leukocyte adhesion 
      molecule-1), which is present on cytokine-activated human endothelial cells.
      Recently, we reported that another carbohydrate antigen, sialyl Lea, can also
      serve as a ligand for ELAM-1 (A. Takada, K. Ohmori, N. Takahashi, K. Tsuyuoka, K.
      Yago, K. Zenita, A. Hasegawa, and R. Kannagi, Biochem. Biophys. Res. Commun.,
      179: 713-719, 1991). Both sialyl Lex and sialyl Lea are expressed in many human
      malignant cells. In order to assess the contribution of these carbohydrate
      antigens to the adhesion of human malignant cells to vascular endothelium, we
      selected a panel of 12 cultured human epithelial cancer cell lines and a panel of
      12 human leukemia cell lines which express sialyl Lex and/or sialyl Lea antigens.
      All 12 epithelial cancer cell lines exhibited a clearly ELAM-1-dependent adhesion
      to cytokine-activated human umbilical vein endothelial cells, while only 3 of the
      12 leukemia cell lines exhibited significant participation of ELAM-1 in the
      adhesion. With regard to epithelial cancer cells, the adhesion of 6 cancer cell
      lines, mostly of colon and pancreas origin, was dependent almost exclusively on
      sialyl Lea. A significant contribution of the sialyl Lex antigen was noted in the
      adhesion of the other 6 cell lines, including cancers of lung and liver origin.
      These results imply that the sialyl Lea/ELAM-1 adhesion system, as well as the
      sialyl Lex/ELAM-1 adhesion system, plays an important role in the adhesion of
      human cancer cells to human umbilical vein endothelial cells. With regard to
      leukemia cells, on the other hand, adhesion of the 3 leukemia cell lines that
      showed ELAM-1-dependent adhesion was mediated by the sialyl Lex antigen, and none
      of these leukemia cell lines expressed sialyl Lea or exhibited sialyl
      Lea-dependent adhesion.
FAU - Takada, A
AU  - Takada A
AD  - Laboratory of Experimental Pathology, Aichi Cancer Center, Nagoya, Japan.
FAU - Ohmori, K
AU  - Ohmori K
FAU - Yoneda, T
AU  - Yoneda T
FAU - Tsuyuoka, K
AU  - Tsuyuoka K
FAU - Hasegawa, A
AU  - Hasegawa A
FAU - Kiso, M
AU  - Kiso M
FAU - Kannagi, R
AU  - Kannagi R
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Cancer Res
JT  - Cancer research
JID - 2984705R
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Cell Adhesion Molecules)
RN  - 0 (E-Selectin)
RN  - 0 (Interleukin-1)
RN  - 0 (Lewis Blood-Group System)
RN  - 0 (Vascular Cell Adhesion Molecule-1)
RN  - 126547-89-5 (Intercellular Adhesion Molecule-1)
SB  - IM
MH  - Antigens, Tumor-Associated, Carbohydrate/*metabolism
MH  - Carbohydrate Sequence
MH  - *Cell Adhesion
MH  - Cell Adhesion Molecules/metabolism
MH  - E-Selectin
MH  - Endothelium, Vascular/*cytology
MH  - Epithelial Cells
MH  - Humans
MH  - Immunologic Techniques
MH  - In Vitro Techniques
MH  - Intercellular Adhesion Molecule-1
MH  - Interleukin-1/pharmacology
MH  - Lewis Blood-Group System/*physiology
MH  - Molecular Sequence Data
MH  - Tumor Cells, Cultured
MH  - Vascular Cell Adhesion Molecule-1
EDAT- 1993/01/15 00:00
MHDA- 1993/01/15 00:01
CRDT- 1993/01/15 00:00
PHST- 1993/01/15 00:00 [pubmed]
PHST- 1993/01/15 00:01 [medline]
PHST- 1993/01/15 00:00 [entrez]
PST - ppublish
SO  - Cancer Res. 1993 Jan 15;53(2):354-61.

PMID- 1732113
OWN - NLM
STAT- MEDLINE
DCOM- 19920225
LR  - 20171228
IS  - 0016-5085 (Print)
IS  - 0016-5085 (Linking)
VI  - 102
IP  - 2
DP  - 1992 Feb
TI  - Lewis antigen alterations in gastric cancer precursors.
PG  - 424-30
AB  - To explore the dynamics of the progressive loss of cell differentiation observed 
      in the gastric precancerous process, the abnormal expression of Lea antigen in
      the gastric epithelium was investigated. Gastric biopsy specimens of 122 subjects
      with Le(a-b+) phenotype who had intestinal metaplasia of the gastric mucosa were 
      studied. The subjects are residents of a rural area in the Colombian Andes with
      very high risk of gastric cancer. The abnormality was detected with increasing
      frequency in lesions with other markers of progression of the precancerous
      process, namely, colonic-type of morphology of the metaplastic cells, expression 
      of sulfomucins, and dysplastic changes. The concomitant expression of the
      abnormal Lea antigen and sulfomucins was found to be a more reliable marker of
      more advanced lesions such as colonic metaplasia and dysplasia than either marker
      alone.
FAU - Torrado, J
AU  - Torrado J
AD  - Department of Anatomic Pathology, Hospital Nuestra Sra. Aranzazu, San Sebastian, 
      Spain.
FAU - Correa, P
AU  - Correa P
FAU - Ruiz, B
AU  - Ruiz B
FAU - Bernardi, P
AU  - Bernardi P
FAU - Zavala, D
AU  - Zavala D
FAU - Bara, J
AU  - Bara J
LA  - eng
GR  - P01-CA28842/CA/NCI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Gastroenterology
JT  - Gastroenterology
JID - 0374630
RN  - 0 (Isoantigens)
RN  - 0 (Lewis Blood-Group System)
SB  - AIM
SB  - IM
MH  - Aging/blood
MH  - Female
MH  - Gastric Mucosa/pathology
MH  - Humans
MH  - Isoantigens/*biosynthesis
MH  - Lewis Blood-Group System/*immunology
MH  - Male
MH  - Metaplasia
MH  - Phenotype
MH  - Precancerous Conditions/*blood/pathology
MH  - Stomach Neoplasms/*blood/pathology
EDAT- 1992/02/01 00:00
MHDA- 1992/02/01 00:01
CRDT- 1992/02/01 00:00
PHST- 1992/02/01 00:00 [pubmed]
PHST- 1992/02/01 00:01 [medline]
PHST- 1992/02/01 00:00 [entrez]
AID - 0016-5085(92)90086-E [pii]
PST - ppublish
SO  - Gastroenterology. 1992 Feb;102(2):424-30.

PMID- 2662714
OWN - NLM
STAT- MEDLINE
DCOM- 19890802
LR  - 20180119
IS  - 0065-230X (Print)
IS  - 0065-230X (Linking)
VI  - 52
DP  - 1989
TI  - Aberrant glycosylation in tumors and tumor-associated carbohydrate antigens.
PG  - 257-331
FAU - Hakomori, S
AU  - Hakomori S
AD  - Biomembrane Institute, Seattle, Washington 98119.
LA  - eng
GR  - CA 42505/CA/NCI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PT  - Review
PL  - United States
TA  - Adv Cancer Res
JT  - Advances in cancer research
JID - 0370416
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
SB  - IM
MH  - Animals
MH  - Antigens, Tumor-Associated, Carbohydrate/*immunology
MH  - Glycosylation
MH  - Humans
MH  - Neoplasms/genetics/immunology/*metabolism
RF  - 358
EDAT- 1989/01/01 00:00
MHDA- 1989/01/01 00:01
CRDT- 1989/01/01 00:00
PHST- 1989/01/01 00:00 [pubmed]
PHST- 1989/01/01 00:01 [medline]
PHST- 1989/01/01 00:00 [entrez]
AID - S0065-230X(08)60215-8 [pii]
PST - ppublish
SO  - Adv Cancer Res. 1989;52:257-331.

PMID- 19674101
OWN - NLM
STAT- MEDLINE
DCOM- 20090915
LR  - 20181201
IS  - 1742-4658 (Electronic)
IS  - 1742-464X (Linking)
VI  - 276
IP  - 18
DP  - 2009 Sep
TI  - A novel, promoter-based, target-specific assay identifies 2-deoxy-D-glucose as an
      inhibitor of globotriaosylceramide biosynthesis.
PG  - 5191-202
LID - 10.1111/j.1742-4658.2009.07215.x [doi]
AB  - Abnormal biosynthesis of globotriaosylceramide (Gb3) is known to be associated
      with Gb3-related diseases, such as Fabry disease. The Gb3 synthase gene (Gb3S)
      codes for alpha1,4-galactosyltransferase, which is a key enzyme involved in Gb3
      biosynthesis in vivo. Transcriptional repression of Gb3S is a way to control Gb3 
      biosynthesis and may be a suitable target for the treatment of Gb3-related
      diseases. To find a transcriptional inhibitor for Gb3S, we developed a convenient
      cell-based chemical screening assay system by constructing a fusion gene
      construct of the human Gb3S promoter and a secreted luciferase as reporter. Using
      this assay, we identified 2-deoxy-D-glucose as a potent inhibitor for the Gb3S
      promoter. In cultured cells, 2-deoxy-D-glucose markedly reduced endogenous Gb3S
      mRNA levels, resulting in a reduction in cellular Gb3 content and a corresponding
      accumulation of the precursor lactosylceramide. Moreover, cytokine-induced
      expression of Gb3 on the cell surface of endothelial cells, which is closely
      related to the onset of hemolytic uremic syndrome in O157-infected patients, was 
      also suppressed by 2-deoxy-D-glucose treatment. These results indicate that
      2-deoxy-D-glucose can control Gb3 biosynthesis through the inhibition of Gb3S
      transcription. Furthermore, we demonstrated the general utility of our novel
      screening assay for the identification of new inhibitors of glycosphingolipid
      biosynthesis.
FAU - Okuda, Tetsuya
AU  - Okuda T
AD  - Glycolipids Function Analysis Team, Health Technology Research Center, National
      Institute of Advanced Industrial Science and Technology, Kagawa, Japan.
      t-okuda@aist.go.jp
FAU - Furukawa, Koichi
AU  - Furukawa K
FAU - Nakayama, Ken-ichi
AU  - Nakayama K
LA  - eng
PT  - Journal Article
DEP - 20090810
PL  - England
TA  - FEBS J
JT  - The FEBS journal
JID - 101229646
RN  - 0 (ATP Binding Cassette Transporter, Subfamily B, Member 1)
RN  - 0 (Enzyme Inhibitors)
RN  - 0 (Repressor Proteins)
RN  - 0 (Trihexosylceramides)
RN  - 0 (Tumor Necrosis Factor-alpha)
RN  - 71965-57-6 (globotriaosylceramide)
RN  - 9G2MP84A8W (Deoxyglucose)
RN  - EC 2.4.1.- (Galactosyltransferases)
RN  - EC 2.4.1.- (UDP-galactose-lactosylceramide alpha 1-4-galactosyltransferase)
SB  - IM
MH  - ATP Binding Cassette Transporter, Subfamily B, Member 1/antagonists & inhibitors
MH  - Cells, Cultured
MH  - Deoxyglucose/*pharmacology
MH  - Enzyme Inhibitors/*pharmacology
MH  - Galactosyltransferases/*antagonists & inhibitors/genetics
MH  - Humans
MH  - *Promoter Regions, Genetic
MH  - Repressor Proteins/physiology
MH  - Trihexosylceramides/biosynthesis
MH  - Tumor Necrosis Factor-alpha/pharmacology
EDAT- 2009/08/14 09:00
MHDA- 2009/09/16 06:00
CRDT- 2009/08/14 09:00
PHST- 2009/08/14 09:00 [entrez]
PHST- 2009/08/14 09:00 [pubmed]
PHST- 2009/09/16 06:00 [medline]
AID - EJB7215 [pii]
AID - 10.1111/j.1742-4658.2009.07215.x [doi]
PST - ppublish
SO  - FEBS J. 2009 Sep;276(18):5191-202. doi: 10.1111/j.1742-4658.2009.07215.x. Epub
      2009 Aug 10.

PMID- 11278338
OWN - NLM
STAT- MEDLINE
DCOM- 20010614
LR  - 20171116
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 276
IP  - 19
DP  - 2001 May 11
TI  - CD15 expression in mature granulocytes is determined by alpha
      1,3-fucosyltransferase IX, but in promyelocytes and monocytes by alpha
      1,3-fucosyltransferase IV.
PG  - 16100-6
AB  - The CD15 carbohydrate epitope is expressed in mature human neutrophils,
      monocytes, and promyelocytes. We aimed to determine the
      alpha1,3-fucosyltransferase responsible for the expression of CD15 in each
      subpopulation of leukocytes. Three alpha1,3-fucosyltransferases, FUT4, FUT7, and 
      FUT9, are expressed in human leukocytes. We demonstrated that FUT9 exhibits
      20-fold stronger activity for CD15 synthesis than FUT4, whereas FUT4 exhibits
      4.5-fold stronger activity for CDw65 synthesis than FUT9. By competitive reverse 
      transcriptase-polymerase chain reaction, FUT9 was found to be strongly expressed 
      in mature granulocytes and peripheral blood mononuclear cell, but not in
      monocytes. CD34(+) and CD15(+) cells in cord blood and myeloid cell lines (HL-60 
      and U937) did not express FUT9 at all. FUT4 transcripts were ubiquitously
      expressed in all blood cells and all cultured cell lines, with HL-60 and U937
      cells in particular expressing a number of FUT4 transcripts. Transfection of the 
      FUT9 gene into Jurkat and U937 cells demonstrated that FUT9 has the potential to 
      express CD15 in myeloid and lymphoid cells. These findings suggest that the
      expression of CD15 in mature granulocytes is directed by FUT9, whereas it is
      determined in promyelocytes and monocytes by FUT4. Measurement of CD15
      synthesizing activity in cell homogenates of each cell population using the
      polylactosamine acceptor further supported these conclusions.
FAU - Nakayama, F
AU  - Nakayama F
AD  - Division of Cell Biology, Institute of Life Science, Soka University, Tokyo
      192-8577, Japan.
FAU - Nishihara, S
AU  - Nishihara S
FAU - Iwasaki, H
AU  - Iwasaki H
FAU - Kudo, T
AU  - Kudo T
FAU - Okubo, R
AU  - Okubo R
FAU - Kaneko, M
AU  - Kaneko M
FAU - Nakamura, M
AU  - Nakamura M
FAU - Karube, M
AU  - Karube M
FAU - Sasaki, K
AU  - Sasaki K
FAU - Narimatsu, H
AU  - Narimatsu H
LA  - eng
PT  - Comparative Study
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20010223
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Antigens, CD)
RN  - 0 (Lewis X Antigen)
RN  - 0 (Recombinant Fusion Proteins)
RN  - EC 2.4.1.- (Fucosyltransferases)
RN  - EC 2.4.1.152 (galactoside 3-fucosyltransferase)
SB  - IM
MH  - Antigens, CD/biosynthesis/chemistry
MH  - Carbohydrate Sequence
MH  - Cells, Cultured
MH  - Fucosyltransferases/*genetics/*metabolism
MH  - Granulocytes/*metabolism
MH  - HL-60 Cells
MH  - Humans
MH  - Jurkat Cells
MH  - Lewis X Antigen/*biosynthesis/chemistry
MH  - Molecular Sequence Data
MH  - Monocytes/*metabolism
MH  - Recombinant Fusion Proteins/metabolism
MH  - Reverse Transcriptase Polymerase Chain Reaction
MH  - Transcription, Genetic
MH  - Transfection
MH  - Tumor Cells, Cultured
MH  - U937 Cells
EDAT- 2001/03/30 10:00
MHDA- 2001/06/15 10:01
CRDT- 2001/03/30 10:00
PHST- 2001/03/30 10:00 [pubmed]
PHST- 2001/06/15 10:01 [medline]
PHST- 2001/03/30 10:00 [entrez]
AID - 10.1074/jbc.M007272200 [doi]
AID - M007272200 [pii]
PST - ppublish
SO  - J Biol Chem. 2001 May 11;276(19):16100-6. doi: 10.1074/jbc.M007272200. Epub 2001 
      Feb 23.

PMID- 16621820
OWN - NLM
STAT- MEDLINE
DCOM- 20060612
LR  - 20181113
IS  - 0021-9193 (Print)
IS  - 0021-9193 (Linking)
VI  - 188
IP  - 9
DP  - 2006 May
TI  - Mutation of waaC, encoding heptosyltransferase I in Campylobacter jejuni 81-176, 
      affects the structure of both lipooligosaccharide and capsular carbohydrate.
PG  - 3273-9
AB  - Campylobacter jejuni 81-176 lipooligosaccharide (LOS) is composed of two
      covalently linked domains: lipid A, a hydrophobic anchor, and a nonrepeating core
      oligosaccharide, consisting of an inner and outer core region. We report the
      isolation and characterization of the deepest rough C. jejuni 81-176 mutant by
      insertional mutagenesis into the waaC gene, encoding heptosyltransferase I that
      catalyzes the transfer of the first L-glycero-D-manno-heptose residue to
      3-deoxy-D-manno-octulosonic residue (Kdo)-lipid A. Tricine gel electrophoresis,
      followed by silver staining, showed that site-specific mutation in the waaC gene 
      resulted in the expression of a severely truncated LOS compared to wild-type
      strain 81-176. Gas-liquid chromatography-mass spectrometry and nuclear magnetic
      resonance spectroscopy showed that the waaC LOS species lacked all sugars distal 
      to Kdo-lipid A. Parallel structural studies of the capsular polysaccharides of
      the wild-type strain 81-176 and waaC mutant revealed loss of the 3-O-methyl group
      in the waaC mutant. Complementation of the C. jejuni mutant by insertion of the
      wild-type C. jejuni waaC gene into a chromosomal locus resulted in LOS and
      capsular structures identical to those expressed in the parent strain. We also
      report here the presence of O-methyl phosphoramidate in wild-type strain 81-176
      capsular polysaccharide.
FAU - Kanipes, Margaret I
AU  - Kanipes MI
AD  - Department of Chemistry, North Carolina Agricultural and Technical State
      University, Greensboro, North Carolina 27411, USA.
FAU - Papp-Szabo, Erzsebet
AU  - Papp-Szabo E
FAU - Guerry, Patricia
AU  - Guerry P
FAU - Monteiro, Mario A
AU  - Monteiro MA
LA  - eng
SI  - GENBANK/AY862985
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - J Bacteriol
JT  - Journal of bacteriology
JID - 2985120R
RN  - 0 (Carbohydrates)
RN  - 0 (DNA, Bacterial)
RN  - 0 (Flavonoids)
RN  - 0 (Lipopolysaccharides)
RN  - 0 (lipid-linked oligosaccharides)
RN  - D51JZL38TQ (tricin)
RN  - EC 2.4.- (Glycosyltransferases)
RN  - EC 2.4.99.- (heptosyltransferase)
SB  - IM
MH  - Bacterial Capsules/*chemistry/metabolism
MH  - Campylobacter jejuni/genetics/*metabolism/pathogenicity
MH  - Carbohydrate Metabolism
MH  - Carbohydrates/analysis/*chemistry
MH  - DNA, Bacterial
MH  - Electrophoresis, Gel, Two-Dimensional
MH  - Flavonoids
MH  - Gastroenteritis/etiology
MH  - Glycosyltransferases/genetics/*metabolism
MH  - Guillain-Barre Syndrome/etiology
MH  - Lipopolysaccharides/*chemistry/metabolism
MH  - Magnetic Resonance Spectroscopy
MH  - Molecular Sequence Data
MH  - Mutagenesis, Insertional
MH  - Virulence
PMC - PMC1447440
EDAT- 2006/04/20 09:00
MHDA- 2006/06/13 09:00
CRDT- 2006/04/20 09:00
PHST- 2006/04/20 09:00 [pubmed]
PHST- 2006/06/13 09:00 [medline]
PHST- 2006/04/20 09:00 [entrez]
AID - 188/9/3273 [pii]
AID - 10.1128/JB.188.9.3273-3279.2006 [doi]
PST - ppublish
SO  - J Bacteriol. 2006 May;188(9):3273-9. doi: 10.1128/JB.188.9.3273-3279.2006.

PMID- 3479188
OWN - NLM
STAT- MEDLINE
DCOM- 19880114
LR  - 20151119
IS  - 0007-1048 (Print)
IS  - 0007-1048 (Linking)
VI  - 67
IP  - 2
DP  - 1987 Oct
TI  - Detection of the Tn antigen in leukaemia using monoclonal anti-Tn antibody and
      immunohistochemistry.
PG  - 153-6
AB  - Exposure of the normally cryptic Tn antigen on haemopoietic cells leading to
      erythrocyte polyagglutination has been reported in a few cases of malignant or
      premalignant haemopoietic disorders and has been attributed to a selective
      deficiency of the enzyme 3-beta-D-galactosyl-transferase. A male patient
      presented with acute myelomonocytic leukaemia with no evidence of Tn expression
      but, 16 months later, in the terminal stage of the disease, the majority of the
      erythrocytes were found to be polyagglutinable. Tn expression was confirmed by
      the use of lectins and by agglutination with a Tn-specific monoclonal antibody,
      FBT3. Retrospective studies of stored blood and bone marrow smears were performed
      by immunocytochemistry using FBT3. Tn positive cells were first detected in the
      marrow 8 months prior to death. They increased progressively in number and, in
      the terminal illness, over 90% of erythroid precursors in the marrow and
      erythrocytes in peripheral blood and 40% of granulocyte precursors of the marrow 
      and 10% of granulocytes in the blood were Tn positive. These observations suggest
      that Tn expression was present in a subclone of cells which became dominant
      during the course of the disease and that there may be a relationship between Tn 
      expression and leukaemic progression.
FAU - Roxby, D J
AU  - Roxby DJ
AD  - Department of Haematology, Flinders Medical Centre, Bedford Park, South
      Australia.
FAU - Morley, A A
AU  - Morley AA
FAU - Burpee, M
AU  - Burpee M
LA  - eng
PT  - Case Reports
PT  - Journal Article
PL  - England
TA  - Br J Haematol
JT  - British journal of haematology
JID - 0372544
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens, Neoplasm)
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Tn antigen)
SB  - IM
MH  - Aged
MH  - Antibodies, Monoclonal
MH  - Antigens, Neoplasm/*analysis
MH  - *Antigens, Tumor-Associated, Carbohydrate
MH  - Hematopoietic Stem Cells/*immunology
MH  - Humans
MH  - Immunohistochemistry
MH  - Leukemia, Myeloid, Acute/*immunology
MH  - Male
EDAT- 1987/10/01 00:00
MHDA- 1987/10/01 00:01
CRDT- 1987/10/01 00:00
PHST- 1987/10/01 00:00 [pubmed]
PHST- 1987/10/01 00:01 [medline]
PHST- 1987/10/01 00:00 [entrez]
PST - ppublish
SO  - Br J Haematol. 1987 Oct;67(2):153-6.

PMID- 3731100
OWN - NLM
STAT- MEDLINE
DCOM- 19860918
LR  - 20041117
IS  - 0008-5472 (Print)
IS  - 0008-5472 (Linking)
VI  - 46
IP  - 9
DP  - 1986 Sep
TI  - Generation of monoclonal antibodies against human lung squamous cell carcinoma
      and adenocarcinoma using mice rendered tolerant to normal human lung.
PG  - 4438-43
AB  - Four murine monoclonal antibodies against human lung carcinoma were generated
      using a novel immunization procedure. BALB/c mice were rendered neonatally
      tolerant to normal human lung tissues and subsequently immunized with human lung 
      tumor tissues. The lower level of antibody-reactivity to the tolerogen was seen
      in the sera of mice rendered neonatally tolerant as compared with the level of
      reactivity in the sera of nontolerant mice. The mice which maintained a
      sufficiently tolerant state were selected for hybridoma production. Two
      monoclonal antibodies, KM-32 and KM-34, were developed from mice immunized with
      lung squamous cell carcinoma tissues and two other monoclonal antibodies, KM-52
      and KM-93, were developed from mice immunized with lung adenocarcinoma tissues.
      Distribution of antigens detected by the monoclonal antibodies were investigated 
      by enzyme-linked immunosorbent assay using membrane fractions prepared from a
      number of tumorous and normal tissues and various human normal and tumor cell
      lines. KM-32 recognized a carbohydrate antigen expressed predominantly on lung
      squamous cell carcinoma cells and its carbohydrate structure appeared to be
      associated with blood group A antigen. KM-93 recognized a sialylated carbohydrate
      epitope on the antigen expressed on lung adeno-carcinoma cells and a few other
      tumor cells. KM-34 and KM-52 detected protein or glycoprotein antigens and they
      showed predominant reactivity to lung squamous cell carcinoma and lung
      adenocarcinoma, respectively. KM-32 and KM-34 antibodies showed
      complement-dependent cytotoxicity against a lung tumor cell line. These results
      suggest that the tolerance technique is useful for efficient screening of murine 
      monoclonal antibodies specific to human tumors. The efficacy of these four
      monoclonal antibodies in diagnosis and therapy of lung cancer will be the subject
      of a sequential study.
FAU - Hanai, N
AU  - Hanai N
FAU - Shitara, K
AU  - Shitara K
FAU - Yoshida, H
AU  - Yoshida H
LA  - eng
PT  - Journal Article
PL  - United States
TA  - Cancer Res
JT  - Cancer research
JID - 2984705R
RN  - 0 (Antibodies, Monoclonal)
SB  - IM
MH  - Adenocarcinoma/*immunology
MH  - Animals
MH  - Antibodies, Monoclonal/*immunology
MH  - Antibody Specificity
MH  - Binding, Competitive
MH  - Carcinoma, Squamous Cell/*immunology
MH  - Cell Line
MH  - Cell Membrane/immunology
MH  - Cytotoxicity Tests, Immunologic
MH  - Enzyme-Linked Immunosorbent Assay
MH  - Hemagglutination Tests
MH  - Humans
MH  - Immune Tolerance
MH  - Lung/immunology
MH  - Lung Neoplasms/*immunology
MH  - Mice
EDAT- 1986/09/01 00:00
MHDA- 1986/09/01 00:01
CRDT- 1986/09/01 00:00
PHST- 1986/09/01 00:00 [pubmed]
PHST- 1986/09/01 00:01 [medline]
PHST- 1986/09/01 00:00 [entrez]
PST - ppublish
SO  - Cancer Res. 1986 Sep;46(9):4438-43.

PMID- 8835180
OWN - NLM
STAT- MEDLINE
DCOM- 19961213
LR  - 20080815
IS  - 1121-760X (Print)
IS  - 1121-760X (Linking)
VI  - 39
IP  - 4
DP  - 1995
TI  - Immunohistochemical localization of chondroitin sulfate in the forestomach of the
      sheep.
PG  - 265-72
AB  - The localization of chondroitin sulfate glycosaminoglycans in the forestomach
      mucosa was examined by use of monoclonal mouse IgMs against chondroitin sulfate
      (CS-56 and 2H6). Under the light microscope, immunoreactive sites were observed
      in subepithelial regions and around blood vessels of the rumen, reticulum and
      omasum. In the reticular papillae and omasal papillae, large areas of core
      regions also reacted with the monoclonal antibodies. The cell surfaces of
      fibroblasts in the core region of the epithelium were intensely stained. Under
      the electron microscope, heavy staining of collagen fibrils beneath the basement 
      membrane of the mucosal epithelium was observed. In addition, products of
      immunoreactions were localized at the abluminal surfaces of endothelial cells, in
      pinocytotic vesicles and on pits of the endothelium, as well as surrounding
      collagen fibrils. At the core regions of reticular papillae and omasal papillae, 
      cell surfaces, interstitial area of collagen fibrils and elastin fibers were
      stained. Some of the rough endoplasmic reticulum in fibroblasts was also stained.
      These results suggest that chondroitin sulfate in the forestomach mucosa might
      serve as a charge barrier in the transport of charged molecules.
FAU - Yamamoto, Y
AU  - Yamamoto Y
AD  - Department of Veterinary Science, Gifu University, Japan.
FAU - Atoji, Y
AU  - Atoji Y
FAU - Oohira, A
AU  - Oohira A
FAU - Suzuki, Y
AU  - Suzuki Y
LA  - eng
PT  - Journal Article
PL  - Italy
TA  - Eur J Histochem
JT  - European journal of histochemistry : EJH
JID - 9207930
RN  - 0 (Antibodies)
RN  - 9007-28-7 (Chondroitin Sulfates)
SB  - IM
MH  - Animals
MH  - Antibodies
MH  - Chondroitin Sulfates/*analysis
MH  - Female
MH  - Immunohistochemistry
MH  - Male
MH  - Microscopy, Electron
MH  - Microscopy, Immunoelectron
MH  - Mucous Membrane/chemistry/ultrastructure
MH  - Omasum/chemistry/ultrastructure
MH  - Rumen/chemistry
MH  - Sheep
MH  - Stomach, Ruminant/*chemistry
EDAT- 1995/01/01 00:00
MHDA- 1995/01/01 00:01
CRDT- 1995/01/01 00:00
PHST- 1995/01/01 00:00 [pubmed]
PHST- 1995/01/01 00:01 [medline]
PHST- 1995/01/01 00:00 [entrez]
PST - ppublish
SO  - Eur J Histochem. 1995;39(4):265-72.

PMID- 16990264
OWN - NLM
STAT- MEDLINE
DCOM- 20070109
LR  - 20061120
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 281
IP  - 47
DP  - 2006 Nov 24
TI  - Crystal structure of the galectin-9 N-terminal carbohydrate recognition domain
      from Mus musculus reveals the basic mechanism of carbohydrate recognition.
PG  - 35884-93
AB  - The galectins are a family of beta-galactoside-binding animal lectins with a
      conserved carbohydrate recognition domain (CRD). They have a high affinity for
      small beta-galactosides, but binding specificity for complex glycoconjugates
      varies considerably within the family. The ligand recognition is essential for
      their proper function, and the structures of several galectins have suggested
      their mechanism of carbohydrate binding. Galectin-9 has two tandem CRDs with a
      short linker, and we report the crystal structures of mouse galectin-9 N-terminal
      CRD (NCRD) in the absence and the presence of four ligand complexes. All
      structures form the same dimer, which is quite different from the canonical
      2-fold symmetric dimer seen for galectin-1 and -2. The beta-galactoside
      recognition mechanism in the galectin-9 NCRD is highly conserved among other
      galectins. In the apo form structure, water molecules mimic the ligand
      hydrogen-bond network. The galectin-9 NCRD can bind both N-acetyllactosamine
      (Galbeta1-4GlcNAc) and T-antigen (Galbeta1-3GalNAc) with the proper location of
      Arg-64. Moreover, the structure of the N-acetyllactosamine dimer
      (Galbeta1-4GlcNAcbeta1-3Galbeta1-4GlcNAc) complex shows a unique binding mode of 
      galectin-9. Finally, surface plasmon resonance assay showed that the galectin-9
      NCRD forms a homophilic dimer not only in the crystal but also in solution.
FAU - Nagae, Masamichi
AU  - Nagae M
AD  - Structural Biology Research Center, Photon Factory, Institute of Materials
      Structure Science, High Energy Accelerator Research Organization, Tsukuba,
      Ibaraki 305-0801, Japan.
FAU - Nishi, Nozomu
AU  - Nishi N
FAU - Murata, Takeomi
AU  - Murata T
FAU - Usui, Taichi
AU  - Usui T
FAU - Nakamura, Takanori
AU  - Nakamura T
FAU - Wakatsuki, Soichi
AU  - Wakatsuki S
FAU - Kato, Ryuichi
AU  - Kato R
LA  - eng
SI  - PDB/2D6K
SI  - PDB/2D6L
SI  - PDB/2D6M
SI  - PDB/2D6N
SI  - PDB/2D6O
SI  - PDB/2D6P
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20060921
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Carbohydrates)
RN  - 0 (Galectins)
RN  - 0 (Ligands)
RN  - 0 (galectin 9, mouse)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Carbohydrates/*chemistry
MH  - Crystallography, X-Ray
MH  - Dimerization
MH  - Dose-Response Relationship, Drug
MH  - Galectins/*chemistry
MH  - Hydrogen Bonding
MH  - Ligands
MH  - Mice
MH  - Models, Molecular
MH  - Molecular Sequence Data
MH  - Protein Structure, Tertiary
MH  - Sequence Homology, Amino Acid
MH  - Surface Plasmon Resonance
EDAT- 2006/09/23 09:00
MHDA- 2007/01/11 09:00
CRDT- 2006/09/23 09:00
PHST- 2006/09/23 09:00 [pubmed]
PHST- 2007/01/11 09:00 [medline]
PHST- 2006/09/23 09:00 [entrez]
AID - M606648200 [pii]
AID - 10.1074/jbc.M606648200 [doi]
PST - ppublish
SO  - J Biol Chem. 2006 Nov 24;281(47):35884-93. doi: 10.1074/jbc.M606648200. Epub 2006
      Sep 21.

PMID- 17090649
OWN - NLM
STAT- MEDLINE
DCOM- 20070402
LR  - 20131121
IS  - 0006-4971 (Print)
IS  - 0006-4971 (Linking)
VI  - 109
IP  - 6
DP  - 2007 Mar 15
TI  - Variations in glycosylation of von Willebrand factor with O-linked sialylated T
      antigen are associated with its plasma levels.
PG  - 2430-7
AB  - The glycosylation profile of von Willebrand factor (VWF) is known to strongly
      influence its plasma levels. VWF contains several carbohydrate structures,
      including O-linked glycans that primarily consist of sialylated T antigen
      (NeuAc(alpha2-3)Gal-(beta1-3)-[NeuAc(alpha2-6)]GalNAc). It is not yet known
      whether O-linked carbohydrates affect VWF levels. We developed an immunosorbent
      assay based on neuraminidase incubation allowing subsequent binding of peanut
      agglutinin (PNA) to desialylated O-linked T antigen on VWF. An inverse relation
      was found between PNA binding and VWF antigen levels in healthy individuals (n = 
      111; Pearson rank = -0.43; P < .001). A similar inverse association was observed 
      in randomly selected plasma samples from our diagnostic laboratory: 252% +/- 125%
      for VWF levels less than 0.5 U/mL (n = 15); 131% +/- 36% for VWF levels between
      0.5 and 1.5 U/mL (n = 32); and 92% +/- 40% for VWF levels more than 1.5 U/mL (n =
      19). Reduced or increased PNA binding was also observed in patients with
      increased (liver cirrhosis) or reduced (von Willebrand disease [VWD] type 1) VWF 
      antigen levels, respectively. VWD type 1 patients further displayed increased
      ratios of propeptide over mature VWF antigen levels (0.38 +/- 0.18 versus 0.17
      +/- 0.03 for patients and controls, respectively; P < .001), which is indicative 
      of reduced VWF survival in these patients. Of interest, a linear relation between
      PNA binding and propeptide/VWF ratio was observed (Spearman rank = 0.47),
      suggesting a potential association between O-linked glycosylation and VWF
      survival. Finally, we detected a marked decrease in PNA binding in post-DDAVP
      (1-deamino-8-D-arginine vasopressin) samples from various patients, indicating
      that the O-linked glycosylation profile of VWF stored in endothelial storage
      organelles may differ from circulating VWF.
FAU - van Schooten, Carina J M
AU  - van Schooten CJ
AD  - Laboratory for Thrombosis and Haemostasis, Department of Clinical Chemistry and
      Haematology, University Medical Center Utrecht, Utrecht, the Netherlands.
FAU - Denis, Cecile V
AU  - Denis CV
FAU - Lisman, Ton
AU  - Lisman T
FAU - Eikenboom, Jeroen C J
AU  - Eikenboom JC
FAU - Leebeek, Frank W
AU  - Leebeek FW
FAU - Goudemand, Jenny
AU  - Goudemand J
FAU - Fressinaud, Edith
AU  - Fressinaud E
FAU - van den Berg, H Marijke
AU  - van den Berg HM
FAU - de Groot, Philip G
AU  - de Groot PG
FAU - Lenting, Peter J
AU  - Lenting PJ
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20061107
PL  - United States
TA  - Blood
JT  - Blood
JID - 7603509
RN  - 0 (Antigens, Viral, Tumor)
RN  - 0 (Peanut Agglutinin)
RN  - 0 (von Willebrand Factor)
RN  - GZP2782OP0 (N-Acetylneuraminic Acid)
SB  - AIM
SB  - IM
MH  - Antigens, Viral, Tumor/*blood/*genetics
MH  - Genetic Variation/*genetics
MH  - Glycosylation
MH  - Humans
MH  - Liver Cirrhosis/blood/genetics
MH  - N-Acetylneuraminic Acid/*metabolism
MH  - Peanut Agglutinin/metabolism
MH  - Protein Binding
MH  - Protein Processing, Post-Translational
MH  - von Willebrand Factor/chemistry/*genetics/*metabolism
EDAT- 2006/11/09 09:00
MHDA- 2007/04/03 09:00
CRDT- 2006/11/09 09:00
PHST- 2006/11/09 09:00 [pubmed]
PHST- 2007/04/03 09:00 [medline]
PHST- 2006/11/09 09:00 [entrez]
AID - blood-2006-06-032706 [pii]
AID - 10.1182/blood-2006-06-032706 [doi]
PST - ppublish
SO  - Blood. 2007 Mar 15;109(6):2430-7. doi: 10.1182/blood-2006-06-032706. Epub 2006
      Nov 7.

PMID- 3731079
OWN - NLM
STAT- MEDLINE
DCOM- 19860917
LR  - 20071114
IS  - 0008-5472 (Print)
IS  - 0008-5472 (Linking)
VI  - 46
IP  - 8
DP  - 1986 Aug
TI  - A murine monoclonal antibody detecting N-acetyl- and N-glycolyl-GM2:
      characterization of cell surface reactivity.
PG  - 4116-20
AB  - Antisera reactive with the ganglioside GM2 were raised by immunizing C57BL/6 mice
      with the C57BL/6 melanoma JB-RH. Fusion with NS-1 was performed using splenic
      mononuclear cells from a mouse with high antibody titer. An immunoglobulin M
      monoclonal antibody (monoclonal antibody 5-3) was identified which was reactive
      with an antigen that was resistant to heat, trypsin, and Pronase. A panel of
      purified glycolipids was used to determine the specificity of monoclonal antibody
      5-3. Reactivity was restricted to N-acetyl- and N-glycolyl-GM2. No reactivity was
      detected with asialo-GM2 or other gangliosides. Monoclonal antibody 5-3 was used 
      to define the expression of GM2 on the cell surface of cultured human normal and 
      malignant cells. Reactivity was seen with cell lines derived from 8 of 8
      astrocytomas, 5 of 5 neuroblastomas, 7 of 9 sarcomas, 4 of 18 human melanomas, 2 
      of 4 murine melanomas, 4 of 37 epithelial cancers and with 0 of 6 skin fibroblast
      and 0 of 2 brain fibroblast lines. GM2, like GD2 and GD3, appears to be a
      differentiation antigen largely restricted to cells of neuroectodermal origin.
FAU - Natoli, E J Jr
AU  - Natoli EJ Jr
FAU - Livingston, P O
AU  - Livingston PO
FAU - Pukel, C S
AU  - Pukel CS
FAU - Lloyd, K O
AU  - Lloyd KO
FAU - Wiegandt, H
AU  - Wiegandt H
FAU - Szalay, J
AU  - Szalay J
FAU - Oettgen, H F
AU  - Oettgen HF
FAU - Old, L J
AU  - Old LJ
LA  - eng
GR  - CA-08748/CA/NCI NIH HHS/United States
GR  - CA-33049/CA/NCI NIH HHS/United States
GR  - CA-36120/CA/NCI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Cancer Res
JT  - Cancer research
JID - 2984705R
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens, Surface)
RN  - 0 (Gangliosides)
RN  - 19600-01-2 (G(M2) Ganglioside)
SB  - IM
MH  - Animals
MH  - Antibodies, Monoclonal/*immunology
MH  - Antigens, Surface/*analysis/immunology
MH  - Cells, Cultured
MH  - Chromatography, Thin Layer
MH  - Enzyme-Linked Immunosorbent Assay
MH  - G(M2) Ganglioside/*analysis
MH  - Gangliosides/*analysis
MH  - Mice
MH  - Mice, Inbred C57BL
EDAT- 1986/08/01 00:00
MHDA- 2001/03/28 10:01
CRDT- 1986/08/01 00:00
PHST- 1986/08/01 00:00 [pubmed]
PHST- 2001/03/28 10:01 [medline]
PHST- 1986/08/01 00:00 [entrez]
PST - ppublish
SO  - Cancer Res. 1986 Aug;46(8):4116-20.

PMID- 8239497
OWN - NLM
STAT- MEDLINE
DCOM- 19931217
LR  - 20181130
IS  - 0250-7005 (Print)
IS  - 0250-7005 (Linking)
VI  - 13
IP  - 5A
DP  - 1993 Sep-Oct
TI  - Different binding properties of three monoclonal antibodies to sialyl Le(x)
      glycolipids in a gastric cancer cell line and normal stomach tissue.
PG  - 1277-82
AB  - We established a mouse monoclonal antibody (Mab) KM93 which recognized sialyl
      Le(x)-carbohydrate epitope determined by solid phase radioimmunoassay using a
      panel of authentic glycolipids. The specificity of KM93 was similar to another
      anti-sialyl Le(x) Mab CSLEX-1 established previously, and different from that of 
      Mab FH6 which recognized sialyl Le(x)-i (sialyl dimeric Le(x)). In a further
      study, however, we found that KM93 reacted with some glycolipids much more
      strongly than CSLEX-1 did on thin-layer chromatography (TLC) plates. We purified 
      two gangliosides named K-1 and K-2 from gastric cancer cell line KATOIII, and
      three gangliosides named H-1, H-2, and H-3 from human stomach. KM93 reacted with 
      all of these glycolipids. CSLEX-1 reacted with K-1 and K-2 with less intensity
      than KM93 did, and faintly reacted with H-1, but not at all with H-2 or H-3. FH6 
      did not react with K-1, K-2 or H-1, while it stained H-2 and H-3. In spite of
      this different reactivity with Mabs, analysis by proton nuclear magnetic
      resonance (1H NMR) proved that carbohydrate structure of K-1 and H-2 were the
      same: NeuAc alpha 2-->3Ga1 beta 1-->4 [Fuc alpha 1-->3] G1cNAc beta 1-->3 Ga1
      beta 1-->4G1c beta 1-->1Cer. The H1 NMR spectrum of H-3 also indicated that H-3
      consisted of the same sugars as K-1. These results indicated that KM93 had wider 
      reactivity than CSLEX-1, and that the distinct reactivity of KM93 from CSLEX-1
      was not caused by sugar moiety. It was also shown that the interaction of sialyl 
      Le(x) sugar determinant with MAb depended on the tissue origin of molecules
      carrying carbohydrate.
FAU - Dohi, T
AU  - Dohi T
AD  - Division of Clinical Biochemistry, National Medical Center, Tokyo, Japan.
FAU - Nemoto, T
AU  - Nemoto T
FAU - Ohta, S
AU  - Ohta S
FAU - Shitara, K
AU  - Shitara K
FAU - Hanai, N
AU  - Hanai N
FAU - Nudelman, E
AU  - Nudelman E
FAU - Hakomori, S
AU  - Hakomori S
FAU - Oshima, M
AU  - Oshima M
LA  - eng
PT  - Journal Article
PL  - Greece
TA  - Anticancer Res
JT  - Anticancer research
JID - 8102988
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens, Neoplasm)
RN  - 0 (Gangliosides)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Antibodies, Monoclonal/*metabolism
MH  - Antibody Specificity
MH  - Antigens, Neoplasm/chemistry/*metabolism
MH  - Chromatography, High Pressure Liquid
MH  - Gangliosides/*metabolism
MH  - Gastric Mucosa/*metabolism
MH  - Humans
MH  - Magnetic Resonance Spectroscopy
MH  - Mice
MH  - Molecular Sequence Data
MH  - Stomach Neoplasms/*metabolism
MH  - Tumor Cells, Cultured
EDAT- 1993/09/01 00:00
MHDA- 1993/09/01 00:01
CRDT- 1993/09/01 00:00
PHST- 1993/09/01 00:00 [pubmed]
PHST- 1993/09/01 00:01 [medline]
PHST- 1993/09/01 00:00 [entrez]
PST - ppublish
SO  - Anticancer Res. 1993 Sep-Oct;13(5A):1277-82.

PMID- 10372971
OWN - NLM
STAT- MEDLINE
DCOM- 19990715
LR  - 20181113
IS  - 0282-0080 (Print)
IS  - 0282-0080 (Linking)
VI  - 15
IP  - 12
DP  - 1998 Dec
TI  - Altered expression of sialylated carbohydrate antigens in HT29 colonic carcinoma 
      cells.
PG  - 1155-63
AB  - To determine whether cell growth conditions impacted carbohydrate expression,
      HT29 cells were gradually transferred from a conventional glucose-containing
      media to a glucose-free galactose containing media. Indirect immunofluorescence
      on acetone fixed cells showed increased expression of sialyl Lewis A antigen
      (CA19-9), sialyl Lewis C (DUPAN2) and Tn/sialyl-Tn on the surface of HT29 cells
      grown in the glucose-free galactose containing media compared to those grown in
      the glucose containing media. Sialyltransferases responsible for the synthesis
      for these sialylated epitopes were Increased in the galactose-fed HT29 cells.
      Media overlying the cells was subjected to isopycnic ultracentrifugation in
      cesium chloride and the fractions derived from both glucose and galactose media
      with equivalent buoyant densities of 1.56 g/L, which are predicted to contain
      mucin glycoforms, were further separated by HPLC using a Mono-Q anion exchange
      column. The chromatograph of eluent from the sample derived from the cells
      growing in the galactose containing media showed an increased peak that reacted
      with the anti-sialyl Lewis A antibody, CA19-9. These results show that alteration
      of in vitro culture conditions may cause HT29 colonic carcinoma cells to alter
      the expression of sialylated carbohydrates.
FAU - Mack, D R
AU  - Mack DR
AD  - Department of Pediatrics, University of Nebraska Medical Center, Omaha 69198,
      USA. drmack@unmc.edu
FAU - Cheng, P W
AU  - Cheng PW
FAU - Perini, F
AU  - Perini F
FAU - Wei, S
AU  - Wei S
FAU - Hollingsworth, M A
AU  - Hollingsworth MA
LA  - eng
GR  - CA57362/CA/NCI NIH HHS/United States
GR  - DK02205/DK/NIDDK NIH HHS/United States
GR  - HL48282/HL/NHLBI NIH HHS/United States
GR  - etc.
PT  - Journal Article
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Glycoconj J
JT  - Glycoconjugate journal
JID - 8603310
RN  - 0 (Antigens, Neoplasm)
RN  - 0 (CA-19-9 Antigen)
RN  - 0 (DU-PAN-2 antigen, human)
RN  - EC 2.4.99.- (Sialyltransferases)
RN  - IY9XDZ35W2 (Glucose)
RN  - X2RN3Q8DNE (Galactose)
SB  - IM
MH  - Adenocarcinoma/*immunology/pathology
MH  - Antigens, Neoplasm/*immunology/isolation & purification
MH  - Blotting, Western
MH  - CA-19-9 Antigen/*immunology/isolation & purification
MH  - Chromatography, High Pressure Liquid
MH  - Chromatography, Ion Exchange
MH  - Colonic Neoplasms/*immunology/pathology
MH  - Fluorescent Antibody Technique, Indirect
MH  - Galactose
MH  - Glucose
MH  - HT29 Cells
MH  - Humans
MH  - Sialyltransferases/metabolism
EDAT- 1999/06/18 00:00
MHDA- 1999/06/18 00:01
CRDT- 1999/06/18 00:00
PHST- 1999/06/18 00:00 [pubmed]
PHST- 1999/06/18 00:01 [medline]
PHST- 1999/06/18 00:00 [entrez]
PST - ppublish
SO  - Glycoconj J. 1998 Dec;15(12):1155-63.

PMID- 3166398
OWN - NLM
STAT- MEDLINE
DCOM- 19881025
LR  - 20071114
IS  - 0008-5472 (Print)
IS  - 0008-5472 (Linking)
VI  - 48
IP  - 19
DP  - 1988 Oct 1
TI  - Expression of blood group-related antigens ABH, Lewis A, Lewis B, Lewis X, Lewis 
      Y, and CA 19-9 in pancreatic cancer cells in comparison with the patient's blood 
      group type.
PG  - 5422-6
AB  - Blood group A, B, H, Le, Leb, Lex, and Ley antigenicity as well as the expression
      of CA 19-9 were examined in pancreatic cancer specimens from 30 patients, using
      monoclonal antibodies to the respective antigen and immunohistochemical
      techniques, and the findings were correlated with the blood group types (ABO and 
      Lewis) of the individuals. Compatible antigen expression was found in 82, 75, and
      50% of tumors from patients with A, B, and O blood group types, respectively.
      Deletion of the compatible antigen was found in 10 (33%) of the cases,
      predominantly in patients of blood group O type, and incompatible expression (of 
      B antigen only) in 4 (13%). Lea was detected in 87%, Leb in 90%, Lex in 30%, and 
      Ley in 43% of the specimens, regardless of ABH and Lewis phenotype of the
      patients. Coexpression of Lea and Leb was found in 87%, of Lex and Ley in 13%, of
      Lea and Lex in 23%, and of Leb and Ley in 40% of the cases. CA 19-9 was expressed
      in 80% of the tumors; it was present in the tumor tissue of 21 of 22 patients
      from Lea-b+, in all 4 individuals from Lea+b-, but in none of the 4 patients from
      Lea-b- phenotype (P less than 0.01). Heterogeneity in the expression of each of
      the antigens was found. The overall results indicate that blood group antigen
      expression in pancreatic tumor differs from that of other gastrointestinal
      cancers and that the Lewis antigen expression in pancreatic cancer cells is
      independent of the blood group phenotype of the patients and thus may be useful
      as a tumor marker.
FAU - Pour, P M
AU  - Pour PM
AD  - Eppley Institute for Research in Cancer and Allied Diseases, University of
      Nebraska Medical Center, Omaha 68105.
FAU - Tempero, M M
AU  - Tempero MM
FAU - Takasaki, H
AU  - Takasaki H
FAU - Uchida, E
AU  - Uchida E
FAU - Takiyama, Y
AU  - Takiyama Y
FAU - Burnett, D A
AU  - Burnett DA
FAU - Steplewski, Z
AU  - Steplewski Z
LA  - eng
GR  - CA36727/CA/NCI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Cancer Res
JT  - Cancer research
JID - 2984705R
RN  - 0 (ABO Blood-Group System)
RN  - 0 (Antigens, Neoplasm)
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Lewis Blood-Group System)
SB  - IM
MH  - ABO Blood-Group System/*immunology
MH  - Adult
MH  - Aged
MH  - Aged, 80 and over
MH  - Antigens, Neoplasm/*immunology
MH  - Antigens, Tumor-Associated, Carbohydrate
MH  - *Blood Grouping and Crossmatching
MH  - Female
MH  - Humans
MH  - Lewis Blood-Group System/*immunology
MH  - Male
MH  - Middle Aged
MH  - Pancreatic Neoplasms/*blood/immunology
MH  - Phenotype
EDAT- 1988/10/01 00:00
MHDA- 1988/10/01 00:01
CRDT- 1988/10/01 00:00
PHST- 1988/10/01 00:00 [pubmed]
PHST- 1988/10/01 00:01 [medline]
PHST- 1988/10/01 00:00 [entrez]
PST - ppublish
SO  - Cancer Res. 1988 Oct 1;48(19):5422-6.

PMID- 19882123
OWN - NLM
STAT- MEDLINE
DCOM- 20100112
LR  - 20141120
IS  - 1940-6029 (Electronic)
IS  - 1064-3745 (Linking)
VI  - 600
DP  - 2010
TI  - In vitro reconstitution of Escherichia coli O86 O antigen repeating unit.
PG  - 93-110
LID - 10.1007/978-1-60761-454-8_7 [doi]
AB  - Polysaccharides constitute a major component of the bacterial cell surface. They 
      play critical roles in the interactions between bacteria and the host
      environments, and consequently contribute to the virulence of pathogens. The
      lipopolysaccharide (LPS) found on the surface of gram-negative bacteria consists 
      of three parts: lipid A, a core oligosaccharide, and the O antigen. The O antigen
      is the outermost part of LPS and contains multiple oligosaccharide repeating
      units. Biosynthesis of the O-repeating unit is the first committed step in LPS
      biosynthesis. We sequenced and characterized the O-antigen biosynthetic gene
      cluster of Escherichia coli serotype O86. Four glycosyltransferases encoded by
      the genes within the cluster were cloned and overexpressed. In vitro
      reconstitution of the O-repeating unit of E. coli 086 was achieved via using
      these enzymes.
FAU - Han, Weiqing
AU  - Han W
AD  - Departments of Chemistry and Biochemistry, The Ohio State University, Columbus,
      OH, USA.
FAU - Li, Lei
AU  - Li L
FAU - Pettit, Nicholas
AU  - Pettit N
FAU - Yi, Wen
AU  - Yi W
FAU - Woodward, Robert
AU  - Woodward R
FAU - Liu, Xianwei
AU  - Liu X
FAU - Guan, Wanyi
AU  - Guan W
FAU - Bhatt, Veer
AU  - Bhatt V
FAU - Song, Jing Katherine
AU  - Song JK
FAU - Wang, Peng George
AU  - Wang PG
LA  - eng
GR  - R01 CA118208/CA/NCI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, N.I.H., Extramural
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, Non-P.H.S.
PL  - United States
TA  - Methods Mol Biol
JT  - Methods in molecular biology (Clifton, N.J.)
JID - 9214969
RN  - 0 (Antigens, Bacterial)
RN  - 0 (DNA, Bacterial)
RN  - 0 (Lipids)
RN  - 0 (Lipopolysaccharides)
RN  - 0 (O Antigens)
RN  - EC 2.4.- (Glycosyltransferases)
SB  - IM
MH  - Antigens, Bacterial/*chemistry
MH  - Biochemistry/methods
MH  - Carbohydrate Sequence
MH  - Cloning, Molecular
MH  - DNA, Bacterial/genetics
MH  - Escherichia coli/*metabolism
MH  - Genes, Bacterial
MH  - Glycosyltransferases/chemistry
MH  - In Vitro Techniques
MH  - Lipids/chemistry
MH  - Lipopolysaccharides/chemistry
MH  - Molecular Biology/*methods
MH  - Molecular Sequence Data
MH  - Multigene Family
MH  - O Antigens/*metabolism
EDAT- 2009/11/03 06:00
MHDA- 2010/01/13 06:00
CRDT- 2009/11/03 06:00
PHST- 2009/11/03 06:00 [entrez]
PHST- 2009/11/03 06:00 [pubmed]
PHST- 2010/01/13 06:00 [medline]
AID - 10.1007/978-1-60761-454-8_7 [doi]
PST - ppublish
SO  - Methods Mol Biol. 2010;600:93-110. doi: 10.1007/978-1-60761-454-8_7.

PMID- 2186036
OWN - NLM
STAT- MEDLINE
DCOM- 19900613
LR  - 20061115
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 265
IP  - 14
DP  - 1990 May 15
TI  - Isolation and characterization of extremely minor gangliosides, GM1b and GD1
      alpha, in adult bovine brains as developmentally regulated antigens.
PG  - 8144-51
AB  - In addition to ganglioside GM1b, an unusual and extremely minor ganglioside, GD1 
      alpha, was efficiently isolated from bovine brain by combination of Q-Sepharose
      and Iatrobeads column chromatographies. In the course of purification steps, the 
      presence of the sialidase-labile ganglioside was proved by a highly sensitive
      TLC/enzyme-immunostaining method. The structure was characterized by gas-liquid
      chromatography, permethylation study, sialidase degradation, immunostaining with 
      specific antibodies, fast atom bombardment-mass spectrometry, and proton magnetic
      resonance spectrometry. The content of the ganglioside was very small (0.016%) in
      the total gangliosides. This finding suggests that a synthetic pathway of asialo 
      GM1----GM1b----GD1 alpha may exist in mammalian brains. A monoclonal antibody
      NA-6 that was obtained by immunizing mice with purified GM1b reacted specifically
      with GM1b but showed no cross-reactivity with other structurally related
      gangliosides such as GM1a, GD1a, and so on. Using the method of
      TLC/immunostaining with NA-6, GM1b was found to be strongly expressed during
      embryonic days 14-17 in chick brains. Thus, it is assumed that extremely minor
      gangliosides like GM1b and GD1 alpha found in adult brains are characterized as
      embryonic molecules.
FAU - Hirabayashi, Y
AU  - Hirabayashi Y
AD  - Department of Biochemistry, University of Shizuoka, School of Pharmaceutical
      Sciences, Japan.
FAU - Hyogo, A
AU  - Hyogo A
FAU - Nakao, T
AU  - Nakao T
FAU - Tsuchiya, K
AU  - Tsuchiya K
FAU - Suzuki, Y
AU  - Suzuki Y
FAU - Matsumoto, M
AU  - Matsumoto M
FAU - Kon, K
AU  - Kon K
FAU - Ando, S
AU  - Ando S
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 101839-44-5 (ganglioside GD1alpha)
RN  - 37758-47-7 (G(M1) Ganglioside)
RN  - 57576-20-2 (ganglioside M1b)
SB  - IM
MH  - Animals
MH  - Brain/embryology/*growth & development
MH  - *Brain Chemistry
MH  - Carbohydrate Conformation
MH  - Carbohydrate Sequence
MH  - Chick Embryo
MH  - Chromatography
MH  - Chromatography, Thin Layer
MH  - G(M1) Ganglioside/*analogs & derivatives/isolation & purification
MH  - Humans
MH  - Immunoenzyme Techniques
MH  - Infant, Newborn
MH  - Magnetic Resonance Spectroscopy
MH  - Mass Spectrometry
MH  - Molecular Sequence Data
MH  - Molecular Structure
EDAT- 1990/05/15 00:00
MHDA- 1990/05/15 00:01
CRDT- 1990/05/15 00:00
PHST- 1990/05/15 00:00 [pubmed]
PHST- 1990/05/15 00:01 [medline]
PHST- 1990/05/15 00:00 [entrez]
PST - ppublish
SO  - J Biol Chem. 1990 May 15;265(14):8144-51.

PMID- 3019521
OWN - NLM
STAT- MEDLINE
DCOM- 19861107
LR  - 20071114
IS  - 0008-5472 (Print)
IS  - 0008-5472 (Linking)
VI  - 46
IP  - 10
DP  - 1986 Oct
TI  - Biosynthesis and expression of the disialoganglioside GD2, a relevant target
      antigen on small cell lung carcinoma for monoclonal antibody-mediated cytolysis.
PG  - 5112-8
AB  - Monoclonal antibodies (MAbs) 126 (immunoglobulin M) and 14.18 (immunoglobulin G3)
      react strongly with the cell surface of small cell carcinoma of the lungs (SCCL) 
      and are unreactive with most normal tissues and other neoplasms with the notable 
      exception of tumors derived from cells of neural crest origin. These MAbs react
      specifically with the oligosaccharide portion of the disialoganglioside GD2.
      Analysis of total gangliosides from cultured cell lines derived from SCCL
      indicates that GD2 is a predominant ganglioside. A comparison of the reactivities
      of MAbs against GD2 with those directed against gangliosides GM2 and GD3, each
      differing from GD2 by a single sugar residue, clearly indicates that GD2 is
      preferentially expressed by cultured cells derived from SCCL. Membranes isolated 
      from these cells exhibit GD2 synthetase activity which specifically converts the 
      precursor GD3 to GD2 in the presence of uridine diphosphate-N-acetyl
      galactosamine as the glycosyl donor. We present evidence that in SCCL, GD2 serves
      as a relevant target antigen for monoclonal antibody-mediated cytolysis.
      Specifically, we demonstrate that MAb 14.18 (immunoglobulin G3), can lyse small
      cell carcinoma of the lung targets by either complement- or antibody-dependent
      cellular cytotoxicity.
FAU - Cheresh, D A
AU  - Cheresh DA
FAU - Rosenberg, J
AU  - Rosenberg J
FAU - Mujoo, K
AU  - Mujoo K
FAU - Hirschowitz, L
AU  - Hirschowitz L
FAU - Reisfeld, R A
AU  - Reisfeld RA
LA  - eng
GR  - CA 28420/CA/NCI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Cancer Res
JT  - Cancer research
JID - 2984705R
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens, Neoplasm)
RN  - 0 (Gangliosides)
RN  - 9007-36-7 (Complement System Proteins)
SB  - IM
MH  - Antibodies, Monoclonal/*immunology/therapeutic use
MH  - Antibody-Dependent Cell Cytotoxicity
MH  - Antigens, Neoplasm/*analysis
MH  - Carcinoma, Small Cell/immunology/*metabolism
MH  - Cell Line
MH  - Complement System Proteins/immunology
MH  - *Cytotoxicity, Immunologic
MH  - Gangliosides/analysis/*biosynthesis/immunology
MH  - Humans
MH  - Immunotherapy
MH  - Lung Neoplasms/immunology/*metabolism
EDAT- 1986/10/01 00:00
MHDA- 1986/10/01 00:01
CRDT- 1986/10/01 00:00
PHST- 1986/10/01 00:00 [pubmed]
PHST- 1986/10/01 00:01 [medline]
PHST- 1986/10/01 00:00 [entrez]
PST - ppublish
SO  - Cancer Res. 1986 Oct;46(10):5112-8.

PMID- 12820722
OWN - NLM
STAT- MEDLINE
DCOM- 20030811
LR  - 20181113
IS  - 0282-0080 (Print)
IS  - 0282-0080 (Linking)
VI  - 18
IP  - 11-12
DP  - 2001 Nov-Dec
TI  - Expression of sialyl-Tn antigen in breast cancer cells transfected with the human
      CMP-Neu5Ac: GalNAc alpha2,6-sialyltransferase (ST6GalNac I) cDNA.
PG  - 883-93
AB  - Sialyl-Tn antigen (STn) is a cancer associated carbohydrate antigen
      over-expressed in several cancers including breast cancer, and currently
      associated with more aggressive diseases and poor prognosis. However, the
      commonly used breast cancer cell lines (MDA-MB-231, T47-D and MCF7) do not
      express STn antigen. The key step in the biosynthesis of STn is the transfer of a
      sialic acid residue in alpha2,6-linkage to GalNAc alpha-O-Ser/Thr. This reaction 
      is mainly catalyzed by a CMP-Neu5Ac GalNAc alpha2,6-sialyltransferase: ST6GalNAc 
      I. In order to generate STn-positive breast cancer cells, we have cloned a cDNA
      encoding the full-length human ST6GalNAc I from HT-29-MTX cells. The stable
      transfection of MDA-MB-231 with an expression vector encoding ST6GalNAc I induces
      the expression of STn antigen at the cell surface. The expression of STn short
      cuts the initial O-glycosylation pattern of these cell lines, by competing with
      the Core-1 beta1,3-galactosyltransferase, the first enzyme involved in the
      elongation of O-glycan chains. Moreover, we show that STn expression is
      associated with morphological changes, decreased growth and increased migration
      of MDA-MB-231 cells.
FAU - Julien, S
AU  - Julien S
AD  - Unite de Glycobiologie Structurale et Fonctionnelle, UMR CNRS no 8576,
      Laboratoire de Chimie Biologique, Universite des Sciences et Technologies de
      Lille, F-59655 Villeneuve d'Ascq, France.
FAU - Krzewinski-Recchi, M A
AU  - Krzewinski-Recchi MA
FAU - Harduin-Lepers, A
AU  - Harduin-Lepers A
FAU - Gouyer, V
AU  - Gouyer V
FAU - Huet, G
AU  - Huet G
FAU - Le Bourhis, X
AU  - Le Bourhis X
FAU - Delannoy, P
AU  - Delannoy P
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Glycoconj J
JT  - Glycoconjugate journal
JID - 8603310
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Biomarkers, Tumor)
RN  - 0 (DNA, Complementary)
RN  - 0 (Tn antigen)
RN  - 0 (sialosyl-Tn antigen)
RN  - EC 2.4.1.- (Galactosyltransferases)
RN  - EC 2.4.1.122 (glycoprotein-N-acetylgalactosamine 3-beta-galactosyltransferase)
RN  - EC 2.4.99.- (Sialyltransferases)
RN  - EC 2.4.99.3 (CMP-N-acetylneuraminate-alpha-N-acetylgalactosaminide
      alpha-2,6-sialyltransferase)
SB  - IM
MH  - Antigens, Tumor-Associated, Carbohydrate/chemistry/*metabolism
MH  - Biomarkers, Tumor
MH  - Breast Neoplasms/genetics/*immunology/*metabolism/pathology
MH  - Carbohydrate Conformation
MH  - Carbohydrate Sequence
MH  - Cell Membrane/immunology/metabolism
MH  - Cell Movement
MH  - Cloning, Molecular
MH  - Colonic Neoplasms/enzymology/genetics
MH  - DNA, Complementary/genetics
MH  - Female
MH  - Galactosyltransferases/metabolism
MH  - Glycosylation
MH  - Humans
MH  - Molecular Sequence Data
MH  - Reverse Transcriptase Polymerase Chain Reaction
MH  - Sialyltransferases/*genetics/metabolism
MH  - Transfection
MH  - Tumor Cells, Cultured
EDAT- 2003/06/25 05:00
MHDA- 2003/08/12 05:00
CRDT- 2003/06/25 05:00
PHST- 2003/06/25 05:00 [pubmed]
PHST- 2003/08/12 05:00 [medline]
PHST- 2003/06/25 05:00 [entrez]
PST - ppublish
SO  - Glycoconj J. 2001 Nov-Dec;18(11-12):883-93.

PMID- 12820721
OWN - NLM
STAT- MEDLINE
DCOM- 20030811
LR  - 20181113
IS  - 0282-0080 (Print)
IS  - 0282-0080 (Linking)
VI  - 18
IP  - 11-12
DP  - 2001 Nov-Dec
TI  - A rat model to study the role of STn antigen in colon cancer.
PG  - 871-82
AB  - Expression of the mucin-associated sialyl-Tn (STn) antigen has been associated
      with a decreased survival in patients with colorectal, gastric, and ovarian
      cancer. To better understand the role of STn antigen in tumor biology, we
      developed STn(+) (called LP) and STn(-) (called LN) clonal cell lines from a
      parental metastatic rat colon carcinoma cell line (LMCR). Both derivative cell
      lines exhibited identical proliferation rates in vitro. LP cells strongly
      expressed STn antigen both in vitro and in vivo, and were poorly tumorigenic when
      given to syngeneic rats. LN cells did not express STn antigen in vitro, but as in
      vivo tumors these cells rapidly acquired STn expression, readily formed tumors,
      and were highly lethal. When rats were given an otherwise lethal inoculum of i.p.
      LN cells, pre-immunization with synthetic STn antigen conjugated to keyhole
      limpet hemocyanin (STn-KLH) resulted in a 60% survival rate. When LN cells were
      injected subcutaneously in the presence of STn-KLH-sensitized lymphocytes, tumor 
      growth was decreased. Distribution of STn antigen in normal organs of host rats
      is quite similar to that of humans. This model mimics human disease and should
      facilitate studies of mucin-associated antigens in tumor biology and the
      development of immunotherapeutic agents based on mucin-related antigens.
FAU - Ogata, S
AU  - Ogata S
AD  - Gastrointestinal Research Laboratory, Department of Medicine, Mount Sinai School 
      of Medicine, NY, NY 10029, USA.
FAU - Ho, I
AU  - Ho I
FAU - Maklansky, J
AU  - Maklansky J
FAU - Chen, A
AU  - Chen A
FAU - Werther, J L
AU  - Werther JL
FAU - Reddish, M
AU  - Reddish M
FAU - Longenecker, B M
AU  - Longenecker BM
FAU - Sigurdson, E
AU  - Sigurdson E
FAU - Iishi, S
AU  - Iishi S
FAU - Zhang, J Y
AU  - Zhang JY
FAU - Itzkowitz, S H
AU  - Itzkowitz SH
LA  - eng
GR  - CA81363/CA/NCI NIH HHS/United States
GR  - R01 CA52491/CA/NCI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Glycoconj J
JT  - Glycoconjugate journal
JID - 8603310
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Cancer Vaccines)
RN  - 0 (Glycoconjugates)
RN  - 0 (Tn antigen)
RN  - 0 (sialosyl-Tn antigen)
RN  - 0 (sialyl-Tn antigen-keyhole-limpet hemocyanin conjugate)
RN  - 9013-72-3 (Hemocyanins)
SB  - IM
MH  - Animals
MH  - Antibody Formation
MH  - Antigens, Tumor-Associated, Carbohydrate/genetics/*immunology/*metabolism
MH  - Cancer Vaccines
MH  - Cell Division/physiology
MH  - Colonic Neoplasms/*immunology/pathology/therapy
MH  - Disease Models, Animal
MH  - Glycoconjugates
MH  - Hemocyanins/immunology
MH  - Immunotherapy/methods
MH  - Injections, Intraperitoneal
MH  - Neoplasm Transplantation
MH  - Rats
MH  - Rats, Inbred Strains
MH  - Survival Rate
MH  - Tissue Distribution
MH  - Tumor Cells, Cultured
EDAT- 2003/06/25 05:00
MHDA- 2003/08/12 05:00
CRDT- 2003/06/25 05:00
PHST- 2003/06/25 05:00 [pubmed]
PHST- 2003/08/12 05:00 [medline]
PHST- 2003/06/25 05:00 [entrez]
PST - ppublish
SO  - Glycoconj J. 2001 Nov-Dec;18(11-12):871-82.

PMID- 12820726
OWN - NLM
STAT- MEDLINE
DCOM- 20030811
LR  - 20181113
IS  - 0282-0080 (Print)
IS  - 0282-0080 (Linking)
VI  - 18
IP  - 11-12
DP  - 2001 Nov-Dec
TI  - Tumor cell MUC1 and CD43 are glycosylated differently with sialyl-Lewis a and x
      epitopes and show variable interactions with E-selectin under physiological flow 
      conditions.
PG  - 925-30
AB  - The mucins secreted from the colon carcinoma cell line COLO 205 have the MUC1 and
      CD43 (leukosialin) as core proteins, where both carry sialyl-Lewis a and MUC1
      sialyl-Lewis x epitopes. The adhesion of E-selectin expressing CHO cells to the
      coated mucins was analyzed in a flow system revealing that the MUC1 mucin adhered
      better than the CD43 mucin. One reason could be their different glycosylation, a 
      difference that was explored by analyzing the biosynthesis of MUC1 and CD43 in
      COLO 205 cells. Both the MUC1 and CD43 mucins became sialyl-Lewis a reactive, but
      after different times as revealed by pulse-chase studies. However, only MUC1
      became sialyl-Lewis x reactive. These differences suggest that MUC1 and CD43 are 
      synthesized in different compartments of the cell. It was also observed that the 
      mucins from colon carcinoma patients had MUC1-type mucins that carried both
      sialyl-Lewis a and x epitopes and CD43-type sialyl-Lewis a mucins with only low
      levels of sialyl-Lewis x epitopes. One could hypothesize that colon carcinoma
      derived MUC1 is decorated with potent E-selectin epitopes, and that this could be
      one of several reasons for the involvement of MUC1 in cancer development.
FAU - Fernandez-Rodriguez, J
AU  - Fernandez-Rodriguez J
AD  - Department of Medical Biochemistry, Goteborg University, Box 440, 405 30
      Gothenburg, Sweden.
FAU - Dwir, O
AU  - Dwir O
FAU - Alon, R
AU  - Alon R
FAU - Hansson, G C
AU  - Hansson GC
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Glycoconj J
JT  - Glycoconjugate journal
JID - 8603310
RN  - 0
      (5-acetylneuraminyl-(2-3)-galactosyl-(1-4)-(fucopyranosyl-(1-3))-N-acetylglucosam
      ine)
RN  - 0 (Antigens, CD)
RN  - 0 (E-Selectin)
RN  - 0 (Epitopes)
RN  - 0 (Gangliosides)
RN  - 0 (Leukosialin)
RN  - 0 (Mucin-1)
RN  - 0 (Oligosaccharides)
RN  - 0 (Sialoglycoproteins)
RN  - 0 (UN1 sialoglycoprotein, human)
RN  - 91847-18-6 (sialyl Le(a) ganglioside)
SB  - IM
MH  - Adenocarcinoma/*immunology/metabolism
MH  - Animals
MH  - *Antigens, CD
MH  - CHO Cells/metabolism
MH  - Carbohydrate Sequence
MH  - Cell Adhesion/physiology
MH  - Colonic Neoplasms/*immunology/metabolism
MH  - Cricetinae
MH  - E-Selectin/genetics/*metabolism
MH  - Epitopes/*metabolism
MH  - Gangliosides/*immunology
MH  - Glycosylation
MH  - HL-60 Cells/pathology
MH  - Humans
MH  - Leukosialin
MH  - Molecular Sequence Data
MH  - Mucin-1/immunology/*metabolism
MH  - Oligosaccharides/*immunology
MH  - Rabbits
MH  - Sialoglycoproteins/immunology/*metabolism
MH  - Stress, Mechanical
MH  - Tumor Cells, Cultured
EDAT- 2003/06/25 05:00
MHDA- 2003/08/12 05:00
CRDT- 2003/06/25 05:00
PHST- 2003/06/25 05:00 [pubmed]
PHST- 2003/08/12 05:00 [medline]
PHST- 2003/06/25 05:00 [entrez]
PST - ppublish
SO  - Glycoconj J. 2001 Nov-Dec;18(11-12):925-30.

PMID- 10952412
OWN - NLM
STAT- MEDLINE
DCOM- 20001207
LR  - 20151119
IS  - 0272-457X (Print)
IS  - 0272-457X (Linking)
VI  - 19
IP  - 3
DP  - 2000 Jun
TI  - A mouse IgG1 monoclonal antibody specific for N-glycolyl GM3 ganglioside
      recognized breast and melanoma tumors.
PG  - 241-7
AB  - 14F7 murine monoclonal antibody (MAb) is an IgG1 immunoglobulin that is generated
      by immunizing Balb/c mice with GM3(NeuGc) ganglioside hydrophobically conjugated 
      with human very-low-density lipoproteins and in the presence of Freund's
      adjuvants. 14F7 MAb binds specifically to GM3(NeuGc), whereas neither N-glycolyl 
      or N-acetyl gangliosides, nor a sulfated glycolipid, are recognized as assessed
      by enzyme-linked immunosorbent assay or immunostaining on thin layer
      chromatograms. Immunohistochemical studies in fresh tumor tissues showed that
      14F7 MAb strongly recognized in antigen expressed in human breast and melanoma
      tumors.
FAU - Carr, A
AU  - Carr A
AD  - Center of Molecular Immunology, Havana, Cuba. adriana@ict.cim.sld.cu
FAU - Mullet, A
AU  - Mullet A
FAU - Mazorra, Z
AU  - Mazorra Z
FAU - Vazquez, A M
AU  - Vazquez AM
FAU - Alfonso, M
AU  - Alfonso M
FAU - Mesa, C
AU  - Mesa C
FAU - Rengifo, E
AU  - Rengifo E
FAU - Perez, R
AU  - Perez R
FAU - Fernandez, L E
AU  - Fernandez LE
LA  - eng
PT  - Journal Article
PL  - United States
TA  - Hybridoma
JT  - Hybridoma
JID - 8202424
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Biomarkers, Tumor)
RN  - 0 (Cholesterol, VLDL)
RN  - 0 (G(M3) Ganglioside)
RN  - 0 (Glycolipids)
RN  - 0 (Immunoglobulin G)
RN  - 115082-64-9 (de-N-acetylneuraminyllactosylceramide)
RN  - 69345-49-9 (N-glycolylneuraminyllactosylceramide)
SB  - IM
MH  - Animals
MH  - Antibodies, Monoclonal/*chemistry
MH  - *Antibody Specificity
MH  - Biomarkers, Tumor/*immunology
MH  - Breast Neoplasms/chemistry/*immunology
MH  - Cholesterol, VLDL/immunology/metabolism
MH  - Female
MH  - G(M3) Ganglioside/*analogs & derivatives/*immunology/metabolism
MH  - Glycolipids/immunology
MH  - Humans
MH  - Immunoglobulin G/chemistry/*metabolism
MH  - Melanoma/chemistry/*immunology
MH  - Mice
MH  - Mice, Inbred BALB C
MH  - Organ Specificity
EDAT- 2000/08/22 11:00
MHDA- 2001/02/28 10:01
CRDT- 2000/08/22 11:00
PHST- 2000/08/22 11:00 [pubmed]
PHST- 2001/02/28 10:01 [medline]
PHST- 2000/08/22 11:00 [entrez]
AID - 10.1089/02724570050109639 [doi]
PST - ppublish
SO  - Hybridoma. 2000 Jun;19(3):241-7. doi: 10.1089/02724570050109639.

PMID- 2400995
OWN - NLM
STAT- MEDLINE
DCOM- 19901019
LR  - 20151119
IS  - 0008-5472 (Print)
IS  - 0008-5472 (Linking)
VI  - 50
IP  - 19
DP  - 1990 Oct 1
TI  - Tumor-associated antigens common to humans and chemically induced colonic tumors 
      of the rat.
PG  - 6358-63
AB  - The expression of human tumor-associated antigens CO17-1A, GA73-3, BR55-2, GICA
      19-9, and CA50 and of carcinoembryonic antigen was immunohistochemically studied 
      in the colonic mucosa of 70 Sprague-Dawley rats. Fifty were treated with
      1,2-dimethylhydrazine (DMH) (with EDTA as a vehicle), ten were treated with EDTA 
      only, and ten were untreated normal rats. The tumors were histogenetically
      divided as: (a) adenocarcinomas arising from villous adenomas; (b)
      adenocarcinomas arising from lymphoid-associated mucosa (LAM); and (c)
      adenocarcinomas arising in flat mucosa. Of 44 colonic adenocarcinomas, BR55-2 was
      expressed in 41 tumors, CO17-1A in 40 tumors, GA73-3 in 38 tumors, and GICA 19-9 
      in 38 tumors. CA50 and carcinoembryonic antigen were not expressed in the tumors.
      The highest antigenic expression (number of cells) was observed in
      adenocarcinomas arising in villous adenomas and the lowest in those arising in
      flat mucosa. Adenocarcinomas arising in LAM had an intermediate expression. The
      expression of these antigens had no correlation to the localization of the tumor 
      and to the differentiation. The expression of these antigens was similar in the
      non-lymphoid-associated normal colonic mucosa of the untreated, EDTA-treated, and
      DMH-treated rats. In DMH-treated rats, LAM demonstrated increased expression
      (number of cells) and increased staining intensity of these tumor-associated
      antigens. In six of the 50 DMH-treated rats, only LAM expressed carcinoembryonic 
      antigen. CA50 was not expressed in the normal colon of untreated, of
      EDTA-treated, and of DMH-treated rats, nor was it in DMH-induced tumors. None of 
      the tumor-associated antigens (GICA 19-9 and CA50 and carcinoembryonic antigen)
      was detected in serum. It is concluded that this animal model would be of value
      in the preclinical evaluations of monoclonal antibodies for therapy in humans.
FAU - Shetye, J D
AU  - Shetye JD
AD  - Department of Pathology, Karolinska Hospital, Stockholm, Sweden.
FAU - Rubio, C A
AU  - Rubio CA
FAU - Harmenberg, U
AU  - Harmenberg U
FAU - Ware, J
AU  - Ware J
FAU - Duvander, A
AU  - Duvander A
FAU - Mellstedt, H T
AU  - Mellstedt HT
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Cancer Res
JT  - Cancer research
JID - 2984705R
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Biomarkers, Tumor)
SB  - IM
MH  - Adenocarcinoma/*immunology/pathology
MH  - Animals
MH  - Antigens, Tumor-Associated, Carbohydrate/*analysis
MH  - Biomarkers, Tumor/*analysis
MH  - Colonic Neoplasms/*immunology/pathology
MH  - Humans
MH  - Intestinal Mucosa/analysis
MH  - Male
MH  - Rats
MH  - Rats, Inbred Strains
EDAT- 1990/10/01 00:00
MHDA- 1990/10/01 00:01
CRDT- 1990/10/01 00:00
PHST- 1990/10/01 00:00 [pubmed]
PHST- 1990/10/01 00:01 [medline]
PHST- 1990/10/01 00:00 [entrez]
PST - ppublish
SO  - Cancer Res. 1990 Oct 1;50(19):6358-63.

PMID- 7287720
OWN - NLM
STAT- MEDLINE
DCOM- 19811215
LR  - 20061115
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 256
IP  - 20
DP  - 1981 Oct 25
TI  - The carbohydrate moiety of band 3 glycoprotein of human erythrocyte membranes.
      Structures of lower molecular weight oligosaccharides.
PG  - 10497-502
AB  - Band 3 glycoprotein purified from human blood group A erythrocyte membranes was
      subjected to hydrazinolysis to release carbohydrate moieties. The neutral
      oligosaccharide fraction, which constituted more than 85% of the total
      carbohydrates released, was fractionated by gel chromatography on a column of
      Sephadex G-50 into two fractions, i.e. higher molecular weight and lower
      molecular weight fractions. From the lower molecular weight fraction, three
      oligosaccharides were obtained by chromatographies on columns of Bio-Gel P-4,
      concanavalin A-Sepharose, and lentil lectin-Sepharose. Their structures were
      investigated by a combination of compositional analyses, glycosidase treatments, 
      methylation and Smith periodate degradation, and proposed to be: Gal beta 1 -
      4GlcNAc beta 1 - 2Man alpha 1 - 6(GlcNAc beta 1 -4) (Gal beta 1 - 4GlcNAc beta 1 
      - 2Man alpha 1 - 3)Man beta 1 - 4GlcNAc beta 1 - 4(Fuc alpha 1 - 6)GlcNAc, Gal
      beta 1 - 4GlcNAc beta 1 - 2Man alpha 1 - 6(Gal beta 1 - 4GlcNAc beta 1 - 2Man
      alpha 1 - 3)Man beta 1 - 4GlcNAc beta 1 - 4(Fuc alpha 1 - 6)GlcNAc, and GlcNAc
      beta 1 - 2Man alpha 1 - 6(GlcNAc beta 1 - 4) (Glc NAc beta 1 - 2Man alpha 1-3)
      Man beta 1 - 4GlcNAc beta 1 - 4(+/-Fuc alpha 1 - 6)GlcNAc. It was also
      demonstrated in this study that most of the higher molecular weight
      oligosaccharides, whose peripheral structure had previously been reported (Tsuji,
      T., Irimura, T., and Osawa, T. (1980) Biochem. J. 187, 677-686), also contained
      the same core hexasaccharide structure, Man alpha 1 - 6(Man alpha 1-3)Man beta 1 
      - 4GlcNAc beta 1 - 4(Fuc alpha 1-6)GlcNAc, as that of the lower molecular weight 
      oligosaccharides.
FAU - Tsuji, T
AU  - Tsuji T
FAU - Irimura, T
AU  - Irimura T
FAU - Osawa, T
AU  - Osawa T
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Anion Exchange Protein 1, Erythrocyte)
RN  - 0 (Blood Proteins)
RN  - 0 (Membrane Proteins)
RN  - 0 (Oligosaccharides)
RN  - EC 3.2.1.- (Glycoside Hydrolases)
SB  - IM
MH  - Anion Exchange Protein 1, Erythrocyte
MH  - *Blood Proteins/isolation & purification
MH  - Carbohydrate Conformation
MH  - Carbohydrate Sequence
MH  - Erythrocyte Membrane/*analysis
MH  - Erythrocytes/*analysis
MH  - Glycoside Hydrolases
MH  - Humans
MH  - *Membrane Proteins/isolation & purification
MH  - Methylation
MH  - Oligosaccharides/*blood
EDAT- 1981/10/25 00:00
MHDA- 1981/10/25 00:01
CRDT- 1981/10/25 00:00
PHST- 1981/10/25 00:00 [pubmed]
PHST- 1981/10/25 00:01 [medline]
PHST- 1981/10/25 00:00 [entrez]
PST - ppublish
SO  - J Biol Chem. 1981 Oct 25;256(20):10497-502.

PMID- 2335739
OWN - NLM
STAT- MEDLINE
DCOM- 19900613
LR  - 20181130
IS  - 0022-1554 (Print)
IS  - 0022-1554 (Linking)
VI  - 38
IP  - 6
DP  - 1990 Jun
TI  - Expression patterns of the T antigen and the cryptic T antigen in rat fetuses:
      detection with the lectin amaranthin.
PG  - 763-74
AB  - The lectin amaranthin, purified from the seeds of Amaranthus caudatus, has been
      shown to react specifically with the Gal beta 1,3GalNAc-alpha and the NeuAc alpha
      2,3Gal beta 1,3GalNAc-alpha sequence which represent the T antigen and the
      cryptic T antigen, respectively. We report here the development of labeling
      techniques that apply amaranthin to stain paraffin sections from rat fetuses.
      Amaranthin staining was inhibited by pre-incubation of lectin-gold complexes with
      10 mM Gal beta 1,3GalNAc-alpha-O-benzyl (synthetic T antigen) or 10 mM Gal beta
      1,3GalNAc-alpha-O-aminophenylethyl-human serum albumin (T antigen
      neoglycoprotein), asialoglycophorin, asialofetuin, and asialomucin. The
      beta-elimination reaction also abolished the lectin staining demonstrating
      specificity for O-glycosidically linked structures. A comparison with monoclonal 
      anti-T antigen antibody immunostaining demonstrated that amaranthin detects the T
      antigen and its cryptic form in tissue sections. Application of the galactose
      oxidase-Schiff sequence abolished amaranthin (and anti-T antibody) binding to the
      T antigen but not to its cryptic form, and therefore permitted their
      differentiation in tissue sections. Histochemical evidence was obtained
      indicating that amaranthin is a more specific anti-T reagent than peanut lectin. 
      Data are presented that show the differential expression of the T antigen and the
      cryptic T antigen in organs and cells of rat fetuses late in gestation.
      Therefore, amaranthin can be used for histochemical detection of the T antigen
      and the cryptic T antigen, and facilitates discrimination between them.
FAU - Sata, T
AU  - Sata T
AD  - Biocenter, University of Basel, Switzerland.
FAU - Zuber, C
AU  - Zuber C
FAU - Rinderle, S J
AU  - Rinderle SJ
FAU - Goldstein, I J
AU  - Goldstein IJ
FAU - Roth, J
AU  - Roth J
LA  - eng
GR  - GM29470/GM/NIGMS NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - J Histochem Cytochem
JT  - The journal of histochemistry and cytochemistry : official journal of the
      Histochemistry Society
JID - 9815334
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Asialoglycoproteins)
RN  - 0 (Disaccharides)
RN  - 0 (Isoantigens)
RN  - 0 (Lectins)
RN  - 0 (Peanut Agglutinin)
RN  - 0 (Plant Lectins)
RN  - 0 (Ribosome Inactivating Proteins, Type 1)
RN  - 0 (Thomsen-Friedenreich antigen, cryptic)
RN  - 0 (Trisaccharides)
RN  - 0 (amaranthin protein, Amaranthus)
RN  - 0 (asialoglycophorin)
RN  - 3554-90-3 (Thomsen-Friedenreich antigen)
RN  - 7440-57-5 (Gold)
RN  - EC 3.2.2.22 (Ribosome Inactivating Proteins)
SB  - IM
MH  - Animals
MH  - Antibodies, Monoclonal
MH  - *Antigens, Tumor-Associated, Carbohydrate
MH  - Asialoglycoproteins
MH  - Carbohydrate Sequence
MH  - Disaccharides/*analysis
MH  - Fetus/*analysis/ultrastructure
MH  - Gold
MH  - Histocytochemistry
MH  - Isoantigens/*analysis
MH  - *Lectins
MH  - Molecular Sequence Data
MH  - Organ Specificity
MH  - Peanut Agglutinin
MH  - *Plant Lectins
MH  - Rats
MH  - Ribosome Inactivating Proteins
MH  - Ribosome Inactivating Proteins, Type 1
MH  - Trisaccharides/*analysis
EDAT- 1990/06/01 00:00
MHDA- 1990/06/01 00:01
CRDT- 1990/06/01 00:00
PHST- 1990/06/01 00:00 [pubmed]
PHST- 1990/06/01 00:01 [medline]
PHST- 1990/06/01 00:00 [entrez]
AID - 10.1177/38.6.2335739 [doi]
PST - ppublish
SO  - J Histochem Cytochem. 1990 Jun;38(6):763-74. doi: 10.1177/38.6.2335739.

PMID- 9815586
OWN - NLM
STAT- MEDLINE
DCOM- 19990225
LR  - 20171116
IS  - 1078-0432 (Print)
IS  - 1078-0432 (Linking)
VI  - 3
IP  - 11
DP  - 1997 Nov
TI  - Preclinical evaluation in nonhuman primates of murine monoclonal anti-idiotype
      antibody that mimics the disialoganglioside GD2.
PG  - 1969-76
AB  - The antiganglioside GD2 monoclonal antibody 14G2a (Ab1) served as an immunogen to
      generate the anti-idiotype (anti-Id) 1A7 (IgG1,kappa), which mimics GD2 both
      antigenically and biologically. Anti-Id 1A7 induced anti-GD2 antibodies in mice
      and rabbits. In this preclinical study, a pair of cynomolgus monkeys, immunized
      with 1A7 that had been mixed with QS-21 adjuvant, produced anti-anti-Id
      antibodies (Ab3), which reacted with the GD2-positive melanoma cell line M21/P6
      cells but not with GD2-negative LS174-T cells. The Ab3 shared Ids with mAb 14G2a 
      (Ab1), as demonstrated by their ability to inhibit binding of 1A7 to this Ab1.
      The Ab3 bound specifically to purified GD2 antigen and competed with the Ab1
      14G2a in binding to a GD2-positive melanoma cell line or to purified GD2,
      suggesting that Ab1 and Ab3 may bind to the same epitope and may behave as an
      Ab1-like antibody (Ab1'). The isotype of the GD2-specific antibodies was mostly
      IgG in nature. The specificity of the antibodies for GD2 was further confirmed by
      dot blot analysis. These antisera also specifically lysed GD2-positive target
      cells in an antibody-dependent cellular cytotoxicity assay. The induction of
      anti-GD2 responses in monkeys did not cause any apparent side effects, despite
      the fact that GD2 antigen is expressed by many normal tissues of these animals.
      Taken together, these results suggest that anti-Id 1A7 can induce GD2-specific
      antibodies in nonhuman primates and can thus serve as a potential network antigen
      for triggering active anti-GD2 antibodies in patients with GD2-positive
      neuroectodermal tumors.
FAU - Sen, G
AU  - Sen G
AD  - Department of Medicine and Markey Cancer Center, University of Kentucky,
      Lexington, Kentucky 40536, USA.
FAU - Chakraborty, M
AU  - Chakraborty M
FAU - Foon, K A
AU  - Foon KA
FAU - Reisfeld, R A
AU  - Reisfeld RA
FAU - Bhattacharya-Chatterjee, M
AU  - Bhattacharya-Chatterjee M
LA  - eng
GR  - R01 CA-72018-01/CA/NCI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Clin Cancer Res
JT  - Clinical cancer research : an official journal of the American Association for
      Cancer Research
JID - 9502500
RN  - 0 (Adjuvants, Immunologic)
RN  - 0 (Antibodies, Anti-Idiotypic)
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Gangliosides)
RN  - 65988-71-8 (ganglioside, GD2)
RN  - 7SQY4ZUD30 (ch14.18 monoclonal antibody)
SB  - IM
MH  - Adjuvants, Immunologic
MH  - Animals
MH  - Antibodies, Anti-Idiotypic/*immunology/toxicity
MH  - Antibodies, Monoclonal/*immunology/toxicity
MH  - Antibody Formation
MH  - Antibody-Dependent Cell Cytotoxicity
MH  - Colonic Neoplasms/immunology
MH  - Gangliosides/*immunology
MH  - Humans
MH  - Macaca fascicularis
MH  - Melanoma/immunology
MH  - Mice
MH  - Mice, Inbred BALB C
MH  - Rabbits
MH  - Tumor Cells, Cultured
EDAT- 1998/11/17 00:00
MHDA- 1998/11/17 00:01
CRDT- 1998/11/17 00:00
PHST- 1998/11/17 00:00 [pubmed]
PHST- 1998/11/17 00:01 [medline]
PHST- 1998/11/17 00:00 [entrez]
PST - ppublish
SO  - Clin Cancer Res. 1997 Nov;3(11):1969-76.

PMID- 15272600
OWN - NLM
STAT- MEDLINE
DCOM- 20040730
LR  - 20171116
IS  - 0385-0684 (Print)
IS  - 0385-0684 (Linking)
VI  - 31
IP  - 7
DP  - 2004 Jul
TI  - [Clinical usefulness of circulating tumor markers].
PG  - 1131-4
AB  - There are many molecular tumor markers for diagnosing and monitoring cancer
      patients. Especially, quantitative assay for serum levels of tumor markers; such 
      as AFP, CEA, PSA, hCG, CA 19-9 and CA 125, are frequently used in daily practice 
      because of their relative specificities and usefulness to the common cancers.
      Though not suitable for early diagnosis, but they are used in monitoring patients
      with advanced caner, especially after treatments. Two of them, AFP and PSA, are
      also used in the screening and monitoring of high-risk groups, namely patients
      with chronic viral hepatitis and old male, who are the high risk for hepatoma and
      proste cancer respectively. Problems in using serum markers are; relatively low
      specificity and low sensitivity to cancer, confusing naming for similar markers
      that recognize almost the same molecule of cancer. Users must understand that CA 
      19-9, CA 50, KM-O 1 and SPAN-1 are in the same sialylated Lewis A group, and CA
      125, CA 130 and CA 602; in the mucin antigen group, and STN, CA 54/61 and CA
      72-4; in the sialyl Tn antigen group. Combination of two or more markers may
      inform us the biological characteristics of the cancer. For example, a germ-cell 
      tumors may produce hCG and placental marker. That is of the choriocarcinoma type.
      Those with hCG and fetal antigens are the ordinal type of germ cell tumors, and
      those with AFP, CEA and cytokeratin are teratoma, and those with LDH and ALP only
      but negative for hCG and AFP must be seminoma. For the bronchial and alveolar
      carcinomas, CEA, SCC, NSE and cytokeratin 19 fragments are useful. Combination
      may be difficult for beginners but once understood, it will be an art in clinical
      oncology.
FAU - Ohkura, Hisanao
AU  - Ohkura H
AD  - Ibaraki Kenritsu Chuo Hospital & Cancer Center, 6528 Koibuchi, Tomobe-machi,
      Nishi-ibaraki-gun, Ibaraki 309-1793, Japan.
LA  - jpn
PT  - Journal Article
PL  - Japan
TA  - Gan To Kagaku Ryoho
JT  - Gan to kagaku ryoho. Cancer & chemotherapy
JID - 7810034
RN  - 0 (Antigens, Neoplasm)
RN  - 0 (Biomarkers)
RN  - 0 (Biomarkers, Tumor)
RN  - 0 (Carcinoembryonic Antigen)
RN  - 0 (Keratin-19)
RN  - 0 (Lewis X Antigen)
RN  - 0 (Protein Precursors)
RN  - 0 (alpha-Fetoproteins)
RN  - 0 (antigen CYFRA21.1)
RN  - 53230-14-1 (acarboxyprothrombin)
RN  - 68238-35-7 (Keratins)
RN  - 9001-26-7 (Prothrombin)
RN  - EC 3.4.21.77 (Prostate-Specific Antigen)
SB  - IM
MH  - Antigens, Neoplasm/blood
MH  - Biomarkers/blood
MH  - Biomarkers, Tumor/*blood/*classification
MH  - Carcinoembryonic Antigen/blood
MH  - Diagnosis, Differential
MH  - Female
MH  - Hepatitis, Viral, Human/diagnosis
MH  - Humans
MH  - Keratin-19
MH  - Keratins
MH  - Lewis X Antigen/blood
MH  - Male
MH  - Neoplasms/*diagnosis
MH  - Prostate-Specific Antigen/blood
MH  - Prostatic Neoplasms/diagnosis
MH  - Protein Precursors/blood
MH  - Prothrombin
MH  - alpha-Fetoproteins/analysis
EDAT- 2004/07/27 05:00
MHDA- 2004/07/31 05:00
CRDT- 2004/07/27 05:00
PHST- 2004/07/27 05:00 [pubmed]
PHST- 2004/07/31 05:00 [medline]
PHST- 2004/07/27 05:00 [entrez]
PST - ppublish
SO  - Gan To Kagaku Ryoho. 2004 Jul;31(7):1131-4.

PMID- 2467192
OWN - NLM
STAT- MEDLINE
DCOM- 19890425
LR  - 20151119
IS  - 0161-5890 (Print)
IS  - 0161-5890 (Linking)
VI  - 26
IP  - 1
DP  - 1989 Jan
TI  - Tn epitope (N-acetyl-D-galactosamine alpha-O-serine/threonine) density in primary
      breast carcinoma: a functional predictor of aggressiveness.
PG  - 1-5
AB  - This interpretive review attempts to dovetail advanced work by different groups
      of investigators on blood group and carcinoma (CA) glycoconjugates that have
      terminal, immunoreactive Tn epitopes (GalNAc alpha-O-Ser/Thr), and on the
      interaction of those structures with complementary antibodies and lectins. Fenlon
      et al. (1987) and Leathem and Brooks (1987) found a positive correlation between 
      primary breast CA aggressiveness and its affinity for Helix pomatia (HPA) lectin.
      This phenomenon was used successfully to accurately predict, in studies on 305
      breast CA patients, early or late CA recurrence and patient survival time. The
      innate specificity of the large HPA combining groove (aside from its avid
      reactivity with appropriately spaced GalNAc alpha-O-) remains obscure, despite
      careful investigation for more than a decade (Baker et al., 1983). Leathem and
      Brooks presumed that HPA recognizes a hitherto "undefined biological marker" that
      indicates a breast CA's aggressiveness. Our own work has shown that the
      chemically fully defined Tn epitope, as measured with human polyclonal and murine
      monoclonal anti-Tn antibodies, occurs in immunoreactive form in approximately 90%
      of all breast and lung adenoCAs studied. Tn is occluded and non-reactive in
      healthy and non-CA-diseased tissues. We found that CA-associated Tn is an
      adhesion molecule in attachment to healthy cells; an increase in its density on
      breast CA cell membranes parallels greater aggressiveness of breast tumors in
      both humans and mice (the only species studied). Thus, Tn may be all or a major
      part of the postulated "as yet undefined biological marker" associated with high 
      breast CA aggressiveness. Besides being helpful in the elucidation of some
      aspects of breast CA pathogenesis, these findings on primary breast CA have
      clinical implications in that they should facilitate stratification of breast CA 
      patients for adjuvant treatment.
FAU - Springer, G F
AU  - Springer GF
AD  - Immunochemistry Research Department, Evanston Hospital, Department of Surgery,
      Northwestern University, Evanston, IL 60201.
LA  - eng
GR  - CA 22540/CA/NCI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PT  - Review
PL  - England
TA  - Mol Immunol
JT  - Molecular immunology
JID - 7905289
RN  - 0 (Antibodies, Neoplasm)
RN  - 0 (Antigens, Neoplasm)
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Biomarkers, Tumor)
RN  - 0 (Epitopes)
RN  - 0 (Tn antigen)
SB  - IM
MH  - Antibodies, Neoplasm/immunology
MH  - Antigens, Neoplasm/*analysis
MH  - *Antigens, Tumor-Associated, Carbohydrate
MH  - Biomarkers, Tumor/analysis
MH  - Breast Neoplasms/*immunology
MH  - Epitopes/*analysis
MH  - Female
MH  - Humans
RF  - 43
EDAT- 1989/01/01 00:00
MHDA- 1989/01/01 00:01
CRDT- 1989/01/01 00:00
PHST- 1989/01/01 00:00 [pubmed]
PHST- 1989/01/01 00:01 [medline]
PHST- 1989/01/01 00:00 [entrez]
PST - ppublish
SO  - Mol Immunol. 1989 Jan;26(1):1-5.

PMID- 11389097
OWN - NLM
STAT- MEDLINE
DCOM- 20010621
LR  - 20071205
IS  - 0008-5472 (Print)
IS  - 0008-5472 (Linking)
VI  - 61
IP  - 11
DP  - 2001 Jun 1
TI  - Overexpression of sialyltransferase CMP-sialic acid:Galbeta1,3GalNAc-R
      alpha6-Sialyltransferase is related to poor patient survival in human colorectal 
      carcinomas.
PG  - 4605-11
AB  - Thomsen-Friedenreich (TF)-related blood group antigens, such as TF, Tn, and their
      sialylated variants, belong to a family of tumor-associated carbohydrates. The
      aim of the present study was to examine tumor-associated alterations of
      glycosyltransferases involved in the biosynthesis of the TF glycotope in
      colorectal carcinomas. To this end, glycosyltransferase expression was examined
      in 40 cases of colorectal carcinoma specimens classified according to the
      WHO/Union International Contre Cancer guidelines and in "normal" mucosa of the
      same patients. Occurrence of TF glycotope was examined by immunohistochemistry
      with the monoclonal antibody A78-G/A7. Expression of sialyltransferases
      CMP-sialic acid:Galbeta1,3GalNAc-R alpha3-sialyltransferase I and II (ST3Gal-I
      and ST3Gal-II) and CMP-sialic acid:Galbeta1,3GalNAc-R alpha6-sialyltransferase
      (ST6GalNAc-II) and of core 2 beta1,6-N-acetylglucosaminyltransferase was
      determined by reverse transcription-PCR in the same cryostat sections used for
      immunohistochemistry. Additionally, alpha2,3-sialyltransferase enzyme activity
      was studied in each of these tissues. The TF glycotope was detected in 7% of the 
      normal mucosa, but in 57% of the carcinoma samples. Expression of
      alpha2,3-sialyltransferases ST3Gal-I, ST3Gal-II, and enzyme activity of
      alpha2,3-sialyltransferase was significantly increased (P < 0.001) in carcinoma
      specimens compared with normal mucosa. ST3Gal-I mRNA expression was significantly
      increased (P = 0.05) in cases showing invasion of lymph vessels. Expression of
      ST6GalNAc-II was significantly increased (P = 0.04) in cases with metastases to
      lymph nodes along the vascular trunk. Moreover, ST6GalNAc-II expression provides 
      an prognostic factor for patient survival (log rank, P = 0.02). In an attempt to 
      study the functional relevance of the glycosyltransferases for TF biosynthesis,
      SW480 colorectal cells were transfected with each of the enzymes, and cell
      surface expression of the TF glycotope was examined by flow cytometry. The
      presence of TF was not altered by transfection of the cells with either
      sialyltransferase ST3Gal-I or ST3Gal-II. However, successful transfection with
      core 2 beta1,6-N-acetylglucosaminyltransferase led to reduced expression of TF.
      In contrast, increased cell surface expression of TF was found after ST6GalNAc-II
      transfection. Thus, expression of TF on the cell surface of SW480 colorectal
      carcinoma cells depends on the ratio of core 2
      beta1,6-N-acetylglucosaminyltransferase and ST6GalNAc-II. Earlier
      immunohistological studies demonstrated that TF is a prognostic factor for
      patient survival. Our results suggest that sialyltransferase ST6GalNAc-II is of
      crucial relevance for the prognostic significance of TF.
FAU - Schneider, F
AU  - Schneider F
AD  - Robert-Rossle-Klinik at the Max Delbruck Center for Molecular Medicine,
      Department for Surgery and Surgical Oncology, Lindenberger Weg 80, D-13122
      Berlin, Germany.
FAU - Kemmner, W
AU  - Kemmner W
FAU - Haensch, W
AU  - Haensch W
FAU - Franke, G
AU  - Franke G
FAU - Gretschel, S
AU  - Gretschel S
FAU - Karsten, U
AU  - Karsten U
FAU - Schlag, P M
AU  - Schlag PM
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Cancer Res
JT  - Cancer research
JID - 2984705R
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Epitopes)
RN  - 0 (Isoenzymes)
RN  - 3554-90-3 (Thomsen-Friedenreich antigen)
RN  - EC 2.4.1.- (N-Acetylglucosaminyltransferases)
RN  - EC 2.4.1.102 (beta-1,3-galactosyl-O-glycosyl-glycoprotein
      beta-1,6-acetylglucosaminyl transferase)
RN  - EC 2.4.99.- (Sialyltransferases)
RN  - EC 2.4.99.- (galactosyl-1-3-N-acetylgalactosaminyl-specific
      2,6-sialyltransferase)
RN  - EC 2.4.99.4 (beta-galactoside alpha-2,3-sialyltransferase)
SB  - IM
MH  - Adult
MH  - Aged
MH  - Aged, 80 and over
MH  - Antigens, Tumor-Associated, Carbohydrate/biosynthesis/immunology/metabolism
MH  - Carbohydrate Sequence
MH  - Colorectal Neoplasms/*enzymology/genetics/immunology
MH  - Epitopes/biosynthesis
MH  - Female
MH  - Humans
MH  - Immunohistochemistry
MH  - Isoenzymes/biosynthesis/genetics
MH  - Male
MH  - Middle Aged
MH  - Molecular Sequence Data
MH  - N-Acetylglucosaminyltransferases/biosynthesis/genetics/metabolism
MH  - Prognosis
MH  - Reverse Transcriptase Polymerase Chain Reaction
MH  - Sialyltransferases/*biosynthesis/genetics/metabolism
MH  - Transfection
EDAT- 2001/06/05 10:00
MHDA- 2001/06/22 10:01
CRDT- 2001/06/05 10:00
PHST- 2001/06/05 10:00 [pubmed]
PHST- 2001/06/22 10:01 [medline]
PHST- 2001/06/05 10:00 [entrez]
PST - ppublish
SO  - Cancer Res. 2001 Jun 1;61(11):4605-11.

PMID- 2466827
OWN - NLM
STAT- MEDLINE
DCOM- 19890502
LR  - 20190510
IS  - 0021-924X (Print)
IS  - 0021-924X (Linking)
VI  - 104
IP  - 5
DP  - 1988 Nov
TI  - A monoclonal antibody that recognizes sialyl-Lea oligosaccharide, but is distinct
      from NS 19-9 as to epitope recognition.
PG  - 817-21
AB  - A murine monoclonal antibody, designated as MSW 113, was generated using a human 
      colonic cancer cell line, SW 1116, as the immunogen. MSW 113 was shown to be
      directed mainly to mucin-type oligosaccharide with sialyl-Lea antigens. The
      reactivity of MSW 113 to sialyl-Lea was stronger than that of NS 19-9, which is
      believed to be raised against the same determinant group. MSW 113 binds to
      sialyl-Lea-ol, LS-tetrasaccharide a, and disialyllacto-N-tetraose with higher
      affinities, compared to NS 19-9. These two antibodies could clearly be
      distinguished in that MSW 113 bound to sialic acid but not to fucose, whereas NS 
      19-9 bound to fucose but not to sialic acid. Thus, MSW 113 is directed more
      toward sialic acid-containing terminal structures while NS 19-9 is directed
      toward fucose-containing internal structures. MSW 113 was found to be useful for 
      detecting antigens in the bloodstream of patients, especially those with pancreas
      cancer. Even NS 19-9 negative patient sera were positive for MSW 113.
FAU - Kitagawa, H
AU  - Kitagawa H
AD  - Department of Biological Chemistry, Faculty of Pharmaceutical Sciences, Kyoto
      University.
FAU - Nakada, H
AU  - Nakada H
FAU - Numata, Y
AU  - Numata Y
FAU - Kurosaka, A
AU  - Kurosaka A
FAU - Fukui, S
AU  - Fukui S
FAU - Funakoshi, I
AU  - Funakoshi I
FAU - Kawasaki, T
AU  - Kawasaki T
FAU - Yamashina, I
AU  - Yamashina I
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - J Biochem
JT  - Journal of biochemistry
JID - 0376600
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens, Neoplasm)
RN  - 0 (Epitopes)
RN  - 0 (Lewis Blood-Group System)
RN  - 0 (Oligosaccharides)
RN  - 0 (sialooligosaccharides)
SB  - IM
MH  - Antibodies, Monoclonal/*immunology
MH  - Antibody Formation
MH  - Antibody Specificity
MH  - Antigens, Neoplasm/immunology
MH  - Colonic Neoplasms/immunology
MH  - Epitopes/*immunology
MH  - Humans
MH  - Hybridomas/immunology
MH  - Lewis Blood-Group System/*immunology
MH  - Oligosaccharides/*immunology
MH  - Tumor Cells, Cultured
EDAT- 1988/11/01 00:00
MHDA- 1988/11/01 00:01
CRDT- 1988/11/01 00:00
PHST- 1988/11/01 00:00 [pubmed]
PHST- 1988/11/01 00:01 [medline]
PHST- 1988/11/01 00:00 [entrez]
AID - 10.1093/oxfordjournals.jbchem.a122555 [doi]
PST - ppublish
SO  - J Biochem. 1988 Nov;104(5):817-21. doi: 10.1093/oxfordjournals.jbchem.a122555.

PMID- 8563144
OWN - NLM
STAT- MEDLINE
DCOM- 19960305
LR  - 20190512
IS  - 0959-6658 (Print)
IS  - 0959-6658 (Linking)
VI  - 5
IP  - 6
DP  - 1995 Sep
TI  - Detection in human blood platelets of sialyl Lewis X gangliosides, potential
      ligands for CD62 and other selectins.
PG  - 571-81
AB  - Activated platelets are known to express P-selectin, a lectin-like adhesion
      receptor (CD62), through which they bind to sialyl Lewis X (sLex) ligands
      displayed on the membranes of leukocytes. To determine whether direct
      platelet-platelet interactions via P-selectin/sLex interactions are also
      possible, we have examined the ganglioside extract of human blood platelets for
      the presence of sLex ligands. Using the sensitive method of high-performance
      thin-layer chromatography (HPTLC)-immunostaining with the monoclonal antibody
      (mAb) CSLEX or with sialidase followed by mAbs MC480 or PM81, eight sLex bands
      were demonstrated at Rf 0.01, 0.03, 0.05, 0.06, 0.08, 0.10, 0.14 and 0.21 in the 
      solvent 45:55:10 chloroform-methanol-aqueous 0.02% CaCl2. The sensitivity of all 
      eight bands to sialidase or endoglycoceramidase confirmed that they were
      gangliosides. Comparison of the HPTLC mobilities and densities of platelet bands 
      with those from five other human tissues (granulocytes, monoblasts, kidney,
      aortic endothelium and erythrocytes) in three different solvents revealed three
      major bands associated with platelets: 3 (Rf0.03), 6 (0.08) and 14 (0.21).
      Platelet bands were demonstrated not to have resulted from granulocyte
      contamination. Partial purification of platelet sLex gangliosides by
      high-performance liquid chromatography and their reaction with 14
      oligosaccharide-specific mAbs (FH4, FH5, LM112-161, LM119-181, A5, 1B2, BR55-2,
      BE2, ES4, MC631, MH04, SH34, P001 and MC813-70) revealed that band 6 is a
      multifucosylated neolacto ganglioside and band 14 is a branched, disialo neolacto
      fucoganglioside. Platelet band 3 combined the features of both bands 6 and 14,
      and reacted differently than granulocyte band 3. These partial structures
      resemble gangliosides associated with adhesion in other cell systems. It is
      concluded that platelets express tissue-specific sLex gangliosides (sLex
      ligands). Thus, it is possible that platelet-platelet binding may be mediated at 
      least partially through P-selectin/sLex interactions, especially after platelet
      activation.
FAU - Cooling, L L
AU  - Cooling LL
AD  - Department of Pathology, University of Iowa College of Medicine, Iowa City
      52242-1182, USA.
FAU - Zhang, D S
AU  - Zhang DS
FAU - Walker, K E
AU  - Walker KE
FAU - Koerner, T A
AU  - Koerner TA
LA  - eng
GR  - R29 HL42395/HL/NHLBI NIH HHS/United States
GR  - T32 HL07344/HL/NHLBI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - England
TA  - Glycobiology
JT  - Glycobiology
JID - 9104124
RN  - 0
      (5-acetylneuraminyl-(2-3)-galactosyl-(1-4)-(fucopyranosyl-(1-3))-N-acetylglucosam
      ine)
RN  - 0 (Gangliosides)
RN  - 0 (Oligosaccharides)
RN  - 0 (P-Selectin)
RN  - 0 (Selectins)
SB  - IM
MH  - Blood Platelets/*metabolism
MH  - Carbohydrate Sequence
MH  - Gangliosides/*metabolism
MH  - Granulocytes/metabolism
MH  - Hemofiltration
MH  - Humans
MH  - Molecular Sequence Data
MH  - Oligosaccharides/*metabolism
MH  - P-Selectin/*metabolism
MH  - Selectins/*metabolism
EDAT- 1995/09/01 00:00
MHDA- 1995/09/01 00:01
CRDT- 1995/09/01 00:00
PHST- 1995/09/01 00:00 [pubmed]
PHST- 1995/09/01 00:01 [medline]
PHST- 1995/09/01 00:00 [entrez]
AID - 10.1093/glycob/5.6.571 [doi]
PST - ppublish
SO  - Glycobiology. 1995 Sep;5(6):571-81. doi: 10.1093/glycob/5.6.571.

PMID- 6189529
OWN - NLM
STAT- MEDLINE
DCOM- 19830708
LR  - 20111117
IS  - 0144-8463 (Print)
IS  - 0144-8463 (Linking)
VI  - 3
IP  - 2
DP  - 1983 Feb
TI  - A monoclonal antibody against human colonic adenoma recognizes difucosylated
      Type-2-blood-group chains.
PG  - 163-70
AB  - A monoclonal antibody C14/1/46/10 showing preferential binding to membranes of
      human colorectal carcinomas over normal colon mucosae was obtained by
      immunization of mice with extra-nuclear membranes of a human colonic adenoma.
      Binding and inhibition of binding assays using blood cells or glycoproteins with 
      known blood-group activities indicated that the antibody recognizes a
      carbohydrate antigen co-existing with the blood-group-H determinant: Fuc alpha 1 
      leads to 2 Gal. Inhibition assays with structurally defined oligosaccharides
      showed that the antigenic determinant involves difucosylated Type-2-blood-group
      chains with the structure: (formula; see text)
FAU - Brown, A
AU  - Brown A
FAU - Feizi, T
AU  - Feizi T
FAU - Gooi, H C
AU  - Gooi HC
FAU - Embleton, M J
AU  - Embleton MJ
FAU - Picard, J K
AU  - Picard JK
FAU - Baldwin, R W
AU  - Baldwin RW
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - Biosci Rep
JT  - Bioscience reports
JID - 8102797
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antibodies, Neoplasm)
RN  - 0 (Blood Group Antigens)
RN  - 0 (Epitopes)
SB  - IM
MH  - Adenoma/*immunology
MH  - Animals
MH  - Antibodies, Monoclonal/*isolation & purification
MH  - *Antibodies, Neoplasm
MH  - Binding Sites, Antibody
MH  - Blood Group Antigens/*immunology
MH  - Colonic Neoplasms/*immunology
MH  - Dogs
MH  - Epitopes
MH  - Humans
MH  - Intestinal Mucosa/immunology
MH  - Mice
MH  - Mice, Inbred BALB C
MH  - Swine
EDAT- 1983/02/01 00:00
MHDA- 1983/02/01 00:01
CRDT- 1983/02/01 00:00
PHST- 1983/02/01 00:00 [pubmed]
PHST- 1983/02/01 00:01 [medline]
PHST- 1983/02/01 00:00 [entrez]
PST - ppublish
SO  - Biosci Rep. 1983 Feb;3(2):163-70.

PMID- 10971172
OWN - NLM
STAT- MEDLINE
DCOM- 20000927
LR  - 20171101
IS  - 0030-2414 (Print)
IS  - 0030-2414 (Linking)
VI  - 59
IP  - 2
DP  - 2000 Aug
TI  - Different expression of sialyl Tn antigen between polypoid and nonpolypoid growth
      types of advanced colorectal carcinoma.
PG  - 131-8
AB  - Colorectal tumors can be classified based on their growth pattern into the
      polypoid growth type (PG-type) and nonpolypoid growth type (NPG-type). We
      examined sialyl Tn antigen expression in advanced colorectal carcinomas that were
      classified as PG-type and NPG-type cancers in order to ascertain whether or not
      such expression correlates with other biologically and clinically important
      differences. A total of 94 advanced colorectal carcinomas were examined for
      sialyl Tn antigen expression, which was immunohistochemically detected by the
      monoclonal antibody TKH2. Univariate and multivariate analyses using logistic
      regression models were performed. Forty carcinomas (42.6%) were negative and 54
      (57.5%) were positive for sialyl Tn antigen. Eighteen carcinomas (19.2%) were of 
      PG type and 76 (80.8%) of NPG type. NPG-type cancers had a higher proportion of
      positive lymph node metastasis than PG-type cancers. Furthermore, sialyl Tn
      antigen was less often detected in NPG-type cancers (39 of 76; 51.3%) than in
      PG-type cancers (15 of 18; 83.3%; p = 0.0167). Multivariate analysis showed that 
      two variables, lymph node metastasis and sialyl Tn antigen expression in
      carcinoma, were independently related to tumor growth patterns, that is NPG type 
      and PG type. These data suggest that the difference in sialyl Tn antigen
      expression between two kinds of tumor growth patterns of advanced colorectal
      carcinomas, PG type and NPG type, may reflect different biological behaviors
      during tumor progression.
CI  - Copyright 2000 S. Karger AG, Basel.
FAU - Nakagoe, T
AU  - Nakagoe T
AD  - First Department of Surgery, Nagasaki University School of Medicine, Nagasaki,
      Japan. nakagoe@net.nagasaki-u.ac.jp
FAU - Nanashima, A
AU  - Nanashima A
FAU - Sawai, T
AU  - Sawai T
FAU - Tuji, T
AU  - Tuji T
FAU - Yamaguchi, E
AU  - Yamaguchi E
FAU - Jibiki, M
AU  - Jibiki M
FAU - Yamaguchi, H
AU  - Yamaguchi H
FAU - Yasutake, T
AU  - Yasutake T
FAU - Ayabe, H
AU  - Ayabe H
FAU - Matuo, T
AU  - Matuo T
FAU - Tagawa, Y
AU  - Tagawa Y
LA  - eng
PT  - Comparative Study
PT  - Journal Article
PL  - Switzerland
TA  - Oncology
JT  - Oncology
JID - 0135054
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (sialosyl-Tn antigen)
SB  - IM
MH  - Aged
MH  - Antibodies, Monoclonal
MH  - Antigens, Tumor-Associated, Carbohydrate/*biosynthesis
MH  - Colorectal Neoplasms/classification/*metabolism/pathology
MH  - Female
MH  - Humans
MH  - Immunohistochemistry
MH  - Male
MH  - Middle Aged
MH  - Multivariate Analysis
EDAT- 2000/09/06 11:00
MHDA- 2000/09/30 11:01
CRDT- 2000/09/06 11:00
PHST- 2000/09/06 11:00 [pubmed]
PHST- 2000/09/30 11:01 [medline]
PHST- 2000/09/06 11:00 [entrez]
AID - 12150 [pii]
AID - 10.1159/000012150 [doi]
PST - ppublish
SO  - Oncology. 2000 Aug;59(2):131-8. doi: 10.1159/000012150.

PMID- 10722702
OWN - NLM
STAT- MEDLINE
DCOM- 20000427
LR  - 20190508
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 275
IP  - 12
DP  - 2000 Mar 24
TI  - New aspects of siglec binding specificities, including the significance of
      fucosylation and of the sialyl-Tn epitope. Sialic acid-binding immunoglobulin
      superfamily lectins.
PG  - 8625-32
AB  - The siglecs (sialic acid-binding immunoglobulin superfamily lectins) are
      immunoglobulin superfamily members recognizing sialylated ligands. Most prior
      studies of siglec specificities focused on alpha2-3- and
      alpha2-6-sialyllactos(amin)es and on one or two of the siglecs at a time. Here,
      we explore several new aspects of specificities of the first six reported
      siglecs, using sialylated glycans presented in multivalent form, on synthetic
      polyacrylamide backbones, or on mucin polypeptides. First, we report that binding
      of siglec-1 (sialoadhesin), siglec-3 (CD33), siglec-4a (myelin-associated
      glycoprotein), and siglec-5 to alpha2-3 sialyllactosamine is affected markedly by
      the presence of an alpha1-3-linked fucose. Thus, while siglecs may not interfere 
      with selectin-mediated recognition, fucosylation could negatively regulate siglec
      binding. Second, in contrast to earlier studies, we find that siglec-3 prefers
      alpha2-6-sialyllactose. Third, siglec-5 binds alpha2-8-linked sialic acid, making
      it the siglec least specific for linkage recognition. Fourth, siglecs-2 (CD22),
      -3, -5, and -6 (obesity-binding protein 1) showed significant binding to
      sialyl-Tn (Neu5Acalpha2-6-GalNAc), a tumor marker associated with poor prognosis.
      Fifth, siglec-6 is an exception among siglecs in not requiring the glycerol side 
      chain of sialic acid for recognition. Sixth, all siglecs require the carboxyl
      group of sialic acid for binding. Finally, the presentation of the sialyl-Tn
      epitope and/or more extended structures that include this motif may be important 
      for optimal recognition by the siglecs. This was concluded from studies using
      ovine, bovine, and porcine submaxillary mucins and Chinese hamster ovary cells
      transfected with ST6GalNAc-I and/or the mucin polypeptide MUC1.
FAU - Brinkman-Van der Linden, E C
AU  - Brinkman-Van der Linden EC
AD  - Glycobiology Research and Training Center and Department of Medicine, University 
      of California San Diego, La Jolla, California 92093, USA.
FAU - Varki, A
AU  - Varki A
LA  - eng
GR  - P01 HL57345/HL/NHLBI NIH HHS/United States
GR  - R01GM3273/GM/NIGMS NIH HHS/United States
PT  - Comparative Study
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Antigens, CD)
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Epitopes)
RN  - 0 (Immunoglobulins)
RN  - 0 (Lectins)
RN  - 0 (sialosyl-Tn antigen)
RN  - 28RYY2IV3F (Fucose)
SB  - IM
MH  - Antigens, CD/metabolism
MH  - Antigens, Tumor-Associated, Carbohydrate/*immunology
MH  - Binding Sites
MH  - Carbohydrate Sequence
MH  - Epitopes/*immunology
MH  - Fucose/*immunology
MH  - Humans
MH  - Immunoglobulins/*metabolism
MH  - Lectins/*metabolism
MH  - Molecular Sequence Data
MH  - Multigene Family
MH  - Protein Binding
MH  - Stereoisomerism
EDAT- 2000/03/18 09:00
MHDA- 2000/04/29 09:00
CRDT- 2000/03/18 09:00
PHST- 2000/03/18 09:00 [pubmed]
PHST- 2000/04/29 09:00 [medline]
PHST- 2000/03/18 09:00 [entrez]
AID - 10.1074/jbc.275.12.8625 [doi]
PST - ppublish
SO  - J Biol Chem. 2000 Mar 24;275(12):8625-32. doi: 10.1074/jbc.275.12.8625.

PMID- 9590134
OWN - NLM
STAT- MEDLINE
DCOM- 19980604
LR  - 20160303
IS  - 0020-7136 (Print)
IS  - 0020-7136 (Linking)
VI  - 76
IP  - 4
DP  - 1998 May 18
TI  - Liver metastasis and adhesion to the sinusoidal endothelium by human colon cancer
      cells is related to mucin carbohydrate chain length.
PG  - 556-62
AB  - Mucin production by human colon cancer cells correlates with liver metastasis in 
      animal models, but it is not known which steps in metastasis depend on specific
      alterations in mucin synthesis. Clonal variants of cell line LS174T selected for 
      differences in mucin core carbohydrate expression have been further characterized
      biochemically, and tested for their ability to participate in metastasis-related 
      events. LS-C mucin contains truncated carbohydrates enriched for sialyl Tn and
      these cells bind to basement membrane matrix to a greater extent than LS-B cells.
      This binding is partially inhibitable by antibody to sialyl Tn. LS-B produces
      more fully glycosylated mucin and preferentially binds to hepatic sinusoidal
      endothelial cells and E-selectin through sialylated peripheral mucin-associated
      carbohydrate structures. Adhesion of LS-B to endothelial cells is inhibited by
      neutralizing antibody to E-selectin, and inhibition of glycosylation or
      desialylation of LS-B mucin abrogates binding to E-selectin in vitro. LS-B cells 
      spontaneously metastasized from cecum to liver and colonized the liver of athymic
      mice after splenic-portal injection to a significantly greater extent than LS-C, 
      suggesting that expression of peripheral mucin carbohydrate structures is most
      important for metastasis of human colon cancer cells.
FAU - Bresalier, R S
AU  - Bresalier RS
AD  - Department of Medicine, Henry Ford Health Sciences Center, Detroit, MI 48202,
      USA. rbresal@mich.com
FAU - Byrd, J C
AU  - Byrd JC
FAU - Brodt, P
AU  - Brodt P
FAU - Ogata, S
AU  - Ogata S
FAU - Itzkowitz, S H
AU  - Itzkowitz SH
FAU - Yunker, C K
AU  - Yunker CK
LA  - eng
GR  - CA-52491/CA/NCI NIH HHS/United States
GR  - CA-69480/CA/NCI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Int J Cancer
JT  - International journal of cancer
JID - 0042124
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Carbohydrates)
RN  - 0 (E-Selectin)
RN  - 0 (Mucins)
RN  - 0 (sialosyl-Tn antigen)
SB  - IM
MH  - Animals
MH  - Antigens, Tumor-Associated, Carbohydrate/metabolism
MH  - Basement Membrane/metabolism
MH  - Carbohydrates/*chemistry
MH  - Cell Adhesion
MH  - Colonic Neoplasms/*metabolism/*pathology
MH  - E-Selectin/metabolism
MH  - Endothelium/metabolism
MH  - Humans
MH  - Liver/cytology
MH  - Liver Neoplasms/*secondary
MH  - Mice
MH  - Mucins/*chemistry
MH  - Neoplasm Metastasis
MH  - Tumor Cells, Cultured
EDAT- 1998/05/20 02:09
MHDA- 2000/06/20 09:00
CRDT- 1998/05/20 02:09
PHST- 1998/05/20 02:09 [pubmed]
PHST- 2000/06/20 09:00 [medline]
PHST- 1998/05/20 02:09 [entrez]
AID - 10.1002/(SICI)1097-0215(19980518)76:4<556::AID-IJC19>3.0.CO;2-5 [pii]
PST - ppublish
SO  - Int J Cancer. 1998 May 18;76(4):556-62.

PMID- 2408796
OWN - NLM
STAT- MEDLINE
DCOM- 19850820
LR  - 20181113
IS  - 0009-9104 (Print)
IS  - 0009-9104 (Linking)
VI  - 60
IP  - 1
DP  - 1985 Apr
TI  - Differences in the fine specificities of monoclonal (Class A) antibodies to human
      myeloid cells.
PG  - 151-8
AB  - Among 13 monoclonal antibodies to human myelomonocytic cells, six could be
      assigned to a group designated Class A with the following properties: (a) they
      react almost exclusively with granulocytes among cells of the peripheral blood,
      (b) they resemble the previously described anti-granulocyte antibodies, VEP8 and 
      VEP9, and the anti-mouse embryo, anti-SSEA-1, in their strong reactions with
      human meconium glycoproteins and ovarian cyst mucins of non-secretor type and (c)
      they recognize the carbohydrate antigen 3-fucosyl-N-acetyllactosamine (alpha
      1----3fucosylated Type 2 blood group chains). The binding of these anti-myeloid
      antibodies is more strongly inhibited by lacto-N-fucopentaose III than by the
      trisaccharide-fucosyl-N-acetyllactosamine, in contrast to anti-SSEA-1 which is
      more strongly inhibited by the trisaccharide. These observations suggest that the
      myeloid Class A antibodies recognize additional determinants on the neolacto (Gal
      beta 1----4GlcNAc beta 1----3Gal beta 1----4) backbone of the pentasaccharide
      which occurs on the glycoproteins and glycolipids of myeloid cells. However, no
      two of the anti-myeloid antibodies were identical in their inhibition patterns
      with the glycoproteins and the two oligosaccharides. They also differed in their 
      cellular reactivities, for example, the proportion of cells in the K-562 cell
      line reacting with each antibody ranged from 15-57%.
FAU - Gooi, H C
AU  - Gooi HC
FAU - Hounsell, E F
AU  - Hounsell EF
FAU - Edwards, A
AU  - Edwards A
FAU - Majdic, O
AU  - Majdic O
FAU - Knapp, W
AU  - Knapp W
FAU - Feizi, T
AU  - Feizi T
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - Clin Exp Immunol
JT  - Clinical and experimental immunology
JID - 0057202
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Epitopes)
RN  - 0 (Glycoproteins)
RN  - 0 (Lewis X Antigen)
RN  - 0 (Oligosaccharides)
RN  - 0 (Trisaccharides)
SB  - IM
MH  - Antibodies, Monoclonal/*immunology
MH  - *Antibody Specificity
MH  - Epitopes
MH  - Glycoproteins/immunology
MH  - Granulocytes/*immunology
MH  - Humans
MH  - Lewis X Antigen/immunology
MH  - Meconium/immunology
MH  - Oligosaccharides/immunology
MH  - Trisaccharides/immunology
PMC - PMC1577016
EDAT- 1985/04/01 00:00
MHDA- 1985/04/01 00:01
CRDT- 1985/04/01 00:00
PHST- 1985/04/01 00:00 [pubmed]
PHST- 1985/04/01 00:01 [medline]
PHST- 1985/04/01 00:00 [entrez]
PST - ppublish
SO  - Clin Exp Immunol. 1985 Apr;60(1):151-8.

PMID- 1644805
OWN - NLM
STAT- MEDLINE
DCOM- 19920910
LR  - 20071114
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 267
IP  - 23
DP  - 1992 Aug 15
TI  - Structural and immunological characterization of O-acetylated GD2. Evidence that 
      GD2 is an acceptor for ganglioside O-acetyltransferase in human melanoma cells.
PG  - 16200-11
AB  - We have shown previously that Golgi-enriched vesicles from the human melanoma
      cell line Melur can transfer [3H]acetate from [acetyl-3H]acetyl-CoA to endogenous
      GD3 to form [acetyl-3H]O-acetyl-GD3 (Manzi, A. E., Sjoberg, E. R., Diaz, S., and 
      Varki, A. (1990) J. Biol. Chem. 265, 13091-13103). Applying the same approach in 
      the human melanoma cell line M21, label was found in [acetyl-3H]O-acetyl-GD3 and 
      also in a species co-migrating with unsubstituted GD3 on TLC. Both were
      sialidase-sensitive and alkali-labile, indicating incorporation as [3H]O-acetyl
      esters on sialic acids. Immunological reactivity, sialidase sensitivity,
      chromatographic behavior, and the known ganglioside pattern of M21 cells
      suggested that the slower migrating species might be [acetyl-3H]O-acetyl-GD2.
      Sialic acids released from this labeled molecule by sialidase showed
      esterification with [3H]acetate at both C7 and C9 hydroxyls. Lipid extracts from 
      cells metabolically labeled with [3H]galactose showed a corresponding
      ganglioside, which upon alkali treatment yielded a species migrating with GD2.
      Analysis of purified ganglioside by high performance thin layer chromatography
      immuno-overlays, fast atom bombardment-mass spectrometry in positive and negative
      ion modes, periodate oxidation resistance, linkage analysis by permethylation and
      gas chromatography-mass spectrometry, and 500 MHz 1H NMR was consistent with the 
      following structure: 9-O Ac-Neu5Ac alpha 2-8Neu5Ac alpha 2-3(GalNAc beta 1-4) Gal
      beta 1-4Gluc beta 1-1' ceramide Total gangliosides from M21 were analyzed by high
      performance thin layer chromatography immuno-overlay with monoclonal antibodies
      D1.1, JONES, 27A, and 8A2, all known to, or suspected of reacting with
      9-O-acetylated gangliosides. The first three bound well to 9-O-acetyl-GD3 and a
      slower migrating 9-O-acetylated ganglioside, which was distinct from
      9-O-acetyl-GD2. Antibody 8A2 reacted weakly with purified 9-O-acetyl-GD2 and
      strongly with two other 9-O-acetylated gangliosides migrating slower than
      9-O-acetyl-GD2. Thus, the family of O-acetylated gangliosides in melanoma cells
      is much more complex than previously appreciated.
FAU - Sjoberg, E R
AU  - Sjoberg ER
AD  - Department of Medicine, University of California, La Jolla 92093.
FAU - Manzi, A E
AU  - Manzi AE
FAU - Khoo, K H
AU  - Khoo KH
FAU - Dell, A
AU  - Dell A
FAU - Varki, A
AU  - Varki A
LA  - eng
GR  - P01 AI 23287/AI/NIAID NIH HHS/United States
GR  - R01-GM32373/GM/NIGMS NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Gangliosides)
RN  - 0 (Sialic Acids)
RN  - 65988-71-8 (ganglioside, GD2)
RN  - 72-89-9 (Acetyl Coenzyme A)
RN  - EC 2.3.1.- (Acetyltransferases)
RN  - EC 2.3.1.- (ganglioside O-acetyltransferase)
SB  - IM
MH  - Acetyl Coenzyme A/*metabolism
MH  - Acetylation
MH  - Acetyltransferases/*metabolism
MH  - Carbohydrate Sequence
MH  - Chromatography, High Pressure Liquid
MH  - Clone Cells
MH  - Gangliosides/chemistry/isolation & purification/*metabolism
MH  - Gas Chromatography-Mass Spectrometry
MH  - Golgi Apparatus/enzymology
MH  - Humans
MH  - Melanoma/*enzymology
MH  - Methylation
MH  - Molecular Sequence Data
MH  - Sialic Acids/isolation & purification/metabolism
EDAT- 1992/08/15 00:00
MHDA- 1992/08/15 00:01
CRDT- 1992/08/15 00:00
PHST- 1992/08/15 00:00 [pubmed]
PHST- 1992/08/15 00:01 [medline]
PHST- 1992/08/15 00:00 [entrez]
PST - ppublish
SO  - J Biol Chem. 1992 Aug 15;267(23):16200-11.

PMID- 15967512
OWN - NLM
STAT- MEDLINE
DCOM- 20050908
LR  - 20111117
IS  - 0165-5728 (Print)
IS  - 0165-5728 (Linking)
VI  - 165
IP  - 1-2
DP  - 2005 Aug
TI  - Characterisation of the immunoglobulin variable region gene usage encoding the
      murine anti-ganglioside antibody repertoire.
PG  - 92-103
AB  - Neuropathogenic murine antibodies reactive with terminal disialylgalactose
      epitopes are innate and preferentially encoded by the VH7183.3b gene. Here we
      have studied antibodies reactive with internal galactose-linked disialosyl
      epitopes and the terminal trisaccharide of GT1b. Antibodies were of moderate
      affinity and unmutated. Anti-GD1b antibodies were often encoded by the VH10.2b
      heavy and gj38c light chain genes. Anti-GT1b antibodies with broader glycan
      binding patterns were encoded by VHQ52 and VHJ558 family genes. These data
      indicate that the discrete specificities of ganglioside-binding antibodies are
      dictated by particular patterns of V gene usage residing within the innate B cell
      repertoire.
FAU - Boffey, Judith
AU  - Boffey J
AD  - University Department of Neurology, Institute of Neurological Sciences, Southern 
      General Hospital, Glasgow, Scotland G51 4TF, United Kingdom.
FAU - Odaka, Masaaki
AU  - Odaka M
FAU - Nicoll, Dawn
AU  - Nicoll D
FAU - Wagner, Eric R
AU  - Wagner ER
FAU - Townson, Kate
AU  - Townson K
FAU - Bowes, Tyrone
AU  - Bowes T
FAU - Conner, Joe
AU  - Conner J
FAU - Furukawa, Koichi
AU  - Furukawa K
FAU - Willison, Hugh J
AU  - Willison HJ
LA  - eng
GR  - R01NS31528/NS/NINDS NIH HHS/United States
GR  - R01NS34846/NS/NINDS NIH HHS/United States
GR  - Wellcome Trust/United Kingdom
PT  - Journal Article
PT  - Research Support, N.I.H., Extramural
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - Netherlands
TA  - J Neuroimmunol
JT  - Journal of neuroimmunology
JID - 8109498
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Gangliosides)
RN  - 0 (Immunoglobulin Variable Region)
RN  - 101839-44-5 (ganglioside GD1alpha)
RN  - 37758-47-7 (G(M1) Ganglioside)
RN  - 59247-13-1 (trisialoganglioside GT1)
RN  - EC 2.4.99.- (Sialyltransferases)
RN  - EC 2.4.99.8 (alpha-N-acetylneuraminate alpha-2,8-sialyltransferase)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Antibodies, Monoclonal/*biosynthesis/metabolism
MH  - Antibody Specificity
MH  - Binding Sites, Antibody
MH  - G(M1) Ganglioside/analogs & derivatives/immunology/metabolism
MH  - Gangliosides/administration & dosage/*immunology/metabolism
MH  - *Gene Rearrangement, B-Lymphocyte, Heavy Chain
MH  - *Gene Rearrangement, B-Lymphocyte, Light Chain
MH  - Immunoglobulin Variable Region/biosynthesis/*genetics/metabolism
MH  - Male
MH  - Mice
MH  - Mice, Inbred C57BL
MH  - Mice, Knockout
MH  - Molecular Sequence Data
MH  - Sialyltransferases/deficiency/genetics
MH  - Surface Plasmon Resonance
EDAT- 2005/06/22 09:00
MHDA- 2005/09/09 09:00
CRDT- 2005/06/22 09:00
PHST- 2005/03/15 00:00 [received]
PHST- 2005/04/22 00:00 [accepted]
PHST- 2005/06/22 09:00 [pubmed]
PHST- 2005/09/09 09:00 [medline]
PHST- 2005/06/22 09:00 [entrez]
AID - S0165-5728(05)00163-3 [pii]
AID - 10.1016/j.jneuroim.2005.04.011 [doi]
PST - ppublish
SO  - J Neuroimmunol. 2005 Aug;165(1-2):92-103. doi: 10.1016/j.jneuroim.2005.04.011.

PMID- 9545556
OWN - NLM
STAT- MEDLINE
DCOM- 19980512
LR  - 20170915
IS  - 0006-3002 (Print)
IS  - 0006-3002 (Linking)
VI  - 1406
IP  - 1
DP  - 1998 Feb 27
TI  - Repressed beta-1,3-galactosyltransferase in the Tn syndrome.
PG  - 115-25
AB  - The human hematopoietic disorder named Tn syndrome has been ascribed to an
      acquired stem cell mutation resulting in loss of beta-1,3-galactosyltransferase
      activity in affected Tn+ cells of the hematopoietic lineages. Recently, we could 
      demonstrate that this deficiency is due to a repression of a functional allele of
      the beta-1,3-Gal-T gene since treatment of Tn+ T-lymphocytes from a patient
      (R.R.) afflicted with the Tn-syndrome with 5-azacytidine or Na n-butyrate
      resulted in re-expression of the Thomsen-Friedenreich (TF) antigen, the product
      of beta-1,3-Gal-T activity [M. Thurnher, S. Rusconi, E.G. Berger. Persistent
      repression of functional allele can be responsible for galactosyltransferase
      deficiency in Tn syndrome. J. Clin. Invest. 91 (1993) 2103-2110]. To reduce these
      observations to a common pathogenetic mechanism responsible for the Tn-syndrome, 
      more Tn patients need to be investigated. Here, we describe similar Tn+
      T-lymphocytes cultured ex vivo from patient M.Z. whose Tn+ syndrome was newly
      recognized. Tn+ and TF+ T-lymphocyte cultures were characterized by flow
      cytometry and measurement of beta-1,3-Gal-T and shown to be deficient in Tn+
      cells. Furthermore, Tn+ cells were treated with 5-azacytidine and Na n-butyrate
      as described before. Reoccurrence of beta-1,3-Gal-T activity dependent epitopes
      on the cell surface of Tn+ cells was shown by flow cytometry. These support the
      notion of beta-1,3-Gal-T gene repression as a common pathogenetic mechanism
      underlying the Tn-syndrome.
FAU - Felner, K M
AU  - Felner KM
AD  - Institute of Physiology, University of Zurich, Switzerland.
FAU - Dinter, A
AU  - Dinter A
FAU - Cartron, J P
AU  - Cartron JP
FAU - Berger, E G
AU  - Berger EG
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - Netherlands
TA  - Biochim Biophys Acta
JT  - Biochimica et biophysica acta
JID - 0217513
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Biomarkers)
RN  - 0 (Tn antigen)
RN  - 3554-90-3 (Thomsen-Friedenreich antigen)
RN  - EC 2.4.1.- (Galactosyltransferases)
SB  - IM
MH  - Antigens, Tumor-Associated, Carbohydrate/*biosynthesis/*genetics/immunology
MH  - Biomarkers
MH  - Galactosyltransferases/*genetics
MH  - *Gene Expression Regulation, Enzymologic
MH  - Hematologic Diseases/*enzymology/*genetics/immunology
MH  - Humans
MH  - Syndrome
EDAT- 1998/04/18 00:00
MHDA- 1998/04/18 00:01
CRDT- 1998/04/18 00:00
PHST- 1998/04/18 00:00 [pubmed]
PHST- 1998/04/18 00:01 [medline]
PHST- 1998/04/18 00:00 [entrez]
AID - S0925-4439(97)00090-2 [pii]
PST - ppublish
SO  - Biochim Biophys Acta. 1998 Feb 27;1406(1):115-25.

PMID- 17823742
OWN - NLM
STAT- MEDLINE
DCOM- 20080514
LR  - 20160815
IS  - 0104-4230 (Print)
IS  - 0104-4230 (Linking)
VI  - 53
IP  - 4
DP  - 2007 Jul-Aug
TI  - [Relationship of the sialomucins (Tn and Stn antigens) with adenocarcinoma in
      Barrett's esophagus].
PG  - 360-4
AB  - OBJECTIVE: Barrett's esophagus (BE) is a consequence of chronic gastroesophageal 
      reflux and is considered a risk factor for adenocarcinoma. The study of the
      mucus, especially acid mucins, such as the sialomucins in the goblet cells which 
      characterize BE, showed that in intestinal metaplasia, frequent in the digestive 
      tract, the organ's original epithelium could express Tn and Stn antigens. These
      antigens have already been detected in gastric and colonic tumors, however
      references in BE were not found. This research aimed to analyze these antigens in
      patients with BE and in adenocarcinoma associated with BE. METHODS: Utilizing
      immunohistochemistry tests, Tn and Stn antigens were studied in the endoscopic
      biopsies of 29 patients with BE and seven with adenocarcinoma in BE, as well as
      eight individuals with normal esophageal epithelium at upper digestive endoscopy.
      RESULTS: The Stn antigen was positive in the goblet cells of patients with BE in 
      100% of the cases and the Tn was positive in 48%. In the columnar cells, Stn was 
      always negative, while Tn was positive in 100% of the cases. However, in
      adenocarcinoma in BE, both antigens were 100% positive. In normal individuals,
      the Tn antigen was positive and the antigen Stn negative in all cases.
      CONCLUSION: It is probable that the BE group in which the Tn antigens in the
      goblet cells are positive, similarly to the same antigen in the adenocarcinoma
      group, might indicate a higher susceptibility for potential occurrence of cancer.
      In the future, trials with sialomucins could be used routinely, thereby
      contributing as a prognostic factor of adenocarcinoma in BE.
FAU - de Faria, Plinio Conte Jr
AU  - de Faria PC Jr
AD  - Departamento de Cirurgia e Gastrocentro, Faculdade de Ciencias Medicas da
      PUCCAMP, Unicamp, Campinas, SP. apmdefaria@uol.com.br
FAU - Andreollo, Nelson Adami
AU  - Andreollo NA
FAU - Trevisan, Miriam Aparecida da Silva
AU  - Trevisan MA
FAU - Lopes, Luiz Roberto
AU  - Lopes LR
LA  - por
PT  - English Abstract
PT  - Journal Article
TT  - A inter-relacao das sialomucinas (antigenos Tn e Stn) com o adenocarcinoma no
      esofago de Barrett.
PL  - Brazil
TA  - Rev Assoc Med Bras (1992)
JT  - Revista da Associacao Medica Brasileira (1992)
JID - 9308586
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Biomarkers, Tumor)
RN  - 0 (Sialomucins)
RN  - 0 (Tn antigen)
RN  - 0 (sialosyl-Tn antigen)
SB  - IM
MH  - Adenocarcinoma/etiology/*immunology/pathology
MH  - Adult
MH  - Aged
MH  - Antigens, Tumor-Associated, Carbohydrate/analysis
MH  - Barrett Esophagus/complications/*immunology/pathology
MH  - Biomarkers, Tumor/analysis
MH  - Biopsy
MH  - Case-Control Studies
MH  - Endoscopy, Gastrointestinal
MH  - Esophageal Neoplasms/etiology/*immunology/pathology
MH  - Esophagus/immunology
MH  - Female
MH  - Humans
MH  - Immunohistochemistry
MH  - Male
MH  - Middle Aged
MH  - Sialomucins/*analysis/immunology
EDAT- 2007/09/08 09:00
MHDA- 2008/05/15 09:00
CRDT- 2007/09/08 09:00
PHST- 2007/01/23 00:00 [received]
PHST- 2007/04/24 00:00 [accepted]
PHST- 2007/09/08 09:00 [pubmed]
PHST- 2008/05/15 09:00 [medline]
PHST- 2007/09/08 09:00 [entrez]
AID - S0104-42302007000400024 [pii]
PST - ppublish
SO  - Rev Assoc Med Bras (1992). 2007 Jul-Aug;53(4):360-4.

PMID- 9385079
OWN - NLM
STAT- MEDLINE
DCOM- 19971216
LR  - 20061115
IS  - 1385-299X (Print)
IS  - 1385-299X (Linking)
VI  - 1
IP  - 2
DP  - 1997 May
TI  - An immunohistochemical technique with a series of monoclonal antibodies to
      gangliosides: their differential distribution in the rat cerebellum.
PG  - 152-6
AB  - Gangliosides, sialic acid-containing glycosphingolipids, are normal membrane
      constituents and are highly expressed in the vertebral central nervous system.
      Owing to their topological localization on the outer surface of neural plasma
      membranes and their unique chemical structure, gangliosides have been implicated 
      in a variety of phenomena. It was, however, difficult to study the localization
      of gangliosides in the central nervous system because of the lack of useful
      probes for gangliosides. We recently established an improved method for the
      generation of mouse MAbs to gangliosides by immunizing C3H/HeN mice with purified
      gangliosides. Using this method, we succeeded in generating a large number of the
      MAbs specific for gangliosides. These MAbs enabled us to determine the
      localization of gangliosides in the rat brain. We previously described the
      differential distribution patterns of gangliosides in the brain regions by an
      immunohistochemical technique with MAbs. In the present paper, we describe an
      immunofluorescence technique for the detection of ganglioside distribution in the
      postnatal rat cerebellar cortex in detail. The principles of immunohistochemistry
      have been described in several review articles.
FAU - Kotani, M
AU  - Kotani M
AD  - Department of Tumor Immunology, Tokyo Metropolitan Institute of Medical Science, 
      Japan.
FAU - Tai, T
AU  - Tai T
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - Netherlands
TA  - Brain Res Brain Res Protoc
JT  - Brain research. Brain research protocols
JID - 9716650
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Gangliosides)
SB  - IM
MH  - Animals
MH  - Animals, Newborn/metabolism
MH  - Antibodies, Monoclonal/*immunology
MH  - Cerebellum/*metabolism
MH  - Female
MH  - *Fluorescent Antibody Technique, Indirect
MH  - Gangliosides/*immunology/*metabolism
MH  - Rats
MH  - Rats, Wistar
MH  - Tissue Distribution
EDAT- 1997/05/01 00:00
MHDA- 1997/12/31 00:01
CRDT- 1997/05/01 00:00
PHST- 1997/05/01 00:00 [pubmed]
PHST- 1997/12/31 00:01 [medline]
PHST- 1997/05/01 00:00 [entrez]
AID - S1385-299X(96)00025-6 [pii]
PST - ppublish
SO  - Brain Res Brain Res Protoc. 1997 May;1(2):152-6.

PMID- 16252298
OWN - NLM
STAT- MEDLINE
DCOM- 20061122
LR  - 20151119
IS  - 1439-4227 (Print)
IS  - 1439-4227 (Linking)
VI  - 6
IP  - 12
DP  - 2005 Dec
TI  - Carbohydrate array analysis of anti-Tn antibodies and lectins reveals unexpected 
      specificities: implications for diagnostic and vaccine development.
PG  - 2229-41
AB  - The Tn antigen is a carbohydrate antigen expressed in most carcinomas, during
      embryogenesis, on pathogenic parasites, and on HIV. It has been evaluated
      extensively as a potential diagnostic marker and several Tn-based vaccines are in
      clinical trials. Based on discrepancies in the literature regarding Tn
      expression, we began to question whether antibodies and lectins used routinely to
      detect the Tn antigen were providing accurate information. To investigate this
      possibility, a carbohydrate microarray and a highly sensitive assay were
      developed and three frequently used Tn receptors (HBTn1, Bric111, and VVL-B4)
      were evaluated. Carbohydrate-array analysis revealed unexpected cross-reactivity 
      with other human carbohydrate epitopes. VVL-B4 bound the Tn antigen,
      GalNAcalpha1-6Gal, and GalNAcalpha1-3Gal. Bric111 bound the Tn antigen, blood
      group A, GalNAcalpha1-6Gal, and GalNAcalpha1-3Gal. HBTn1 showed the best
      selectivity, but still displayed moderate binding to blood group A. Implications 
      for the development of Tn-based diagnostics and vaccines are discussed.
FAU - Manimala, Joseph C
AU  - Manimala JC
AD  - Laboratory of Medicinal Chemistry, Center for Cancer Research, NCI-Frederick, 376
      Boyles Street, Building 376, Room109, Frederick, MD 21702, USA.
FAU - Li, Zhitao
AU  - Li Z
FAU - Jain, Amit
AU  - Jain A
FAU - VedBrat, Sharanjeet
AU  - VedBrat S
FAU - Gildersleeve, Jeffrey C
AU  - Gildersleeve JC
LA  - eng
GR  - Intramural NIH HHS/United States
PT  - Journal Article
PT  - Research Support, N.I.H., Intramural
PL  - Germany
TA  - Chembiochem
JT  - Chembiochem : a European journal of chemical biology
JID - 100937360
RN  - 0 (Antibodies)
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Carbohydrates)
RN  - 0 (Lectins)
RN  - 0 (Tn antigen)
RN  - 0 (Vaccines)
SB  - IM
MH  - Antibodies/*analysis
MH  - Antigens, Tumor-Associated, Carbohydrate/*immunology
MH  - *Carbohydrates
MH  - Diagnostic Techniques and Procedures
MH  - Enzyme-Linked Immunosorbent Assay/methods/standards
MH  - Humans
MH  - Lectins/*analysis
MH  - Microarray Analysis
MH  - Sensitivity and Specificity
MH  - Vaccines
EDAT- 2005/10/28 09:00
MHDA- 2006/12/09 09:00
CRDT- 2005/10/28 09:00
PHST- 2005/10/28 09:00 [pubmed]
PHST- 2006/12/09 09:00 [medline]
PHST- 2005/10/28 09:00 [entrez]
AID - 10.1002/cbic.200500165 [doi]
PST - ppublish
SO  - Chembiochem. 2005 Dec;6(12):2229-41. doi: 10.1002/cbic.200500165.

PMID- 8542587
OWN - NLM
STAT- MEDLINE
DCOM- 19960213
LR  - 20041117
IS  - 0008-5472 (Print)
IS  - 0008-5472 (Linking)
VI  - 56
IP  - 2
DP  - 1996 Jan 15
TI  - Expression of alpha-1,3-fucosyltransferase type IV and VII genes is related to
      poor prognosis in lung cancer.
PG  - 325-9
AB  - To date, five alpha-1,3-fucosyltransferase genes (Fuc-TIII, IV, V, VI, and VII)
      have been cloned. To examine the role of alpha-1,3-fucosyltransferase in the
      synthesis of sialyl Lewis x and the prognosis of lung cancer, PCR amplification
      of five fucosyltransferase genes and immunohistochemical staining of sialyl Lewis
      x were performed in 333 patients with lung cancer who underwent surgical
      resection from 1980 to 1993. The frequencies of Fuc-TIII/V, Fuc-TVI, Fuc-TIV, and
      Fuc-TVII expression were 9%, 26%, 75%, and 66%, respectively. The frequency of
      sialyl Lewis x expression (75%) was comparable to Fuc-TIV and Fuc-TVII
      expression. However, the grading of sialyl Lewis x staining correlated only with 
      the grading of Fuc-TVII gene amplification. Survival of the patients whose tumors
      showed strong expression of Fuc-TIV and/or FucT-VII was significantly shorter
      than that of the patients whose tumors did not express either Fuc-TIV or
      Fuc-TVII. These results suggest that Fuc-TIV and Fuc-TVII expression may be of
      prognostic value among patients with lung cancer by participating in the
      biosynthesis of sialyl Lewis x.
FAU - Ogawa, J
AU  - Ogawa J
AD  - First Department of Surgery, School of Medicine, Tokai University, Kanagawa,
      Japan.
FAU - Inoue, H
AU  - Inoue H
FAU - Koide, S
AU  - Koide S
LA  - eng
PT  - Journal Article
PL  - United States
TA  - Cancer Res
JT  - Cancer research
JID - 2984705R
RN  - 0
      (5-acetylneuraminyl-(2-3)-galactosyl-(1-4)-(fucopyranosyl-(1-3))-N-acetylglucosam
      ine)
RN  - 0 (DNA, Neoplasm)
RN  - 0 (Oligosaccharides)
RN  - EC 2.4.1.- (Fucosyltransferases)
RN  - EC 2.4.1.152 (galactoside 3-fucosyltransferase)
SB  - IM
MH  - Adult
MH  - Aged
MH  - Aged, 80 and over
MH  - Base Sequence
MH  - DNA, Neoplasm/genetics
MH  - Female
MH  - Fucosyltransferases/analysis/biosynthesis/*genetics
MH  - Gene Expression
MH  - Humans
MH  - Immunohistochemistry
MH  - Lung Neoplasms/*enzymology/*genetics
MH  - Male
MH  - Middle Aged
MH  - Molecular Sequence Data
MH  - Oligosaccharides/analysis
MH  - Prognosis
EDAT- 1996/01/15 00:00
MHDA- 1996/01/15 00:01
CRDT- 1996/01/15 00:00
PHST- 1996/01/15 00:00 [pubmed]
PHST- 1996/01/15 00:01 [medline]
PHST- 1996/01/15 00:00 [entrez]
PST - ppublish
SO  - Cancer Res. 1996 Jan 15;56(2):325-9.

PMID- 7334007
OWN - NLM
STAT- MEDLINE
DCOM- 19820527
LR  - 20190512
IS  - 0021-924X (Print)
IS  - 0021-924X (Linking)
VI  - 90
IP  - 6
DP  - 1981 Dec
TI  - Presence of asialo GM1 and glucosylceramide in the intestinal mucosa of mice and 
      induction of fucosyl asialo GM1 by conventionalization of germ-free mice.
PG  - 1731-8
AB  - Two major neutral glycolipids of the intestinal mucosa were purified by a series 
      of column chromatographies and the structures were determined to be
      glucosylceramide and asialo GM1 by gas liquid chromatography. The carbohydrate
      structure of asialo GM1 was also confirmed from the reactivity of the glycolipid 
      to rabbit anti-asialo GM1 antibody by an enzyme linked-immunosorbent antibody.
      The ceramide portion of both glycolipids had an extremely hydrophilic nature and 
      more than 90% of the ceramide was composed of phytosphingosine and alpha-hydroxy 
      fatty acids. In the previous paper we reported that the induction of a fucolipid 
      in the microvillus membrane of mouse intestinal mucosa by conventionalization was
      observed on monitoring the incorporation of radiolabeled fucose in vivo. A
      fucoglycolipid having the same mobility on an autoradiogram as the fucolipid
      labeled in vivo was produced by in vitro incubation of intestinal asialo GM1 and 
      GDP-[14C]fucose with the mucosal homogenates. Moreover, asialo GM1 prepared from 
      brain gangliosides exhibited a similar ability to accept fucose and it was
      converted to fucosyl asialo GM1 which moved faster than the product from
      intestinal asialo GM1. The difference is considered to be due to the ceramide
      composition. These results suggest that conventionalization can induce the
      fucosyl asialo GM1 in the microvillus membrane probably through the induction of 
      fucosyltransferase. Understanding the molecular mechanism of interaction between 
      the physiological flora and host is the matter of further study.
FAU - Umesaki, Y
AU  - Umesaki Y
FAU - Suzuki, A
AU  - Suzuki A
FAU - Kasama, T
AU  - Kasama T
FAU - Tohyama, K
AU  - Tohyama K
FAU - Mutai, M
AU  - Mutai M
FAU - Yamakawa, T
AU  - Yamakawa T
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - J Biochem
JT  - Journal of biochemistry
JID - 0376600
RN  - 0 (Cerebrosides)
RN  - 0 (Glucosylceramides)
RN  - 0 (Glycolipids)
RN  - 0 (Glycosphingolipids)
RN  - 37758-47-7 (G(M1) Ganglioside)
RN  - EC 2.4.1.- (Fucosyltransferases)
SB  - IM
MH  - Animals
MH  - Cerebrosides/*analysis
MH  - Fucosyltransferases/metabolism
MH  - G(M1) Ganglioside/analysis
MH  - *Germ-Free Life
MH  - Glucosylceramides/*analysis
MH  - Glycolipids/*analysis/metabolism
MH  - Glycosphingolipids/*analysis
MH  - Intestinal Mucosa/*analysis
MH  - Mice
EDAT- 1981/12/01 00:00
MHDA- 1981/12/01 00:01
CRDT- 1981/12/01 00:00
PHST- 1981/12/01 00:00 [pubmed]
PHST- 1981/12/01 00:01 [medline]
PHST- 1981/12/01 00:00 [entrez]
AID - 10.1093/oxfordjournals.jbchem.a133650 [doi]
PST - ppublish
SO  - J Biochem. 1981 Dec;90(6):1731-8. doi: 10.1093/oxfordjournals.jbchem.a133650.

PMID- 107170
OWN - NLM
STAT- MEDLINE
DCOM- 19790629
LR  - 20061115
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 254
IP  - 9
DP  - 1979 May 10
TI  - Characterization of a blood group I-active ganglioside. Structural requirements
      for I and i specificities.
PG  - 3221-8
FAU - Watanabe, K
AU  - Watanabe K
FAU - Hakomori, S I
AU  - Hakomori SI
FAU - Childs, R A
AU  - Childs RA
FAU - Feizi, T
AU  - Feizi T
LA  - eng
PT  - Journal Article
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Blood Group Antigens)
RN  - 0 (Carbohydrates)
RN  - 0 (Cerebrosides)
RN  - 0 (Gangliosides)
RN  - 0 (Glycolipids)
RN  - 0 (I Blood-Group System)
RN  - EC 3.2.1.23 (beta-Galactosidase)
SB  - IM
MH  - Animals
MH  - *Blood Group Antigens
MH  - Carbohydrates/analysis
MH  - Cattle
MH  - Cerebrosides/blood
MH  - Escherichia/enzymology
MH  - *Gangliosides/blood
MH  - Glycolipids/blood
MH  - Humans
MH  - *I Blood-Group System
MH  - Molecular Conformation
MH  - beta-Galactosidase
EDAT- 1979/05/10 00:00
MHDA- 1979/05/10 00:01
CRDT- 1979/05/10 00:00
PHST- 1979/05/10 00:00 [pubmed]
PHST- 1979/05/10 00:01 [medline]
PHST- 1979/05/10 00:00 [entrez]
PST - ppublish
SO  - J Biol Chem. 1979 May 10;254(9):3221-8.

PMID- 7841802
OWN - NLM
STAT- MEDLINE
DCOM- 19950309
LR  - 20181113
IS  - 0282-0080 (Print)
IS  - 0282-0080 (Linking)
VI  - 11
IP  - 3
DP  - 1994 Jun
TI  - Coexpression of cancer-associated carbohydrate antigens, Tn and sialyl Tn.
PG  - 262-5
AB  - The expression of cancer-associated antigens, Tn and sialyl Tn, was examined
      using monoclonal antibodies, MLS 128 and MLS 102, recognizing these two antigens,
      respectively. A cell lysate from a human carcinoma cell line, LS 180 cells, was
      analysed by Western blotting using these two antibodies. Three glycoprotein bands
      were discernible with each antibody, of which two, corresponding to 250 and 210
      kDa, were reactive with both the antibodies. LS 180 cells were metabolically
      labelled with 3H-glucosamine and then the lysate from these cells was applied to 
      two immunoaffinity columns. Sixty-five per cent of the Tn antigenic
      glycoproteins, based on radioactivity, bound to the MLS 102 affinity column. On
      the other hand, 45% of the sialyl Tn antigenic glycoproteins bound to the MLS 128
      affinity column. These results indicate that some Tn and sialyl Tn antigens were 
      expressed on the same polypeptide chains. The presence of non-sialylated GalNAc
      residues on the polypeptide chain with many Sia-GalNAc residues appears to be due
      to the incapability of three consecutive moieties of GalNAc-Ser/Thr to accept
      sialic acid.
FAU - Nakada, H
AU  - Nakada H
AD  - Department of Biotechnology, Faculty of Engineering, Kyoto Sangyo University,
      Japan.
FAU - Inoue, M
AU  - Inoue M
FAU - Tanaka, N
AU  - Tanaka N
FAU - Yamashina, I
AU  - Yamashina I
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Glycoconj J
JT  - Glycoconjugate journal
JID - 8603310
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Sialic Acids)
RN  - 0 (Tn antigen)
RN  - 0 (sialosyl-Tn antigen)
RN  - GZP2782OP0 (N-Acetylneuraminic Acid)
SB  - IM
MH  - Antigens, Tumor-Associated, Carbohydrate/*biosynthesis/immunology/isolation &
      purification
MH  - Blotting, Western
MH  - Carbohydrate Sequence
MH  - Chromatography, Affinity/methods
MH  - Colorectal Neoplasms/immunology
MH  - Electrophoresis, Polyacrylamide Gel
MH  - Humans
MH  - Molecular Sequence Data
MH  - N-Acetylneuraminic Acid
MH  - Sialic Acids
MH  - Tumor Cells, Cultured
EDAT- 1994/06/01 00:00
MHDA- 1994/06/01 00:01
CRDT- 1994/06/01 00:00
PHST- 1994/06/01 00:00 [pubmed]
PHST- 1994/06/01 00:01 [medline]
PHST- 1994/06/01 00:00 [entrez]
PST - ppublish
SO  - Glycoconj J. 1994 Jun;11(3):262-5.

PMID- 8417827
OWN - NLM
STAT- MEDLINE
DCOM- 19930203
LR  - 20141120
IS  - 0008-5472 (Print)
IS  - 0008-5472 (Linking)
VI  - 53
IP  - 2
DP  - 1993 Jan 15
TI  - BR96 sFv-PE40, a potent single-chain immunotoxin that selectively kills carcinoma
      cells.
PG  - 334-9
AB  - We have constructed a single-chain immunotoxin composed of the carcinoma-reactive
      antibody BR96 and a truncated form of Pseudomonas exotoxin. The chimeric
      molecule, BR96 sFv-PE40, was expressed in Escherichia coli and localized to the
      inclusion bodies. We purified and identified two species of BR96 sFv-PE40,
      monomers and aggregates. The monomeric form was able to bind well to the BR96
      antigen, a Lewisy-related antigen, while the aggregate was not. The binding
      affinity of the monomeric recombinant immunotoxin was 5-fold less than intact
      BR96 IgG, and its specificity for the BR96 antigen was confirmed by competition
      analysis. Monomeric BR96 sFv-PE40 was found to be extremely cytotoxic against
      cancer cells displaying the BR96 antigen. The cytotoxicity of the fusion protein 
      correlates directly with antigen density on the tumor cell lines tested. The
      breast carcinoma cell line MCF-7, which has the highest density of BR96 antigen, 
      was the most sensitive to BR96 sFv-PE40, with a concentration producing 50%
      protein synthesis inhibition of 5 pM. BR96 sFv-PE40 was found to have a t1/2 in
      serum of 28.5 min in athymic mice, compared to that of the chemical conjugate,
      chiBR96-LysPE40, which was 54 min. These data indicate that the single-chain
      immunotoxin BR96 sFv-PE40 is a potent inhibitor of protein synthesis in target
      cell lines and may be an effective agent for the treatment of cancer.
FAU - Friedman, P N
AU  - Friedman PN
AD  - Bristol-Myers Squibb Pharmaceutical Research Institute, Molecular Immunology
      Department, Seattle, WA 98121.
FAU - McAndrew, S J
AU  - McAndrew SJ
FAU - Gawlak, S L
AU  - Gawlak SL
FAU - Chace, D
AU  - Chace D
FAU - Trail, P A
AU  - Trail PA
FAU - Brown, J P
AU  - Brown JP
FAU - Siegall, C B
AU  - Siegall CB
LA  - eng
PT  - Journal Article
PL  - United States
TA  - Cancer Res
JT  - Cancer research
JID - 2984705R
RN  - 0 (Antibodies, Neoplasm)
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Bacterial Toxins)
RN  - 0 (Exotoxins)
RN  - 0 (Immunotoxins)
RN  - 0 (Lewis Blood-Group System)
RN  - 0 (Oligonucleotides)
RN  - 0 (Recombinant Fusion Proteins)
RN  - 0 (Virulence Factors)
RN  - EC 2.4.2.- (ADP Ribose Transferases)
RN  - EC 2.4.2.31 (toxA protein, Pseudomonas aeruginosa)
SB  - IM
MH  - *ADP Ribose Transferases
MH  - Antibodies, Neoplasm/chemistry
MH  - Antigens, Tumor-Associated, Carbohydrate/immunology
MH  - *Bacterial Toxins
MH  - Base Sequence
MH  - Breast Neoplasms/immunology/therapy
MH  - Carcinoma/immunology/therapy
MH  - Cloning, Molecular
MH  - Exotoxins/chemistry
MH  - Humans
MH  - *Immunotoxins/metabolism
MH  - In Vitro Techniques
MH  - Lewis Blood-Group System/immunology
MH  - Metabolic Clearance Rate
MH  - Molecular Sequence Data
MH  - Oligonucleotides/chemistry
MH  - *Recombinant Fusion Proteins/metabolism
MH  - Tumor Cells, Cultured
MH  - *Virulence Factors
EDAT- 1993/01/15 00:00
MHDA- 1993/01/15 00:01
CRDT- 1993/01/15 00:00
PHST- 1993/01/15 00:00 [pubmed]
PHST- 1993/01/15 00:01 [medline]
PHST- 1993/01/15 00:00 [entrez]
PST - ppublish
SO  - Cancer Res. 1993 Jan 15;53(2):334-9.

PMID- 1724444
OWN - NLM
STAT- MEDLINE
DCOM- 19920403
LR  - 20190510
IS  - 0021-924X (Print)
IS  - 0021-924X (Linking)
VI  - 110
IP  - 6
DP  - 1991 Dec
TI  - Production of monoclonal antibodies specific for ganglioside GD3.
PG  - 889-95
AB  - Four kinds of anti-GD3 monoclonal antibodies, DSG-1, -2, -3, and -4, of the IgM
      class were obtained by the immunization of BALB/c mice with enzootic bovine
      leukosis tumor tissue-derived ganglioside GD3 inserted into liposomes with
      Salmonella minnesota R595 lipopolysaccharides. The specificities of the
      monoclonal antibodies obtained were defined by complement-dependent liposome
      immune lysis assay and by enzyme immunostaining on thin-layer chromatography. The
      reactivities of the monoclonal antibodies obtained to four ganglioside GD3
      variants [GD3(NeuAc-NeuAc), GD3(NeuAc-NeuGc), GD3(NeuGc-NeuAc), and
      GD3(NeuGc-NeuGc)] were tested. All of the monoclonal antibodies were found to
      react with GD3(NeuAc-NeuAc) and GD3(NeuAc-NeuGc) but not with GD3(NeuGc-NeuAc) or
      GD3(NeuGc-NeuGc). Furthermore, various purified glycosphingolipids were used to
      determine the specificity of these monoclonal antibodies. All 4 antibodies
      reacted only with ganglioside GD3 [GD3(NeuAc-NeuAc) and GD3(NeuAc-NeuGc)], but
      not with several gangliosides linking the GalNAc, Gal beta 1-3GalNAc, NeuAc alpha
      2-3Gal beta 1-3GalNAc, or NeuAc alpha 2-8NeuAc alpha 2-3Gal beta 1-3GalNAc
      residue to the Gal moiety of ganglioside GD3 (GD2, GD1b, GT1b, or GQ1b,
      respectively), ganglioside GT1a having the same terminal NeuAc alpha 2-8NeuAc
      alpha 2-3Gal residue as ganglioside GD3, other gangliosides, and neutral
      glycosphingolipids. These findings suggest that the 4 monoclonal antibodies
      obtained may be specific for the epitope of NeuAc-alpha 2-8Sia alpha 2-3Gal beta 
      1-4Glc residue of ganglioside GD3.
FAU - Watarai, S
AU  - Watarai S
AD  - Department of Cell Chemistry, Okayama University Medical School.
FAU - Onuma, M
AU  - Onuma M
FAU - Yasuda, T
AU  - Yasuda T
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - J Biochem
JT  - Journal of biochemistry
JID - 0376600
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Epitopes)
RN  - 0 (Gangliosides)
RN  - 0 (Liposomes)
RN  - 62010-37-1 (ganglioside, GD3)
SB  - IM
MH  - Animals
MH  - *Antibodies, Monoclonal/biosynthesis
MH  - Antibody Specificity
MH  - Carbohydrate Sequence
MH  - Epitopes/chemistry
MH  - Gangliosides/chemistry/*immunology
MH  - Immunization
MH  - Liposomes
MH  - Mice
MH  - Mice, Inbred BALB C
MH  - Molecular Sequence Data
EDAT- 1991/12/01 00:00
MHDA- 1991/12/01 00:01
CRDT- 1991/12/01 00:00
PHST- 1991/12/01 00:00 [pubmed]
PHST- 1991/12/01 00:01 [medline]
PHST- 1991/12/01 00:00 [entrez]
AID - 10.1093/oxfordjournals.jbchem.a123685 [doi]
PST - ppublish
SO  - J Biochem. 1991 Dec;110(6):889-95. doi: 10.1093/oxfordjournals.jbchem.a123685.

PMID- 11465993
OWN - NLM
STAT- MEDLINE
DCOM- 20010809
LR  - 20061115
IS  - 0014-4894 (Print)
IS  - 0014-4894 (Linking)
VI  - 98
IP  - 2
DP  - 2001 Jun
TI  - O-glycosylation in Echinococcus granulosus: identification and characterization
      of the carcinoma-associated Tn antigen.
PG  - 100-9
AB  - In the present work we demonstrate that the cancer-associated O-glycosylated Tn
      antigen (GalNAc-O-Ser/Thr) is expressed by the cestode Echinococcus granulosus.
      This antigen was detected in both larval and adult worm extracts, with the
      highest specific activity observed in the adult excretion/secretion preparation. 
      Histochemical analysis showed that Tn is preferentially expressed in the
      parenchyma in both parasite stages and the external part of tegument in adult
      worms. A similar pattern was observed for sialyl-Tn, a related O-linked antigen. 
      Tn glycoproteins from protoscoleces were resolved by SDS-PAGE in two main
      components of 43 and 49 kDa. After purification, this material was reactive with 
      lectins which bind GlcNAc/sialic acid, GalNAc, and T antigen. In a preliminary
      evaluation, high levels of Tn antigen were detected in serum samples from
      patients with hydatid cyst, suggesting that the measure of Tn in serum could be a
      biomarker of this disease, although extensive work is necessary in order to
      determine the clinical usefulness of this assay. The results reported here, the
      first evidence of O-glycosylation pathways in E. granulosus and the presence of
      Tn antigen in cestodes, suggest that the evaluation of O-glycosylated antigens
      might give new insights in the host-parasite relationship.
CI  - Copyright 2001 Academic Press.
FAU - Alvarez Errico, D
AU  - Alvarez Errico D
AD  - Depto. de Bioquimica, Facultad de Medicina, Montevideo, Uruguay.
FAU - Medeiros, A
AU  - Medeiros A
FAU - Miguez, M
AU  - Miguez M
FAU - Casaravilla, C
AU  - Casaravilla C
FAU - Malgor, R
AU  - Malgor R
FAU - Carmona, C
AU  - Carmona C
FAU - Nieto, A
AU  - Nieto A
FAU - Osinaga, E
AU  - Osinaga E
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Exp Parasitol
JT  - Experimental parasitology
JID - 0370713
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Lectins)
RN  - 0 (Tn antigen)
SB  - IM
MH  - Adult
MH  - Animals
MH  - Antigens, Tumor-Associated, Carbohydrate/blood/*isolation &
      purification/metabolism
MH  - Blotting, Western
MH  - Breast Neoplasms/blood/immunology
MH  - Chromatography, Affinity
MH  - Dogs
MH  - Echinococcosis/blood/*immunology
MH  - Echinococcus/*immunology/metabolism
MH  - Electrophoresis, Polyacrylamide Gel
MH  - Enzyme-Linked Immunosorbent Assay
MH  - Female
MH  - Fluorescent Antibody Technique
MH  - Glycosylation
MH  - Humans
MH  - Lectins/metabolism
MH  - Male
EDAT- 2001/07/24 10:00
MHDA- 2001/08/10 10:01
CRDT- 2001/07/24 10:00
PHST- 2001/07/24 10:00 [pubmed]
PHST- 2001/08/10 10:01 [medline]
PHST- 2001/07/24 10:00 [entrez]
AID - 10.1006/expr.2001.4620 [doi]
AID - S0014-4894(01)94620-X [pii]
PST - ppublish
SO  - Exp Parasitol. 2001 Jun;98(2):100-9. doi: 10.1006/expr.2001.4620.

PMID- 1567169
OWN - NLM
STAT- MEDLINE
DCOM- 19920519
LR  - 20061115
IS  - 0250-7005 (Print)
IS  - 0250-7005 (Linking)
VI  - 12
IP  - 1
DP  - 1992 Jan-Feb
TI  - Monoclonal antibody 83D4 immunoreactivity in human tissues: cellular distribution
      and microcytophotometric analysis of immunoprecipitates on tissue sections.
PG  - 209-23
AB  - Immunocytochemical assays were performed on cell cultures as well as on a wide
      range of human tissues using a monoclonal antibody, MAb 83D4, produced by a
      murine hybridoma generated by immunization with a cell suspension from a paraffin
      block of human breast carcinoma tissue. Frozen breast tissue samples (n = 49)
      were compared to fixed and paraffin-embedded samples (n = 62). Paraffin sections 
      (n = 194) from a variety of human tissues were compared to breast
      immunoreactivity. Immunoprecipitates, resulting from positive reactions between
      83D4 and Avidin Biotin Peroxidase, were evaluated by computer-assisted
      microcytophotometry (SAMBA). In some frozen breast samples (n = 27), 83D4 antigen
      distribution was correlated with tumor cell DNA index, ploidy balance, growth
      fraction (Ki67), hormone receptor (ER, PR) antigenic sites, NORsAg and
      oncoprotein pHER-2/neu cell content. MAb 83D4 reacted with 3 breast cancer cells 
      lines (MCF7, T47D and H466B) but not with normal epithelial breast cells in
      culture. The immunostaining in frozen paraffin sections from breast were similar.
      Like most normal tissues, normal breast did not react with 83D4. Cellular MAb
      83D4 antigen concentration increases with the degree of malignancy but is
      independent of DNA nuclear content, ER, PR, growth fraction and pHER-2neu in
      cancers. These results suggested that routine immunohistochemical procedures
      using MAb 83D4 could facilitate the grading of breast cancer, in particular by
      allowing detection of microvascular invasions in the breast as well as at a
      distance and of blood-born micrometastases, especially in bone marrow.
FAU - Charpin, C
AU  - Charpin C
AD  - Department of Pathology, CHU Timone, Marseille, France.
FAU - Pancino, G
AU  - Pancino G
FAU - Osinaga, E
AU  - Osinaga E
FAU - Bonnier, P
AU  - Bonnier P
FAU - Lavaut, M N
AU  - Lavaut MN
FAU - Allasia, C
AU  - Allasia C
FAU - Roseto, A
AU  - Roseto A
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - Greece
TA  - Anticancer Res
JT  - Anticancer research
JID - 8102988
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens, Neoplasm)
RN  - 0 (Glycoproteins)
RN  - 0 (tumor-associated antigen 72)
SB  - IM
MH  - Antibodies, Monoclonal/*immunology
MH  - Antibody Specificity
MH  - Antigens, Neoplasm/*analysis
MH  - Breast Neoplasms/*immunology
MH  - Carcinoma/*immunology
MH  - Cells, Cultured
MH  - Female
MH  - Glycoproteins/analysis
MH  - Humans
MH  - Precipitin Tests
EDAT- 1992/01/01 00:00
MHDA- 1992/01/01 00:01
CRDT- 1992/01/01 00:00
PHST- 1992/01/01 00:00 [pubmed]
PHST- 1992/01/01 00:01 [medline]
PHST- 1992/01/01 00:00 [entrez]
PST - ppublish
SO  - Anticancer Res. 1992 Jan-Feb;12(1):209-23.

PMID- 16030209
OWN - NLM
STAT- MEDLINE
DCOM- 20050823
LR  - 20181113
IS  - 0021-9193 (Print)
IS  - 0021-9193 (Linking)
VI  - 187
IP  - 15
DP  - 2005 Aug
TI  - Identification of a D-glycero-D-manno-heptosyltransferase gene from Helicobacter 
      pylori.
PG  - 5156-65
AB  - We have identified a Helicobacter pylori d-glycero-d-manno-heptosyltransferase
      gene, HP0479, which is involved in the biosynthesis of the outer core region of
      H. pylori lipopolysaccharide (LPS). Insertional inactivation of HP0479 resulted
      in formation of a truncated LPS molecule lacking an alpha-1,6-glucan-,
      dd-heptose-containing outer core region and O-chain polysaccharide. Detailed
      structural analysis of purified LPS from HP0479 mutants of strains SS1, 26695,
      O:3, and PJ1 by a combination of chemical and mass spectrometric methods showed
      that HP0479 likely encodes alpha-1,2-d-glycero-d-manno-heptosyltransferase, which
      adds a d-glycero-d-manno-heptose residue (DDHepII) to a distal dd-heptose of the 
      core oligosaccharide backbone of H. pylori LPS. When the wild-type HP0479 gene
      was reintegrated into the chromosome of strain 26695 by using an "antibiotic
      cassette swapping" method, the complete LPS structure was restored. Introduction 
      of the HP0479 mutation into the H. pylori mouse-colonizing Sydney (SS1) strain
      and the clinical isolate PJ1, which expresses dd-heptoglycan, resulted in the
      loss of colonization in a mouse model. This indicates that H. pylori expressing a
      deeply truncated LPS is unable to successfully colonize the murine stomach and
      provides evidence for a critical role of the outer core region of H. pylori LPS
      in colonization.
FAU - Hiratsuka, Koji
AU  - Hiratsuka K
AD  - Institute for Biological Sciences, National Research Council of Canada, Ottawa,
      Ontario, Canada.
FAU - Logan, Susan M
AU  - Logan SM
FAU - Conlan, J Wayne
AU  - Conlan JW
FAU - Chandan, Vandana
AU  - Chandan V
FAU - Aubry, Annie
AU  - Aubry A
FAU - Smirnova, Natalia
AU  - Smirnova N
FAU - Ulrichsen, Heather
AU  - Ulrichsen H
FAU - Chan, Kenneth H N
AU  - Chan KH
FAU - Griffith, Douglas W
AU  - Griffith DW
FAU - Harrison, Blair A
AU  - Harrison BA
FAU - Li, Jianjun
AU  - Li J
FAU - Altman, Eleonora
AU  - Altman E
LA  - eng
SI  - GENBANK/AY885679
SI  - GENBANK/AY885680
SI  - GENBANK/AY885681
PT  - Comparative Study
PT  - Journal Article
PL  - United States
TA  - J Bacteriol
JT  - Journal of bacteriology
JID - 2985120R
RN  - 0 (Lipopolysaccharides)
RN  - EC 2.4.- (Glycosyltransferases)
RN  - EC 2.4.99.- (heptosyltransferase)
SB  - IM
MH  - Animals
MH  - Carbohydrate Sequence
MH  - Cloning, Molecular
MH  - Genes, Bacterial
MH  - Glycosyltransferases/*genetics/metabolism
MH  - Helicobacter pylori/*genetics/metabolism/pathogenicity
MH  - Lipopolysaccharides/biosynthesis/chemistry
MH  - Mice
MH  - Molecular Sequence Data
MH  - Mutation
MH  - Sequence Homology
MH  - Stomach/microbiology
MH  - Virulence/genetics
PMC - PMC1196013
EDAT- 2005/07/21 09:00
MHDA- 2005/08/24 09:00
CRDT- 2005/07/21 09:00
PHST- 2005/07/21 09:00 [pubmed]
PHST- 2005/08/24 09:00 [medline]
PHST- 2005/07/21 09:00 [entrez]
AID - 187/15/5156-a [pii]
AID - 10.1128/JB.187.15.5156-5165.2005 [doi]
PST - ppublish
SO  - J Bacteriol. 2005 Aug;187(15):5156-65. doi: 10.1128/JB.187.15.5156-5165.2005.

PMID- 2450649
OWN - NLM
STAT- MEDLINE
DCOM- 19880512
LR  - 20151119
IS  - 0008-5472 (Print)
IS  - 0008-5472 (Linking)
VI  - 48
IP  - 8
DP  - 1988 Apr 15
TI  - Preparation and characterization of monoclonal antibodies directed to the
      tumor-associated O-linked sialosyl-2----6 alpha-N-acetylgalactosaminyl
      (sialosyl-Tn) epitope.
PG  - 2214-20
AB  - Two monoclonal antibodies, TKH1 and TKH2, directed toward the sialosyl-Tn
      structure (NeuAc alpha 2----6GalNAc alpha 1----O-Ser or Thr), which display a
      remarkable immunohistological tumor specificity, were generated by immunization
      with ovine submaxillary mucin. The reactivity of these antibodies was monitored
      by solid phase enzyme-linked immunosorbent assay with different native and
      glycosidase-treated mucins and glycoproteins. Binding of the antibody to ovine
      submaxillary mucin glycoprotein was strongly inhibited by the O-linked
      disaccharide NeuAc alpha 2----6GalNAc alpha 1----O-serine, less strongly by NeuAc
      alpha 2----6GalNAc beta 1----O-propyl, and weakly by the monosaccharide GalNac.
      The reactivity was compared with previously established anti-Tn antibodies B72.3,
      NCC-Lu-35, and NCC-Lu-81. The antibody B72.3 was prepared previously after
      immunization with metastatic breast adenocarcinoma and its epitope was claimed to
      be GalNAc alpha 1----O-Ser (or - Thr) by Springer and associates [Springer, G.F.,
      et al. In: T. Dao, et al. (eds.), Tumor Markers and Their Significance in the
      Management of Breast Cancer, pp. 47-70. New York: A.R. Liss, 1986]. The antibody 
      was found to show very similar reactivity as that of TKH1/TKH2, and its
      reactivity to ovine submaxillary mucin was inhibited specifically by NeuAc alpha 
      2----6GalNAc alpha 1----O-serine, indicating that the antibody is clearly
      directed to sialosyl-Tn antigen. Immunohistological study of the distribution of 
      this antigen in various normal human tissues and carcinomas by TKH1/TKH2
      antibodies, as well as B72.3 and monoclonal antibodies NCC-Lu-35/81, which are
      directed to GalNAc alpha 1----O-Ser or Thr (Tn), was performed. The sialosyl-Tn
      antigen was not found in normal tissue except for a weak expression in Leydig
      cells of the testis, goblet cells of the colon, and parietal cells of the
      stomach. In contrast, the sialosyl-Tn antigen was strongly expressed in a large
      number of adenocarcinomas. As expected from the specificity studies, B72.3 shows 
      the same reactivity as TKH1 and TKH2. Thus, both sialosyl-Tn (NeuAc alpha
      2----6GalNAc alpha 1----O-Ser/Thr) and Tn (GalNAc alpha 1----O-Ser/Thr) are good 
      tumor markers, and combined use of antibodies directed to these structures might 
      be useful in the screening and classification of cancer.
FAU - Kjeldsen, T
AU  - Kjeldsen T
AD  - Department of Pathobiology, University of Washington, Seattle 98119.
FAU - Clausen, H
AU  - Clausen H
FAU - Hirohashi, S
AU  - Hirohashi S
FAU - Ogawa, T
AU  - Ogawa T
FAU - Iijima, H
AU  - Iijima H
FAU - Hakomori, S
AU  - Hakomori S
LA  - eng
GR  - CA42505/CA/NCI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Cancer Res
JT  - Cancer research
JID - 2984705R
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens, Neoplasm)
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Biomarkers, Tumor)
RN  - 0 (Disaccharides)
RN  - 0 (Epitopes)
RN  - 0 (Monosaccharides)
RN  - 0 (Tn antigen)
RN  - 0 (sialosyl-Tn antigen)
SB  - IM
MH  - Animals
MH  - Antibodies, Monoclonal/biosynthesis/*immunology
MH  - Antibody Specificity
MH  - Antigens, Neoplasm/*immunology
MH  - *Antigens, Tumor-Associated, Carbohydrate
MH  - Biomarkers, Tumor/*immunology
MH  - Disaccharides/pharmacology
MH  - Epitopes/*analysis
MH  - Mice
MH  - Mice, Inbred BALB C
MH  - Monosaccharides/pharmacology
EDAT- 1988/04/15 00:00
MHDA- 1988/04/15 00:01
CRDT- 1988/04/15 00:00
PHST- 1988/04/15 00:00 [pubmed]
PHST- 1988/04/15 00:01 [medline]
PHST- 1988/04/15 00:00 [entrez]
PST - ppublish
SO  - Cancer Res. 1988 Apr 15;48(8):2214-20.

PMID- 17694322
OWN - NLM
STAT- MEDLINE
DCOM- 20071207
LR  - 20181113
IS  - 0945-6317 (Print)
IS  - 0945-6317 (Linking)
VI  - 451
IP  - 4
DP  - 2007 Oct
TI  - Changes in the profile of simple mucin-type O-glycans and polypeptide
      GalNAc-transferases in human testis and testicular neoplasms are associated with 
      germ cell maturation and tumour differentiation.
PG  - 805-14
AB  - Testicular germ cell tumours (TGCT) exhibit remarkable ability to differentiate
      into virtually all somatic tissue types. In this study, we investigated changes
      in mucin-type O-glycosylation, which have been associated with somatic cell
      differentiation and cancer. Expression profile of simple mucin-type O-glycans
      (Tn, sialyl-Tn, T), histo-blood group H and A variants and six polypeptide
      GalNAc-transferases (T1-4, T6, T11) that control the site and density of
      O-glycosylation were analysed by immunohistochemistry during human testis
      development and in TGCT. Normal testis showed a restricted pattern; gonocytes
      expressed abundant sialyl-Tn and sialyl-T, and adult spermatogonia were devoid of
      any glycans, whereas spermatocytes and spermatids expressed exclusively glycans
      Tn and T and the GalNAc-T3 isoform. A subset of mature ejaculated spermatozoa
      expressed an additional glycan sialyl-T. The pattern found in testicular
      neoplasms recapitulated the developmental order: Pre-invasive carcinoma in situ
      (CIS) cells and seminoma expressed fetal type sialylated glycans in keeping with 
      their gonocyte-like phenotype. Neither simple mucin-type O-glycans nor
      GalNAc-transferase isoforms were found in undifferentiated nonseminoma, i.e.
      embryonal carcinoma, whereas teratomas expressed them all to some extent but in a
      disorganized manner. We concluded that simple mucin-type O-glycans and their
      transferases are developmentally regulated in the human testis, with profound
      changes associated with neoplasia. The restricted O-glycosylation pattern in
      haploid germ cells suggests a role in their maturation or egg
      recognition/fertilization warranting further studies in male infertility, whereas
      the findings in TGCT provide new diagnostic tools and support our hypothesis that
      testicular cancer is a developmental disease of germ cell differentiation.
FAU - Rajpert-De Meyts, E
AU  - Rajpert-De Meyts E
AD  - University Department of Growth and Reproduction, Section GR-5064,
      Rigshospitalet, Blegdamsvej 9, 2100 Copenhagen, Denmark. erm@rh.hosp.dk
FAU - Poll, S N
AU  - Poll SN
FAU - Goukasian, I
AU  - Goukasian I
FAU - Jeanneau, C
AU  - Jeanneau C
FAU - Herlihy, A S
AU  - Herlihy AS
FAU - Bennett, E P
AU  - Bennett EP
FAU - Skakkebaek, N E
AU  - Skakkebaek NE
FAU - Clausen, H
AU  - Clausen H
FAU - Giwercman, A
AU  - Giwercman A
FAU - Mandel, U
AU  - Mandel U
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20070811
PL  - Germany
TA  - Virchows Arch
JT  - Virchows Archiv : an international journal of pathology
JID - 9423843
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Antigens, Viral, Tumor)
RN  - 0 (Tn antigen)
RN  - 0 (sialosyl-Tn antigen)
RN  - EC 2.4.1.- (N-Acetylgalactosaminyltransferases)
RN  - EC 2.4.1.41 (polypeptide N-acetylgalactosaminyltransferase)
SB  - IM
MH  - Antigens, Tumor-Associated, Carbohydrate/genetics/*metabolism
MH  - Antigens, Viral, Tumor/genetics/*metabolism
MH  - Cell Differentiation/physiology
MH  - Cell Transformation, Neoplastic/*metabolism/pathology
MH  - Gene Expression Profiling
MH  - Gene Expression Regulation, Neoplastic
MH  - Humans
MH  - Male
MH  - N-Acetylgalactosaminyltransferases/genetics/*metabolism
MH  - Phenotype
MH  - Spermatogenesis/physiology
MH  - Spermatozoa/pathology
MH  - Testicular Neoplasms/*metabolism/pathology
MH  - Testis/*metabolism/pathology
EDAT- 2007/08/19 09:00
MHDA- 2007/12/08 09:00
CRDT- 2007/08/19 09:00
PHST- 2007/02/05 00:00 [received]
PHST- 2007/07/13 00:00 [accepted]
PHST- 2007/07/11 00:00 [revised]
PHST- 2007/08/19 09:00 [pubmed]
PHST- 2007/12/08 09:00 [medline]
PHST- 2007/08/19 09:00 [entrez]
AID - 10.1007/s00428-007-0478-4 [doi]
PST - ppublish
SO  - Virchows Arch. 2007 Oct;451(4):805-14. doi: 10.1007/s00428-007-0478-4. Epub 2007 
      Aug 11.

PMID- 8608270
OWN - NLM
STAT- MEDLINE
DCOM- 19960530
LR  - 20190512
IS  - 0959-6658 (Print)
IS  - 0959-6658 (Linking)
VI  - 5
IP  - 7
DP  - 1995 Oct
TI  - The biosynthesis of Lewis X in Helicobacter pylori.
PG  - 683-8
AB  - The biosynthesis of the Lewis X determinant (Gal beta 1-4 [Fuc alpha 1-3]GlcNAc
      beta-) in three strains of Helicobacter pylori has been investigated. Strains UA 
      861, UA 802 and UA 1182 contain alpha 1,3 fucosyltransferase and beta 1,4
      galactosyltransferase activities that synthesize the Lewis X structure by the
      transfer of monosaccharides from GDP-fucose and UDP-galactose donors,
      respectively. The enzyme reaction products that formed were characterized by
      capillary zone electrophoresis and by 1H-NMR spectroscopy. The biosynthetic
      pathway is therefore identical to that found in humans. In the three strains, the
      fucosyltransferase and galactosyltransferase activities differed in various
      cellular fractions. Km values for their donor and acceptor substrates also
      differed.
FAU - Chan, N W
AU  - Chan NW
AD  - Department of Chemistry, University of Alberta, Edmonton, Canada.
FAU - Stangier, K
AU  - Stangier K
FAU - Sherburne, R
AU  - Sherburne R
FAU - Taylor, D E
AU  - Taylor DE
FAU - Zhang, Y
AU  - Zhang Y
FAU - Dovichi, N J
AU  - Dovichi NJ
FAU - Palcic, M M
AU  - Palcic MM
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - Glycobiology
JT  - Glycobiology
JID - 9104124
RN  - 0 (Lewis X Antigen)
RN  - 15839-70-0 (Guanosine Diphosphate Fucose)
RN  - 2956-16-3 (Uridine Diphosphate Galactose)
RN  - EC 2.4.1.- (Fucosyltransferases)
RN  - EC 2.4.1.152 (galactoside 3-fucosyltransferase)
RN  - EC 2.4.1.90 (N-Acetyllactosamine Synthase)
SB  - IM
MH  - Carbohydrate Sequence
MH  - Fucosyltransferases/metabolism
MH  - Guanosine Diphosphate Fucose/metabolism
MH  - Helicobacter pylori/isolation & purification/*metabolism/ultrastructure
MH  - Humans
MH  - Kinetics
MH  - Lewis X Antigen/*biosynthesis/chemistry
MH  - Microscopy, Immunoelectron
MH  - Molecular Sequence Data
MH  - N-Acetyllactosamine Synthase/metabolism
MH  - Substrate Specificity
MH  - Uridine Diphosphate Galactose/metabolism
EDAT- 1995/10/01 00:00
MHDA- 1995/10/01 00:01
CRDT- 1995/10/01 00:00
PHST- 1995/10/01 00:00 [pubmed]
PHST- 1995/10/01 00:01 [medline]
PHST- 1995/10/01 00:00 [entrez]
AID - 10.1093/glycob/5.7.683 [doi]
PST - ppublish
SO  - Glycobiology. 1995 Oct;5(7):683-8. doi: 10.1093/glycob/5.7.683.

PMID- 1691018
OWN - NLM
STAT- MEDLINE
DCOM- 19900515
LR  - 20170915
IS  - 0006-3002 (Print)
IS  - 0006-3002 (Linking)
VI  - 1043
IP  - 3
DP  - 1990 Apr 17
TI  - Characterization of the binding epitope of the monoclonal antibody DMAb-1 to
      ganglioside GM2.
PG  - 267-72
AB  - Several derivatives of ganglioside GM2 were synthesized for mapping of the
      binding epitope of a monoclonal antibody raised against this ganglioside. The GM2
      ganglioside was modified in both the hydrophobic and the hydrophobilic part of
      the molecule. The synthesized derivatives were characterized with fast atom
      bombardment mass spectrometry (FAB-MS). Affinity of the monoclonal antibody for
      the GM2 derivatives was determined by enzyme-linked immunosorbent assay (ELISA)
      on microtitre plates or by TLC immunostaining. Modifying the GM2 sialic acid by
      deacetylation or blocking of the carboxyl moiety abolished the binding to the
      monoclonal antibody while the cleaving of the glycol group on the sialic acid
      tail led to a 70% reduced binding affinity. Removal of the fatty acid (lyso-GM2) 
      eliminated the binding to the antibody. GM2 derivatives with fatty acid moieties 
      of 8 carbon atoms or less showed almost no reactivity. GM2 with saturated fatty
      acids 16:0, 18:0 and 20:0 had binding affinity similar to natural GM2, while the 
      24:0 fatty acid had only half the binding affinity. The results demonstrate the
      importance of ganglioside fatty acid composition with regard to ligand binding
      between the monoclonal antibody and its specific ganglioside antigen. Thus,
      caution must be shown in the application of immunaffinity methods with monoclonal
      antibodies for the quantitative determination of glycosphingolipids from
      different tissues.
FAU - Karlsson, G
AU  - Karlsson G
AD  - Department of Psychiatry and Neurochemistry, Gothenburg University, St. Jorgen
      Hospital, Hisings Backa, Sweden.
FAU - Mansson, J E
AU  - Mansson JE
FAU - Wikstrand, C
AU  - Wikstrand C
FAU - Bigner, D
AU  - Bigner D
FAU - Svennerholm, L
AU  - Svennerholm L
LA  - eng
GR  - CA 32672/CA/NCI NIH HHS/United States
GR  - NS 20023/NS/NINDS NIH HHS/United States
GR  - R37 CA 11898/CA/NCI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - Netherlands
TA  - Biochim Biophys Acta
JT  - Biochimica et biophysica acta
JID - 0217513
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Epitopes)
RN  - 0 (Gangliosides)
RN  - 0 (Sialic Acids)
RN  - 19600-01-2 (G(M2) Ganglioside)
SB  - IM
MH  - Antibodies, Monoclonal/*immunology
MH  - Antibody Affinity
MH  - Chromatography, Thin Layer
MH  - Enzyme-Linked Immunosorbent Assay
MH  - Epitopes
MH  - G(M2) Ganglioside/*immunology
MH  - Gangliosides/*immunology
MH  - Humans
MH  - In Vitro Techniques
MH  - Molecular Structure
MH  - Sialic Acids/immunology
MH  - Structure-Activity Relationship
EDAT- 1990/04/17 00:00
MHDA- 1990/04/17 00:01
CRDT- 1990/04/17 00:00
PHST- 1990/04/17 00:00 [pubmed]
PHST- 1990/04/17 00:01 [medline]
PHST- 1990/04/17 00:00 [entrez]
AID - 0005-2760(90)90026-T [pii]
PST - ppublish
SO  - Biochim Biophys Acta. 1990 Apr 17;1043(3):267-72.

PMID- 15770530
OWN - NLM
STAT- MEDLINE
DCOM- 20050519
LR  - 20151119
IS  - 0167-6806 (Print)
IS  - 0167-6806 (Linking)
VI  - 90
IP  - 1
DP  - 2005 Mar
TI  - Stable expression of sialyl-Tn antigen in T47-D cells induces a decrease of cell 
      adhesion and an increase of cell migration.
PG  - 77-84
AB  - Sialyl-Tn is a carbohydrate antigen overexpressed in several epithelial cancers
      including breast cancer, and usually associated with poor prognosis. Sialyl-Tn is
      synthesized by a CMP-Neu5Ac: GalNAc alpha2,6-sialyltransferase: ST6GalNAc I,
      which catalyzes the transfer of a sialic acid residue in alpha2,6-linkage to the 
      GalNAcalpha1-O-Ser/Thr structure. The resulting disaccharide
      (Neu5Acalpha2-6GalNAcalpha1-O-Ser/Thr) cannot be further elongated and sialyl-Tn 
      expression results therefore in a shortening of the O-glycan chains. However,
      usual breast cancer cell lines express neither ST6GalNAc I nor sialyl-Tn antigen.
      We have previously shown that stable transfection of MDA-MB-231 cells with the
      hST6GalNAc I cDNA induces the sialyl-Tn antigen expression at the cell surface
      and leads to a decreased cell growth and an increased cell migration. We describe
      herein the generation of new T47-D clones expressing sialyl-Tn antigen after
      hST6GalNAc I cDNA stable transfection. sialyl-Tn antigen is carried by several
      high molecular weight membrane bound O-glycoproteins, including MUC1. We show
      that sialyl-Tn expression induces a decrease of cell growth and adhesion, and an 
      increase of cell migration in sialyl-Tn positive clones compared to mock
      transfected cells. These observations show that the alteration of the O-glycans
      pattern is sufficient to modify the biological features of cancer cells. These
      T47-D sialyl-Tn expressing clones might allow further in vivo investigation to
      determine precisely the impact of such O-glycosylation modifications on breast
      cancer development.
FAU - Julien, Sylvain
AU  - Julien S
AD  - Unite de Glycobiologie Structurale et Fonctionnelle, UMR CNRS no. 8576, GDR CNRS 
      no. 2590, France.
FAU - Lagadec, Chann
AU  - Lagadec C
FAU - Krzewinski-Recchi, Marie-Ange
AU  - Krzewinski-Recchi MA
FAU - Courtand, Gilles
AU  - Courtand G
FAU - Le Bourhis, Xuefen
AU  - Le Bourhis X
FAU - Delannoy, Philippe
AU  - Delannoy P
LA  - eng
PT  - Evaluation Studies
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - Netherlands
TA  - Breast Cancer Res Treat
JT  - Breast cancer research and treatment
JID - 8111104
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Biomarkers, Tumor)
RN  - 0 (sialosyl-Tn antigen)
RN  - EC 2.4.99.- (Sialyltransferases)
RN  - EC 2.4.99.3 (CMP-N-acetylneuraminate-alpha-N-acetylgalactosaminide
      alpha-2,6-sialyltransferase)
SB  - IM
MH  - Antigens, Tumor-Associated, Carbohydrate/*metabolism
MH  - Biomarkers, Tumor/*metabolism
MH  - Breast Neoplasms/*metabolism
MH  - *Cell Adhesion
MH  - Cell Line, Tumor/metabolism
MH  - *Cell Movement
MH  - Glycosylation
MH  - Humans
MH  - Sialyltransferases/metabolism
EDAT- 2005/03/17 09:00
MHDA- 2005/05/20 09:00
CRDT- 2005/03/17 09:00
PHST- 2005/03/17 09:00 [pubmed]
PHST- 2005/05/20 09:00 [medline]
PHST- 2005/03/17 09:00 [entrez]
AID - 10.1007/s10549-004-3137-3 [doi]
PST - ppublish
SO  - Breast Cancer Res Treat. 2005 Mar;90(1):77-84. doi: 10.1007/s10549-004-3137-3.

PMID- 15179519
OWN - NLM
STAT- MEDLINE
DCOM- 20041210
LR  - 20181113
IS  - 0179-0358 (Print)
IS  - 0179-0358 (Linking)
VI  - 20
IP  - 7
DP  - 2004 Jul
TI  - Unexpected mortality in pediatric patients with postoperative Hirschsprung's
      disease.
PG  - 525-8
AB  - Hirschsprung's disease is characterized by lower intestinal obstruction. In this 
      retrospective study, we investigated the postoperative complications and the
      causes of death in pediatric patients with Hirschsprung's disease. Between
      January 1981 and June 1998, 147 patients with Hirschsprung's disease underwent
      surgical intervention (129 with both colostomy and Soave's pull-through
      procedures) at Mackay Hospital. Of 147 total patients, 83.67% had aganglionosis
      in the rectosigmoid, 5.44% had colon involvement, and 4.08% had total colon
      aganglionosis, documented pathologically after a Soave's pull-through procedure. 
      Any post-pull-through patient who showed symptoms of fever, leukocytosis,
      diarrhea, and clinical sepsis was diagnosed with Hirschsprung's enterocolitis.
      Four patients died within 4.5 months of surgery, and one patient died more than 4
      years after surgery; these five patients were positive for Thomsen (T-) antigen. 
      One patient died soon after rectal irrigation was performed in preparation for
      the surgery. All five of these patients had sepsis clinically, and anaerobic
      sepsis was attributed as the main cause of their deaths. Of interest in these
      cases is the presence of T-antigen, a potentially useful marker for anaerobic
      bacterial infection that may not be well known to most pediatricians. We
      recommend (1) determining the presence of T-antigen in patients with recurrent
      Hirschsprung's enterocolitis, (2) administering empirical antibiotics with
      anti-anaerobic activity as soon as possible, and (3) irrigating the colon in
      those patients who develop sepsis after a pull-through procedure.
FAU - Wang, Jin-Sheng
AU  - Wang JS
AD  - Department of Pediatrics, Kaohsiung Municipal United Hospital, Taiwan.
FAU - Lee, Hung-Chang
AU  - Lee HC
FAU - Huang, Fu-Yuan
AU  - Huang FY
FAU - Chang, Pei-Yeh
AU  - Chang PY
FAU - Sheu, Jin-Cherng
AU  - Sheu JC
LA  - eng
PT  - Journal Article
DEP - 20040604
PL  - Germany
TA  - Pediatr Surg Int
JT  - Pediatric surgery international
JID - 8609169
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Biomarkers)
RN  - 0 (Isoantigens)
RN  - 3554-90-3 (Thomsen-Friedenreich antigen)
SB  - IM
MH  - Anal Canal/surgery
MH  - Anastomosis, Surgical/mortality
MH  - Antigens, Tumor-Associated, Carbohydrate/analysis
MH  - Biomarkers/analysis
MH  - Colon/surgery
MH  - Colostomy/mortality
MH  - Enterocolitis/epidemiology
MH  - Female
MH  - Hirschsprung Disease/*mortality/surgery
MH  - Humans
MH  - Infant
MH  - Infant, Newborn
MH  - Isoantigens/analysis
MH  - Male
MH  - Patient Readmission/statistics & numerical data
MH  - Postoperative Complications/epidemiology/*mortality
MH  - Rectum/surgery
MH  - Retrospective Studies
MH  - Survival Rate
MH  - Taiwan/epidemiology
EDAT- 2004/06/05 05:00
MHDA- 2004/12/16 09:00
CRDT- 2004/06/05 05:00
PHST- 2003/04/03 00:00 [accepted]
PHST- 2004/06/05 05:00 [pubmed]
PHST- 2004/12/16 09:00 [medline]
PHST- 2004/06/05 05:00 [entrez]
AID - 10.1007/s00383-004-1213-8 [doi]
PST - ppublish
SO  - Pediatr Surg Int. 2004 Jul;20(7):525-8. doi: 10.1007/s00383-004-1213-8. Epub 2004
      Jun 4.

PMID- 1972718
OWN - NLM
STAT- MEDLINE
DCOM- 19900727
LR  - 20171116
IS  - 0022-1767 (Print)
IS  - 0022-1767 (Linking)
VI  - 145
IP  - 1
DP  - 1990 Jul 1
TI  - High idiotypic connectivity of the VH7183-encoded antibodies directed to a murine
      embryonic carbohydrate antigen, Lewis Y, as ascertained by syngenic anti-idiotype
      monoclonal antibodies.
PG  - 224-32
AB  - The Lewis Y Ag is a carbohydrate Ag which is closely related to a well-known
      murine embryonic Ag, the stage-specific embryonic Ag-1 (SSEA-1), in its
      biochemical structure. It is expressed at the surface of murine embryonic cells
      as well as many murine cancer cells. For the analysis of idiotopes carried by the
      anti-Lewis Y antibodies, we generated two syngenic anti-idiotypic mAb, Id-A1 and 
      Id-B4 (both BALB/c IgG1), which are directed to the idiotypic determinants
      carried by the anti-Lewis Y mAb, AH-6 (BALB/c IgM). Both Id-A1 and Id-B4 (Ab2)
      recognized paratope-related idiotopes carried by the AH-6 antibody (Ab1); they
      specifically inhibited the binding of AH-6 to the Lewis Y Ag. The high idiotypic 
      connectivity of anti-Lewis Y antibodies was noted; the polyclonal anti-idiotype
      antibody, produced in the sera of BALB/c mice by immunizing AH-6 antibody,
      cross-reacted with several anti-Lewis Y mAb which has been established in
      different laboratories. Id-B4 and Id-A1 seem to represent such cross-reactive
      anti-idiotypic antibodies. Id-A1 recognized an idiotope carried by two out of six
      panel Ab1 mAb directed to the Lewis Y Ag. Id-B4 reacted with four out of the six 
      panel antibodies, and was considered to recognize a recurrent idiotope of
      anti-Lewis Y antibodies which occurs more commonly than the idiotope recognized
      by Id-A1. All of the anti-Lewis Y antibodies which carry idiotopes that react
      with Id-A1 or Id-B4 were encoded by the VH genes of the VH7183 family; the most
      D-J proximal VH gene family in BALB/c mice, which is known to be preferentially
      expressed in embryonic B cells. Immunization of BALB/c mice with keyhole limpet
      hemocyanin-conjugated Id-B4 and/or Id-A1 induced a significant titer of
      anti-Lewis Y antibodies (Ab1-like Ab3) in the sera.
FAU - Hirashima, K
AU  - Hirashima K
AD  - Department of Laboratory Medicine and Clinical Science, Kyoto University, School 
      of Medicine, Japan.
FAU - Zenita, K
AU  - Zenita K
FAU - Takada, A
AU  - Takada A
FAU - Kitahara, A
AU  - Kitahara A
FAU - Ishihara, G
AU  - Ishihara G
FAU - Harada, R
AU  - Harada R
FAU - Ohmori, K
AU  - Ohmori K
FAU - Hirohashi, S
AU  - Hirohashi S
FAU - Kyoizumi, S
AU  - Kyoizumi S
FAU - Akiyama, M
AU  - Akiyama M
AU  - et al.
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - J Immunol
JT  - Journal of immunology (Baltimore, Md. : 1950)
JID - 2985117R
RN  - 0 (Antibodies, Anti-Idiotypic)
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens, Neoplasm)
RN  - 0 (Carbohydrates)
RN  - 0 (Glycolipids)
RN  - 0 (Immunoglobulin Idiotypes)
RN  - 0 (Lewis X Antigen)
SB  - AIM
SB  - IM
MH  - Animals
MH  - Antibodies, Anti-Idiotypic/*immunology
MH  - Antibodies, Monoclonal/immunology
MH  - Antibody Formation
MH  - Antigens, Neoplasm/*immunology
MH  - Carbohydrates/immunology
MH  - Glycolipids/*immunology
MH  - Immunoglobulin Idiotypes/*immunology
MH  - Lewis X Antigen
MH  - Mice
MH  - Mice, Inbred BALB C/immunology
EDAT- 1990/07/01 00:00
MHDA- 1990/07/01 00:01
CRDT- 1990/07/01 00:00
PHST- 1990/07/01 00:00 [pubmed]
PHST- 1990/07/01 00:01 [medline]
PHST- 1990/07/01 00:00 [entrez]
PST - ppublish
SO  - J Immunol. 1990 Jul 1;145(1):224-32.

PMID- 2414279
OWN - NLM
STAT- MEDLINE
DCOM- 19851129
LR  - 20061115
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 260
IP  - 24
DP  - 1985 Oct 25
TI  - Syngeneic monoclonal antibody against melanoma antigen with interspecies
      cross-reactivity recognizes GM3, a prominent ganglioside of B16 melanoma.
PG  - 13328-33
AB  - It has previously been reported that a mouse (C57BL/6) monoclonal antibody,
      M2590, was established against syngeneic melanoma B16 cells, which was shown to
      react only with melanoma cells from various species but not with other tumor
      cells or normal tissues (Taniguchi, M., and Wakabayashi, S. (1984) Gann 75,
      418-426). In the present study, the specificity of M2590 antibody was shown to be
      directed to a saccharide arrangement (NeuAc alpha 2-3Gal beta 1-4Glc (or
      -GlcNAc)) of gangliosides by three different assay systems including enzyme
      immunostaining on thin layer plates, sandwich radioimmunoassay, and enzyme-linked
      immunoadsorbent assays using a variety of glycolipids with known structures.
      Neither gangliosides having NeuGc terminus, including NeuGc alpha 2-3Gal beta
      1-4Glc-ceramide and NeuGc alpha 2-3Gal beta 1-4GlcNAc beta 1-3Gal beta
      1-4Glc-ceramide, nor ganglio series gangliosides carrying NeuAc reacted with the 
      antibody. An M2590 antibody-reactive antigen was isolated from B16 melanoma
      cells, and its structure was determined to be NeuAc alpha 2-3Gal beta
      1-4Glc-ceramide by fast atom bombardment mass spectrometry, methylation analysis,
      and exoglycosidase treatment. The ceramide was composed of d18:1 as its
      long-chain base and C16:0, C24:1, and C24:0 as major fatty acids. The same
      ganglioside was also detected in the culture supernatant of the melanoma cells as
      shedding antigen.
FAU - Hirabayashi, Y
AU  - Hirabayashi Y
FAU - Hamaoka, A
AU  - Hamaoka A
FAU - Matsumoto, M
AU  - Matsumoto M
FAU - Matsubara, T
AU  - Matsubara T
FAU - Tagawa, M
AU  - Tagawa M
FAU - Wakabayashi, S
AU  - Wakabayashi S
FAU - Taniguchi, M
AU  - Taniguchi M
LA  - eng
PT  - Journal Article
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens)
RN  - 0 (Epitopes)
RN  - 0 (G(M3) Ganglioside)
RN  - 0 (Gangliosides)
RN  - 69345-49-9 (N-glycolylneuraminyllactosylceramide)
SB  - IM
MH  - Animals
MH  - Antibodies, Monoclonal/*immunology
MH  - Antibody Specificity
MH  - Antigens/*immunology
MH  - Cell Line
MH  - Enzyme-Linked Immunosorbent Assay
MH  - Epitopes/immunology
MH  - G(M3) Ganglioside/analogs & derivatives/*immunology
MH  - Gangliosides/*immunology
MH  - Immunoenzyme Techniques
MH  - Mass Spectrometry
MH  - Melanoma/*immunology
MH  - Mice
MH  - Mice, Inbred BALB C
MH  - Mice, Inbred C57BL
MH  - Radioimmunoassay
MH  - Species Specificity
EDAT- 1985/10/25 00:00
MHDA- 1985/10/25 00:01
CRDT- 1985/10/25 00:00
PHST- 1985/10/25 00:00 [pubmed]
PHST- 1985/10/25 00:01 [medline]
PHST- 1985/10/25 00:00 [entrez]
PST - ppublish
SO  - J Biol Chem. 1985 Oct 25;260(24):13328-33.

PMID- 17253960
OWN - NLM
STAT- MEDLINE
DCOM- 20070507
LR  - 20181113
IS  - 1470-8728 (Electronic)
IS  - 0264-6021 (Linking)
VI  - 403
IP  - 3
DP  - 2007 May 1
TI  - Involvement of chondroitin sulfate synthase-3 (chondroitin synthase-2) in
      chondroitin polymerization through its interaction with chondroitin synthase-1 or
      chondroitin-polymerizing factor.
PG  - 545-52
AB  - Previously, we have demonstrated that co-expression of ChSy-1 (chondroitin
      synthase-1), with ChPF (chondroitin-polymerizing factor) resulted in a marked
      augmentation of glycosyltransferase activities and the expression of the
      chondroitin polymerase activity of ChSy-1. These results prompted us to evaluate 
      the effects of co-expression of the recently cloned CSS3 (chondroitin sulfate
      synthase-3) with ChPF, because ChSy-1 and CSS3 have similar properties, i.e. they
      possess GalNAcT-II (N-acetylgalactosaminyltransferase-II) and GlcAT-II
      (glucuronyltransferase-II) activities responsible for the elongation of CS
      (chondroitin sulfate) chains but cannot polymerize chondroitin chains by
      themselves. Co-expressed CSS3 and ChPF showed not only substantial GalNAcT-II and
      GlcAT-II activities but also chondroitin polymerase activity. Interestingly,
      co-expressed ChSy-1 and CSS3 also exhibited polymerase activity. The chain length
      of chondroitin formed by the co-expressed proteins in various combinations was
      different. In addition, interactions between any two of ChSy-1, CSS3 and ChPF
      were demonstrated by pull-down assays. Moreover, overexpression of CSS3 increased
      the amount of CS in HeLa cells, while the RNA interference of CSS3 resulted in a 
      reduction in the amount of CS in the cells. Altogether these results suggest that
      chondroitin polymerization is achieved by multiple combinations of ChSy-1, CSS3
      and ChPF. Based on these characteristics, we have renamed CSS3 ChSy-2
      (chondroitin synthase-2).
FAU - Izumikawa, Tomomi
AU  - Izumikawa T
AD  - Department of Biochemistry, Kobe Pharmaceutical University, Higashinada-ku, Kobe 
      658-8558, Japan.
FAU - Uyama, Toru
AU  - Uyama T
FAU - Okuura, Yuka
AU  - Okuura Y
FAU - Sugahara, Kazuyuki
AU  - Sugahara K
FAU - Kitagawa, Hiroshi
AU  - Kitagawa H
LA  - eng
SI  - GENBANK/AB175496
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - Biochem J
JT  - The Biochemical journal
JID - 2984726R
RN  - 0 (Membrane Proteins)
RN  - EC 2.4.- (Glycosyltransferases)
RN  - EC 2.4.1.- (Hexosyltransferases)
RN  - EC 2.4.1.- (N-Acetylgalactosaminyltransferases)
RN  - EC 2.4.1.- (chondroitin sulfate synthase-2)
RN  - EC 2.4.1.175 (CHSY3 protein, human)
RN  - EC 2.4.1.175 (chondroitin synthase)
SB  - IM
MH  - Animals
MH  - Base Sequence
MH  - COS Cells
MH  - Cercopithecus aethiops
MH  - Glycosyltransferases/*metabolism
MH  - HeLa Cells
MH  - Hexosyltransferases/*metabolism
MH  - Humans
MH  - Membrane Proteins/*metabolism
MH  - Molecular Sequence Data
MH  - N-Acetylgalactosaminyltransferases
PMC - PMC1876374
EDAT- 2007/01/27 09:00
MHDA- 2007/05/08 09:00
CRDT- 2007/01/27 09:00
PHST- 2007/01/27 09:00 [pubmed]
PHST- 2007/05/08 09:00 [medline]
PHST- 2007/01/27 09:00 [entrez]
AID - BJ20061876 [pii]
AID - 10.1042/BJ20061876 [doi]
PST - ppublish
SO  - Biochem J. 2007 May 1;403(3):545-52. doi: 10.1042/BJ20061876.

PMID- 17485527
OWN - NLM
STAT- MEDLINE
DCOM- 20070621
LR  - 20070508
IS  - 0022-1317 (Print)
IS  - 0022-1317 (Linking)
VI  - 88
IP  - Pt 6
DP  - 2007 Jun
TI  - Glycoprotein I of herpes simplex virus type 1 contains a unique polymorphic
      tandem-repeated mucin region.
PG  - 1683-8
AB  - Glycoprotein I (gI) of herpes simplex virus type 1 (HSV-1) contains a tandem
      repeat (TR) region including the amino acids serine and threonine, residues that 
      can be utilized for O-glycosylation. The length of this TR region was determined 
      for 82 clinical HSV-1 isolates and the results revealed a polymorphic
      distribution of two to six or eight repeated blocks with a majority harbouring
      between two and four repeats. Assessment of the O-glycosylation capacity of an
      acceptor peptide (STPSTTTSTPSTTT), representing two of the gI blocks, showed that
      the peptide was a universal substrate for O-glycosylation not only for the two
      most commonly expressed N-acetyl-d-galactosamine (GalNAc)-T1 and -T2
      transferases, but also for the GalNAc-T3, -T4 and -T11 transferases.
      Immunoblotting of virus-infected cells showed that gI was exclusively
      O-glycosylated with GalNAc monosaccharides (Tn antigen). A polymorphic mucin
      region has not been described previously for HSV-1 and is a unique finding, as
      repeated blocks within gI homologues are lacking in other alphaherpesviruses.
FAU - Norberg, Peter
AU  - Norberg P
AD  - Department of Virology, University of Goteborg, Guldhedsgatan 10B, S-413 46
      Goteborg, Sweden.
FAU - Olofsson, Sigvard
AU  - Olofsson S
FAU - Tarp, Mads Agervig
AU  - Tarp MA
FAU - Clausen, Henrik
AU  - Clausen H
FAU - Bergstrom, Tomas
AU  - Bergstrom T
FAU - Liljeqvist, Jan Ake
AU  - Liljeqvist JA
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - J Gen Virol
JT  - The Journal of general virology
JID - 0077340
RN  - 0 (Viral Envelope Proteins)
RN  - 0 (glycoprotein I, herpes simplex virus type 1)
RN  - EC 2.4.1.- (N-Acetylgalactosaminyltransferases)
SB  - IM
MH  - Glycosylation
MH  - Herpesvirus 1, Human/*chemistry/genetics/metabolism
MH  - Immunoblotting
MH  - N-Acetylgalactosaminyltransferases/metabolism
MH  - *Polymorphism, Genetic
MH  - Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
MH  - *Tandem Repeat Sequences
MH  - Viral Envelope Proteins/*chemistry/*genetics/metabolism
EDAT- 2007/05/09 09:00
MHDA- 2007/06/22 09:00
CRDT- 2007/05/09 09:00
PHST- 2007/05/09 09:00 [pubmed]
PHST- 2007/06/22 09:00 [medline]
PHST- 2007/05/09 09:00 [entrez]
AID - 88/6/1683 [pii]
AID - 10.1099/vir.0.82500-0 [doi]
PST - ppublish
SO  - J Gen Virol. 2007 Jun;88(Pt 6):1683-8. doi: 10.1099/vir.0.82500-0.

PMID- 9015359
OWN - NLM
STAT- MEDLINE
DCOM- 19970219
LR  - 20171116
IS  - 0006-291X (Print)
IS  - 0006-291X (Linking)
VI  - 230
IP  - 3
DP  - 1997 Jan 23
TI  - Sulfated sialyl Lewis X, the putative L-selectin ligand, detected on endothelial 
      cells of high endothelial venules by a distinct set of anti-sialyl Lewis X
      antibodies.
PG  - 546-51
AB  - Endothelial cells of high endothelial venules (HEV) in human peripheral lymph
      nodes expressed a distinct type of sialyl Lewis X antigen, which was detected
      preferentially with a set of anti-sialyl Lewis X antibodies, 2F3, 2H5 and
      HECA-452 in immunohistochemistry, while another set of anti-sialyl Lewis X
      antibodies, FH-6 and CSLEX-1, failed to detect it. The adhesion of cells
      expressing L-selectin to HEV was inhibited by members of the former set of
      antibodies in Stamper-Woodruff assays performed on frozen sections of human
      peripheral lymph nodes. Transfection of a cultured endothelial cell line with a
      human alpha1-->3 fucosyltransferase, Fuc-T VII, resulted in the expression of a
      distinct type of sialyl Lewis X antigen having the reactivity similar to that of 
      HEV; i.e., the antigen appearing on the transfectant clone was detectable only
      with the set of 2F3, 2H5 and HECA-452, but not with the set of FH-6 and CSLEX-1. 
      Treatment of transfectant cells with sodium chlorate, a metabolic inhibitor of
      sulfation, resulted in reactivity to the members of the latter set of antibodies,
      suggesting that sulfation of sialyl Lewis X moiety was the cause of the
      discrepancy in the reactivity of the anti-sialyl Lewis X antibodies. When tested 
      against various authentic sulfated sialyl Lewis X determinants, 6-sulfo sialyl
      Lewis X and 6,6'-bis-sulfo sialyl Lewis X were found to be reactive to the
      antibodies, 2F3, 2H5 and HECA-452, but not with antibodies FH-6 and CSLEX-1,
      suggesting that the distinct type of sialyl Lewis X determinant on the HEV
      endothelial cells and Fuc-T VII-transfected endothelial cell clone are mainly
      6-sulfo and/or 6,6'-bis-sulfo sialyl Lewis X determinants.
FAU - Mitsuoka, C
AU  - Mitsuoka C
AD  - Program of Experimental Pathology, Aichi Cancer Center, Research Institute,
      Nagoya, Japan.
FAU - Kawakami-Kimura, N
AU  - Kawakami-Kimura N
FAU - Kasugai-Sawada, M
AU  - Kasugai-Sawada M
FAU - Hiraiwa, N
AU  - Hiraiwa N
FAU - Toda, K
AU  - Toda K
FAU - Ishida, H
AU  - Ishida H
FAU - Kiso, M
AU  - Kiso M
FAU - Hasegawa, A
AU  - Hasegawa A
FAU - Kannagi, R
AU  - Kannagi R
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Biochem Biophys Res Commun
JT  - Biochemical and biophysical research communications
JID - 0372516
RN  - 0 (Epitopes)
RN  - 0 (Isoantibodies)
RN  - 0 (Lewis X Antigen)
RN  - 0 (Sulfates)
RN  - EC 2.4.1.- (Fucosyltransferases)
RN  - EC 2.4.1.152 (galactoside 3-fucosyltransferase)
SB  - IM
EIN - Biochem Biophys Res Commun 1997 Apr 17;233(2):576
MH  - Animals
MH  - Antigen-Antibody Reactions
MH  - Binding, Competitive/immunology
MH  - Cell Adhesion/immunology
MH  - Cell Line
MH  - Endothelium, Lymphatic/cytology/*immunology/metabolism
MH  - Endothelium, Vascular/cytology/*immunology/metabolism
MH  - Epitopes/biosynthesis
MH  - Fucosyltransferases/genetics
MH  - Humans
MH  - Isoantibodies/*chemistry/pharmacology
MH  - Leukemia, T-Cell
MH  - Lewis X Antigen/chemistry/*immunology/*metabolism
MH  - Lymph Nodes/immunology/metabolism
MH  - Male
MH  - Mice
MH  - Mice, Inbred BALB C
MH  - Mice, Inbred C57BL
MH  - Mice, Nude
MH  - Sulfates/*metabolism
MH  - Transfection
MH  - Tumor Cells, Cultured
EDAT- 1997/01/23 00:00
MHDA- 1997/01/23 00:01
CRDT- 1997/01/23 00:00
PHST- 1997/01/23 00:00 [pubmed]
PHST- 1997/01/23 00:01 [medline]
PHST- 1997/01/23 00:00 [entrez]
AID - S0006-291X(96)96012-X [pii]
AID - 10.1006/bbrc.1996.6012 [doi]
PST - ppublish
SO  - Biochem Biophys Res Commun. 1997 Jan 23;230(3):546-51. doi:
      10.1006/bbrc.1996.6012.

PMID- 8616877
OWN - NLM
STAT- MEDLINE
DCOM- 19960612
LR  - 20151119
IS  - 0008-5472 (Print)
IS  - 0008-5472 (Linking)
VI  - 56
IP  - 9
DP  - 1996 May 1
TI  - Expression of Tn and sialyl-Tn antigens in the neoplastic transformation of
      uterine cervical epithelial cells.
PG  - 2229-32
AB  - The expression of simple mucin-type carbohydrate antigens, Tn and sialyl-Tn
      antigens, was evaluated by immunohistochemical staining with monoclonal
      antibodies in normal squamous epithelium, dysplasia, carcinoma in situ, and
      invasive squamous cell carcinoma of the uterine cervix. The expression of the Tn 
      antigen detected by HB-Tn1 and B1.1 was found in 17 (20%) and 19 (23%) of the 83 
      invasive carcinomas, respectively, but was not found in the 36 normal squamous
      epithelia, 22 severe dysplasias, or 24 carcinomas in situ. The sialyl-Tn antigen 
      was detected by HB-STn1 and TKH-2 in 14 (64%) and 11 (50%) of the 22 severe
      dysplasias, 13 (54%) and 10 (42%) of the 24 carcinomas in situ and 48 (58%) and
      42 (51%) of the 83 invasive carcinomas, respectively, but was completely absent
      in 36 normal squamous epithelia. Coexpression of the sialyl-Tn antigen was
      observed in 89% of the cases expressing the Tn antigen. No significant difference
      was observed between the immunoreactivities of the antigens in the metastatic
      lymph nodes and primary tumors. No correlation was found between the expression
      of each antigen and clinical state, histologic type, depth of invasion,
      parametrial spread, lymphatic and vessel permeation, lymph node metastasis, or
      5-year survival rate. The expression of Tn and sialyl-Tn demonstrates a specific 
      change in the neoplastic progression from carcinoma in situ to invasive carcinoma
      and from normal to dysplasia, respectively, in squamous cell neoplastic lesions
      of the cervix. Tn and sialyl-Tn antigens may be useful markers for biologic
      investigation of neoplastic transformation in cervical squamous cell carcinoma.
FAU - Terasawa, K
AU  - Terasawa K
AD  - Department of Obstetrics and Gynecology, School of Medicine, University of
      Tokushima, Japan.
FAU - Furumoto, H
AU  - Furumoto H
FAU - Kamada, M
AU  - Kamada M
FAU - Aono, T
AU  - Aono T
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Cancer Res
JT  - Cancer research
JID - 2984705R
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Biomarkers, Tumor)
RN  - 0 (Tn antigen)
RN  - 0 (sialosyl-Tn antigen)
SB  - IM
MH  - Antigens, Tumor-Associated, Carbohydrate/*biosynthesis
MH  - *Biomarkers, Tumor
MH  - Carcinoma/*metabolism/pathology
MH  - Epithelium/metabolism/pathology
MH  - Female
MH  - Humans
MH  - Neoplasm Metastasis
MH  - Uterine Cervical Neoplasms/*metabolism/pathology
MH  - Uterus/metabolism/pathology
EDAT- 1996/05/01 00:00
MHDA- 1996/05/01 00:01
CRDT- 1996/05/01 00:00
PHST- 1996/05/01 00:00 [pubmed]
PHST- 1996/05/01 00:01 [medline]
PHST- 1996/05/01 00:00 [entrez]
PST - ppublish
SO  - Cancer Res. 1996 May 1;56(9):2229-32.

PMID- 12385579
OWN - NLM
STAT- MEDLINE
DCOM- 20030421
LR  - 20171116
IS  - 0392-9078 (Print)
IS  - 0392-9078 (Linking)
VI  - 21
IP  - 3
DP  - 2002 Sep
TI  - Increased expression of sialyl Lewis(x) antigen in penetrating growth type A
      early gastric cancer.
PG  - 363-9
AB  - Early gastric cancer can be divided morphologically into two categories,
      penetrating growth type-A (Pen-A type) and other growth types (non-Pen-A types). 
      Sialyl Lewis(x) antigen has been demonstrated to play an important role in tumor 
      metastasis by serving as a functional ligand in the cell adhesion system. The aim
      of this study is to ascertain whether or not sialyl Le(x) antigen expression
      correlates with tumor growth patterns of early gastric carcinoma. An
      immunohistochemical assay was performed using monoclonal antibody CSLEX1 in 12
      Pen-A type and 79 non-Pen-A type cancers. Scoring was based on the percentage of 
      immunoreactive cells: negative, low expression (< or = 25%), and high expression 
      (> 25%). Lymph node metastasis was found more frequently in Pen-A type than
      non-Pen-A type cancers (P=0.0004). Furthermore, sialyl Le(x) antigen high
      expression was detected more often in Pen-A type cancers (7 out of 12; 58.3%)
      than non-Pen-A type cancers (13 out of 79; 16.5%) (P=0.0036). Multivariate
      logistic regression analysis showed that these variables are related
      independently to the Pen-A type and the non-Pen-A type tumor growth patterns.
      These data suggest that the difference in sialyl Le(x) antigen expression between
      the Pen-A type and non-Pen-A type tumor growth patterns of early gastric cancer
      may, at least partially, reflect different biological behavior during tumor
      progression.
FAU - Nakagoe, T
AU  - Nakagoe T
AD  - First Dept. of Surgery, Nagasaki University School of Medicine, Japan.
      nakagoe@net.nagasaki-u.ac.jp
FAU - Fukushima, K
AU  - Fukushima K
FAU - Sawai, T
AU  - Sawai T
FAU - Tsuji, T
AU  - Tsuji T
FAU - Jibiki, M
AU  - Jibiki M
FAU - Nanashima, A
AU  - Nanashima A
FAU - Tanaka, K
AU  - Tanaka K
FAU - Yamaguchi, H
AU  - Yamaguchi H
FAU - Yasutake, T
AU  - Yasutake T
FAU - Ayabe, H
AU  - Ayabe H
FAU - Ishikawa, H
AU  - Ishikawa H
LA  - eng
PT  - Comparative Study
PT  - Journal Article
PL  - England
TA  - J Exp Clin Cancer Res
JT  - Journal of experimental & clinical cancer research : CR
JID - 8308647
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Biomarkers, Tumor)
RN  - 0 (Lewis X Antigen)
SB  - IM
MH  - Adenocarcinoma/*metabolism/secondary
MH  - Antibodies, Monoclonal/immunology
MH  - Biomarkers, Tumor
MH  - Cell Differentiation
MH  - Female
MH  - Gastrectomy
MH  - Gastric Mucosa/metabolism/pathology
MH  - Humans
MH  - Immunoenzyme Techniques
MH  - Lewis X Antigen/*metabolism
MH  - Lymphatic Metastasis
MH  - Male
MH  - Middle Aged
MH  - Neoplasm Invasiveness
MH  - Neoplasm Staging
MH  - Prognosis
MH  - Stomach Neoplasms/*metabolism/pathology
MH  - Survival Rate
EDAT- 2002/10/19 04:00
MHDA- 2003/04/22 05:00
CRDT- 2002/10/19 04:00
PHST- 2002/10/19 04:00 [pubmed]
PHST- 2003/04/22 05:00 [medline]
PHST- 2002/10/19 04:00 [entrez]
PST - ppublish
SO  - J Exp Clin Cancer Res. 2002 Sep;21(3):363-9.

PMID- 3516392
OWN - NLM
STAT- MEDLINE
DCOM- 19860625
LR  - 20041117
IS  - 0008-5472 (Print)
IS  - 0008-5472 (Linking)
VI  - 46
IP  - 6
DP  - 1986 Jun
TI  - Distribution of oncofetal antigen tumor-associated glycoprotein-72 defined by
      monoclonal antibody B72.3.
PG  - 3118-24
AB  - Murine monoclonal antibody B72.3, prepared against a membrane-enriched extract of
      human metastatic carcinoma, was reacted with a spectrum of adult and fetal human 
      tissues using avidin-biotin-complex immunohistochemical techniques to evaluate
      the expression of the reactive tumor associated glycoprotein (TAG)-72 antigen.
      TAG-72 was shown to be expressed in several epithelial-derived cancers including 
      94% of colonic adenocarcinomas, 84% of invasive ductal carcinomas of the breast, 
      96% of non-small cell lung carcinomas, 100% of common epithelial ovarian
      carcinomas, as well as the majority of pancreatic, gastric, and esophageal
      cancers evaluated. TAG-72 expression was not observed, however, in tumors of
      neural, hematopoietic, or sarcomatous derivation, suggesting that the TAG-72
      antigen is "pancarcinoma" in nature. Appreciable monoclonal antibody B72.3
      reactivity was generally not observed in adult normal tissues, with limited
      reactivity noted in a few benign lesions of the breast and colon. TAG-72 antigen 
      expression was detected, however, in fetal colon, stomach, and esophagus, thus
      defining TAG-72 as an oncofetal antigen. TAG-72 has previously been shown to be
      distinct from carcinoembryonic antigen and other tumor associated antigens. The
      pancarcinoma distribution and lack of significant reactivity with normal adult
      tissues of monoclonal antibody B72.3 suggest its potential diagnostic and
      therapeutic utility for human carcinomas.
FAU - Thor, A
AU  - Thor A
FAU - Ohuchi, N
AU  - Ohuchi N
FAU - Szpak, C A
AU  - Szpak CA
FAU - Johnston, W W
AU  - Johnston WW
FAU - Schlom, J
AU  - Schlom J
LA  - eng
PT  - Journal Article
PL  - United States
TA  - Cancer Res
JT  - Cancer research
JID - 2984705R
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens, Neoplasm)
RN  - 0 (Glycoproteins)
RN  - 0 (tumor-associated antigen 72)
SB  - IM
MH  - Animals
MH  - Antibodies, Monoclonal/*immunology
MH  - Antigens, Neoplasm/*analysis
MH  - Breast Neoplasms/immunology
MH  - Colonic Neoplasms/immunology
MH  - Female
MH  - Fetus/immunology
MH  - Glycoproteins/*analysis
MH  - Histocytochemistry
MH  - Humans
MH  - Immunoenzyme Techniques
MH  - Mice
MH  - Neoplasms/diagnosis/*immunology
MH  - Pregnancy
EDAT- 1986/06/01 00:00
MHDA- 1986/06/01 00:01
CRDT- 1986/06/01 00:00
PHST- 1986/06/01 00:00 [pubmed]
PHST- 1986/06/01 00:01 [medline]
PHST- 1986/06/01 00:00 [entrez]
PST - ppublish
SO  - Cancer Res. 1986 Jun;46(6):3118-24.

PMID- 9556613
OWN - NLM
STAT- MEDLINE
DCOM- 19980602
LR  - 20190508
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 273
IP  - 18
DP  - 1998 May 1
TI  - Identification of a major carbohydrate capping group of the L-selectin ligand on 
      high endothelial venules in human lymph nodes as 6-sulfo sialyl Lewis X.
PG  - 11225-33
AB  - We investigated the molecular species of sulfated sialyl Lewis X determinants,
      the putative L-selectin ligand, expressed on high endothelial venules (HEV) in
      human lymph nodes. Comparison of the reactivity pattern of HEV with the
      reactivity of the pure 6-sulfo, 6'-sulfo, or 6,6'-bissulfo sialyl Lewis X
      determinant with hitherto known anti-sialyl Lewis X antibodies strongly suggested
      6-sulfo sialyl Lewis X to be the best candidate for the major sulfated sialyl
      Lewis X determinant on HEV, followed by 6,6'-bissulfo sialyl Lewis X, whereas
      6'-sulfo sialyl Lewis X was unlikely. We newly generated monoclonal antibodies
      (mAbs) G152 and G72 directed against 6-sulfo sialyl Lewis X, which intensely
      labeled HEV in immunohistochemical examination and inhibited binding of
      recombinant L-selectin-IgG to HEV, suggesting that the determinant serves as a
      ligand for L-selectin. To test the concomitant expression of 6, 6'-bissulfo
      sialyl Lewis X, specific mAbs (G2706, G27011, G27037, and G27039) were generated,
      but all antibodies failed to react to HEV. Next, we established mAbs (AG97 and
      AG273) directed against 6-sulfo Lewis X, the asialo form of 6-sulfo sialyl Lewis 
      X. The antibodies were not reactive to untreated HEV, but strongly reacted to
      sialidase-treated HEV. This indicated the predominance of the sialylated form of 
      6-sulfo sialyl Lewis X and minimal expression of its asialo form, corroborating
      that it was synthesized by fucosyltransferase VII, the isoenzyme that
      preferentially produces the sialylated form of the determinant.
FAU - Mitsuoka, C
AU  - Mitsuoka C
AD  - Program of Experimental Pathology,, Japan.
FAU - Sawada-Kasugai, M
AU  - Sawada-Kasugai M
FAU - Ando-Furui, K
AU  - Ando-Furui K
FAU - Izawa, M
AU  - Izawa M
FAU - Nakanishi, H
AU  - Nakanishi H
FAU - Nakamura, S
AU  - Nakamura S
FAU - Ishida, H
AU  - Ishida H
FAU - Kiso, M
AU  - Kiso M
FAU - Kannagi, R
AU  - Kannagi R
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (6'-sulfated sialyl Lewis x)
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Carbohydrates)
RN  - 0 (Lewis X Antigen)
RN  - 0 (Ligands)
RN  - 0 (Oligosaccharides)
RN  - 126880-86-2 (L-Selectin)
RN  - EC 3.2.1.18 (Neuraminidase)
SB  - IM
MH  - Antibodies, Monoclonal/immunology
MH  - Carbohydrate Sequence
MH  - Carbohydrates/*chemistry
MH  - Endothelium, Vascular/*metabolism
MH  - Humans
MH  - L-Selectin/*chemistry/metabolism
MH  - Lewis X Antigen/analogs & derivatives
MH  - Ligands
MH  - Lymph Nodes/*blood supply
MH  - Molecular Sequence Data
MH  - Neuraminidase/metabolism
MH  - Oligosaccharides/*chemistry/immunology/metabolism
MH  - Tumor Cells, Cultured
MH  - Venules/*metabolism
EDAT- 1998/06/06 00:00
MHDA- 1998/06/06 00:01
CRDT- 1998/06/06 00:00
PHST- 1998/06/06 00:00 [pubmed]
PHST- 1998/06/06 00:01 [medline]
PHST- 1998/06/06 00:00 [entrez]
AID - 10.1074/jbc.273.18.11225 [doi]
PST - ppublish
SO  - J Biol Chem. 1998 May 1;273(18):11225-33. doi: 10.1074/jbc.273.18.11225.

PMID- 2302702
OWN - NLM
STAT- MEDLINE
DCOM- 19900321
LR  - 20151119
IS  - 0008-5472 (Print)
IS  - 0008-5472 (Linking)
VI  - 50
IP  - 5
DP  - 1990 Mar 1
TI  - Profiles of Lewisx-containing glycoproteins and glycolipids in sera of patients
      with adenocarcinoma.
PG  - 1375-80
AB  - Oligosaccharides with Lex determinant (Gal beta 1----4[Fuc alpha 1----3]GlcNAc)
      are accumulated in large quantities in various adenocarcinomas. Monoclonal
      antibodies recognizing mono-, di-, or trimeric Lex showed a preferential staining
      of specific stages of human fetal tissues and various human adenocarcinomas.
      Thus, these carbohydrate epitopes are typical of oncodevelopmental antigens. The 
      present study investigated the presence of Lex epitope in sera of normal
      individuals and cancer patients, utilizing two high-affinity monoclonal
      antibodies, SH1 and SH2, directed to mono- and dimeric Lex structures,
      respectively. The Lex antigen in serum was eluted in the void volume fraction of 
      a gel filtration column, determined by using monoclonal antibody SH1, and found
      to be carried on a glycoprotein with a molecular weight of approximately 200,000.
      The Lex antigen was present in the void volume fraction of the majority (85%) of 
      sera from adenocarcinoma patients. Although the Lex epitope was also detected in 
      a smaller proportion (33%) of normal sera, its levels were significantly lower
      than in cancer sera. Lex antigen was also detected in serum glycolipid fraction; 
      however, no significant differences were observed in normal and cancer sera. A
      double determinant solid phase immunoassay utilizing SH2 as the capture antibody 
      and SH1 as the detecting antibody allowed direct determination of Lex levels in
      sera. By the use of this direct assay, the levels of serum Lex were found to
      increase in association with the progression of colorectal cancer (Dukes A to D).
      The percentage of detectability in sera from colon cancer patients was as
      follows: Dukes A, 20%; Dukes B, 45%; Dukes C, 67%; and Dukes D, 74%. The levels
      of serum Lex were also of prognostic value in Dukes C cancer patients after
      surgery and during postoperative follow-up.
FAU - Singhal, A K
AU  - Singhal AK
AD  - Biomembrane Institute, Seattle, Washington.
FAU - Orntoft, T F
AU  - Orntoft TF
FAU - Nudelman, E
AU  - Nudelman E
FAU - Nance, S
AU  - Nance S
FAU - Schibig, L
AU  - Schibig L
FAU - Stroud, M R
AU  - Stroud MR
FAU - Clausen, H
AU  - Clausen H
FAU - Hakomori, S
AU  - Hakomori S
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Cancer Res
JT  - Cancer research
JID - 2984705R
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens)
RN  - 0 (Glycolipids)
RN  - 0 (Glycoproteins)
RN  - 0 (Lewis Blood-Group System)
SB  - IM
MH  - Adenocarcinoma/*blood/immunology
MH  - Antibodies, Monoclonal
MH  - Antigens/*analysis
MH  - Colonic Neoplasms/blood/pathology
MH  - Glycolipids/*blood/isolation & purification
MH  - Glycoproteins/*blood/isolation & purification
MH  - Humans
MH  - *Lewis Blood-Group System
MH  - Molecular Weight
MH  - Neoplasm Staging
EDAT- 1990/03/01 00:00
MHDA- 1990/03/01 00:01
CRDT- 1990/03/01 00:00
PHST- 1990/03/01 00:00 [pubmed]
PHST- 1990/03/01 00:01 [medline]
PHST- 1990/03/01 00:00 [entrez]
PST - ppublish
SO  - Cancer Res. 1990 Mar 1;50(5):1375-80.

PMID- 10428856
OWN - NLM
STAT- MEDLINE
DCOM- 19990902
LR  - 20190508
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 274
IP  - 32
DP  - 1999 Aug 6
TI  - OB-BP1/Siglec-6. a leptin- and sialic acid-binding protein of the immunoglobulin 
      superfamily.
PG  - 22729-38
AB  - We report the expression cloning of a novel leptin-binding protein of the
      immunoglobulin superfamily (OB-BP1) and a cross-hybridizing clone (OB-BP2) that
      is identical to a recently described sialic acid-binding I-type lectin called
      Siglec-5. Comparisons to other known Siglec family members (CD22, CD33,
      myelin-associated glycoprotein, and sialoadhesin) show that OB-BP1,
      OB-BP2/Siglec-5, and CD33/Siglec-3 constitute a unique related subgroup with a
      high level of overall amino acid identity: OB-BP1 versus Siglec-5 (59%), OB-BP1
      versus CD33 (63%), and OB-BP2/Siglec-5 versus CD33 (56%). The cytoplasmic domains
      are not as highly conserved, but display novel motifs which are putative sites of
      tyrosine phosphorylation, including an immunoreceptor tyrosine kinase inhibitory 
      motif and a motif found in SLAM and SLAM-like proteins. Human tissues showed high
      levels of OB-BP1 mRNA in placenta and moderate expression in spleen, peripheral
      blood leukocytes, and small intestine. OB-BP2/Siglec-5 mRNA was detected in
      peripheral blood leukocytes, lung, spleen, and placenta. A monoclonal antibody
      specific for OB-BP1 confirmed high expression in the cyto- and
      syncytiotrophoblasts of the placenta. Using this antibody on peripheral blood
      leukocytes showed an almost exclusive expression pattern on B cells. Recombinant 
      forms of the extracellular domains of OB-BP1, OB-BP2/Siglec-5, and CD33/Siglec-3 
      were assayed for specific binding of leptin. While OB-BP1 exhibited tight binding
      (K(d) 91 nM), the other two showed weak binding with K(d) values in the 1-2
      microM range. Studies with sialylated ligands indicated that OB-BP1 selectively
      bound Neu5Acalpha2-6GalNAcalpha (sialyl-Tn) allowing its formal designation as
      Siglec-6. The identification of OB-BP1/Siglec-6 as a Siglec family member,
      coupled with its restricted expression pattern, suggests that it may mediate
      cell-cell recognition events by interacting with sialylated glycoprotein ligands 
      expressed on specific cell populations. We also propose a role for OB-BP1 in
      leptin physiology, as a molecular sink to regulate leptin serum levels.
FAU - Patel, N
AU  - Patel N
AD  - Molecular Biology Department, DNAX Research Institute, Palo Alto, California
      94304, USA.
FAU - Brinkman-Van der Linden, E C
AU  - Brinkman-Van der Linden EC
FAU - Altmann, S W
AU  - Altmann SW
FAU - Gish, K
AU  - Gish K
FAU - Balasubramanian, S
AU  - Balasubramanian S
FAU - Timans, J C
AU  - Timans JC
FAU - Peterson, D
AU  - Peterson D
FAU - Bell, M P
AU  - Bell MP
FAU - Bazan, J F
AU  - Bazan JF
FAU - Varki, A
AU  - Varki A
FAU - Kastelein, R A
AU  - Kastelein RA
LA  - eng
SI  - GENBANK/U71382
SI  - GENBANK/U71383
GR  - R01 GM32373/GM/NIGMS NIH HHS/United States
PT  - Comparative Study
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Antigens, CD)
RN  - 0 (Antigens, Differentiation, Myelomonocytic)
RN  - 0 (CD33 protein, human)
RN  - 0 (DNA, Complementary)
RN  - 0 (Immunoglobulins)
RN  - 0 (Lectins)
RN  - 0 (Leptin)
RN  - 0 (Ligands)
RN  - 0 (Proteins)
RN  - 0 (SIGLEC6 protein, human)
RN  - 0 (Sialic Acid Binding Ig-like Lectin 3)
RN  - GZP2782OP0 (N-Acetylneuraminic Acid)
SB  - IM
EIN - J Biol Chem 1999 Sep 24;274(39):28058
MH  - Amino Acid Sequence
MH  - Antigens, CD/genetics/isolation & purification/*metabolism
MH  - Antigens, Differentiation, Myelomonocytic/genetics/isolation &
      purification/*metabolism
MH  - Cloning, Molecular
MH  - DNA, Complementary/genetics
MH  - Evolution, Molecular
MH  - Female
MH  - Gene Expression
MH  - Humans
MH  - Immunoglobulins/*genetics
MH  - *Lectins
MH  - Leptin
MH  - Ligands
MH  - Molecular Sequence Data
MH  - *Multigene Family
MH  - N-Acetylneuraminic Acid/*metabolism
MH  - Placenta/chemistry
MH  - Pregnancy
MH  - Protein Binding
MH  - Proteins/*metabolism
MH  - Sequence Analysis, DNA
MH  - Sequence Homology, Amino Acid
MH  - Sialic Acid Binding Ig-like Lectin 3
MH  - Tissue Distribution
EDAT- 1999/07/31 00:00
MHDA- 1999/07/31 00:01
CRDT- 1999/07/31 00:00
PHST- 1999/07/31 00:00 [pubmed]
PHST- 1999/07/31 00:01 [medline]
PHST- 1999/07/31 00:00 [entrez]
AID - 10.1074/jbc.274.32.22729 [doi]
PST - ppublish
SO  - J Biol Chem. 1999 Aug 6;274(32):22729-38. doi: 10.1074/jbc.274.32.22729.

PMID- 1720922
OWN - NLM
STAT- MEDLINE
DCOM- 19920116
LR  - 20190510
IS  - 0002-9173 (Print)
IS  - 0002-9173 (Linking)
VI  - 96
IP  - 6
DP  - 1991 Dec
TI  - Expression of Tn and sialyl-Tn antigens in tumor tissues of the ovary.
PG  - 711-6
AB  - The expression of sialyl-Tn and Tn antigens in various benign, borderline, and
      malignant ovarian tumors was examined immunohistochemically using newly developed
      antibodies specific for sialyl-Tn and Tn antigens. Sialyl-Tn antigen was detected
      in only one benign tumor, a mucinous adenoma that showed faint cytoplasmic
      staining in a few cells. However, sialyl-Tn was present in 5 of 12 serous
      borderline tumors, 10 of 19 mucinous borderline tumors, 10 of 13 serous
      adenocarcinomas, 15 of 16 mucinous adenocarcinomas, 14 of 15 endometrioid
      adenocarcinomas, and 7 of 7 clear cell carcinomas of the ovary. The antigen
      expression was observed throughout the cytoplasm of cancer cells and in the
      apical cytoplasm and luminal contents of some glands. The incidence and intensity
      of staining for sialyl-Tn antigen were higher in malignant tumors than in
      borderline tumors, but these results did not correlate with the histologic
      classification or differentiation. Coexpression of sialyl-Tn antigen and Tn
      antigen was observed in two serous adenocarcinomas, six mucinous borderline
      tumors, five mucinous adenocarcinomas, eight endometrioid, and seven clear cell
      carcinomas. In no case was Tn antigen expressed without concomitant sialyl-Tn
      antigen expression. Accumulation of sialyl-Tn antigen seems to be an early event 
      of carcinogenesis of the ovary.
FAU - Inoue, M
AU  - Inoue M
AD  - Department of Obstetrics and Gynecology, Osaka University Medical School, Japan.
FAU - Ton, S M
AU  - Ton SM
FAU - Ogawa, H
AU  - Ogawa H
FAU - Tanizawa, O
AU  - Tanizawa O
LA  - eng
PT  - Journal Article
PL  - England
TA  - Am J Clin Pathol
JT  - American journal of clinical pathology
JID - 0370470
RN  - 0 (Antigens, Neoplasm)
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Biomarkers, Tumor)
RN  - 0 (Tn antigen)
RN  - 0 (sialosyl-Tn antigen)
SB  - AIM
SB  - IM
MH  - Antigens, Neoplasm/*analysis
MH  - *Antigens, Tumor-Associated, Carbohydrate
MH  - Biomarkers, Tumor/analysis
MH  - Female
MH  - Humans
MH  - Immunohistochemistry/methods
MH  - Ovarian Neoplasms/*immunology
MH  - Staining and Labeling
EDAT- 1991/12/01 00:00
MHDA- 1991/12/01 00:01
CRDT- 1991/12/01 00:00
PHST- 1991/12/01 00:00 [pubmed]
PHST- 1991/12/01 00:01 [medline]
PHST- 1991/12/01 00:00 [entrez]
AID - 10.1093/ajcp/96.6.711 [doi]
PST - ppublish
SO  - Am J Clin Pathol. 1991 Dec;96(6):711-6. doi: 10.1093/ajcp/96.6.711.

PMID- 8586620
OWN - NLM
STAT- MEDLINE
DCOM- 19960325
LR  - 20190512
IS  - 0021-924X (Print)
IS  - 0021-924X (Linking)
VI  - 117
IP  - 5
DP  - 1995 May
TI  - Production of monoclonal antibodies directed to Hanganutziu-Deicher active
      gangliosides, N-glycolylneuraminic acid-containing gangliosides.
PG  - 1062-9
AB  - We have established three kinds of monoclonal antibodies against gangliosides
      containing N-glycolylneuraminic acid (NeuGc) by immunization of BALB/c mice with 
      the purified gangliosides inserted into liposomes comprising Salmonella minnesota
      R595 lipopolysaccharides, and fusion of spleen cells with a mouse myeloma cell
      line. One monoclonal antibody, SHS-1, which was generated by immunizing mice with
      purified i-active ganglioside(NeuGc), reacted specifically with the i-active
      ganglioside(NeuGc) used as an immunogen. Structurally related gangliosides, such 
      as GM3(NeuGc), sialosylparagloboside (SPG) (NeuGc), or I-active
      ganglioside(NeuGc), corresponding gangliosides [GM3 containing N-acetylneuraminic
      acid (NeuAc), SPG(NeuAc), i-active ganglioside(NeuAc), and I-active
      ganglioside(NeuAc)], other gangliosides, or neutral glycosphingolipid (GSL) were 
      not recognized by the monoclonal antibody. These findings indicate that the SHS-1
      monoclonal antibody may be specific for NeuGc-containing i-active ganglioside. On
      the other hand, the other two monoclonal antibodies, MSG-1 and SPS-20, which were
      generated by immunizing mice with purified ganglioside GM3(NeuGc) and SPG(NeuGc),
      respectively, showed cross-reactivity to structurally related gangliosides. The
      MSG-1 monoclonal antibody exhibited reactivity to ganglioside GM3(NeuAc). The
      SPS-20 monoclonal antibody also cross-reacted with SPG(NeuAc), i-active
      ganglioside(NeuGc), and i-active ganglioside(NeuAc). Neither MSG-1 nor SPS-20
      reacted with corresponding gangliosides, other gangliosides, or neutral GSLs
      tested. Using the SHS-1 antibody specific for i-active ganglioside(NeuGc), we
      studied the expression of NeuGc-containing antigen in human colon cancer tissue. 
      An NeuGc-containing glycoconjugate was detected in the colon cancer tissue.
FAU - Watarai, S
AU  - Watarai S
AD  - Department of Cell Chemistry, Okayama University Medical School.
FAU - Kushi, Y
AU  - Kushi Y
FAU - Shigeto, R
AU  - Shigeto R
FAU - Misawa, N
AU  - Misawa N
FAU - Eishi, Y
AU  - Eishi Y
FAU - Handa, S
AU  - Handa S
FAU - Yasuda, T
AU  - Yasuda T
LA  - eng
PT  - Journal Article
PL  - England
TA  - J Biochem
JT  - Journal of biochemistry
JID - 0376600
RN  - 0 (Antibodies, Heterophile)
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens, Heterophile)
RN  - 0 (Antigens, Neoplasm)
RN  - 0 (Gangliosides)
RN  - 0 (Globosides)
RN  - 0 (Liposomes)
RN  - 0 (Neuraminic Acids)
RN  - 71833-57-3 (sialosylparagloboside)
SB  - IM
EIN - J Biochem (Tokyo) 1995 Aug;118(2):461
MH  - Animals
MH  - Antibodies, Heterophile/*immunology
MH  - Antibodies, Monoclonal/*biosynthesis
MH  - Antibody Formation
MH  - Antibody Specificity
MH  - Antigens, Heterophile/*immunology
MH  - Antigens, Neoplasm/analysis/chemistry/immunology
MH  - Carbohydrate Sequence
MH  - Colonic Neoplasms/chemistry/immunology
MH  - Gangliosides/chemistry/*immunology
MH  - Globosides/immunology
MH  - Humans
MH  - Immunohistochemistry
MH  - Liposomes/chemistry/immunology
MH  - Mice
MH  - Mice, Inbred BALB C
MH  - Molecular Sequence Data
MH  - Neuraminic Acids/immunology
EDAT- 1995/05/01 00:00
MHDA- 1995/05/01 00:01
CRDT- 1995/05/01 00:00
PHST- 1995/05/01 00:00 [pubmed]
PHST- 1995/05/01 00:01 [medline]
PHST- 1995/05/01 00:00 [entrez]
AID - 10.1093/oxfordjournals.jbchem.a124807 [doi]
PST - ppublish
SO  - J Biochem. 1995 May;117(5):1062-9. doi: 10.1093/oxfordjournals.jbchem.a124807.

PMID- 10368296
OWN - NLM
STAT- MEDLINE
DCOM- 19990506
LR  - 20170804
IS  - 0969-2126 (Print)
IS  - 0969-2126 (Linking)
VI  - 7
IP  - 3
DP  - 1999 Mar 15
TI  - A 30-angstrom-long U-shaped catalytic tunnel in the crystal structure of
      polyamine oxidase.
PG  - 265-76
AB  - BACKGROUND: Polyamines are essential for cell growth and differentiation;
      compounds interfering with their metabolism are potential anticancer agents.
      Polyamine oxidase (PAO) plays a central role in polyamine homeostasis. The enzyme
      utilises an FAD cofactor to catalyse the oxidation of the secondary amino groups 
      of spermine and spermidine. RESULTS: The first crystal structure of a polyamine
      oxidase has been determined to a resolution of 1.9 Angstroms. PAO from Zea mays
      contains two domains, which define a remarkable 30 Angstrom long U-shaped
      catalytic tunnel at their interface. The structure of PAO in complex with the
      inhibitor MDL72527 reveals the residues forming the catalytic machinery and
      unusual enzyme-inhibitor CH.O H bonds. A ring of glutamate and aspartate residues
      surrounding one of the two tunnel openings contributes to the steering of the
      substrate towards the inside of the tunnel. CONCLUSIONS: PAO specifically
      oxidizes substrates that have both primary and secondary amino groups. The
      complex with MDL72527 shows that the primary amino groups are essential for the
      proper alignment of the substrate with respect to the flavin. Conservation of an 
      N-terminal sequence motif indicates that PAO is member of a novel family of
      flavoenzymes. Among these, monoamine oxidase displays significant sequence
      homology with PAO, suggesting a similar overall folding topology.
FAU - Binda, C
AU  - Binda C
AD  - Dipartimento di Genetica e Microbiologia, Universita di Pavia, Via Abbiategrasso 
      207, I-27100 Pavia, Italy.
FAU - Coda, A
AU  - Coda A
FAU - Angelini, R
AU  - Angelini R
FAU - Federico, R
AU  - Federico R
FAU - Ascenzi, P
AU  - Ascenzi P
FAU - Mattevi, A
AU  - Mattevi A
LA  - eng
PT  - Comparative Study
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Structure
JT  - Structure (London, England : 1993)
JID - 101087697
RN  - 0 (Enzyme Inhibitors)
RN  - 0 (Plant Proteins)
RN  - 0 (Polyamines)
RN  - 146-14-5 (Flavin-Adenine Dinucleotide)
RN  - 1YVR349GN4 (MDL 72527)
RN  - EC 1.4.3.4 (Monoamine Oxidase)
RN  - EC 1.5.- (Oxidoreductases Acting on CH-NH Group Donors)
RN  - EC 1.5.3.- (polyamine oxidase)
RN  - V10TVZ52E4 (Putrescine)
SB  - IM
MH  - Amino Acid Sequence
MH  - Binding Sites
MH  - Catalytic Domain
MH  - Crystallography, X-Ray
MH  - Enzyme Inhibitors/pharmacology
MH  - Flavin-Adenine Dinucleotide/metabolism
MH  - Glycosylation
MH  - Hydrogen Bonding
MH  - Models, Molecular
MH  - Molecular Sequence Data
MH  - Monoamine Oxidase/chemistry
MH  - Oxidoreductases Acting on CH-NH Group Donors/antagonists & inhibitors/*chemistry
MH  - Plant Proteins/antagonists & inhibitors/*chemistry
MH  - Polyamines/metabolism
MH  - *Protein Conformation
MH  - Protein Processing, Post-Translational
MH  - Putrescine/analogs & derivatives/pharmacology
MH  - Sequence Alignment
MH  - Sequence Homology, Amino Acid
MH  - Substrate Specificity
MH  - Zea mays/enzymology
EDAT- 1999/06/16 00:00
MHDA- 1999/06/16 00:01
CRDT- 1999/06/16 00:00
PHST- 1999/06/16 00:00 [pubmed]
PHST- 1999/06/16 00:01 [medline]
PHST- 1999/06/16 00:00 [entrez]
AID - S0969-2126(99)80037-9 [pii]
PST - ppublish
SO  - Structure. 1999 Mar 15;7(3):265-76.

PMID- 6386148
OWN - NLM
STAT- MEDLINE
DCOM- 19841128
LR  - 20071114
IS  - 0008-5472 (Print)
IS  - 0008-5472 (Linking)
VI  - 44
IP  - 11
DP  - 1984 Nov
TI  - Characterization of sialosylated Lewisx as a new tumor-associated antigen.
PG  - 5279-85
AB  - A monoclonal antibody CSLEX1 which reacts with sialosyl Lex but not with sialosyl
      Lea has been produced. The CSLEX1 antigen has a tissue distribution similar to
      that of Lex, appearing characteristically in the proximal tubules of the kidney
      and on granulocytes. It is tumor associated in that 14 of 34 (41%) of tumor lines
      tested reacted with the CSLEX1 antibody, and 50 of 74 (68%) of tumor tissues
      tested reacted with the antibody. Loss of immunoperoxidase staining of tissues
      after neuraminidase treatment showed that the antibody is reacting to sialyl
      derivatives. The antibody reacted in solid-phase radioimmunoassay to
      sialosyllactofucopentaosyl(III)ceramide and sialosyldifucosylganglioside (6B).
      These results indicate that the CSLEX1 epitope has the following structure:
      (formula: see text) This structure had not previously been known to be tumor
      associated.
FAU - Fukushima, K
AU  - Fukushima K
FAU - Hirota, M
AU  - Hirota M
FAU - Terasaki, P I
AU  - Terasaki PI
FAU - Wakisaka, A
AU  - Wakisaka A
FAU - Togashi, H
AU  - Togashi H
FAU - Chia, D
AU  - Chia D
FAU - Suyama, N
AU  - Suyama N
FAU - Fukushi, Y
AU  - Fukushi Y
FAU - Nudelman, E
AU  - Nudelman E
FAU - Hakomori, S
AU  - Hakomori S
LA  - eng
GR  - CA10016/CA/NCI NIH HHS/United States
GR  - GM23100/GM/NIGMS NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Cancer Res
JT  - Cancer research
JID - 2984705R
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigen-Antibody Complex)
RN  - 0 (Antigens, Neoplasm)
RN  - EC 3.2.1.18 (Neuraminidase)
SB  - IM
MH  - Antibodies, Monoclonal
MH  - Antigen-Antibody Complex
MH  - Antigens, Neoplasm/*analysis
MH  - Carbohydrate Conformation
MH  - Carbohydrate Sequence
MH  - Cell Line
MH  - Erythrocytes/immunology
MH  - Female
MH  - Fluorescent Antibody Technique
MH  - Humans
MH  - Immunoenzyme Techniques
MH  - Leukocytes/immunology
MH  - Neoplasms/immunology
MH  - Neuraminidase
EDAT- 1984/11/01 00:00
MHDA- 1984/11/01 00:01
CRDT- 1984/11/01 00:00
PHST- 1984/11/01 00:00 [pubmed]
PHST- 1984/11/01 00:01 [medline]
PHST- 1984/11/01 00:00 [entrez]
PST - ppublish
SO  - Cancer Res. 1984 Nov;44(11):5279-85.

PMID- 6200484
OWN - NLM
STAT- MEDLINE
DCOM- 19840511
LR  - 20071114
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 259
IP  - 7
DP  - 1984 Apr 10
TI  - Novel fucolipids accumulating in human adenocarcinoma. II. Selective isolation of
      hybridoma antibodies that differentially recognize mono-, di-, and trifucosylated
      type 2 chain.
PG  - 4681-5
AB  - A series of glycolipids having the X determinant (Gal beta 1----4 [Fuc
      alpha----3]GlcNAc) at the terminus and a fucosyl alpha 1----3 residue at the
      internal GlcNAc residue have been isolated and characterized from tumor tissues
      (Hakomori, S., Nudelman, E., Levery, S.B., and Kannagi, R. (1984) J. Biol. Chem. 
      259, 4672-4680. A series of monoclonal antibodies that differentially recognize
      glycolipids with mono-, di-, and trifucosylated type 2 chain have been isolated
      and characterized. The antibody FH4 shows a remarkable preferential reactivity
      towards di-/or trifucosylated type 2 chain, i.e. it does not react with
      monofucosylated structures, including lactofucopentaosyl (III) ceramide
      (III3FucnLc4), monofucosyl neolactonorhexaosylceramide (y2, V3FucnLc6), and
      monofucosyl neolactonoroctaosylceramide (Z1, VII3FucnLc8), but reacts well with
      di- and trifucosylated type 2 chain structures such as difucosyl
      neolactonorhexaosylceramide (III3V3Fuc2nLc6) and trifucosyl
      neolactonoroctaosylceramide (III3V3VII3Fuc3nLc8). Two other monoclonal
      antibodies, FH5 and ACFH18, preferentially react with trifucosylated type 2 chain
      structure (III3V3VII3Fuc3nLc8), although cross-reactivity with difucosylated type
      2 chain (III3V3Fuc2nLc6) was observed. They showed a minimal cross-reaction with 
      monofucosylated type 2 chain. In contrast, the antibody FH1 does not react with
      III3FucnLc4 but reacts with V3FucnLc6, III3V3Fuc2nLc6, and III3V3VII3Fuc3nLc8.
      Two monoclonal antibodies, FH2 and FH3, do not discriminate among various
      glycolipids having fucosylated type 2 chain, and their reactivities are
      essentially similar to previously established antibodies directed to the X
      determinant, such as anti-SSEA-1, WGHS 29, VEP8 and 9, My-1, etc. This series of 
      antibodies will be useful to detect the specific type of glycolipid with
      fucosylated type 2 chain accumulating in human cancer and in undifferentiated
      cells.
FAU - Fukushi, Y
AU  - Fukushi Y
FAU - Hakomori, S
AU  - Hakomori S
FAU - Nudelman, E
AU  - Nudelman E
FAU - Cochran, N
AU  - Cochran N
LA  - eng
GR  - CA20026/CA/NCI NIH HHS/United States
GR  - GM23100/GM/NIGMS NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigen-Antibody Complex)
RN  - 0 (Epitopes)
RN  - 0 (Glycolipids)
RN  - 0 (fucolipids)
SB  - IM
MH  - Adenocarcinoma/*analysis
MH  - Antibodies, Monoclonal
MH  - Antigen-Antibody Complex
MH  - Carbohydrate Conformation
MH  - Carbohydrate Sequence
MH  - Cell Line
MH  - Epitopes/analysis
MH  - Glycolipids/*analysis/immunology
MH  - Humans
MH  - Hybridomas/immunology
MH  - Structure-Activity Relationship
EDAT- 1984/04/10 00:00
MHDA- 1984/04/10 00:01
CRDT- 1984/04/10 00:00
PHST- 1984/04/10 00:00 [pubmed]
PHST- 1984/04/10 00:01 [medline]
PHST- 1984/04/10 00:00 [entrez]
PST - ppublish
SO  - J Biol Chem. 1984 Apr 10;259(7):4681-5.

PMID- 8652594
OWN - NLM
STAT- MEDLINE
DCOM- 19960730
LR  - 20061115
IS  - 0006-2960 (Print)
IS  - 0006-2960 (Linking)
VI  - 35
IP  - 7
DP  - 1996 Feb 20
TI  - Lipopolysaccharides of Helicobacter pylori strains P466 and MO19: structures of
      the O antigen and core oligosaccharide regions.
PG  - 2498-504
AB  - Lipopolysaccharides (LPS) from phenol-water extraction of dyspeptic (P466) and
      asymptomatic (MO19) strains of Helicobacter pylori were each isolated as
      water-soluble material of high relative molecular mass (high M(r)) and as
      water-insoluble gels of low M(r). Chemical and spectroscopic analyses of the
      soluble LPS and oligosaccharides liberated from the water-insoluble gels led to
      proposed structures for chains comprising the O antigen, intervening, and core
      regions. As in the LPS from the type strain NCTC 11637 [Aspinall, G. O., et al.
      (1996) Biochemistry 35, 2489-2497], the O antigen region of the P466 LPS is
      characterized by the presence of extended chains with fucosylated and
      nonfucosylated N-acetyllactosamine units, the former carrying
      alpha-L-fucopyranose units at O-3 of beta-D-GlcNAc residues. This structure
      differs from that of the type strain in termination of the O chain by a Lewis(y) 
      (Le(y)) antigenic determinant
      [alpha-L-Fuc(1-->2)beta-D-Gal(1-->4)[alpha-L-Fuc(1-->3)]beta-D-GlcNAc] but also
      has internal Lewis(x) (Le(x)) units. The inner core region of the P466 LPS is
      indistinguishable from that in the type strain. In contrast, the O antigen region
      of the LPS from strain MO19 consists of a single Le(y) epitope linked via a
      3-linked beta-D-Gal to an intervening region on the basis of a sequence of
      3-linked D-glycero-alpha-D-manno-heptose residues which is in turn linked to an
      inner core identical to that in the type strain and the P466 strain. Results in
      this and the preceding paper show that LPS from the three H. pylori strains
      display molecular mimicry of human cell surface glycoconjugates but may vary in
      the expression of Le(x) or Le(y) determinants, the degree of O antigen chain
      extension, or in the presence of an additional region between the inner core and 
      the O antigen.
FAU - Aspinall, G O
AU  - Aspinall GO
AD  - Department of Chemistry, York University, Toronto, Ontario, Canada.
FAU - Monteiro, M A
AU  - Monteiro MA
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Biochemistry
JT  - Biochemistry
JID - 0370623
RN  - 0 (O Antigens)
RN  - 0 (Oligosaccharides)
SB  - IM
MH  - Carbohydrate Conformation
MH  - Carbohydrate Sequence
MH  - Helicobacter pylori/*chemistry
MH  - Magnetic Resonance Spectroscopy
MH  - Molecular Sequence Data
MH  - O Antigens/*chemistry
MH  - Oligosaccharides/*chemistry
MH  - Spectrometry, Mass, Fast Atom Bombardment
EDAT- 1996/02/20 00:00
MHDA- 1996/02/20 00:01
CRDT- 1996/02/20 00:00
PHST- 1996/02/20 00:00 [pubmed]
PHST- 1996/02/20 00:01 [medline]
PHST- 1996/02/20 00:00 [entrez]
AID - 10.1021/bi951853k [doi]
AID - bi951853k [pii]
PST - ppublish
SO  - Biochemistry. 1996 Feb 20;35(7):2498-504. doi: 10.1021/bi951853k.

PMID- 12390975
OWN - NLM
STAT- MEDLINE
DCOM- 20021213
LR  - 20190513
IS  - 0006-8950 (Print)
IS  - 0006-8950 (Linking)
VI  - 125
IP  - Pt 11
DP  - 2002 Nov
TI  - Localization of major gangliosides in the PNS: implications for immune
      neuropathies.
PG  - 2491-506
AB  - Antibodies targeting major gangliosides that are broadly distributed in the
      nervous system are sometimes associated with clinical symptoms that imply
      selective nerve damage. For example, anti-GD1a antibodies are associated with
      acute motor axonal neuropathy (AMAN), a form of Guillain-Barre syndrome that
      selectively affects motor nerves, despite reports that GD1a is present in human
      axons and myelin and is not expressed differentially in motor versus sensory
      roots. We used a series of high-affinity monoclonal antibodies (mAbs) against the
      major nervous system gangliosides GM1, GD1a, GD1b and GT1b to test whether any of
      them bind motor or sensory fibres differentially in rodent and human peripheral
      nerves. The following observations were made. (i) Some of the anti-GD1a
      antibodies preferentially stained motor fibres, supporting the association of
      human anti-GD1a antibodies with predominant motor neuropathies such as AMAN. (ii)
      A GD1b antibody preferentially stained the large dorsal root ganglion (DRG)
      neurones, in keeping with the proposed role of human anti-GD1b antibodies in
      sensory ataxic neuropathies. (iii) Two mAbs with broad structural
      cross-reactivity bound to both gangliosides and peripheral nerve proteins. (iv)
      Myelin was poorly stained; all clones stained axons nearly exclusively. Our
      findings suggest that anti-ganglioside antibody fine specificity as well as
      differences in ganglioside accessibility in axons and myelin influence the
      selectivity of injury to different fibre systems and cell types in human
      autoimmune neuropathies.
FAU - Gong, Y
AU  - Gong Y
AD  - Department of Neurology, Johns Hopkins Medical Institutions, Baltimore, MD 21205,
      USA.
FAU - Tagawa, Y
AU  - Tagawa Y
FAU - Lunn, M P T
AU  - Lunn MP
FAU - Laroy, W
AU  - Laroy W
FAU - Heffer-Lauc, M
AU  - Heffer-Lauc M
FAU - Li, C Y
AU  - Li CY
FAU - Griffin, J W
AU  - Griffin JW
FAU - Schnaar, R L
AU  - Schnaar RL
FAU - Sheikh, K A
AU  - Sheikh KA
LA  - eng
GR  - NS31528/NS/NINDS NIH HHS/United States
GR  - NS42888/NS/NINDS NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - England
TA  - Brain
JT  - Brain : a journal of neurology
JID - 0372537
RN  - 0 (Gangliosides)
RN  - 12707-58-3 (ganglioside, GD1a)
RN  - 37758-47-7 (G(M1) Ganglioside)
RN  - 59247-13-1 (trisialoganglioside GT1)
SB  - AIM
SB  - IM
MH  - Animals
MH  - Axons/immunology/metabolism/pathology
MH  - Female
MH  - G(M1) Ganglioside/immunology/metabolism
MH  - Ganglia, Spinal/immunology/metabolism/pathology
MH  - Gangliosides/immunology/*metabolism
MH  - Humans
MH  - Immunohistochemistry
MH  - Male
MH  - Mice
MH  - Motor Neurons/immunology/metabolism/pathology
MH  - Neurons, Afferent/immunology/metabolism/pathology
MH  - Peripheral Nervous System/immunology/*metabolism/pathology
MH  - Peripheral Nervous System Diseases/immunology/*metabolism/pathology
MH  - Polyradiculoneuropathy/immunology/*metabolism/pathology
MH  - Rats
EDAT- 2002/10/23 04:00
MHDA- 2002/12/17 04:00
CRDT- 2002/10/23 04:00
PHST- 2002/10/23 04:00 [pubmed]
PHST- 2002/12/17 04:00 [medline]
PHST- 2002/10/23 04:00 [entrez]
AID - 10.1093/brain/awf258 [doi]
PST - ppublish
SO  - Brain. 2002 Nov;125(Pt 11):2491-506. doi: 10.1093/brain/awf258.

PMID- 10096092
OWN - NLM
STAT- MEDLINE
DCOM- 19990715
LR  - 20171116
IS  - 0950-382X (Print)
IS  - 0950-382X (Linking)
VI  - 31
IP  - 4
DP  - 1999 Feb
TI  - Molecular genetic basis for the variable expression of Lewis Y antigen in
      Helicobacter pylori: analysis of the alpha (1,2) fucosyltransferase gene.
PG  - 1265-74
AB  - Helicobacter pylori lipopolysaccharides (LPS) express human oncofetal antigens
      Lewis X and Lewis Y. The synthesis of Lewis Y involves the actions of alpha (1,3)
      and alpha (1,2) fucosyltransferases (FucTs). Here, we report the molecular
      cloning and characterization of genes encoding H. pylori alpha (1,2) FucT (Hp
      fucT2) from various H. pylori strains. We constructed Hp fucT2 knock-out mutants 
      and demonstrated the loss of Lewis Y production in these mutants by enzyme-linked
      immunosorbent assay (ELISA) and immunoelectron microscopy. The Hp fucT2 gene
      contains a hypermutable sequence [poly (C) and TAA repeats], which provides a
      possibility of frequent shifting into and out of coding frame by a polymerase
      slippage mechanism. Thus, the Hp fucT2 gene displays two major genotypes,
      consisting of either a single full-length open reading frame (ORF; as in the
      strain UA802) or truncated ORFs (as in the strain 26695). In vitro expression of 
      Hp fucT2 genes demonstrated that both types of the gene have the potential to
      produce the full-length protein. The production of the full-length protein by the
      26695 fucT2 gene could be attributed to translational-1 frameshifting, as a
      perfect translation frameshift cassette resembling that of the Escherichia coli
      dnaX gene is present. Examination of the strain UA1174 revealed that its fucT2
      gene has a frameshifted ORF at the DNA level, which cannot be compensated by
      translation frameshifting, accounting for its Lewis Y off phenotype. In another
      strain, UA1218, the fucT2 gene is apparently turned off because of the loss of
      its promoter. Based on these data, we proposed a model for the variable
      expression of Lewis Y by H. pylori, in which regulation at the level of
      replication slippage (mutation), transcription and translation of the fucT2 gene 
      may all be involved.
FAU - Wang, G
AU  - Wang G
AD  - Department of Medical Microbiology and Immunology, University of Alberta,
      Edmonton, Canada.
FAU - Rasko, D A
AU  - Rasko DA
FAU - Sherburne, R
AU  - Sherburne R
FAU - Taylor, D E
AU  - Taylor DE
LA  - eng
SI  - GENBANK/AF076779
SI  - GENBANK/AF093828
SI  - GENBANK/AF093829
SI  - GENBANK/AF093830
SI  - GENBANK/AF093831
SI  - GENBANK/AF093832
SI  - GENBANK/AF093833
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - Mol Microbiol
JT  - Molecular microbiology
JID - 8712028
RN  - 0 (DNA, Bacterial)
RN  - 0 (Lewis Blood-Group System)
RN  - 0 (Lewis X Antigen)
RN  - 0 (Lewis Y antigen)
RN  - EC 2.4.1.- (Fucosyltransferases)
RN  - EC 2.4.1.69 (galactoside 2-alpha-L-fucosyltransferase)
SB  - IM
MH  - Amino Acid Sequence
MH  - Base Sequence
MH  - DNA, Bacterial/genetics
MH  - Electrophoresis, Polyacrylamide Gel
MH  - Enzyme-Linked Immunosorbent Assay
MH  - Fucosyltransferases/chemistry/*genetics/*metabolism
MH  - Helicobacter pylori/enzymology/*genetics
MH  - Humans
MH  - Immunoblotting
MH  - Lewis Blood-Group System/*biosynthesis
MH  - Lewis X Antigen/biosynthesis
MH  - Microscopy, Immunoelectron
MH  - Molecular Sequence Data
MH  - Mutagenesis, Insertional
MH  - Plasmids/genetics
MH  - Sequence Analysis, DNA
EDAT- 1999/03/30 00:00
MHDA- 1999/03/30 00:01
CRDT- 1999/03/30 00:00
PHST- 1999/03/30 00:00 [pubmed]
PHST- 1999/03/30 00:01 [medline]
PHST- 1999/03/30 00:00 [entrez]
PST - ppublish
SO  - Mol Microbiol. 1999 Feb;31(4):1265-74.

PMID- 14670721
OWN - NLM
STAT- MEDLINE
DCOM- 20040712
LR  - 20131121
IS  - 0008-6215 (Print)
IS  - 0008-6215 (Linking)
VI  - 338
IP  - 23
DP  - 2003 Nov 14
TI  - Chemo-enzymatic synthesis of a tetra- and octasaccharide fragment of the capsular
      polysaccharide of Streptococcus pneumoniae type 14.
PG  - 2611-27
AB  - The chemo-enzymatic synthesis is described of tetrasaccharide
      beta-D-Galp-(1-->4)-beta-D-Glcp-(1-->6)-[beta-D-Galp-(1-->4)]-beta-D-GlcpNAc-(1--
      >O(CH(2))(6)NH(2) (1) and octasaccharide
      beta-D-Galp-(1-->4)-beta-D-Glcp-(1-->6)-[beta-D-Galp-(1-->4)]-beta-D-GlcpNAc-(1--
      >3)-beta-D-Galp-(1-->4)-beta-D-Glcp-(1-->6)-[beta-D-Galp-(1-->4)]-beta-D-GlcpNAc-
      (1-->O(CH(2))(6)NH(2) (2), representing one and two tetrasaccharide repeating
      units of Streptococcus pneumoniae serotype 14 capsular polysaccharide. In a
      chemical approach, the intermediate linear trisaccharide 3 and hexasaccharide 4
      were synthesized. Galactose residues were beta-(1-->4)-connected to the internal 
      N-acetyl-beta-D-glucosamine residues by using bovine milk
      beta-1,4-galactosyltransferase. Both title oligosaccharides will be conjugated to
      carrier proteins to be tested as potential vaccines in animal models.
FAU - Joosten, John A F
AU  - Joosten JA
AD  - Bijvoet Center, Department of Bio-Organic Chemistry, Section of Glycoscience and 
      Biocatalysis, Utrecht University, Padualaan 8, NL-3584 CH Utrecht, The
      Netherlands.
FAU - Kamerling, Johannis P
AU  - Kamerling JP
FAU - Vliegenthart, Johannes F G
AU  - Vliegenthart JF
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - Netherlands
TA  - Carbohydr Res
JT  - Carbohydrate research
JID - 0043535
RN  - 0 (Carbohydrates)
RN  - 0 (Polysaccharides)
RN  - 0 (Polysaccharides, Bacterial)
RN  - EC 2.4.1.90 (N-Acetyllactosamine Synthase)
RN  - N08U5BOQ1K (Glucosamine)
SB  - IM
MH  - Animals
MH  - Carbohydrate Sequence
MH  - Carbohydrates/chemistry
MH  - Cattle
MH  - Glucosamine/chemistry
MH  - Magnetic Resonance Spectroscopy
MH  - Molecular Sequence Data
MH  - N-Acetyllactosamine Synthase/metabolism
MH  - Polysaccharides/chemical synthesis
MH  - Polysaccharides, Bacterial/*chemistry
MH  - Streptococcus pneumoniae/*metabolism
MH  - Temperature
EDAT- 2003/12/13 05:00
MHDA- 2004/07/13 05:00
CRDT- 2003/12/13 05:00
PHST- 2003/12/13 05:00 [pubmed]
PHST- 2004/07/13 05:00 [medline]
PHST- 2003/12/13 05:00 [entrez]
AID - S0008621503003136 [pii]
PST - ppublish
SO  - Carbohydr Res. 2003 Nov 14;338(23):2611-27.

PMID- 3516890
OWN - NLM
STAT- MEDLINE
DCOM- 19860612
LR  - 20160303
IS  - 0020-7136 (Print)
IS  - 0020-7136 (Linking)
VI  - 37
IP  - 5
DP  - 1986 May 15
TI  - Immunohistologic expression of blood-group antigens in normal human
      gastrointestinal tract and colonic carcinoma.
PG  - 667-76
AB  - A panel of 7 mouse monoclonal antibodies and the lectin from Ulex europeus,
      detecting blood-group-related antigens of the ABH and Lewis systems, have been
      used to define the distribution of these antigenic structures within the human
      gastrointestinal tract, and to characterize their expression and modulation in
      colorectal carcinomas. The reagents employed detect the following blood-group
      specificities: A (all variants), B, H (type 2), Lewisa, Lewisb, X (Lewisx), Y
      (Lewisy) and type 1 precursor chain. Immunohistochemical studies demonstrate that
      these antigens are differentially expressed in various cell types and
      developmental stages of the human gastrointestinal tract. ABH expression
      undergoes developmental modulation in the human colorectal tract from positive to
      negative during embryogenesis, and is lost in adult cells. Colorectal tumors
      exhibit neosynthesis of ABH specificities that appear in tumor cells, and
      accumulation of the precursor antigens. They also show increased expression of
      Lewis antigens, especially Y determinant, which has a restricted pattern of
      distribution in normal tissues and is not found in normal colonic mucosa.
      Enhancement of the Lewis antigens is observed in all colorectal tumors analyzed, 
      regardless of blood-group type and secretory status of the individuals studied.
      Tumor modulation of these antigens may be related to activation of suppressed
      genes and enhancement of fucosyltransferases.
FAU - Cordon-Cardo, C
AU  - Cordon-Cardo C
FAU - Lloyd, K O
AU  - Lloyd KO
FAU - Sakamoto, J
AU  - Sakamoto J
FAU - McGroarty, M E
AU  - McGroarty ME
FAU - Old, L J
AU  - Old LJ
FAU - Melamed, M R
AU  - Melamed MR
LA  - eng
GR  - CA-08148/CA/NCI NIH HHS/United States
GR  - CA-34039/CA/NCI NIH HHS/United States
GR  - CA-34134/CA/NCI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Int J Cancer
JT  - International journal of cancer
JID - 0042124
RN  - 0 (ABO Blood-Group System)
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Blood Group Antigens)
RN  - 0 (Lectins)
RN  - 0 (Lewis Blood-Group System)
RN  - 0 (Plant Lectins)
RN  - 0 (Ulex europaeus lectins)
SB  - IM
MH  - ABO Blood-Group System/immunology
MH  - Adult
MH  - Aged
MH  - Antibodies, Monoclonal
MH  - Blood Group Antigens/*immunology
MH  - Carcinoma/*immunology
MH  - Colonic Neoplasms/*immunology
MH  - Digestive System/*immunology
MH  - Female
MH  - Fluorescent Antibody Technique
MH  - Humans
MH  - Immunoenzyme Techniques
MH  - Intestinal Mucosa/immunology
MH  - Lectins
MH  - Lewis Blood-Group System/immunology
MH  - Male
MH  - Middle Aged
MH  - *Plant Lectins
MH  - Rectal Neoplasms/*immunology
EDAT- 1986/05/15 00:00
MHDA- 1986/05/15 00:01
CRDT- 1986/05/15 00:00
PHST- 1986/05/15 00:00 [pubmed]
PHST- 1986/05/15 00:01 [medline]
PHST- 1986/05/15 00:00 [entrez]
PST - ppublish
SO  - Int J Cancer. 1986 May 15;37(5):667-76.

PMID- 10950950
OWN - NLM
STAT- MEDLINE
DCOM- 20010104
LR  - 20171116
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 275
IP  - 45
DP  - 2000 Nov 10
TI  - Binding of a large chondroitin sulfate/dermatan sulfate proteoglycan, versican,
      to L-selectin, P-selectin, and CD44.
PG  - 35448-56
AB  - Here we show that a large chondroitin sulfate proteoglycan, versican, derived
      from a renal adenocarcinoma cell line ACHN, binds L-selectin, P-selectin, and
      CD44. The binding was mediated by the interaction of the chondroitin sulfate (CS)
      chain of versican with the carbohydrate-binding domain of L- and P-selectin and
      CD44. The binding of versican to L- and P-selectin was inhibited by CS B, CS E,
      and heparan sulfate (HS) but not by any other glycosaminoglycans tested. On the
      other hand, the binding to CD44 was inhibited by hyaluronic acid, chondroitin
      (CH), CS A, CS B, CS C, CS D, and CS E but not by HS or keratan sulfate. A
      cross-blocking study indicated that L- and P-selectin recognize close or
      overlapping sites on versican, whereas CD44 recognizes separate sites. We also
      show that soluble L- and P-selectin directly bind to immobilized CS B, CS E, and 
      HS and that soluble CD44 directly binds to immobilized hyaluronic acid, CH, and
      all the CS chains examined. Consistent with these results, structural analysis
      showed that versican is modified with at least CS B and CS C. Thus, proteoglycans
      sufficiently modified with the appropriate glycosaminoglycans should be able to
      bind L-selectin, P-selectin, and/or CD44.
FAU - Kawashima, H
AU  - Kawashima H
AD  - Department of Bioregulation, Biomedical Research Center, Osaka University
      Graduate School of Medicine 2-2, Yamada-oka, Suita 565-0871, Japan.
FAU - Hirose, M
AU  - Hirose M
FAU - Hirose, J
AU  - Hirose J
FAU - Nagakubo, D
AU  - Nagakubo D
FAU - Plaas, A H
AU  - Plaas AH
FAU - Miyasaka, M
AU  - Miyasaka M
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Chondroitin Sulfate Proteoglycans)
RN  - 0 (Cross-Linking Reagents)
RN  - 0 (Cspg2 protein, mouse)
RN  - 0 (DNA, Complementary)
RN  - 0 (Glycosaminoglycans)
RN  - 0 (Hyaluronan Receptors)
RN  - 0 (Lectins, C-Type)
RN  - 0 (P-Selectin)
RN  - 0 (Proteoglycans)
RN  - 0 (VCAN protein, human)
RN  - 126880-86-2 (L-Selectin)
RN  - 126968-45-4 (Versicans)
RN  - 24967-94-0 (Dermatan Sulfate)
RN  - 9004-61-9 (Hyaluronic Acid)
RN  - 9007-27-6 (Chondroitin)
RN  - 9007-28-7 (Chondroitin Sulfates)
RN  - 9056-36-4 (Keratan Sulfate)
RN  - EC 4.2.2.- (Chondroitinases and Chondroitin Lyases)
RN  - EC 4.2.2.20 (Chondroitin ABC Lyase)
SB  - IM
MH  - Animals
MH  - Biotinylation
MH  - Blotting, Western
MH  - Chondroitin/pharmacology
MH  - Chondroitin ABC Lyase/pharmacology
MH  - Chondroitin Sulfate Proteoglycans/*metabolism
MH  - Chondroitin Sulfates/*metabolism
MH  - Chondroitinases and Chondroitin Lyases/pharmacology
MH  - Cross-Linking Reagents/pharmacology
MH  - DNA, Complementary/metabolism
MH  - Dermatan Sulfate/*metabolism
MH  - Dose-Response Relationship, Drug
MH  - Electrophoresis
MH  - Electrophoresis, Polyacrylamide Gel
MH  - Enzyme-Linked Immunosorbent Assay
MH  - Glycosaminoglycans/metabolism
MH  - Humans
MH  - Hyaluronan Receptors/*metabolism
MH  - Hyaluronic Acid/pharmacology
MH  - Keratan Sulfate/pharmacology
MH  - Kinetics
MH  - L-Selectin/*metabolism
MH  - Lectins, C-Type
MH  - Lipid Metabolism
MH  - Mice
MH  - P-Selectin/*metabolism
MH  - Protein Binding
MH  - Proteoglycans/*metabolism
MH  - Transfection
MH  - Tumor Cells, Cultured
MH  - Versicans
EDAT- 2000/08/22 11:00
MHDA- 2001/02/28 10:01
CRDT- 2000/08/22 11:00
PHST- 2000/08/22 11:00 [pubmed]
PHST- 2001/02/28 10:01 [medline]
PHST- 2000/08/22 11:00 [entrez]
AID - 10.1074/jbc.M003387200 [doi]
AID - M003387200 [pii]
PST - ppublish
SO  - J Biol Chem. 2000 Nov 10;275(45):35448-56. doi: 10.1074/jbc.M003387200.

PMID- 9228738
OWN - NLM
STAT- MEDLINE
DCOM- 19970813
LR  - 20171223
IS  - 0008-6215 (Print)
IS  - 0008-6215 (Linking)
VI  - 301
IP  - 1-2
DP  - 1997 Jun 11
TI  - Structural characterisation of the exocellular polysaccharide produced by
      Streptococcus thermophilus OR 901.
PG  - 41-50
AB  - The exocellular polysaccharide of Streptococcus thermophilus OR 901, isolated
      from partially deproteinised whey, is a heteropolymer of D-galactopyranose and
      L-rhamnopyranose residues in the molar ratio 5:2. The structure was established
      by methylation analysis and 1D and 2D NMR spectroscopy of the native
      polysaccharide, in combination with characterisation of oligosaccharide
      fragments, obtained by partial acid hydrolysis, using methylation analysis and 1D
      1H NMR spectroscopy. The polysaccharide has a branched heptasaccharide repeating 
      unit with the following structure: [sequence: see text]
FAU - Bubb, W A
AU  - Bubb WA
AD  - Department of Biochemistry, University of Sydney, NSW, Australia.
      wab@biochem.usyd.edu.au
FAU - Urashima, T
AU  - Urashima T
FAU - Fujiwara, R
AU  - Fujiwara R
FAU - Shinnai, T
AU  - Shinnai T
FAU - Ariga, H
AU  - Ariga H
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - Netherlands
TA  - Carbohydr Res
JT  - Carbohydrate research
JID - 0043535
RN  - 0 (Monosaccharides)
RN  - 0 (Polysaccharides, Bacterial)
RN  - 0 (exopolysaccharide, Streptococcus)
SB  - IM
MH  - Carbohydrate Conformation
MH  - Carbohydrate Sequence
MH  - Magnetic Resonance Spectroscopy
MH  - Molecular Sequence Data
MH  - Monosaccharides/analysis/chemistry
MH  - Polysaccharides, Bacterial/*chemistry
MH  - Sequence Analysis
MH  - Streptococcus/*chemistry
EDAT- 1997/06/11 00:00
MHDA- 1997/06/11 00:01
CRDT- 1997/06/11 00:00
PHST- 1997/06/11 00:00 [pubmed]
PHST- 1997/06/11 00:01 [medline]
PHST- 1997/06/11 00:00 [entrez]
AID - S0008-6215(97)00083-9 [pii]
PST - ppublish
SO  - Carbohydr Res. 1997 Jun 11;301(1-2):41-50.

PMID- 3345524
OWN - NLM
STAT- MEDLINE
DCOM- 19880414
LR  - 20151119
IS  - 0008-5472 (Print)
IS  - 0008-5472 (Linking)
VI  - 48
IP  - 6
DP  - 1988 Mar 15
TI  - Detection of patients with cancer by monoclonal antibody directed to
      lactoneotetraosylceramide (paragloboside).
PG  - 1512-6
AB  - A hybridoma producing monoclonal antibody (H11) directed to
      lactoneotetraosylceramide (paragloboside) has been established from spleen cells 
      of a mouse immunized with paragloboside. The monoclonal antibody H11
      (immunoglobulin M type) was selected from five clones showing different
      reactivities with paragloboside. The monoclonal antibody was highly specific to
      paragloboside and lacked reactivity with other glycolipids including
      glucosylceramide, lactosylceramide, globotriaosylceramide,
      globotetraosylceramide, gangliotriaosylceramide, gangliotetraosylceramide, and
      GalNAc beta 1-4[NeuAc alpha 2-3]Gal beta 1-4Glc beta 1-1Cer. However, the
      monoclonal antibody (H11) was found to bind to lactosamine-containing glycolipids
      at their terminals, such as i- and I-type glycolipids as well as paragloboside. A
      two-step sandwich radioimmunoassay method for paragloboside antigen in serum was 
      established by using the monoclonal antibody. The mean paragloboside antigen
      concentration in the sera from 20 normal individuals was 25.3 ng/ml. If the
      cutoff value was set at 80.9 ng/ml [25.3 + 2 x 27.8 (SD)], only 1 of 20 healthy
      controls had an elevated paragloboside value in the serum, whereas sera from 9 of
      12 (75.0%) hepatoma, 4 of 10 (40%) pancreatic cancer, 16 of 40 (40.0%) stomach
      cancer, and 6 of 10 (60%) lung cancer patients had elevated paragloboside values.
      Sera from 3 of 8 hepatitis patients and 7 of 10 liver cirrhosis patients were
      estimated to be positive but sera from 16 patients with benign disease had
      paragloboside levels lower than the cutoff value. A larger amount of the antigen 
      was found in liver metastases from colorectal carcinoma compared to the normal
      counterpart. The antigen was also detected in the medium of various human cancer 
      cells and meconium. However, the antigen in the sera, medium, meconium, and
      cancer tissue seemed to be associated with glycoprotein or lipoprotein, because
      most of the antigen activity was eluted in the void volume fraction on
      high-performance liquid chromatography with a gel filtration column.
FAU - Myoga, A
AU  - Myoga A
AD  - Institute of Dainabot Co., Ltd., Chiba, Japan.
FAU - Taki, T
AU  - Taki T
FAU - Arai, K
AU  - Arai K
FAU - Sekiguchi, K
AU  - Sekiguchi K
FAU - Ikeda, I
AU  - Ikeda I
FAU - Kurata, K
AU  - Kurata K
FAU - Matsumoto, M
AU  - Matsumoto M
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Cancer Res
JT  - Cancer research
JID - 2984705R
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Culture Media)
RN  - 0 (Globosides)
RN  - 0 (Glycosphingolipids)
RN  - 56573-54-7 (paragloboside)
SB  - IM
MH  - *Antibodies, Monoclonal
MH  - Antibody Specificity
MH  - Culture Media/analysis
MH  - Globosides/*analysis/immunology
MH  - Glycosphingolipids/*analysis
MH  - Humans
MH  - Meconium/analysis
MH  - Neoplasms/*analysis/diagnosis
MH  - Radioimmunoassay
MH  - Tumor Cells, Cultured/analysis
EDAT- 1988/03/15 00:00
MHDA- 1988/03/15 00:01
CRDT- 1988/03/15 00:00
PHST- 1988/03/15 00:00 [pubmed]
PHST- 1988/03/15 00:01 [medline]
PHST- 1988/03/15 00:00 [entrez]
PST - ppublish
SO  - Cancer Res. 1988 Mar 15;48(6):1512-6.

PMID- 6983878
OWN - NLM
STAT- MEDLINE
DCOM- 19830214
LR  - 20061115
IS  - 0006-291X (Print)
IS  - 0006-291X (Linking)
VI  - 108
IP  - 3
DP  - 1982 Oct 15
TI  - Radioimmuno-thin-layer chromatographic detection of Forssman antigen in human
      carcinoma cell lines.
PG  - 926-32
FAU - Mori, E
AU  - Mori E
FAU - Mori, T
AU  - Mori T
FAU - Sanai, Y
AU  - Sanai Y
FAU - Nagai, Y
AU  - Nagai Y
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Biochem Biophys Res Commun
JT  - Biochemical and biophysical research communications
JID - 0372516
RN  - 0 (Antigens, Heterophile)
RN  - 9013-60-9 (Forssman Antigen)
SB  - IM
MH  - Animals
MH  - Antigens, Heterophile/*analysis
MH  - Breast Neoplasms/analysis
MH  - Cell Line
MH  - Chromatography, Thin Layer/methods
MH  - Forssman Antigen/*analysis
MH  - Guinea Pigs
MH  - Humans
MH  - Lung Neoplasms/analysis
MH  - Neoplasms/*analysis
MH  - Radioimmunoassay/methods
MH  - Rectal Neoplasms/analysis
MH  - Stomach Neoplasms/analysis
EDAT- 1982/10/15 00:00
MHDA- 1982/10/15 00:01
CRDT- 1982/10/15 00:00
PHST- 1982/10/15 00:00 [pubmed]
PHST- 1982/10/15 00:01 [medline]
PHST- 1982/10/15 00:00 [entrez]
AID - 0006-291X(82)92087-3 [pii]
PST - ppublish
SO  - Biochem Biophys Res Commun. 1982 Oct 15;108(3):926-32.

PMID- 6770273
OWN - NLM
STAT- MEDLINE
DCOM- 19800825
LR  - 20071115
IS  - 0028-0836 (Print)
IS  - 0028-0836 (Linking)
VI  - 285
IP  - 5764
DP  - 1980 Jun 5
TI  - K562 human leukaemic cells express fetal type (i) antigen on different
      glycoproteins from circulating erythrocytes.
PG  - 405-7
AB  - During the ontogenic change from fetal to adult human erythrocytes, as well as
      fetal haemoglobin being replaced by adult haemoglobin, the cell-surface antigen i
      is converted to I (ref. 1). Recently it has been shown that this antigenic change
      is the conversion of the linear repeating Gal beta 1 leads to 4GlcNac beta 1
      leads to 3Gal structure to branched Gal beta 1 leads to 4GlcNac beta 1 leads to
      3(Gal beta 1 leads to 4GlcNac beta 1 leads to 6)Gal structure. We have shown that
      cell-surface labelling followed by endo-beta-galactosidase digestion can
      distinguish these two forms on the cell surface, and that band 3 and band 4.5 are
      the major carriers for these antigens on mature erythrocytes. Human leukaemic
      cell line K562, originally isolated from a patient at blast crisis of chronic
      myelocytic leukaemia, has recently been shown to synthesize glycophorin A, and to
      be capable of synthesizing haemoglobin upon induction. I demonstrate here that
      K562 cells express the fetal type (i) antigen on distinctly different
      glycoproteins from those of erythrocytes, by the use of cell-surface labelling
      followed by endo-beta-galactosidase digestion or followed by immunoprecipitation 
      with specific antibodies.
FAU - Fukuda, M
AU  - Fukuda M
LA  - eng
PT  - Journal Article
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - England
TA  - Nature
JT  - Nature
JID - 0410462
RN  - 0 (Antigens, Neoplasm)
RN  - 0 (Antigens, Surface)
RN  - 0 (Carbohydrates)
RN  - 0 (Glycoproteins)
RN  - 0 (I Blood-Group System)
RN  - EC 3.2.1.23 (beta-Galactosidase)
SB  - IM
MH  - Antigens, Neoplasm/*analysis
MH  - Antigens, Surface/*analysis
MH  - Carbohydrates/immunology
MH  - Cell Line
MH  - Erythrocyte Membrane/*immunology
MH  - Erythrocytes/*immunology
MH  - Fetus/immunology
MH  - Glycoproteins/*immunology
MH  - Humans
MH  - I Blood-Group System
MH  - Leukemia, Myeloid, Acute/*immunology
MH  - beta-Galactosidase/metabolism
EDAT- 1980/06/05 00:00
MHDA- 1980/06/05 00:01
CRDT- 1980/06/05 00:00
PHST- 1980/06/05 00:00 [pubmed]
PHST- 1980/06/05 00:01 [medline]
PHST- 1980/06/05 00:00 [entrez]
PST - ppublish
SO  - Nature. 1980 Jun 5;285(5764):405-7.

PMID- 1705547
OWN - NLM
STAT- MEDLINE
DCOM- 19910408
LR  - 20061115
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 266
IP  - 7
DP  - 1991 Mar 5
TI  - The structure of a neural specific carbohydrate epitope of horseradish peroxidase
      recognized by anti-horseradish peroxidase antiserum.
PG  - 4168-72
AB  - Antiserum raised against horseradish peroxidase (HRP) recognizes a neural
      specific carbohydrate antigen in Drosophila and other insects. The epitopic
      activity of the carbohydrate moiety of HRP recognized by anti-HRP antiserum was
      measured by a newly developed enzyme-linked immunosorbent assay, in which HRP
      glycopeptides conjugated with bovine serum albumin were coated onto the wells and
      then reacted with goat anti-HRP antiserum. HRP sugar moieties released by almond 
      glycopeptidase A digestion of HRP pepsin digests were subjected to
      pyridylamination. Pyridylamino oligosaccharides were separated into seven
      fractions by reverse-phase high performance liquid chromatography. The major
      fraction, which comprised about 80% of the total sugars, reacted strongly with
      anti-HRP antiserum. The carbohydrate structure of this fraction was determined by
      sugar composition analysis and 600-MHz 1H NMR spectroscopy as follows: Man alpha 
      1----6(Man alpha 1----3)(Xyl beta 1----2)Man beta 1----4GlcNAc beta 1----4(Fuc
      alpha 1----3)GlcNAc. Analyses of reactivity with anti-HRP antiserum of various
      oligosaccharide derivatives obtained from the major fraction by exoglycosidase
      digestion and partial acid hydrolysis indicated that alpha 1----6-linked mannose 
      and alpha 1----3-linked fucose are predominantly involved in the epitopic
      structure.
FAU - Kurosaka, A
AU  - Kurosaka A
AD  - Department of Biotechnology, Faculty of Engineering, Sangyo University, Japan.
FAU - Yano, A
AU  - Yano A
FAU - Itoh, N
AU  - Itoh N
FAU - Kuroda, Y
AU  - Kuroda Y
FAU - Nakagawa, T
AU  - Nakagawa T
FAU - Kawasaki, T
AU  - Kawasaki T
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Epitopes)
RN  - 0 (Glycoconjugates)
RN  - 0 (Oligosaccharides)
RN  - EC 1.11.1.- (Horseradish Peroxidase)
SB  - IM
MH  - Carbohydrate Sequence
MH  - Chromatography, High Pressure Liquid
MH  - Enzyme-Linked Immunosorbent Assay
MH  - Epitopes
MH  - Glycoconjugates/*immunology
MH  - Horseradish Peroxidase/chemistry/*immunology
MH  - Magnetic Resonance Spectroscopy
MH  - Molecular Sequence Data
MH  - Neurons/*immunology
MH  - Oligosaccharides/immunology
EDAT- 1991/03/05 00:00
MHDA- 1991/03/05 00:01
CRDT- 1991/03/05 00:00
PHST- 1991/03/05 00:00 [pubmed]
PHST- 1991/03/05 00:01 [medline]
PHST- 1991/03/05 00:00 [entrez]
PST - ppublish
SO  - J Biol Chem. 1991 Mar 5;266(7):4168-72.

PMID- 15223242
OWN - NLM
STAT- MEDLINE
DCOM- 20040916
LR  - 20071114
IS  - 0165-5728 (Print)
IS  - 0165-5728 (Linking)
VI  - 152
IP  - 1-2
DP  - 2004 Jul
TI  - Innate murine B cells produce anti-disialosyl antibodies reactive with
      Campylobacter jejuni LPS and gangliosides that are polyreactive and encoded by a 
      restricted set of unmutated V genes.
PG  - 98-111
AB  - In Guillain-Barre syndrome following Campylobacter enteritis,
      anti-lipopolysaccharide antibodies cross-react with neural gangliosides, thereby 
      precipitating autoimmune neuropathy. We examined the properties of 15 murine
      anti-LPS/ganglioside mAbs specific for NeuAc(alpha2-8)NeuAc-Gal disialosyl
      epitopes. Many mAbs displayed features of an innate B cell origin including
      polyreactivity (13/15), hybridoma CD5 mRNA expression (5/15), predominance of IgM
      (9/15) or IgG3 (3/6) isotype, low affinity, and utilisation of unmutated VH and
      VL VDJ rearrangements. Antibody specificity resided in highly selective V gene
      usage, with 6/15 mAbs being encoded by the VH7183.3b gene. These data indicate
      that neuropathogenic antiganglioside autoantibodies can arise from the natural
      autoantibody repertoire.
FAU - Boffey, Judith
AU  - Boffey J
AD  - University Department of Neurology, Institute of Neurological Sciences, Southern 
      General Hospital, Glasgow, Scotland G51 4TF, UK.
FAU - Nicholl, Dawn
AU  - Nicholl D
FAU - Wagner, Eric R
AU  - Wagner ER
FAU - Townson, Kate
AU  - Townson K
FAU - Goodyear, Carl
AU  - Goodyear C
FAU - Furukawa, Keiko
AU  - Furukawa K
FAU - Furukawa, Koichi
AU  - Furukawa K
FAU - Conner, Joe
AU  - Conner J
FAU - Willison, Hugh J
AU  - Willison HJ
LA  - eng
GR  - R01NS31528/NS/NINDS NIH HHS/United States
GR  - R01NS34846/NS/NINDS NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - Netherlands
TA  - J Neuroimmunol
JT  - Journal of neuroimmunology
JID - 8109498
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Autoantibodies)
RN  - 0 (Epitopes, B-Lymphocyte)
RN  - 0 (Gangliosides)
RN  - 0 (Immunoglobulin G)
RN  - 0 (Immunoglobulin M)
RN  - 0 (Immunoglobulin Variable Region)
RN  - 0 (Lipopolysaccharides)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Antibodies, Monoclonal/immunology
MH  - Antibody Affinity
MH  - *Antibody Specificity
MH  - Autoantibodies/*immunology
MH  - B-Lymphocytes/*immunology
MH  - Base Sequence
MH  - Campylobacter jejuni/*immunology
MH  - Epitopes, B-Lymphocyte/immunology
MH  - Gangliosides/genetics/*immunology
MH  - Immunoglobulin Class Switching
MH  - Immunoglobulin G/genetics/immunology
MH  - Immunoglobulin M/genetics/immunology
MH  - Immunoglobulin Variable Region/genetics
MH  - Lipopolysaccharides/*immunology
MH  - Mice
MH  - Molecular Sequence Data
MH  - Polymerase Chain Reaction
EDAT- 2004/06/30 05:00
MHDA- 2004/09/17 05:00
CRDT- 2004/06/30 05:00
PHST- 2004/02/04 00:00 [received]
PHST- 2004/04/07 00:00 [revised]
PHST- 2004/04/07 00:00 [accepted]
PHST- 2004/06/30 05:00 [pubmed]
PHST- 2004/09/17 05:00 [medline]
PHST- 2004/06/30 05:00 [entrez]
AID - 10.1016/j.jneuroim.2004.04.002 [doi]
AID - S0165572804001195 [pii]
PST - ppublish
SO  - J Neuroimmunol. 2004 Jul;152(1-2):98-111. doi: 10.1016/j.jneuroim.2004.04.002.

PMID- 1714447
OWN - NLM
STAT- MEDLINE
DCOM- 19910913
LR  - 20171116
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 266
IP  - 23
DP  - 1991 Aug 15
TI  - A carbohydrate domain common to both sialyl Le(a) and sialyl Le(X) is recognized 
      by the endothelial cell leukocyte adhesion molecule ELAM-1.
PG  - 14869-72
AB  - The specificity of endothelial cell leukocyte adhesion molecule-1, ELAM-1, for
      binding to a panel of carbohydrate structures was determined by a sensitive cell 
      binding assay with immobilized synthetic glycoconjugates. ELAM-1 cDNA
      transfectants were found to bind Sialyl Lea (sialylated lacto-N-fucopentaose II) 
      or sialylated Lewis a antigen (NeuAc alpha 2-3Gal beta 1-3(Fuc alpha 1-4)GlcNAc),
      as well as or slightly better than Sialyl Lex (sialylated lacto-N-fucopentaose
      III) or sialylated Lewis X antigen (NeuAc alpha 2-3 Gal beta 1-4(Fuc alpha
      1-3)GlcNAc). A monoclonal antibody, HECA-452, which has been identified recently 
      as recognizing ELAM-1 ligands in addition to those containing Sialyl Lex, was
      also found to bind both Sialyl Lex and Sialyl Lea. Hard sphere exo-anomeric
      (HSEA) calculations were performed on these two hexasaccharides. The
      conformations indicate that Sialyl Lea and Sialyl Lex show a high degree of
      similarity in both the nonreducing and reducing termini. As Lea and Lex show much
      weaker reactivity, the determinants recognized by ELAM-1 and HECA-452 probably
      involve neuraminic acid and fucose residues which on one face of both Sialyl Lex 
      and Sialyl Lea can be similarly positioned. The finding that Sialyl Lea is a
      potent ligand for ELAM-1 is important, as circulating Sialyl Lea and Sialyl Lex
      containing mucins which are elevated in the serum of many cancer patients may
      block leukocyte interactions with ELAM-1 and may contribute to the pathological
      immunodepression observed in these patients.
FAU - Berg, E L
AU  - Berg EL
AD  - Department of Pathology, Stanford University, California 94305.
FAU - Robinson, M K
AU  - Robinson MK
FAU - Mansson, O
AU  - Mansson O
FAU - Butcher, E C
AU  - Butcher EC
FAU - Magnani, J L
AU  - Magnani JL
LA  - eng
GR  - GM37734/GM/NIGMS NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Antigens, Neoplasm)
RN  - 0 (Cell Adhesion Molecules)
RN  - 0 (E-Selectin)
RN  - 0 (Lewis X Antigen)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Oligosaccharides)
RN  - 117978-16-2 (sialyl-Le(a) oligosaccharide)
RN  - 9007-49-2 (DNA)
SB  - IM
MH  - Animals
MH  - Antigens, Neoplasm/immunology/metabolism
MH  - Binding Sites
MH  - Binding, Competitive
MH  - *Carbohydrate Metabolism
MH  - Carbohydrate Sequence
MH  - Cell Adhesion Molecules/*metabolism
MH  - Cell Line
MH  - DNA/genetics
MH  - E-Selectin
MH  - Lewis X Antigen/immunology/*metabolism
MH  - Membrane Glycoproteins/*metabolism
MH  - Mice
MH  - Molecular Sequence Data
MH  - Oligosaccharides/immunology/*metabolism
MH  - Transfection
EDAT- 1991/08/15 00:00
MHDA- 1991/08/15 00:01
CRDT- 1991/08/15 00:00
PHST- 1991/08/15 00:00 [pubmed]
PHST- 1991/08/15 00:01 [medline]
PHST- 1991/08/15 00:00 [entrez]
PST - ppublish
SO  - J Biol Chem. 1991 Aug 15;266(23):14869-72.

PMID- 3805024
OWN - NLM
STAT- MEDLINE
DCOM- 19870304
LR  - 20041117
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 262
IP  - 3
DP  - 1987 Jan 25
TI  - Monoclonal antibodies directed to chemically synthesized
      lactogangliotetraosylceramide, a leukemia-associated antigen having a novel
      branching structure.
PG  - 1358-62
AB  - Murine leukemia cells (M1), in their undifferentiated state, have been
      characterized by the presence of cancer-associated lactoganglio-series
      glycolipids, one of which was identified as lactogangliotetraosylceramide (LcGg4)
      having a novel branching at the II-Gal of lactosylceramide through GlcNAc beta
      1----3 and GalNAc beta 1----4 linkage, as shown below (Kannagi, R., Levery, S.B.,
      and Hakomori, S. (1984) J. Biol. Chem., 259, 8444-8451): GalNAc beta 1----4 Gal
      beta 1----4Glc beta 1----1Cer GlcNac beta 1----3 Since this glycolipid is a very 
      minor component, it has been difficult to obtain enough of the purified
      glycolipid for the preparation of a monoclonal antibody. We developed a method to
      chemically synthesize this glycolipid using a lactose unit, a ceramide unit, and 
      two hexosamine donors as synthons and made the synthetic glycolipid available as 
      an immunogen. The two monoclonal antibodies we obtained (YI328-18 and YI328-51,
      both IgG3) specifically recognized the novel branching structure and had no
      cross-reactivity with gangliotriaosylceramide or lactotriaosylceramide. Thus, the
      antibodies were found to be useful probes to detect lactogangliotetraosylceramide
      expressed in undifferentiated M1 leukemia cells, which disappears on induced
      differentiation. The results of this study indicate a new strategy to establish
      monoclonal antibody directed to novel minor glycolipid markers or their
      artificially designed analogs, employing chemically synthesized glycolipid
      antigens.
FAU - Shigeta, K
AU  - Shigeta K
FAU - Ito, Y
AU  - Ito Y
FAU - Ogawa, T
AU  - Ogawa T
FAU - Kirihata, Y
AU  - Kirihata Y
FAU - Hakomori, S
AU  - Hakomori S
FAU - Kannagi, R
AU  - Kannagi R
LA  - eng
PT  - Journal Article
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens, Neoplasm)
RN  - 0 (Gangliosides)
RN  - 107221-01-2 (lactogangliotetraosylceramide)
SB  - IM
MH  - Animals
MH  - Antibodies, Monoclonal/*immunology
MH  - Antibody Specificity
MH  - Antigens, Neoplasm/*immunology
MH  - Carbohydrate Conformation
MH  - Cell Differentiation
MH  - Cell Line
MH  - Chromatography, Thin Layer
MH  - Gangliosides/chemical synthesis/*immunology
MH  - Humans
MH  - Leukemia, Experimental/*immunology
MH  - Mice
EDAT- 1987/01/25 00:00
MHDA- 1987/01/25 00:01
CRDT- 1987/01/25 00:00
PHST- 1987/01/25 00:00 [pubmed]
PHST- 1987/01/25 00:01 [medline]
PHST- 1987/01/25 00:00 [entrez]
PST - ppublish
SO  - J Biol Chem. 1987 Jan 25;262(3):1358-62.

PMID- 16107727
OWN - NLM
STAT- MEDLINE
DCOM- 20050922
LR  - 20181113
IS  - 0270-7306 (Print)
IS  - 0270-7306 (Linking)
VI  - 25
IP  - 17
DP  - 2005 Sep
TI  - Abnormalities caused by carbohydrate alterations in
      Ibeta6-N-acetylglucosaminyltransferase-deficient mice.
PG  - 7828-38
AB  - Ibeta6-N-acetylglucosaminyltransferase (IGnT) catalyzes the branching of
      poly-N-acetyllactosamine carbohydrate chains. In both humans and mice, three
      spliced forms of IGnT have been identified, and a common exon is present in all
      of them. We generated mice deficient in the common exon to understand the
      physiological function of poly-N-acetyllactosamine branching. IGnT activity was
      abolished in the stomach, kidney, bone marrow, and cerebellum of the deficient
      mice, while a low level of the activity persisted in the small intestine.
      Immunohistochemical analysis confirmed the loss of I antigen from the lung,
      stomach, and kidney. The deficient mice had reduced spontaneous locomotive
      activity. The number of peripheral blood lymphocytes was also reduced and renal
      function decreased in the deficient mice. Furthermore, in aged mice,
      vacuolization occurred in the kidney, and epidermoid cysts were frequently
      formed. However, cataracts did not develop earlier in the deficient mice.
      Decreased levels of lysosomal proteins, LAMP-2 and synaptotagmin VII, were found 
      in the kidney of the deficient mice and correlated with renal abnormalities.
FAU - Chen, Guo-Yun
AU  - Chen GY
AD  - Department of Biochemistry, Nagoya University School of Medicine, Japan.
FAU - Muramatsu, Hisako
AU  - Muramatsu H
FAU - Kondo, Mineo
AU  - Kondo M
FAU - Kurosawa, Nobuyuki
AU  - Kurosawa N
FAU - Miyake, Yozo
AU  - Miyake Y
FAU - Takeda, Naoki
AU  - Takeda N
FAU - Muramatsu, Takashi
AU  - Muramatsu T
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Mol Cell Biol
JT  - Molecular and cellular biology
JID - 8109087
RN  - 0 (Antigens, CD)
RN  - 0 (Calcium-Binding Proteins)
RN  - 0 (Lamp1 protein, mouse)
RN  - 0 (Lysosomal-Associated Membrane Protein 1)
RN  - 0 (Lysosome-Associated Membrane Glycoproteins)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Nerve Tissue Proteins)
RN  - 0 (Synaptotagmin II)
RN  - 0 (Syt2 protein, mouse)
RN  - 0 (Syt7 protein, mouse)
RN  - 134193-27-4 (Synaptotagmins)
RN  - EC 2.4.- (N-acetylglucosaminyltransferase IGnT)
RN  - EC 2.4.1.- (N-Acetylglucosaminyltransferases)
SB  - IM
MH  - Animals
MH  - Antigens, CD/metabolism
MH  - Calcium-Binding Proteins/metabolism
MH  - *Carbohydrate Metabolism
MH  - Cataract/enzymology/genetics
MH  - Epidermal Cyst/enzymology/genetics/pathology
MH  - Gene Deletion
MH  - Intracellular Membranes/enzymology
MH  - Kidney/*abnormalities/enzymology/metabolism/pathology
MH  - Lymphocyte Count
MH  - Lymphocytes/cytology
MH  - Lysosomal-Associated Membrane Protein 1
MH  - Lysosome-Associated Membrane Glycoproteins
MH  - Lysosomes/enzymology/genetics
MH  - Membrane Glycoproteins/metabolism
MH  - Mice
MH  - Mice, Knockout
MH  - Motor Activity
MH  - N-Acetylglucosaminyltransferases/*deficiency/genetics/*metabolism
MH  - Nerve Tissue Proteins/metabolism
MH  - Protein Binding
MH  - Synaptotagmin II
MH  - Synaptotagmins
MH  - Time Factors
PMC - PMC1190280
EDAT- 2005/08/19 09:00
MHDA- 2005/09/24 09:00
CRDT- 2005/08/19 09:00
PHST- 2005/08/19 09:00 [pubmed]
PHST- 2005/09/24 09:00 [medline]
PHST- 2005/08/19 09:00 [entrez]
AID - 25/17/7828 [pii]
AID - 10.1128/MCB.25.17.7828-7838.2005 [doi]
PST - ppublish
SO  - Mol Cell Biol. 2005 Sep;25(17):7828-38. doi: 10.1128/MCB.25.17.7828-7838.2005.

PMID- 2302705
OWN - NLM
STAT- MEDLINE
DCOM- 19900321
LR  - 20071114
IS  - 0008-5472 (Print)
IS  - 0008-5472 (Linking)
VI  - 50
IP  - 5
DP  - 1990 Mar 1
TI  - Biochemical and serological characteristics of natural 9-O-acetyl GD3 from human 
      melanoma and bovine buttermilk and chemically O-acetylated GD3.
PG  - 1403-10
AB  - Because its expression appears to be largely restricted to human melanomas,
      9-O-acetyl-GD3 is a candidate antigen for vaccine construction. Searching for
      potential sources, we compared chemically O-acetylated calf brain GD3 and
      9-O-acetyl-GD3 extracted from bovine buttermilk with 9-O-acetyl-GD3 from human
      melanoma. Three fractions (F1-F3) of chemically O-acetylated GD3 differed in the 
      number and position of O-acetyl groups. O-Acetylation sites were the lactose
      portion in F1 and lactose as well as sialic acid in F2 and F3. Natural (melanoma-
      or buttermilk-derived) 9-O-acetyl-GD3 was O-acetylated solely on the sialic acid 
      moiety. While F1 was not reactive with monoclonal antibodies against
      9-O-acetyl-GD3, F2 and F3 were as reactive as the natural products. Immunization 
      with the natural products induced high-titer antibodies against natural
      9-O-acetyl-GD3 as well as F2 and F3. In contrast, mice immunized with the
      synthetic fractions produced antibodies only against the immunogen but not
      against natural 9-O-acetyl-GD3. Only immunization with the natural products
      induced production of antibodies reactive with surface antigens of melanoma cells
      expressing 9-O-acetyl-GD3. The findings suggest (a) that C-9 of the subterminal
      sialic acid is the site of chemical O-acetylation in F2 and F3, as opposed to C-9
      of the terminal sialic acid in the natural products; (b) that O-acetylation of
      both the terminal and subterminal sialic acid moieties of GD3 results in
      recognition by three murine monoclonal antibodies (D1.1, ME 311, and Jones)
      reactive with human melanoma cells; (c) that O-acetylation of the terminal sialic
      acid is critical, on the other hand, for inducing an immune response against
      melanoma 9-O-acetyl-GD3; and (d) that O-acetyl GD3 from bovine buttermilk can
      substitute as immunogen for inducing an immune response against human melanoma
      cell surface antigens in the mouse.
FAU - Ritter, G
AU  - Ritter G
AD  - Memorial Sloan-Kettering Cancer Center, New York, New York 10021.
FAU - Boosfeld, E
AU  - Boosfeld E
FAU - Markstein, E
AU  - Markstein E
FAU - Yu, R K
AU  - Yu RK
FAU - Ren, S L
AU  - Ren SL
FAU - Stallcup, W B
AU  - Stallcup WB
FAU - Oettgen, H F
AU  - Oettgen HF
FAU - Old, L J
AU  - Old LJ
FAU - Livingston, P O
AU  - Livingston PO
LA  - eng
GR  - CA-08748/CA/NCI NIH HHS/United States
GR  - CA-43971/CA/NCI NIH HHS/United States
GR  - NS-11853/NS/NINDS NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Cancer Res
JT  - Cancer research
JID - 2984705R
RN  - 0 (Gangliosides)
RN  - 0 (Immunoglobulin G)
RN  - 62010-37-1 (ganglioside, GD3)
RN  - 8029-34-3 (Butter)
RN  - 98743-26-1 (9-O-acetyl-GD3 ganglioside)
SB  - IM
MH  - Acetylation
MH  - Animals
MH  - Butter/analysis
MH  - Chromatography, High Pressure Liquid
MH  - Chromatography, Thin Layer
MH  - Female
MH  - Gangliosides/*analysis/chemical synthesis/immunology/metabolism
MH  - Humans
MH  - Immunization
MH  - Immunoglobulin G/*biosynthesis
MH  - Melanoma/*analysis/immunology
MH  - Mice
MH  - Mice, Inbred BALB C
MH  - Mice, Inbred C57BL
EDAT- 1990/03/01 00:00
MHDA- 1990/03/01 00:01
CRDT- 1990/03/01 00:00
PHST- 1990/03/01 00:00 [pubmed]
PHST- 1990/03/01 00:01 [medline]
PHST- 1990/03/01 00:00 [entrez]
PST - ppublish
SO  - Cancer Res. 1990 Mar 1;50(5):1403-10.

PMID- 6172429
OWN - NLM
STAT- MEDLINE
DCOM- 19820313
LR  - 20190508
IS  - 0021-9525 (Print)
IS  - 0021-9525 (Linking)
VI  - 91
IP  - 3 Pt 2
DP  - 1981 Dec
TI  - Extracellular matrix.
PG  - 205s-223s
FAU - Hay, E D
AU  - Hay ED
LA  - eng
GR  - HD-00143/HD/NICHD NIH HHS/United States
PT  - Journal Article
PT  - Research Support, U.S. Gov't, P.H.S.
PT  - Review
PL  - United States
TA  - J Cell Biol
JT  - The Journal of cell biology
JID - 0375356
RN  - 0 (Epitopes)
RN  - 0 (Fibronectins)
RN  - 0 (Glycoproteins)
RN  - 0 (Macromolecular Substances)
RN  - 0 (Procollagen)
RN  - 0 (Proteoglycans)
RN  - 9004-61-9 (Hyaluronic Acid)
RN  - 9007-34-5 (Collagen)
RN  - 9007-58-3 (Elastin)
SB  - IM
MH  - Animals
MH  - Cell Differentiation
MH  - Chemical Phenomena
MH  - Chemistry
MH  - *Collagen/analysis/immunology/metabolism
MH  - Connective Tissue/*analysis
MH  - Elastin/analysis
MH  - Embryo, Mammalian/physiology
MH  - Epitopes
MH  - Extracellular Space/*analysis/physiology
MH  - Fibronectins/analysis
MH  - Glycoproteins/analysis
MH  - Humans
MH  - Hyaluronic Acid/analysis
MH  - Hydroxylation
MH  - Macromolecular Substances
MH  - Models, Biological
MH  - Procollagen
MH  - Protein Conformation
MH  - Proteoglycans/analysis
RF  - 245
PMC - PMC2112832
EDAT- 1981/12/01 00:00
MHDA- 1981/12/01 00:01
CRDT- 1981/12/01 00:00
PHST- 1981/12/01 00:00 [pubmed]
PHST- 1981/12/01 00:01 [medline]
PHST- 1981/12/01 00:00 [entrez]
AID - 10.1083/jcb.91.3.205s [doi]
PST - ppublish
SO  - J Cell Biol. 1981 Dec;91(3 Pt 2):205s-223s. doi: 10.1083/jcb.91.3.205s.

PMID- 429966
OWN - NLM
STAT- MEDLINE
DCOM- 19790629
LR  - 20190508
IS  - 0022-1007 (Print)
IS  - 0022-1007 (Linking)
VI  - 149
IP  - 4
DP  - 1979 Apr 1
TI  - Three types of blood group I specificity among monoclonal anti-I autoantibodies
      revealed by analogues of a branched erythrocyte glycolipid.
PG  - 975-80
AB  - Blood group I activities of the purified glycosphingolipid lacto-N-iso-octaosyl
      ceramide (Fromula: see text) and 8 of its analogues have been evaluated with 11
      anti-I sera including 5 anti-I sera previously tested. All but one of the
      antisera were inhibited by the lacto-N-iso-octaosyl structure. Three types of
      I-specificity could be distinguished although none of the anti-I sera was
      identical in its inhibition patterns with the nine glycophingolipid analogues.
      The anti-I sera Ma and Woj represent the first type and require an intact
      Galbeta1 leads to 4GlcNAcbeta1 leads to 6 chain, the anti-I sera Step, Gra, Ver, 
      and Ful represent the second type which requires Galbeta1 leads to 4GlcNAcbeta1
      leads to 3 chain with branching, and the anti-I sera Phi, Da, Sch, and Low belong
      to the third type which requires both branches to be intact. Anti-I antibodies
      varry in their ability to react with their antigenic determinants in the presence
      of external substitutions with alpha-linked galactose or sialic acid.
FAU - Feizi, T
AU  - Feizi T
FAU - Childs, R A
AU  - Childs RA
FAU - Watanabe, K
AU  - Watanabe K
FAU - Hakomori, S I
AU  - Hakomori SI
LA  - eng
PT  - Journal Article
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - J Exp Med
JT  - The Journal of experimental medicine
JID - 2985109R
RN  - 0 (Autoantibodies)
RN  - 0 (Blood Group Antigens)
RN  - 0 (Glycolipids)
RN  - 0 (Glycosphingolipids)
RN  - 0 (I Blood-Group System)
RN  - 0 (Isoantibodies)
SB  - IM
MH  - Antibody Specificity
MH  - Autoantibodies
MH  - Binding Sites, Antibody
MH  - *Blood Group Antigens
MH  - Clone Cells/immunology
MH  - Erythrocytes/*immunology
MH  - Glycolipids/blood/*immunology
MH  - Glycosphingolipids/blood/immunology
MH  - Humans
MH  - *I Blood-Group System
MH  - Isoantibodies
MH  - Structure-Activity Relationship
PMC - PMC2184841
EDAT- 1979/04/01 00:00
MHDA- 1979/04/01 00:01
CRDT- 1979/04/01 00:00
PHST- 1979/04/01 00:00 [pubmed]
PHST- 1979/04/01 00:01 [medline]
PHST- 1979/04/01 00:00 [entrez]
AID - 10.1084/jem.149.4.975 [doi]
PST - ppublish
SO  - J Exp Med. 1979 Apr 1;149(4):975-80. doi: 10.1084/jem.149.4.975.

PMID- 16332389
OWN - NLM
STAT- MEDLINE
DCOM- 20070919
LR  - 20131121
IS  - 0145-2126 (Print)
IS  - 0145-2126 (Linking)
VI  - 30
IP  - 7
DP  - 2006 Jul
TI  - Establishment and characterization of a new erythroblastic leukemia cell line,
      EEB: phosphatidylglucoside-mediated erythroid differentiation and apoptosis.
PG  - 829-39
AB  - A new erythroblastic leukemia cell line (EEB) was established from a patient with
      early erythroblastic leukemia. The cells had features of immature erythroblasts, 
      including an agranular basophilic cytoplasm and CD36, CD71, CD175s (sialyl-Tn)
      and CD235a (glycophorin A) expression without CD41 expression, myeloperoxidase
      activity and platelet-peroxidase activity. The cells were confirmed to be of the 
      erythroid lineage based on expression of the gamma-globin message. They were
      induced to differentiate into benzidine-positive cells by hemin and delta-amino
      levulinic acid (delta-ALA). An analysis of cell membrane lipids showed that EEB
      cells contain a type of glycerolipid, phosphatidylglucose (PhGlc), but not
      unbranched type 2 chains, i antigens. GL-7 which is a recombinant Fab fragment of
      GL-2 and binds to PhGlc, induced production of hemoglobin F (HbF) associated with
      accumulation of the gamma-globin (gamma-globin) message in EEB cells. The
      GL-7-mediated erythroid differentiation was associated with apoptosis. These
      results suggest that direct signaling to PhGlc mediates erythroid differentiation
      and apoptosis in EEB cells.
FAU - Kawano-Yamamoto, Chizuru
AU  - Kawano-Yamamoto C
AD  - Division of Hematology, Department of Medicine, Jichi Medical School,
      Minamikawachi, Tochigi 329-0498, Japan.
FAU - Muroi, Kazuo
AU  - Muroi K
FAU - Nagatsuka, Yasuko
AU  - Nagatsuka Y
FAU - Higuchi, Masato
AU  - Higuchi M
FAU - Kikuchi, Satoru
AU  - Kikuchi S
FAU - Nagai, Tadashi
AU  - Nagai T
FAU - Hakomori, Sen-Itiroh
AU  - Hakomori SI
FAU - Ozawa, Keiya
AU  - Ozawa K
LA  - eng
PT  - Case Reports
PT  - Journal Article
DEP - 20051205
PL  - England
TA  - Leuk Res
JT  - Leukemia research
JID - 7706787
RN  - 0 (GL-7 Fab fragment)
RN  - 0 (Glycerophospholipids)
RN  - 0 (Immunoglobulin Fab Fragments)
RN  - 0 (phosphatidylglucose)
RN  - 42HK56048U (Tyrosine)
RN  - 9004-22-2 (Globins)
SB  - IM
MH  - Apoptosis/*drug effects
MH  - Cell Differentiation/drug effects
MH  - *Cell Line, Tumor
MH  - Cytogenetic Analysis
MH  - Drug Screening Assays, Antitumor
MH  - Erythroid Cells/cytology/*drug effects
MH  - Globins/drug effects/genetics
MH  - Glycerophospholipids/analysis/*pharmacology
MH  - Humans
MH  - Immunoglobulin Fab Fragments/*pharmacology
MH  - Immunophenotyping
MH  - Leukemia, Erythroblastic, Acute/*drug therapy/genetics/*metabolism
MH  - Male
MH  - Middle Aged
MH  - Phosphorylation/drug effects
MH  - Reverse Transcriptase Polymerase Chain Reaction/methods
MH  - Sensitivity and Specificity
MH  - Structure-Activity Relationship
MH  - Tyrosine/drug effects/metabolism
EDAT- 2005/12/08 09:00
MHDA- 2007/09/20 09:00
CRDT- 2005/12/08 09:00
PHST- 2005/03/23 00:00 [received]
PHST- 2005/10/20 00:00 [revised]
PHST- 2005/10/22 00:00 [accepted]
PHST- 2005/12/08 09:00 [pubmed]
PHST- 2007/09/20 09:00 [medline]
PHST- 2005/12/08 09:00 [entrez]
AID - S0145-2126(05)00422-4 [pii]
AID - 10.1016/j.leukres.2005.10.021 [doi]
PST - ppublish
SO  - Leuk Res. 2006 Jul;30(7):829-39. doi: 10.1016/j.leukres.2005.10.021. Epub 2005
      Dec 5.

PMID- 3112156
OWN - NLM
STAT- MEDLINE
DCOM- 19870917
LR  - 20171116
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 262
IP  - 23
DP  - 1987 Aug 15
TI  - Oncofetal expression of Lex carbohydrate antigens in human colonic
      adenocarcinomas. Regulation through type 2 core chain synthesis rather than
      fucosylation.
PG  - 11331-8
AB  - The mechanism of expression of a series of glycolipid antigens carrying the Lex
      determinant structure, Gal beta 1----4[Fuc alpha 1----3]GlcNAc beta 1----, and
      characterized by oncofetal expression in fetal colon and colonic adenocarcinomas 
      has been studied in human fetal and adult proximal colon tissue. Results
      presented from TLC immunostain analysis of neutral glycolipids isolated from
      normal adult colonic mucosa have indicated the presence of only barely detectable
      quantities of both an Lex-active glycolipid that co-migrated with III3V3Fuc2nLc6 
      and its precursor nLc6. These structures were found in large quantities in
      glycolipid fractions from human adenocarcinoma tumors and human small cell lung
      carcinoma NCI-H69 cells. In contrast, type 1 chain-based Lea antigen structures
      were found in both normal mucosa and adenocarcinomas. Analysis of gangliosides of
      normal colonic mucosa by TLC immunostain indicated the presence of a series of
      type 2 chain-based gangliosides; however, sialyl-Lex was not detected. The
      ability of normal colonic mucosa to synthesize type 2 chain core structures was
      demonstrated by the presence of a beta 1----4 galactosyltransferase activity with
      Lc3 as an acceptor in an amount equivalent to 60-65% of the total
      galactosyltransferase activity. An alpha 1----3 fucosyltransferase was also found
      to be expressed in significant quantity in adult colonic mucosa. Kinetic studies 
      indicated that this is most probably the alpha 1----3/4 fucosyltransferase
      suggested to be a product of the Lewis gene (Le). Thus, although normal adult
      colonic mucosa contained the enzymes to synthesize Lex and sialyl-Lex structures,
      these antigens were not found. Tissue immunofluorescence studies indicated that
      type 2 chain precursors and the alpha 1----3/4 fucosyltransferase were found in
      different cell populations in adult proximal colonic mucosa. However, both type 2
      chain core structures and their fucosylated derivatives were found to be
      associated with epithelial cells of fetal colon. These results indicate that
      oncofetal expression of Lex antigens in fetal colonic epithelium and in
      adenocarcinomas but not in normal adult mucosa is due to the retrogenetic
      expression of type 2 chain precursors which are not found in normal adult colonic
      epithelial cells.
FAU - Holmes, E H
AU  - Holmes EH
FAU - Ostrander, G K
AU  - Ostrander GK
FAU - Clausen, H
AU  - Clausen H
FAU - Graem, N
AU  - Graem N
LA  - eng
GR  - CA41521/CA/NCI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Antigens, Neoplasm)
RN  - 0 (Glycolipids)
RN  - 28RYY2IV3F (Fucose)
RN  - EC 2.4.1.- (Fucosyltransferases)
RN  - EC 2.4.1.- (Galactosyltransferases)
RN  - EC 2.4.1.86 (glucosaminylgalactosylglucosylceramide beta-galactosyltransferase)
SB  - IM
MH  - Adenocarcinoma/*immunology
MH  - Antigens, Neoplasm/*biosynthesis/genetics
MH  - Colon/embryology/*immunology
MH  - Colonic Neoplasms/*immunology
MH  - Epithelium/immunology
MH  - Fetus/*immunology
MH  - Fluorescent Antibody Technique
MH  - Fucose/metabolism
MH  - Fucosyltransferases/metabolism
MH  - Galactosyltransferases/metabolism
MH  - *Gene Expression Regulation
MH  - Glycolipids/*biosynthesis/genetics/immunology
MH  - Humans
MH  - Immunoassay
MH  - Intestinal Mucosa/immunology
EDAT- 1987/08/15 00:00
MHDA- 1987/08/15 00:01
CRDT- 1987/08/15 00:00
PHST- 1987/08/15 00:00 [pubmed]
PHST- 1987/08/15 00:01 [medline]
PHST- 1987/08/15 00:00 [entrez]
PST - ppublish
SO  - J Biol Chem. 1987 Aug 15;262(23):11331-8.

PMID- 7531823
OWN - NLM
STAT- MEDLINE
DCOM- 19950316
LR  - 20171116
IS  - 0028-0836 (Print)
IS  - 0028-0836 (Linking)
VI  - 373
IP  - 6515
DP  - 1995 Feb 16
TI  - The E-selectin-ligand ESL-1 is a variant of a receptor for fibroblast growth
      factor.
PG  - 615-20
AB  - E-SELECTIN is an inducible cell-adhesion molecule on endothelial cells, which
      mediates the binding of neutrophils and functions as a Ca(2+)-dependent lectin.
      We have recently identified a 150K glycoprotein as the major ligand for
      E-selectin on myeloid cells, using a recombinant antibody-like form of mouse
      E-selectin as an affinity probe. Here we report the isolation of a mouse
      complementary DNA for this E-selectin ligand (ESL-1). The predicted amino-acid
      sequence of ESL-1 is 94% identical (over 1,078 amino acids) to the recently
      identified chicken cysteine-rich fibroblast growth-factor receptor, except for a 
      unique 70-amino-acid aminoterminal domain of mature ESL-1. Fucosylation of ESL-1 
      is imperative for affinity isolation with E-selectin-IgG. A fucosylated,
      recombinant antibody-like form of ESL-1, but not of L-selectin, supports adhesion
      of E-selectin-transfected Chinese hamster ovary cells. Antibodies against ESL-1
      block the binding of mouse myeloid cells to E-selectin. ESL-1, with a structure
      essentially identical to that of a receptor, thus functions as a cell adhesion
      ligand of E-selectin.
FAU - Steegmaier, M
AU  - Steegmaier M
AD  - Hans-Spemann-Laboratory, Max-Planck-Institute for Immunobiology, Freiburg,
      Germany.
FAU - Levinovitz, A
AU  - Levinovitz A
FAU - Isenmann, S
AU  - Isenmann S
FAU - Borges, E
AU  - Borges E
FAU - Lenter, M
AU  - Lenter M
FAU - Kocher, H P
AU  - Kocher HP
FAU - Kleuser, B
AU  - Kleuser B
FAU - Vestweber, D
AU  - Vestweber D
LA  - eng
SI  - GENBANK/U28811
SI  - GENBANK/X84037
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - Nature
JT  - Nature
JID - 0410462
RN  - 0 (Cell Adhesion Molecules)
RN  - 0 (DNA, Complementary)
RN  - 0 (E-Selectin)
RN  - 0 (Glycoproteins)
RN  - 0 (Immunoglobulin G)
RN  - 0 (Ligands)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Receptors, Fibroblast Growth Factor)
RN  - 0 (Receptors, Immunologic)
RN  - 0 (Recombinant Fusion Proteins)
RN  - 0 (Sialoglycoproteins)
RN  - 0 (cysteine-rich fibroblast growth factor receptor)
RN  - 28RYY2IV3F (Fucose)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Base Sequence
MH  - CHO Cells
MH  - Cell Adhesion Molecules/*metabolism
MH  - Chickens
MH  - Cloning, Molecular
MH  - Cricetinae
MH  - DNA, Complementary
MH  - E-Selectin
MH  - Fucose/metabolism
MH  - Glycoproteins/chemistry/genetics/*isolation & purification/metabolism
MH  - Humans
MH  - Immunoglobulin G/genetics/metabolism
MH  - Ligands
MH  - Membrane Glycoproteins/genetics/*isolation & purification/metabolism
MH  - Mice
MH  - Molecular Sequence Data
MH  - Neutrophils/metabolism
MH  - Precipitin Tests
MH  - Protein Binding
MH  - Receptors, Fibroblast Growth Factor/*chemistry/genetics/*isolation &
      purification/metabolism
MH  - Receptors, Immunologic/genetics/isolation & purification/metabolism
MH  - Recombinant Fusion Proteins/genetics/metabolism
MH  - Sequence Homology, Amino Acid
MH  - Sialoglycoproteins
MH  - Transfection
EDAT- 1995/02/16 00:00
MHDA- 1995/02/16 00:01
CRDT- 1995/02/16 00:00
PHST- 1995/02/16 00:00 [pubmed]
PHST- 1995/02/16 00:01 [medline]
PHST- 1995/02/16 00:00 [entrez]
AID - 10.1038/373615a0 [doi]
PST - ppublish
SO  - Nature. 1995 Feb 16;373(6515):615-20. doi: 10.1038/373615a0.

PMID- 6188690
OWN - NLM
STAT- MEDLINE
DCOM- 19830617
LR  - 20181113
IS  - 0093-7711 (Print)
IS  - 0093-7711 (Linking)
VI  - 17
IP  - 5
DP  - 1983
TI  - Mouse monoclonal antibody F-3 recognizes the difucosyl type-2 blood group
      structure.
PG  - 537-41
FAU - Lloyd, K O
AU  - Lloyd KO
FAU - Larson, G
AU  - Larson G
FAU - Stromberg, N
AU  - Stromberg N
FAU - Thurin, J
AU  - Thurin J
FAU - Karlsson, K A
AU  - Karlsson KA
LA  - eng
GR  - CA-08748/CA/NCI NIH HHS/United States
GR  - CA-26184/CA/NCI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Immunogenetics
JT  - Immunogenetics
JID - 0420404
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Blood Group Antigens)
RN  - 0 (Epitopes)
RN  - 0 (Glycosphingolipids)
RN  - 0 (difucosyl heptaglycosylceramide)
RN  - 28RYY2IV3F (Fucose)
SB  - IM
MH  - Animals
MH  - Antibodies, Monoclonal/*immunology
MH  - Blood Group Antigens/*immunology
MH  - Epitopes
MH  - Fucose/immunology
MH  - Glycosphingolipids/*immunology
MH  - Humans
MH  - Mice
EDAT- 1983/01/01 00:00
MHDA- 1983/01/01 00:01
CRDT- 1983/01/01 00:00
PHST- 1983/01/01 00:00 [pubmed]
PHST- 1983/01/01 00:01 [medline]
PHST- 1983/01/01 00:00 [entrez]
PST - ppublish
SO  - Immunogenetics. 1983;17(5):537-41.

PMID- 3944091
OWN - NLM
STAT- MEDLINE
DCOM- 19860303
LR  - 20131121
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 261
IP  - 3
DP  - 1986 Jan 25
TI  - Novel blood group H glycolipid antigens exclusively expressed in blood group A
      and AB erythrocytes (type 3 chain H). I. Isolation and chemical characterization.
PG  - 1380-7
AB  - A series of blood group H antigens reacting with monoclonal antibody MBrl has
      been found in human blood group A and AB erythrocytes, but not in O or B
      erythrocytes. These H antigens are clearly different from the globo-H structure
      (Fuc alpha 1----2Gal beta 1----3GalNAc beta 1----3Gal alpha 1----4Gal beta
      1----4Glc beta 1----1Cer), which was previously isolated from O erythrocytes and 
      is also reactive with the MBrl antibody. The new series of H antigens associated 
      with blood group A has been characterized as having TLC mobilities which
      approximately coincide with those of H2, H3, and H4 glycolipids. One of these
      A-associated H antigens, having a similar TLC mobility as the H2 glycolipid, was 
      isolated from A erythrocytes and was characterized by 1H NMR spectroscopy,
      methylation analysis, and enzymatic degradation as having the structure shown
      below: (formula, see text). The structure represents a precursor of the
      repetitive A epitope attached to type 2 chain, previously called type 3 chain A
      (Clausen, H., Levery, S. B., Nudelman, E., Tsuchiya, S., and Hakomori, S. (1985) 
      Proc. Natl. Acad. Sci. U.S.A. 82, 1199-1203). This A-associated H structure is
      hereby called type 3 chain H.
FAU - Clausen, H
AU  - Clausen H
FAU - Levery, S B
AU  - Levery SB
FAU - Kannagi, R
AU  - Kannagi R
FAU - Hakomori, S
AU  - Hakomori S
LA  - eng
GR  - CA19224/CA/NCI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (ABO Blood-Group System)
RN  - 0 (Glycolipids)
RN  - YOW8V9698H (Dimethyl Sulfoxide)
SB  - IM
MH  - *ABO Blood-Group System
MH  - Carbohydrate Sequence
MH  - Chromatography, Thin Layer
MH  - Dimethyl Sulfoxide/pharmacology
MH  - Erythrocytes/*analysis
MH  - Glycolipids/*analysis
MH  - Humans
MH  - Magnetic Resonance Spectroscopy
EDAT- 1986/01/25 00:00
MHDA- 1986/01/25 00:01
CRDT- 1986/01/25 00:00
PHST- 1986/01/25 00:00 [pubmed]
PHST- 1986/01/25 00:01 [medline]
PHST- 1986/01/25 00:00 [entrez]
PST - ppublish
SO  - J Biol Chem. 1986 Jan 25;261(3):1380-7.

PMID- 3840699
OWN - NLM
STAT- MEDLINE
DCOM- 19860103
LR  - 20170915
IS  - 0006-3002 (Print)
IS  - 0006-3002 (Linking)
VI  - 837
IP  - 3
DP  - 1985 Dec 4
TI  - Mouse monoclonal antibodies with specificity for the melanoma-associated
      ganglioside disialyllactosylceramide (GD3) also react with the structural
      analogue disialylparagloboside.
PG  - 349-53
AB  - A mouse monoclonal IgM antibody, 4.2, has previously been shown to bind
      preferentially to the surface of human malignant melanoma cells and to have
      specificity for the GD3 ganglioside (NeuAc alpha 2----8NeuAc alpha 2----3Gal beta
      1----4GlcCer). Using overlay of antibodies on thin-layer chromatograms with
      glycolipids of various sources, it was shown that antibody 4.2, a further IgM and
      two IgG3 mouse monoclonal antibodies, selected on the basis of reactivity with
      GD3, also bound with similar strength to the structural analogue NeuAc alpha
      2----8NeuAc alpha 2----3Gal beta 1----4GlcNac beta 1----3Gal beta 1----4GlcCer or
      disialylparagloboside. The SK-MEL 28 melanoma cell line used for immunization was
      shown to contain a large amount of GD3 but to lack disialylparagloboside. The
      demonstrated cross-reactivity may be of importance when considering the use of
      these antibodies for biochemical and medical purposes.
FAU - Brodin, T
AU  - Brodin T
FAU - Hellstrom, I
AU  - Hellstrom I
FAU - Hellstrom, K E
AU  - Hellstrom KE
FAU - Karlsson, K A
AU  - Karlsson KA
FAU - Sjogren, H O
AU  - Sjogren HO
FAU - Stromberg, N
AU  - Stromberg N
FAU - Thurin, J
AU  - Thurin J
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - Netherlands
TA  - Biochim Biophys Acta
JT  - Biochimica et biophysica acta
JID - 0217513
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Gangliosides)
RN  - 0 (Globosides)
RN  - 0 (Glycosphingolipids)
RN  - 62010-37-1 (ganglioside, GD3)
RN  - 83713-05-7 (disialosyl paragloboside)
SB  - IM
MH  - Animals
MH  - Antibodies, Monoclonal/*immunology
MH  - *Antibody Specificity
MH  - Carbohydrate Sequence
MH  - Cell Line
MH  - Chromatography, Thin Layer
MH  - Cross Reactions
MH  - Gangliosides/*immunology
MH  - Globosides/*immunology
MH  - Glycosphingolipids/*immunology
MH  - Humans
MH  - Melanoma/*analysis
MH  - Mice
MH  - Rats
EDAT- 1985/12/04 00:00
MHDA- 1985/12/04 00:01
CRDT- 1985/12/04 00:00
PHST- 1985/12/04 00:00 [pubmed]
PHST- 1985/12/04 00:01 [medline]
PHST- 1985/12/04 00:00 [entrez]
AID - 0005-2760(85)90059-1 [pii]
PST - ppublish
SO  - Biochim Biophys Acta. 1985 Dec 4;837(3):349-53.

PMID- 12761161
OWN - NLM
STAT- MEDLINE
DCOM- 20040121
LR  - 20190513
IS  - 0021-924X (Print)
IS  - 0021-924X (Linking)
VI  - 133
IP  - 3
DP  - 2003 Mar
TI  - SRCL/CL-P1 recognizes GalNAc and a carcinoma-associated antigen, Tn antigen.
PG  - 271-7
AB  - SRCL /CL-P1 was recently identified as a scavenger receptor with a C-type lectin 
      domain, which was expressed in vascular endothelial cells and could bind to
      Gram-positive and Gram-negative bacteria, yeast and oxidized LDL. We found that
      SRCL was expressed in some but not all nurse-like cells examined. Furthermore, to
      characterize the C-type lectin domain of SRCL, the secreted form of the C-type
      lectin domain (LEC-AP) of SRCL, which was fused to the signal sequence of IgG and
      alkaline phosphatase, was expressed in 293/EBNA-1 cells and the culture medium
      was used for the in vitro binding assay. LEC-AP specifically bound to
      GalNAc-conjugated gel in a Ca(2+)-dependent manner, and this binding was
      inhibited by free GalNAc, L-, D-fucose, D-galactose, lactose, and especially T
      antigen and Tn antigen. Furthermore, we examined whether or not SRCL could take
      up saccharide-conjugated particles. 293/EBNA-1 cells stably expressing SRCL were 
      found to take up GalNAc but not mannose-conjugated particles on confocal
      microscopy. The binding of GalNAc-conjugated particles to these cells was
      quantitatively measured by comparing the x-means of individual cell populations. 
      An approximately 2.1-fold increase in immunofluorescence intensity was observed
      for the SRCL transfectants compared to control vector transfectants. Our results 
      provide a basis for understanding the scavenger function of SRCL as to
      carbohydrate-containing ligands.
FAU - Yoshida, Tetsuya
AU  - Yoshida T
AD  - Discovery Research Laboratories, Shionogi & Co., Ltd., 2-5-1 Mishima, Settsu,
      Osaka 566-0022, Japan. tetsuya.yoshida@shionogi.co.jp
FAU - Tsuruta, Yuji
AU  - Tsuruta Y
FAU - Iwasaki, Makoto
AU  - Iwasaki M
FAU - Yamane, Shoji
AU  - Yamane S
FAU - Ochi, Takahiro
AU  - Ochi T
FAU - Suzuki, Ryuji
AU  - Suzuki R
LA  - eng
PT  - Journal Article
PL  - England
TA  - J Biochem
JT  - Journal of biochemistry
JID - 0376600
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (COLEC12 protein, human)
RN  - 0 (Collectins)
RN  - 0 (Receptors, Immunologic)
RN  - 0 (Receptors, Scavenger)
RN  - 0 (Tn antigen)
RN  - KM15WK8O5T (Acetylgalactosamine)
SB  - IM
MH  - Acetylgalactosamine/chemistry/*metabolism
MH  - Antigens, Tumor-Associated, Carbohydrate/chemistry/*metabolism
MH  - Cell Line
MH  - Collectins/chemistry/genetics/*metabolism
MH  - Humans
MH  - Protein Binding/genetics
MH  - Receptors, Immunologic/chemistry/genetics/*metabolism
MH  - Receptors, Scavenger
MH  - Transfection
EDAT- 2003/05/23 05:00
MHDA- 2004/01/22 05:00
CRDT- 2003/05/23 05:00
PHST- 2003/05/23 05:00 [pubmed]
PHST- 2004/01/22 05:00 [medline]
PHST- 2003/05/23 05:00 [entrez]
AID - 10.1093/jb/mvg037 [doi]
PST - ppublish
SO  - J Biochem. 2003 Mar;133(3):271-7. doi: 10.1093/jb/mvg037.

PMID- 7681597
OWN - NLM
STAT- MEDLINE
DCOM- 19930423
LR  - 20190501
IS  - 0027-8424 (Print)
IS  - 0027-8424 (Linking)
VI  - 90
IP  - 6
DP  - 1993 Mar 15
TI  - Epitopic structure of Tn glycophorin A for an anti-Tn antibody (MLS 128).
PG  - 2495-9
AB  - Glycophorin A was digested with glycoprotease (Pasteurella haemolytica) and the
      digest was fractionated by a combination of high-pressure column chromatographies
      to produce the glycopeptides GPA-1 to GPA-6. Sequence analysis of the
      glycopeptides revealed that two serine residues (Ser-14 and Ser-15) are not
      glycosylated, Thr-17 and Ser-19 being glycosylated instead, in disagreement with 
      the accepted structure. The glycopeptides thus obtained were treated with
      sialidase and beta-galactosidase. The Tn antigenicity, as assayed by the binding 
      to a monoclonal anti-Tn antibody (MLS 128), was found exclusively in the
      glycopeptides including three (cluster I) or four (cluster II) consecutive
      residues of GalNAc-Ser/Thr, whereas the glycopeptide (GPA-2) containing two
      nonconsecutive GalNAc-Ser/Thr residues had practically no Tn antigenicity. The
      immunoreactivities of GPA-1 and GPA-3, containing both clusters I and II, and
      GPA-4, containing cluster II, were 63% (calcd. 67%), 81% (calcd. 86%), and 50%
      (calcd. 50%), respectively, of the immunoreactivity of GPA-5 or GPA-6, containing
      cluster I (the average being taken as the basis), based on the reactivity per
      GalNAc residue. These results indicate that clusters I and II react with the
      antibody to the same extent. The structure consisting of three consecutive
      glycosylated Ser/Thr residues may be essential for Tn antigenicity in the light
      of previous results for ovine submaxillary mucin.
FAU - Nakada, H
AU  - Nakada H
AD  - Department of Biotechnology, Faculty of Engineering, Kyoto Sangyo University,
      Japan.
FAU - Inoue, M
AU  - Inoue M
FAU - Numata, Y
AU  - Numata Y
FAU - Tanaka, N
AU  - Tanaka N
FAU - Funakoshi, I
AU  - Funakoshi I
FAU - Fukui, S
AU  - Fukui S
FAU - Mellors, A
AU  - Mellors A
FAU - Yamashina, I
AU  - Yamashina I
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Proc Natl Acad Sci U S A
JT  - Proceedings of the National Academy of Sciences of the United States of America
JID - 7505876
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Epitopes)
RN  - 0 (Glycopeptides)
RN  - 0 (Glycophorin)
RN  - 0 (Mucins)
RN  - 0 (Tn antigen)
RN  - EC 3.4.24.- (Metalloendopeptidases)
RN  - EC 3.4.24.57 (O-sialoglycoprotein endopeptidase)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Antibodies, Monoclonal
MH  - Antigens, Tumor-Associated, Carbohydrate/chemistry/*immunology
MH  - Chromatography, Gel
MH  - Chromatography, High Pressure Liquid
MH  - Epitopes/*analysis/chemistry
MH  - Glycopeptides/chemistry/immunology/isolation & purification
MH  - Glycophorin/*chemistry/immunology
MH  - Humans
MH  - Mannheimia haemolytica/enzymology
MH  - Metalloendopeptidases
MH  - Molecular Sequence Data
MH  - Mucins/physiology
MH  - Sheep
PMC - PMC46114
EDAT- 1993/03/15 00:00
MHDA- 1993/03/15 00:01
CRDT- 1993/03/15 00:00
PHST- 1993/03/15 00:00 [pubmed]
PHST- 1993/03/15 00:01 [medline]
PHST- 1993/03/15 00:00 [entrez]
AID - 10.1073/pnas.90.6.2495 [doi]
PST - ppublish
SO  - Proc Natl Acad Sci U S A. 1993 Mar 15;90(6):2495-9. doi: 10.1073/pnas.90.6.2495.

PMID- 16135558
OWN - NLM
STAT- MEDLINE
DCOM- 20060301
LR  - 20061115
IS  - 0959-6658 (Print)
IS  - 0959-6658 (Linking)
VI  - 16
IP  - 1
DP  - 2006 Jan
TI  - ST6GalNAc I expression in MDA-MB-231 breast cancer cells greatly modifies their
      O-glycosylation pattern and enhances their tumourigenicity.
PG  - 54-64
AB  - Sialyl-Tn is a carbohydrate antigen overexpressed in several epithelial cancers, 
      including breast cancer, and usually associated with poor prognosis. Sialyl-Tn is
      synthesized by a CMP-Neu5Ac:GalNAcalpha2,6-sialyltransferase: CMP-Neu5Ac:
      R-GalNAcalpha1-O-Ser/Thr alpha2,6-sialyltransferase (EC 2.4.99.3) (ST6GalNAc I), 
      which transfers a sialic acid residue in alpha2,6-linkage to the
      GalNAcalpha1-O-Ser/Thr structure. However, established breast cancer cell lines
      express neither ST6GalNAc I nor sialyl-Tn. We have previously shown that stable
      transfection of MDA-MB-231, a human breast cancer cell line, with ST6GalNAc I
      cDNA induces sialyl-Tn antigen (STn) expression. We report here the modifications
      of the O-glycosylation pattern of a MUC1-related recombinant protein secreted by 
      MDA-MB-231 sialyl-Tn positive cells. We also show that sialyl-Tn expression and
      concomitant changes in the overall O-glycan profiles induce a decrease of
      adhesion and an increase of migration of MDA-MB-231. Moreover, STn positive
      clones exhibit an increased tumour growth in severe combined immunodeficiency
      (SCID) mice. These observations suggest that modification of the O-glycosylation 
      pattern induced by ST6GalNAc I expression are sufficient to enhance the
      tumourigenicity of MDA-MB-231 breast cancer cells.
FAU - Julien, S
AU  - Julien S
AD  - Centre Commun de Mesures Imagerie Cellulaire, Universite des Sciences et
      Technologies de Lille, F-59655 Villeneuve d'Ascq, France.
FAU - Adriaenssens, E
AU  - Adriaenssens E
FAU - Ottenberg, K
AU  - Ottenberg K
FAU - Furlan, A
AU  - Furlan A
FAU - Courtand, G
AU  - Courtand G
FAU - Vercoutter-Edouart, A-S
AU  - Vercoutter-Edouart AS
FAU - Hanisch, F-G
AU  - Hanisch FG
FAU - Delannoy, P
AU  - Delannoy P
FAU - Le Bourhis, X
AU  - Le Bourhis X
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20050831
PL  - England
TA  - Glycobiology
JT  - Glycobiology
JID - 9104124
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (sialosyl-Tn antigen)
RN  - EC 2.4.99.- (Sialyltransferases)
RN  - EC 2.4.99.3 (CMP-N-acetylneuraminate-alpha-N-acetylgalactosaminide
      alpha-2,6-sialyltransferase)
SB  - IM
MH  - Animals
MH  - Antigens, Tumor-Associated, Carbohydrate/*metabolism
MH  - Breast Neoplasms/*enzymology/pathology
MH  - Cell Line, Tumor
MH  - *Gene Expression Regulation, Enzymologic
MH  - *Gene Expression Regulation, Neoplastic
MH  - Glycosylation
MH  - Humans
MH  - Mice
MH  - Mice, SCID
MH  - Neoplasm Transplantation
MH  - *Protein Modification, Translational
MH  - Sialyltransferases/*biosynthesis
EDAT- 2005/09/02 09:00
MHDA- 2006/03/02 09:00
CRDT- 2005/09/02 09:00
PHST- 2005/09/02 09:00 [pubmed]
PHST- 2006/03/02 09:00 [medline]
PHST- 2005/09/02 09:00 [entrez]
AID - cwj033 [pii]
AID - 10.1093/glycob/cwj033 [doi]
PST - ppublish
SO  - Glycobiology. 2006 Jan;16(1):54-64. doi: 10.1093/glycob/cwj033. Epub 2005 Aug 31.

PMID- 2823004
OWN - NLM
STAT- MEDLINE
DCOM- 19871204
LR  - 20151119
IS  - 0023-6837 (Print)
IS  - 0023-6837 (Linking)
VI  - 57
IP  - 4
DP  - 1987 Oct
TI  - Differentiation antigens defined by mouse monoclonal antibodies against human
      germ cell tumors.
PG  - 350-8
AB  - We have developed two mouse monoclonal antibodies, M912-2A2 and M912-2G10,
      against cell surface antigens of a human infantile embryonal carcinoma cell line,
      MTE. The distribution of these antigens (designated as 2A2 and 2G10) was almost
      identical in human germ cell tumors in which they hallmarked yolk sac components 
      and some tubular endodermal structures. Immunoelectron-microscopically, the
      antigens were located on the microvilli of MTE tumor cells. These antigens were
      not found on other common childhood tumors. In normal and fetal tissues they
      exhibited quite different distributions. In the kidney, 2A2 and 2G10 were present
      on the collecting tubules and proximal/distal tubules, respectively. Expression
      of both antigens was already observed in fetal kidneys of 10 weeks gestational
      age. In hematopoietic cells 2G10 was present only on granulocytes and on
      erythrocytes regardless of ABO blood group, whereas 2A2 was not present on any
      peripheral blood cells. Both antigens were equally expressed in testis and
      epididymis. Biochemically, reactivity of both antibodies was abolished with
      periodate treatment, suggesting their carbohydrate nature. Further biochemical
      characterization revealed that antibody to 2G10 reacts with the nonreducing
      terminal structure of type 2 carbohydrate chain, Ga1 beta 1-4G1cNAc, common to
      nLc4 (paragloboside), nLc6 (neolactohexaose), and Y4 neutral glycolipids of
      O-type erythrocytes. These data illustrate the complexity of carbohydrate
      antigens on yolk sac components of human germ cell tumors and provide a basis for
      the study of primitive endodermal and yolk sac differentiation in these tumors.
FAU - Fujimoto, J
AU  - Fujimoto J
AD  - Department of Pathology, National Children's Medical Research Center, Tokyo,
      Japan.
FAU - Hata, J
AU  - Hata J
FAU - Ishii, E
AU  - Ishii E
FAU - Tanaka, S
AU  - Tanaka S
FAU - Kannagi, R
AU  - Kannagi R
FAU - Ueyama, Y
AU  - Ueyama Y
FAU - Tamaoki, N
AU  - Tamaoki N
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Lab Invest
JT  - Laboratory investigation; a journal of technical methods and pathology
JID - 0376617
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens, Differentiation)
RN  - 0 (Antigens, Neoplasm)
RN  - 0 (Biomarkers, Tumor)
RN  - 0 (Carbohydrates)
SB  - IM
MH  - Animals
MH  - *Antibodies, Monoclonal/immunology
MH  - Antigens, Differentiation/*analysis/immunology
MH  - Antigens, Neoplasm/*analysis/immunology
MH  - Biomarkers, Tumor/analysis
MH  - Carbohydrates/immunology
MH  - Cell Membrane/immunology
MH  - Endoderm/immunology
MH  - Humans
MH  - Kidney/embryology/immunology
MH  - Mice
MH  - Mice, Inbred BALB C
MH  - Microscopy, Electron
MH  - Neoplasm Transplantation
MH  - Neoplasms/immunology
MH  - Neoplasms, Germ Cell and Embryonal/*immunology
MH  - Teratoma/immunology
MH  - Tissue Distribution
MH  - Tumor Cells, Cultured
EDAT- 1987/10/01 00:00
MHDA- 1987/10/01 00:01
CRDT- 1987/10/01 00:00
PHST- 1987/10/01 00:00 [pubmed]
PHST- 1987/10/01 00:01 [medline]
PHST- 1987/10/01 00:00 [entrez]
PST - ppublish
SO  - Lab Invest. 1987 Oct;57(4):350-8.

PMID- 11919403
OWN - NLM
STAT- MEDLINE
DCOM- 20020606
LR  - 20171101
IS  - 0250-8095 (Print)
IS  - 0250-8095 (Linking)
VI  - 22
IP  - 1
DP  - 2002 Jan-Feb
TI  - High endothelial venule-like vessels in the interstitial lesions of human
      glomerulonephritis.
PG  - 48-57
AB  - To clarify the characteristics of high endothelial venule (HEV) -like vessels in 
      the interstitium of human glomerulonephritis, we investigated the expression of
      HEVs related molecules such as P-selectin and L-selectin ligands; MECA-79 epitope
      and variant sulfated forms of sialyl Lewis X (variant sLe(X), clones 2H5, 2F3,
      GS-13 and GS-36) in kidney specimens by means of immunohistochemical studies, and
      P-selectin and hevin mRNA signals by using in situ hybridization analyses. In
      lymphoid organs, HEVs strongly expressed P-selectin, MECA-79, variant sLe(X) and 
      hevin mRNA signals. In normal kidneys (n = 4), only P-selectin was faintly
      positive in the vessels of interstitium, but other molecules could not be
      detected. Interstitial P-selectin expression was upregulated in patients with
      tubulointerstitial diseases (n = 4) and proliferative glomerulonephritis (n = 51)
      such as IgA-related nephropathy (n = 39), membranoproliferative
      glomerulonephritis (n = 4) and crescentic glomerulonephritis (n = 2), but not in 
      nonproliferative glomerular diseases (n = 39) such as minimal change nephrotic
      syndrome (n = 18) (1.00 +/- 0.41, 0.64 +/- 0.11, 0.21 +/- 0.05, respectively).
      Interstitial P-selectin expression also correlated with interstitial local
      cellular infiltration (r = 0.60, p < 0.0001). In addition, P-selectin mRNA
      signals were detected on the peritubular capillaries and HEV-like vascular
      endothelial cells. MECA-79 and variant sLe(X) (2H5 and 2F3) were weakly expressed
      on the HEV-like vessels located at the corticomedullary regions in three cases
      (7%) and in nine cases (27%) with interstitial cellular infiltration,
      respectively. However, we could not detect GS-13, GS-36 or hevin mRNA signals in 
      the diseased kidney specimens. In conclusion, HEV-like vessels in renal
      interstitium expressed molecules somewhat different from HEVs in lymphoid organs 
      and were associated with interstitial leukocyte accumulation in human
      proliferative glomerulonephritis possibly through the de novo expression of
      P-selectin and partly L-selectin ligands (MECA-79 epitope and variant sLe(X)) in 
      the interstitial lesions.
CI  - Copyright 2002 S. Karger AG, Basel
FAU - Takaeda, Masayoshi
AU  - Takaeda M
AD  - Department of Gastroenterology and Nephrology, Graduate School of Medicine,
      Kanazawa University, Kanazawa, Japan. dialysis@medf.m.kanazawa-u.ac.jp
FAU - Yokoyama, Hitoshi
AU  - Yokoyama H
FAU - Segawa-Takaeda, Chikako
AU  - Segawa-Takaeda C
FAU - Wada, Takashi
AU  - Wada T
FAU - Kobayashi, Ken-ichi
AU  - Kobayashi K
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - Switzerland
TA  - Am J Nephrol
JT  - American journal of nephrology
JID - 8109361
RN  - 0
      (5-acetylneuraminyl-(2-3)-galactosyl-(1-4)-(fucopyranosyl-(1-3))-N-acetylglucosam
      ine)
RN  - 0 (Ligands)
RN  - 0 (Oligosaccharides)
RN  - 0 (P-Selectin)
RN  - 126880-86-2 (L-Selectin)
SB  - IM
MH  - Endothelium, Vascular/*cytology
MH  - Female
MH  - Glomerulonephritis/metabolism/*pathology
MH  - Humans
MH  - Immunohistochemistry
MH  - L-Selectin/metabolism
MH  - Ligands
MH  - Male
MH  - Oligosaccharides/metabolism
MH  - P-Selectin/metabolism
EDAT- 2002/03/29 10:00
MHDA- 2002/06/12 10:01
CRDT- 2002/03/29 10:00
PHST- 2002/03/29 10:00 [pubmed]
PHST- 2002/06/12 10:01 [medline]
PHST- 2002/03/29 10:00 [entrez]
AID - 46674 [pii]
AID - 10.1159/000046674 [doi]
PST - ppublish
SO  - Am J Nephrol. 2002 Jan-Feb;22(1):48-57. doi: 10.1159/000046674.

PMID- 2355641
OWN - NLM
STAT- MEDLINE
DCOM- 19900720
LR  - 20151119
IS  - 0047-1852 (Print)
IS  - 0047-1852 (Linking)
VI  - 48 Suppl
DP  - 1990 Feb
TI  - [2D3 series, MSW 113 and other monoclonal antibodies directed to type 1 chain
      carbohydrate antigens].
PG  - 992-8
FAU - Kannagi, R
AU  - Kannagi R
AD  - Department of Laboratory Medicine and Clinical Science, Faculty of Medicine,
      Kyoto University.
FAU - Takada, A
AU  - Takada A
FAU - Shigeta, K
AU  - Shigeta K
FAU - Itai, S
AU  - Itai S
FAU - Hashimoto, K
AU  - Hashimoto K
LA  - jpn
PT  - Journal Article
PL  - Japan
TA  - Nihon Rinsho
JT  - Nihon rinsho. Japanese journal of clinical medicine
JID - 0420546
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
SB  - IM
MH  - *Antibodies, Monoclonal
MH  - Antigens, Tumor-Associated, Carbohydrate/*analysis
MH  - Digestive System Neoplasms/diagnosis
MH  - Humans
MH  - Pancreatic Neoplasms/*diagnosis
EDAT- 1990/02/01 00:00
MHDA- 1990/02/01 00:01
CRDT- 1990/02/01 00:00
PHST- 1990/02/01 00:00 [pubmed]
PHST- 1990/02/01 00:01 [medline]
PHST- 1990/02/01 00:00 [entrez]
PST - ppublish
SO  - Nihon Rinsho. 1990 Feb;48 Suppl:992-8.

PMID- 8652593
OWN - NLM
STAT- MEDLINE
DCOM- 19960730
LR  - 20061115
IS  - 0006-2960 (Print)
IS  - 0006-2960 (Linking)
VI  - 35
IP  - 7
DP  - 1996 Feb 20
TI  - Lipopolysaccharide of the Helicobacter pylori type strain NCTC 11637 (ATCC
      43504): structure of the O antigen chain and core oligosaccharide regions.
PG  - 2489-97
AB  - Smooth- and rough-form lipopolysaccharides from phenol-water extraction of cells 
      from Helicobacter pylori type strain NCTC 11637 were isolated as the
      water-soluble component of high-M(r) and water-insoluble low-M(r) gel. Structural
      investigations were performed on the intact water-soluble smooth-form
      lipopolysaccharide, various oligosaccharides formed as chemical and enzymic
      degradation products, and three oligosaccharide fractions liberated by acetic
      acid hydrolysis from the water-insoluble rough-form lipopolysaccharide. A
      structure is proposed for the complete polysaccharide component of the
      smooth-form lipopolysaccharide comprising the O antigen chain, an intervening
      region, and the inner core oligosaccharide on the basis of 1H and 13C NMR
      experiments, fast atom bombardment/mass spectrometry, and methylation linkage
      analysis of permethylated oligo- and polysaccharide derivatives. The most
      striking feature of the O antigen region in the lipopolysaccharide is the
      presence of extended chains with fucosylated and nonfucosylated
      N-acetyllactosamine (LacNAc) units that mimic human cell surface glycoconjugates 
      in normal human granulocytes. The chains are terminated by di- or trimeric
      Lewis(x) (Le(x)) determinants, which are also found in tumor-associated
      carbohydrate antigens in many adenocarcinomas.
FAU - Aspinall, G O
AU  - Aspinall GO
AD  - Department of Chemistry, York University, Toronto, Ontario, Canada.
FAU - Monteiro, M A
AU  - Monteiro MA
FAU - Pang, H
AU  - Pang H
FAU - Walsh, E J
AU  - Walsh EJ
FAU - Moran, A P
AU  - Moran AP
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Biochemistry
JT  - Biochemistry
JID - 0370623
RN  - 0 (O Antigens)
RN  - 0 (Oligosaccharides)
SB  - IM
MH  - Carbohydrate Conformation
MH  - Carbohydrate Sequence
MH  - Helicobacter pylori/*chemistry
MH  - Humans
MH  - Molecular Sequence Data
MH  - O Antigens/*chemistry
MH  - Oligosaccharides/*chemistry
EDAT- 1996/02/20 00:00
MHDA- 1996/02/20 00:01
CRDT- 1996/02/20 00:00
PHST- 1996/02/20 00:00 [pubmed]
PHST- 1996/02/20 00:01 [medline]
PHST- 1996/02/20 00:00 [entrez]
AID - 10.1021/bi951852s [doi]
AID - bi951852s [pii]
PST - ppublish
SO  - Biochemistry. 1996 Feb 20;35(7):2489-97. doi: 10.1021/bi951852s.

PMID- 10092871
OWN - NLM
STAT- MEDLINE
DCOM- 19990422
LR  - 20161017
IS  - 0014-2956 (Print)
IS  - 0014-2956 (Linking)
VI  - 259
IP  - 3
DP  - 1999 Feb
TI  - N-glycan structures of matrix metalloproteinase-1 derived from human fibroblasts 
      and from HT-1080 fibrosarcoma cells.
PG  - 829-40
AB  - Matrix metalloproteinase-1 (MMP-1) is a collagenolytic metalloproteinase capable 
      of cleaving native triple-helical forms of several collagen subtypes, as well as 
      a number of non-collagenous substrates. The role of MMP-1 in various diseases
      affecting the connective tissue is well characterized. MMP-1 is secreted as both 
      glycosylated and unglycosylated species, and the two forms have been shown to be 
      identical with respect to substrate specificity, specific activity and inhibitory
      profile. No function for the glycan moiety of the enzyme has been ascribed to
      date. In the present study, we report on the detailed characterization of
      MMP-1-derived oligosaccharides. Using strategies based on sequential
      exoglycosidase digestion combined with matrix-assisted laser desorption
      ionization-time of flight MS and electrospray tandem MS, we have characterized
      the N-glycan structures of MMP-1, derived from human dermal fibroblasts and from 
      the HT-1080 fibrosarcoma cell line. MMP-1 derived from fibroblasts was found to
      carry mainly alpha 2,3-sialylated complex-type diantennary glycans. On the other 
      hand, HT-1080 cells produce MMP-1 that has a heterogeneous glycosylation pattern,
      comprising diantennary glycans carrying Lewis X, LacdiNAc, sialylated LacdiNAc
      and GalNAc beta 1,4 (Fuc alpha 1,3)GlcNAc (LacdiNAc analogue of Lewis X) as
      terminal elements. We also show that, of the two potential glycosylation sites in
      the MMP-1 sequence, only Asn120 is used.
FAU - Saarinen, J
AU  - Saarinen J
AD  - Institute of Biotechnology, University of Helsinki, Finland.
      juhani.saarinen@helsinki.fi
FAU - Welgus, H G
AU  - Welgus HG
FAU - Flizar, C A
AU  - Flizar CA
FAU - Kalkkinen, N
AU  - Kalkkinen N
FAU - Helin, J
AU  - Helin J
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - Eur J Biochem
JT  - European journal of biochemistry
JID - 0107600
RN  - 0 (Oligosaccharides)
RN  - 0 (Polysaccharides)
RN  - EC 3.2.1.- (Glycoside Hydrolases)
RN  - EC 3.4.24.- (Collagenases)
RN  - EC 3.4.24.7 (Matrix Metalloproteinase 1)
SB  - IM
MH  - Carbohydrate Sequence
MH  - Cells, Cultured
MH  - Collagenases/*chemistry
MH  - Glycoside Hydrolases/metabolism
MH  - Glycosylation
MH  - Humans
MH  - Mass Spectrometry
MH  - Matrix Metalloproteinase 1
MH  - Molecular Sequence Data
MH  - Oligosaccharides/chemistry
MH  - Polysaccharides/*chemistry
EDAT- 1999/03/27 00:00
MHDA- 1999/03/27 00:01
CRDT- 1999/03/27 00:00
PHST- 1999/03/27 00:00 [pubmed]
PHST- 1999/03/27 00:01 [medline]
PHST- 1999/03/27 00:00 [entrez]
PST - ppublish
SO  - Eur J Biochem. 1999 Feb;259(3):829-40.

PMID- 18678667
OWN - NLM
STAT- MEDLINE
DCOM- 20081016
LR  - 20181113
IS  - 1098-5522 (Electronic)
IS  - 0019-9567 (Linking)
VI  - 76
IP  - 10
DP  - 2008 Oct
TI  - Identification of the smallest structure capable of evoking opsonophagocytic
      antibodies against Streptococcus pneumoniae type 14.
PG  - 4615-23
LID - 10.1128/IAI.00472-08 [doi]
AB  - Synthetic overlapping oligosaccharide fragments of Streptococcus pneumoniae
      serotype 14 capsular polysaccharide (Pn14PS),
      [6)-[beta-D-Galp-(1-->4)-]beta-D-GlcpNAc-(1-->3)-beta-D-Galp-(1-->4)-beta-D-Glcp-
      (1-->](n), were conjugated to CRM(197) protein and injected into mice to
      determine the smallest immunogenic structure. The resulting antibodies were then 
      tested for Pn14PS specificity and for their capacity to promote the phagocytosis 
      of S. pneumoniae type 14 bacteria. Earlier studies have reported that the
      oligosaccharide corresponding to one structural repeating unit of Pn14PS, i.e.,
      Gal-Glc-(Gal-)GlcNAc, induces a specific antibody response to Pn14PS. The broader
      study described here, which evaluated 16 oligosaccharides, showed that the
      branched trisaccharide element Glc-(Gal-)GlcNAc is essential in inducing
      Pn14PS-specific antibodies and that the neighboring galactose unit at the
      nonreducing end contributes clearly to the immunogenicity of the epitope. Only
      the oligosaccharide conjugates that produce antibodies recognizing Pn14PS were
      capable of promoting the phagocytosis of S. pneumoniae type 14. In conclusion,
      the branched tetrasaccharide Gal-Glc-(Gal-)GlcNAc may be a serious candidate for 
      a synthetic oligosaccharide conjugate vaccine against infections caused by S.
      pneumoniae type 14.
FAU - Safari, Dodi
AU  - Safari D
AD  - Department of Medical Microbiology, University Medical Center Utrecht, Utrecht,
      The Netherlands.
FAU - Dekker, Huberta A T
AU  - Dekker HA
FAU - Joosten, John A F
AU  - Joosten JA
FAU - Michalik, Dirk
AU  - Michalik D
FAU - de Souza, Adriana Carvalho
AU  - de Souza AC
FAU - Adamo, Roberto
AU  - Adamo R
FAU - Lahmann, Martina
AU  - Lahmann M
FAU - Sundgren, Andreas
AU  - Sundgren A
FAU - Oscarson, Stefan
AU  - Oscarson S
FAU - Kamerling, Johannis P
AU  - Kamerling JP
FAU - Snippe, Harm
AU  - Snippe H
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20080804
PL  - United States
TA  - Infect Immun
JT  - Infection and immunity
JID - 0246127
RN  - 0 (Antibodies, Bacterial)
RN  - 0 (Bacterial Proteins)
RN  - 0 (Epitopes)
RN  - 0 (Immunoglobulin G)
RN  - 0 (Opsonin Proteins)
RN  - 0 (Vaccines, Conjugate)
RN  - 08VC9WC084 (CRM197 (non-toxic variant of diphtheria toxin))
SB  - IM
MH  - Animals
MH  - Antibodies, Bacterial/*blood
MH  - Bacterial Capsules/*immunology
MH  - Bacterial Proteins/immunology
MH  - Carbohydrate Sequence
MH  - Epitopes/immunology
MH  - Female
MH  - Immunoglobulin G/blood
MH  - Mice
MH  - Mice, Inbred BALB C
MH  - Molecular Sequence Data
MH  - Molecular Structure
MH  - Opsonin Proteins/*blood
MH  - Phagocytosis/*immunology
MH  - Streptococcus pneumoniae/*immunology
MH  - Vaccines, Conjugate/immunology
PMC - PMC2546832
EDAT- 2008/08/06 09:00
MHDA- 2008/10/17 09:00
CRDT- 2008/08/06 09:00
PHST- 2008/08/06 09:00 [pubmed]
PHST- 2008/10/17 09:00 [medline]
PHST- 2008/08/06 09:00 [entrez]
AID - IAI.00472-08 [pii]
AID - 10.1128/IAI.00472-08 [doi]
PST - ppublish
SO  - Infect Immun. 2008 Oct;76(10):4615-23. doi: 10.1128/IAI.00472-08. Epub 2008 Aug
      4.

PMID- 2010622
OWN - NLM
STAT- MEDLINE
DCOM- 19910503
LR  - 20180602
IS  - 0022-1759 (Print)
IS  - 0022-1759 (Linking)
VI  - 137
IP  - 1
DP  - 1991 Mar 1
TI  - In vitro immunization of rat spleen lymphocytes with Forssman glycosphingolipid
      antigen and the generation of a monoclonal antibody.
PG  - 95-102
AB  - A procedure for in vitro immunization of splenic lymphocytes with a glycolipid
      antigen is described. Culture medium supernatant of ConA- and PHA-stimulated
      spleen cells and that of Con A-stimulated human Jurkat T cell line (IL-2-rich
      medium) were used as sources of cytokines to support T and B cell stimulation,
      and anti-mu was used to support B cell differentiation. Unprimed rat spleen cells
      (2 x 10(6)/ml) were stimulated with 2 micrograms/ml Forssman glycolipid antigen
      coupled to Sepharose for 4 days. The cells were fused with a mouse myeloma cell
      line P3-X63-Ag8-U1. At initial screening, 12% of the colony forming wells were
      secreting specific antibody. After cloning, a stable hybridoma cell line
      (designated 4C3) was established which secreted a monoclonal IgM antibody
      directed against the carbohydrate moiety of Forssman glycosphingolipid (GalNAc
      alpha 1-3GalNAc beta 1-3Gal alpha 1-4Gal beta 1-4Glc-ceramide).
FAU - Gathuru, J K
AU  - Gathuru JK
AD  - Department of Biochemistry, Faculty of Veterinary Medicine, Hokkaido University, 
      Sapporo, Japan.
FAU - Miyoshi, I
AU  - Miyoshi I
FAU - Naiki, M
AU  - Naiki M
LA  - eng
PT  - Journal Article
PL  - Netherlands
TA  - J Immunol Methods
JT  - Journal of immunological methods
JID - 1305440
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Globosides)
RN  - 60267-39-2 (Forssman glycolipid)
RN  - 9013-60-9 (Forssman Antigen)
SB  - IM
MH  - Animals
MH  - Antibodies, Monoclonal/*biosynthesis
MH  - Forssman Antigen/*immunology
MH  - Globosides/*immunology
MH  - Immunization
MH  - Lymphocyte Activation
MH  - Lymphocytes/*immunology
MH  - Male
MH  - Rats
MH  - Spleen/*immunology
MH  - Time Factors
EDAT- 1991/03/01 00:00
MHDA- 1991/03/01 00:01
CRDT- 1991/03/01 00:00
PHST- 1991/03/01 00:00 [pubmed]
PHST- 1991/03/01 00:01 [medline]
PHST- 1991/03/01 00:00 [entrez]
AID - 0022-1759(91)90398-Y [pii]
PST - ppublish
SO  - J Immunol Methods. 1991 Mar 1;137(1):95-102.

PMID- 9359491
OWN - NLM
STAT- MEDLINE
DCOM- 19971117
LR  - 20181211
IS  - 0020-7136 (Print)
IS  - 0020-7136 (Linking)
VI  - 73
IP  - 3
DP  - 1997 Nov 4
TI  - Stimulation of proliferation in human colon cancer cells by human monoclonal
      antibodies against the TF antigen (galactose beta1-3 N-acetyl-galactosamine).
PG  - 424-31
AB  - In many tissues, the TF (Thomsen-Friedenreich) blood group antigen
      (Galbeta1-3GalNAc alpha-) behaves as an onco-foetal carbohydrate antigen, showing
      increased expression in malignancy and hyperplasia. Dietary lectins which bind
      the TF antigen have marked effects on proliferation of epithelial cells without
      cytotoxicity. This led us to speculate that anti-TF antibodies, including those
      that naturally occur in humans, might have similar effects. Five anti-TF
      antibodies, TF2 (human), TF5 (human), 5A8 (mouse), 8D8 (mouse) and BM22 (mouse), 
      but not TFI (human) or 49H.9 (mouse), showed marked dose-dependent stimulation
      (95-192%) of [3H]thymidine incorporation by HT29 human colon cancer cells.
      Similar stimulation of proliferation of HT29 cells by these monoclonal antibodies
      (MAbs) was found when cell count assessment was used. Antibody-stimulated
      proliferation was inhibited by co-incubation with glycoproteins expressing
      Galbeta1-3GalNAc alpha- (asialo glycophorin or [Galbeta1-3GalNAc
      alpha-O-p-aminophenyl]n-human serum albumin). A proliferative effect of these
      antibodies was also demonstrated on human colon cancer cell lines LS174T and
      HT29-MTX but not on Caco-2 cells. Although immunoblotting showed similar binding 
      patterns of all the antibodies on HT29 cell membrane extracts, there was little
      correlation between cell surface binding assessed by immunofluorescence and
      proliferative response, and internalization of the biotinylated antibody TF5 was 
      demonstrated by confocal microscopy. Our results provide further evidence that
      cell surface glycoproteins which express TF antigen may play an important role in
      the regulation of cell proliferation and also suggest that human anti-TF
      antibodies may have proliferative effects on cells which express TF antigen.
FAU - Yu, L G
AU  - Yu LG
AD  - Department of Medicine, University of Liverpool, UK. lgyu@liv.ac.uk
FAU - Jansson, B
AU  - Jansson B
FAU - Fernig, D G
AU  - Fernig DG
FAU - Milton, J D
AU  - Milton JD
FAU - Smith, J A
AU  - Smith JA
FAU - Gerasimenko, O V
AU  - Gerasimenko OV
FAU - Jones, M
AU  - Jones M
FAU - Rhodes, J M
AU  - Rhodes JM
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Int J Cancer
JT  - International journal of cancer
JID - 0042124
RN  - 0 (Antibodies)
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 3554-90-3 (Thomsen-Friedenreich antigen)
RN  - 3HG052TF3I (Thomsen-Friedenreich antibodies)
SB  - IM
MH  - Antibodies/metabolism/*pharmacology
MH  - Antibodies, Monoclonal/metabolism/*pharmacology
MH  - Antigens, Tumor-Associated, Carbohydrate/*immunology
MH  - Caco-2 Cells
MH  - Cell Division/drug effects
MH  - Colonic Neoplasms/immunology/metabolism/*pathology
MH  - Erythrocytes/drug effects
MH  - Hemagglutination Tests
MH  - Humans
MH  - Tumor Cells, Cultured
EDAT- 1997/11/14 00:29
MHDA- 2000/06/20 09:00
CRDT- 1997/11/14 00:29
PHST- 1997/11/14 00:29 [pubmed]
PHST- 2000/06/20 09:00 [medline]
PHST- 1997/11/14 00:29 [entrez]
AID - 10.1002/(SICI)1097-0215(19971104)73:3<424::AID-IJC18>3.0.CO;2-C [pii]
PST - ppublish
SO  - Int J Cancer. 1997 Nov 4;73(3):424-31.

PMID- 3192544
OWN - NLM
STAT- MEDLINE
DCOM- 19890103
LR  - 20151119
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 263
IP  - 34
DP  - 1988 Dec 5
TI  - Analysis of the expression of N-glycolylneuraminic acid-containing gangliosides
      in cells and tissues using two human monoclonal antibodies.
PG  - 18507-12
AB  - The specificities of two human monoclonal antibodies (2-39M and 32-27M), produced
      by hybridomas derived from the lymphocytes of melanoma patients (Yamaguchi, H.,
      Furukawa, K., Fortunato, S. R., Livingston, P. O., Lloyd, K. O., Oettgen, H. F., 
      and Old, L. J. (1987) Proc. Natl. Acad. Sci. U.S.A. 84, 2416-2420) have been
      elucidated. Using a large panel of glycolipids, it has been shown that the two
      monoclonal antibodies (mAbs) identified a number of N-glycolylneuraminic acid
      (NeuGc)-containing gangliosides. mAb 2-39M reacted with (NeuGc)GM3,
      (NeuGc)sialylparagloboside, and (NeuGc)sialylhexaglycosylceramide; no reactivity 
      was observed with gangliosides containing only N-acetylneuraminic acid (NeuAc) or
      with disialogangliosides. These reactive species have the NeuGc alpha 2----3Gal- 
      sequence in common. mAb 32-27M reacted strongly with (NeuGc)2 GD3 and
      (NeuGc)2disialylparagloboside, and moderately with (NeuAc-NeuGc-)GD3 and
      (NeuAc-NeuGc-)disialylparagloboside. The reactive species have sialic acid alpha 
      2----8NeuGc alpha 2----3Gal- sequences in common. These two antibodies were used 
      to demonstrate the species-related presence of different NeuGc-containing
      gangliosides in various animal erythrocytes by thin layer chromatography
      immunostaining. No reactivity of either mAb was observed with gangliosides
      isolated from fresh human colon cancer, melanoma specimens, or some normal
      tissues, including brain. On the other hand, it was shown that mAb 32-27M reacted
      with gangliosides isolated from human melanoma and astrocytoma cells grown in
      fetal bovine serum but not from those grown in synthetic medium. Within the
      sensitivities of the methods used, these data, and related chemical analyses, do 
      not support the presence of NeuGc-containing gangliosides in human tumors.
FAU - Furukawa, K
AU  - Furukawa K
AD  - Memorial Sloan-Kettering Cancer Center, New York, New York 10021.
FAU - Yamaguchi, H
AU  - Yamaguchi H
FAU - Oettgen, H F
AU  - Oettgen HF
FAU - Old, L J
AU  - Old LJ
FAU - Lloyd, K O
AU  - Lloyd KO
LA  - eng
GR  - CA 08478/CA/NCI NIH HHS/United States
GR  - CA 47427/CA/NCI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Gangliosides)
RN  - 0 (Neuraminic Acids)
RN  - 1113-83-3 (N-glycolylneuraminic acid)
SB  - IM
MH  - Animals
MH  - *Antibodies, Monoclonal
MH  - Carbohydrate Sequence
MH  - Gangliosides/*analysis/immunology
MH  - Hemagglutination
MH  - Humans
MH  - Hybridomas/immunology
MH  - Lymphocytes/immunology
MH  - Melanoma/immunology
MH  - Neuraminic Acids/*analysis
MH  - Species Specificity
EDAT- 1988/12/05 00:00
MHDA- 1988/12/05 00:01
CRDT- 1988/12/05 00:00
PHST- 1988/12/05 00:00 [pubmed]
PHST- 1988/12/05 00:01 [medline]
PHST- 1988/12/05 00:00 [entrez]
PST - ppublish
SO  - J Biol Chem. 1988 Dec 5;263(34):18507-12.

PMID- 1727929
OWN - NLM
STAT- MEDLINE
DCOM- 19920127
LR  - 20170210
IS  - 0732-183X (Print)
IS  - 0732-183X (Linking)
VI  - 10
IP  - 1
DP  - 1992 Jan
TI  - Serum sialyl Tn as an independent predictor of poor prognosis in patients with
      epithelial ovarian cancer.
PG  - 95-101
AB  - PURPOSE: Monoclonal antibody (moAB) TKH-2 directed to the tumor-associated
      O-linked sialyl 2-6-alpha-N-acetylgalactosaminyl (sialyl Tn; STN) epitope was
      generated by immunization with ovine submaxillary mucin (Kjeldsen et al, Cancer
      Res 48:2214-2220, 1988). We investigated whether circulating serum levels of STN 
      antigen might influence the prognosis of patients with ovarian cancer. PATIENTS
      AND METHODS: Serum samples were obtained from 126 healthy nonpregnant women, 157 
      patients with benign gynecologic disease, and 89 patients with histologically
      proven epithelial ovarian cancer. Circulating serum STN-antigen concentrations
      (U/mL) were determined by a competitive radioimmunoassay kit (Otsuka Assay
      Laboratories, Tokushima, Japan) in a one-step procedure. RESULTS: Serum antigen
      levels were elevated in 48.3% of the patients. The levels of STN antigen were
      significantly higher in the sera of patients with cancer when compared with
      levels in benign and healthy controls (P less than .05). The 5-year survival rate
      for patients with STN-negative (serum STN levels less than 50.0 U/mL) versus
      STN-positive (greater than or equal to 50 U/mL) tumors was 76.9% versus 10.8%,
      respectively (P less than .05). The progression-free interval (PFI) at 5 years
      was 51.9% versus 5.4%, respectively (P less than .05). The overall survival
      probability and PFI were worse in patients with STN-positive sera. Multivariate
      regression analysis revealed that stage, residual tumor size, positive STN,
      performance status, and histologic grade were the five important variables for
      predicting overall survival. CONCLUSION: We conclude that a positive STN-antigen 
      level in sera is an independent predictor of poor prognosis in ovarian cancer.
FAU - Kobayashi, H
AU  - Kobayashi H
AD  - Department of Obstetrics and Gynecology, Hamamatsu University School of Medicine,
      Shizuoka, Japan.
FAU - Terao, T
AU  - Terao T
FAU - Kawashima, Y
AU  - Kawashima Y
LA  - eng
PT  - Journal Article
PL  - United States
TA  - J Clin Oncol
JT  - Journal of clinical oncology : official journal of the American Society of
      Clinical Oncology
JID - 8309333
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens, Neoplasm)
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Biomarkers, Tumor)
RN  - 0 (sialosyl-Tn antigen)
SB  - IM
MH  - Adult
MH  - Aged
MH  - Antibodies, Monoclonal
MH  - Antigens, Neoplasm/*blood
MH  - *Antigens, Tumor-Associated, Carbohydrate
MH  - Biomarkers, Tumor/*blood
MH  - Carcinoma/*immunology/*mortality/pathology
MH  - Female
MH  - Humans
MH  - Middle Aged
MH  - Multivariate Analysis
MH  - Neoplasm Staging
MH  - Ovarian Neoplasms/*immunology/*mortality/pathology
MH  - Prognosis
MH  - Proportional Hazards Models
MH  - Radioimmunoassay
MH  - Survival Analysis
EDAT- 1992/01/01 00:00
MHDA- 1992/01/01 00:01
CRDT- 1992/01/01 00:00
PHST- 1992/01/01 00:00 [pubmed]
PHST- 1992/01/01 00:01 [medline]
PHST- 1992/01/01 00:00 [entrez]
AID - 10.1200/JCO.1992.10.1.95 [doi]
PST - ppublish
SO  - J Clin Oncol. 1992 Jan;10(1):95-101. doi: 10.1200/JCO.1992.10.1.95.

PMID- 11550317
OWN - NLM
STAT- MEDLINE
DCOM- 20011025
LR  - 20181023
IS  - 1522-8517 (Print)
IS  - 1522-8517 (Linking)
VI  - 1
IP  - 4
DP  - 1999 Oct
TI  - Immunohistochemical staining for ganglioside GD1b as a diagnostic and prognostic 
      marker for primary human brain tumors.
PG  - 261-7
LID - 10.1093/neuonc/1.4.261 [doi]
AB  - Immunohistochemical staining intensity for ganglioside GD1b was determined for
      108 human neuroectodermal tumors. Most of the tissue elements that immunostained 
      were tumor cells; only a few axons and occasional neurons reacted in some
      specimens. All pilocytic astrocytomas stained very positively, whereas none of
      the ependymomas and only 11% of primitive neuroectodermal tumors, 20% of
      glioblastomas, and 28% of anaplastic astrocytomas showed more than faint
      staining. A similar association between grade and immunostaining was seen in
      tumors containing an oligodendrogliomatous component, but reactivity was not as
      strong as in astrocytic tumors or primitive neuroectodermal tumors. Results of
      Cox regression showed significant associations between immunostaining intensity
      and survival for all cases taken together (P = 0.007); for the group consisting
      of astrocytomas, oligoastrocytomas, and oligodendrogliomas (P = 0.002); and for
      astrocytomas alone (P = 0.04). Results were also significant using a proportional
      hazards model controlling for patient age (all cases P = 0.005; astrocytomas only
      P = 0.02), but not when controlling for tumor grade. Our results indicate that
      immunohistochemical staining for GD1b is correlated with tumor grade and that it 
      may be of prognostic utility in some primary human brain tumors, especially
      astrocytomas.
FAU - Comas, T C
AU  - Comas TC
AD  - Ohio State University, Columbus, OH 43210, USA.
FAU - Tai, T
AU  - Tai T
FAU - Kimmel, D
AU  - Kimmel D
FAU - Scheithauer, B W
AU  - Scheithauer BW
FAU - Burger, P C
AU  - Burger PC
FAU - Pearl, D K
AU  - Pearl DK
FAU - Jewell, S D
AU  - Jewell SD
FAU - Yates, A J
AU  - Yates AJ
LA  - eng
GR  - P30 CA16058/CA/NCI NIH HHS/United States
GR  - UO1-CA50905/CA/NCI NIH HHS/United States
GR  - UO1-CA50910/CA/NCI NIH HHS/United States
GR  - UO1-CA64928/CA/NCI NIH HHS/United States
PT  - Comparative Study
PT  - Evaluation Studies
PT  - Journal Article
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - England
TA  - Neuro Oncol
JT  - Neuro-oncology
JID - 100887420
RN  - 0 (Biomarkers, Tumor)
RN  - 0 (Gangliosides)
RN  - 19553-76-5 (ganglioside, GD1b)
SB  - IM
MH  - Astrocytoma/chemistry/mortality
MH  - Biomarkers, Tumor/*analysis/chemistry
MH  - Brain Neoplasms/*chemistry/mortality
MH  - Carbohydrate Sequence
MH  - Gangliosides/*analysis/chemistry
MH  - Humans
MH  - Immunoenzyme Techniques
MH  - Life Tables
MH  - Molecular Sequence Data
MH  - Neuroectodermal Tumors, Primitive/chemistry/mortality
MH  - Oligodendroglioma/chemistry/mortality
MH  - Prognosis
MH  - Proportional Hazards Models
MH  - Reproducibility of Results
MH  - Survival Analysis
PMC - PMC1920757
EDAT- 2001/09/12 10:00
MHDA- 2001/10/26 10:01
CRDT- 2001/09/12 10:00
PHST- 2001/09/12 10:00 [pubmed]
PHST- 2001/10/26 10:01 [medline]
PHST- 2001/09/12 10:00 [entrez]
AID - 10.1093/neuonc/1.4.261 [doi]
PST - ppublish
SO  - Neuro Oncol. 1999 Oct;1(4):261-7. doi: 10.1093/neuonc/1.4.261.

PMID- 17855742
OWN - NLM
STAT- MEDLINE
DCOM- 20071219
LR  - 20071018
IS  - 0959-6658 (Print)
IS  - 0959-6658 (Linking)
VI  - 17
IP  - 11
DP  - 2007 Nov
TI  - Sulfatide binding properties of murine and human antiganglioside antibodies.
PG  - 1156-66
AB  - Antiganglioside antibodies form an important component of the innate and adaptive
      B cell repertoire, where they provide antimicrobial activity through binding
      encapsulated bacterial glycans. In an aberrant role, they target peripheral nerve
      gangliosides to induce autoimmune nerve injury. An important characteristic of
      antiganglioside antibodies is their ability to selectively recognize highly
      defined glycan structures. Since sialylated and sulfated glycans often share
      lectin recognition patterns, we here explored the possibility that certain
      antiganglioside antibodies might also bind 3-O-sulfo-beta-D-galactosylceramide
      (sulfatide), an abundant constituent of plasma and peripheral nerve myelin, that 
      could thereby influence any immunoregulatory or autoimmune properties. Out of 25 
      antiganglioside antibodies screened in solid phase assays, 20 also bound
      sulfatide (10(-5) to 10(-6) M range) in addition to their favored ganglioside
      glycan epitope ( approximately 10(-7) M range). Solution inhibition studies
      demonstrated competition between ganglioside and sulfatide, indicating close
      proximity or sharing of the antigen binding variable region domain. Sulfatide and
      3-O-sulfo-beta-D-galactose were unique in having this property amongst a wide
      range of sulfated glycans screened, including 4- and 6-O-sulfo-beta-D-galactose
      analogues. Antiganglioside antibody binding to 3-O-sulfo-beta-D-galactose was
      highly dependent upon the spatial presentation of the ligand, being completely
      inhibited by conjugation to protein or polyacrylamide (PAA) matrices. Binding was
      also absent when sulfatide was incorporated into plasma membranes, including
      myelin, under conditions in which antibody binding to ganglioside was retained.
      These data demonstrate that sulfatide binding is a common property of
      antiganglioside antibodies that may provide functional insights into, and
      consequences for this component of the innate immune repertoire.
FAU - Townson, Kate
AU  - Townson K
AD  - Division of Clinical Neurosciences, Glasgow Biomedical Research Centre,
      University of Glasgow, G12 8TA Scotland. k.townson@clinmed.gla.ac.uk
FAU - Greenshields, Kay N
AU  - Greenshields KN
FAU - Veitch, Jean
AU  - Veitch J
FAU - Nicholl, Dawn
AU  - Nicholl D
FAU - Eckhardt, Matthias
AU  - Eckhardt M
FAU - Galanina, Oxana
AU  - Galanina O
FAU - Bovin, Nicolai
AU  - Bovin N
FAU - Samain, Eric
AU  - Samain E
FAU - Antoine, Tatiana
AU  - Antoine T
FAU - Bundle, David
AU  - Bundle D
FAU - Zhang, Ping
AU  - Zhang P
FAU - Ling, Chang Chun
AU  - Ling CC
FAU - Willison, Hugh J
AU  - Willison HJ
LA  - eng
GR  - gr060349/Wellcome Trust/United Kingdom
GR  - gr077041/Wellcome Trust/United Kingdom
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20070913
PL  - England
TA  - Glycobiology
JT  - Glycobiology
JID - 9104124
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Gangliosides)
RN  - 0 (Sulfoglycosphingolipids)
SB  - IM
MH  - Animals
MH  - Antibodies, Monoclonal/*immunology
MH  - Cell Membrane/metabolism
MH  - Enzyme-Linked Immunosorbent Assay
MH  - Gangliosides/*immunology
MH  - Humans
MH  - Kinetics
MH  - Mice
MH  - PC12 Cells
MH  - Rats
MH  - Sulfoglycosphingolipids/chemistry/*immunology/metabolism
EDAT- 2007/09/15 09:00
MHDA- 2007/12/20 09:00
CRDT- 2007/09/15 09:00
PHST- 2007/09/15 09:00 [pubmed]
PHST- 2007/12/20 09:00 [medline]
PHST- 2007/09/15 09:00 [entrez]
AID - cwm095 [pii]
AID - 10.1093/glycob/cwm095 [doi]
PST - ppublish
SO  - Glycobiology. 2007 Nov;17(11):1156-66. doi: 10.1093/glycob/cwm095. Epub 2007 Sep 
      13.

PMID- 6094178
OWN - NLM
STAT- MEDLINE
DCOM- 19850110
LR  - 20181130
IS  - 0261-4189 (Print)
IS  - 0261-4189 (Linking)
VI  - 3
IP  - 10
DP  - 1984 Oct
TI  - Blood group-active carbohydrate chains on the receptor for epidermal growth
      factor of A431 cells.
PG  - 2227-33
AB  - The antigens expressed on the carbohydrate chains of the receptor for epidermal
      growth factor of A431 cells were studied by immunoblotting with monoclonal
      antibodies. Blood group A and the Type 1 based blood group ALeb and Lea antigens 
      were detected as well as antigens associated with unsubstituted, monofucosylated 
      and difucosylated Type 2 blood group chains. The Lea and the difucosylated Type 2
      antigen activities were abolished by treating the blotted receptor with
      endo-beta-galactosidase, indicating that they are expressed on backbone
      structures of poly-lacto/neolacto type. (The term 'poly-lacto/neolacto' is used
      here to describe oligosaccharide backbone structures consisting of repeating Type
      1, Gal beta 1-3GlcNAc (lacto) or Type 2, Gal beta 1-4GlcNAc (neolacto)
      sequences.) The glycosidic linkage of oligosaccharides to protein was
      investigated using Pronase digests of the receptor biosynthetically labelled with
      [3H]glucosamine or [3H]fucose. The oligosaccharides were alkali-resistant,
      consistent with N- rather than O-glycosidically linked chains. A proportion of
      [3H]fucose-labelled glycopeptides was susceptible to endo-beta-galactosidase,
      confirming the immunoblotting experiment using antibodies against the Lea and the
      difucosylated Type 2 antigenic determinants. Oligosaccharides were released from 
      the [3H]fucose- and [3H]-glucosamine-labelled glycopeptides by hydrazinolysis.
      Chromatography of the oligosaccharides on Bio-Gel P6 and Concanavalin A columns
      indicated a spectrum of oligosaccharides which include those of high mannose type
      labelled with [3H]glucosamine, and a mixture of oligosaccharides labelled with
      [3H]fucose and [3H]glucosamine of bi- and multiantennary complex types of which a
      subpopulation is susceptible to digestion with endo-beta-galactosidase.
FAU - Childs, R A
AU  - Childs RA
FAU - Gregoriou, M
AU  - Gregoriou M
FAU - Scudder, P
AU  - Scudder P
FAU - Thorpe, S J
AU  - Thorpe SJ
FAU - Rees, A R
AU  - Rees AR
FAU - Feizi, T
AU  - Feizi T
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - EMBO J
JT  - The EMBO journal
JID - 8208664
RN  - 0 (ABO Blood-Group System)
RN  - 0 (Oligosaccharides)
RN  - 0 (Receptors, Cell Surface)
RN  - 28RYY2IV3F (Fucose)
RN  - EC 2.7.10.1 (ErbB Receptors)
RN  - EC 3.2.1.18 (Neuraminidase)
RN  - N08U5BOQ1K (Glucosamine)
SB  - IM
MH  - ABO Blood-Group System/*immunology
MH  - Animals
MH  - Carbohydrate Sequence
MH  - Carcinoma, Squamous Cell/*analysis
MH  - Cell Line
MH  - ErbB Receptors
MH  - Fucose/metabolism
MH  - Glucosamine/metabolism
MH  - Humans
MH  - Mice
MH  - Molecular Weight
MH  - Neuraminidase/metabolism
MH  - Oligosaccharides/*immunology
MH  - Receptors, Cell Surface/*analysis
PMC - PMC557674
EDAT- 1984/10/01 00:00
MHDA- 1984/10/01 00:01
CRDT- 1984/10/01 00:00
PHST- 1984/10/01 00:00 [pubmed]
PHST- 1984/10/01 00:01 [medline]
PHST- 1984/10/01 00:00 [entrez]
PST - ppublish
SO  - EMBO J. 1984 Oct;3(10):2227-33.

PMID- 18301385
OWN - NLM
STAT- MEDLINE
DCOM- 20080804
LR  - 20180822
IS  - 0818-9641 (Print)
IS  - 0818-9641 (Linking)
VI  - 86
IP  - 4
DP  - 2008 May-Jun
TI  - Distribution of the alphaGal- and the non-alphaGal T-antigens in the pig kidney: 
      potential targets for rejection in pig-to-man xenotransplantation.
PG  - 363-71
LID - 10.1038/icb.2008.1 [doi]
AB  - Carbohydrate antigens, present on pig vascular endothelial cells, seem to be the 
      prime agents responsible for graft rejection, and although genetically modified
      animals that express less amounts of carbohydrate antigen are available, it is
      still useful to decide the localization of the reactive xenoantigens in organs
      contemplated for xenotransplantation. Here we compare the distribution in pig
      kidney of antigens important in xenograft destruction, namely the Galalpha1-3Gal 
      (alphaGal) glycans, with the localization of the T-antigen (Galbeta1-3GalNAc).
      The alpha-galactose-specific lectin Griffonia simplicifolia isolectin 1B4 was
      used to detect the Galalpha1-3Gal glycans, whereas Arachis hypogaea (PNA) lectin 
      and a monoclonal antibody (3C9) detected T-antigen. In addition, two vascular
      markers (anti-caveolin-1 and anti-von Willebrand factor) served to identify
      vascular structures of the kidney. Both conventional fluorescence and confocal
      microscopy were used to distinguish lectin and immunohistochemical staining. On
      the basis of fluorescence signals, the results indicate that the carbohydrate
      antigens are heterogeneously distributed in the pig kidney. alphaGal epitopes
      were sparse in the capillary loops forming the glomeruli and in the capillaries
      surrounding the convoluted tubules, but showed stronger staining in capillaries
      surrounding the limbs of Henle. In addition, the brush border and basement
      membranes of the convoluted tubules strongly reacted with the GS1-B4-lectin.
      Finally, the Galalpha1-3Gal glycans were also present on epithelial cells of the 
      large collecting tubules. Regarding the T-antigen, PNA and 3C9 reacted with
      different glomerular cells, whereas both reacted strongly with the endothelial
      cells lining the large kidney vessels. Human serum incubation of pig kidney
      sections, in which the alphaGal epitopes were blocked by unconjugated GS1-B4,
      showed staining of the same vascular structures as were obtained after incubation
      with the T-antigen-detecting agents. The study thus proves a complex spatial
      distribution of carbohydrate antigens relevant for xenotransplantation of pig
      kidney.
FAU - Kirkeby, Svend
AU  - Kirkeby S
AD  - Department of Oral Medicine, The Panum Institute, School of Dentistry, University
      of Copenhagen, Copenhagen N, Denmark. sk@odont.ku.dk
FAU - Mikkelsen, Hanne B
AU  - Mikkelsen HB
LA  - eng
PT  - Journal Article
DEP - 20080226
PL  - United States
TA  - Immunol Cell Biol
JT  - Immunology and cell biology
JID - 8706300
RN  - 0 (Antigens)
RN  - 0 (Griffonia simplicifolia lectins)
RN  - 0 (Plant Lectins)
RN  - X2RN3Q8DNE (Galactose)
SB  - IM
MH  - Animals
MH  - Antigens/*immunology
MH  - Female
MH  - Galactose/*immunology
MH  - Graft Rejection/*immunology
MH  - Humans
MH  - Immunohistochemistry
MH  - Kidney/*immunology
MH  - Plant Lectins/immunology
MH  - Swine/*immunology
MH  - Transplantation, Heterologous/*immunology
EDAT- 2008/02/28 09:00
MHDA- 2008/08/05 09:00
CRDT- 2008/02/28 09:00
PHST- 2008/02/28 09:00 [pubmed]
PHST- 2008/08/05 09:00 [medline]
PHST- 2008/02/28 09:00 [entrez]
AID - icb20081 [pii]
AID - 10.1038/icb.2008.1 [doi]
PST - ppublish
SO  - Immunol Cell Biol. 2008 May-Jun;86(4):363-71. doi: 10.1038/icb.2008.1. Epub 2008 
      Feb 26.

PMID- 1864848
OWN - NLM
STAT- MEDLINE
DCOM- 19910911
LR  - 20071219
IS  - 0021-924X (Print)
IS  - 0021-924X (Linking)
VI  - 109
IP  - 2
DP  - 1991 Feb
TI  - A new monoclonal antibody directed to sialyl alpha 2-3lactoneotetraosylceramide
      and its application for detection of human gastrointestinal neoplasms.
PG  - 354-60
AB  - A new monoclonal antibody (NS24) directed to the N-acetylneuraminyl alpha 2-3Gal 
      beta 1-4GlcNAc residue in type II sugar chain of
      N-acetylneuraminyllactoneotetraosylceramide [sialylparagloboside,
      IV3(NeuAc)nLc4Cer] was prepared by hybridoma technique. Liposomes composed of
      dipalmitoylphosphatidylcholine, cholesterol, IV3(NeuAc)nLc4Cer, and
      lipopolysaccharides from Salmonella minnesota R595 were used for immunization
      with IV3(NeuAc)nLc4Cer isolated from human erythrocytes. This method allowed the 
      fusion of spleen cells of immunized mouse with myeloma cells only three days
      after immunization. NS24 reacted specifically to both naturally occurring and
      chemically synthesized IV3-(NeuAc)nLc4Cer, whereas it has no reactivity to
      structurally related gangliosides, such as IV6(NeuAc)nLc4Cer,
      N-glycolylneuraminyl alpha 2-3lactoneotetraosylceramide [IV3(NeuGc)-nLc4Cer],
      i-active ganglioside [VI3(NeuAc)nLc6Cer], I-active ganglioside
      [VIII3(NeuAc)-VI3(NeuAc)IV6kladoLc8Cer], GM4(NeuAc), GM3(NeuAc), GM3(NeuGc),
      GM1b(NeuAc), GD3-(NeuAc), other ganglio-series gangliosides, sulfatide, and
      paragloboside (nLc4Cer). Synthetic N-acetylneuraminyl alpha
      2-3lactotetraosylceramide [IV3(NeuAc)Lc4Cer] and its asialo-derivative (Lc4Cer)
      carrying type I sugar chain also showed no reaction with NS24. One to 100 pmol of
      IV3(NeuAc)nLc4Cer was detected dose-dependently by a thin-layer
      chromatography/enzyme immunostaining procedure. Human gastric carcinomas showed
      positive reactions with NS24 immunochemically and histochemically. NS24 reacted
      preferentially with poorly differentiated adenocarcinomas rather than well
      differentiated ones.
FAU - Suzuki, Y
AU  - Suzuki Y
AD  - Department of Biochemistry, University of Shizuoka, School of Pharmaceutical
      Science.
FAU - Nishi, H
AU  - Nishi H
FAU - Hidari, K
AU  - Hidari K
FAU - Hirabayashi, Y
AU  - Hirabayashi Y
FAU - Matsumoto, M
AU  - Matsumoto M
FAU - Kobayashi, T
AU  - Kobayashi T
FAU - Watarai, S
AU  - Watarai S
FAU - Yasuda, T
AU  - Yasuda T
FAU - Nakayama, J
AU  - Nakayama J
FAU - Maeda, H
AU  - Maeda H
AU  - et al.
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - J Biochem
JT  - Journal of biochemistry
JID - 0376600
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Globosides)
RN  - 0 (Immunoglobulin M)
RN  - 71833-57-3 (sialosylparagloboside)
SB  - IM
MH  - Adenocarcinoma/*diagnosis/immunology/pathology
MH  - Antibodies, Monoclonal/*immunology
MH  - Antibody Specificity
MH  - Carbohydrate Sequence
MH  - Chromatography, Thin Layer
MH  - Erythrocytes/chemistry
MH  - Gastrointestinal Neoplasms/*diagnosis/immunology/pathology
MH  - Globosides/*immunology
MH  - Humans
MH  - Hybridomas/immunology
MH  - Immunoglobulin M/immunology
MH  - Molecular Sequence Data
MH  - Sensitivity and Specificity
EDAT- 1991/02/01 00:00
MHDA- 1991/02/01 00:01
CRDT- 1991/02/01 00:00
PHST- 1991/02/01 00:00 [pubmed]
PHST- 1991/02/01 00:01 [medline]
PHST- 1991/02/01 00:00 [entrez]
PST - ppublish
SO  - J Biochem. 1991 Feb;109(2):354-60.

PMID- 7560094
OWN - NLM
STAT- MEDLINE
DCOM- 19951113
LR  - 20181113
IS  - 0021-9738 (Print)
IS  - 0021-9738 (Linking)
VI  - 96
IP  - 4
DP  - 1995 Oct
TI  - Impairment of selectin-mediated leukocyte adhesion to venular endothelium in
      spontaneously hypertensive rats.
PG  - 2009-16
AB  - The present study was designed to elucidate whether molecular mechanisms for
      leukocyte adhesion to microvascular endothelium may differ between spontaneously 
      hypertensive rats and Wistar Kyoto rats. Leukocyte rolling and adhesion were
      investigated while monitoring venular wall shear rates in the mesenteric
      microcirculation stimulated with histamine or tert-butyl hydroperoxide in the two
      strains. In Wistar Kyoto rats, 10 microM histamine as well as 500 microM
      tertbutyl hydroperoxide promoted a significant reduction of venular leukocyte
      rolling velocity and subsequent adhesion. These changes in leukocyte behavior
      were blocked by monoclonal antibodies against P-selectin (PB 1.3) and against
      sialyl Lewis X-like carbohydrates (2H5). However, spontaneously hypertensive rats
      exhibited a blunted response of the stimulus-elicited leukocyte rolling, which
      was associated with impairment of venular P-selectin expression as well as a
      decrease in the expression of sialyl Lewis X-like carbohydrates on circulating
      neutrophils. No significant differences were detected between the two strains not
      only in the surface CD11b/CD18 expression but also in the CD18-mediated
      adhesivity of neutrophils to intracellular adhesion molecule-1 transfectants in
      vitro. These results suggest that impairment of selectin-mediated leukocyte
      adhesion is an event responsible for disorders of inflammatory responses in
      spontaneously hypertensive rats.
FAU - Suematsu, M
AU  - Suematsu M
AD  - Department of Bioengineering, University of California, San Diego, La Jolla
      92093-0412, USA.
FAU - Suzuki, H
AU  - Suzuki H
FAU - Tamatani, T
AU  - Tamatani T
FAU - Iigou, Y
AU  - Iigou Y
FAU - DeLano, F A
AU  - DeLano FA
FAU - Miyasaka, M
AU  - Miyasaka M
FAU - Forrest, M J
AU  - Forrest MJ
FAU - Kannagi, R
AU  - Kannagi R
FAU - Zweifach, B W
AU  - Zweifach BW
FAU - Ishimura, Y
AU  - Ishimura Y
AU  - et al.
LA  - eng
GR  - HL-10881/HL/NHLBI NIH HHS/United States
GR  - HL-43026/HL/NHLBI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - J Clin Invest
JT  - The Journal of clinical investigation
JID - 7802877
RN  - 0 (P-Selectin)
RN  - 0 (Peroxides)
RN  - 820484N8I3 (Histamine)
RN  - 955VYL842B (tert-Butylhydroperoxide)
SB  - AIM
SB  - IM
MH  - Animals
MH  - CHO Cells
MH  - Cell Adhesion
MH  - Cricetinae
MH  - Endothelium, Vascular/cytology/*physiology
MH  - Histamine/pharmacology
MH  - Hypertension/*blood
MH  - Leukocytes/*physiology
MH  - Male
MH  - Neutrophils/physiology
MH  - P-Selectin/analysis/*physiology
MH  - Peroxides/pharmacology
MH  - Rats
MH  - Rats, Inbred SHR
MH  - Rats, Inbred WKY
MH  - tert-Butylhydroperoxide
PMC - PMC185839
EDAT- 1995/10/01 00:00
MHDA- 1995/10/01 00:01
CRDT- 1995/10/01 00:00
PHST- 1995/10/01 00:00 [pubmed]
PHST- 1995/10/01 00:01 [medline]
PHST- 1995/10/01 00:00 [entrez]
AID - 10.1172/JCI118248 [doi]
PST - ppublish
SO  - J Clin Invest. 1995 Oct;96(4):2009-16. doi: 10.1172/JCI118248.

PMID- 2473071
OWN - NLM
STAT- MEDLINE
DCOM- 19890818
LR  - 20071114
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 264
IP  - 21
DP  - 1989 Jul 25
TI  - A new ganglioside of the lactotetraose series, GalNAc-3'-isoLM1, detected in
      human meconium.
PG  - 12122-5
AB  - A monoclonal antibody produced by immunization with cells of the human glioma
      cell line D-54 MG reacted with ganglioside GM2. The binding epitope of the
      antibody was found to be GalNAc beta 1-4(NeuAc alpha 2-3)Gal. Immunological
      detection of glycolipid antigens on thin-layer plates with this monoclonal
      antibody, DMAb-1, revealed the presence of a new ganglioside. This ganglioside,
      co-migrating with NeuAc alpha 2-6Gal beta 1-4GlcNAc beta 1-3Gal beta 1-4Glc beta 
      1-1Cer(6'-LM1) and GalNAc beta 1-4(NeuAc alpha 2-3)Gal beta 1-3GalNAc beta 1-4Gla
      beta 1-4Glc beta 1-1Cer (GalNAc-isoGM1) at chromatographic separation was
      isolated from human meconium. Its structure was determined by permethylation and 
      fast atom bombardment-mass spectometry analyses. The new ganglioside was found to
      be a combination of the lacto and ganglio series gangliosides, and the structure 
      found to be GalNAc beta 1-4(NeuAc alpha 2-3)Gal beta 1-3GlcNAc alpha 1-3Gal beta 
      1-4Glc beta 1-1Cer(GalNAc-3'-isoLM1).
FAU - Fredman, P
AU  - Fredman P
AD  - Department of Psychiatry and Neurochemistry, Gothenburg University, St. Jorgen
      Hospital, Hisings Backa, Sweden.
FAU - Mansson, J E
AU  - Mansson JE
FAU - Wikstrand, C J
AU  - Wikstrand CJ
FAU - Vrionis, F D
AU  - Vrionis FD
FAU - Rynmark, B M
AU  - Rynmark BM
FAU - Bigner, D D
AU  - Bigner DD
FAU - Svennerholm, L
AU  - Svennerholm L
LA  - eng
GR  - CA32672/CA/NCI NIH HHS/United States
GR  - NS 20023/NS/NINDS NIH HHS/United States
GR  - R37 CA11898/CA/NCI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Epitopes)
RN  - 0 (Gangliosides)
RN  - 0 (Glycolipids)
RN  - 122932-83-6 (GalNAc-3'-isoL(M1) ganglioside)
RN  - 19600-01-2 (G(M2) Ganglioside)
SB  - IM
MH  - Antibodies, Monoclonal
MH  - Carbohydrate Conformation
MH  - Carbohydrate Sequence
MH  - Epitopes/analysis
MH  - G(M2) Ganglioside/isolation & purification
MH  - Gangliosides/immunology/*isolation & purification
MH  - Glycolipids/immunology
MH  - Humans
MH  - Infant, Newborn
MH  - Mass Spectrometry
MH  - Meconium/*analysis
MH  - Molecular Sequence Data
EDAT- 1989/07/25 00:00
MHDA- 1989/07/25 00:01
CRDT- 1989/07/25 00:00
PHST- 1989/07/25 00:00 [pubmed]
PHST- 1989/07/25 00:01 [medline]
PHST- 1989/07/25 00:00 [entrez]
PST - ppublish
SO  - J Biol Chem. 1989 Jul 25;264(21):12122-5.

PMID- 2342728
OWN - NLM
STAT- MEDLINE
DCOM- 19900626
LR  - 20151119
IS  - 0029-7844 (Print)
IS  - 0029-7844 (Linking)
VI  - 75
IP  - 6
DP  - 1990 Jun
TI  - Clinical value of sialyl Tn antigen in patients with gynecologic tumors.
PG  - 1032-6
AB  - Sialyl Tn antigen was measured by the immunoradiometric competitive inhibition
      assay in sera from patients with various gynecologic tumors: 49 uterine myomas,
      97 cervical cancers, 42 endometrial cancers, 63 benign ovarian tumors, and 59
      ovarian cancers including eight cases of borderline malignancy. Among the
      patients with uterine malignancies, a few cases showed a sialyl Tn antigen level 
      in excess of the cutoff limit (39 U/mL). In the patients with ovarian cancers,
      serum sialyl Tn antigen was significantly elevated: clinical stage I, 31%; stage 
      II, 29%; and stage III, 69%. The antigen level also correlated with the effect of
      treatment. In addition, malignant fluid exhibited a high sialyl Tn antigen level,
      whereas benign fluid showed no elevation. However, serum sialyl Tn antigen was
      elevated in 6% of the patients with benign ovarian cysts and in 1.5% of normal
      volunteers. The current findings demonstrate that the lack of tumor specificity
      of sialyl Tn antigen limits its diagnostic value in gynecologic malignancies, but
      that serial measurement of this antigen appears to be useful for monitoring
      patients and evaluating therapy.
FAU - Inoue, M
AU  - Inoue M
AD  - Department of Obstetrics and Gynecology, Osaka University Medical School, Japan.
FAU - Ogawa, H
AU  - Ogawa H
FAU - Nakanishi, K
AU  - Nakanishi K
FAU - Tanizawa, O
AU  - Tanizawa O
FAU - Karino, K
AU  - Karino K
FAU - Endo, J
AU  - Endo J
LA  - eng
PT  - Journal Article
PL  - United States
TA  - Obstet Gynecol
JT  - Obstetrics and gynecology
JID - 0401101
RN  - 0 (ABO Blood-Group System)
RN  - 0 (Antigens, Neoplasm)
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Biomarkers, Tumor)
RN  - 0 (Lewis Blood-Group System)
RN  - 0 (sialosyl-Tn antigen)
SB  - AIM
SB  - IM
MH  - ABO Blood-Group System
MH  - Antigens, Neoplasm/*analysis
MH  - *Antigens, Tumor-Associated, Carbohydrate
MH  - Biomarkers, Tumor/*analysis
MH  - Female
MH  - Humans
MH  - Lewis Blood-Group System
MH  - Ovarian Neoplasms/blood/*diagnosis/pathology
MH  - Radioimmunoassay
MH  - Uterine Cervical Neoplasms/diagnosis
MH  - Uterine Neoplasms/blood/*diagnosis/pathology
EDAT- 1990/06/01 00:00
MHDA- 1990/06/01 00:01
CRDT- 1990/06/01 00:00
PHST- 1990/06/01 00:00 [pubmed]
PHST- 1990/06/01 00:01 [medline]
PHST- 1990/06/01 00:00 [entrez]
PST - ppublish
SO  - Obstet Gynecol. 1990 Jun;75(6):1032-6.

PMID- 2537068
OWN - NLM
STAT- MEDLINE
DCOM- 19890317
LR  - 20061115
IS  - 0003-9985 (Print)
IS  - 0003-9985 (Linking)
VI  - 113
IP  - 2
DP  - 1989 Feb
TI  - Blood-group-related antigen Lewis(x) and Lewis(y) in the differential diagnosis
      of cholangiocarcinoma and hepatocellular carcinoma.
PG  - 139-42
AB  - Distribution of Lewis(x) (Le(x)) and Lewis(y) (Le(y)) blood-group antigens was
      studied in nine formaldehyde-fixed, paraffin-embedded cholangiocarcinomas (CCs), 
      26 hepatocellular carcinomas (HCCs), and eight normal livers. All CCs, with one
      exception, expressed both Le(x) and Le(y) antigens on few or many cells. In HCCs 
      Lex was expressed infrequently (8%), while Le(y) was detected in 31% of cases.
      Both markers, when present in HCCs, tended to be spotty. Fibrolamellar carcinomas
      and normal livers did not react with either Le(x) or Le(y) antigens; however,
      Le(y) antigen was observed occasionally in bile duct epithelial and ductular
      cells. In conclusion, inappropriate tissue distribution of Le(y) blood-group
      antigens was observed in CCs and, much less frequently, in HCCs. The high
      frequency of Le(x) antigen in CCs but not in HCCs may help in the differential
      diagnosis of these two tumors.
FAU - Jovanovic, R
AU  - Jovanovic R
AD  - Immunopathology Laboratory, Veterans Administration Medical Center, Bronx, NY
      10468.
FAU - Jagirdar, J
AU  - Jagirdar J
FAU - Thung, S N
AU  - Thung SN
FAU - Paronetto, F
AU  - Paronetto F
LA  - eng
PT  - Journal Article
PT  - Research Support, U.S. Gov't, Non-P.H.S.
PL  - United States
TA  - Arch Pathol Lab Med
JT  - Archives of pathology & laboratory medicine
JID - 7607091
RN  - 0 (Isoantigens)
RN  - 0 (Lewis Blood-Group System)
SB  - AIM
SB  - IM
MH  - Adenoma, Bile Duct/*diagnosis/immunology/pathology
MH  - Carcinoma, Hepatocellular/*diagnosis/immunology/pathology
MH  - Diagnosis, Differential
MH  - Humans
MH  - Immunohistochemistry
MH  - Isoantigens/*analysis
MH  - *Lewis Blood-Group System
MH  - Liver Neoplasms/*diagnosis/immunology/pathology
EDAT- 1989/02/01 00:00
MHDA- 1989/02/01 00:01
CRDT- 1989/02/01 00:00
PHST- 1989/02/01 00:00 [pubmed]
PHST- 1989/02/01 00:01 [medline]
PHST- 1989/02/01 00:00 [entrez]
PST - ppublish
SO  - Arch Pathol Lab Med. 1989 Feb;113(2):139-42.

PMID- 1674743
OWN - NLM
STAT- MEDLINE
DCOM- 19910701
LR  - 20171116
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 266
IP  - 16
DP  - 1991 Jun 5
TI  - Characterization of a novel Le(x)-active ganglioside from chick intestinal
      tissues recognized by murine monoclonal antibody 188C1.
PG  - 10268-74
AB  - A monoclonal antibody, 188C1, raised against skin tissue from the back of
      bullfrogs (Rana catesbeiana) was found to recognize a common antigen in neural
      and intestinal tissues of chicken (Fujita, S. (1989) in Biological Transduction
      Mechanisms (Kasai, M., Yoshioka, T., and Suzuki, H., eds) pp. 159-177, Japan
      Scientific Societies Press, Tokyo Japan). The 188C1 antigen was isolated from
      chick intestinal tissues and characterized as a novel ganglioside by means of
      Q-Sepharose and Iatrobeads column chromatography, and chemical, immunochemical,
      and immunohistochemical analyses. The chemical structure was as follows: Gal beta
      1-4 GlcNAc beta 1-3Gal beta 1-3GalNAc beta 1-4Gal beta 1-4Glc beta 1-1'Cer Fuc
      alpha 1-3 NeuAc alpha 2-3 This represents a novel hybrid structure of type 2
      Le(x) epitope and GM1 ganglioside core structure, designated as Le(x)-GM1.
      Monoclonal antibody 188C1 reacted strongly with Le(x)-GM1 on thin layer
      chromatography, but its reactivity was greatly reduced when sialic acid was
      removed from the antigen. This indicated that the internal sialic acid residue
      might participate in antigenicity of the Le(x) determinant. In addition to 188C1,
      a more specific antibody reacting with Le(x)-GM1 but not with asialo-Le(x)-GM1
      was raised by immunizing a rabbit with Le(x)-GM1. TLC/enzyme immunostaining using
      this specific antibody showed the presence of Le(x)-GM1 in chick intestinal
      tissue, but not in chick brain.
FAU - Hirabayashi, Y
AU  - Hirabayashi Y
AD  - Department of Biochemistry, University of Shizuoka, School of Pharmaceutical
      Sciences, Japan.
FAU - Fujita, S C
AU  - Fujita SC
FAU - Kon, K
AU  - Kon K
FAU - Ando, S
AU  - Ando S
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Ceramides)
RN  - 0 (Gangliosides)
RN  - 0 (Lewis X Antigen)
SB  - IM
MH  - Animals
MH  - Antibodies, Monoclonal/*immunology
MH  - Cattle
MH  - Ceramides/chemistry
MH  - Chick Embryo
MH  - Chromatography, Gel
MH  - Chromatography, Thin Layer
MH  - Enzyme-Linked Immunosorbent Assay
MH  - Gangliosides/*chemistry
MH  - Gas Chromatography-Mass Spectrometry
MH  - Immunohistochemistry
MH  - Lewis X Antigen
MH  - Methylation
MH  - Rana catesbeiana
MH  - Spectrometry, Mass, Fast Atom Bombardment
EDAT- 1991/06/05 00:00
MHDA- 1991/06/05 00:01
CRDT- 1991/06/05 00:00
PHST- 1991/06/05 00:00 [pubmed]
PHST- 1991/06/05 00:01 [medline]
PHST- 1991/06/05 00:00 [entrez]
PST - ppublish
SO  - J Biol Chem. 1991 Jun 5;266(16):10268-74.

PMID- 2404571
OWN - NLM
STAT- MEDLINE
DCOM- 19900309
LR  - 20131121
IS  - 0008-5472 (Print)
IS  - 0008-5472 (Linking)
VI  - 50
IP  - 3
DP  - 1990 Feb 1
TI  - Glycine to aspartic acid mutations at codon 13 of the c-Ki-ras gene in human
      gastrointestinal cancers.
PG  - 480-2
AB  - Point mutations of c-ras genes were analyzed in human gastrointestinal cancers.
      DNA obtained from the tissues was amplified by polymerase chain reaction and then
      analyzed by dot blot hybridization assay with oligonucleotide probes to detect
      mutations at codons 12, 13, and 61 of c-Ki-ras, c-Ha-ras, and c-N-ras. In two of 
      25 cases of stomach cancer point mutations at codon 13 of c-Ki-ras were found. In
      colorectal cancer, eight of 30 cases showed mutations: four cases of codon 12 and
      one case at codon 13 of c-Ki-ras and two cases at codon 61 and one case at codon 
      13 of c-N-ras. These results may indicate involvement of a wide variety of c-ras 
      gene point mutations, in addition to those at codon 12 of c-Ki-ras, in
      oncogenesis of human gastrointestinal cancers. In all three mutations of c-Ki-ras
      at codon 13 which had been seldom found in human cancers, glycine to aspartic
      acid mutations due to identical G to A transition at the second nucleotide were
      observed.
FAU - Nagata, Y
AU  - Nagata Y
AD  - Department of Oncology, Nagasaki University School of Medicine, Japan.
FAU - Abe, M
AU  - Abe M
FAU - Kobayashi, K
AU  - Kobayashi K
FAU - Yoshida, K
AU  - Yoshida K
FAU - Ishibashi, T
AU  - Ishibashi T
FAU - Naoe, T
AU  - Naoe T
FAU - Nakayama, E
AU  - Nakayama E
FAU - Shiku, H
AU  - Shiku H
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Cancer Res
JT  - Cancer research
JID - 2984705R
RN  - 0 (DNA, Neoplasm)
RN  - 0 (Oligonucleotide Probes)
RN  - 0 (Proto-Oncogene Proteins)
RN  - 30KYC7MIAI (Aspartic Acid)
RN  - EC 3.6.5.2 (HRAS protein, human)
RN  - EC 3.6.5.2 (Proto-Oncogene Proteins p21(ras))
RN  - TE7660XO1C (Glycine)
SB  - IM
MH  - Aspartic Acid
MH  - Base Sequence
MH  - DNA, Neoplasm/genetics
MH  - Gastrointestinal Neoplasms/*genetics/pathology
MH  - *Genes, ras
MH  - Glycine
MH  - Humans
MH  - Molecular Sequence Data
MH  - Mutation
MH  - Oligonucleotide Probes
MH  - Polymerase Chain Reaction
MH  - Proto-Oncogene Proteins/*genetics
MH  - Proto-Oncogene Proteins p21(ras)
EDAT- 1990/02/01 00:00
MHDA- 1990/02/01 00:01
CRDT- 1990/02/01 00:00
PHST- 1990/02/01 00:00 [pubmed]
PHST- 1990/02/01 00:01 [medline]
PHST- 1990/02/01 00:00 [entrez]
PST - ppublish
SO  - Cancer Res. 1990 Feb 1;50(3):480-2.

PMID- 11004681
OWN - NLM
STAT- MEDLINE
DCOM- 20001115
LR  - 20160303
IS  - 0020-7136 (Print)
IS  - 0020-7136 (Linking)
VI  - 88
IP  - 2
DP  - 2000 Oct 15
TI  - Expression of SIALYL-Le(x) antigen defined by MAb AM-3 is an independent
      prognostic marker in colorectal carcinoma patients.
PG  - 281-6
AB  - Expression of mucin-bound sialyl-Le(x) antigen during the progression of
      colorectal carcinoma and its potential prognostic value were analysed in sections
      of tumours from 182 patients with a documented follow-up by immunohistochemistry 
      using the monoclonal antibody (MAb) AM-3. Two groups of colonic carcinomas with
      weak (n = 79) and strong (n = 103) sialyl-Le(x) expression were discerned. The
      percentage of strongly expressing tumours increased with the progression of the
      disease (UICC stage I = 10%, stage II = 46%, stage III = 63%, stage IV = 68%, p <
      0.0001). Seventy-four percent of patients with carcinomas exhibiting a strong
      sialyl-Le(x) expression but only 34% of patients with weak sialyl-Le(x)
      expression died of the disease (p = 0.0026). In multivariate analysis, strong
      sialyl-Le(x) expression increased the relative risk of cancer-related death
      3.8-fold (95% CI = 1.8-7.9, p = 0.00034). The separate analyses of patients in
      UICC stage II (n = 56), III (n =5 9) and IV (n = 57) revealed that strong
      sialyl-Le(x) expression was associated with a reduction of the 5-year overall
      survival rate in UICC stage II (84% vs. 54%, p = 0.0013) and in stage III
      patients (86% vs. 35%, p = 0.0008) after curative resection but was not relevant 
      in patients with distant metastases. In conclusion, the strong expression of
      sialyl-Le(x) antigen defined by the MAb AM-3 in colorectal carcinomas is an
      independent unfavourable prognostic factor after curative resection in stage II
      and III patients. The predictive power of the sialyl-Le(x) expression may be
      helpful to define subgroups of patients at high risk for whom preventive adjuvant
      therapy can be selectively applied before the occurrence of detectable
      metastases.
CI  - Copyright 2000 Wiley-Liss, Inc.
FAU - Grabowski, P
AU  - Grabowski P
AD  - Department of Gastroenterology, Universitatsklinikum Benjamin Franklin, Freie
      Universitat Berlin, Berlin, Germany.
FAU - Mann, B
AU  - Mann B
FAU - Mansmann, U
AU  - Mansmann U
FAU - Lovin, N
AU  - Lovin N
FAU - Foss, H D
AU  - Foss HD
FAU - Berger, G
AU  - Berger G
FAU - Scherubl, H
AU  - Scherubl H
FAU - Riecken, E O
AU  - Riecken EO
FAU - Buhr, H J
AU  - Buhr HJ
FAU - Hanski, C
AU  - Hanski C
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Int J Cancer
JT  - International journal of cancer
JID - 0042124
RN  - 0
      (5-acetylneuraminyl-(2-3)-galactosyl-(1-4)-(fucopyranosyl-(1-3))-N-acetylglucosam
      ine)
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Lewis Blood-Group System)
RN  - 0 (Oligosaccharides)
SB  - IM
MH  - Adult
MH  - Aged
MH  - Aged, 80 and over
MH  - Antibodies, Monoclonal
MH  - Colorectal Neoplasms/mortality/*pathology/surgery
MH  - Disease-Free Survival
MH  - Female
MH  - Follow-Up Studies
MH  - Humans
MH  - Immunohistochemistry
MH  - Lewis Blood-Group System/analysis
MH  - Male
MH  - Middle Aged
MH  - Neoplasm Staging
MH  - Oligosaccharides/*analysis
MH  - Predictive Value of Tests
MH  - Prognosis
MH  - Retrospective Studies
MH  - Survival Rate
MH  - Time Factors
EDAT- 2000/09/27 11:00
MHDA- 2001/02/28 10:01
CRDT- 2000/09/27 11:00
PHST- 2000/09/27 11:00 [pubmed]
PHST- 2001/02/28 10:01 [medline]
PHST- 2000/09/27 11:00 [entrez]
AID - 10.1002/1097-0215(20001015)88:2<281::AID-IJC21>3.0.CO;2-2 [pii]
PST - ppublish
SO  - Int J Cancer. 2000 Oct 15;88(2):281-6.

PMID- 12954105
OWN - NLM
STAT- MEDLINE
DCOM- 20040420
LR  - 20081121
IS  - 1536-8599 (Print)
IS  - 1536-8599 (Linking)
VI  - 22
IP  - 3
DP  - 2003 Jun
TI  - Monoclonal antibodies against blood group A secretors and nonsecretors saliva.
PG  - 183-6
AB  - To obtain monoclonal antibodies (MAbs) that distinguish secretor and nonsecretor 
      from their saliva in forensic casework, two (K7405 and K7422) and one (K7516)
      MAbs reacting to blood group A antigen were produced by immunization of mice with
      salivary mucin obtained from blood group A secretors and nonsecretors,
      respectively. K7405, produced by immunization with salivary mucin obtained from A
      secretor, reacted with the A substances bound to the carrier protein but not with
      the A substance separated from the carrier protein. On the other hand, the K7422 
      and K7516 were reactive to the A substance separated from carrier protein. From
      these results, we conclude that K7405 recognizes the A substances clustered on
      the carrier protein and K7422 and K7516 recognize the isolated A substance. In
      the forensic blood typing of body fluids, A secretors and A nonsecretors can be
      clearly discriminated by the combined application of two MAbs (K7405 and K7516), 
      which react differently against saliva samples.
FAU - Ohmori, Takeshi
AU  - Ohmori T
AD  - National Research Institute of Police Science, 6-3-1, Kashiwanoba, Kashiwa,
      Chiba, 277-0882, Japan. ohmori@nrips.go.jp
FAU - Iwanari, Hiroko
AU  - Iwanari H
FAU - Aoi, Rie
AU  - Aoi R
FAU - Shiraishi, Tomoko
AU  - Shiraishi T
FAU - Ito, Yukio
AU  - Ito Y
FAU - Sato, Hajime
AU  - Sato H
LA  - eng
PT  - Journal Article
PL  - United States
TA  - Hybrid Hybridomics
JT  - Hybridoma and hybridomics
JID - 101131136
RN  - 0 (ABO Blood-Group System)
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Epitopes)
RN  - 0 (Mucins)
RN  - 0 (Oligosaccharides)
RN  - 0 (Salivary Proteins and Peptides)
SB  - IM
MH  - *ABO Blood-Group System
MH  - Animals
MH  - Antibodies, Monoclonal/*chemistry
MH  - Enzyme-Linked Immunosorbent Assay
MH  - Epitopes/chemistry
MH  - Mice
MH  - Mice, Inbred BALB C
MH  - Mucins/chemistry
MH  - Oligosaccharides/chemistry
MH  - Saliva/*chemistry
MH  - Salivary Proteins and Peptides/chemistry
EDAT- 2003/09/05 05:00
MHDA- 2004/04/21 05:00
CRDT- 2003/09/05 05:00
PHST- 2003/09/05 05:00 [pubmed]
PHST- 2004/04/21 05:00 [medline]
PHST- 2003/09/05 05:00 [entrez]
AID - 10.1089/153685903322286610 [doi]
PST - ppublish
SO  - Hybrid Hybridomics. 2003 Jun;22(3):183-6. doi: 10.1089/153685903322286610.

PMID- 18474217
OWN - NLM
STAT- MEDLINE
DCOM- 20080620
LR  - 20121115
IS  - 1090-2104 (Electronic)
IS  - 0006-291X (Linking)
VI  - 372
IP  - 1
DP  - 2008 Jul 18
TI  - Down-modulation of B cell signal transduction by ligation of mucins to CD22.
PG  - 45-50
LID - 10.1016/j.bbrc.2008.04.175 [doi]
AB  - Epithelial cancer cells secrete mucins carrying carbohydrate antigens such as a
      sialyl-Tn antigen into cancer tissues and/or the bloodstream, in which mucins may
      interact with CD22 (Siglec-2). Mucins isolated from colon cancer cells and bovine
      submaxillary mucins bound to CD22 cDNA transfectants and a human B cell line,
      Daudi cell, and the binding of soluble recombinant CD22 to the mucins was
      confirmed by means of a plate assay. The binding specificity was demonstrated by 
      the fact that the mucins bound to the recombinant CD22 with an intact ectodomain 
      but not to that with a mutated ectodomain. Daudi cells were stimulated with
      anti-IgM F(ab')(2) in the presence or absence of mucins. Ligation of mucins to
      CD22 decreased the phosphorylation of CD22 and SHP-1 recruitment, and the
      phosphorylation of ERK-1/2 prominently. The in vivo effect of mucins on splenic B
      cells in the tumor-bearing state was investigated using mucin-producing (TA3-Ha) 
      and non-producing (TA3-St) mammary adenocarcinoma-bearing mice. When
      fluorescence-labeled epiglycanins were administered to normal mice, a portion of 
      them was taken up by the spleen and became associated with splenic B cells. We
      found that splenic B cells were reduced in TA3-Ha-bearing mice but not in
      TA3-St-bearing ones. These results suggest that in the tumor-bearing state a
      portion of the mucins in the bloodstream was taken up by the spleen and ligated
      to CD22 expressed on splenic B cells, which may have led to down-regulation of
      signal transduction.
FAU - Toda, Munetoyo
AU  - Toda M
AD  - Department of Biotechnology, Faculty of Engineering, Kyoto Sangyo University,
      Kamigamo-Motoyama, Kita-ku, Kyoto 603-8555, Japan.
FAU - Akita, Kaoru
AU  - Akita K
FAU - Inoue, Mizue
AU  - Inoue M
FAU - Taketani, Shigeru
AU  - Taketani S
FAU - Nakada, Hiroshi
AU  - Nakada H
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20080512
PL  - United States
TA  - Biochem Biophys Res Commun
JT  - Biochemical and biophysical research communications
JID - 0372516
RN  - 0 (Immunoglobulin Fab Fragments)
RN  - 0 (Immunoglobulin M)
RN  - 0 (Mucins)
RN  - 0 (Receptors, Antigen, B-Cell)
RN  - 0 (Sialic Acid Binding Ig-like Lectin 2)
RN  - EC 2.7.11.24 (Mitogen-Activated Protein Kinase 1)
RN  - EC 2.7.11.24 (Mitogen-Activated Protein Kinase 3)
RN  - EC 3.1.3.48 (Protein Tyrosine Phosphatase, Non-Receptor Type 6)
SB  - IM
MH  - Animals
MH  - B-Lymphocytes/*immunology
MH  - Cattle
MH  - Cell Line, Tumor
MH  - Colonic Neoplasms/*immunology
MH  - Down-Regulation
MH  - Humans
MH  - Immune Tolerance
MH  - Immunoglobulin Fab Fragments/immunology
MH  - Immunoglobulin M/immunology
MH  - Mice
MH  - Mice, Inbred Strains
MH  - Mitogen-Activated Protein Kinase 1/metabolism
MH  - Mitogen-Activated Protein Kinase 3/metabolism
MH  - Mucins/*metabolism
MH  - Phosphorylation
MH  - Protein Tyrosine Phosphatase, Non-Receptor Type 6/metabolism
MH  - Receptors, Antigen, B-Cell/metabolism
MH  - Sialic Acid Binding Ig-like Lectin 2/genetics/*metabolism
MH  - *Signal Transduction
MH  - Spleen/immunology
EDAT- 2008/05/14 09:00
MHDA- 2008/06/21 09:00
CRDT- 2008/05/14 09:00
PHST- 2008/04/22 00:00 [received]
PHST- 2008/04/28 00:00 [accepted]
PHST- 2008/05/14 09:00 [pubmed]
PHST- 2008/06/21 09:00 [medline]
PHST- 2008/05/14 09:00 [entrez]
AID - S0006-291X(08)00849-8 [pii]
AID - 10.1016/j.bbrc.2008.04.175 [doi]
PST - ppublish
SO  - Biochem Biophys Res Commun. 2008 Jul 18;372(1):45-50. doi:
      10.1016/j.bbrc.2008.04.175. Epub 2008 May 12.

PMID- 3005335
OWN - NLM
STAT- MEDLINE
DCOM- 19860415
LR  - 20190508
IS  - 0021-9525 (Print)
IS  - 0021-9525 (Linking)
VI  - 102
IP  - 3
DP  - 1986 Mar
TI  - Disialogangliosides GD2 and GD3 are involved in the attachment of human melanoma 
      and neuroblastoma cells to extracellular matrix proteins.
PG  - 688-96
AB  - Human melanoma cells express relatively large amounts of the disialogangliosides 
      GD3 and GD2 on their surface whereas neuroblastoma cells express GD2 as a major
      ganglioside. Monoclonal antibodies (Mabs) directed specifically to the
      carbohydrate moiety of GD3 and GD2 inhibit melanoma and neuroblastoma cell
      attachment to various substrate adhesive proteins, e.g. collagen, vitronectin,
      laminin, fibronectin, and a heptapeptide,
      glycyl-L-arginyl-glycyl-L-aspartyl-L-seryl-L-prolyl-L-cysteine, which constitutes
      the cell attachment site of fibronectin. Cells that are preattached to a
      fibronectin substrate can also be induced to detach and round up in the presence 
      of purified anti-ganglioside Mab. Moreover, when melanoma cells that contain both
      GD2 and GD3 are incubated with Mabs directed to both of these molecules an
      additive inhibition is observed. The specificity of this inhibition is
      demonstrated since Mabs of various isotypes directed to either protein or
      carbohydrate epitopes on a number of other major melanoma or neuroblastoma cell
      surface antigens have no effect on cell attachment. A study of the kinetics
      involved in this inhibition indicates that significant effects occur during the
      first 5 min of cell attachment, suggesting an important role for GD2 and GD3 in
      the initial events of cell-substrate interactions. The role of gangliosides in
      cell attachment apparently does not directly involve a strong interaction with
      fibronectin since we could not observe any binding of radiolabeled fibronectin or
      fragments of the molecule known to contain the cell attachment site to melanoma
      gangliosides separated on thin-layer chromatograms. An alternative explanation
      would be that gangliosides may play a role in the electrostatic requirements for 
      cell-substrate interactions. In this regard, controlled periodate oxidation of
      terminal, unsubstituted sialic acid residues on the cell surface not only
      specifically destroys the antigenic epitopes on GD2 and GD3 recognized by
      specific Mabs but also inhibits melanoma cell and neuroblastoma cell attachment. 
      In fact, the periodate-induced ganglioside oxidation and the inhibition of cell
      attachment are equally dose dependent. These data suggest that cell-substratum
      interactions may depend in part on the electrostatic environment provided by
      terminal sialic acid residues of cell surface gangliosides and possibly other
      anionic glycoconjugates.
FAU - Cheresh, D A
AU  - Cheresh DA
FAU - Pierschbacher, M D
AU  - Pierschbacher MD
FAU - Herzig, M A
AU  - Herzig MA
FAU - Mujoo, K
AU  - Mujoo K
LA  - eng
GR  - CA 28420/CA/NCI NIH HHS/United States
GR  - CA 38352/CA/NCI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - J Cell Biol
JT  - The Journal of cell biology
JID - 0375356
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens, Surface)
RN  - 0 (Fibronectins)
RN  - 0 (Gangliosides)
RN  - 0 (Laminin)
RN  - 10450-60-9 (Periodic Acid)
RN  - 62010-37-1 (ganglioside, GD3)
RN  - 65988-71-8 (ganglioside, GD2)
RN  - B45A1BUM4Q (metaperiodate)
SB  - IM
MH  - Adenocarcinoma/metabolism
MH  - Antibodies, Monoclonal/immunology
MH  - Antigens, Surface/immunology
MH  - *Cell Adhesion
MH  - Cell Line
MH  - Extracellular Matrix/*metabolism
MH  - Fibronectins/metabolism
MH  - Gangliosides/immunology/*physiology
MH  - Humans
MH  - Laminin/metabolism
MH  - Lung Neoplasms/metabolism
MH  - Melanoma/*metabolism
MH  - Neuroblastoma/*metabolism
MH  - Periodic Acid/pharmacology
PMC - PMC2114134
EDAT- 1986/03/01 00:00
MHDA- 1986/03/01 00:01
CRDT- 1986/03/01 00:00
PHST- 1986/03/01 00:00 [pubmed]
PHST- 1986/03/01 00:01 [medline]
PHST- 1986/03/01 00:00 [entrez]
AID - 10.1083/jcb.102.3.688 [doi]
PST - ppublish
SO  - J Cell Biol. 1986 Mar;102(3):688-96. doi: 10.1083/jcb.102.3.688.

PMID- 1577766
OWN - NLM
STAT- MEDLINE
DCOM- 19920605
LR  - 20061115
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 267
IP  - 13
DP  - 1992 May 5
TI  - Occurrence of collagen and proteoglycan forms of type IX collagen in chick embryo
      cartilage. Production and characterization of a collagen form-specific antibody.
PG  - 9391-7
AB  - Type IX collagen from chick embryonic cartilage is a proteoglycan bearing a
      single chondroitin sulfate chain covalently linked to the alpha 2(IX) polypeptide
      chain. We have isolated type IX collagen metabolically labeled with [3H]proline
      using an antibody to type IX collagen and have found that the molecule is
      synthesized in two forms, a collagen form (COLIX) and a proteoglycan form (PGIX).
      In cultured chondrocytes, the two forms of type IX collagen showed a different
      ability to be deposited in the matrix. We have suggested the possibility that
      both forms may arise from an alternative substitution of a chondroitin sulfate
      chain to the NC3 domain of the alpha 2(IX) chain. Based on the reported amino
      acid sequence at the NC3 domain of alpha 2(IX), we have synthesized
      undecapeptides containing the sequence around the glycosaminoglycan attachment
      site of the alpha 2(IX) chain. Antibody against the peptide, which was raised in 
      rabbit, only recognized COLIX and made it possible to distinguish COLIX from
      PGIX. Evidence shows that this could be due to a difference in antigenicity of
      the NC3 domain of the alpha 2(IX) chain between COLIX and PGIX caused by the
      substitution of a chondroitin sulfate chain to the serine residue in this domain.
      Therefore, this antibody may be useful as a probe for studies on the functions of
      glycosaminoglycan substitution in type IX collagen.
FAU - Yada, T
AU  - Yada T
AD  - Institute for Molecular Science of Medicine, Aichi Medical University, Japan.
FAU - Arai, M
AU  - Arai M
FAU - Suzuki, S
AU  - Suzuki S
FAU - Kimata, K
AU  - Kimata K
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Proteoglycans)
RN  - 9007-34-5 (Collagen)
RN  - EC 4.2.2.- (Chondroitin Lyases)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Blotting, Western
MH  - Cartilage/cytology/*metabolism
MH  - Cells, Cultured
MH  - Chick Embryo
MH  - Chondroitin Lyases/metabolism
MH  - Chromatography, Liquid
MH  - Collagen/*metabolism
MH  - Electrophoresis, Polyacrylamide Gel
MH  - Enzyme-Linked Immunosorbent Assay
MH  - Molecular Sequence Data
MH  - Precipitin Tests
MH  - Protein Processing, Post-Translational
MH  - Proteoglycans/*metabolism
EDAT- 1992/05/05 00:00
MHDA- 1992/05/05 00:01
CRDT- 1992/05/05 00:00
PHST- 1992/05/05 00:00 [pubmed]
PHST- 1992/05/05 00:01 [medline]
PHST- 1992/05/05 00:00 [entrez]
PST - ppublish
SO  - J Biol Chem. 1992 May 5;267(13):9391-7.

PMID- 9565568
OWN - NLM
STAT- MEDLINE
DCOM- 19980605
LR  - 20190508
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 273
IP  - 19
DP  - 1998 May 8
TI  - Simultaneous expression of type 1 and type 2 Lewis blood group antigens by
      Helicobacter pylori lipopolysaccharides. Molecular mimicry between h. pylori
      lipopolysaccharides and human gastric epithelial cell surface glycoforms.
PG  - 11533-43
AB  - Previous structural investigations performed on the lipopolysaccharides (LPSs)
      from the human gastric pathogen Helicobacter pylori have revealed that these cell
      surface glycan molecules express type 2 partially fucosylated, glucosylated, or
      galactosylated N-acetyllactosamine O antigen chains (O-chains) of various
      lengths, which may or may not be terminated at the nonreducing end by Lewis X
      (Lex) and/or Ley blood group epitopes in mimicry of human cell surface
      glycoconjugates and glycolipids. Subsequently, serological experiments with
      commercially available Lewis-specific monoclonal antibodies also have recognized 
      the presence of Lex and Ley blood group antigens in H. pylori but, in addition,
      have indicated the presence of type 1 chain Lea, Leb, and Led (H-type 1) blood
      group epitopes in some H. pylori strains. To confirm their presence, structural
      studies and additional serological experiments were undertaken on H. pylori
      strains suspected of carrying type 1 chain epitopes. These investigations
      revealed that the O-chain region of H. pylori strain UA948 carried both Lea (type
      1) and Lex (type 2) blood group determinants. The O-chain from H. pylori UA955
      LPS expressed the terminal Lewis disaccharide (type 1 chain) and Lex and Ley
      antigens (type 2). The O-chain of H. pylori J223 LPS carried the type 1 chain
      precursor Lec, the H-1 epitope (Led, type 1 chain) and an elongated
      nonfucosylated type 2 N-acetyllactosamine chain (i antigen). Thus, O-chains from 
      H. pylori LPSs can also express fucosylated type 1 sequences, and the LPS from a 
      single H. pylori strain may carry O-chains with type 1 and 2 Lewis blood groups
      simultaneously. That monoclonal antibodies putatively specific for the Leb
      determinant can detect glycan substructures (Le disaccharide, Lec, and Led) of
      Leb indicates their nonspecificity. The expression of both type 1 and 2 Lewis
      antigens by H. pylori LPSs mimics the cell surface glycomolecules present in both
      the gastric superficial (which expresses mainly type 1 determinants) and the
      superficial and glandular epithelium regions (both of which express predominantly
      type 2 determinants). Therefore, each H. pylori strain may have a different niche
      within the gastric mucosa, and each individual LPS blood group antigen may have a
      dissimilar role in H. pylori adaptation.
FAU - Monteiro, M A
AU  - Monteiro MA
AD  - Canadian Bacterial Diseases Network, National Research Council, Ottawa, K1A 0R6
      Ontario, Canada. Mario.Monteiro@nrc.ca
FAU - Chan, K H
AU  - Chan KH
FAU - Rasko, D A
AU  - Rasko DA
FAU - Taylor, D E
AU  - Taylor DE
FAU - Zheng, P Y
AU  - Zheng PY
FAU - Appelmelk, B J
AU  - Appelmelk BJ
FAU - Wirth, H P
AU  - Wirth HP
FAU - Yang, M
AU  - Yang M
FAU - Blaser, M J
AU  - Blaser MJ
FAU - Hynes, S O
AU  - Hynes SO
FAU - Moran, A P
AU  - Moran AP
FAU - Perry, M B
AU  - Perry MB
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, Non-P.H.S.
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Lewis Blood-Group System)
RN  - 0 (Lipopolysaccharides)
SB  - IM
MH  - Carbohydrate Sequence
MH  - Chromatography, Gas
MH  - Epithelial Cells/immunology
MH  - Gastric Mucosa/*immunology
MH  - Helicobacter pylori/chemistry/*immunology
MH  - Humans
MH  - Lewis Blood-Group System/*immunology
MH  - Lipopolysaccharides/chemistry/*immunology
MH  - Mass Spectrometry
MH  - *Molecular Mimicry
MH  - Molecular Sequence Data
EDAT- 1998/06/13 00:00
MHDA- 1998/06/13 00:01
CRDT- 1998/06/13 00:00
PHST- 1998/06/13 00:00 [pubmed]
PHST- 1998/06/13 00:01 [medline]
PHST- 1998/06/13 00:00 [entrez]
AID - 10.1074/jbc.273.19.11533 [doi]
PST - ppublish
SO  - J Biol Chem. 1998 May 8;273(19):11533-43. doi: 10.1074/jbc.273.19.11533.

PMID- 6830241
OWN - NLM
STAT- MEDLINE
DCOM- 19830415
LR  - 20171116
IS  - 0003-9861 (Print)
IS  - 0003-9861 (Linking)
VI  - 220
IP  - 1
DP  - 1983 Jan
TI  - Many monoclonal antibodies with an apparent specificity for certain lung cancers 
      are directed against a sugar sequence found in lacto-N-fucopentaose III.
PG  - 318-20
FAU - Huang, L C
AU  - Huang LC
FAU - Brockhaus, M
AU  - Brockhaus M
FAU - Magnani, J L
AU  - Magnani JL
FAU - Cuttitta, F
AU  - Cuttitta F
FAU - Rosen, S
AU  - Rosen S
FAU - Minna, J D
AU  - Minna JD
FAU - Ginsburg, V
AU  - Ginsburg V
LA  - eng
GR  - 1 KOA-AM-00212/AM/NIADDK NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Arch Biochem Biophys
JT  - Archives of biochemistry and biophysics
JID - 0372430
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antibodies, Neoplasm)
RN  - 0 (Cerebrosides)
RN  - 0 (Lewis X Antigen)
RN  - 0 (Oligosaccharides)
RN  - 0 (lacto-N-fucopentaosyl(III)ceramide)
SB  - IM
MH  - Antibodies, Monoclonal/*physiology
MH  - Antibodies, Neoplasm/physiology
MH  - Antibody Specificity
MH  - Carbohydrate Sequence
MH  - Cerebrosides/*immunology
MH  - Humans
MH  - Lewis X Antigen/*immunology
MH  - Lung Neoplasms/*immunology
MH  - Oligosaccharides/*immunology
EDAT- 1983/01/01 00:00
MHDA- 1983/01/01 00:01
CRDT- 1983/01/01 00:00
PHST- 1983/01/01 00:00 [pubmed]
PHST- 1983/01/01 00:01 [medline]
PHST- 1983/01/01 00:00 [entrez]
AID - 0003-9861(83)90417-4 [pii]
PST - ppublish
SO  - Arch Biochem Biophys. 1983 Jan;220(1):318-20.

PMID- 11028065
OWN - NLM
STAT- Publisher
LR  - 20001011
IS  - 1521-3773 (Electronic)
IS  - 1433-7851 (Linking)
VI  - 39
IP  - 18
DP  - 2000 Sep 15
TI  - Calcium-Dependent Carbohydrate-Carbohydrate Recognition between Lewis(X) Blood
      Group Antigens This research was supported by the Deutsche Forschungsgemeinschaft
      and the Fonds der Chemischen Industrie.
PG  - 3245-3249
FAU - Geyer
AU  - Geyer A
AD  - Fachbereich Chemie M716 der Universitat Konstanz 78457 Konstanz (Germany).
FAU - Gege
AU  - Gege C
FAU - Schmidt
AU  - Schmidt RR
LA  - eng
PT  - Journal Article
PL  - Germany
TA  - Angew Chem Int Ed Engl
JT  - Angewandte Chemie (International ed. in English)
JID - 0370543
EDAT- 2000/10/12 00:00
MHDA- 2000/10/12 00:00
CRDT- 2000/10/12 00:00
PHST- 2000/10/12 00:00 [pubmed]
PHST- 2000/10/12 00:00 [medline]
PHST- 2000/10/12 00:00 [entrez]
AID - 10.1002/1521-3773(20000915)39:18<3245::AID-ANIE3245>3.0.CO;2-9 [pii]
PST - ppublish
SO  - Angew Chem Int Ed Engl. 2000 Sep 15;39(18):3245-3249.

PMID- 11550228
OWN - NLM
STAT- MEDLINE
DCOM- 20011204
LR  - 20151119
IS  - 0360-4012 (Print)
IS  - 0360-4012 (Linking)
VI  - 65
IP  - 6
DP  - 2001 Sep 15
TI  - Developmental expression of a unique carbohydrate antigen, Tn antigen, in mouse
      central nervous tissues.
PG  - 595-603
AB  - Using an anti-Tn monoclonal antibody, the Tn antigen was detected
      immunohistochemically in prenatal and early postnatal central nervous tissues. On
      embryonic day 9 (E9), the antigen was distributed throughout the single
      neuroepithelial layer in the neocortex and then became more prominent in the
      preplate than in the ventricular zone along with formation of the preplate.
      Following division of the preplate and concomitant formation of the cortical
      plate, distinct labeling of the neocortex occurred in the marginal, subplate and 
      intermediate zones, whereas in the cortical plate and ventricular zone were
      virtually not immunostained. It is notable that thalamocortical afferent fibers
      were also immunostained specifically on E14. After birth, the localization of the
      antigen became less noticeable and by 3 weeks after birth, the antigen had
      substantially disappeared. In the developing cerebellum, prominent labeling was
      also observed in the molecular layer and outskirts of the cerebellar nuclei on
      early postnatal days. To characterize the glycoprotein bearing the Tn antigen
      biochemically, immunoblot analysis was performed. The glycoprotein, most of which
      was extracted with a salt solution, migrated as a broad smeared band
      corresponding to a molecular weight of about 250 kDa on SDS-PAGE. Among the
      various tissues examined, this glycoprotein was only detected in the brain and
      its amount increased until an early postnatal stage with a peak on postnatal day 
      3 (P3), and then decreased gradually with age. This spatially and developmentally
      regulated expression of the Tn antigen suggests that this antigen plays a
      significant role in brain development.
CI  - Copyright 2001 Wiley-Liss, Inc.
FAU - Akita, K
AU  - Akita K
AD  - Department of Biotechnology, Faculty of Engineering, Kyoto Sangyo University,
      Kyoto, Japan.
FAU - Fushiki, S
AU  - Fushiki S
FAU - Fujimoto, T
AU  - Fujimoto T
FAU - Inoue, M
AU  - Inoue M
FAU - Oguri, K
AU  - Oguri K
FAU - Okayama, M
AU  - Okayama M
FAU - Yamashina, I
AU  - Yamashina I
FAU - Nakada, H
AU  - Nakada H
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - J Neurosci Res
JT  - Journal of neuroscience research
JID - 7600111
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Glycoproteins)
RN  - 0 (Lectins)
RN  - 0 (Tn antigen)
SB  - IM
MH  - Afferent Pathways/embryology/growth & development/metabolism
MH  - Aging/immunology
MH  - Animals
MH  - Animals, Newborn
MH  - Antibody Specificity/physiology
MH  - Antigens, Tumor-Associated, Carbohydrate/immunology/*metabolism
MH  - Axons/metabolism
MH  - Central Nervous System/embryology/growth & development/*metabolism
MH  - Cerebellum/embryology/growth & development/metabolism
MH  - Cerebral Cortex/embryology/growth & development/metabolism
MH  - Fetus
MH  - Glycoproteins/immunology/*metabolism
MH  - Immunoblotting
MH  - Immunohistochemistry
MH  - Lectins/immunology
MH  - Mice
MH  - Mice, Inbred ICR
MH  - Neurons/cytology/*metabolism
MH  - Spinal Cord/embryology/growth & development/metabolism
MH  - Thalamus/embryology/growth & development/metabolism
EDAT- 2001/09/11 10:00
MHDA- 2002/01/05 10:01
CRDT- 2001/09/11 10:00
PHST- 2001/09/11 10:00 [pubmed]
PHST- 2002/01/05 10:01 [medline]
PHST- 2001/09/11 10:00 [entrez]
AID - 10.1002/jnr.1190 [pii]
AID - 10.1002/jnr.1190 [doi]
PST - ppublish
SO  - J Neurosci Res. 2001 Sep 15;65(6):595-603. doi: 10.1002/jnr.1190.

PMID- 14685826
OWN - NLM
STAT- MEDLINE
DCOM- 20040324
LR  - 20061115
IS  - 1434-5161 (Print)
IS  - 1434-5161 (Linking)
VI  - 49
IP  - 1
DP  - 2004
TI  - Structural and immunocytochemical studies on alpha-N-acetylgalactosaminidase
      deficiency (Schindler/Kanzaki disease).
PG  - 1-8
AB  - Alpha-N-acetylgalactosaminidase (alpha-NAGA) deficiency (Schindler/Kanzaki
      disease) is a clinically and pathologically heterogeneous genetic disease with a 
      wide spectrum including an early onset neuroaxonal dystrophy (Schindler disease) 
      and late onset angiokeratoma corporis diffusum (Kanzaki disease). In alpha-NAGA
      deficiency, there are discrepancies between the genotype and phenotype, and also 
      between urinary excretion products (sialyl glycoconjugates) and a theoretical
      accumulated material (Tn-antigen; Gal NAcalpha1-O-Ser/Thr) resulting from a
      defect in alpha-NAGA. As for the former issue, previously reported genetic,
      biochemical and pathological data raise the question whether or not E325K
      mutation found in Schindler disease patients really leads to the severe phenotype
      of alpha-NAGA deficiency. The latter issue leads to the question of whether
      alpha-NAGA deficiency is associated with the basic pathogenesis of this disease. 
      To clarify the pathogenesis of this disease, we performed structural and
      immunocytochemical studies. The structure of human alpha-NAGA deduced on homology
      modeling is composed of two domains, domain I, including the active site, and
      domain II. R329W/Q, identified in patients with Kanzaki disease have been deduced
      to cause drastic changes at the interface between domains I and II. The
      structural change caused by E325K found in patients with Schindler disease is
      localized on the N-terminal side of the tenth beta-strand in domain II and is
      smaller than those caused by R329W/Q. Immunocytochemical analysis revealed that
      the main lysosomal accumulated material in cultured fibroblasts from patients
      with Kanzaki disease is Tn-antigen. These data suggest that a prototype of
      alpha-NAGA deficiency in Kanzaki disease and factors other than the defect of
      alpha-NAGA may contribute to severe neurological disorders, and Kanzaki disease
      is thought to be caused by a single enzyme deficiency.
FAU - Sakuraba, Hitoshi
AU  - Sakuraba H
AD  - Department of Clinical Genetics, The Tokyo Metropolitan Institute of Medical
      Science, Tokyo Metropolitan Organization for Medical Research, 3-18-22
      Honkomagome, Bunkyo-ku, Tokyo 113-8613, Japan. sakuraba@rinshoken.or.jp
FAU - Matsuzawa, Fumiko
AU  - Matsuzawa F
FAU - Aikawa, Sei-ichi
AU  - Aikawa S
FAU - Doi, Hirofumi
AU  - Doi H
FAU - Kotani, Masaharu
AU  - Kotani M
FAU - Nakada, Hiroshi
AU  - Nakada H
FAU - Fukushige, Tomoko
AU  - Fukushige T
FAU - Kanzaki, Tamotsu
AU  - Kanzaki T
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20031219
PL  - England
TA  - J Hum Genet
JT  - Journal of human genetics
JID - 9808008
RN  - 0 (Antigens, CD)
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Lysosome-Associated Membrane Glycoproteins)
RN  - 0 (Tn antigen)
RN  - EC 3.2.1.- (Hexosaminidases)
RN  - EC 3.2.1.49 (NAGA protein, human)
RN  - EC 3.2.1.49 (alpha-N-Acetylgalactosaminidase)
SB  - IM
MH  - Antigens, CD/metabolism
MH  - Antigens, Tumor-Associated, Carbohydrate/metabolism
MH  - Crystallography
MH  - Fabry Disease/enzymology/*genetics
MH  - Fibroblasts/metabolism
MH  - Hexosaminidases/*deficiency/genetics/metabolism
MH  - Humans
MH  - Immunohistochemistry
MH  - Lysosome-Associated Membrane Glycoproteins
MH  - Models, Molecular
MH  - Neuroaxonal Dystrophies/*genetics
MH  - Protein Structure, Tertiary/genetics
MH  - Structural Homology, Protein
MH  - alpha-N-Acetylgalactosaminidase
EDAT- 2003/12/20 05:00
MHDA- 2004/03/25 05:00
CRDT- 2003/12/20 05:00
PHST- 2003/07/29 00:00 [received]
PHST- 2003/09/30 00:00 [accepted]
PHST- 2003/12/20 05:00 [pubmed]
PHST- 2004/03/25 05:00 [medline]
PHST- 2003/12/20 05:00 [entrez]
AID - 10.1007/s10038-003-0098-z [doi]
PST - ppublish
SO  - J Hum Genet. 2004;49(1):1-8. doi: 10.1007/s10038-003-0098-z. Epub 2003 Dec 19.

PMID- 3100030
OWN - NLM
STAT- MEDLINE
DCOM- 19870319
LR  - 20071114
IS  - 0008-5472 (Print)
IS  - 0008-5472 (Linking)
VI  - 47
IP  - 4
DP  - 1987 Feb 15
TI  - Disialoganglioside GD2 on human neuroblastoma cells: target antigen for
      monoclonal antibody-mediated cytolysis and suppression of tumor growth.
PG  - 1098-104
AB  - A murine monoclonal antibody 14.18 specifically recognizes disialoganglioside
      GD2, the major ganglioside expressed on the surface of human neuroblastoma cells.
      This monoclonal antibody (Mab) is of immunoglobulin G3 isotype, has an affinity
      constant (KA) of 3.5 X 10(8) M-1, and reacts preferentially with tumor cells and 
      fresh frozen tumor tissues of neuroectodermal origin in enzyme-linked
      immunosorbent assay and immunoperoxidase assays, respectively. Mab 14.18
      effectively lyses a number of human neuroblastoma cell lines by two distinct
      mechanisms, i.e., antibody-dependent cellular cytotoxicity and
      complement-dependent cytotoxicity. There is a good correlation between the
      average number of antibody-binding sites per neuroblastoma cell and the amount of
      cell lysis observed in complement-dependent cytotoxicity and antibody-dependent
      cellular cytotoxicity. In addition, Mab 14.18 suppresses establishment as well as
      growth of progressively growing, established human neuroblastoma tumors in nude
      mice when injected 24 h and 9 days, respectively, after the initial s.c.
      inoculation of tumor cells. These data suggest that Mab 14.18 can mediate tumor
      cell killing in vivo and in vitro and may thereby prove useful for immunotherapy 
      of human neuroblastoma.
FAU - Mujoo, K
AU  - Mujoo K
FAU - Cheresh, D A
AU  - Cheresh DA
FAU - Yang, H M
AU  - Yang HM
FAU - Reisfeld, R A
AU  - Reisfeld RA
LA  - eng
GR  - CA 42508/CA/NCI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Cancer Res
JT  - Cancer research
JID - 2984705R
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Gangliosides)
SB  - IM
MH  - Antibodies, Monoclonal/*therapeutic use
MH  - Cell Line
MH  - Enzyme-Linked Immunosorbent Assay
MH  - Flow Cytometry
MH  - Gangliosides/*immunology
MH  - Humans
MH  - Immunoenzyme Techniques
MH  - *Immunotherapy
MH  - Mathematics
MH  - Neuroblastoma/*therapy
EDAT- 1987/02/15 00:00
MHDA- 1987/02/15 00:01
CRDT- 1987/02/15 00:00
PHST- 1987/02/15 00:00 [pubmed]
PHST- 1987/02/15 00:01 [medline]
PHST- 1987/02/15 00:00 [entrez]
PST - ppublish
SO  - Cancer Res. 1987 Feb 15;47(4):1098-104.

PMID- 10542057
OWN - NLM
STAT- MEDLINE
DCOM- 20000110
LR  - 20171116
IS  - 0014-2956 (Print)
IS  - 0014-2956 (Linking)
VI  - 266
IP  - 1
DP  - 1999 Nov
TI  - Structural studies on lipopolysaccharides of serologically non-typable strains of
      Helicobacter pylori, AF1 and 007, expressing Lewis antigenic determinants.
PG  - 123-31
AB  - In contrast to other Helicobacter pylori strains, which have serologically
      detectable Lewis(x)+ (Le(x)) and Lewis(y)++ (++Le(y)) antigenic determinants in
      the O-specific polysaccharide chains of the lipopolysaccharides, H. pylori AF1
      and 007 were non-typable with anti-Le(x) and anti-Le(y) antibodies. The
      carbohydrate portions of the lipopolysaccharides were liberated by mild acid
      hydrolysis and subsequently studied by sugar and methylation analyses, 1H-NMR
      spectroscopy and electrospray ionization-mass spectrometry. Compared with each
      other, and with lipopolysaccharides of strains studied previously, the
      lipopolysaccharides of both AF1 and 007 showed similarities, but also
      differences, in the structures of the core region and O-specific polysaccharide
      chains. The O-specific polysaccharide chains of both strains consisted of a short
      or long polyfucosylated poly-N-acetyl-beta-lactosamine chains, which were
      distinguished from those of other strains by a high degree of fucosylation
      producing a polymeric Le(x)chain terminating with Le(x) or Le(y) units:[sequence:
      see text] where n = 0 or 1 in strain AF1 and 0 in strain 007, m = 0-2, 6-7 in
      strain AF1 and m = 0-2, 6-7 or approximately 40 in strain 007, the medium-size
      species being predominant. Therefore, compared with other strains, the lack of
      reactivity of lipopolysaccharide of H. pylori AF1 and 007 with anti-Le(x) and
      anti-Le(y) may reflect the presence of a polymeric Le(x) chain and has important 
      implications for serological and pathogenesis studies. As the substitution
      pattern of a D-glycero-D-manno-heptose residue in the outer core varied in the
      two strains, and an extended DD-heptan chain was present in some
      lipopolysaccharide species but not in others, this region was less conservative
      than the inner core region. The inner core L-glycero-D-manno-heptose region of
      both strains carried a 2-aminoethyl phosphate group, rather than a phosphate
      group, as reported previously for other H. pylori strains.
FAU - Knirel, Y A
AU  - Knirel YA
AD  - Karolinska Institute, Clinical Research Center, Huddinge University Hospital,
      Sweden.
FAU - Kocharova, N A
AU  - Kocharova NA
FAU - Hynes, S O
AU  - Hynes SO
FAU - Widmalm, G
AU  - Widmalm G
FAU - Andersen, L P
AU  - Andersen LP
FAU - Jansson, P E
AU  - Jansson PE
FAU - Moran, A P
AU  - Moran AP
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - Eur J Biochem
JT  - European journal of biochemistry
JID - 0107600
RN  - 0 (Antigens, Bacterial)
RN  - 0 (Carbohydrates)
RN  - 0 (Lewis Blood-Group System)
RN  - 0 (Lewis X Antigen)
RN  - 0 (Lewis Y antigen)
RN  - 0 (Lipopolysaccharides)
RN  - 0 (Oligosaccharides)
SB  - IM
MH  - Antigens, Bacterial/*chemistry/immunology
MH  - Carbohydrate Conformation
MH  - Carbohydrate Sequence
MH  - Carbohydrates/chemistry
MH  - Helicobacter pylori/*chemistry/classification/immunology
MH  - Lewis Blood-Group System/*analysis
MH  - Lewis X Antigen/*analysis
MH  - Lipopolysaccharides/*chemistry/immunology
MH  - Magnetic Resonance Spectroscopy
MH  - Mass Spectrometry
MH  - Molecular Sequence Data
MH  - Oligosaccharides/*chemistry/isolation & purification
MH  - Serotyping
EDAT- 1999/10/29 00:00
MHDA- 1999/10/29 00:01
CRDT- 1999/10/29 00:00
PHST- 1999/10/29 00:00 [pubmed]
PHST- 1999/10/29 00:01 [medline]
PHST- 1999/10/29 00:00 [entrez]
AID - ejb831 [pii]
PST - ppublish
SO  - Eur J Biochem. 1999 Nov;266(1):123-31.

PMID- 7720892
OWN - NLM
STAT- MEDLINE
DCOM- 19950525
LR  - 20180605
IS  - 0748-7983 (Print)
IS  - 0748-7983 (Linking)
VI  - 21
IP  - 2
DP  - 1995 Apr
TI  - Immunohistochemical expression of sialyl Tn and sialyl Lewis(a) antigens in
      stromal tissue correlates with peritoneal dissemination in stage IV human gastric
      cancer.
PG  - 168-75
AB  - Immunohistochemical expression of sialyl Tn antigen (TKH2 and B72.3), sialyl
      Lewis(a) antigen (CA19-9) and CEA was examined in 52 cases with Stage IV gastric 
      cancer, the objective being to examine whether or not these tumour-associated
      antigens show different expression between peritoneal dissemination and liver
      metastasis. Stromal type for TKH2, B72.3, CA19-9 and CEA were seen in 14 (50%),
      13 (46%), 18 (64%) and nine (32%) cases with peritoneal dissemination,
      respectively, and in four (17%), three (13%), four (17%) and four (17%) cases
      with liver metastasis, respectively. The stromal type correlated to peritoneal
      dissemination in TKH2 (P < 0.05) B72.3 (P < 0.05) and CA19-9 (P < 0.05). In other
      clinicopathological factors, the stromal type for TKH2, B72.3 and CA19-9
      correlated to the undifferentiated type. However, even in the undifferentiated
      type group, the stromal type correlated to peritoneal dissemination in TKH2 (P < 
      0.05), B72.3 (P < 0.05) and CA19-9 (P < 0.05). Based on these results, the spread
      of sialyl-rich tumour-associated antigens into the surrounding stroma in the
      undifferentiated type of gastric cancer may be associated with peritoneal
      dissemination.
FAU - Ikeda, Y
AU  - Ikeda Y
AD  - Second Department of Surgery, Faculty of Medicine, Kyushu University, Fukuoka,
      Japan.
FAU - Mori, M
AU  - Mori M
FAU - Kamakura, T
AU  - Kamakura T
FAU - Saku, M
AU  - Saku M
FAU - Sugimachi, K
AU  - Sugimachi K
LA  - eng
PT  - Comparative Study
PT  - Journal Article
PL  - England
TA  - Eur J Surg Oncol
JT  - European journal of surgical oncology : the journal of the European Society of
      Surgical Oncology and the British Association of Surgical Oncology
JID - 8504356
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Biomarkers, Tumor)
RN  - 0 (CA-19-9 Antigen)
RN  - 0 (Carcinoembryonic Antigen)
RN  - 0 (sialosyl-Tn antigen)
SB  - IM
MH  - Antibodies, Monoclonal
MH  - Antigens, Tumor-Associated, Carbohydrate/*analysis
MH  - Biomarkers, Tumor/*analysis
MH  - CA-19-9 Antigen/*analysis
MH  - Carcinoembryonic Antigen/analysis
MH  - Humans
MH  - Immunoenzyme Techniques
MH  - Japan
MH  - Liver Neoplasms/*immunology/secondary
MH  - Neoplasm Staging
MH  - Peritoneal Neoplasms/*immunology/secondary
MH  - Stomach Neoplasms/*immunology/pathology
EDAT- 1995/04/01 00:00
MHDA- 1995/04/01 00:01
CRDT- 1995/04/01 00:00
PHST- 1995/04/01 00:00 [pubmed]
PHST- 1995/04/01 00:01 [medline]
PHST- 1995/04/01 00:00 [entrez]
AID - S0748-7983(95)90369-0 [pii]
PST - ppublish
SO  - Eur J Surg Oncol. 1995 Apr;21(2):168-75.

PMID- 11193738
OWN - NLM
STAT- MEDLINE
DCOM- 20010308
LR  - 20151119
IS  - 0941-1291 (Print)
IS  - 0941-1291 (Linking)
VI  - 30
IP  - 12
DP  - 2000
TI  - Lymph node metastasis-related carbohydrate epitopes of gastric cancer with
      submucosal invasion.
PG  - 1073-82
AB  - This study was conducted to examine the lymph node metastasis-related
      carbohydrate epitopes of cancer cells in primary lesions of gastric cancer with
      submucosal invasion (sm gastric cancer). A total of 118 formalin-fixed and
      paraffin-embedded surgical specimens were studied. Carbohydrate epitopes were
      detected histochemically using 17 kinds of biotin-labeled lectins and three kinds
      of monoclonal antibodies (mAbs) against Thomsen-Friedenreich antigen (HB-T1), Tn 
      (HB-Tn1), and sialyl Tn antigens (HB-STn1). The node-positive group showed
      significantly lower reactivities with Ricinus communis I (RCA-I), Lotus
      tetragonolobus (Lotus), Triticum vulgaris (WGA), and Concanavalia ensiformis
      (ConA), and higher reactivities with HB-STn1. When sm gastric cancer was
      classified into differentiated and undifferentiated types, lower reactivities
      with RCA-I and ConA were observed in the differentiated type cancers, whereas
      lower reactivities with Lotus, WGA, and higher reactivity with HB-STn1 were
      observed in the undifferentiated type cancers. Nodal status was able to be
      predicted with high precision by a combination of these carbohydrates and
      histological subtypes. Since neuraminidase treatment rarely changed the
      reactivity of cancer cells with these lectins, we conclude that the loss of
      certain kinds of carbohydrates that are restricted by histological subtypes is
      related to lymph node metastasis in sm gastric cancer.
FAU - Takano, Y
AU  - Takano Y
AD  - Department of Surgery, Southern Tohoku Research Institute of Neuroscience,
      Koriyama-shi, Fukushima, Japan.
FAU - Teranishi, Y
AU  - Teranishi Y
FAU - Terashima, S
AU  - Terashima S
FAU - Motoki, R
AU  - Motoki R
FAU - Kawaguchi, T
AU  - Kawaguchi T
LA  - eng
PT  - Journal Article
PL  - Japan
TA  - Surg Today
JT  - Surgery today
JID - 9204360
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Carbohydrates)
RN  - 0 (Epitopes)
RN  - 0 (Lectins)
SB  - IM
MH  - Adult
MH  - Antibodies, Monoclonal
MH  - Carbohydrates/*analysis
MH  - Epitopes
MH  - Female
MH  - Humans
MH  - Lectins/analysis
MH  - *Lymphatic Metastasis
MH  - Male
MH  - Middle Aged
MH  - Neoplasm Invasiveness
MH  - Stomach Neoplasms/*pathology
EDAT- 2001/02/24 12:00
MHDA- 2001/03/10 10:01
CRDT- 2001/02/24 12:00
PHST- 2001/02/24 12:00 [pubmed]
PHST- 2001/03/10 10:01 [medline]
PHST- 2001/02/24 12:00 [entrez]
AID - 10.1007/s005950070004 [pii]
AID - 10.1007/s005950070004 [doi]
PST - ppublish
SO  - Surg Today. 2000;30(12):1073-82. doi: 10.1007/s005950070004.

PMID- 14960498
OWN - NLM
STAT- MEDLINE
DCOM- 20040503
LR  - 20061115
IS  - 0006-8950 (Print)
IS  - 0006-8950 (Linking)
VI  - 127
IP  - Pt 3
DP  - 2004 Mar
TI  - Synthetic disialylgalactose immunoadsorbents deplete anti-GQ1b antibodies from
      autoimmune neuropathy sera.
PG  - 680-91
AB  - Acute and chronic autoimmune neuropathies, including Guillain-Barre syndromes
      (GBS) are often characterized by the presence of autoantibodies that react with
      neural gangliosides. Evidence from human and animal studies indicates that
      anti-ganglioside antibodies play a primary neuropathogenic role, and their rapid 
      elimination from the circulation through specific immunoadsorption therapy thus
      has the potential to ameliorate the course of the disease. Here we have tested
      this therapeutic principle in the Miller Fisher variant of GBS that is associated
      serologically with acute phase anti-GQ1b ganglioside immunoglobulin G (IgG)
      antibodies, and in chronic ataxic neuropathies associated with persistently
      elevated immunoglobulin M (IgM) antibodies that react with GQ1b, GD3 and other
      disialylated gangliosides. Human and mouse anti-GQ1b IgG and IgM antibodies may
      also react with GD3, suggesting the shared terminal disialoside epitope could be 
      involved in antibody binding. We thus synthesized the terminal trisaccharide,
      NeuAc(alpha2-8)NeuAc(alpha2-3)Gal common to GQ1b and GD3, and conjugated it to
      bovine serum albumin (BSA). This disialylgalactose glycoconjugate (DSG-BSA) binds
      anti-GQ1b antibodies in 32/58 (55%) human sera containing IgG or IgM anti-GQ1b
      antibodies at titres up to 1/130 000; it also binds a wide range of mouse
      monoclonal anti-GQ1b and -GD3 antibodies. When conjugated to Sepharose as mock
      therapeutic immmunoaffinity columns, the immobilized trisaccharide
      (DSG-Sepharose) eliminates anti-GQ1b antibodies from positive sera in proportion 
      to their level of binding to DSG-BSA. Oligosaccharide-specific immunoadsorption
      therapy thus provides a new therapeutic approach to anti-GQ1b antibody-associated
      syndromes that could be applied to clinical practice. Furthermore, modification
      of the immobilized oligosaccharide epitopes to incorporate other glycan
      structures may allow this approach to be adapted to other forms of autoimmune
      neuropathy associated with uniform anti-glycolipid antibody profiles.
FAU - Willison, Hugh J
AU  - Willison HJ
AD  - Clinical Neurosciences Division, University of Glasgow and Department of
      Neurology, Southern General Hospital, Glasgow, Scotland.
      h.j.willison@clinmed.gla.ac.uk
FAU - Townson, Kate
AU  - Townson K
FAU - Veitch, Jean
AU  - Veitch J
FAU - Boffey, Judith
AU  - Boffey J
FAU - Isaacs, Neil
AU  - Isaacs N
FAU - Andersen, Soren M
AU  - Andersen SM
FAU - Zhang, Ping
AU  - Zhang P
FAU - Ling, Chang-Chun
AU  - Ling CC
FAU - Bundle, David R
AU  - Bundle DR
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20040211
PL  - England
TA  - Brain
JT  - Brain : a journal of neurology
JID - 0372537
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Gangliosides)
RN  - 0 (Glycolipids)
RN  - 0 (Immunoglobulin G)
RN  - 0 (Immunoglobulin M)
RN  - 0 (Immunosorbents)
RN  - 62010-37-1 (ganglioside, GD3)
RN  - 68652-37-9 (GQ1b ganglioside)
SB  - AIM
SB  - IM
MH  - Animals
MH  - Antibodies, Monoclonal/immunology/isolation & purification
MH  - Antigen-Antibody Reactions
MH  - Gangliosides/*blood/immunology
MH  - Glycolipids/immunology
MH  - Guillain-Barre Syndrome/*immunology
MH  - Humans
MH  - Immunoglobulin G/immunology
MH  - Immunoglobulin M/immunology
MH  - Immunosorbent Techniques
MH  - Immunosorbents/*pharmacology
MH  - Mice
MH  - Mice, Inbred Strains
MH  - Mice, Knockout
EDAT- 2004/02/13 05:00
MHDA- 2004/05/05 05:00
CRDT- 2004/02/13 05:00
PHST- 2004/02/13 05:00 [pubmed]
PHST- 2004/05/05 05:00 [medline]
PHST- 2004/02/13 05:00 [entrez]
AID - 10.1093/brain/awh083 [doi]
AID - awh083 [pii]
PST - ppublish
SO  - Brain. 2004 Mar;127(Pt 3):680-91. doi: 10.1093/brain/awh083. Epub 2004 Feb 11.

PMID- 16776550
OWN - NLM
STAT- MEDLINE
DCOM- 20070531
LR  - 20070410
IS  - 0031-8655 (Print)
IS  - 0031-8655 (Linking)
VI  - 82
IP  - 5
DP  - 2006 Sep-Oct
TI  - Binding of T-antigen disaccharides to Artocarpus hirsuta lectin and jacalin are
      energetically different.
PG  - 1315-8
AB  - The thermodynamics of binding of Me-alpha(-GalNAc, Gal-beta-1-3GalNAc-alpha-O-Me 
      (T-antigen-alpha), Gal-beta-1-3GalNAc and Gal-alpha-1-6Glc (mellibiose) to
      Artocarpus hirsuta lectin was studied using fluorescence spectroscopy. The
      binding affinities of the saccharides are in the order
      Gal-beta-1-3GalNAc-alpha-O-Me > Me-alpha-GalNAc > Me-alpha-Gal >
      Gal-beta-1-3GalNAc > Gal-alpha-1-6Glc. The binding affinities were comparable to 
      those for jacalin. However, binding of the saccharides to the A. hirsuta lectin
      was not affected as strongly by temperature as observed in jacalin and the trend 
      was found to be reversed. Values for AH and AS were found to be positive in A.
      hirsuta lectin-disaccharide binding despite similar binding affinities. Thus,
      with 99% structural and 96% sequence homology, with similar sugar specificity and
      affinity, the energetics of the disaccharide binding of the two lectins seem to
      be different. Me-alpha-GalNAc binding to A. hirsuta lectin is enthalpically
      driven, because the association constant decreases with increasing temperature.
      However, the binding of the T-antigen disaccharides and mellibiose disaccharides 
      to the lectin is entropically driven. The difference in the molecular
      associations in the packing and variation of the C-terminal length of the beta
      chain of the A. hirsuta lectin could be reflected in the different disaccharide
      binding energetics.
FAU - Gaikwad, Sushama M
AU  - Gaikwad SM
AD  - Biochemical Sciences Division, National Chemical Laboratory, June 411008, India.
FAU - Khan, M Islam
AU  - Khan MI
LA  - eng
PT  - Journal Article
PL  - United States
TA  - Photochem Photobiol
JT  - Photochemistry and photobiology
JID - 0376425
RN  - 0 (Antigens, Viral, Tumor)
RN  - 0 (Disaccharides)
RN  - 0 (Plant Lectins)
RN  - 0 (jacalin)
SB  - IM
MH  - Antigens, Viral, Tumor/*chemistry
MH  - Artocarpus
MH  - Disaccharides/chemistry/*metabolism
MH  - Kinetics
MH  - Plant Lectins/*chemistry
MH  - Spectrophotometry
MH  - Structure-Activity Relationship
MH  - Thermodynamics
EDAT- 2006/06/17 09:00
MHDA- 2007/06/01 09:00
CRDT- 2006/06/17 09:00
PHST- 2006/06/17 09:00 [pubmed]
PHST- 2007/06/01 09:00 [medline]
PHST- 2006/06/17 09:00 [entrez]
AID - 2006-05-04-RN-892 [pii]
AID - 10.1562/2006-05-04-RN-892 [doi]
PST - ppublish
SO  - Photochem Photobiol. 2006 Sep-Oct;82(5):1315-8. doi: 10.1562/2006-05-04-RN-892.

PMID- 9767440
OWN - NLM
STAT- MEDLINE
DCOM- 19981215
LR  - 20190512
IS  - 0019-2805 (Print)
IS  - 0019-2805 (Linking)
VI  - 94
IP  - 4
DP  - 1998 Aug
TI  - Characterization of E-selectin-binding epitopes expressed by skin-homing T cells.
PG  - 523-8
AB  - The glycoprotein counter-receptors for E-selectin borne on skin-homing T cells
      are poorly defined. In this study we have used flow cytometry to investigate the 
      surface expression of potential carbohydrate ligands for E-selectin on HUT78, a
      skin-homing cutaneous T-cell lymphoma. These cells possessed high surface
      expression of the KM-93 epitope but not HECA 452 or CSLEX1 epitopes. The KM-93
      antibody also blocked the binding of HUT78 cells to E-selectin. All these
      antibodies are reported to recognize sialyl Lewis X (sLex)-like molecules. Using 
      an E-selectin affinity matrix, the main glycoprotein isolated from HUT78 cells
      was a molecular species of 90 000 MW. Other minor species of molecular weights 40
      000, 60 000, 100 000, 120 000 and 200 000 were also identified as potential
      counter-receptors for E-selectin. Four of the purified counter-receptors (90 000,
      100 000, 120 000 and 200 000 MW) stained positive with the KM-93 antibody.
      Immunoblot analysis of these purified glycoproteins established the identity of
      the 90 000 MW glycoprotein as l-selectin. Furthermore, an anti-l-selectin
      antibody inhibited the binding of HUT78 cells to E-selectin, probably by steric
      inhibition of the carbohydrate ligand for E-selectin that is borne on the C-type 
      lectin domain of l-selectin. These results suggest that a carbohydrate epitope on
      l-selectin may act as a ligand for E-selectin on skin-homing T cells.
FAU - Priest, R
AU  - Priest R
AD  - Glycobiology Research Unit, Division of Cellular Science, Glaxo-Wellcome
      Medicines Research Centre, Stevenage, Hertfordshire, UK.
FAU - Bird, M I
AU  - Bird MI
FAU - Malhotra, R
AU  - Malhotra R
LA  - eng
PT  - Journal Article
PL  - England
TA  - Immunology
JT  - Immunology
JID - 0374672
RN  - 0
      (5-acetylneuraminyl-(2-3)-galactosyl-(1-4)-(fucopyranosyl-(1-3))-N-acetylglucosam
      ine)
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (E-Selectin)
RN  - 0 (Epitopes)
RN  - 0 (Lewis Blood-Group System)
RN  - 0 (Lewis X Antigen)
RN  - 0 (Oligosaccharides)
RN  - 0 (Receptors, Cell Surface)
SB  - IM
MH  - Antibodies, Monoclonal
MH  - E-Selectin/*immunology
MH  - Epitopes/*isolation & purification
MH  - Flow Cytometry
MH  - Humans
MH  - Lewis Blood-Group System
MH  - Lewis X Antigen
MH  - Lymphoma, T-Cell, Cutaneous
MH  - Molecular Weight
MH  - Oligosaccharides/immunology
MH  - Receptors, Cell Surface/*isolation & purification
MH  - Skin/*immunology
MH  - Skin Neoplasms
MH  - Tumor Cells, Cultured
PMC - PMC1364230
EDAT- 1998/10/10 00:00
MHDA- 1998/10/10 00:01
CRDT- 1998/10/10 00:00
PHST- 1998/10/10 00:00 [pubmed]
PHST- 1998/10/10 00:01 [medline]
PHST- 1998/10/10 00:00 [entrez]
AID - 10.1046/j.1365-2567.1998.00551.x [doi]
PST - ppublish
SO  - Immunology. 1998 Aug;94(4):523-8. doi: 10.1046/j.1365-2567.1998.00551.x.

PMID- 1659106
OWN - NLM
STAT- MEDLINE
DCOM- 19911211
LR  - 20181113
IS  - 0001-6322 (Print)
IS  - 0001-6322 (Linking)
VI  - 82
IP  - 1
DP  - 1991
TI  - Disialoganglioside GD2 in human neuroectodermal tumor cell lines and gliomas.
PG  - 45-54
AB  - Monoclonal antibodies (mAbs) recognizing the disialoganglioside
      II3(NeuAc)2GgOse3Cer (GD2) were produced by immunizing mice with the
      GD2-expressing neuroblastoma cell line LAN-1 and a prefusion boost with purified 
      GD2 coupled to Salmonella minnesota. Two IgM mAbs were isolated which
      demonstrated high levels of reactivity (binding ratios in excess of 100) with GD2
      by solid-phase radioimmunoassay and positivity in high-performance thin-layer
      chromatography (HPTLC) immunostain; only one (DMAb-20) was subsequently shown by 
      analysis with a panel of defined ganglioside species to be specific for the
      minimum epitope of GD2 GalNAc beta 1-4(NeuAc alpha 2-8-NeuAc alpha 2-3)Gal-,
      DMAb-20 was used to evaluate the expression of GD2 by malignant glioma and
      medulloblastoma cell lines using cell surface radioimmunoassay. indirect membrane
      immunofluorescence. HPTLC immunostain, and densitometric analysis of extracted
      gangliosides from selected cell lines. Sixteen of 20 (80%) malignant glioma and 5
      of 5 medulloblastoma cell lines reacted with DMAb-20; in agreement with previous 
      studies, 5 of 5 neuroblastoma and 2 of 3 melanoma cell lines also reacted with
      DMAb-20, GD2 was proportionally increased in the glioma and medulloblastoma cell 
      lines relative to levels in normal brain, as determined by densitometric
      analysis. In a phenotypic survey of malignant glioma biopsies, tumor cells in 24 
      of 30 (80%) cases stained positively with DMAb-20. Reactive astrocytes, both
      within the adjacent to tumors, were frequently intensely stained. Among the
      morphological variants of glioblastoma examined, the most intense staining with
      DMAb-20 was observed in neoplastic gemistocytes, with the weakest or absent
      staining in small cell glioblastomas. As GD2 is a commonly expressed surface
      antigen of gliomas and medulloblastomas, expression of which is retained in
      tissue culture. DMAb-20 will be useful in determining the functional role of GD2 
      in cell-cell interaction, adhesion, and invasion, and in defining altered growth 
      control mechanisms of central nervous system neoplasms in in vitro models.
FAU - Longee, D C
AU  - Longee DC
AD  - Department of Pathology, Duke University Medical Center, Durham, NC 27710.
FAU - Wikstrand, C J
AU  - Wikstrand CJ
FAU - Mansson, J E
AU  - Mansson JE
FAU - He, X
AU  - He X
FAU - Fuller, G N
AU  - Fuller GN
FAU - Bigner, S H
AU  - Bigner SH
FAU - Fredman, P
AU  - Fredman P
FAU - Svennerholm, L
AU  - Svennerholm L
FAU - Bigner, D D
AU  - Bigner DD
LA  - eng
GR  - CA 32672/CA/NCI NIH HHS/United States
GR  - NS 20023/NS/NINDS NIH HHS/United States
GR  - R37 CA 11898/CA/NCI NIH HHS/United States
GR  - etc.
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - Germany
TA  - Acta Neuropathol
JT  - Acta neuropathologica
JID - 0412041
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Gangliosides)
RN  - 65988-71-8 (ganglioside, GD2)
SB  - IM
MH  - Animals
MH  - Antibodies, Monoclonal
MH  - Antibody Specificity
MH  - Brain Neoplasms/*pathology
MH  - Cell Line
MH  - Female
MH  - Fluorescent Antibody Technique
MH  - Gangliosides/*analysis
MH  - Glioblastoma/pathology
MH  - Glioma/chemistry/*pathology
MH  - Humans
MH  - Immunoenzyme Techniques
MH  - Mice
MH  - Mice, Inbred BALB C/immunology
MH  - Radioimmunoassay
EDAT- 1991/01/01 00:00
MHDA- 1991/01/01 00:01
CRDT- 1991/01/01 00:00
PHST- 1991/01/01 00:00 [pubmed]
PHST- 1991/01/01 00:01 [medline]
PHST- 1991/01/01 00:00 [entrez]
PST - ppublish
SO  - Acta Neuropathol. 1991;82(1):45-54.

PMID- 3545444
OWN - NLM
STAT- MEDLINE
DCOM- 19870330
LR  - 20041117
IS  - 0008-5472 (Print)
IS  - 0008-5472 (Linking)
VI  - 47
IP  - 5
DP  - 1987 Mar 1
TI  - Distribution of lung adenocarcinoma-associated antigens in human tissues and sera
      defined by monoclonal antibodies KM-52 and KM-93.
PG  - 1267-72
AB  - Two monoclonal antibodies to human lung adenocarcinoma, KM-52 and KM-93, were
      generated by the novel immunizing procedure using mice rendered tolerant to the
      normal human lung (N. Hanai et al., Cancer Res., 46: 4438-4443, 1986). KM-93
      recognized sialylated carbohydrate epitope on the antigen different from CA19-9
      and DU-PAN-2, while KM-52 recognized the protein antigen. Both antigens were
      different from carcinoembryonic antigen, alpha-fetoprotein, and beta
      2-microglobulin. Distribution of KA-52 and KA-93, the antigens recognized by
      KM-52 and KM-93, respectively, in various tissues and sera was investigated. In
      immunoperoxidase staining, KM-93 reacted strongly and frequently with tumor cells
      of lung adenocarcinoma and partially with those of lung squamous cell carcinoma, 
      large cell carcinoma, and small cell carcinoma. In normal adult and fetal
      tissues, KA-93 was expressed on the surface of a small number of cells of the
      lung, pancreas, liver, kidney, and bone marrow. KM-52 reacted selectively with
      tumor cells of adenocarcinoma among four different histological types of lung
      carcinoma. In normal adult and fetal tissues, KA-52 was distributed on a small
      number of cells of the lung, stomach, intestine, and pancreas. Of the two
      monoclonal antibodies, KM-93 could be used in detecting the antigen in sera of
      patients with lung cancer. The KA-93 level in sera was determined by the
      sandwich-type enzyme-linked immunosorbent assay. Serum with a high KA-93 level
      was found in 34 of 70 patients with lung adenocarcinoma (48.6%), one of 67
      healthy adults (1.5%), and none of 32 patients with benign diseases (0%).
      Combined detection by KA-93 with KA-32, a new tumor marker of lung squamous cell 
      carcinoma (N. Hanai et al., Cancer Res., 46: 5206-5210, 1986), elevated the
      positive percentage in patients with lung squamous cell carcinoma (52.7%) and
      with lung adenocarcinoma (59.5%). These results suggested that KM-52 and KM-93
      would be potential monoclonal antibodies in immunohistological diagnosis and
      serum diagnosis of lung adenocarcinoma, respectively.
FAU - Shitara, K
AU  - Shitara K
FAU - Hanai, N
AU  - Hanai N
FAU - Yoshida, H
AU  - Yoshida H
LA  - eng
PT  - Journal Article
PL  - United States
TA  - Cancer Res
JT  - Cancer research
JID - 2984705R
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens, Neoplasm)
SB  - IM
MH  - Adenocarcinoma/diagnosis/*immunology
MH  - Animals
MH  - Antibodies, Monoclonal/*immunology
MH  - Antigens, Neoplasm/*analysis/immunology
MH  - Cell Line
MH  - Enzyme-Linked Immunosorbent Assay
MH  - Humans
MH  - Immunoenzyme Techniques
MH  - Lung Neoplasms/diagnosis/*immunology
MH  - Mice
EDAT- 1987/03/01 00:00
MHDA- 1987/03/01 00:01
CRDT- 1987/03/01 00:00
PHST- 1987/03/01 00:00 [pubmed]
PHST- 1987/03/01 00:01 [medline]
PHST- 1987/03/01 00:00 [entrez]
PST - ppublish
SO  - Cancer Res. 1987 Mar 1;47(5):1267-72.

PMID- 7981088
OWN - NLM
STAT- MEDLINE
DCOM- 19950103
LR  - 20190515
IS  - 0007-0920 (Print)
IS  - 0007-0920 (Linking)
VI  - 70
IP  - 6
DP  - 1994 Dec
TI  - Expression of sialyl-Tn predicts the effect of adjuvant chemotherapy in
      node-positive breast cancer.
PG  - 1272-5
AB  - Sialyl-Tn (STn) is a carcinoma-associated carbohydrate determinant expressed on
      cancer-associated mucins and has the structure NANA alpha(2-6)alpha GalNAc.
      Expression of STn in colon and ovarian cancer is associated with a poor prognosis
      independent of tumour grade, stage or histological type. We have examined 237
      cases of primary breast cancer for expression of this antigen using the antibody 
      HB-STn (Dako). The frequency of STn expression was 31% in the whole group, 36% in
      the node-negative and 28% in the node-positive group. Survival was lower, but not
      significantly so, in the STn-positive group (P = 0.07), but this effect was
      highly significant for patients with node-positive disease (P < 0.002), the
      curves for node-negative disease being coincident (P = 0.31). In node-positive
      disease the effect was limited to those receiving adjuvant chemotherapy (P =
      0.001). In a multivariate (Cox) analysis on the whole group STn staining,
      combined with adjuvant chemotherapy, showed a highly significant correlation with
      survival. In STn-negative cases, adjuvant chemotherapy improved survival
      (relative risk 2.3, 95% confidence intervals 1.4-3.9), whereas adjuvant
      chemotherapy did not influence survival in patients which expressed STn (relative
      risk 1.1, 95% confidence intervals 0.6-2.2). Thus, by either direct or indirect
      mechanisms, STn positivity appears to be a marker of resistance to adjuvant
      chemotherapy.
FAU - Miles, D W
AU  - Miles DW
AD  - ICRF Clinical Oncology Unit, Guy's Hospital, London, UK.
FAU - Happerfield, L C
AU  - Happerfield LC
FAU - Smith, P
AU  - Smith P
FAU - Gillibrand, R
AU  - Gillibrand R
FAU - Bobrow, L G
AU  - Bobrow LG
FAU - Gregory, W M
AU  - Gregory WM
FAU - Rubens, R D
AU  - Rubens RD
LA  - eng
PT  - Clinical Trial
PT  - Controlled Clinical Trial
PT  - Journal Article
PL  - England
TA  - Br J Cancer
JT  - British journal of cancer
JID - 0370635
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Biomarkers, Tumor)
RN  - 0 (sialosyl-Tn antigen)
SB  - IM
MH  - Antigens, Tumor-Associated, Carbohydrate/*metabolism
MH  - Biomarkers, Tumor
MH  - Breast Neoplasms/*diagnosis/drug therapy/pathology
MH  - Carcinoma, Ductal, Breast/*diagnosis/drug therapy
MH  - Humans
MH  - Lymphatic Metastasis
MH  - Prognosis
MH  - Survival Analysis
PMC - PMC2033699
EDAT- 1994/12/01 00:00
MHDA- 1994/12/01 00:01
CRDT- 1994/12/01 00:00
PHST- 1994/12/01 00:00 [pubmed]
PHST- 1994/12/01 00:01 [medline]
PHST- 1994/12/01 00:00 [entrez]
AID - 10.1038/bjc.1994.486 [doi]
PST - ppublish
SO  - Br J Cancer. 1994 Dec;70(6):1272-5. doi: 10.1038/bjc.1994.486.

PMID- 7509790
OWN - NLM
STAT- MEDLINE
DCOM- 19940401
LR  - 20071114
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 269
IP  - 8
DP  - 1994 Feb 25
TI  - Common tetrasaccharide epitope NeuAc alpha 2-->3Gal beta 1-->3(Neu-Ac alpha
      2-->6)GalNAc, presented by different carrier glycosylceramides or O-linked
      peptides, is recognized by different antibodies and ligands having distinct
      specificities.
PG  - 5644-52
AB  - A novel globo-series disialoganglioside, disialosyl galactosyl globoside
      (Structure 1 below), defined by new monoclonal antibody (mAb) RM2, was isolated
      and characterized as having terminal structure identical to that of
      ganglio-series ganglioside GD1 alpha (Structure 2) and a common mucin-type
      epitope (Structure 3) widely distributed in glycoproteins such as glycophorin A. 
      While these three structures share a common nonreducing tetrasaccharide terminus,
      mAb RM2 showed strong specific reactivity only with Structure 1, not with
      Structures 2 or 3. Another mAb, QSH2, reacted strongly with Structure 3 but did
      not cross-react with Structures 1 or 2. Conformational molecular models based on 
      minimum energy hard sphere exoanomeric calculations suggest that Structure 1
      presents a unique surface topology distinct from that of Structures 2 or 3. Our
      findings suggest the novel concept that reactivity of a common carbohydrate
      epitope with different antibodies or ligands is highly dependent on the type of
      carrier glycosylceramide or carrier O-linked peptide. [formula: see text]
FAU - Saito, S
AU  - Saito S
AD  - Biomembrane Institute, Seattle, Washington 98119.
FAU - Levery, S B
AU  - Levery SB
FAU - Salyan, M E
AU  - Salyan ME
FAU - Goldberg, R I
AU  - Goldberg RI
FAU - Hakomori, S
AU  - Hakomori S
LA  - eng
GR  - CA42505/CA/NCI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Ceramides)
RN  - 0 (Epitopes)
RN  - 0 (Gangliosides)
RN  - 0 (Peptides)
RN  - 71764-07-3 (disialosyl galactosyl globoside)
SB  - IM
MH  - Animals
MH  - Antibodies, Monoclonal/*immunology
MH  - Antibody Specificity
MH  - Carbohydrate Conformation
MH  - Carbohydrate Sequence
MH  - Ceramides/chemistry/*immunology
MH  - Epitopes/*chemistry/immunology
MH  - Gangliosides/*chemistry/immunology
MH  - Gas Chromatography-Mass Spectrometry
MH  - Humans
MH  - Kidney Neoplasms/immunology
MH  - Magnetic Resonance Spectroscopy
MH  - Mice
MH  - Mice, Inbred BALB C
MH  - Models, Molecular
MH  - Molecular Sequence Data
MH  - Peptides/chemistry/*immunology
MH  - Spectrometry, Mass, Fast Atom Bombardment
MH  - Tumor Cells, Cultured
EDAT- 1994/02/25 00:00
MHDA- 1994/02/25 00:01
CRDT- 1994/02/25 00:00
PHST- 1994/02/25 00:00 [pubmed]
PHST- 1994/02/25 00:01 [medline]
PHST- 1994/02/25 00:00 [entrez]
PST - ppublish
SO  - J Biol Chem. 1994 Feb 25;269(8):5644-52.

PMID- 7516636
OWN - NLM
STAT- MEDLINE
DCOM- 19940718
LR  - 20151119
IS  - 0250-7005 (Print)
IS  - 0250-7005 (Linking)
VI  - 14
IP  - 2B
DP  - 1994 Mar-Apr
TI  - Simple mucins (T, sialosyl-T, Tn and sialosyl-Tn) are not diagnostic for
      malignant breast lesions.
PG  - 609-15
AB  - Immunohistochemical study of the distribution of carbohydrate core-structures on 
      O-linked glycoproteins (T, sialosyl-T, Tn and sialosyl-Tn) was performed using
      specific monoclonal antibodies on 148 primary breast lesions, including 10 normal
      breast tissues, 16 benign lesions and 122 invasive carcinomas (79 localized and
      43 metastatic lesions). T antigen, not observed in normal breast tissue, was
      present in 31% of the benign lesions and in some cases of morphologically normal 
      epithelium adjacent to tumor cells, compatible with altered glycosylation being
      an early event. Sialosyl-T (s-T) antigen was present in all cases of normal
      epithelium and in 81% of the benign lesions. Both Tn and sialosyl-Tn (s-Tn)
      antigen were present in normal breast lesions. Both Tn and sialosyl-Tn (s-Tn)
      antigen were present in normal breast tissue (30%) and benign lesions (31% and
      19%). In the malignant lesions, 20% were positive for T antigen, 82% for s-T
      antigen, 66% for Tn antigen and 22% for s-Tn antigen. The staining pattern was
      nearly identical for carcinomas with and without lymph node metastases. In
      conclusion, immunostaining for simple mucins does not permit a clear distinction 
      between benign and malignant breast lesions.
FAU - Reed, W
AU  - Reed W
AD  - Department of Pathology, Norwegian Radium Hospital, Oslo, Norway.
FAU - Bryne, M
AU  - Bryne M
FAU - Clausen, H
AU  - Clausen H
FAU - Dabelsteen, E
AU  - Dabelsteen E
FAU - Nesland, J M
AU  - Nesland JM
LA  - eng
PT  - Journal Article
PL  - Greece
TA  - Anticancer Res
JT  - Anticancer research
JID - 8102988
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Antigens, Viral, Tumor)
RN  - 0 (Biomarkers)
RN  - 0 (Biomarkers, Tumor)
RN  - 0 (Carbohydrates)
RN  - 0 (Epitopes)
RN  - 0 (Mucins)
RN  - 0 (Oligosaccharides)
RN  - 0 (Tn antigen)
RN  - 0 (sialosyl-T antigen)
RN  - 0 (sialosyl-Tn antigen)
SB  - IM
MH  - Antibodies, Monoclonal
MH  - Antigens, Tumor-Associated, Carbohydrate/*analysis
MH  - Antigens, Viral, Tumor/*analysis
MH  - Biomarkers/analysis
MH  - Biomarkers, Tumor/*analysis
MH  - Breast/*cytology/*pathology
MH  - Breast Neoplasms/*pathology
MH  - Carbohydrate Sequence
MH  - Carbohydrates/analysis
MH  - Carcinoma, Ductal, Breast/pathology
MH  - Epithelial Cells
MH  - Epithelium/pathology
MH  - Epitopes
MH  - Female
MH  - Humans
MH  - Immunohistochemistry
MH  - Molecular Sequence Data
MH  - Mucins/*analysis
MH  - Neoplasm Invasiveness
MH  - Neoplasm Metastasis
MH  - Oligosaccharides/analysis
EDAT- 1994/03/01 00:00
MHDA- 1994/03/01 00:01
CRDT- 1994/03/01 00:00
PHST- 1994/03/01 00:00 [pubmed]
PHST- 1994/03/01 00:01 [medline]
PHST- 1994/03/01 00:00 [entrez]
PST - ppublish
SO  - Anticancer Res. 1994 Mar-Apr;14(2B):609-15.

PMID- 16310781
OWN - NLM
STAT- MEDLINE
DCOM- 20060123
LR  - 20131121
IS  - 0014-5793 (Print)
IS  - 0014-5793 (Linking)
VI  - 579
IP  - 30
DP  - 2005 Dec 19
TI  - Structural basis for the specificity of basic winged bean lectin for the
      Tn-antigen: a crystallographic, thermodynamic and modelling study.
PG  - 6775-80
AB  - The crystal structure of winged bean basic agglutinin in complex with
      GalNAc-alpha-O-Ser (Tn-antigen) has been elucidated at 2.35 angstroms resolution 
      in order to characterize the mode of binding of Tn-antigen with the lectin. The
      Gal moiety occupies the primary binding site and makes interactions similar to
      those found in other Gal/GalNAc specific legume lectins. The nitrogen and oxygen 
      atoms of the acetamido group of the sugar make two hydrogen bonds with the
      protein atoms whereas its methyl group is stabilized by hydrophobic interactions.
      A water bridge formed between the terminal oxygen atoms of the serine residue of 
      the Tn-antigen and the side chain oxygen atom of Asn128 of the lectin increase
      the affinity of the lectin for Tn-antigen compared to that for GalNAc. A
      comparison with the available structures reveals that while the interactions of
      the glyconic part of the antigen are conserved, the mode of stabilization of the 
      serine residue differs and depends on the nature of the protein residues in its
      vicinity. The structure provides a qualitative explanation for the thermodynamic 
      parameters of the complexation of the lectin with Tn-antigen. Modeling studies
      indicate the possibility of an additional hydrogen bond with the lectin when the 
      antigen is part of a glycoprotein.
FAU - Kulkarni, Kiran A
AU  - Kulkarni KA
AD  - Molecular Biophysics Unit, Indian Institute of Science, CVRaman Avenue,
      Bangalore, Karnataka 560 012, India.
FAU - Sinha, Sharmistha
AU  - Sinha S
FAU - Katiyar, Samiksha
AU  - Katiyar S
FAU - Surolia, Avadhesha
AU  - Surolia A
FAU - Vijayan, Mamannamana
AU  - Vijayan M
FAU - Suguna, Kaza
AU  - Suguna K
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20051121
PL  - England
TA  - FEBS Lett
JT  - FEBS letters
JID - 0155157
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Lectins)
RN  - 0 (Plant Lectins)
RN  - 0 (Tn antigen)
RN  - 0 (winged bean lectin)
RN  - 059QF0KO0R (Water)
SB  - IM
EIN - FEBS Lett. 2006 May 15;580(11):2808
MH  - Antigens, Tumor-Associated, Carbohydrate/*metabolism
MH  - Binding Sites
MH  - Carbohydrate Conformation
MH  - Carbohydrate Sequence
MH  - Computer Simulation
MH  - *Crystallography, X-Ray
MH  - Dimerization
MH  - Hydrogen Bonding
MH  - Hydrophobic and Hydrophilic Interactions
MH  - Lectins/chemistry/metabolism
MH  - Models, Molecular
MH  - Plant Lectins/*chemistry/*metabolism
MH  - Sensitivity and Specificity
MH  - Spectrum Analysis, Raman
MH  - Substrate Specificity
MH  - *Thermodynamics
MH  - Water/chemistry
EDAT- 2005/11/29 09:00
MHDA- 2006/01/24 09:00
CRDT- 2005/11/29 09:00
PHST- 2005/09/01 00:00 [received]
PHST- 2005/10/12 00:00 [revised]
PHST- 2005/11/03 00:00 [accepted]
PHST- 2005/11/29 09:00 [pubmed]
PHST- 2006/01/24 09:00 [medline]
PHST- 2005/11/29 09:00 [entrez]
AID - S0014-5793(05)01358-X [pii]
AID - 10.1016/j.febslet.2005.11.011 [doi]
PST - ppublish
SO  - FEBS Lett. 2005 Dec 19;579(30):6775-80. doi: 10.1016/j.febslet.2005.11.011. Epub 
      2005 Nov 21.

PMID- 7496150
OWN - NLM
STAT- MEDLINE
DCOM- 19960118
LR  - 20181113
IS  - 0282-0080 (Print)
IS  - 0282-0080 (Linking)
VI  - 12
IP  - 3
DP  - 1995 Jun
TI  - Expression of the T antigen on a T-lymphoid cell line, supT1.
PG  - 356-9
AB  - We have measured glycosyltransferase activities of SupT1 cells, a T-lymphoid cell
      line shown to react with autoantibodies in the sera of many HIV patients. Since
      considerable alpha-N-acetylgalactosaminyl-transferase and beta 1, 3
      galactosyltransferase activities were found in SupT1 cells, at least the O-glycan
      core 1 structure can probably be synthesized. FACS analysis using an anti-T
      monoclonal antibody showed expression of the T antigen (Gal beta 1-3 GalNAc).
      Glycoproteins with the T antigen were isolated by immunoprecipitation with the
      anti-T antibody from a SupT1 cell lysate labelled metabolically with
      3H-glucosamine and then analysed by SDS-PAGE. It was revealed that the
      precipitate contained a glycoprotein with a molecular weight corresponding to
      that of leukosialin. O-glycans were prepared from the immunoprecipitate by
      alkaline-borohydride treatment and then fractionated on Bio-Gel P-2, GalNAcOH and
      Gal-GalNAcOH being identified inter alia. These results suggest that an anti-T
      antibody may be included in the autoantibodies found in HIV-1 infected
      individuals.
FAU - Nakada, H
AU  - Nakada H
AD  - Department of Biotechnology, Faculty of Engineering, Kyoto, Japan.
FAU - Inoue, M
AU  - Inoue M
FAU - Tanaka, N
AU  - Tanaka N
FAU - Wakamiya, N
AU  - Wakamiya N
FAU - Yamashina, I
AU  - Yamashina I
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Glycoconj J
JT  - Glycoconjugate journal
JID - 8603310
RN  - 0 (Antigens, CD)
RN  - 0 (Antigens, Viral, Tumor)
RN  - 0 (Autoantibodies)
RN  - 0 (Leukosialin)
RN  - 0 (Polysaccharides)
RN  - 0 (Sialoglycoproteins)
RN  - 0 (UN1 sialoglycoprotein, human)
SB  - IM
SB  - X
MH  - Antigens, CD/*blood
MH  - Antigens, Viral, Tumor/*blood
MH  - Autoantibodies/blood
MH  - Carbohydrate Sequence
MH  - Cell Line
MH  - HIV-1/*immunology
MH  - Humans
MH  - Leukosialin
MH  - Molecular Sequence Data
MH  - Polysaccharides/blood
MH  - Sialoglycoproteins/*immunology
MH  - T-Lymphocytes/*immunology
EDAT- 1995/06/01 00:00
MHDA- 1995/06/01 00:01
CRDT- 1995/06/01 00:00
PHST- 1995/06/01 00:00 [pubmed]
PHST- 1995/06/01 00:01 [medline]
PHST- 1995/06/01 00:00 [entrez]
PST - ppublish
SO  - Glycoconj J. 1995 Jun;12(3):356-9.

PMID- 8905297
OWN - NLM
STAT- MEDLINE
DCOM- 19970516
LR  - 20061115
IS  - 0171-9335 (Print)
IS  - 0171-9335 (Linking)
VI  - 71
IP  - 2
DP  - 1996 Oct
TI  - Role of acetylated gangliosides on neurite extension.
PG  - 192-8
AB  - We have investigated the role of 9-O-acetylated gangliosides identified by the
      Jones monoclonal antibody (Jones mAb) in the elongation of neurites extended by
      neurons of embryonic rat dorsal root ganglia (DRG) explants grown on laminin
      substratum. The behavior of individual growth cones was recorded using a
      time-lapse video-enhanced imaging system before and after the addition of
      antibodies that recognize specific gangliosides known to be expressed on these
      growth cones. It was possible to demonstrate that the advance of growth cones on 
      laminin was halted in the presence of Jones mAb. The onset of effects was rapid
      and signaled by an immediate cessation of elongation, a loss of lamellipodia and 
      a retrieval of axoplasm. This effect was partially reverted by washing the
      explants for several minutes with culture medium. mAb A2B5 which also recognizes 
      gangliosides expressed on these growth cones does not induce any change on the
      growth rate. Our findings show that 9-O-acetylated gangliosides may play an
      important role on the extension of growth cones and consequently influence
      navigation and pathway finding during development.
FAU - Mendez-Otero, R
AU  - Mendez-Otero R
AD  - Instituto de Biofisica Carlos Chagas Filho, Universidade Federal do Rio de
      Janeiro, Brazil.
FAU - Friedman, J E
AU  - Friedman JE
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - Germany
TA  - Eur J Cell Biol
JT  - European journal of cell biology
JID - 7906240
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Gangliosides)
RN  - 0 (Laminin)
SB  - IM
MH  - Age Factors
MH  - Animals
MH  - Antibodies, Monoclonal/pharmacology
MH  - Ganglia, Spinal/chemistry/*physiology
MH  - Gangliosides/*physiology
MH  - Immunohistochemistry
MH  - Laminin/physiology
MH  - Microscopy, Video
MH  - Neurites/chemistry/*physiology
MH  - Rats
MH  - Rats, Sprague-Dawley
MH  - Time Factors
EDAT- 1996/10/01 00:00
MHDA- 1996/10/01 00:01
CRDT- 1996/10/01 00:00
PHST- 1996/10/01 00:00 [pubmed]
PHST- 1996/10/01 00:01 [medline]
PHST- 1996/10/01 00:00 [entrez]
PST - ppublish
SO  - Eur J Cell Biol. 1996 Oct;71(2):192-8.

PMID- 1370965
OWN - NLM
STAT- MEDLINE
DCOM- 19920309
LR  - 20181130
IS  - 0023-6837 (Print)
IS  - 0023-6837 (Linking)
VI  - 66
IP  - 2
DP  - 1992 Feb
TI  - Studies on the Thomsen-Friedenreich antigen in human colon with the lectin
      Amaranthin. Normal and neoplastic epithelium express only cryptic T antigen.
PG  - 175-86
AB  - The lectin Amaranthin has been shown to be highly specific for the galactose beta
      1,3 N-acetylgalactosamine-alpha and sialic acid alpha 2,3 galactose beta 1,3
      N-acetylgalactosamine-alpha sequence which represents the Thomsen-Friedenreich
      (T) antigen and its cryptic form, respectively. Previously, we demonstrated the
      usefulness of gold-labeled Amaranthin for the histochemical detection of the T
      antigen and its cryptic form. Application of the galactose oxidase (GO)-Schiff
      sequence abolished lectin binding to the T antigen but not its cryptic form, and 
      therefore permitted their differentiation. In the present study we have analyzed 
      by light and electron microscopy the distribution and subcellular localization of
      Amaranthin binding sites in normal, dysplastic and neoplastic colonic epithelium.
      Furthermore, a monoclonal antibody raised against synthetic galactose bera 1,3
      N-acetylgalactosamine-alpha-bovine serum albumin was applied as a reagent for the
      T antigen. In normal colonic mucosa, two different Amaranthin staining patterns
      existed: (a) reactivity restricted to the lower portion of the crypts which was
      principally observed in the left colon, and (b) reactivity along the entire
      length of the crypts and in the surface epithelium with goblet cell staining in
      the upper portion of the crypts which was principally observed in the right
      colon. This Amaranthin staining was resistant to GO-Schiff treatment. No
      immunostaining with the monoclonal anti-T antigen was observed. Investigation of 
      transitional mucosa, adenocarcinomas of different degrees of differentiation and 
      mucinous carcinomas as well as adenomas with different degrees of dysplasia all
      revealed positive Amaranthin staining. The lectin staining was resistant to
      GO-Schiff treatment, and immunolabeling with the monoclonal antibody against the 
      T antigen was absent. These results indicate that only the cryptic form of the T 
      antigen is expressed in normal, dysplastic and neoplastic human colonic
      epithelium.
FAU - Sata, T
AU  - Sata T
AD  - Department of Pathology, National Institute of Health, Tokyo, Japan.
FAU - Roth, J
AU  - Roth J
FAU - Zuber, C
AU  - Zuber C
FAU - Stamm, B
AU  - Stamm B
FAU - Rinderle, S J
AU  - Rinderle SJ
FAU - Goldstein, I J
AU  - Goldstein IJ
FAU - Heitz, P U
AU  - Heitz PU
LA  - eng
GR  - GM29470/GM/NIGMS NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Lab Invest
JT  - Laboratory investigation; a journal of technical methods and pathology
JID - 0376617
RN  - 0 (Antigens, Neoplasm)
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Disaccharides)
RN  - 0 (Lectins)
RN  - 0 (Plant Lectins)
RN  - 0 (Ribosome Inactivating Proteins, Type 1)
RN  - 0 (amaranthin protein, Amaranthus)
RN  - 3554-90-3 (Thomsen-Friedenreich antigen)
RN  - EC 3.2.2.22 (Ribosome Inactivating Proteins)
SB  - IM
MH  - Antigens, Neoplasm/analysis
MH  - *Antigens, Tumor-Associated, Carbohydrate
MH  - Colon/cytology/*immunology
MH  - Colonic Neoplasms/*immunology/pathology
MH  - Disaccharides/*analysis
MH  - Epithelium/immunology
MH  - Humans
MH  - Immunohistochemistry
MH  - Intestinal Mucosa/immunology
MH  - *Lectins
MH  - *Plant Lectins
MH  - Ribosome Inactivating Proteins
MH  - Ribosome Inactivating Proteins, Type 1
MH  - Staining and Labeling
EDAT- 1992/02/01 00:00
MHDA- 1992/02/01 00:01
CRDT- 1992/02/01 00:00
PHST- 1992/02/01 00:00 [pubmed]
PHST- 1992/02/01 00:01 [medline]
PHST- 1992/02/01 00:00 [entrez]
PST - ppublish
SO  - Lab Invest. 1992 Feb;66(2):175-86.

PMID- 14638629
OWN - NLM
STAT- MEDLINE
DCOM- 20041019
LR  - 20061115
IS  - 0959-6658 (Print)
IS  - 0959-6658 (Linking)
VI  - 14
IP  - 2
DP  - 2004 Feb
TI  - The parasitic trematode Fasciola hepatica exhibits mammalian-type glycolipids as 
      well as Gal(beta1-6)Gal-terminating glycolipids that account for cestode
      serological cross-reactivity.
PG  - 115-26
AB  - Neutral glycosphingolipids from sheep-derived Fasciola hepatica liver flukes were
      isolated and characterized both structurally and serologically. After HPLC
      fractionation, glycolipids were analyzed by linkage analysis, enzymatic cleavage,
      and MALDI-TOF as well as electrospray ionization mass spectrometry. Obtained
      results revealed the presence of two types of neutral glycolipids. The first
      group represented mammalian-type species comprising globo- and
      isoglobotriaosylceramides (Gal(alpha1-4)Gal(beta1-4)Glc(1-1)ceramide and
      Gal(alpha1-3)Gal(beta1-4)Glc(1-1)ceramide, respectively) as well as Forssman
      antigen
      (GalNAc(alpha1-3)GalNAc(beta1-3/4)Gal(alpha1-4/3)Gal(beta1-4)Glc(1-1)ceramide).
      Applying Helix pomatia agglutinin, recognizing terminal alpha-linked GalNAc, to
      cryosections of adult flukes, the latter glycolipid could be localized to the F. 
      hepatica gut. As Forssman antigen from the parasite and sheep host led to
      identical MALDI-TOF MS profiles, this glycolipid might be acquired from the
      definitive host. As a second group, highly antigenic glycolipids were
      structurally characterized as Gal(beta1-6)Gal(beta1-4)Glc(1-1)ceramide,
      Gal(beta1-6)Gal(alpha1-3/4)Gal(beta1-4)Glc(1-1)ceramide and
      Gal(beta1-6)Gal(beta1-6)Gal(alpha1-3/4)Gal(beta1-4)Glc(1-1)ceramide, the latter
      two structures of which exhibited both isoglobo- or globo-series core structures.
      Terminal Gal(beta1-6)Gal1-motifs have previously been shown to represent
      antigenic epitopes of neogala-series glycosphingolipids from tape worms. Using
      human Echinococcus granulosus infection sera, Gal(beta1-6)Gal-terminating
      glycolipids could be allocated to the gut in adult liver fluke cryosections.
      Corresponding neogala-reactive antibodies in F. hepatica infection serum were
      detected by their binding to E. granulosus and Taenia crassiceps
      neogala-glycosphingolipids. These antibodies might contribute to the known
      serological cross-reactivity between F. hepatica and parasitic cestode
      infections.
FAU - Wuhrer, Manfred
AU  - Wuhrer M
AD  - Institute of Biochemistry, Medical Faculty, University of Giessen, D-35392
      Giessen, Germany.
FAU - Grimm, Christiane
AU  - Grimm C
FAU - Dennis, Roger D
AU  - Dennis RD
FAU - Idris, Mohamed A
AU  - Idris MA
FAU - Geyer, Rudolf
AU  - Geyer R
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20031124
PL  - England
TA  - Glycobiology
JT  - Glycobiology
JID - 9104124
RN  - 0 (Glycolipids)
RN  - 0 (Glycosphingolipids)
RN  - 0 (Oligosaccharides)
RN  - 9013-60-9 (Forssman Antigen)
SB  - IM
MH  - Animals
MH  - Carbohydrate Conformation
MH  - Carbohydrate Sequence
MH  - Cestode Infections/immunology/*metabolism
MH  - Cross Reactions
MH  - Fasciola hepatica/*chemistry/metabolism
MH  - Forssman Antigen/immunology
MH  - Glycolipids/*chemistry
MH  - Glycosphingolipids/chemistry
MH  - Immunohistochemistry
MH  - Oligosaccharides/chemistry
MH  - Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
EDAT- 2003/11/26 05:00
MHDA- 2004/10/20 09:00
CRDT- 2003/11/26 05:00
PHST- 2003/11/26 05:00 [pubmed]
PHST- 2004/10/20 09:00 [medline]
PHST- 2003/11/26 05:00 [entrez]
AID - 10.1093/glycob/cwh021 [doi]
AID - cwh021 [pii]
PST - ppublish
SO  - Glycobiology. 2004 Feb;14(2):115-26. doi: 10.1093/glycob/cwh021. Epub 2003 Nov
      24.

PMID- 9399674
OWN - NLM
STAT- MEDLINE
DCOM- 19980108
LR  - 20160303
IS  - 0020-7136 (Print)
IS  - 0020-7136 (Linking)
VI  - 73
IP  - 6
DP  - 1997 Dec 10
TI  - Le(y) glycolipid acts as a co-factor for tumor procoagulant activity.
PG  - 903-9
AB  - We have generated a monoclonal antibody (MAb), FS01, which inhibits the
      procoagulant activity (CCA-1) produced by a human squamous cell carcinoma cell
      line, LK52. Expression of the antigen recognized by FS01 MAb in various cancer
      cell lines correlated well with the procoagulant activities of the expressing
      cell lines. Our objective was to characterize the molecule reacting with FS01 MAb
      and to analyze its involvement in the CCA-1 procoagulant activity. The molecule
      was identified as a glycolipid and found to be involved in the procoagulant
      activity because both procoagulant activity and reactivity to FS01 MAb were lost 
      after endoglycoceramidase treatment of CCA-1. Furthermore, FS01 MAb recognized
      the Lewis Y (Le[y]) antigen. To confirm the involvement of a glycolipid
      incorporating the Le(y) antigen in the procoagulant activity, we attempted to
      purify CCA-1 from LK52 culture supernatant. In one of the purification steps, a
      fraction containing low procoagulant activity (CCA-1p) separated from the
      Le(y)-positive fraction (CCA-1c). Although CCA-1c alone did not show procoagulant
      activity, the procoagulant activity of CCA-1p was augmented by CCA-1c and this
      augmentation was inhibited by FS01 MAb. Furthermore, CCA-1c enhanced the
      procoagulant activity of 33 cell lines tested as well as CCA-1p. In addition,
      purified Le(y) glycolipid from canine intestine augmented the procoagulant
      activity of CCA-1p, and this augmentation also could be inhibited by FS01 MAb. We
      conclude that Le(y) glycolipid is a co-factor for the procoagulant activity
      derived from cancer cells.
FAU - Suzuki, M
AU  - Suzuki M
AD  - Fujisaki Institute, Hayashibara Biochemical Laboratories Inc., Okayama, Japan.
      Fujih@po.harenet.or.jp
FAU - Inufusa, H
AU  - Inufusa H
FAU - Yamamoto, S
AU  - Yamamoto S
FAU - Hamada, T
AU  - Hamada T
FAU - Aga, M
AU  - Aga M
FAU - Ando, O
AU  - Ando O
FAU - Ohta, T
AU  - Ohta T
FAU - Yasutomi, M
AU  - Yasutomi M
FAU - Kurimoto, M
AU  - Kurimoto M
LA  - eng
PT  - Journal Article
PL  - United States
TA  - Int J Cancer
JT  - International journal of cancer
JID - 0042124
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens, Neoplasm)
RN  - 0 (Blood Coagulation Factors)
RN  - 0 (Glycolipids)
RN  - 0 (Lewis Blood-Group System)
RN  - 0 (Lewis Y antigen)
RN  - 0 (Membrane Glycoproteins)
SB  - IM
MH  - Animals
MH  - Antibodies, Monoclonal/immunology
MH  - Antigens, Neoplasm/immunology/isolation & purification/*metabolism
MH  - Blood Coagulation Factors/*metabolism
MH  - COS Cells
MH  - Cells, Cultured
MH  - Cercopithecus aethiops
MH  - Dogs
MH  - Female
MH  - Glycolipids/chemistry/immunology
MH  - Humans
MH  - Immunoblotting
MH  - Lewis Blood-Group System/*immunology/*physiology
MH  - Membrane Glycoproteins/chemistry/immunology
MH  - Neoplasms/chemistry/immunology/*metabolism
MH  - Tumor Cells, Cultured
MH  - Vero Cells
EDAT- 1997/12/17 02:45
MHDA- 2000/06/20 09:00
CRDT- 1997/12/17 02:45
PHST- 1997/12/17 02:45 [pubmed]
PHST- 2000/06/20 09:00 [medline]
PHST- 1997/12/17 02:45 [entrez]
AID - 10.1002/(SICI)1097-0215(19971210)73:6<903::AID-IJC24>3.0.CO;2-3 [pii]
PST - ppublish
SO  - Int J Cancer. 1997 Dec 10;73(6):903-9.

PMID- 1358980
OWN - NLM
STAT- MEDLINE
DCOM- 19921207
LR  - 20171116
IS  - 0022-202X (Print)
IS  - 0022-202X (Linking)
VI  - 99
IP  - 5
DP  - 1992 Nov
TI  - Human epidermal keratinocyte expression of sialyl-Lewis X.
PG  - 601-7
AB  - Cell-surface oligosaccharides can function as ligands for intercellular adhesion 
      receptors, matrix proteins, and growth factors. We report that human neonatal and
      adult epidermal keratinocytes (KC) express sialyl Lewis X [s-Le(x); SA alpha
      2-3Gal beta 1-4(Fuc alpha 1-3)GlcNAc beta 1-3R], a ligand for endothelial and
      platelet selectins. Freshly isolated or cultured KC bind FH6 monoclonal antibody 
      (MoAb), which is specific for s-Le(x)-containing oligosaccharides. The relevant
      epitope is bona fide s-Le(x), because sialidase treatment of KC suspensions
      abrogates FH6 binding while generating de novo KC reactivity with anti-Le(x). KC 
      stained in ice-cold suspension display a knobby membrane distribution of s-Le(x) 
      detectable by immunofluorescence microscopy. As others have reported, FH6
      appeared not to bind KC in perpendicular skin sections. However, basal KC in
      intact epidermal sheets exhibited obvious "honeycomb" reactivity with FH6 when
      stained and viewed en face, suggesting that s-Le(x) in intact epidermis may occur
      in bands that parallel the major tissue axis. FH6 specifically immunoprecipitated
      proteins of Mr 34 kd, 44 kd, and 56 kd from [35S]-labeled KC, and anti-Le(x)
      precipitated similar proteins from sialidase-treated KC. The enzymatic basis for 
      KC s-Le(x) expression was studied by analyzing acceptor specificities and other
      properties of KC fucosyltransferases. Results indicate that KC express both
      Lewis- and myeloid-type alpha 1-3fucosyltransferases. KC s-Le(x) could be an
      important element of the epithelial milieu, because both epithelial cells and
      immune cells that home to epithelia express s-Le(x) and related structures, and
      because KC s-Le(x) is well positioned for selectin-mediated platelet binding
      after trans-cutaneous wounding. The apparent distributions of s-Le(x) in
      epidermis and on isolated KC are compatible with a functional role for s-Le(x) in
      these intercellular interactions.
FAU - Symington, F W
AU  - Symington FW
AD  - Seattle Biomedical Research Institute, WA 98109-1651.
FAU - Holmes, E H
AU  - Holmes EH
FAU - Symington, B E
AU  - Symington BE
LA  - eng
GR  - AI28523/AI/NIAID NIH HHS/United States
GR  - CA41521/CA/NCI NIH HHS/United States
GR  - K04 CA01343/CA/NCI NIH HHS/United States
GR  - etc.
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - J Invest Dermatol
JT  - The Journal of investigative dermatology
JID - 0426720
RN  - 0 (Antigens, Surface)
RN  - 0 (Lewis X Antigen)
RN  - 0 (Membrane Glycoproteins)
SB  - IM
MH  - Adult
MH  - Antigens, Surface/analysis
MH  - Carbohydrate Sequence
MH  - Cells, Cultured
MH  - Humans
MH  - Infant, Newborn
MH  - Keratinocytes/*immunology
MH  - Lewis X Antigen/*analysis
MH  - Male
MH  - Membrane Glycoproteins/analysis
MH  - Molecular Sequence Data
EDAT- 1992/11/01 00:00
MHDA- 1992/11/01 00:01
CRDT- 1992/11/01 00:00
PHST- 1992/11/01 00:00 [pubmed]
PHST- 1992/11/01 00:01 [medline]
PHST- 1992/11/01 00:00 [entrez]
AID - S0022-202X(92)90687-Y [pii]
PST - ppublish
SO  - J Invest Dermatol. 1992 Nov;99(5):601-7.

PMID- 7287743
OWN - NLM
STAT- MEDLINE
DCOM- 19811221
LR  - 20071114
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 256
IP  - 21
DP  - 1981 Nov 10
TI  - Two monoclonal anticarbohydrate antibodies directed to glycosphingolipids with a 
      lacto-N-glycosyl type II chain.
PG  - 10967-72
AB  - Two monoclonal antibodies directed to the Type II carbohydrate chain of
      glycosphingolipids have been prepared by the murine hybridoma technique. Their
      reactivity was determined by liposome lysis, plate-binding assay, complement
      fixation, and hemagglutination inhibition. One antibody was specific for
      glycolipids having the nonreducing terminal N-acetyllactosamine (Gal beta 1 leads
      to 4GlcNAc beta 1 leads to R) structure and did not react with glycolipids having
      either a Type I chain (Gal beta 1 leads to 3GlcNAc beta 1 leads to R), a
      ganglio-series structure (Gal beta 1 leads to 3GalNAc beta 1 leads to R), or a
      sialosyl or fucosyl substitution at the N-acetyllactosamine residue. This
      antibody readily agglutinated adult human erythrocytes of all ABO types but did
      not agglutinate umbilical cord cells. The other antibody reacted with the Type II
      chain H structure (Fuc alpha 1 leads to 2Gal beta 1 leads to 4GlcNAc beta 1 leads
      to R) but reacted only weakly with the Type I chain H (Fuc alpha 1 leads to 2Gal 
      beta 1 leads to 3GlcNAc beta 1 leads to R) and ganglio-series H (Fuc alpha 1
      leads to 2Gal beta 1 leads to 3GalNAc beta 1 leads to R) structures. At 37
      degrees C this antibody agglutinated human erythrocytes of types O and A2 but was
      unable to cause detectable agglutination of types B and A1. Because of their
      narrow, well defined specificity, these monoclonal anticarbohydrate reagents will
      be useful in the study of the distribution, quantity, and function of specific
      carbohydrates on the cell surface.
FAU - Young, W W Jr
AU  - Young WW Jr
FAU - Portoukalian, J
AU  - Portoukalian J
FAU - Hakomori, S
AU  - Hakomori S
LA  - eng
GR  - 5 507 RR-5431-19/RR/NCRR NIH HHS/United States
GR  - CA 29539/CA/NCI NIH HHS/United States
GR  - GM 23100/GM/NIGMS NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigen-Antibody Complex)
RN  - 0 (Glycolipids)
RN  - 0 (Glycosphingolipids)
RN  - 0 (Immunoglobulin G)
RN  - 0 (Immunoglobulin M)
SB  - IM
MH  - Animals
MH  - *Antibodies, Monoclonal
MH  - Antigen-Antibody Complex
MH  - Complement Fixation Tests
MH  - Glycolipids/immunology
MH  - Glycosphingolipids/*immunology
MH  - Hemagglutination
MH  - Humans
MH  - Hybridomas/enzymology
MH  - Immunoglobulin G
MH  - Immunoglobulin M
MH  - Mice
MH  - Mice, Inbred BALB C
MH  - Structure-Activity Relationship
EDAT- 1981/11/10 00:00
MHDA- 2001/03/28 10:01
CRDT- 1981/11/10 00:00
PHST- 1981/11/10 00:00 [pubmed]
PHST- 2001/03/28 10:01 [medline]
PHST- 1981/11/10 00:00 [entrez]
PST - ppublish
SO  - J Biol Chem. 1981 Nov 10;256(21):10967-72.

PMID- 8609406
OWN - NLM
STAT- MEDLINE
DCOM- 19960529
LR  - 20171116
IS  - 0022-1767 (Print)
IS  - 0022-1767 (Linking)
VI  - 156
IP  - 8
DP  - 1996 Apr 15
TI  - A carbohydrate structure associated with CD15 (Lewis x) on myeloid cells is a
      novel ligand for human CD2.
PG  - 2866-73
AB  - The T cell and NK cell adhesion molecule CD2 interacts with different ligands,
      viz, CD58, CD48, and CD59. Using a fluorescent multimeric construct of rCD2, we
      previously identified an additional CD2 ligand (CD2L) on the erythroleukemic cell
      line K562. CD2L bound to a different region of CD2 than known ligands and was
      N-glycosylation dependent. In this study we show that mAbs specific for the
      carbohydrate Ag Lewis x (CD15, Gal-beta 1-4 GlcNAc alpha 1-3Fuc) inhibit
      multimeric rCD2 binding to CD2L. CD2L is restricted in expression to myeloid
      cells, where it is co-expressed with CD58 on monocytes and is the dominant, if
      not sole, CD2 ligand on neutrophils. Sugar specificity studies show that CD2L is 
      not CD15. Thus, whereas soluble Lewis x inhibits binding of CD15 mAb to K562 and 
      neutrophils, binding of multimeric rCD2 is unaffected. Furthermore, multimeric
      rCD2 binding to K562 is inhibited by L-fucose and following treatment of K562
      with an alpha 1-6 fucosidase, whereas these treatments do not inhibit the binding
      of CD15 mAb. Thus, it is likely that CD2L is a carbohydrate structure closely
      associated with, yet distinct from, CD15, which can be sterically blocked by CD15
      mAb. Functional studies revealed that CD2L is probably an important CD2 ligand in
      the non-MHC-restricted NK cell killing of K562 target cells, since this activity 
      was strongly inhibited by CD15 mAb. Collectively, this study indicates that a
      CD15 (Lewis x)-associated carbohydrate structure(s), which has previously been
      shown to be a selectin ligand, also may function as an important CD2 ligand on
      myeloid cells.
FAU - Warren, H S
AU  - Warren HS
AD  - Cancer Research Unit, Woden Valley Hospital, Australia.
FAU - Altin, J G
AU  - Altin JG
FAU - Waldron, J C
AU  - Waldron JC
FAU - Kinnear, B F
AU  - Kinnear BF
FAU - Parish, C R
AU  - Parish CR
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - J Immunol
JT  - Journal of immunology (Baltimore, Md. : 1950)
JID - 2985117R
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (CD2 Antigens)
RN  - 0 (Epitopes)
RN  - 0 (Lewis Blood-Group System)
RN  - 0 (Lewis X Antigen)
RN  - 0 (Ligands)
SB  - AIM
SB  - IM
MH  - Antibodies, Monoclonal/chemistry/pharmacology
MH  - Antigen-Antibody Reactions
MH  - B-Lymphocytes/chemistry/immunology
MH  - Binding, Competitive/immunology
MH  - CD2 Antigens/immunology/*metabolism/physiology
MH  - Carbohydrate Sequence
MH  - Epitopes/chemistry
MH  - Hematopoietic Stem Cells/*chemistry/*immunology
MH  - Humans
MH  - Leukemia, Erythroblastic, Acute
MH  - Lewis Blood-Group System/*chemistry
MH  - Lewis X Antigen/immunology/*metabolism
MH  - Ligands
MH  - Melanoma
MH  - Molecular Sequence Data
MH  - Structure-Activity Relationship
MH  - Tumor Cells, Cultured
EDAT- 1996/04/15 00:00
MHDA- 1996/04/15 00:01
CRDT- 1996/04/15 00:00
PHST- 1996/04/15 00:00 [pubmed]
PHST- 1996/04/15 00:01 [medline]
PHST- 1996/04/15 00:00 [entrez]
PST - ppublish
SO  - J Immunol. 1996 Apr 15;156(8):2866-73.

PMID- 1716885
OWN - NLM
STAT- MEDLINE
DCOM- 19911022
LR  - 20171116
IS  - 0006-291X (Print)
IS  - 0006-291X (Linking)
VI  - 179
IP  - 2
DP  - 1991 Sep 16
TI  - Adhesion of human cancer cells to vascular endothelium mediated by a carbohydrate
      antigen, sialyl Lewis A.
PG  - 713-9
AB  - Recently the lectin-like domain on ELAM-1 (endothelial leukocyte adhesion
      molecule-1) was shown to recognize a carbohydrate antigen, sialyl Lewis x. In
      this paper we demonstrate, by a series of inhibition experiments utilizing
      specific monoclonal antibodies and pure glycolipid preparations, that the sialyl 
      Lewis a antigen serves as a specific ligand for ELAM-1 as well as sialyl Lewis x 
      and plays a significant role in the ELAM-1-mediated binding of human cancer cells
      to activated endothelial cells.
FAU - Takada, A
AU  - Takada A
AD  - Department of Laboratory Medicine, Kyoto University, School of Medicine, Japan.
FAU - Ohmori, K
AU  - Ohmori K
FAU - Takahashi, N
AU  - Takahashi N
FAU - Tsuyuoka, K
AU  - Tsuyuoka K
FAU - Yago, A
AU  - Yago A
FAU - Zenita, K
AU  - Zenita K
FAU - Hasegawa, A
AU  - Hasegawa A
FAU - Kannagi, R
AU  - Kannagi R
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Biochem Biophys Res Commun
JT  - Biochemical and biophysical research communications
JID - 0372516
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Cell Adhesion Molecules)
RN  - 0 (Drug Carriers)
RN  - 0 (E-Selectin)
RN  - 0 (Gangliosides)
RN  - 0 (Interleukin-1)
RN  - 0 (Lewis Blood-Group System)
RN  - 0 (Lewis X Antigen)
RN  - 0 (Ligands)
RN  - 0 (Liposomes)
RN  - 0 (Recombinant Proteins)
RN  - 91847-18-6 (sialyl Le(a) ganglioside)
SB  - IM
MH  - Antibodies, Monoclonal
MH  - Antigens, Tumor-Associated, Carbohydrate/*metabolism
MH  - Carbohydrate Sequence
MH  - Cell Adhesion
MH  - Cell Adhesion Molecules/metabolism
MH  - Drug Carriers
MH  - E-Selectin
MH  - Endothelium, Vascular/*metabolism
MH  - Gangliosides/*metabolism
MH  - Humans
MH  - Interleukin-1/metabolism
MH  - *Lewis Blood-Group System
MH  - Lewis X Antigen/metabolism
MH  - Ligands
MH  - Liposomes
MH  - Molecular Sequence Data
MH  - Recombinant Proteins/metabolism
MH  - Tumor Cells, Cultured/metabolism
EDAT- 1991/09/16 00:00
MHDA- 1991/09/16 00:01
CRDT- 1991/09/16 00:00
PHST- 1991/09/16 00:00 [pubmed]
PHST- 1991/09/16 00:01 [medline]
PHST- 1991/09/16 00:00 [entrez]
AID - 0006-291X(91)91875-D [pii]
PST - ppublish
SO  - Biochem Biophys Res Commun. 1991 Sep 16;179(2):713-9.

PMID- 20954701
OWN - NLM
STAT- MEDLINE
DCOM- 20110524
LR  - 20151119
IS  - 1535-3907 (Electronic)
IS  - 1535-3893 (Linking)
VI  - 9
IP  - 12
DP  - 2010 Dec 3
TI  - Identification of a novel type of CA19-9 carrier in human bile and sera of cancer
      patients: an implication of the involvement in nonsecretory exocytosis.
PG  - 6345-53
LID - 10.1021/pr100600u [doi]
AB  - Carbohydrate antigen 19-9 (CA19-9) is a well-known tumor marker for pancreatic
      cancer. Although the CA19-9 level is measured using anti-sialyl Lewis A
      antibodies, it remains unknown which molecules carry CA19-9 other than mucins.
      Here we report the identification and characterization of a novel type of CA19-9 
      carrier, BGM (bile globular membrane), which is thought to exist in normal bile
      and to be secreted into sera of patients with pancreatic cancer. We purified the 
      BGM from bile juice using a beta-casein column because surface plasmon resonance 
      analysis could detect such carrier vesicles binding to beta-casein in sera of
      patients with pancreatic cancer. We identified characteristic molecules for BGM
      such as AHNAK (desmoykoin) and a novel golgin family member, CABIN (CAsein
      Binding domain integral protein with golgIN motif) by mass spectrometry analysis.
      BGM was detected in the sera of patients with pancreatic cancer as well as
      athymic mice with transplanted pancreatic cancer cells. Down regulation of CABIN 
      inhibited the secretion of CA19-9 on BGM in pancreatic cancer cell lines. We
      measured and visualized BGM in sera of patients with cancer. Thus, BGM might be
      another CA19-9 carrier (glyco-lipids on membrane vesicles) other than mucins and 
      could be applied to the diagnosis of pancreatic cancer.
FAU - Uozumi, Naofumi
AU  - Uozumi N
AD  - Department of Molecular Biochemistry and Clinical Investigation, Osaka University
      Graduate School of Medicine, 1-7 Yamada-oka, Suita 565-0871, Japan.
FAU - Gao, Congxiao
AU  - Gao C
FAU - Yoshioka, Tomoko
AU  - Yoshioka T
FAU - Nakano, Miyako
AU  - Nakano M
FAU - Moriwaki, Kenta
AU  - Moriwaki K
FAU - Nakagawa, Tsutomu
AU  - Nakagawa T
FAU - Masuda, Tomomi
AU  - Masuda T
FAU - Tanabe, Makoto
AU  - Tanabe M
FAU - Miyoshi, Eiji
AU  - Miyoshi E
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20101110
PL  - United States
TA  - J Proteome Res
JT  - Journal of proteome research
JID - 101128775
RN  - 0 (AHNAK protein, human)
RN  - 0 (Biomarkers, Tumor)
RN  - 0 (CA-19-9 Antigen)
RN  - 0 (Caseins)
RN  - 0 (Membrane Proteins)
RN  - 0 (Neoplasm Proteins)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Bile/chemistry
MH  - Biomarkers, Tumor/*analysis/blood
MH  - CA-19-9 Antigen/*analysis
MH  - Caseins/metabolism
MH  - Cell Line, Tumor
MH  - Cells, Cultured
MH  - Exocytosis
MH  - Humans
MH  - Mass Spectrometry
MH  - Membrane Proteins/genetics/metabolism
MH  - Mice
MH  - Mice, Nude
MH  - Molecular Sequence Data
MH  - Neoplasm Proteins/genetics/metabolism
MH  - Neoplasm Transplantation
MH  - Pancreatic Neoplasms/blood/*immunology/pathology
MH  - Protein Binding
MH  - Rats
MH  - Sequence Homology, Amino Acid
MH  - Surface Plasmon Resonance
MH  - Transplantation, Heterologous
MH  - Transport Vesicles/*chemistry/metabolism
EDAT- 2010/10/20 06:00
MHDA- 2011/05/25 06:00
CRDT- 2010/10/20 06:00
PHST- 2010/10/20 06:00 [entrez]
PHST- 2010/10/20 06:00 [pubmed]
PHST- 2011/05/25 06:00 [medline]
AID - 10.1021/pr100600u [doi]
PST - ppublish
SO  - J Proteome Res. 2010 Dec 3;9(12):6345-53. doi: 10.1021/pr100600u. Epub 2010 Nov
      10.

PMID- 11268468
OWN - NLM
STAT- MEDLINE
DCOM- 20010412
LR  - 20151119
IS  - 0250-7005 (Print)
IS  - 0250-7005 (Linking)
VI  - 20
IP  - 5C
DP  - 2000 Sep-Oct
TI  - Prognostic value of circulating sialyl Tn antigen in colorectal cancer patients.
PG  - 3863-9
AB  - To examine the prognostic value of assessing the concentration of circulating
      sialyl Tn antigen (STN) after surgery, we determined serum STN levels in
      peripheral venous blood (designated "p-") in 308 colorectal cancer patients and
      what we have termed the "d-p gradient" (obtained by subtracting the serum
      concentration in peripheral venous blood from that in the tumor's drainage venous
      blood) in 144 patients. The prognostic value of STN and carcinoembryonic antigen 
      (CEA) was compared. Patients were divided into low or high p-antigen groups and
      low, intermediate, or high d-p gradient groups. Univariate and multivariate
      analyses revealed that high STN d-p gradient, high p-CEA, or high CEA d-p
      gradient were each independent variables for poor patient outcome after surgery, 
      separate from stage. In conclusion, a high STN d-p gradient was a predictor of
      poor outcome after resection for colorectal cancer, while p-STN was not
      independent of stage.
FAU - Nakagoe, T
AU  - Nakagoe T
AD  - First Department of Surgery, Nagasaki University School of Medicine, 1-7-1
      Sakamoto, Nagasaki 852-8501, Japan. nakagoe@net.nagasaki-u.acjp
FAU - Sawai, T
AU  - Sawai T
FAU - Tsuji, T
AU  - Tsuji T
FAU - Jibiki, M
AU  - Jibiki M
FAU - Nanashima, A
AU  - Nanashima A
FAU - Yamaguchi, H
AU  - Yamaguchi H
FAU - Kurosaki, N
AU  - Kurosaki N
FAU - Yasutake, T
AU  - Yasutake T
FAU - Ayabe, H
AU  - Ayabe H
FAU - Tagawa, Y
AU  - Tagawa Y
LA  - eng
PT  - Comparative Study
PT  - Journal Article
PL  - Greece
TA  - Anticancer Res
JT  - Anticancer research
JID - 8102988
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Biomarkers, Tumor)
RN  - 0 (Carcinoembryonic Antigen)
RN  - 0 (sialosyl-Tn antigen)
SB  - IM
MH  - Adult
MH  - Aged
MH  - Aged, 80 and over
MH  - Analysis of Variance
MH  - Antigens, Tumor-Associated, Carbohydrate/*blood
MH  - Biomarkers, Tumor/*blood
MH  - Carcinoembryonic Antigen/blood
MH  - Colorectal Neoplasms/*blood/mortality/pathology/surgery
MH  - Female
MH  - Humans
MH  - Male
MH  - Middle Aged
MH  - Multivariate Analysis
MH  - Neoplasm Staging
MH  - Predictive Value of Tests
MH  - Prognosis
MH  - Survival Analysis
EDAT- 2001/03/28 10:00
MHDA- 2001/04/17 10:01
CRDT- 2001/03/28 10:00
PHST- 2001/03/28 10:00 [pubmed]
PHST- 2001/04/17 10:01 [medline]
PHST- 2001/03/28 10:00 [entrez]
PST - ppublish
SO  - Anticancer Res. 2000 Sep-Oct;20(5C):3863-9.

PMID- 2355463
OWN - NLM
STAT- MEDLINE
DCOM- 19900726
LR  - 20151119
IS  - 0021-4949 (Print)
IS  - 0021-4949 (Linking)
VI  - 36
IP  - 7
DP  - 1990 Jun
TI  - [An immunohistochemical evaluation of Warthin's tumor using the monoclonal
      anti-human lung adenocarcinoma antibody KM-93 and the anti-human gastric
      carcinoma antibody KM-231].
PG  - 783-6
AB  - An immunohistochemical identification of a human lung adenocarcinoma antigen and 
      a gastric carcinoma antigen, detected by means of the monoclonal antibodies
      (MoAbs) KM-93 and KM-231, respectively, has been investigated in cases of a
      Warthin's tumor and in normal salivary glands. The ductal basal cells of the
      excretory duct epithelium in normal salivary glands are characterized by their
      positive staining to MoAb KM-231, whereas MoAb KM-231 staining is confined to
      basal tumor cells in cases of Warthin's tumor. Further, MoAb KM-93 staining is
      slightly positive when luminal tumor cells are present. These results suggest
      that the histogenesis of Warthin's basal tumor cells might originate in the
      excretory duct epithelium.
FAU - Tsuji, T
AU  - Tsuji T
AD  - Dept. of Oral & Maxillofacial Surgery, Yamaguchi Univ. School of Med.
FAU - Kimura, Y
AU  - Kimura Y
FAU - Murakami, T
AU  - Murakami T
FAU - Sasaki, K
AU  - Sasaki K
FAU - Shinozaki, F
AU  - Shinozaki F
LA  - jpn
PT  - English Abstract
PT  - Journal Article
PL  - Japan
TA  - Gan No Rinsho
JT  - Gan no rinsho. Japan journal of cancer clinics
JID - 1257753
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens, Neoplasm)
SB  - IM
MH  - Adenocarcinoma/*immunology
MH  - Adenolymphoma/*immunology
MH  - *Antibodies, Monoclonal
MH  - Antigens, Neoplasm/*analysis
MH  - Humans
MH  - Immunohistochemistry
MH  - Lung Neoplasms/*immunology
MH  - Salivary Glands/immunology
MH  - Stomach Neoplasms/*immunology
EDAT- 1990/06/01 00:00
MHDA- 1990/06/01 00:01
CRDT- 1990/06/01 00:00
PHST- 1990/06/01 00:00 [pubmed]
PHST- 1990/06/01 00:01 [medline]
PHST- 1990/06/01 00:00 [entrez]
PST - ppublish
SO  - Gan No Rinsho. 1990 Jun;36(7):783-6.

PMID- 8985092
OWN - NLM
STAT- MEDLINE
DCOM- 19970127
LR  - 20160303
IS  - 0020-7136 (Print)
IS  - 0020-7136 (Linking)
VI  - 70
IP  - 1
DP  - 1997 Jan 6
TI  - Human monoclonal antibodies specific for the tumour associated
      Thomsen-Friedenreich antigen.
PG  - 63-71
AB  - Five hybridomas producing human monoclonal antibodies (MAbs) of IgA and IgM
      isotypes reacting with the tumour associated TF antigen were generated after in
      vitro immunisation or antigen specific isolation of normal peripheral blood B
      cells using asialoglycophorin, a TF containing antigen. All 5 antibodies produced
      by the hybridomas bound strongly to asialoglycophorin and to synthetic
      glycoprotein containing the TF-epitope, with preference to the beta form
      (Galb1-3GalNAc-beta-O-CETE-BSA) as compared to the alpha form
      (Galbl-3GalNAc-alpha-O-APE-HSA) in ELISA. Flow cytometry analysis revealed
      binding to carcinoma cell lines of different origin such as breast, colon,
      pancreas, ovary, bladder, lung and, in addition, to some tumour cell lines of
      haematopoietic origin. Immunohistochemical analysis of tumour tissues revealed
      staining patterns typical for mucins, and the antibodies were found to bind to
      glycoproteins among the MUC-1 positive high m.w. fraction shed from a TF antigen 
      positive ovarian carcinoma cell line.
FAU - Dahlenborg, K
AU  - Dahlenborg K
AD  - BioInvent International AB, Lund, Sweden.
FAU - Hultman, L
AU  - Hultman L
FAU - Carlsson, R
AU  - Carlsson R
FAU - Jansson, B
AU  - Jansson B
LA  - eng
PT  - Journal Article
PL  - United States
TA  - Int J Cancer
JT  - International journal of cancer
JID - 0042124
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens, Neoplasm)
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Epitopes)
RN  - 0 (Isoantigens)
RN  - 3554-90-3 (Thomsen-Friedenreich antigen)
SB  - IM
MH  - Animals
MH  - Antibodies, Monoclonal/*immunology/metabolism
MH  - Antigens, Neoplasm/*immunology
MH  - Antigens, Tumor-Associated, Carbohydrate/*immunology
MH  - Enzyme-Linked Immunosorbent Assay
MH  - Epitopes/immunology
MH  - Humans
MH  - Hybridomas/immunology
MH  - Isoantigens/*immunology
MH  - Mice
MH  - Tumor Cells, Cultured/immunology/metabolism
EDAT- 1997/01/06 00:00
MHDA- 2000/06/20 09:00
CRDT- 1997/01/06 00:00
PHST- 1997/01/06 00:00 [pubmed]
PHST- 2000/06/20 09:00 [medline]
PHST- 1997/01/06 00:00 [entrez]
AID - 10.1002/(SICI)1097-0215(19970106)70:1<63::AID-IJC10>3.0.CO;2-E [pii]
PST - ppublish
SO  - Int J Cancer. 1997 Jan 6;70(1):63-71.

PMID- 3815333
OWN - NLM
STAT- MEDLINE
DCOM- 19870330
LR  - 20071114
IS  - 0008-5472 (Print)
IS  - 0008-5472 (Linking)
VI  - 47
IP  - 5
DP  - 1987 Mar 1
TI  - Monoclonal antibody-defined correlations in melanoma between levels of GD2 and
      GD3 antigens and antibody-mediated cytotoxicity.
PG  - 1229-33
AB  - A monoclonal antibody is described that specifically detects the ganglioside
      antigens GD2 and GD3, binding preferentially to GD2, in melanoma. Antibody
      specificity was demonstrated with solid-phase radioimmunoassay and enzyme-linked 
      immunosorbent assay as well as by immunostaining on thin-layer chromatography
      plates using structurally characterized gangliosides. Binding of both the IgG3
      antibody and its IgG2a switch variant were assayed on live cells by
      cytofluorography and by immunoperoxidase staining on frozen tissue sections. The 
      binding patterns correlated with antitumor activity in antibody-dependent
      cellular cytotoxicity and complement-dependent cytotoxicity assays with human
      effector cells and complement in an 111In-release assay using cell lines derived 
      from the same individual. The significant level of killing in all tumor cells
      tested that express GD2, GD3, or both, suggests the importance of multiple
      specificity towards tumor antigens, i.e., binding of a monoclonal antibody to two
      or more tumor-associated antigens.
FAU - Thurin, J
AU  - Thurin J
FAU - Thurin, M
AU  - Thurin M
FAU - Kimoto, Y
AU  - Kimoto Y
FAU - Herlyn, M
AU  - Herlyn M
FAU - Lubeck, M D
AU  - Lubeck MD
FAU - Elder, D E
AU  - Elder DE
FAU - Smereczynska, M
AU  - Smereczynska M
FAU - Karlsson, K A
AU  - Karlsson KA
FAU - Clark, W M Jr
AU  - Clark WM Jr
FAU - Steplewski, Z
AU  - Steplewski Z
AU  - et al.
LA  - eng
GR  - CA-10815/CA/NCI NIH HHS/United States
GR  - CA-21124/CA/NCI NIH HHS/United States
GR  - CA-25874/CA/NCI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Cancer Res
JT  - Cancer research
JID - 2984705R
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens, Neoplasm)
RN  - 0 (Gangliosides)
RN  - 62010-37-1 (ganglioside, GD3)
RN  - 65988-71-8 (ganglioside, GD2)
RN  - 9007-36-7 (Complement System Proteins)
SB  - IM
MH  - Animals
MH  - Antibodies, Monoclonal/*immunology
MH  - Antibody Specificity
MH  - Antigens, Neoplasm/*analysis
MH  - Complement System Proteins/immunology
MH  - *Cytotoxicity, Immunologic
MH  - Enzyme-Linked Immunosorbent Assay
MH  - Gangliosides/*analysis/immunology
MH  - Humans
MH  - Melanoma/*immunology
MH  - Mice
MH  - Mice, Inbred BALB C
EDAT- 1987/03/01 00:00
MHDA- 2001/03/28 10:01
CRDT- 1987/03/01 00:00
PHST- 1987/03/01 00:00 [pubmed]
PHST- 2001/03/28 10:01 [medline]
PHST- 1987/03/01 00:00 [entrez]
PST - ppublish
SO  - Cancer Res. 1987 Mar 1;47(5):1229-33.

PMID- 2736629
OWN - NLM
STAT- MEDLINE
DCOM- 19890728
LR  - 20171118
IS  - 0008-8749 (Print)
IS  - 0008-8749 (Linking)
VI  - 121
IP  - 2
DP  - 1989 Jul
TI  - Expression of Thomsen-Friedenreich (TF) antigens on lymphocytes. I. Distribution 
      of cryptic and exposed TF antigens on murine lymphocytes from different lymphoid 
      organs: detection with an anti-TF monoclonal antibody and peanut agglutinin.
PG  - 360-5
AB  - Cryptic Thomsen-Friedenreich (TF) antigens were detected by the lectin peanut
      agglutinin (PNA) on the surface of murine lymphocytes after treatment of cells
      with neuraminidase. Thereby, a particular TF antigen could be distinguished using
      a monoclonal anti-TF antibody 49H8. In contrast to the known general galactoside 
      specificity of PNA, the mAb was restricted to Gal beta(1-3)GalNAc/GlcNAc.
      Preincubation of cells with PNA abolished mAb 49H8 binding completely. However,
      only the intensity of staining with PNA was reduced by prior incubation of cells 
      with the mAb. Cryptic TF antigens detected by the mAb were expressed on 39% of
      murine bone marrow cells, 88% of thymocytes, 62% of lymph node cells, and 65% of 
      spleen cells. On the other hand, over 80% of the lymphatic cells carried cryptic 
      PNA binding sites independent of the lymphoid organ they derived. In the thymus, 
      a subpopulation of cells (76%) could be detected by PNA without neuraminidase
      treatment. Twenty-eight percent of thymocytes carried exposed mAb binding sites, 
      too. All of them were shown to express further binding sites for PNA constantly. 
      Therefore, a subpopulation of PNA-reactive, immature thymocytes can be
      distinguished by the mAb 49H8. During activation of splenic lymphocytes with PHA,
      the lymphoblasts completely lost their cryptic mAb binding sites while PNA
      reactivity was not affected. We conclude that the anti-TF mAb recognizes a
      particular TF antigen exposed on thymocytes and present in a cryptic form on
      other lymphocytes. The number of cells carrying mAb 49H8 binding sites varied,
      dependent on the organ from which the lymphocytes derived. PNA-reactive
      lymphocytes are distributed homogeneously in the lymphoid organs.
FAU - Wolf, M F
AU  - Wolf MF
AD  - Department of Hematology, Oncology, and Immunology, Robert-Bosch-Krankenhaus,
      Stuttgart, Federal Republic of Germany.
FAU - Schmitt, H R
AU  - Schmitt HR
FAU - Schumacher, K
AU  - Schumacher K
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - Netherlands
TA  - Cell Immunol
JT  - Cellular immunology
JID - 1246405
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Disaccharides)
RN  - 0 (Lectins)
RN  - 0 (Peanut Agglutinin)
RN  - 3554-90-3 (Thomsen-Friedenreich antigen)
SB  - IM
MH  - Animals
MH  - *Antibodies, Monoclonal
MH  - *Antigens, Tumor-Associated, Carbohydrate
MH  - Bone Marrow/immunology
MH  - Disaccharides/analysis/*immunology
MH  - *Lectins
MH  - Lymphocytes/*immunology
MH  - Male
MH  - Mice
MH  - Mice, Inbred C3H
MH  - Peanut Agglutinin
MH  - Thymus Gland/immunology
EDAT- 1989/07/01 00:00
MHDA- 1989/07/01 00:01
CRDT- 1989/07/01 00:00
PHST- 1989/07/01 00:00 [pubmed]
PHST- 1989/07/01 00:01 [medline]
PHST- 1989/07/01 00:00 [entrez]
AID - 0008-8749(89)90034-8 [pii]
PST - ppublish
SO  - Cell Immunol. 1989 Jul;121(2):360-5.

PMID- 11214861
OWN - NLM
STAT- MEDLINE
DCOM- 20010426
LR  - 20080815
IS  - 1121-760X (Print)
IS  - 1121-760X (Linking)
VI  - 44
IP  - 4
DP  - 2000
TI  - Expression of Tn, sialosyl-Tn and T antigens in human foetal large intestine.
PG  - 359-63
AB  - Tn, sialosyl-Tn and T antigens are simple mucin-type carbohydrate antigens that
      may be expressed in human neoplasies due to alteration of the glycoprotein
      biosynthetic pathway. Utilising specific monoclonal antibodies (HB-Tn1, HB-STn1
      and HB-T1), we have investigated the expression of these simple mucin-type
      carbohydrate antigens in large intestine of 8 human foetuses at early gestational
      age (9-10 weeks), obtained after therapeutic abortion. In all cases the
      expression of Tn antigen was mainly localised as a thin rim at the cell membrane 
      and occasionally in the supranuclear region of epithelial cells, while
      sialosyl-Tn antigen was documented in some goblet cell vacuoles and occasionally 
      in the cytoplasm of columnar cells. T antigen was not expressed in any case.
      These results indicate that Tn and sialosyl-Tn antigens are expressed as early as
      nine weeks of gestation, further supporting the notion that they may be
      considered as oncodevelopmental cancer-associated antigens in the large
      intestine.
FAU - Grosso, M
AU  - Grosso M
AD  - Department of Human Pathology, University of Messina, Italy.
FAU - Vitarelli, E
AU  - Vitarelli E
FAU - Giuffre, G
AU  - Giuffre G
FAU - Tuccari, G
AU  - Tuccari G
FAU - Barresi, G
AU  - Barresi G
LA  - eng
PT  - Journal Article
PL  - Italy
TA  - Eur J Histochem
JT  - European journal of histochemistry : EJH
JID - 9207930
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Antigens, Viral, Tumor)
RN  - 0 (Tn antigen)
RN  - 0 (sialosyl-Tn antigen)
SB  - IM
MH  - Antigens, Tumor-Associated, Carbohydrate/*analysis
MH  - Antigens, Viral, Tumor/*analysis
MH  - Humans
MH  - Intestine, Large/embryology/*immunology
EDAT- 2001/02/24 12:00
MHDA- 2001/05/01 10:01
CRDT- 2001/02/24 12:00
PHST- 2001/02/24 12:00 [pubmed]
PHST- 2001/05/01 10:01 [medline]
PHST- 2001/02/24 12:00 [entrez]
PST - ppublish
SO  - Eur J Histochem. 2000;44(4):359-63.

PMID- 8912871
OWN - NLM
STAT- MEDLINE
DCOM- 19970107
LR  - 20061115
IS  - 0008-5472 (Print)
IS  - 0008-5472 (Linking)
VI  - 56
IP  - 22
DP  - 1996 Nov 15
TI  - Correlation between tumor-associated glycoprotein 72 mucin levels in tumor and
      serum of colorectal patients as measured by the quantitative CA 72-4 immunoassay.
PG  - 5293-8
AB  - Colorectal tissue biopsies were obtained from 110 patients diagnosed with primary
      colorectal carcinoma (tumor and normal colonic mucosa samples), 20 patients
      diagnosed with benign colorectal disease, and 31 healthy donors. The level of
      expression of tumor-associated glycoprotein 72 (TAG-72) was quantitatively
      measured in each sample using a double-determinant RIA with monoclonal antibodies
      B72.3 and CC49 and detecting the sialyl-Tn epitope; this assay was termed CA
      72-4. Statistical analysis revealed a significant (approximately 10-fold)
      increase of TAG-72 expression in the colon tumor biopsies when compared with the 
      expression in normal colonic mucosa from the same patients. A regression analysis
      revealed a significant correlation (r = 0.459; P < 0.001) between TAG-72 levels
      measured in biopsies from the tumor lesions and those found in the corresponding 
      normal colonic mucosa. Furthermore, regression analysis showed a significant
      positive correlation between TAG-72 levels in the tumors and sera of the same
      patients (r = 0.491; P < 0.001). TAG-72 levels in normal colonic mucosa from
      healthy donors and patients diagnosed with colorectal cancer were compared.
      TAG-72 expression was 5-fold higher in the normal mucosa from the colorectal
      carcinoma patients. No relationship between TAG-72 tumor tissue content and stage
      of disease was found. Moreover, the correlation between TAG-72 distribution and
      degree of tumor differentiation observed (P < 0.05) was not any more evident when
      mucinous carcinomas were excluded. Finally, the results provide further evidence 
      that TAG-72 may be considered an important early marker for colorectal cancer
      and/or other dysplastic colonic diseases. The statistical correlation between
      TAG-72 levels in tumors and circulating TAG-72 indicates that patients with
      elevated levels of serum TAG-72, as measured by the CA 72-4 assay, would be most 
      suited for diagnostic and/or therapeutic intervention with the anti-TAG-72
      monoclonal antibodies B72.3 or CC49 or vaccine trials using the sialyl-Tn
      epitope.
FAU - Guadagni, F
AU  - Guadagni F
AD  - Laboratory of Clinical Pathology, Regina Elena Cancer Institute, Rome, Italy.
FAU - Roselli, M
AU  - Roselli M
FAU - Cosimelli, M
AU  - Cosimelli M
FAU - Spila, A
AU  - Spila A
FAU - Cavaliere, F
AU  - Cavaliere F
FAU - Tedesco, M
AU  - Tedesco M
FAU - Arcuri, R
AU  - Arcuri R
FAU - Abbolito, M R
AU  - Abbolito MR
FAU - Casale, V
AU  - Casale V
FAU - Pericoli, M N
AU  - Pericoli MN
FAU - Vecchione, A
AU  - Vecchione A
FAU - Casciani, C U
AU  - Casciani CU
FAU - Greiner, J W
AU  - Greiner JW
FAU - Schlom, J
AU  - Schlom J
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Cancer Res
JT  - Cancer research
JID - 2984705R
RN  - 0 (Antigens, Neoplasm)
RN  - 0 (Glycoproteins)
RN  - 0 (Neoplasm Proteins)
RN  - 0 (tumor-associated antigen 72)
SB  - IM
MH  - Adult
MH  - Aged
MH  - Aged, 80 and over
MH  - Antigens, Neoplasm/*analysis/blood
MH  - Colorectal Neoplasms/blood/*chemistry
MH  - Female
MH  - Glycoproteins/*analysis/blood
MH  - Humans
MH  - Intestinal Mucosa/chemistry
MH  - Male
MH  - Middle Aged
MH  - Neoplasm Proteins/*analysis/blood
EDAT- 1996/11/15 00:00
MHDA- 1996/11/15 00:01
CRDT- 1996/11/15 00:00
PHST- 1996/11/15 00:00 [pubmed]
PHST- 1996/11/15 00:01 [medline]
PHST- 1996/11/15 00:00 [entrez]
PST - ppublish
SO  - Cancer Res. 1996 Nov 15;56(22):5293-8.

PMID- 6083447
OWN - NLM
STAT- MEDLINE
DCOM- 19850207
LR  - 20171116
IS  - 0161-5890 (Print)
IS  - 0161-5890 (Linking)
VI  - 21
IP  - 11
DP  - 1984 Nov
TI  - Further studies of the specificities of monoclonal anti-i and anti-I antibodies
      using chemically synthesized, linear oligosaccharides of the
      poly-N-acetyllactosamine series.
PG  - 1099-104
AB  - The I- and i-antigen activities of chemically synthesized, linear
      oligosaccharides of the neolacto series containing one, two or three
      N-acetyllactosamine (Gal beta 1----4GlcNAc) units have been tested by inhibition 
      of binding of five anti-i and eight anti-I monoclonal antibodies to
      radioiodinated I- and i-active glycoproteins. The inhibitory activities of the
      milk oligosaccharides lacto-N-neotetraose (Gal beta 1----4GlcNAc beta 1----3Gal
      beta 1----4Glc) and lacto-N-tetraose (Gal beta 1----3GlcNAc beta 1----3Gal beta
      1----4Glc) have also been determined. The results clearly show that: (a) the
      determinants that best fit the combining sites of anti-i antibodies are at least 
      hexasaccharides of the neolacto series, (b) linear tetra- and hexasaccharides of 
      the neolacto series can strongly inhibit the binding of anti-I antibodies of
      group 2 which are known to be primarily directed at the repeating Gal beta
      1----4GlcNAc beta 1----3 domains of branched neolacto sequences, (c) the beta-
      but not the alpha-methyl anomer of the glycoside Gal beta 1----4GlcNAc beta
      1-O-Me inhibits the binding of anti-I antibodies of group 1 which recognise the
      branch point sequence Gal beta 1----4GlcNAc beta 1----6-, (d) the reactivity of
      the beta-methylglycoside is impaired if the sequence is further elongated as in
      Gal beta 1----4GlcNAc beta 1----3Gal beta 1----4GlcNAc beta-O-Me, and (e)
      lacto-N-tetraose has no inhibitory activity with any of the anti-i or anti-I
      antibodies tested.
FAU - Gooi, H C
AU  - Gooi HC
FAU - Veyrieres, A
AU  - Veyrieres A
FAU - Alais, J
AU  - Alais J
FAU - Scudder, P
AU  - Scudder P
FAU - Hounsell, E F
AU  - Hounsell EF
FAU - Feizi, T
AU  - Feizi T
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - Mol Immunol
JT  - Molecular immunology
JID - 7905289
RN  - 0 (Amino Sugars)
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Blood Group Antigens)
RN  - 0 (Epitopes)
RN  - 0 (Glycoproteins)
RN  - 0 (I Blood-Group System)
RN  - 0 (Methylglycosides)
RN  - 0 (Oligosaccharides)
RN  - 3Y5B2K5OOK (N-acetyllactosamine)
RN  - BY63N40B1L (lacto-N-neotetraose)
SB  - IM
MH  - Amino Sugars/immunology
MH  - Antibodies, Monoclonal/*immunology
MH  - Antibody Specificity
MH  - Binding Sites, Antibody
MH  - Binding, Competitive
MH  - Blood Group Antigens/*immunology
MH  - Epitopes/immunology
MH  - Glycoproteins/immunology
MH  - Humans
MH  - I Blood-Group System/*immunology
MH  - Methylglycosides/immunology
MH  - Oligosaccharides/immunology
MH  - Structure-Activity Relationship
EDAT- 1984/11/01 00:00
MHDA- 1984/11/01 00:01
CRDT- 1984/11/01 00:00
PHST- 1984/11/01 00:00 [pubmed]
PHST- 1984/11/01 00:01 [medline]
PHST- 1984/11/01 00:00 [entrez]
PST - ppublish
SO  - Mol Immunol. 1984 Nov;21(11):1099-104.

PMID- 11072212
OWN - NLM
STAT- MEDLINE
DCOM- 20001222
LR  - 20061115
IS  - 0959-8049 (Print)
IS  - 0959-8049 (Linking)
VI  - 36
IP  - 17
DP  - 2000 Nov
TI  - Cervical cancer screening in Luxembourg.
PG  - 2240-3
AB  - In 1962, a programme for early detection of cervical cancer was established at
      the national level. The programme is based on the collaboration of different
      groups of doctors and not on a system of sending out invitations to every woman. 
      This programme was re-adapted twice according to the needs for assuring quality
      in a system of mainly liberal medicine. At present the programme is
      'institutionalised' and is carried out according to the criteria defined in 1990.
      This includes a centralisation of the smear readings and handing out the material
      needed to take the smears. The contribution of the doctors is regulated by a
      system of bonuses given by the government and a reimbursement by the Health Fund.
      The annual cervical smear is free of charge for every woman. The participation of
      the women targeted by the programme (>15 years old) has increased by
      approximately 50% every decade from the early 1970s increasing from 10950 in 1972
      to 70441 in 1999. Between 1980 and 1999, the number of women at risk taking part 
      in the programme increased from 10.80 to 38.92%. The number of all the doctors
      taking smear samples increased from 68 to 105 and the number of gynaecologists
      increased from 19 (ratio Gyn/GP (gynaecologists/General Practitioners) of 28%) to
      52 (ratio Gyn/GP of 50%). The mortality rate has decreased continuously from 6.
      1/100000 in 1990 to 0.9/100000 in 1997. In conclusion, to be successful, a
      cervical cancer screening programme should be flexible enough to allow short-term
      adaptations to unexpected local situations and needs a highly motivated team of
      the different participants involved in the regional and national health policy.
FAU - Scheiden, R
AU  - Scheiden R
AD  - Division of Clinical Cytology, National Health Laboratory, 1 rue Auguste Lumiere,
      L-1950, Luxembourg. pathologie@lns.etat.lu
FAU - Knolle, U
AU  - Knolle U
FAU - Wagener, C
AU  - Wagener C
FAU - Wehenkel, A M
AU  - Wehenkel AM
FAU - Capesius, C
AU  - Capesius C
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - Eur J Cancer
JT  - European journal of cancer (Oxford, England : 1990)
JID - 9005373
SB  - IM
MH  - Data Collection/methods
MH  - Female
MH  - Health Personnel
MH  - Humans
MH  - Luxembourg
MH  - Mass Screening/*organization & administration/standards
MH  - Program Evaluation
MH  - Quality Assurance, Health Care/organization & administration
MH  - Risk Factors
MH  - Uterine Cervical Neoplasms/*prevention & control
EDAT- 2000/11/10 11:00
MHDA- 2001/02/28 10:01
CRDT- 2000/11/10 11:00
PHST- 2000/11/10 11:00 [pubmed]
PHST- 2001/02/28 10:01 [medline]
PHST- 2000/11/10 11:00 [entrez]
AID - S0959-8049(00)00323-3 [pii]
PST - ppublish
SO  - Eur J Cancer. 2000 Nov;36(17):2240-3.

PMID- 2420639
OWN - NLM
STAT- MEDLINE
DCOM- 19860507
LR  - 20061115
IS  - 0014-5793 (Print)
IS  - 0014-5793 (Linking)
VI  - 198
IP  - 1
DP  - 1986 Mar 17
TI  - Differential expression of fucosyl GM1 and a disialoganglioside with a NeuAc
      alpha 2-6GalNAc linkage (GD1e) in various rat ascites hepatoma cells.
PG  - 66-70
AB  - A distinct difference in ganglioside composition among various rat ascites
      hepatomas and Yoshida sarcoma was observed on TLC-immunostaining with
      anti-fucosyl GM1 antibody, and chemical and enzymatic analyses. Yoshida sarcoma
      and ascites hepatomas, AH13, AH66F and AH66, but not the other 9 tumor cell lines
      investigated, specifically contained a disialoganglioside, NeuAc alpha 2-3Gal
      beta 1-3(NeuAc alpha 2-6)GalNAc beta 1-4Gal beta 1-4Glc beta 1-1ceramide (GD1e), 
      whereas the 9 ascites hepatoma cells without GD1e contained fucosyl GM1. The
      differential expression of fucosyl GM1 and GD1e in various tumor cell lines
      indicates that different cell lineages express distinct metabolic pathways for
      gangliosides, and that the gangliosides are useful markers for distinguishing
      tumor cell lines.
FAU - Iwamori, M
AU  - Iwamori M
FAU - Sunada, S
AU  - Sunada S
FAU - Ishihara, E
AU  - Ishihara E
FAU - Moki, M
AU  - Moki M
FAU - Fujimoto, S
AU  - Fujimoto S
FAU - Nagai, Y
AU  - Nagai Y
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - FEBS Lett
JT  - FEBS letters
JID - 0155157
RN  - 0 (Gangliosides)
RN  - 37758-47-7 (G(M1) Ganglioside)
RN  - 71812-11-8 (fucosyl GM1 ganglioside)
SB  - IM
MH  - Animals
MH  - Cell Line
MH  - Chromatography, Thin Layer
MH  - G(M1) Ganglioside/*analogs & derivatives/analysis/immunology
MH  - Gangliosides/*analysis/metabolism
MH  - Liver Neoplasms, Experimental/*analysis
MH  - Rats
MH  - Sarcoma, Yoshida/analysis
MH  - Staining and Labeling
EDAT- 1986/03/17 00:00
MHDA- 1986/03/17 00:01
CRDT- 1986/03/17 00:00
PHST- 1986/03/17 00:00 [pubmed]
PHST- 1986/03/17 00:01 [medline]
PHST- 1986/03/17 00:00 [entrez]
PST - ppublish
SO  - FEBS Lett. 1986 Mar 17;198(1):66-70.

PMID- 1955453
OWN - NLM
STAT- MEDLINE
DCOM- 19911227
LR  - 20190508
IS  - 0021-9525 (Print)
IS  - 0021-9525 (Linking)
VI  - 115
IP  - 4
DP  - 1991 Nov
TI  - Subcellular localization of Forssman glycolipid in epithelial MDCK cells by
      immuno-electronmicroscopy after freeze-substitution.
PG  - 1009-19
AB  - Forssman antigen, a neutral glycosphingolipid carrying five monosaccharides, was 
      localized in epithelial MDCK cells by the immunogold technique. Labeling with a
      well defined mAb and protein A-gold after freeze-substitution and low temperature
      embedding in Lowicryl HM20 of aldehyde-fixed and cryoprotected cells, resulted in
      high levels of specific labeling and excellent retention of cellular
      ultrastructure compared to ultra-thin cryosections. No Forssman glycolipid was
      lost from the cells during freeze-substitution as measured by
      radio-immunostaining of lipid extracts. Redistribution of the glycolipid between 
      membranes did not occur. Forssman glycolipid, abundantly expressed on the surface
      of MDCK II cells, did not move to neighboring cell surfaces in cocultures with
      Forssman negative MDCK I cells, even though they were connected by tight
      junctions. The labeling density on the apical plasma membrane was 1.4-1.6 times
      higher than basolateral. Roughly two-thirds of the gold particles were found
      intracellularly. The Golgi complex was labeled for Forssman as were endosomes,
      identified by endocytosed albumin-gold, and lysosomes, defined by double labeling
      for cathepsin D. In most cases, the nuclear envelope was Forssman positive, but
      the labeling density was 10-fold less than on the plasma membrane. Mitochondria
      and peroxisomes, the latter identified by catalase, remained free of label,
      consistent with the notion that they do not receive transport vesicles carrying
      glycosphingolipids. The present method of lipid immunolabeling holds great
      potential for the localization of other antigenic lipids.
FAU - van Genderen, I L
AU  - van Genderen IL
AD  - Department of Cell Biology, Medical School, University of Utrecht, The
      Netherlands.
FAU - van Meer, G
AU  - van Meer G
FAU - Slot, J W
AU  - Slot JW
FAU - Geuze, H J
AU  - Geuze HJ
FAU - Voorhout, W F
AU  - Voorhout WF
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - J Cell Biol
JT  - The Journal of cell biology
JID - 0375356
RN  - 0 (Antigens, Surface)
RN  - 9013-60-9 (Forssman Antigen)
SB  - IM
MH  - Animals
MH  - Antigens, Surface/analysis
MH  - Cell Line
MH  - Epithelium/chemistry/ultrastructure
MH  - Forssman Antigen/*analysis/immunology
MH  - Freezing
MH  - Immunohistochemistry
MH  - Intercellular Junctions/chemistry
MH  - Microscopy, Immunoelectron
PMC - PMC2289941
EDAT- 1991/11/01 00:00
MHDA- 1991/11/01 00:01
CRDT- 1991/11/01 00:00
PHST- 1991/11/01 00:00 [pubmed]
PHST- 1991/11/01 00:01 [medline]
PHST- 1991/11/01 00:00 [entrez]
AID - 10.1083/jcb.115.4.1009 [doi]
PST - ppublish
SO  - J Cell Biol. 1991 Nov;115(4):1009-19. doi: 10.1083/jcb.115.4.1009.

PMID- 1520302
OWN - NLM
STAT- MEDLINE
DCOM- 19921007
LR  - 20131121
IS  - 0006-291X (Print)
IS  - 0006-291X (Linking)
VI  - 187
IP  - 1
DP  - 1992 Aug 31
TI  - Cancer-associated glycoproteins defined by a monoclonal antibody, MLS 128,
      recognizing the Tn antigen.
PG  - 217-24
AB  - A murine monoclonal antibody, MLS 128, recognizing the Tn antigen, was
      established and used for characterization of glycoproteins expressing the Tn
      antigen. The Tn antigen was expressed on three polypeptide chains with molecular 
      weights of 250k, 210k and 150k daltons. LS 180 cells were labeled with
      3H-glucosamine or 35S-sulfate metabolically, and then the immunoprecipitate
      derived from the cell lysate was subjected to SDS-PAGE followed by fluorography. 
      It was revealed that these Tn antigen glycoproteins were produced through the
      processing of a high molecular weight precursor. The carbohydrate moieties of the
      Tn antigen glycoproteins labeled with 3H-glucosamine were released with
      alkaline-borohydride, and the released sugars were examined by gel filtration and
      paper chromatography. The carbohydrates predominantly consisted of GalNAc and
      sialyl GalNAc (greater than 90%), with a nearly equal distribution.
FAU - Nakada, H
AU  - Nakada H
AD  - Department of Biotechnology, Faculty of Engineering, Kyoto Sangyo University,
      Japan.
FAU - Inoue, M
AU  - Inoue M
FAU - Numata, Y
AU  - Numata Y
FAU - Tanaka, N
AU  - Tanaka N
FAU - Funakoshi, I
AU  - Funakoshi I
FAU - Fukui, S
AU  - Fukui S
FAU - Yamashina, I
AU  - Yamashina I
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Biochem Biophys Res Commun
JT  - Biochemical and biophysical research communications
JID - 0372516
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens, Neoplasm)
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Glycoproteins)
RN  - 0 (Neoplasm Proteins)
RN  - 0 (Oligosaccharides)
RN  - 0 (Tn antigen)
RN  - N08U5BOQ1K (Glucosamine)
SB  - IM
MH  - *Antibodies, Monoclonal
MH  - Antigens, Neoplasm/*immunology
MH  - *Antigens, Tumor-Associated, Carbohydrate
MH  - Blotting, Western
MH  - Carbohydrate Conformation
MH  - Chromatography
MH  - Electrophoresis, Polyacrylamide Gel
MH  - Glucosamine
MH  - Glycoproteins/*immunology/isolation & purification
MH  - Immunosorbent Techniques
MH  - Molecular Weight
MH  - Neoplasm Proteins/*immunology
MH  - Oligosaccharides/isolation & purification
MH  - Tumor Cells, Cultured
EDAT- 1992/08/31 00:00
MHDA- 1992/08/31 00:01
CRDT- 1992/08/31 00:00
PHST- 1992/08/31 00:00 [pubmed]
PHST- 1992/08/31 00:01 [medline]
PHST- 1992/08/31 00:00 [entrez]
AID - S0006-291X(05)81481-0 [pii]
PST - ppublish
SO  - Biochem Biophys Res Commun. 1992 Aug 31;187(1):217-24.

PMID- 7819038
OWN - NLM
STAT- MEDLINE
DCOM- 19950216
LR  - 20190515
IS  - 0007-0920 (Print)
IS  - 0007-0920 (Linking)
VI  - 71
IP  - 1
DP  - 1995 Jan
TI  - Correlation between sialyl Tn antigen and lymphatic metastasis in patients with
      Borrmann type IV gastric carcinoma.
PG  - 191-5
AB  - The expression of sialyl Tn (STn) antigen in 180 patients with Borrmann type IV
      gastric carcinomas was examined immunohistochemically. The rate of positive STn
      staining was 32% (57/180) for the primary tumours, and this positive staining
      correlated well with tumour extension, lymph node metastasis (P < 0.05) and
      peritoneal dissemination (P < 0.01). One-third (5/15) of patients with positive
      STn-staining cancer cells had a high level of serum STn. Lesions with positive
      STn staining were related to a lower survival rate for the patients (P < 0.05).
      Proliferative activity of the tumour, as measured by proliferating nuclear
      antigen (PCNA) labelling percentage and argyrophilic nucleolar organiser region
      (AgNOR) count, was significantly higher (41.5 +/- 13.0%, 3.78 +/- 0.98) in the
      STn-positive group than in the STn-negative group (34.2 +/- 13.2%, 3.48 +/- 0.85)
      (P < 0.01, P < 0.05 respectively). Estimating STn antigen may be useful for
      predicting the likelihood of lymph node metastasis or peritoneal dissemination
      and the clinical prognosis for patients with Borrmann type IV gastric carcinoma.
FAU - Kakeji, Y
AU  - Kakeji Y
AD  - Department of Gastroenterologic Surgery, National Kyushu Cancer Center, Fukuoka, 
      Japan.
FAU - Maehara, Y
AU  - Maehara Y
FAU - Morita, M
AU  - Morita M
FAU - Matsukuma, A
AU  - Matsukuma A
FAU - Furusawa, M
AU  - Furusawa M
FAU - Takahashi, I
AU  - Takahashi I
FAU - Kusumoto, T
AU  - Kusumoto T
FAU - Ohno, S
AU  - Ohno S
FAU - Sugimachi, K
AU  - Sugimachi K
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - Br J Cancer
JT  - British journal of cancer
JID - 0370635
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Biomarkers, Tumor)
RN  - 0 (sialosyl-Tn antigen)
SB  - IM
MH  - Adult
MH  - Aged
MH  - Antigens, Tumor-Associated, Carbohydrate/*analysis
MH  - Biomarkers, Tumor/*analysis
MH  - Cell Division
MH  - Female
MH  - Humans
MH  - Lymphatic Metastasis
MH  - Male
MH  - Middle Aged
MH  - Prognosis
MH  - Stomach Neoplasms/*chemistry/mortality/pathology
MH  - Survival Rate
PMC - PMC2033471
EDAT- 1995/01/01 00:00
MHDA- 1995/01/01 00:01
CRDT- 1995/01/01 00:00
PHST- 1995/01/01 00:00 [pubmed]
PHST- 1995/01/01 00:01 [medline]
PHST- 1995/01/01 00:00 [entrez]
AID - 10.1038/bjc.1995.39 [doi]
PST - ppublish
SO  - Br J Cancer. 1995 Jan;71(1):191-5. doi: 10.1038/bjc.1995.39.

PMID- 2837767
OWN - NLM
STAT- MEDLINE
DCOM- 19880725
LR  - 20190501
IS  - 0027-8424 (Print)
IS  - 0027-8424 (Linking)
VI  - 85
IP  - 12
DP  - 1988 Jun
TI  - Recognition of galactosylgloboside by monoclonal antibodies derived from patients
      with primary lung cancer.
PG  - 4441-5
AB  - Lymph node lymphocytes from patients with primary lung cancer were immortalized
      with Epstein-Barr virus, and culture supernatants were screened for cell-surface 
      reactivity against allogeneic cancer cell lines. The percentage of wells
      containing detectable antibodies in initial screening ranged from 1 to 17%, but
      the vast majority of the cultures lost antibody activity on subsequent expansion.
      Two antibody-secreting clones, J309 and D579, derived from separate individuals
      and reactive with anaplastic lung cancer cell lines, were successfully expanded
      and fused with the NS-1 mouse myeloma cell line. The antibodies produced by these
      clones exhibited identical restricted serologic reactivity against cultured cell 
      lines and detected a carbohydrate antigen present in the neutral glycolipid
      fraction of MCF-7 breast cancer cells. Serologic, immunochemical, and chemical
      analyses revealed that the antigen recognized by antibodies J309 and D579 is
      galactosylgloboside [Gal(beta 1----3)GalNAc(beta 1----3)Gal(alpha 1----4)Gal(beta
      1----4)- GlcCer]. Conclusions regarding the significance of these findings with
      respect to the biology of lung cancer await further information concerning the
      distribution of galactosylgloboside in normal and malignant tissues and the
      frequency of antibodies to this structure in normal and tumor-bearing
      individuals.
FAU - Schrump, D S
AU  - Schrump DS
AD  - Memorial Sloan-Kettering Cancer Center, New York, NY 10021.
FAU - Furukawa, K
AU  - Furukawa K
FAU - Yamaguchi, H
AU  - Yamaguchi H
FAU - Lloyd, K O
AU  - Lloyd KO
FAU - Old, L J
AU  - Old LJ
LA  - eng
GR  - CA-08748/CA/NCI NIH HHS/United States
GR  - CA-09149-12/CA/NCI NIH HHS/United States
GR  - CA-47427/CA/NCI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Proc Natl Acad Sci U S A
JT  - Proceedings of the National Academy of Sciences of the United States of America
JID - 7505876
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens, Neoplasm)
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Carbohydrates)
RN  - 0 (Globosides)
RN  - 0 (Glycosphingolipids)
RN  - 0 (Stage-Specific Embryonic Antigens)
RN  - 0 (stage-specific embryonic antigen-3)
RN  - EC 3.2.1.- (Glycoside Hydrolases)
SB  - IM
MH  - *Antibodies, Monoclonal
MH  - Antigens, Neoplasm/*immunology
MH  - Antigens, Tumor-Associated, Carbohydrate
MH  - Carbohydrate Conformation
MH  - Carbohydrate Sequence
MH  - Carbohydrates/analysis
MH  - Carcinoma, Small Cell/*immunology
MH  - Globosides/analysis/*immunology
MH  - Glycoside Hydrolases
MH  - Glycosphingolipids/*immunology
MH  - Humans
MH  - Lung Neoplasms/*immunology
MH  - Lymphocytes/*immunology
MH  - Stage-Specific Embryonic Antigens
PMC - PMC280445
EDAT- 1988/06/01 00:00
MHDA- 1988/06/01 00:01
CRDT- 1988/06/01 00:00
PHST- 1988/06/01 00:00 [pubmed]
PHST- 1988/06/01 00:01 [medline]
PHST- 1988/06/01 00:00 [entrez]
AID - 10.1073/pnas.85.12.4441 [doi]
PST - ppublish
SO  - Proc Natl Acad Sci U S A. 1988 Jun;85(12):4441-5. doi: 10.1073/pnas.85.12.4441.

PMID- 11551197
OWN - NLM
STAT- MEDLINE
DCOM- 20011018
LR  - 20121115
IS  - 0006-2960 (Print)
IS  - 0006-2960 (Linking)
VI  - 40
IP  - 37
DP  - 2001 Sep 18
TI  - Differential activity and structure of highly similar peroxidases. Spectroscopic,
      crystallographic, and enzymatic analyses of lignifying Arabidopsis thaliana
      peroxidase A2 and horseradish peroxidase A2.
PG  - 11013-21
AB  - Anionic Arabidopsis thaliana peroxidase ATP A2 was expressed in Escherichia coli 
      and used as a model for the 95% identical commercially available horseradish
      peroxidase HRP A2. The crystal structure of ATP A2 at 1.45 A resolution at 100 K 
      showed a water molecule only 2.1 A from heme iron [Ostergaard, L., et al. (2000) 
      Plant Mol. Biol. 44, 231-243], whereas spectroscopic studies of HRP A2 in
      solution at room temperature [Feis, A., et al. (1998) J. Raman Spectrosc. 29,
      933-938] showed five-coordinated heme iron, which is common in peroxidases.
      Presented here, the X-ray crystallographic, single-crystal, and solution
      resonance Raman studies at room temperature confirmed that the sixth coordination
      position of heme iron of ATP A2 is essentially vacant. Furthermore, electronic
      absorption and resonance Raman spectroscopy showed that the heme environments of 
      recombinant ATP A2 and glycosylated plant HRP A2 are indistinguishable at neutral
      and alkaline pH, from room temperature to 12 K, and are highly flexible compared 
      with other plant peroxidases. Ostergaard et al. (2000) also demonstrated that ATP
      A2 expression and lignin formation coincide in Arabidopsis tissues, and docking
      of lignin precursors into the substrate binding site of ATP A2 predicted that
      coniferyl and p-coumaryl alcohols were good substrates. In contrast, the
      additional methoxy group of the sinapyl moiety gave rise to steric hindrance, not
      only in A2 type peroxidases but also in all peroxidases. We confirm these
      predictions for ATP A2, HRP A2, and HRP C. The specific activity of ATP A2 was
      lower than that of HRP A2 (pH 4-8), although a steady-state study at pH 5
      demonstrated very little difference in their rate constants for reaction with
      H2O2 (k1 = 1.0 microM(-1) x s(-1). The oxidation of coniferyl alcohol, ferulic,
      p-coumaric, and sinapic acids by HRP A2, and ATP A2, however, gave modest but
      significantly different k3 rate constants of 8.7 +/- 0.3, 4.0 +/- 0.2, 0.70 +/-
      0.03, and 0.04 +/- 0.2 microM(-1) x s(-1) for HRP A2, respectively, and 4.6 +/-
      0.2, 2.3 +/- 0.1, 0.25 +/- 0.01, and 0.01 +/- 0.004 microM(-1) x s(-1) for ATP
      A2, respectively. The structural origin of the differential reactivity is
      discussed in relation to glycosylation and amino acid substitutions. The results 
      are of general importance to the use of homologous models and structure
      determination at low temperatures.
FAU - Nielsen, K L
AU  - Nielsen KL
AD  - Institut for Bioteknologi, Aalborg Universitet, Sohngaardsholmsvej 49, DK-9000
      Aalborg, Denmark.
FAU - Indiani, C
AU  - Indiani C
FAU - Henriksen, A
AU  - Henriksen A
FAU - Feis, A
AU  - Feis A
FAU - Becucci, M
AU  - Becucci M
FAU - Gajhede, M
AU  - Gajhede M
FAU - Smulevich, G
AU  - Smulevich G
FAU - Welinder, K G
AU  - Welinder KG
LA  - eng
SI  - PDB/1Q04
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Biochemistry
JT  - Biochemistry
JID - 0370623
RN  - 0 (Coumaric Acids)
RN  - 0 (Phenols)
RN  - 0 (Plant Proteins)
RN  - 0 (Recombinant Proteins)
RN  - E7SM92591P (coniferyl alcohol)
RN  - EC 1.11.1.- (Horseradish Peroxidase)
RN  - EC 1.11.1.- (Peroxidases)
RN  - EC 1.11.1.- (lignin-forming peroxidase)
RN  - EC 1.11.1.7 (anionic peroxidase)
SB  - IM
MH  - Arabidopsis/enzymology
MH  - Catalytic Domain
MH  - Coumaric Acids/metabolism
MH  - Crystallography, X-Ray
MH  - Horseradish Peroxidase/chemistry/classification/metabolism
MH  - Models, Molecular
MH  - Peroxidases/*chemistry/classification/metabolism
MH  - Phenols/metabolism
MH  - Plant Proteins/chemistry/classification/metabolism
MH  - Recombinant Proteins
MH  - Spectrum Analysis, Raman
MH  - Substrate Specificity
EDAT- 2001/09/12 10:00
MHDA- 2001/10/19 10:01
CRDT- 2001/09/12 10:00
PHST- 2001/09/12 10:00 [pubmed]
PHST- 2001/10/19 10:01 [medline]
PHST- 2001/09/12 10:00 [entrez]
AID - bi010661o [pii]
PST - ppublish
SO  - Biochemistry. 2001 Sep 18;40(37):11013-21.

PMID- 18690650
OWN - NLM
STAT- MEDLINE
DCOM- 20081216
LR  - 20121115
IS  - 1615-9861 (Electronic)
IS  - 1615-9853 (Linking)
VI  - 8
IP  - 16
DP  - 2008 Aug
TI  - Mucin-induced apoptosis of monocyte-derived dendritic cells during maturation.
PG  - 3342-9
LID - 10.1002/pmic.200800039 [doi]
AB  - Many tumors arising from epithelial tissues produce mucins, which readily come
      into contact with infiltrating cells in cancer tissues. MUC2 mucins were purified
      from the conditioned medium of a colorectal cancer cell line, LS180 cells. It is 
      known that in cancer patients, the number of dendritic cells (DCs) is reduced and
      their function is impaired. Mature DCs were generated from human peripheral blood
      monocytes through successive treatments with GM-CSF and IL-4, and then with
      proinflammatory mediators. When monocytes were cultured in the presence of MUC2
      mucins in addition to GM-CSF and IL-4 at an early stage of development, mature
      DCs expressing CD83 decreased and apoptotic cells increased in a dose-dependent
      manner. During the development of DCs, sialic acid-binding Ig-like lectin
      (Siglec)-3 was constantly expressed. We prepared recombinant soluble Siglec-3
      corresponding to the ectodomain of Siglec-3 and confirmed the binding of soluble 
      Siglec-3 to the MUC2 mucins, probably through alpha2,6-sialic acid-containing
      O-glycans including a sialyl Tn antigen, which is known to bind to Siglec-3.
      Apoptosis was partially inhibited by anti-Siglec-3 mAb or recombinant soluble
      Siglec-3. These results suggest that apoptosis was partially induced through the 
      ligation of the MUC2 mucins with Siglec-3.
FAU - Ishida, Akiko
AU  - Ishida A
AD  - Department of Biotechnology, Faculty of Engineering, Kyoto Sangyo University,
      Kyoto, Japan.
FAU - Ohta, Mariko
AU  - Ohta M
FAU - Toda, Munetoyo
AU  - Toda M
FAU - Murata, Takeomi
AU  - Murata T
FAU - Usui, Taichi
AU  - Usui T
FAU - Akita, Kaoru
AU  - Akita K
FAU - Inoue, Mizue
AU  - Inoue M
FAU - Nakada, Hiroshi
AU  - Nakada H
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - Germany
TA  - Proteomics
JT  - Proteomics
JID - 101092707
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Lectins)
RN  - 0 (Mucin-2)
RN  - 0 (Recombinant Proteins)
RN  - 0 (Sialic Acid Binding Immunoglobulin-like Lectins)
RN  - 207137-56-2 (Interleukin-4)
RN  - 83869-56-1 (Granulocyte-Macrophage Colony-Stimulating Factor)
SB  - IM
MH  - Antibodies, Monoclonal/pharmacology
MH  - Apoptosis/*drug effects
MH  - Cell Differentiation/drug effects
MH  - Cell Line, Tumor
MH  - Dendritic Cells/cytology/*drug effects
MH  - Flow Cytometry
MH  - Granulocyte-Macrophage Colony-Stimulating Factor/pharmacology
MH  - Humans
MH  - Interleukin-4/pharmacology
MH  - Lectins/genetics/immunology/metabolism
MH  - Monocytes/cytology/*drug effects
MH  - Mucin-2/metabolism/*pharmacology
MH  - Protein Binding
MH  - Recombinant Proteins/metabolism/pharmacology
MH  - Sialic Acid Binding Immunoglobulin-like Lectins
MH  - U937 Cells
EDAT- 2008/08/12 09:00
MHDA- 2008/12/17 09:00
CRDT- 2008/08/12 09:00
PHST- 2008/08/12 09:00 [pubmed]
PHST- 2008/12/17 09:00 [medline]
PHST- 2008/08/12 09:00 [entrez]
AID - 10.1002/pmic.200800039 [doi]
PST - ppublish
SO  - Proteomics. 2008 Aug;8(16):3342-9. doi: 10.1002/pmic.200800039.

PMID- 9697259
OWN - NLM
STAT- MEDLINE
DCOM- 19981014
LR  - 20181113
IS  - 0941-1291 (Print)
IS  - 0941-1291 (Linking)
VI  - 28
IP  - 7
DP  - 1998
TI  - Sialyl-Tn antigen as a useful predictor of poor prognosis in patients with
      advanced stomach cancer.
PG  - 682-6
AB  - Sialyl-Tn antigen (STn) expression was studied immunohistochemically in 211
      primary advanced gastric carcinomas. The overall rate of positive STn staining
      was 17% (35/211), and positive STn staining was found not to be correlated with
      tumor size, depth of invasion, lymph node metastasis, liver metastasis, or
      peritoneal metastasis. However, patients with tumors that were immunoreactive for
      STn demonstrated significantly lower survival (P < 0.05). Multivariate analysis
      revealed that STn staining was an independent prognostic factor. From these
      findings we conclude that careful followup and intense postoperative therapy are 
      required for patients with advanced gastric cancer who have positive
      immunoreactivity for STn.
FAU - Terashima, S
AU  - Terashima S
AD  - First Department of Surgery, Fukushima Medical School, Japan.
FAU - Takano, Y
AU  - Takano Y
FAU - Ohori, T
AU  - Ohori T
FAU - Kanno, T
AU  - Kanno T
FAU - Kimura, T
AU  - Kimura T
FAU - Motoki, R
AU  - Motoki R
FAU - Kawaguchi, T
AU  - Kawaguchi T
LA  - eng
PT  - Journal Article
PL  - Japan
TA  - Surg Today
JT  - Surgery today
JID - 9204360
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Biomarkers, Tumor)
RN  - 0 (sialosyl-Tn antigen)
SB  - IM
MH  - Adult
MH  - Aged
MH  - Aged, 80 and over
MH  - Antigens, Tumor-Associated, Carbohydrate/*analysis
MH  - Biomarkers, Tumor/*analysis
MH  - Female
MH  - Humans
MH  - Immunohistochemistry
MH  - Male
MH  - Middle Aged
MH  - Neoplasm Invasiveness
MH  - Prognosis
MH  - Stomach Neoplasms/*immunology/pathology
MH  - Survival Analysis
EDAT- 1998/08/11 00:00
MHDA- 1998/08/11 00:01
CRDT- 1998/08/11 00:00
PHST- 1998/08/11 00:00 [pubmed]
PHST- 1998/08/11 00:01 [medline]
PHST- 1998/08/11 00:00 [entrez]
AID - 10.1007/BF02484612 [pii]
AID - 10.1007/BF02484612 [doi]
PST - ppublish
SO  - Surg Today. 1998;28(7):682-6. doi: 10.1007/BF02484612.

PMID- 8261467
OWN - NLM
STAT- MEDLINE
DCOM- 19940121
LR  - 20171116
IS  - 0008-5472 (Print)
IS  - 0008-5472 (Linking)
VI  - 54
IP  - 1
DP  - 1994 Jan 1
TI  - Tn antigen is expressed on leukosialin from T-lymphoid cells.
PG  - 85-8
AB  - Various T-lymphoid cells were labeled with [3H] glucosamine and then cell lysates
      were prepared from them. The Tn antigen was immunoprecipitated and analyzed by
      sodium dodecyl sulfate-polyacrylamide gel electrophoresis followed by
      fluorography. The Tn antigen was found to be expressed on leukosialin, a major
      glycoprotein of T-lymphoid cells. The carbohydrate moieties of leukosialin were
      isolated from Jurkat and Molt 4 cells by alkaline borohydride treatment. The
      leukosialin in both cases predominantly contained single N-acetylgalactosamine
      residues, consistent with expression of the Tn antigen. Tryptic glycopeptides
      containing antigenic sites were isolated using an MLS 128 immunoaffinity column
      and purified by gel filtration and reverse phase column chromatographies.
      Sequence analyses revealed that all the glycopeptides obtained contained three
      consecutive residues of N-acetylgalactosamine-Ser/Thr, supporting the idea that
      the epitopic structure is a cluster of N-acetylgalactosamine-Ser/Thr.
FAU - Inoue, M
AU  - Inoue M
AD  - Department of Biotechnology, Faculty of Engineering, Kyoto Sangyo University,
      Kyoto, Japan.
FAU - Nakada, H
AU  - Nakada H
FAU - Tanaka, N
AU  - Tanaka N
FAU - Yamashina, I
AU  - Yamashina I
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Cancer Res
JT  - Cancer research
JID - 2984705R
RN  - 0 (Antigens, CD)
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Leukosialin)
RN  - 0 (Polysaccharides)
RN  - 0 (Sialoglycoproteins)
RN  - 0 (Tn antigen)
RN  - 0 (UN1 sialoglycoprotein, human)
RN  - EC 2.4.1.- (Galactosyltransferases)
SB  - IM
MH  - *Antigens, CD
MH  - Antigens, Tumor-Associated, Carbohydrate/*analysis
MH  - Cell Line
MH  - Galactosyltransferases/analysis
MH  - Humans
MH  - Leukosialin
MH  - Polysaccharides/analysis
MH  - Sialoglycoproteins/*chemistry/immunology
MH  - T-Lymphocytes/*chemistry/immunology
EDAT- 1994/01/01 00:00
MHDA- 1994/01/01 00:01
CRDT- 1994/01/01 00:00
PHST- 1994/01/01 00:00 [pubmed]
PHST- 1994/01/01 00:01 [medline]
PHST- 1994/01/01 00:00 [entrez]
PST - ppublish
SO  - Cancer Res. 1994 Jan 1;54(1):85-8.

PMID- 1419648
OWN - NLM
STAT- MEDLINE
DCOM- 19921215
LR  - 20190515
IS  - 0007-0920 (Print)
IS  - 0007-0920 (Linking)
VI  - 66
IP  - 5
DP  - 1992 Nov
TI  - Sialyl Tn as a prognostic marker in epithelial ovarian cancer.
PG  - 984-5
FAU - Kobayashi, H
AU  - Kobayashi H
FAU - Terao, T
AU  - Terao T
FAU - Kawashima, Y
AU  - Kawashima Y
LA  - eng
PT  - Letter
PL  - England
TA  - Br J Cancer
JT  - British journal of cancer
JID - 0370635
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Biomarkers, Tumor)
RN  - 0 (sialosyl-Tn antigen)
SB  - IM
MH  - Antigens, Tumor-Associated, Carbohydrate/*blood
MH  - Biomarkers, Tumor/*blood
MH  - Epithelium/pathology
MH  - Female
MH  - Humans
MH  - Multivariate Analysis
MH  - Ovarian Neoplasms/blood/*immunology/mortality
MH  - Prognosis
PMC - PMC1977998
EDAT- 1992/11/01 00:00
MHDA- 1992/11/01 00:01
CRDT- 1992/11/01 00:00
PHST- 1992/11/01 00:00 [pubmed]
PHST- 1992/11/01 00:01 [medline]
PHST- 1992/11/01 00:00 [entrez]
AID - 10.1038/bjc.1992.397 [doi]
PST - ppublish
SO  - Br J Cancer. 1992 Nov;66(5):984-5. doi: 10.1038/bjc.1992.397.

PMID- 2422274
OWN - NLM
STAT- MEDLINE
DCOM- 19860613
LR  - 20071114
IS  - 0022-1767 (Print)
IS  - 0022-1767 (Linking)
VI  - 136
IP  - 11
DP  - 1986 Jun 1
TI  - A human monoclonal antibody directed to blood group i antigen: heterohybridoma
      between human lymphocytes from regional lymph nodes of a lung cancer patient and 
      mouse myeloma.
PG  - 4163-8
AB  - A fusion of human lymphocytes released from regional lymph nodes of papillary
      adenocarcinoma of lung cancer with mouse myeloma P3-X63-Ag8-U1 cells resulted in 
      a stable hybridoma-secreting human IgM antibody (NCC-1004) that reacts with a
      large proportion of squamous cell carcinomas of lung and esophagus as well as
      carcinoma of thyroid glands. However, the antibody also reacts with normal red
      blood cells, B lymphocytes, and a few other limited loci in normal tissues such
      as the basal cells of bronchial epithelium and the basal cell layer of stratified
      squamous epithelium, as well as endothelium and alveolar lining epithelium. The
      antigen defined by NCC-1004 has been characterized as blood group i antigen on
      the basis of the following results. The antibody preferentially agglutinates cord
      erythrocytes in contrast to adult erythrocytes. The agglutination was obvious at 
      4 degrees C, but diminished greatly at 37 degrees C, and was enhanced after
      sialidase treatment. The antibody specifically reacts with
      lacto-norhexaosylceramide (nLc6) and sialosyllacto-norhexaosylceramide
      (IV3NeuAcnLc6), but does not react with lacto-neotetraosylceramide (nLc4),
      sialosyllacto-neotetraosylceramide (IV3NeuAcnLc4), lacto-isooctaosylceramide
      (IV6Gal beta 1----4GlcNAcnLc6; I antigen), and other standard glycolipids so far 
      tested. The properties of the antibody and its antigen are identical to those
      previously described for the i blood group system. Inasmuch as the hybridoma was 
      established by hybridization of lymphocytes derived from regional lymph nodes of 
      lung cancer, and the antigen was found in the patient's lung cancer tissue, the i
      antigen in lung cancer is probably recognized as a tumor-associated antigen by
      the host's immune cell system.
FAU - Hirohashi, S
AU  - Hirohashi S
FAU - Clausen, H
AU  - Clausen H
FAU - Nudelman, E
AU  - Nudelman E
FAU - Inoue, H
AU  - Inoue H
FAU - Shimosato, Y
AU  - Shimosato Y
FAU - Hakomori, S
AU  - Hakomori S
LA  - eng
GR  - CA19224/CA/NCI NIH HHS/United States
GR  - GM23100/GM/NIGMS NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - J Immunol
JT  - Journal of immunology (Baltimore, Md. : 1950)
JID - 2985117R
RN  - 0 (Antibodies, Heterophile)
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Blood Group Antigens)
RN  - 0 (Epitopes)
RN  - 0 (I Blood-Group System)
RN  - 0 (Immunoglobulin M)
SB  - AIM
SB  - IM
MH  - Adenocarcinoma, Papillary/*immunology
MH  - Animals
MH  - Antibodies, Heterophile/analysis/biosynthesis
MH  - Antibodies, Monoclonal/*analysis/biosynthesis
MH  - Antibody Specificity
MH  - Blood Group Antigens/*immunology
MH  - Epitopes/immunology
MH  - Female
MH  - Humans
MH  - Hybridomas/*immunology/metabolism
MH  - I Blood-Group System/*immunology
MH  - Immunoglobulin M/biosynthesis
MH  - Lung Neoplasms/*immunology
MH  - Lymph Nodes
MH  - Lymphocytes/immunology/metabolism
MH  - Mice
MH  - Middle Aged
MH  - Plasmacytoma/*immunology
MH  - Staining and Labeling
EDAT- 1986/06/01 00:00
MHDA- 1986/06/01 00:01
CRDT- 1986/06/01 00:00
PHST- 1986/06/01 00:00 [pubmed]
PHST- 1986/06/01 00:01 [medline]
PHST- 1986/06/01 00:00 [entrez]
PST - ppublish
SO  - J Immunol. 1986 Jun 1;136(11):4163-8.

PMID- 3396010
OWN - NLM
STAT- MEDLINE
DCOM- 19880908
LR  - 20041117
IS  - 0008-5472 (Print)
IS  - 0008-5472 (Linking)
VI  - 48
IP  - 16
DP  - 1988 Aug 15
TI  - Generation and characterization of B72.3 second generation monoclonal antibodies 
      reactive with the tumor-associated glycoprotein 72 antigen.
PG  - 4588-96
AB  - Monoclonal antibody (MAb) B72.3 was generated using a membrane-enriched fraction 
      of a human mammary carcinoma biopsy. It has demonstrated reactivity to the
      majority of human adenocarcinomas including colorectal, gastric, pancreatic,
      ovarian, endometrial, mammary, and non-small cell lung cancer and no or weak
      reactivity to normal adult tissues, with the exception of secretory endometrium. 
      The B72.3-reactive antigen, termed tumor-associated glycoprotein (TAG)-72, has
      been purified and used as an immunogen to generate B72.3 second generation MAbs. 
      Since the source of purified TAG-72 was a human colon cancer (CC) xenograft,
      these MAbs have been given a CC designation. Twenty-eight CC MAbs, all
      immunoglobulin Gs, have been generated and shown to be reactive with TAG-72 and
      via both radioimmunoassay and immunohistochemical analyses show differential
      reactivity to carcinoma versus normal adult tissue biopsies. Nine CC MAbs (CC11, 
      15, 29, 30, 40, 46, 49, 83, and 92) were selected for further characterization.
      As a result of analyses using direct-binding radioimmunoassay to a range of human
      carcinomas, Western blotting, live cell surface binding assays, five liquid
      competition radioimmunoassays, and Ka measurements, all nine CC MAbs could be
      distinguished from each other and from B72.3. The Ka of B72.3 was determined to
      be 2.54 X 10(9) M-1; all the CC MAbs demonstrated higher KaS with MAbs CC92, 49, 
      and 83 having KaS of 14.26, 16.18, and 27.72 X 10(9) M-1, respectively. These
      studies thus demonstrate that one or more of the anti-TAG-72 CC MAbs may be more 
      efficient than B72.3, or useful in combination with B72.3, toward the further
      study of human carcinoma cell population and the diagnostic and therapeutic
      procedures presently utilizing MAb B72.3.
FAU - Muraro, R
AU  - Muraro R
AD  - Laboratory of Tumor Immunology and Biology, National Cancer Institute, Bethesda, 
      MD 20892.
FAU - Kuroki, M
AU  - Kuroki M
FAU - Wunderlich, D
AU  - Wunderlich D
FAU - Poole, D J
AU  - Poole DJ
FAU - Colcher, D
AU  - Colcher D
FAU - Thor, A
AU  - Thor A
FAU - Greiner, J W
AU  - Greiner JW
FAU - Simpson, J F
AU  - Simpson JF
FAU - Molinolo, A
AU  - Molinolo A
FAU - Noguchi, P
AU  - Noguchi P
AU  - et al.
LA  - eng
PT  - Journal Article
PL  - United States
TA  - Cancer Res
JT  - Cancer research
JID - 2984705R
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens, Neoplasm)
RN  - 0 (Antigens, Surface)
RN  - 0 (Glycoproteins)
SB  - IM
MH  - Animals
MH  - Antibodies, Monoclonal/biosynthesis/*immunology
MH  - Antigens, Neoplasm/*analysis/immunology
MH  - Antigens, Surface/analysis
MH  - Breast Neoplasms/immunology
MH  - Colonic Neoplasms/immunology
MH  - Female
MH  - Glycoproteins/*analysis/immunology
MH  - Humans
MH  - Immunohistochemistry
MH  - Mice
MH  - Mice, Inbred BALB C
MH  - Radioimmunoassay
EDAT- 1988/08/15 00:00
MHDA- 1988/08/15 00:01
CRDT- 1988/08/15 00:00
PHST- 1988/08/15 00:00 [pubmed]
PHST- 1988/08/15 00:01 [medline]
PHST- 1988/08/15 00:00 [entrez]
PST - ppublish
SO  - Cancer Res. 1988 Aug 15;48(16):4588-96.

PMID- 1421410
OWN - NLM
STAT- MEDLINE
DCOM- 19921207
LR  - 20071114
IS  - 0006-4971 (Print)
IS  - 0006-4971 (Linking)
VI  - 80
IP  - 9
DP  - 1992 Nov 1
TI  - O-linked oligosaccharides of glycophorins A and B in erythrocytes of two
      individuals with the Tn polyagglutinability syndrome.
PG  - 2388-95
AB  - Tn polyagglutinability syndrome is an acquired condition where erythrocytes
      express Tn neo-antigen and become susceptible to hemagglutination by the
      naturally occurring anti-Tn present in normal sera. Early studies had indicated
      that O-linked N-acetyl galactosamine was the sole serologic Tn determinant, but
      more recently O-linked NeuNAc alpha 2, 6GalNAc also has been implicated as a Tn
      antigen (sialosyl-Tn). However, none of these studies were performed on purified 
      glycoproteins. In this report we examine oligosaccharides of glycophorins A and B
      purified from Tn erythrocytes of two affected individuals to establish how N- and
      O-linked saccharides differ from normal. Analysis of carbohydrate composition and
      treatment with N-glycanase showed that the Asn-linked unit of glycophorin A was
      not affected. O-linked oligosaccharides were obtained by beta-elimination in the 
      presence of tritiated sodium borohydride. The reduced radiolabeled products were 
      fractionated by Bio-Gel P-2 chromatography, and their structures were
      investigated by comparison with standards, by monosaccharide quantification, and 
      by neuraminidases of known specificities. The results show that Tn glycophorins
      from both donors contain intact and truncated forms of trisaccharide and
      tetrasaccharide NeuNAc alpha 2,3Gal beta 1,3GalNAc and NeuNAc alpha 2,3Gal beta
      1,3- (NeuNAc alpha 2,6)GalNAc usually present in glycophorins A and B. The
      truncated forms include the protein O-linked monosaccharide, GalNAc and
      disaccharide, NeuNAc alpha 2,6GalNAc (major isomer). The presence of intact
      glycans in the total population of Tn erythrocytes was confirmed by their
      susceptibility to T activation after treatment with neuraminidase. The proportion
      of the four species was not identical in glycophorins of these two donors but, in
      both, the truncated units predominated and the amount of the disaccharide was
      approximately one half of that of the monosaccharide. The data are consistent
      with alterations in UDPGal:GalNAc beta 1,3galactosyl transferase that may have
      multiple molecular origins and with induction of a specific GalNAc protein alpha 
      2,6 sialosyl transferase in Tn hematopoietic precursor cells. The molecular basis
      for these alterations awaits further study.
FAU - Blumenfeld, O O
AU  - Blumenfeld OO
AD  - Department of Biochemistry, Albert Einstein College of Medicine, Bronx, NY 10461.
FAU - Lalezari, P
AU  - Lalezari P
FAU - Khorshidi, M
AU  - Khorshidi M
FAU - Puglia, K
AU  - Puglia K
FAU - Fukuda, M
AU  - Fukuda M
LA  - eng
GR  - CA 33000/CA/NCI NIH HHS/United States
GR  - R01 GM16389/GM/NIGMS NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Blood
JT  - Blood
JID - 7603509
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Glycophorin)
RN  - 0 (Oligosaccharides)
SB  - AIM
SB  - IM
MH  - Antibodies, Monoclonal
MH  - Carbohydrate Sequence
MH  - Chromatography, Gel
MH  - Electrophoresis, Polyacrylamide Gel
MH  - Erythrocytes/chemistry/*physiology
MH  - Glycophorin/*chemistry/isolation & purification
MH  - *Hemagglutination
MH  - Hematologic Diseases/*blood
MH  - Humans
MH  - Molecular Sequence Data
MH  - Oligosaccharides/blood/*chemistry/isolation & purification
MH  - Syndrome
EDAT- 1992/11/01 00:00
MHDA- 1992/11/01 00:01
CRDT- 1992/11/01 00:00
PHST- 1992/11/01 00:00 [pubmed]
PHST- 1992/11/01 00:01 [medline]
PHST- 1992/11/01 00:00 [entrez]
PST - ppublish
SO  - Blood. 1992 Nov 1;80(9):2388-95.

PMID- 8370596
OWN - NLM
STAT- MEDLINE
DCOM- 19931012
LR  - 20180220
IS  - 0165-2478 (Print)
IS  - 0165-2478 (Linking)
VI  - 36
IP  - 3
DP  - 1993 Jun
TI  - Use of O-glycosylation-defective human lymphoid cell lines and flow cytometry to 
      delineate the specificity of Moluccella laevis lectin and monoclonal antibody 5F4
      for the Tn antigen (GalNAc alpha 1-O-Ser/Thr).
PG  - 239-43
AB  - The Tn antigen (GalNAc alpha 1-O-Ser/Thr) is a disease-related O-linked
      (mucin-type) carbohydrate neoantigen which is expressed in idiopathic Tn
      syndrome, AIDS, T-cell lymphoma and in many carcinomas. In the present study, we 
      took advantage of a Tn antigen expressing T-lymphocyte clone derived from a
      patient with the idiopathic form of the Tn syndrome and the Tn+ Jurkat cell line 
      to characterize new reagents that should identify Tn antigens (monoclonal
      antibody 5F4 and a lectin newly isolated from Moluccella laevis seeds). Flow
      cytometry revealed that both reagents strongly bound to Tn antigen expressing T
      lymphocytes but not to normal donor T cells, which are Tn negative. In contrast
      to mAb 5F4, Moluccella laevis lectin weakly bound to normal donor cells after
      sialidase pretreatment, indicating its broader specificity.
      N-Acetyl-D-galactosamine at a concentration of 100 mM significantly reduced
      antibody binding and abolished lectin binding, completely demonstrating the sugar
      specificity of both reagents. These reagents should be useful tools in
      glycobiology and for clinical purposes.
FAU - Thurnher, M
AU  - Thurnher M
AD  - Institute of Physiology, University of Zurich, Switzerland.
FAU - Clausen, H
AU  - Clausen H
FAU - Sharon, N
AU  - Sharon N
FAU - Berger, E G
AU  - Berger EG
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - Netherlands
TA  - Immunol Lett
JT  - Immunology letters
JID - 7910006
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Lectins)
RN  - 0 (Plant Lectins)
RN  - 0 (Tn antigen)
SB  - IM
MH  - Antibodies, Monoclonal
MH  - *Antibody Specificity
MH  - Antigens, Tumor-Associated, Carbohydrate/*immunology
MH  - Cell Line
MH  - Cells, Cultured
MH  - Flow Cytometry
MH  - Glycosylation
MH  - Humans
MH  - Lectins/*immunology
MH  - Lymphocyte Activation
MH  - Plant Lectins
MH  - Plants/*immunology
MH  - T-Lymphocytes/enzymology/*immunology
EDAT- 1993/06/01 00:00
MHDA- 1993/06/01 00:01
CRDT- 1993/06/01 00:00
PHST- 1993/06/01 00:00 [pubmed]
PHST- 1993/06/01 00:01 [medline]
PHST- 1993/06/01 00:00 [entrez]
AID - 0165-2478(93)90095-J [pii]
PST - ppublish
SO  - Immunol Lett. 1993 Jun;36(3):239-43.

PMID- 6469974
OWN - NLM
STAT- MEDLINE
DCOM- 19840928
LR  - 20071114
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 259
IP  - 16
DP  - 1984 Aug 25
TI  - Novel fucolipids accumulating in human adenocarcinoma. III. A hybridoma antibody 
      (FH6) defining a human cancer-associated difucoganglioside
      (VI3NeuAcV3III3Fuc2nLc6).
PG  - 10511-7
AB  - A new fucoganglioside, 6B, which accumulates in human colonic adenocarcinoma but 
      is absent in normal colonic mucosa, was isolated from a monosialoganglioside
      fraction of colonic adenocarcinomas. The structure of this ganglioside was
      identified as shown below by methylation analysis, direct probe mass
      spectrometry, and enzymatic degradation followed by examination of the
      degradation products with specific monoclonal antibodies. (formula; see text) The
      hybridoma (FH6) secreting a monoclonal IgM antibody directed to this glycolipid
      was selected by reactivity of the antibody with this ganglioside and lack of
      reactivity with other glycolipids having a closely related structure, such as
      sialosyllactoneotetraosylceramide (IV3NeuAcnLc4),
      sialosyllactofucopentaosy(III)ceramide (IV3NeuAcIII3FucnLc4),
      sialosyllactofucopentaosy(II)ceramide (sialosyl-Lea glycolipid;
      IV3NeuAcIII4FucLc4), and 6C fucoganglioside (sialosyl 2 leads to 6
      fucoganglioside; VI6NeuAcIII3FucnLc6). The antibody was highly reactive with a
      large variety of human cancer cells, but was less reactive or did not react with 
      a variety of normal cells.
FAU - Fukushi, Y
AU  - Fukushi Y
FAU - Nudelman, E
AU  - Nudelman E
FAU - Levery, S B
AU  - Levery SB
FAU - Hakomori, S
AU  - Hakomori S
FAU - Rauvala, H
AU  - Rauvala H
LA  - eng
GR  - CA 20026/CA/NCI NIH HHS/United States
GR  - GM 23100/GM/NIGMS NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Gangliosides)
RN  - 0 (Glycolipids)
RN  - 0 (fucogangliosides)
RN  - 0 (fucolipids)
SB  - IM
MH  - Adenocarcinoma/*analysis
MH  - Antibodies, Monoclonal
MH  - Carbohydrate Conformation
MH  - Carbohydrate Sequence
MH  - Cell Line
MH  - Colonic Neoplasms/*analysis
MH  - Gangliosides/*analysis/isolation & purification
MH  - Glycolipids/*analysis
MH  - Humans
MH  - Hybridomas/immunology
MH  - Mass Spectrometry
EDAT- 1984/08/25 00:00
MHDA- 1984/08/25 00:01
CRDT- 1984/08/25 00:00
PHST- 1984/08/25 00:00 [pubmed]
PHST- 1984/08/25 00:01 [medline]
PHST- 1984/08/25 00:00 [entrez]
PST - ppublish
SO  - J Biol Chem. 1984 Aug 25;259(16):10511-7.

PMID- 2140570
OWN - NLM
STAT- MEDLINE
DCOM- 19900702
LR  - 20171116
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 265
IP  - 16
DP  - 1990 Jun 5
TI  - Biosynthesis of truncated O-glycans in the T cell line Jurkat. Localization of
      O-glycan initiation.
PG  - 9264-71
AB  - Glycoproteins from the human T leukemia cells Jurkat were found to bind to the
      GalNAc alpha 1----Ser/Thr-specific lectin from Salvia sclarea seeds. The analysis
      of the O-linked saccharides of immunopurified leukosialin, the major
      [3H]glucosamine-labeled glycoprotein in Jurkat cell lysate, revealed the presence
      of mainly GalNAc alpha 1----Ser/Thr with only minor amounts (approximately 17%)
      of more complex O-glycans. A comparison between Jurkat and K562 cell
      glycosyltransferase involved in the biosynthesis of O-linked carbohydrates showed
      that a markedly lower activity of UDP-Gal:GalNAc alpha 1----Ser/Thr beta
      1----3galactosyltransferase is apparently responsible for the presence of
      truncated O-glycans in the Jurkat cell line. The O-glycosylation defect makes
      Jurkat cells an ideal model to study the initiation of O-linked saccharides.
      Pulse-chase experiments with [35S] methionine showed that the addition of GalNAc 
      to leukosialin is responsible for the decreased mobility of the mature
      glycoprotein on sodium dodecyl sulfate-polyacrylamide gel electrophoresis.
      Furthermore, no biosynthetic intermediates between the O-glycan-free precursor
      and the fully O-glycosylated form could be detected either with an
      anti-leukosialin antiserum or with the GalNAc-specific lectin. Lowering the chase
      temperature to 15 degrees C completely inhibited the transfer of GalNAc to the
      peptide core indicating that O-glycan initiation takes place in the first Golgi
      elements and not in transitional vesicles between endoplasmic reticulum and
      Golgi. In addition, treatment of the cells with monensin did not inhibit GalNAc
      transfer to leukosialin apoprotein. These results indicate that the initiation of
      O-glycosylation in Jurkat cells starts in the cis-Golgi stacks.
FAU - Piller, V
AU  - Piller V
AD  - La Jolla Cancer Research Foundation, Cancer Research Center, California 92037.
FAU - Piller, F
AU  - Piller F
FAU - Fukuda, M
AU  - Fukuda M
LA  - eng
GR  - R01 CA 33895/CA/NCI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Antigens, CD)
RN  - 0 (Glycoproteins)
RN  - 0 (Lectins)
RN  - 0 (Leukosialin)
RN  - 0 (Polysaccharides)
RN  - 0 (Sialoglycoproteins)
RN  - 0 (UN1 sialoglycoprotein, human)
RN  - EC 2.4.1.- (Galactosyltransferases)
RN  - KM15WK8O5T (Acetylgalactosamine)
SB  - IM
MH  - Acetylgalactosamine/metabolism
MH  - *Antigens, CD
MH  - Carbohydrate Conformation
MH  - Carbohydrate Sequence
MH  - Electrophoresis, Polyacrylamide Gel
MH  - Galactosyltransferases/metabolism
MH  - Glycoproteins/metabolism
MH  - Glycosylation
MH  - Humans
MH  - Immunosorbent Techniques
MH  - Lectins/metabolism
MH  - Leukemia, Lymphoid/*metabolism
MH  - Leukosialin
MH  - Molecular Sequence Data
MH  - Polysaccharides/*biosynthesis
MH  - Sialoglycoproteins/metabolism
MH  - Tumor Cells, Cultured
EDAT- 1990/06/05 00:00
MHDA- 1990/06/05 00:01
CRDT- 1990/06/05 00:00
PHST- 1990/06/05 00:00 [pubmed]
PHST- 1990/06/05 00:01 [medline]
PHST- 1990/06/05 00:00 [entrez]
PST - ppublish
SO  - J Biol Chem. 1990 Jun 5;265(16):9264-71.

PMID- 8551046
OWN - NLM
STAT- MEDLINE
DCOM- 19960220
LR  - 20181211
IS  - 0022-1759 (Print)
IS  - 0022-1759 (Linking)
VI  - 188
IP  - 2
DP  - 1995 Dec 27
TI  - Anti-Thomsen-Friedenreich (T) antibody-based ELISA and its application to human
      breast carcinoma detection.
PG  - 175-85
AB  - An anti-Thomsen-Friedenreich (T) antibody-based enzyme-linked immunosorbent assay
      (ELISA) with high efficacy in human breast carcinoma detection is described.
      Immunoreactive T epitopes occur in approximately 90% of all carcinomata; all
      humans have anti-T antibodies, naturally occurring anti-carcinoma antibodies,
      induced by their own intestinal flora. Carcinoma patients, but not control
      subjects, show alterations of serum anti-T hemagglutinin levels. Human anti-T
      antibodies are predominantly IgM. In the protocol presented here, anti-T IgM
      antibodies are quantitated by ELISA using Immulon 2 wells coated with human blood
      group O erythrocyte-derived T antigen as solid phase; in addition, total IgM in
      each serum is quantitated by ELISA in parallel with the anti-T IgM. Inter-assay
      coefficient of variation was 2% for both ELISAs. Although anti-T IgM values alone
      distinguish between carcinoma patients and control subjects, use of the quotient,
      QMe, which also considers total IgM, increases this distinction. For a given
      serum, QMe was obtained by the formula: QMe = (100 x (anti-T IgM)2/total IgM).
      Sera of 242 subjects, 117 breast carcinoma patients, 36 benign breast disease
      patients and 89 healthy persons were analyzed. QMe identified 88% of the breast
      carcinoma patients: it all six (100%) in situ, 11/13 (85%) Stage I, 48/58 (83%)
      Stage II and III and 38/40 (95%) Stage IV patients. Sera from 83% of the 36
      benign breast disease patients were negative, i.e. within normal range; five of
      the six positive sera originated from patients with increased long-term risk of
      breast carcinoma, while sera from 11 other patients with increased carcinoma risk
      were negative. Overall, 90% of the 125 non-carcinoma control subjects were
      negative by both anti-T IgM and QMe. In preliminary studies, the ELISA protocol
      detected 11/14 (79%) patients with carcinomata other than those of the breast.
      The identification of all six in situ breast carcinoma patients by QMe points to 
      its usefulness in carcinoma detection, especially early.
FAU - Desai, P R
AU  - Desai PR
AD  - Heather M. Bligh Cancer Research Laboratories, Department of
      Microbiology-Immunology, Chicago Medical School, IL 60064, USA.
FAU - Ujjainwala, L H
AU  - Ujjainwala LH
FAU - Carlstedt, S C
AU  - Carlstedt SC
FAU - Springer, G F
AU  - Springer GF
LA  - eng
GR  - CA 22540/CA/NCI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - Netherlands
TA  - J Immunol Methods
JT  - Journal of immunological methods
JID - 1305440
RN  - 0 (Antibodies)
RN  - 0 (Antigens, Neoplasm)
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Biomarkers, Tumor)
RN  - 0 (Immunoglobulin G)
RN  - 0 (Immunoglobulin M)
RN  - 0 (Isoantigens)
RN  - 3554-90-3 (Thomsen-Friedenreich antigen)
RN  - 3HG052TF3I (Thomsen-Friedenreich antibodies)
SB  - IM
CIN - J Immunol Methods. 1995 Dec 27;188(2):171-3. PMID: 8551045
MH  - Adult
MH  - Aged
MH  - Antibodies/*analysis
MH  - Antigens, Neoplasm/blood/immunology
MH  - Antigens, Tumor-Associated, Carbohydrate/blood/immunology
MH  - Biomarkers, Tumor/*analysis
MH  - Breast Neoplasms/*diagnosis
MH  - Cohort Studies
MH  - Enzyme-Linked Immunosorbent Assay/*methods
MH  - Female
MH  - Humans
MH  - Immunoglobulin G/analysis
MH  - Immunoglobulin M/analysis
MH  - Isoantigens/blood/immunology
MH  - Middle Aged
MH  - Neoplasm Staging
MH  - Reproducibility of Results
MH  - Sensitivity and Specificity
EDAT- 1995/12/27 00:00
MHDA- 1995/12/27 00:01
CRDT- 1995/12/27 00:00
PHST- 1995/12/27 00:00 [pubmed]
PHST- 1995/12/27 00:01 [medline]
PHST- 1995/12/27 00:00 [entrez]
AID - 0022175995002464 [pii]
PST - ppublish
SO  - J Immunol Methods. 1995 Dec 27;188(2):175-85.

PMID- 7734848
OWN - NLM
STAT- MEDLINE
DCOM- 19950608
LR  - 20190512
IS  - 0959-6658 (Print)
IS  - 0959-6658 (Linking)
VI  - 4
IP  - 6
DP  - 1994 Dec
TI  - Immunohistochemical localization of minor gangliosides in the rat central nervous
      system.
PG  - 855-65
AB  - We previously described the differential distribution of major gangliosides (GM1,
      GD1a, GD1b, GT1b and GQ1b) in adult rat brain detected by specific antibodies
      (Kotani, M., Kawashima, I., Ozawa, I., Terashima, T. and Tai, T. Glycobiology, 3,
      137-146, 1993). We report here the distribution of minor gangliosides in the
      adult rat brain by an immunofluorescence technique with mouse monoclonal
      antibodies (MAbs). Ten MAbs (GMR6, GMB28, GMR11, GMR19, GMR2, GMR7, GGR51, AMR10,
      NGR54 and NGR53) that specifically recognize GM3, GM2, GT1a, GD3,
      O-Acdisialoganglioside, GD2, GM1b, GM4, IV3NeuAc alpha-nLc4Cer and IV6NeuAc
      alpha-nLc4Cer, respectively, were used. Our study revealed that there is a cell
      type-specific expression of minor gangliosides, as well as major gangliosides, in
      the rat brain. In the cerebellar cortex, GM3 was expressed intensely in the white
      matter and slightly in the granular layer. GD3 was present in both the granular
      layer and the white matter, but not in the Purkinje cell layer or in the
      molecular layer. An O-Ac-disialoganglioside, which was suggested to be O-Ac-LD1, 
      was detected exclusively in both the molecular layer and Purkinje cell layer. The
      presence of GD2 was restricted to the granular layer. GM4 was associated with
      some astrocytes, but not with myelin or oligodendrocytes. GM2, GT1a, GM1b,
      IV3NeuAc alpha-nLc4Cer and IV6NeuAc alpha-nLc4Cer gangliosides were not clearly
      detected in the cerebellar cortex. In other regions, such as cerebral cortex,
      hippocampal formation and spinal cord, the expression of the gangliosides was
      also highly localized to a specific cell type and layer.
FAU - Kotani, M
AU  - Kotani M
AD  - Department of Tumor Immunology, Tokyo Metropolitan Institute of Medical Science, 
      Japan.
FAU - Kawashima, I
AU  - Kawashima I
FAU - Ozawa, H
AU  - Ozawa H
FAU - Ogura, K
AU  - Ogura K
FAU - Ishizuka, I
AU  - Ishizuka I
FAU - Terashima, T
AU  - Terashima T
FAU - Tai, T
AU  - Tai T
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - Glycobiology
JT  - Glycobiology
JID - 9104124
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Gangliosides)
SB  - IM
MH  - Animals
MH  - Antibodies, Monoclonal
MH  - Antibody Specificity
MH  - Carbohydrate Sequence
MH  - Central Nervous System/anatomy & histology/*metabolism
MH  - Cerebellar Cortex/metabolism
MH  - Cerebral Cortex/metabolism
MH  - Gangliosides/chemistry/immunology/*metabolism
MH  - Hippocampus/metabolism
MH  - Immunohistochemistry
MH  - Molecular Sequence Data
MH  - Rats
MH  - Spinal Cord/metabolism
EDAT- 1994/12/01 00:00
MHDA- 1994/12/01 00:01
CRDT- 1994/12/01 00:00
PHST- 1994/12/01 00:00 [pubmed]
PHST- 1994/12/01 00:01 [medline]
PHST- 1994/12/01 00:00 [entrez]
AID - 10.1093/glycob/4.6.855 [doi]
PST - ppublish
SO  - Glycobiology. 1994 Dec;4(6):855-65. doi: 10.1093/glycob/4.6.855.

PMID- 3791209
OWN - NLM
STAT- MEDLINE
DCOM- 19870202
LR  - 20061115
IS  - 0008-5472 (Print)
IS  - 0008-5472 (Linking)
VI  - 47
IP  - 1
DP  - 1987 Jan 1
TI  - Fluctuations in the expression of a glycolipid antigen associated with
      differentiation of melanoma cells monitored by a monoclonal antibody, Leo Mel 3.
PG  - 225-30
AB  - A monoclonal antibody, Leo Mel 3, raised against a melanoma cell line (LiBr),
      binds to a carbohydrate determinant of cell surface gangliosides, the simplest of
      which is GD3. This monoclonal antibody was screened for by its capacity to block 
      the recognition and lysis of the melanoma cells by cytotoxic T-lymphocytes with
      anomalous killer cell function, illustrating a novel approach for identifying
      monoclonal antibody to biologically relevant tumor-associated antigens. Leo Mel 3
      reacted selectively with melanoma cells by indirect immunofluorescent and
      immunoperoxidase staining; it reacted with tissue from all primary and metastatic
      melanoma tested, and it bound to cells from all but one of six cultured melanoma 
      cell lines. Leo Mel 3 did not react with a variety of carcinomas, lymphomas,
      leukemias, and other neuroectodermal tumors, nor with adult or fetal tissues,
      except fetal liver. Very weak staining of cutaneous basal melanocytes was noted
      in a minority of skin sections, and 50 to 80% of melanocytes in four of seven
      benign nevi showed weak to moderate reactivity. The antibody was relatively
      specific for human adherent melanoma cells, since it did not bind to the adherent
      murine B16 melanoma line nor to a nonadherent human melanoma cell line (PMC-22). 
      Expression of the Leo Mel 3-defined antigen was unrelated to changes in cell
      cycle. When cells from an adherent melanoma cell line were detached and
      maintained briefly in suspension culture, the cells became markedly less reactive
      with Leo Mel 3 and, after readherence to plastic, they rapidly reexpressed higher
      levels of the ganglioside antigen; since Leo Mel 3 prevented attachment and
      growth of melanoma cells in vitro, a functional role for the ganglioside is
      suggested in cell adhesion and metastasis. Differentiation of melanoma cells with
      dimethyl sulfoxide, retinoic acid, and theophylline resulted in a marked and
      selective increase in the amount of Leo Mel 3-defined antigen, together with an
      increase in the target cell binding ability of these cells, assessed by cold
      target competition assays using anomalous killer cells.
FAU - Werkmeister, J A
AU  - Werkmeister JA
FAU - Triglia, T
AU  - Triglia T
FAU - Mackay, I R
AU  - Mackay IR
FAU - Dowling, J P
AU  - Dowling JP
FAU - Varigos, G A
AU  - Varigos GA
FAU - Morstyn, G
AU  - Morstyn G
FAU - Burns, G F
AU  - Burns GF
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Cancer Res
JT  - Cancer research
JID - 2984705R
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens, Neoplasm)
RN  - 0 (Gangliosides)
RN  - 0 (Suspensions)
RN  - 62010-37-1 (ganglioside, GD3)
SB  - IM
MH  - Antibodies, Monoclonal/*immunology
MH  - Antigens, Neoplasm/*analysis/biosynthesis
MH  - Cell Adhesion
MH  - Cell Cycle
MH  - Cell Differentiation
MH  - Cell Line
MH  - Freezing
MH  - Gangliosides/*analysis/immunology
MH  - Humans
MH  - Melanoma/*immunology/pathology
MH  - Suspensions
EDAT- 1987/01/01 00:00
MHDA- 1987/01/01 00:01
CRDT- 1987/01/01 00:00
PHST- 1987/01/01 00:00 [pubmed]
PHST- 1987/01/01 00:01 [medline]
PHST- 1987/01/01 00:00 [entrez]
PST - ppublish
SO  - Cancer Res. 1987 Jan 1;47(1):225-30.

PMID- 18184719
OWN - NLM
STAT- MEDLINE
DCOM- 20080729
LR  - 20171116
IS  - 1460-2423 (Electronic)
IS  - 0959-6658 (Linking)
VI  - 18
IP  - 3
DP  - 2008 Mar
TI  - Embryonic stem cells deficient in I beta1,6-N-acetylglucosaminyltransferase
      exhibit reduced expression of embryoglycan and the loss of a Lewis X antigen,
      4C9.
PG  - 242-9
LID - 10.1093/glycob/cwm138 [doi]
AB  - Embryoglycan is a class of branched high-molecular-weight
      poly-N-acetyllactosamines characteristically expressed in early embryonic cells
      and has been shown to be involved in the intercellular adhesion of early
      embryonic cells in vitro. Branching of poly-N-acetyllactosamine chains is
      performed by beta1,6-N-acetylglucosaminylation of the galactosyl residue. We
      previously knocked out the gene encoding I beta1,
      6-N-acetylglucosaminyltransferase (IGnT), and the resultant deficient mice were
      born without any abnormality, although the mice exhibited various deficits in
      later life. In the present investigation, we produced embryonic stem (ES) cells
      from IGnT-deficient embryos. The mutant ES cells exhibited a reduced capability
      in embryoglycan synthesis. Thus, IGnT is a major enzyme involved in the branching
      of poly-N-acetyllactosamine chains in embryoglycan. Since ES cells are equivalent
      to multipotential cells of the embryonic ectoderm in early postimplantation
      embryos, this result indicates that an abundance of embryoglycan in these cells
      is not essential for normal embryogenesis. The IGnT-deficient ES cells continued 
      to express SSEA-1, but lacked the expression of 4C9 antigen, although the epitope
      of 4C9 antigen was confirmed to be Lewis X by a transfection experiment. The
      result establishes the distinct nature of 4C9 antigenicity, which requires either
      Lewis X epitope on I-branch or clustering of Lewis X epitope, best accomplished
      by poly-N-acetyllactosamine branching. Alpha6-integrin was newly identified as a 
      carrier of embryoglycan. The IGnT-deficient ES cells adhered to dishes coated
      with laminin, which is a ligand for alpha6-integrin, significantly less than
      wild-type ES cells, raising the possibility that embryoglycan in ES cells
      enhances alpha6-integrin-dependent adhesion in vitro.
FAU - Muramatsu, Hisako
AU  - Muramatsu H
AD  - Department of Biochemistry, Center for Neurological Disease and Cancer, Nagoya
      University Graduate School of Medicine, Nagoya 468-8550, Japan.
FAU - Kusano, Taiki
AU  - Kusano T
FAU - Sato, Masahiro
AU  - Sato M
FAU - Oda, Yoshihiro
AU  - Oda Y
FAU - Kobori, Kyoko
AU  - Kobori K
FAU - Muramatsu, Takashi
AU  - Muramatsu T
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20080109
PL  - England
TA  - Glycobiology
JT  - Glycobiology
JID - 9104124
RN  - 0 (Integrin alpha6)
RN  - 0 (Laminin)
RN  - 0 (Lewis X Antigen)
RN  - 0 (Polysaccharides)
RN  - 0 (embryoglycan)
RN  - EC 2.4.- (N-acetylglucosaminyltransferase IGnT)
RN  - EC 2.4.1.- (N-Acetylglucosaminyltransferases)
SB  - IM
MH  - Animals
MH  - Cell Adhesion/immunology
MH  - Cell Differentiation
MH  - Cell Line
MH  - Embryonic Stem Cells/*metabolism
MH  - Humans
MH  - Immunohistochemistry
MH  - Integrin alpha6/metabolism
MH  - Laminin/metabolism
MH  - Lewis X Antigen/*metabolism
MH  - Mice
MH  - Mice, Knockout
MH  - N-Acetylglucosaminyltransferases/*deficiency/genetics/immunology
MH  - Polysaccharides/*metabolism
MH  - Reverse Transcriptase Polymerase Chain Reaction
EDAT- 2008/01/11 09:00
MHDA- 2008/07/30 09:00
CRDT- 2008/01/11 09:00
PHST- 2008/01/11 09:00 [pubmed]
PHST- 2008/07/30 09:00 [medline]
PHST- 2008/01/11 09:00 [entrez]
AID - cwm138 [pii]
AID - 10.1093/glycob/cwm138 [doi]
PST - ppublish
SO  - Glycobiology. 2008 Mar;18(3):242-9. doi: 10.1093/glycob/cwm138. Epub 2008 Jan 9.

PMID- 2416034
OWN - NLM
STAT- MEDLINE
DCOM- 19860116
LR  - 20170124
IS  - 1010-4283 (Print)
IS  - 1010-4283 (Linking)
VI  - 6
IP  - 3
DP  - 1985
TI  - Circulating blood group-related antigen(s) in cancer patients detected by the
      monoclonal antibodies produced against hepatocellular carcinoma cell line.
PG  - 257-72
AB  - Two murine monoclonal antibodies (MAbs) S1 and S3 produced against a human
      hepatoma cell line were found to recognize both H (type II) antigen and difucosyl
      type II structure (Y-antigen). Both MAbs reacted with hepatoma tissues obtained
      from surgical resection. A double determinant enzyme immunoassay (DDEI) employing
      these MAbs successfully detected the corresponding antigen(s) in the supernatant 
      which is either released or shed from the immunizing hepatoma cell line. DDEI
      also revealed that these antibodies reacted with the corresponding antigen(s) in 
      the sera from cancer patients. Among the sera from O blood group donors,
      individuals with primary hepatoma showed markedly higher levels of antigen
      concentration than the normal control group. Several cases with gall bladder,
      lung and pancreas carcinomas, which are of O blood type, also had significantly
      higher levels of antigen. One case with ovarian cancer of B blood type showed
      higher antigen concentration than normal O blood group donors suggesting a change
      in the carbohydrate structure of the corresponding antigen(s) in the serum. These
      data suggest that the release or the shedding of the antigen(s) from the cells
      may increase due to the malignant transformation, resulting in higher amounts of 
      the antigen(s) in the serum of certain cancer patients.
FAU - Imai, K
AU  - Imai K
FAU - Sasanami, T
AU  - Sasanami T
FAU - Nakanishi, T
AU  - Nakanishi T
FAU - Noguchi, T
AU  - Noguchi T
FAU - Yachi, A
AU  - Yachi A
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Tumour Biol
JT  - Tumour biology : the journal of the International Society for Oncodevelopmental
      Biology and Medicine
JID - 8409922
RN  - 0 (ABO Blood-Group System)
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens)
RN  - 0 (Epitopes)
SB  - IM
MH  - ABO Blood-Group System/*immunology
MH  - Antibodies, Monoclonal/biosynthesis/immunology
MH  - Antigens/analysis
MH  - Carcinoma, Hepatocellular/*blood/immunology
MH  - Cell Line
MH  - Epitopes/analysis
MH  - Female
MH  - Hemagglutination Tests
MH  - Histocytochemistry
MH  - Humans
MH  - Immunoenzyme Techniques
MH  - Liver Neoplasms/*blood/immunology
MH  - Rosette Formation
EDAT- 1985/01/01 00:00
MHDA- 1985/01/01 00:01
CRDT- 1985/01/01 00:00
PHST- 1985/01/01 00:00 [pubmed]
PHST- 1985/01/01 00:01 [medline]
PHST- 1985/01/01 00:00 [entrez]
PST - ppublish
SO  - Tumour Biol. 1985;6(3):257-72.

PMID- 17616966
OWN - NLM
STAT- MEDLINE
DCOM- 20070921
LR  - 20131121
IS  - 0014-2980 (Print)
IS  - 0014-2980 (Linking)
VI  - 37
IP  - 8
DP  - 2007 Aug
TI  - MGL-mediated internalization and antigen presentation by dendritic cells: a role 
      for tyrosine-5.
PG  - 2075-81
AB  - Professional antigen-presenting cells are essential for the initiation of
      adaptive immune responses; however, they also play a vital role in the
      maintenance of tolerance towards self-antigens. C-type lectins can function as
      antigen receptors by capturing carbohydrate ligands for processing and
      presentation. Here, we focused on the dendritic cell (DC)-expressed macrophage
      galactose-type lectin (MGL), a C-type lectin with a unique specificity for
      terminal GalNAc residues, such as the tumor-associated Tn antigen. Soluble model 
      antigens are efficiently internalized by MGL and subsequently presented to
      responder CD4+ T cells. The tyrosine-5 residue in the YENF motif, present in the 
      MGL cytoplasmic domain, was essential for the MGL-mediated endocytosis in CHO
      cells. In conclusion, MGL contributes to the antigen processing and presentation 
      capacities of DC and may provide a suitable target for the initiation of
      anti-tumor immune responses.
FAU - van Vliet, Sandra J
AU  - van Vliet SJ
AD  - Department of Molecular Cell Biology & Immunology, VU University Medical Center, 
      Amsterdam, The Netherlands.
FAU - Aarnoudse, Corlien A
AU  - Aarnoudse CA
FAU - Broks-van den Berg, Venice C M
AU  - Broks-van den Berg VC
FAU - Boks, Martine
AU  - Boks M
FAU - Geijtenbeek, Teunis B H
AU  - Geijtenbeek TB
FAU - van Kooyk, Yvette
AU  - van Kooyk Y
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - Germany
TA  - Eur J Immunol
JT  - European journal of immunology
JID - 1273201
RN  - 0 (Lectins, C-Type)
RN  - 0 (MGL lectin, human)
RN  - 42HK56048U (Tyrosine)
SB  - IM
MH  - Amino Acid Motifs/immunology
MH  - Amino Acid Sequence
MH  - Animals
MH  - Antigen Presentation/*immunology
MH  - CHO Cells
MH  - Cricetinae
MH  - Cricetulus
MH  - Dendritic Cells/*immunology
MH  - Endocytosis/immunology
MH  - Flow Cytometry
MH  - Humans
MH  - Lectins, C-Type/chemistry/genetics/*immunology
MH  - Microscopy, Confocal
MH  - Molecular Sequence Data
MH  - Tyrosine
EDAT- 2007/07/10 09:00
MHDA- 2007/09/22 09:00
CRDT- 2007/07/10 09:00
PHST- 2007/07/10 09:00 [pubmed]
PHST- 2007/09/22 09:00 [medline]
PHST- 2007/07/10 09:00 [entrez]
AID - 10.1002/eji.200636838 [doi]
PST - ppublish
SO  - Eur J Immunol. 2007 Aug;37(8):2075-81. doi: 10.1002/eji.200636838.

PMID- 9166429
OWN - NLM
STAT- MEDLINE
DCOM- 19970630
LR  - 20190508
IS  - 0022-1007 (Print)
IS  - 0022-1007 (Linking)
VI  - 185
IP  - 11
DP  - 1997 Jun 2
TI  - 9-O-Acetylation of sialomucins: a novel marker of murine CD4 T cells that is
      regulated during maturation and activation.
PG  - 1997-2013
AB  - Terminal sialic acids on cell surface glycoconjugates can carry 9-O-acetyl
      esters. For technical reasons, it has previously been difficult to determine
      their precise distribution on different cell types. Using a recombinant soluble
      form of the Influenza C virus hemagglutinin-esterase as a probe for
      9-O-acetylated sialic acids, we demonstrate here their preferential expression on
      the CD4 T cell lineage in normal B10.A mouse lymphoid organs. Of total
      thymocytes, 8-10% carry 9-O-acetylation; the great majority of these are the more
      mature PNA-, HSA-, and TCRhi medullary cells. While low levels of 9-O-acetylation
      are seen on some CD4/CD8 double positive (DP) and CD8 single positive (SP) cells,
      high levels are present primarily on 80- 85% of CD4 SP cells. Correlation with
      CD4 and CD8 levels suggests that 9-O-acetylation appears as an early
      differentiation marker as cells mature from the DP to the CD4 SP phenotype. This 
      high degree of 9-O-acetylation is also present on 90-95% of peripheral spleen and
      lymph node CD4 T cells. In contrast, only a small minority of CD8 T cells and B
      cells show such levels of 9-O-acetylation. Among mature peripheral CD4 T
      lymphocytes, the highly O-acetylated cells are Mel 14(hi), CD44(lo), and
      CD45R(exon B)hi, features typical of naive cells. Digestions with trypsin and
      O-sialoglycoprotease (OSGPase) and ELISA studies of lipid extracts indicate that 
      the 9-O-acetylated sialic acids on peripheral CD4 T cells are predominantly on
      O-linked mucintype glycoproteins and to a lesser degree, on sialylated
      glycolipids (gangliosides). In contrast, sialic acids on mucin type molecules of 
      CD8 T cells are not O-acetylated; instead these molecules mask the recognition of
      O-acetylated gangliosides that seem to be present at similar levels as on CD4
      cells. The 9-O-acetylated gangliosides on mouse T cells are not bound by CD60
      antibodies, which recognize O-acetylated gangliosides in human T cells. Tethering
      9-O-acetylated mucins with the Influenza C probe with or without secondary
      cross-linking did not cause activation of CD4 T cells. However, activation by
      other stimuli including TCR ligation is associated with a substantial decrease in
      surface 9-O-acetylation, primarily in the mucin glycoprotein component. Thus,
      9-O-acetylation of sialic acids on cell surface mucins is a novel marker on CD4 T
      cells that appears on maturation and is modulated downwards upon activation.
FAU - Krishna, M
AU  - Krishna M
AD  - Glycobiology Program, UCSD Cancer Center, the Department of Medicine, University 
      of California, San Diego, La Jolla, California 92093, USA.
FAU - Varki, A
AU  - Varki A
LA  - eng
GR  - R01 GM032373/GM/NIGMS NIH HHS/United States
GR  - R01-GM32373/GM/NIGMS NIH HHS/United States
PT  - Journal Article
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - J Exp Med
JT  - The Journal of experimental medicine
JID - 2985109R
RN  - 0 (Antigens, CD)
RN  - 0 (Antigens, Differentiation, B-Lymphocyte)
RN  - 0 (Biomarkers)
RN  - 0 (CD4 Antigens)
RN  - 0 (CD8 Antigens)
RN  - 0 (Cd22 protein, mouse)
RN  - 0 (Cell Adhesion Molecules)
RN  - 0 (Gangliosides)
RN  - 0 (Hemagglutinins, Viral)
RN  - 0 (Lectins)
RN  - 0 (Leukosialin)
RN  - 0 (Ligands)
RN  - 0 (Mucins)
RN  - 0 (Sialic Acid Binding Ig-like Lectin 2)
RN  - 0 (Sialic Acids)
RN  - 0 (Sialoglycoproteins)
RN  - 0 (Sialomucins)
RN  - 0 (Spn protein, mouse)
RN  - 0 (Viral Fusion Proteins)
RN  - 0 (Viral Proteins)
RN  - 0 (hemagglutinin esterase)
RN  - 12UHW9R67N (Isoflurophate)
RN  - 55717-54-9 (9-O-acetyl-N-acetylneuraminic acid)
RN  - EC 3.1.1.- (Carboxylic Ester Hydrolases)
RN  - EC 3.1.1.6 (Acetylesterase)
RN  - EC 3.1.1.6 (sialate O-acetylesterase)
RN  - EC 3.1.3.48 (Leukocyte Common Antigens)
RN  - EC 3.4.21.4 (Trypsin)
SB  - IM
SB  - X
MH  - Acetylation
MH  - Acetylesterase
MH  - Animals
MH  - Antigens, CD/metabolism
MH  - Antigens, Differentiation, B-Lymphocyte/metabolism
MH  - Biomarkers
MH  - CD4 Antigens/analysis
MH  - CD4-Positive T-Lymphocytes/*immunology/metabolism
MH  - CD8 Antigens/analysis
MH  - CD8-Positive T-Lymphocytes/immunology/metabolism
MH  - Carboxylic Ester Hydrolases/metabolism
MH  - *Cell Adhesion Molecules
MH  - Gangliosides/chemistry
MH  - Hemagglutinins, Viral
MH  - Influenzavirus C/enzymology
MH  - Isoflurophate/pharmacology
MH  - *Lectins
MH  - Leukocyte Common Antigens/metabolism
MH  - Leukosialin
MH  - Ligands
MH  - *Lymphocyte Activation
MH  - Mice
MH  - Mice, Inbred Strains
MH  - Mucins/*metabolism
MH  - Sialic Acid Binding Ig-like Lectin 2
MH  - Sialic Acids/*metabolism
MH  - Sialoglycoproteins/metabolism
MH  - Sialomucins
MH  - Trypsin/metabolism
MH  - *Viral Fusion Proteins
MH  - Viral Proteins
PMC - PMC2196344
EDAT- 1997/06/02 00:00
MHDA- 1997/06/02 00:01
CRDT- 1997/06/02 00:00
PHST- 1997/06/02 00:00 [pubmed]
PHST- 1997/06/02 00:01 [medline]
PHST- 1997/06/02 00:00 [entrez]
AID - 10.1084/jem.185.11.1997 [doi]
PST - ppublish
SO  - J Exp Med. 1997 Jun 2;185(11):1997-2013. doi: 10.1084/jem.185.11.1997.

PMID- 1523927
OWN - NLM
STAT- MEDLINE
DCOM- 19921009
LR  - 20061115
IS  - 0001-5547 (Print)
IS  - 0001-5547 (Linking)
VI  - 36
IP  - 5
DP  - 1992 Sep-Oct
TI  - Application of a panel of antiganglioside monoclonal antibodies to cytologic
      specimens.
PG  - 697-705
AB  - The cytologic evaluation of poorly differentiated tumors frequently poses a
      diagnostic dilemma as to the tissue of origin. To assess the diagnostic utility
      of monoclonal antibodies (MAbs) in these situations, we applied a panel of three 
      highly purified MAbs specific for tumor-associated ganglioside epitopes to a
      diverse series of cytologic specimens. The panel was composed of DMAb-3, reactive
      with the epitope GalNAc beta 1-4 (NeuAc alpha 2-3)Gal- of GM2; DMAb-7, reactive
      with the epitope (NeuAc alpha 2-8NeuAc alpha 2-3)Gal beta 1-4(Glc or GlcNAc)- of 
      GD3 and 3'8'-LD1; and DMAb-20, reactive with the epitope GalNAc beta 1-4(NeuAc
      alpha 2-8NeuAc alpha 2-3)Gal- of GD2. The cytologic material consisted of
      air-dried Cytospin preparations prepared predominantly from fine needle aspirates
      and stained with the ABC immunohistochemical method. Positive reactivity was
      recognized when greater than 5% of tumor cells stained with the antibody; lesser 
      reactivity was called negative. DMAb-3 stained 9/14 (64%) glial tumors, 4/13
      (31%) nonglial central nervous system tumors, 1/21 (5%) melanomas, 7/38 (18%)
      non-small cell carcinomas (NSCC), 1/15 (7%) small cell carcinomas (SCC), 0/9 (0%)
      lymphomas/leukemias, 2/10 (20%) sarcomas, 1/7 (14%) miscellaneous tumors and 2/2 
      (100%) reactive fluids. DMAb-7 recognized 14/14 (100%) glial tumors, 9/13 (69%)
      non-glial central nervous system tumors, 19/22 (86%) melanomas, 19/43 (44%) NSCC,
      5/15 (33%) SCC, 2/9 (22%) lymphomas/leukemias, 6/10 (60%) sarcomas, 1/7 (14%)
      miscellaneous tumors and 4/4 (100%) reactive fluids. DMAb-20 stained 6/14 (43%)
      glial tumors, 2/13 (15%) nonglial central nervous system tumors, 1/21 (5%)
      melanomas, 4/38 (10%) NSCC, 0/15 (0%) SCC, 0/9 (0%) lymphomas/leukemias, 1/10
      (10%) sarcomas, 1/7 (14%) miscellaneous tumors and 1/3 (33%) reactive fluids. The
      GD3-reactive DMAb-7 recognized a large portion of many tumor types and thus is
      not diagnostically useful alone. DMAb-3 and DMAb-20 were more selective and
      showed the strongest reactivity for glial tumors and minimal reactivity for
      melanomas, small cell carcinomas, and lymphomas or leukemias. DMAb-3 and DMAb-20 
      may be useful as components of a larger panel of MAbs in distinguishing between
      poorly differentiated tumors in samples derived from the central nervous system.
FAU - Vick, W W
AU  - Vick WW
AD  - Department of Pathology, Duke University Medical Center, Durham, North Carolina
      27710.
FAU - Tello, J W
AU  - Tello JW
FAU - Wikstrand, C J
AU  - Wikstrand CJ
FAU - He, X
AU  - He X
FAU - Longee, D
AU  - Longee D
FAU - Fredman, P
AU  - Fredman P
FAU - Svennerholm, L
AU  - Svennerholm L
FAU - Bigner, D D
AU  - Bigner DD
FAU - Johnston, W W
AU  - Johnston WW
FAU - Bigner, S H
AU  - Bigner SH
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - Switzerland
TA  - Acta Cytol
JT  - Acta cytologica
JID - 0370307
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Gangliosides)
SB  - IM
MH  - *Antibodies, Monoclonal
MH  - Carcinoma/pathology
MH  - Cytodiagnosis
MH  - Gangliosides/*immunology
MH  - Humans
MH  - Immunoenzyme Techniques
MH  - Lymphoma/pathology
MH  - Melanoma/pathology
MH  - Neoplasms/immunology/*pathology
MH  - Sarcoma/pathology
EDAT- 1992/09/01 00:00
MHDA- 1992/09/01 00:01
CRDT- 1992/09/01 00:00
PHST- 1992/09/01 00:00 [pubmed]
PHST- 1992/09/01 00:01 [medline]
PHST- 1992/09/01 00:00 [entrez]
PST - ppublish
SO  - Acta Cytol. 1992 Sep-Oct;36(5):697-705.

PMID- 15864748
OWN - NLM
STAT- MEDLINE
DCOM- 20051027
LR  - 20061115
IS  - 1021-7770 (Print)
IS  - 1021-7770 (Linking)
VI  - 12
IP  - 1
DP  - 2005
TI  - Lectinochemical studies on the glyco-recognition factors of a Tn
      (GalNAcalpha1-->Ser/Thr) specific lectin isolated from the seeds of Salvia
      sclarea.
PG  - 167-84
AB  - The lectin extracted from the seeds of Salvia sclarea (SSL) recognizes the Tn
      antigen (GalNAc alpha1-->Ser/Thr) expressed in certain human carcinomas. In
      previous studies, knowledge of the binding properties of SSL was restricted to
      GalNAcalpha1--> related oligosaccharides and glycopeptides. Thus, the
      requirements of functional groups in monosaccharide and high-density polyvalent
      carbohydrate structural units for SSL binding and an updated affinity profile
      were further evaluated by enzyme-linked lectinosorbent (ELLSA) and inhibition
      assays. Among the glycoproteins (gps) tested for interaction, a high density of
      exposed Tn-containing glycoproteins such as in the armadillo salivary Tn
      glycoprotein and asialo ovine salivary glycoprotein reacted best with SSL. When
      the gps were tested for inhibition of SSL binding, which was expressed as 50%
      nanogram inhibition, the high density polyvalent Tn present in macromolecules was
      the most potent inhibitor. Among the monosaccharide and carbohydrate structural
      units studied, which were expressed as nanomole inhibition, GalNAc
      alpha1-->3GalNAc beta1-->3Gal alpha1-->4Gal beta1-->4Glc (Fp), GalNAc
      alpha1-->3Gal beta1-->4Glc (A(L)), GalNAc alpha1-->3GalNAc beta1-->Me (F beta),
      GalNAc alpha1-->3GalNAc alpha1-->Me (F alpha) and GalNAc alpha1--> Ser/Thr (Tn)
      were the most active ligands, being 2.5-5.0 x 10(3) and 1.25-2.5 times more
      active than Gal and GalNAc, respectively. From the results, it is suggested that 
      the combining site of SSL is a shallow groove type, recognizing the
      monosaccharide of GalNAc as the major binding site or Tn up to the Forssman
      pentasaccharide (Fp). It can be concluded that the three critical factors for SSL
      binding are the -NH CH(3)CO at carbon-2 in Gal, the configuration of carbon-3 in 
      GalNAc, and the polyvalent Tn (GalNAc alpha1-->Ser/Thr) present in
      macromolecules. These results should assist in understanding the
      glyco-recognition factors involved in carbohydrate-lectin interactions in
      biological processes. The effect of the polyvalent F alpha, F beta and GalNAc
      beta1-->3Gal alpha1--> (P alpha) glycotopes on binding should be examined.
      However, this is hampered by the lack of availability of suitable reagents.
FAU - Wu, Albert M
AU  - Wu AM
AD  - Glyco-Immunochemistry Research Laboratory, Institute of Molecular and Cellular
      Biology, College of Medicine, Chang-Gung University, Kweishan, Taoyuan 333,
      Taiwan. amwu@mail.cgu.edu.tw
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - J Biomed Sci
JT  - Journal of biomedical science
JID - 9421567
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Glycoproteins)
RN  - 0 (Lectins)
RN  - 0 (Oligosaccharides)
RN  - 0 (Plant Extracts)
RN  - 0 (Tn antigen)
SB  - IM
MH  - Antigens, Tumor-Associated, Carbohydrate/*metabolism
MH  - Carbohydrate Sequence
MH  - Glycoproteins/chemistry/metabolism
MH  - Humans
MH  - Lectins/*metabolism
MH  - Molecular Sequence Data
MH  - Oligosaccharides/chemistry/metabolism
MH  - Plant Extracts/*chemistry
MH  - Protein Binding
MH  - Salvia/*chemistry
MH  - Seeds/*chemistry
EDAT- 2005/05/03 09:00
MHDA- 2005/10/28 09:00
CRDT- 2005/05/03 09:00
PHST- 2005/05/03 09:00 [pubmed]
PHST- 2005/10/28 09:00 [medline]
PHST- 2005/05/03 09:00 [entrez]
AID - 10.1007/s11373-004-8180-x [doi]
PST - ppublish
SO  - J Biomed Sci. 2005;12(1):167-84. doi: 10.1007/s11373-004-8180-x.

PMID- 9600862
OWN - NLM
STAT- MEDLINE
DCOM- 19980709
LR  - 20061115
IS  - 0882-4010 (Print)
IS  - 0882-4010 (Linking)
VI  - 24
IP  - 5
DP  - 1998 May
TI  - Monoclonal antibodies to the epitope alpha-Gal-(1-4)-beta-Gal-(1- of Moraxella
      catarrhalis LPS react with a similar epitope in type IV pili of Neisseria
      meningitidis.
PG  - 299-308
AB  - Murine monoclonal antibodies (MAbs) against the A, B and C LPS serotypes of M.
      catarrhalis were generated and their binding specificity was examined in an
      enzyme-linked immunosorbent assay (ELISA). Two broadly cross-reactive monoclonal 
      antibodies (MCA1 and MCC2) against the outer core region of LPS were further
      characterized. A panel of synthetic glycoproteins and glycolipids was used to
      determine the binding specificity of the MAbs. MCA1 and MCC2 bound specifically
      to alpha-Gal-(1-4)-beta-Gal of galabiose and globotriose glycoconjugates. The
      reactivity of the MAbs with galabiose was higher than that with globotriose. The 
      MAbs could recognize the alpha-Gal-(1-4)-beta-Gal epitope only when it was in a
      terminal position. MCA1 was further shown to react with a similar epitope in the 
      glycosylated type IV pili of N. meningitidis, which has been shown to contain a
      1-4 linked digalactose at the terminal part of the saccharide present in the
      pili. MCA1 could efficiently recognize this epitope indicating that it was
      exposed on the surface of the pili.
CI  - Copyright 1998 Academic Press Limited.
FAU - Rahman, M
AU  - Rahman M
AD  - Microbiology and Tumorbiology Center, Karolinska Institute, Stockholm, S-171 77, 
      Sweden.
FAU - Jonsson, A B
AU  - Jonsson AB
FAU - Holme, T
AU  - Holme T
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - Microb Pathog
JT  - Microbial pathogenesis
JID - 8606191
RN  - 0 (Antibodies, Bacterial)
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens, Bacterial)
RN  - 0 (Epitopes)
RN  - 0 (Lipopolysaccharides)
SB  - IM
MH  - Animals
MH  - Antibodies, Bacterial/immunology
MH  - *Antibodies, Monoclonal/immunology
MH  - Antibody Specificity/immunology
MH  - Antigens, Bacterial
MH  - Cross Reactions
MH  - Enzyme-Linked Immunosorbent Assay
MH  - Epitopes/*analysis
MH  - Fimbriae, Bacterial/*chemistry/immunology
MH  - Humans
MH  - Lipopolysaccharides/*analysis/immunology
MH  - Mice
MH  - Mice, Inbred BALB C
MH  - Moraxella (Branhamella) catarrhalis/*chemistry/immunology/pathogenicity
MH  - Neisseria meningitidis/*chemistry/immunology
EDAT- 1998/06/13 00:00
MHDA- 1998/06/13 00:01
CRDT- 1998/06/13 00:00
PHST- 1998/06/13 00:00 [pubmed]
PHST- 1998/06/13 00:01 [medline]
PHST- 1998/06/13 00:00 [entrez]
AID - S0882-4010(97)90191-1 [pii]
AID - 10.1006/mpat.1997.0191 [doi]
PST - ppublish
SO  - Microb Pathog. 1998 May;24(5):299-308. doi: 10.1006/mpat.1997.0191.

PMID- 16234847
OWN - NLM
STAT- MEDLINE
DCOM- 20060518
LR  - 20051019
IS  - 0829-8211 (Print)
IS  - 0829-8211 (Linking)
VI  - 83
IP  - 5
DP  - 2005 Oct
TI  - Characterization of murine monoclonal antibodies against Helicobacter pylori
      lipopolysaccharide specific for Lex and Ley blood group determinants.
PG  - 589-96
AB  - The cell envelope of Helicobacter pylori contains lipopolysaccharide (LPS), the
      O-chain of which expresses type 2 Lex and Ley blood group antigens, which mimic
      human gastric mucosal cell-surface glycoconjugates and may contribute to the
      survival of H. pylori in gastric mucosa. Here we describe the generation of
      monoclonal antibodies specific for Lex and Ley blood group determinants and the
      characterization of their binding properties using purified, structurally defined
      H. pylori LPS, synthetic glycoconjugates, and H. pylori cells. Analysis of
      oligosaccharide binding by SPR provided a rapid and reliable means for
      characterization of antibody affinities. One of the antibodies, anti-Lex, was of 
      IgG3 subclass and had superior binding characteristics as compared with the
      commercially available anti-Lex IgM. These antibodies could have potential in the
      immunodiagnosis of certain types of cancer, in serotyping of H. pylori isolates, 
      and in structure-function studies.
FAU - Altman, Eleonora
AU  - Altman E
AD  - Institute for Biological Sciences, NationalResearch Council of Canada, Ottawa, ON
      K1A 0R6, Canada. Eleonora.altman@nrc-cnrc.gc.ca
FAU - Harrison, Blair A
AU  - Harrison BA
FAU - Hirama, Tomoko
AU  - Hirama T
FAU - Chandan, Vandana
AU  - Chandan V
FAU - To, Rebecca
AU  - To R
FAU - MacKenzie, Roger
AU  - MacKenzie R
LA  - eng
PT  - Journal Article
PL  - Canada
TA  - Biochem Cell Biol
JT  - Biochemistry and cell biology = Biochimie et biologie cellulaire
JID - 8606068
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (DNA, Complementary)
RN  - 0 (Lewis Blood-Group System)
RN  - 0 (Lipopolysaccharides)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Antibodies, Monoclonal/*immunology
MH  - Antibody Affinity
MH  - Base Sequence
MH  - Carbohydrate Sequence
MH  - DNA, Complementary
MH  - Enzyme-Linked Immunosorbent Assay
MH  - Gastric Mucosa/microbiology
MH  - Helicobacter pylori/*immunology/isolation & purification
MH  - Lewis Blood-Group System/*immunology
MH  - Lipopolysaccharides/chemistry/*immunology/isolation & purification
MH  - Mice
MH  - Mice, Inbred BALB C
MH  - Microscopy, Fluorescence
MH  - Molecular Sequence Data
MH  - Sequence Homology, Amino Acid
MH  - Surface Plasmon Resonance
EDAT- 2005/10/20 09:00
MHDA- 2006/05/19 09:00
CRDT- 2005/10/20 09:00
PHST- 2005/10/20 09:00 [pubmed]
PHST- 2006/05/19 09:00 [medline]
PHST- 2005/10/20 09:00 [entrez]
AID - o05-052 [pii]
AID - 10.1139/o05-052 [doi]
PST - ppublish
SO  - Biochem Cell Biol. 2005 Oct;83(5):589-96. doi: 10.1139/o05-052.

PMID- 1371229
OWN - NLM
STAT- MEDLINE
DCOM- 19920323
LR  - 20161126
IS  - 0006-3002 (Print)
IS  - 0006-3002 (Linking)
VI  - 1123
IP  - 2
DP  - 1992 Jan 24
TI  - Generation of one set of monoclonal antibodies specific for b-pathway
      ganglio-series gangliosides.
PG  - 184-90
AB  - We established six murine monoclonal antibodies (MAbs) specific for b-pathway
      ganglio-series gangliosides by immunizing C3H/HeN mice with these purified
      gangliosides adsorbed to Salmonella minnesota mutant R595. The binding
      specificities of these MAbs were determined by an enzyme-linked immunosorbent
      assay and immunostaining on thin-layer chromatogram. These six MAbs, designated
      GGB19, GMR2, GMR7, GGR12, GMR5, and GGR13 reacted strongly with the gangliosides 
      GD3, O-Ac-GD3, GD2, GD1b, GT1b, and GQ1b, respectively, that were used as
      immunogens. All these MAbs except GGB19 showed highly restricted binding
      specificities, reacting only with the immunizing ganglioside. None of other
      various authentic gangliosides or neutral glycolipids were recognized. On the
      other hand, MAb GGB19 exhibited a broader specificity, cross-reacting weakly with
      O-Ac-GD3, GQ1b, and GT1a, but not with other gangliosides or neutral glycolipids.
      Using these MAbs, we determined the expression of these gangliosides, especially 
      GD1b, GT1b, and GQ1b on mouse, rat, and human leukemia cells. GD1b was expressed 
      on rat leukemia cells, but not on mouse and human leukemia cells tested. Neither 
      GT1b nor GQ1b was detected in these cell lines.
FAU - Ozawa, H
AU  - Ozawa H
AD  - Tokyo Metropolitan Institute of Medical Science, Department of Tumor Immunology, 
      Japan.
FAU - Kotani, M
AU  - Kotani M
FAU - Kawashima, I
AU  - Kawashima I
FAU - Tai, T
AU  - Tai T
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - Netherlands
TA  - Biochim Biophys Acta
JT  - Biochimica et biophysica acta
JID - 0217513
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Gangliosides)
RN  - 0 (Glycolipids)
SB  - IM
MH  - Animals
MH  - Antibodies, Monoclonal/*biosynthesis
MH  - *Antibody Specificity
MH  - Carbohydrate Sequence
MH  - Cell Line
MH  - Chromatography, Thin Layer
MH  - Enzyme-Linked Immunosorbent Assay
MH  - Flow Cytometry
MH  - Gangliosides/chemistry/*immunology
MH  - Glycolipids/immunology
MH  - Humans
MH  - Mice
MH  - Mice, Inbred BALB C
MH  - Mice, Inbred C3H
MH  - Mice, Nude
MH  - Molecular Sequence Data
MH  - Staining and Labeling
MH  - Tumor Cells, Cultured
EDAT- 1992/01/24 00:00
MHDA- 1992/01/24 00:01
CRDT- 1992/01/24 00:00
PHST- 1992/01/24 00:00 [pubmed]
PHST- 1992/01/24 00:01 [medline]
PHST- 1992/01/24 00:00 [entrez]
AID - 0005-2760(92)90110-H [pii]
PST - ppublish
SO  - Biochim Biophys Acta. 1992 Jan 24;1123(2):184-90.

PMID- 16155793
OWN - NLM
STAT- MEDLINE
DCOM- 20060127
LR  - 20151119
IS  - 0167-6806 (Print)
IS  - 0167-6806 (Linking)
VI  - 92
IP  - 3
DP  - 2005 Aug
TI  - Lack of polymorphism in MUC1 tandem repeats in cancer cells is related to breast 
      cancer progression in Japanese women.
PG  - 223-30
AB  - MUC1 is a transmembrane molecule characterized by a repeated sequence of 20 amino
      acid (TAP PAHGVTSAPDTRPAPGS). Abnormal overexpression of MUC1 in cancer cells is 
      thought to contribute to their aggressive growth, but molecular mechanisms
      associated with this effect are still unclear. Our current study aimed to clarify
      whether MUC1 expression as recognized by VU-3C6 anti-MUC1 mouse IgG monoclonal
      antibody (MAb) with a dominant epitope of 12 amino acids: GVTSAPDTRPAP,
      correlated with aggressive properties of human breast cancer. Immunohistochemical
      studies of 309 samples of formalin-fixed and paraffin-embedded materials showed
      no statistical correlation between MUC1 expression and clinicopathological
      parameters, as well as several breast cancer aggressiveness-related markers.
      Expression or nonexpression of MUC1 in 50 frozen samples, as determined by
      Western blotting, demonstrated no correlation with aggressive properties of
      breast cancer. However, samples with one MUC1-positive band more often had
      lymphatic vessel invasion and lymph node metastasis than those with more than two
      or three MUC1-positive bands (p<0.014 and p<0.043, respectively). Because VU-3C6 
      MAb recognizes MUC1 with short branches of O-glycosylated core carbohydrates, we 
      used immunohistological methods to examine Tn antigen (precursor antigen:
      GalNAcalpha-O-Ser/Thr), Thomsen-Friedenreich (T) antigen, and sialyl-Tn antigen
      (STn) antigen. We found a strong correlation between expression of MUC1 and Tn
      antigen (p<0.0006), and samples with Tn antigen expression had more lymphatic
      metastasis than those with no such expression (p<0.08). We concluded that the
      lack of polymorphic MUC1 expression with Tn antigen is one characteristic related
      to aggressive breast cancer.
FAU - Kawaguchi, Takanori
AU  - Kawaguchi T
AD  - Second Department of Pathology, Fukushima Medical University School of Medicine, 
      Hikariga-oka 1, Fukushima, 960-1295, Japan.
FAU - Takazawa, Hiroshi
AU  - Takazawa H
FAU - Imai, Shunsuke
AU  - Imai S
FAU - Morimoto, Junji
AU  - Morimoto J
FAU - Watanabe, Takanori
AU  - Watanabe T
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - Netherlands
TA  - Breast Cancer Res Treat
JT  - Breast cancer research and treatment
JID - 8111104
RN  - 0 (Antigens)
RN  - 0 (Antigens, Neoplasm)
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Biomarkers, Tumor)
RN  - 0 (Glycoproteins)
RN  - 0 (MUC1 protein, human)
RN  - 0 (Mucin-1)
RN  - 0 (Mucins)
RN  - 0 (Tn antigen)
SB  - IM
MH  - Antigens/*genetics
MH  - Antigens, Neoplasm
MH  - Antigens, Tumor-Associated, Carbohydrate/metabolism
MH  - Biomarkers, Tumor
MH  - Breast Neoplasms/epidemiology/*genetics/pathology
MH  - Carcinoma, Ductal, Breast/epidemiology/*genetics/pathology
MH  - Female
MH  - Glycoproteins/*genetics
MH  - Humans
MH  - Immunohistochemistry
MH  - Japan/epidemiology
MH  - Lymphatic Metastasis/genetics
MH  - Middle Aged
MH  - Mucin-1
MH  - Mucins/*genetics
MH  - Neoplasm Invasiveness/*genetics
MH  - *Polymorphism, Genetic
MH  - Tandem Repeat Sequences/genetics
EDAT- 2005/09/13 09:00
MHDA- 2006/01/28 09:00
CRDT- 2005/09/13 09:00
PHST- 2005/09/13 09:00 [pubmed]
PHST- 2006/01/28 09:00 [medline]
PHST- 2005/09/13 09:00 [entrez]
AID - 10.1007/s10549-005-2469-y [doi]
PST - ppublish
SO  - Breast Cancer Res Treat. 2005 Aug;92(3):223-30. doi: 10.1007/s10549-005-2469-y.

PMID- 1699667
OWN - NLM
STAT- MEDLINE
DCOM- 19901213
LR  - 20171116
IS  - 0092-8674 (Print)
IS  - 0092-8674 (Linking)
VI  - 63
IP  - 3
DP  - 1990 Nov 2
TI  - ELAM-1--dependent cell adhesion to vascular endothelium determined by a
      transfected human fucosyltransferase cDNA.
PG  - 475-84
AB  - Adhesion of circulating leukocytes to the vascular endothelium during
      inflammation is mediated in part by their interaction with the
      endothelial-leukocyte adhesion molecule ELAM-1. ELAM-1, a member of the LEC-CAM
      family of cell adhesion molecules, expresses an N-terminal carbohydrate
      recognition domain (CRD) homologous to various calcium-dependent mammalian
      lectins. However, the contribution of the CRD to cell adhesion and its
      carbohydrate binding specificity have not been elucidated. This study
      demonstrates that transfection of a human fucosyltransferase cDNA into nonmyeloid
      cell lines confers ELAM-1--dependent endothelial adhesion. Binding activity
      correlates with de novo cell surface expression of the sialylated Lewis x
      tetrasaccharide, whose biosynthesis is determined by the transfected
      fucosyltransferase cDNA. We propose that specific alpha(1,3)fucosyltransferases
      regulate cell adhesion to ELAM-1 by modulating cell surface expression of one or 
      more alpha(2,3)sialylated, alpha(1,3)fucosylated lactosaminoglycans represented
      by the sialyl Lewis x carbohydrate determinant.
FAU - Lowe, J B
AU  - Lowe JB
AD  - Howard Hughes Medical Institute, University of Michigan Medical School, Ann Arbor
      48109-0650.
FAU - Stoolman, L M
AU  - Stoolman LM
FAU - Nair, R P
AU  - Nair RP
FAU - Larsen, R D
AU  - Larsen RD
FAU - Berhend, T L
AU  - Berhend TL
FAU - Marks, R M
AU  - Marks RM
LA  - eng
GR  - DK38482/DK/NIDDK NIH HHS/United States
GR  - R01CA49256/CA/NCI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Cell
JT  - Cell
JID - 0413066
RN  - 0 (Cell Adhesion Molecules)
RN  - 0 (E-Selectin)
RN  - 0 (Gangliosides)
RN  - 0 (Lewis X Antigen)
RN  - 0 (Oligosaccharides)
RN  - EC 2.4.1.- (Fucosyltransferases)
SB  - IM
MH  - Animals
MH  - Cell Adhesion
MH  - Cell Adhesion Molecules/*physiology
MH  - Cell Line
MH  - Cloning, Molecular
MH  - E-Selectin
MH  - Endothelium, Vascular/cytology/*physiology
MH  - Flow Cytometry
MH  - Fucosyltransferases/genetics/*metabolism
MH  - Gangliosides
MH  - Guinea Pigs
MH  - Humans
MH  - Lewis X Antigen
MH  - Oligosaccharides/biosynthesis
MH  - *Transfection
EDAT- 1990/11/02 00:00
MHDA- 1990/11/02 00:01
CRDT- 1990/11/02 00:00
PHST- 1990/11/02 00:00 [pubmed]
PHST- 1990/11/02 00:01 [medline]
PHST- 1990/11/02 00:00 [entrez]
AID - 0092-8674(90)90444-J [pii]
PST - ppublish
SO  - Cell. 1990 Nov 2;63(3):475-84.

PMID- 9456330
OWN - NLM
STAT- MEDLINE
DCOM- 19980309
LR  - 20190508
IS  - 0021-9525 (Print)
IS  - 0021-9525 (Linking)
VI  - 140
IP  - 3
DP  - 1998 Feb 9
TI  - L-Selectin ligands that are O-glycoprotease resistant and distinct from MECA-79
      antigen are sufficient for tethering and rolling of lymphocytes on human high
      endothelial venules.
PG  - 721-31
AB  - During the process of lymphocyte recirculation, lymphocytes bind via L-selectin
      to sulfated sialyl-Lewisx (sLex)-containing carbohydrate ligands expressed on the
      surface of high endothelial venules (HEV). We have examined the expression of
      sLex on HEV using a panel of mAbs specific for sLex and sLex-related structures, 
      and have examined the function of different sLex-bearing structures using an in
      vitro assay of lymphocyte rolling on HEV. We report that three sLex mAbs, 2F3,
      2H5, and CSLEX-1, previously noted to bind with high affinity to
      glycolipid-linked sLex, vary in their ability to stain HEV in different lymphoid 
      tissues and bind differentially to O-linked versus N-linked sLex on
      glycoproteins. Treatment of tissue sections with neuraminidase abolished staining
      with all three mAbs but slightly increased staining with MECA-79, a mAb to a
      sulfation-dependent HEV-associated carbohydrate determinant. Treatment of tissue 
      sections with O-sialoglycoprotease under conditions that removed the vast
      majority of MECA-79 staining, only partially reduced staining with the 2F3 and
      2H5 mAbs. Using a novel rolling assay in which cells bind under flow to HEV of
      frozen tissue sections, we demonstrate that a pool of
      O-sialoglycoprotease-resistant molecules is present on HEV that is sufficient for
      attachment and rolling of lymphocytes via L-selectin. This interaction is not
      inhibited by the mAb MECA-79. Furthermore, MECA-79 mAb blocks binding to
      untreated sections by only 30%, whereas the sLex mAb 2H5 blocks binding by
      approximately 60% and a combination of MECA-79 and 2H5 mAb blocks binding by 75%.
      We conclude that a pool of O-glycoprotease-resistant sLex-like L-selectin ligands
      exist on human HEV that is distinct from the mucin-associated moieties recognized
      by MECA-79 mAb. We postulate that these ligands may participate in lymphocyte
      binding to HEV.
FAU - Clark, R A
AU  - Clark RA
AD  - The Center for Blood Research and Harvard Medical School, Department of
      Pathology, Boston, Massachusetts 02115, USA.
FAU - Fuhlbrigge, R C
AU  - Fuhlbrigge RC
FAU - Springer, T A
AU  - Springer TA
LA  - eng
GR  - R01 CA031798/CA/NCI NIH HHS/United States
GR  - R37 CA031798/CA/NCI NIH HHS/United States
GR  - CA31798/CA/NCI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - J Cell Biol
JT  - The Journal of cell biology
JID - 0375356
RN  - 0
      (5-acetylneuraminyl-(2-3)-galactosyl-(1-4)-(fucopyranosyl-(1-3))-N-acetylglucosam
      ine)
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens, Surface)
RN  - 0 (L-selectin counter-receptors)
RN  - 0 (Ligands)
RN  - 0 (Membrane Proteins)
RN  - 0 (Oligosaccharides)
RN  - 126880-86-2 (L-Selectin)
RN  - EC 3.2.1.18 (Neuraminidase)
RN  - EC 3.4.24.- (Metalloendopeptidases)
RN  - EC 3.4.24.57 (O-sialoglycoprotein endopeptidase)
SB  - IM
MH  - Antibodies, Monoclonal
MH  - Antigens, Surface/immunology/metabolism
MH  - Cell Movement
MH  - Endothelium, Lymphatic/chemistry/*metabolism
MH  - Humans
MH  - Immunoblotting
MH  - L-Selectin/*metabolism
MH  - Ligands
MH  - Lymphocytes/*metabolism/physiology
MH  - Lymphoid Tissue/chemistry/metabolism
MH  - Membrane Proteins
MH  - Metalloendopeptidases/metabolism
MH  - Neuraminidase/metabolism
MH  - Oligosaccharides/analysis/immunology/*metabolism
PMC - PMC2140156
EDAT- 1998/03/14 00:00
MHDA- 1998/03/14 00:01
CRDT- 1998/03/14 00:00
PHST- 1998/03/14 00:00 [pubmed]
PHST- 1998/03/14 00:01 [medline]
PHST- 1998/03/14 00:00 [entrez]
AID - 10.1083/jcb.140.3.721 [doi]
PST - ppublish
SO  - J Cell Biol. 1998 Feb 9;140(3):721-31. doi: 10.1083/jcb.140.3.721.

PMID- 3880667
OWN - NLM
STAT- MEDLINE
DCOM- 19850125
LR  - 20181211
IS  - 0008-5472 (Print)
IS  - 0008-5472 (Linking)
VI  - 45
IP  - 1
DP  - 1985 Jan
TI  - Comparative immunoperoxidase demonstration of T-antigens in human colorectal
      carcinomas and morphologically abnormal mucosa.
PG  - 447-52
AB  - The T-antigen (Thomsen-Friedenreich antigen) is a well-characterized
      tumor-associated glycoprotein that is immunologically reactive in humans. In
      order to demonstrate the presence of T-antigens in colorectal tissue, benign and 
      malignant tissue from 46 patients with colorectal cancer were examined by means
      of an immunoperoxidase method. Peanut agglutinin and a polyclonal immune rabbit
      antiserum were used to demonstrate T-antigens on 72% of formalin-fixed malignant 
      specimens and on more than 92% of frozen malignant specimens. Both ligands bound 
      to the cell membrane and secreted mucus, but only the rabbit serum showed routine
      staining of the cytoplasm. The T-antigen distribution was heterogeneous without
      relation to degree of differentiation. Transitional mucosa adjacent to malignant 
      tissue showed a strong anti-T binding to secreted mucus. Slightly morphologically
      altered crypts remote from the carcinoma expressed T-antigens. Unexpectedly, both
      ligands bound to nerve cells of the enteric ganglia. These contain gangliosides
      with immunodominant oligosaccharides identical with those on the T-antigen.
      Therefore, cross-reactions might have occurred between the gangliosides and the
      used ligands. The T-antigens now seem to be present in various widespread
      cancers, and they probably occur early in malignant transformation.
FAU - Orntoft, T F
AU  - Orntoft TF
FAU - Mors, N P
AU  - Mors NP
FAU - Eriksen, G
AU  - Eriksen G
FAU - Jacobsen, N O
AU  - Jacobsen NO
FAU - Poulsen, H S
AU  - Poulsen HS
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Cancer Res
JT  - Cancer research
JID - 2984705R
RN  - 0 (Antibodies)
RN  - 0 (Antigens, Neoplasm)
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Disaccharides)
RN  - 3554-90-3 (Thomsen-Friedenreich antigen)
RN  - 3HG052TF3I (Thomsen-Friedenreich antibodies)
SB  - IM
MH  - Antibodies/*analysis
MH  - Antigens, Neoplasm/*analysis
MH  - *Antigens, Tumor-Associated, Carbohydrate
MH  - Colonic Neoplasms/*immunology/pathology
MH  - Disaccharides/*analysis
MH  - Humans
MH  - Immunoenzyme Techniques
MH  - Intestinal Mucosa/*immunology/pathology
MH  - Rectal Neoplasms/*immunology/pathology
EDAT- 1985/01/01 00:00
MHDA- 1985/01/01 00:01
CRDT- 1985/01/01 00:00
PHST- 1985/01/01 00:00 [pubmed]
PHST- 1985/01/01 00:01 [medline]
PHST- 1985/01/01 00:00 [entrez]
PST - ppublish
SO  - Cancer Res. 1985 Jan;45(1):447-52.

PMID- 14741734
OWN - NLM
STAT- MEDLINE
DCOM- 20040302
LR  - 20071205
IS  - 0024-3205 (Print)
IS  - 0024-3205 (Linking)
VI  - 74
IP  - 14
DP  - 2004 Feb 20
TI  - Recognition profile of Bauhinia purpurea agglutinin (BPA).
PG  - 1763-79
AB  - Bauhinia purpurea agglutinin (BPA) is a Galbeta1-3GalNAc (T) specific leguminous 
      lectin that has been widely used in multifarious cytochemical and immunological
      studies of cells and tissues under pathological or malignant conditions. Despite 
      these diverse applications, knowledge of its carbohydrate specificity was mainly 
      limited to molecular or submolecular T disaccharides. Thus, the requirement of
      high density polyvalent or multi-antennary carbohydrate structural units for BPA 
      binding and an updated affinity profile were further evaluated by enzyme-linked
      lectinosorbent (ELLSA) and inhibition assays. Among the glycoproteins (gps)
      tested and expressed as 50% nanogram inhibition, the high density polyvalent
      GalNAcalpha1-Ser/Thr (Tn) and Galbeta1-3/4GlcNAc (I/II) glycotopes present on
      macromolecules generated a great enhancement of binding affinity for BPA as
      compared to their monomers. The most potent inhibitors were a Tn-containing gp
      (asialo OSM) and a I/II containing gp (human blood group precursor gp), which
      were up to 1.7 x 10(4) and 2.3 x 10(3) times more potent than monovalent Gal and 
      GalNAc, respectively. However, multi-antennary glycopeptides, such as
      tri-antennary Galbeta1-4GlcNAc, which was slightly more active than II or Gal,
      gave only a minor contribution. Regarding the carbohydrate structural units
      studied by the inhibition assay, blood group GalNAcbeta1-3/4Gal (P/S) active
      glycotopes were active ligands. The overall binding profile of BPA was: high
      density polyvalent T/Tn and II clusters >>> Tn-glycopeptides (M.W. <3.0 x
      10(3))/Talpha monomer > monovalent P/S > Tn monomer and GalNAc > tri-antennary II
      > Gal >> Man and Glc (inactive). These findings give evidence for the binding of 
      this lectin to dense cell surface T, Tn and I/II glycoconjugates and should
      facilitate future usage of this lectin in biotechnological and medical
      applications.
FAU - Wu, Albert M
AU  - Wu AM
AD  - Glyco-Immunochemistry Research Laboratory, Chang-Gung Medical College, Institute 
      of Molecular and Cellular Biology, Kwei-San, Tao-Yuan 333, Taiwan.
      amwu@mail.cgu.edu.tw
FAU - Wu, June H
AU  - Wu JH
FAU - Liu, Jia-Hua
AU  - Liu JH
FAU - Singh, Tanuja
AU  - Singh T
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - Netherlands
TA  - Life Sci
JT  - Life sciences
JID - 0375521
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Bauhinia purpurea lectin)
RN  - 0 (Glycoconjugates)
RN  - 0 (Glycoproteins)
RN  - 0 (Plant Lectins)
RN  - 0 (Tn antigen)
RN  - 3554-90-3 (Thomsen-Friedenreich antigen)
SB  - IM
MH  - Antigens, Tumor-Associated, Carbohydrate/*metabolism
MH  - Binding Sites
MH  - Dose-Response Relationship, Drug
MH  - *Fabaceae
MH  - Glycoconjugates/metabolism
MH  - Glycoproteins/*metabolism
MH  - Humans
MH  - Plant Lectins/antagonists & inhibitors/*metabolism
MH  - Substrate Specificity
EDAT- 2004/01/27 05:00
MHDA- 2004/03/03 05:00
CRDT- 2004/01/27 05:00
PHST- 2004/01/27 05:00 [pubmed]
PHST- 2004/03/03 05:00 [medline]
PHST- 2004/01/27 05:00 [entrez]
AID - S0024320503010944 [pii]
PST - ppublish
SO  - Life Sci. 2004 Feb 20;74(14):1763-79.

PMID- 6619101
OWN - NLM
STAT- MEDLINE
DCOM- 19831123
LR  - 20190511
IS  - 0021-924X (Print)
IS  - 0021-924X (Linking)
VI  - 94
IP  - 1
DP  - 1983 Jul
TI  - Differential reactivities of fucosyl GM1 and GM1 gangliosides on rat erythrocyte 
      membrane revealed by analysis with anti-fucosyl GM1 and GM1 antisera.
PG  - 1-10
AB  - Rat erythrocytes contained ganglio-series gangliosides, GM1, fucosyl GM1, and
      GD1a, in a high concentration. The concentrations of GM1, fucosyl GM1, and GD1a
      in rat erythrocyte ghosts were 889.0 nmol, 470.6 nmol, and 462.0 nmol per g dry
      weight, respectively, and the molar ratio of lipid-bound sialic acid, cholesterol
      and lipid-bound phosphorus was 3.1:73.9:100.0. The reactions of fucosyl GM1 and
      GM1 on rat erythrocytes with rabbit anti-fucosyl GM1 and anti-GM1 antisera were
      measured by means of haemolysis in the presence of complement and a binding assay
      of antibodies with a FACS after staining erythrocytes by the indirect membrane
      immunofluorescence technique. When measured by ELISA, anti-fucosyl GM1 antiserum 
      was found to react almost exclusively with fucosyl GM1 with a slight
      cross-reaction with GM1, but anti-GM1 antiserum cross-reacted to a significant
      extent with asialo GM1. Rat erythrocytes were haemolyzed specifically with
      anti-fucosyl GM1 antiserum, but not with antisera to GM1, asialo GM1, asialo GM2,
      Forssman and globoside, and the haemolysis was proved to be definitely caused by 
      the specific recognition of fucosyl GM1 on rat erythrocytes by anti-fucosyl GM1
      antibody according to the haemolysis inhibition reaction using various
      glycosphingolipid-containing liposomes as inhibitors. In addition, although the
      binding of anti-fucosyl GM1 antibody on rat erythrocytes was clearly demonstrated
      with a FACS, anti-GM1 antibody did not bind. The observations that the haemolysis
      of rat erythrocytes and the binding of antibody to rat erythrocytes were found
      only with anti-fucosyl GM1 antiserum, and not with anti-GM1 antiserum, but that
      nevertheless the titer of anti-GM1 antiserum was higher than that of anti-fucosyl
      GM1 antiserum and GM1 on rat erythrocytes was more abundant in concentration than
      fucosyl GM1, seem to be a matter of great importance in assessing the specificity
      of anti-ganglioside antibody and the surface distribution of gangliosides on the 
      cell.
FAU - Iwamori, M
AU  - Iwamori M
FAU - Shimomura, J
AU  - Shimomura J
FAU - Tsuyuhara, S
AU  - Tsuyuhara S
FAU - Mogi, M
AU  - Mogi M
FAU - Ishizaki, S
AU  - Ishizaki S
FAU - Nagai, Y
AU  - Nagai Y
LA  - eng
PT  - Comparative Study
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - J Biochem
JT  - Journal of biochemistry
JID - 0376600
RN  - 0 (Gangliosides)
RN  - 0 (Glycosphingolipids)
RN  - 0 (Immune Sera)
RN  - 0 (Lipids)
RN  - 37758-47-7 (G(M1) Ganglioside)
RN  - 71812-11-8 (fucosyl GM1 ganglioside)
SB  - IM
MH  - Animals
MH  - Complement Fixation Tests
MH  - Enzyme-Linked Immunosorbent Assay
MH  - Erythrocyte Membrane/*metabolism
MH  - Fluorescence
MH  - G(M1) Ganglioside/analogs & derivatives/*blood/immunology
MH  - Gangliosides/*blood
MH  - Glycosphingolipids/blood
MH  - Goats
MH  - Hemolysis/drug effects
MH  - Immune Sera
MH  - In Vitro Techniques
MH  - Lipids/blood
MH  - Mice
MH  - Rabbits
MH  - Rats
MH  - Rats, Inbred Strains
EDAT- 1983/07/01 00:00
MHDA- 1983/07/01 00:01
CRDT- 1983/07/01 00:00
PHST- 1983/07/01 00:00 [pubmed]
PHST- 1983/07/01 00:01 [medline]
PHST- 1983/07/01 00:00 [entrez]
AID - 10.1093/oxfordjournals.jbchem.a134316 [doi]
PST - ppublish
SO  - J Biochem. 1983 Jul;94(1):1-10. doi: 10.1093/oxfordjournals.jbchem.a134316.

PMID- 9428379
OWN - NLM
STAT- MEDLINE
DCOM- 19980127
LR  - 20180213
IS  - 0030-2414 (Print)
IS  - 0030-2414 (Linking)
VI  - 55
IP  - 1
DP  - 1998 Jan-Feb
TI  - F1 alpha: a novel mucin antigen associated with gastric carcinogenesis.
PG  - 70-6
AB  - In a previous study, we obtained a novel monoclonal antibody (F1 alpha-75)
      directed against a synthetic mucin antigen termed F1 alpha, and demonstrated that
      this antigen was expressed in a high percentage (80.2%; 89/111) of gastric
      carcinomas. In the present study, we compared the expression of F1 alpha with
      that of sialyl-Tn antigen, a mucin antigen similar to F1 alpha, in 54 human early
      gastric carcinomas, intestinal metaplasia and adenomatous polyps of the stomach
      to determine how differences in the expression of these antigens correlated with 
      gastric carcinogenesis. The rate of expression of F1 alpha in early gastric
      carcinoma tissues, 81.5%, was higher than that of sialyl-Tn antigen, 57.4%. No
      correlation was found between the rate of expression and histological type, depth
      of cancerous invasion or lymph node metastasis. Sialyl-Tn antigen was extensively
      expressed in 77.5% of specimens of complete intestinal metaplasia and in 78.6% of
      those of incomplete intestinal metaplasia; however, the expression of F1 alpha in
      those specimens was rare and sporadic, with rates of only 25.0 and 27.7%,
      respectively. In adenomatous polyps, the rate of expression of F1 alpha is 6.25% 
      and that of sialyl-Tn antigen is 43.8%. Our findings indicate that F1 alpha is a 
      more specific antigen for gastric cancer than sialyl-Tn antigen, and that F1
      alpha is an antigen associated with carcinogenesis of the stomach.
FAU - Yamashita, Y
AU  - Yamashita Y
AD  - First Department of Surgery, Osaka City University Medical School, Japan.
FAU - Chung, Y S
AU  - Chung YS
FAU - Sawada, T
AU  - Sawada T
FAU - Horie, R
AU  - Horie R
FAU - Saito, T
AU  - Saito T
FAU - Murayama, K
AU  - Murayama K
FAU - Kannagi, R
AU  - Kannagi R
FAU - Sowa, M
AU  - Sowa M
LA  - eng
PT  - Journal Article
PL  - Switzerland
TA  - Oncology
JT  - Oncology
JID - 0135054
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (F1alpha antigen)
RN  - 0 (Glycoproteins)
SB  - IM
MH  - Antigens, Tumor-Associated, Carbohydrate/*analysis/chemistry
MH  - Carcinoma/immunology
MH  - Gene Expression Regulation, Neoplastic
MH  - Glycoproteins/*analysis/chemistry
MH  - Humans
MH  - Immunohistochemistry
MH  - Metaplasia/immunology
MH  - Polyps/immunology
MH  - Stomach/immunology/pathology
MH  - Stomach Neoplasms/*immunology
EDAT- 1998/01/15 04:19
MHDA- 2000/10/06 11:01
CRDT- 1998/01/15 04:19
PHST- 1998/01/15 04:19 [pubmed]
PHST- 2000/10/06 11:01 [medline]
PHST- 1998/01/15 04:19 [entrez]
AID - ocl55070 [pii]
AID - 10.1159/000011838 [doi]
PST - ppublish
SO  - Oncology. 1998 Jan-Feb;55(1):70-6. doi: 10.1159/000011838.

PMID- 9874495
OWN - NLM
STAT- MEDLINE
DCOM- 19990122
LR  - 20161124
IS  - 0300-9475 (Print)
IS  - 0300-9475 (Linking)
VI  - 48
IP  - 6
DP  - 1998 Dec
TI  - Tyrosine phosphorylation of p72syk induced by anti-9-O-acetyl GD3 antibodies in
      human peripheral blood mononuclear cells.
PG  - 615-22
AB  - We have previously shown that a subpopulation of peripheral blood CD4+ T-cells
      are strongly positive for the ganglioside 9-O-acetyl GD3. Treatment of peripheral
      blood mononuclear cells (PBMC) with monoclonal anti-9-O-acetyl GD3 antibodies
      (MoAb 27A) induced a dose-dependent proliferative response in the cells. Here we 
      show that binding of 27A IgG to PBMC induces rapid tyrosine phosphorylation of
      p72syk and mobilization of phosphoinositides. Equal phosphorylation was not seen 
      after stimulation of PBMC with anti-GD3 antibodies (MoAb R24) despite the
      apparent similar cell surface distribution of the two gangliosides. This suggests
      that the O-acetyl modification enhances the signal transduction mediated by GD3
      ganglioside.
FAU - Reivinen, J
AU  - Reivinen J
AD  - Department of Bacteriology and Immunology, The Haartman Institute, University of 
      Helsinki, Finland.
FAU - Holthofer, H
AU  - Holthofer H
FAU - Miettinen, A
AU  - Miettinen A
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - Scand J Immunol
JT  - Scandinavian journal of immunology
JID - 0323767
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens, Surface)
RN  - 0 (Enzyme Precursors)
RN  - 0 (Gangliosides)
RN  - 0 (Intracellular Signaling Peptides and Proteins)
RN  - 0 (Phosphatidylinositols)
RN  - 42HK56048U (Tyrosine)
RN  - 62010-37-1 (ganglioside, GD3)
RN  - 98743-26-1 (9-O-acetyl-GD3 ganglioside)
RN  - EC 2.7.10.1 (Protein-Tyrosine Kinases)
RN  - EC 2.7.10.2 (SYK protein, human)
RN  - EC 2.7.10.2 (Syk Kinase)
SB  - IM
MH  - Antibodies, Monoclonal/metabolism
MH  - Antigens, Surface/immunology/*metabolism
MH  - Cell Membrane/metabolism
MH  - Enzyme Precursors/*metabolism
MH  - Gangliosides/immunology/*metabolism
MH  - Humans
MH  - Intracellular Signaling Peptides and Proteins
MH  - Leukocytes, Mononuclear/metabolism
MH  - Phosphatidylinositols/metabolism
MH  - Phosphorylation
MH  - Protein-Tyrosine Kinases/*metabolism
MH  - Syk Kinase
MH  - Tyrosine/*metabolism
EDAT- 1999/01/05 00:00
MHDA- 1999/01/05 00:01
CRDT- 1999/01/05 00:00
PHST- 1999/01/05 00:00 [pubmed]
PHST- 1999/01/05 00:01 [medline]
PHST- 1999/01/05 00:00 [entrez]
PST - ppublish
SO  - Scand J Immunol. 1998 Dec;48(6):615-22.

PMID- 11549599
OWN - NLM
STAT- MEDLINE
DCOM- 20011011
LR  - 20181113
IS  - 0002-9440 (Print)
IS  - 0002-9440 (Linking)
VI  - 159
IP  - 3
DP  - 2001 Sep
TI  - Involvement of lipid rafts in nephrin phosphorylation and organization of the
      glomerular slit diaphragm.
PG  - 1069-77
AB  - NPHS1 has recently been identified as the gene whose mutations cause congenital
      nephrotic syndrome of the Finnish type. The respective gene product nephrin is a 
      transmembrane protein expressed in glomerular podocytes and primarily localized
      to the glomerular slit diaphragm. This interpodocyte junction functions in the
      glomerular filtration by restricting the passage of plasma proteins into the
      urinary space in a size-selective manner. The functional role of nephrin in this 
      filtration process is so far not very well understood. In this study, we show
      that nephrin associates in an oligomerized form with signaling microdomains, also
      known as lipid rafts, and that these localize to the slit diaphragm. We also show
      that the nephrin-containing rafts can be immunoisolated with the 27A antibody
      recognizing a podocyte-specific 9-O-acetylated GD3 ganglioside. In a previous
      study it has been shown that the in vivo injection of this antibody leads to
      morphological changes of the filtration slits resembling foot process effacement.
      Here, we report that, in this model of foot process effacement, nephrin
      dislocates to the apical pole of the narrowed filtration slits and also that it
      is tyrosine phosphorylated. We suggest that lipid rafts are important in the
      spatial organization of the glomerular slit diaphragm under physiological and
      pathological conditions.
FAU - Simons, M
AU  - Simons M
AD  - Department of Medicine and Department of Anatomy and Structural Biology, Albert
      Einstein College of Medicine, Bronx, New York 10461, USA.
FAU - Schwarz, K
AU  - Schwarz K
FAU - Kriz, W
AU  - Kriz W
FAU - Miettinen, A
AU  - Miettinen A
FAU - Reiser, J
AU  - Reiser J
FAU - Mundel, P
AU  - Mundel P
FAU - Holthofer, H
AU  - Holthofer H
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Am J Pathol
JT  - The American journal of pathology
JID - 0370502
RN  - 0 (Antibodies)
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Detergents)
RN  - 0 (Gangliosides)
RN  - 0 (Immunoglobulin G)
RN  - 0 (Lipids)
RN  - 0 (Membrane Proteins)
RN  - 0 (Proteins)
RN  - 0 (nephrin)
RN  - 42HK56048U (Tyrosine)
RN  - 97C5T2UQ7J (Cholesterol)
RN  - 98743-26-1 (9-O-acetyl-GD3 ganglioside)
SB  - AIM
SB  - IM
MH  - Animals
MH  - Antibodies
MH  - Antibodies, Monoclonal/pharmacology
MH  - Cell Membrane/drug effects
MH  - Cholesterol/physiology
MH  - Detergents/pharmacology
MH  - Drug Resistance
MH  - Endoplasmic Reticulum/physiology
MH  - Female
MH  - Gangliosides/pharmacology
MH  - Immunoglobulin G/pharmacology
MH  - Kidney Glomerulus/*metabolism/*ultrastructure
MH  - Lipids/physiology
MH  - Membrane Proteins
MH  - Nephrotic Syndrome/*metabolism/*pathology
MH  - Phosphorylation
MH  - Precipitin Tests
MH  - Proteins/*metabolism/physiology
MH  - Rats
MH  - Rats, Sprague-Dawley
MH  - Tyrosine/metabolism
PMC - PMC1850447
EDAT- 2001/09/11 10:00
MHDA- 2001/10/12 10:01
CRDT- 2001/09/11 10:00
PHST- 2001/09/11 10:00 [pubmed]
PHST- 2001/10/12 10:01 [medline]
PHST- 2001/09/11 10:00 [entrez]
AID - S0002-9440(10)61782-8 [pii]
AID - 10.1016/S0002-9440(10)61782-8 [doi]
PST - ppublish
SO  - Am J Pathol. 2001 Sep;159(3):1069-77. doi: 10.1016/S0002-9440(10)61782-8.

PMID- 2426270
OWN - NLM
STAT- MEDLINE
DCOM- 19860919
LR  - 20071114
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 261
IP  - 24
DP  - 1986 Aug 25
TI  - Domain-specific distribution of carbohydrates in human fibronectins and the
      transformation-dependent translocation of branched type 2 chain defined by
      monoclonal antibody C6.
PG  - 11295-301
AB  - Fibronectins purified from human plasma (termed pFN), spent culture media of
      human fibroblasts WI38 (termed cFN), and SV40 virus-transformed WI38/VA13 cells
      (termed tFN) and their cleavage fragments were compared with respect to their
      binding activities to lectins and anti-carbohydrate antibodies reacting with
      chemically well-defined structures. The following findings were of particular
      interest. About 25-35% of cFN and tFN carried a binary sialosyl type 2 chain
      (NeuAc alpha 2----3/or 6Gal beta 1----4GlcNAc) linked beta 1----3/beta 1----6 to 
      the galactose residue and defined by monoclonal antibody C6. This structure was
      not detected in pFN. In cFN, the C6-defined structure was localized within the
      gelatin-binding domain, whereas in tFN the same structure was absent from this
      domain but was located at the NH2-terminal region of the central domain. Other
      carbohydrate determinants, defined by Ricinus communis lectin and concanavalin A 
      before and after sialidase treatment, showed essentially identical domain
      distribution patterns among cFN, tFN, and pFN and were all located at the
      gelatin-binding domain (44 kDa), its precursor (60 kDa), and the Cell/Hep-2
      domain (155/145 kDa). Although both cFN and tFN were reactive with lentil lectin,
      pFN was not. Fibronectin from transformed cells (tFN) showed much greater
      reactivity than cFN and pFN with wheat germ lectin before sialidase treatment and
      showed enhanced reactivity with R. communis lectin and peanut lectin after
      sialidase treatment, indicating that tFN is more highly sialylated than cFN and
      pFN. All fibronectins examined were strongly reactive with monoclonal antibody
      AH8-28, which binds to Gal beta 1----3GalNAc residues, and this reactivity was
      localized to both the NH2-terminal half and COOH-terminal half of the
      S-cyanylation-cleaved fibronectin molecule.
FAU - Nichols, E J
AU  - Nichols EJ
FAU - Fenderson, B A
AU  - Fenderson BA
FAU - Carter, W G
AU  - Carter WG
FAU - Hakomori, S
AU  - Hakomori S
LA  - eng
GR  - CA23907/CA/NCI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Carbohydrates)
RN  - 0 (Culture Media)
RN  - 0 (Epitopes)
RN  - 0 (Fibronectins)
SB  - IM
MH  - *Antibodies, Monoclonal
MH  - Carbohydrates/*analysis
MH  - *Cell Transformation, Viral
MH  - Culture Media
MH  - Epitopes/analysis
MH  - Fibroblasts/analysis
MH  - Fibronectins/*analysis
MH  - Humans
MH  - Simian virus 40
EDAT- 1986/08/25 00:00
MHDA- 1986/08/25 00:01
CRDT- 1986/08/25 00:00
PHST- 1986/08/25 00:00 [pubmed]
PHST- 1986/08/25 00:01 [medline]
PHST- 1986/08/25 00:00 [entrez]
PST - ppublish
SO  - J Biol Chem. 1986 Aug 25;261(24):11295-301.

PMID- 8793500
OWN - NLM
STAT- MEDLINE
DCOM- 19961107
LR  - 20180217
IS  - 0378-7346 (Print)
IS  - 0378-7346 (Linking)
VI  - 41
IP  - 4
DP  - 1996
TI  - Tn and sialyl-Tn antigens as potential prognostic markers in human ovarian
      carcinoma.
PG  - 278-83
AB  - OBJECTIVE: Carcinoma-associated Tn and sialyl-Tn antigens have been shown to aid 
      in the prediction of tumor aggressiveness. The purpose of this study was to
      evaluate the prognostic value of Tn and sialyl-Tn antigen expression in human
      ovarian carcinoma. METHODS: Formalin-fixed, paraffin-embedded tissue sections
      from 32 primary ovarian carcinomas, 6 benign and 2 normal ovarian tissues were
      immunostained using monoclonal antibodies against Tn and sialyl-Tn antigens and a
      streptavidin-biotin-peroxidase method Immunostainings were assessed
      semiquantitatively and the measurements were then correlated with the established
      prognostic factors of ovarian carcinoma. i.e. disease stage and histological
      grade. RESULTS: Of the 32 ovarian carcinomas, 22 (69%) expressed Tn and 28
      (87.5%) sialyl-Tn antigens. Immunostaining measures for Tn antigen were
      significantly associated with the clinical stage (p < or = 0.02) and histological
      grade (p < or = 0.05) of the tumors. The results for sialyl-Tn antigen revealed
      more significant associations with the clinical stage (p < or = 0.002) and
      histological grade (p < or = 0.007). The clinical stage and histologic grade of
      the tumors were also highly correlated with each other. Similarly, combined Tn
      and sialyl-Tn antigen expression revealed significant correlations with the
      prognostic factors. Benign and normal ovarian tissues showed no reactive Tn and
      sialyl-Tn antigen. CONCLUSIONS: The extent of Tn and sialyl-Tn antigen expression
      in primary ovarian carcinoma may contribute to the prognosis of the disease.
FAU - Ogawa, H
AU  - Ogawa H
AD  - Department of Obstetrics and Gynecology, WHO Collaborating Center for Research
      and Training in Diagnostic Electron Microscopy, Nippon Medical School, Tokyo,
      Japan.
FAU - Ghazizadeh, M
AU  - Ghazizadeh M
FAU - Araki, T
AU  - Araki T
LA  - eng
PT  - Journal Article
PL  - Switzerland
TA  - Gynecol Obstet Invest
JT  - Gynecologic and obstetric investigation
JID - 7900587
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Biomarkers, Tumor)
RN  - 0 (Tn antigen)
RN  - 0 (sialosyl-Tn antigen)
SB  - IM
MH  - Antigens, Tumor-Associated, Carbohydrate/*analysis
MH  - Biomarkers, Tumor/*analysis
MH  - Female
MH  - Humans
MH  - Immunoenzyme Techniques
MH  - Ovarian Neoplasms/*immunology/pathology
MH  - Prognosis
EDAT- 1996/01/01 00:00
MHDA- 1996/01/01 00:01
CRDT- 1996/01/01 00:00
PHST- 1996/01/01 00:00 [pubmed]
PHST- 1996/01/01 00:01 [medline]
PHST- 1996/01/01 00:00 [entrez]
AID - 10.1159/000292284 [doi]
PST - ppublish
SO  - Gynecol Obstet Invest. 1996;41(4):278-83. doi: 10.1159/000292284.

PMID- 10975398
OWN - NLM
STAT- MEDLINE
DCOM- 20010208
LR  - 20190116
IS  - 1042-8194 (Print)
IS  - 1026-8022 (Linking)
VI  - 39
IP  - 1-2
DP  - 2000 Sep
TI  - Differential expression of sialyl and non-sialyl-CD15 antigens on
      Hodgkin-Reed-Sternberg cells: significance in Hodgkin's disease.
PG  - 185-94
AB  - CD15 expression has been used for years to confirm the diagnosis of Hodgkin's
      disease (HD). Little is, however, known on the relevance of the CD15 antigen to
      the pathobiology of the disease and there is conflicting evidence as to the
      prognostic value of its expression. To investigate the significance of the
      differential expression of CD15 in Hodgkin's disease, a retrospective study of
      102 patients with "classical" Hodgkin's disease was performed.
      Immunohistochemical studies were carried out using antibodies against two types
      of CD15: non-sialylated CD15 (LeuM1 and 80H5) and sialylated CD15 (FH6 and
      CSLEX1). Cases that were negative for non-sialylated CD15 or positive for the
      sialylated variant were stained again following neuraminidase pretreatment. The
      cohort included 27 patients in whom sequential biopsies were available. Both CD15
      expression in its non-sialylated form and absence of sialyl-CD15 expression
      correlate with a favorable outcome. Subsequent biopsies show a preferential
      expression of sialyl-CD15, notably in bone marrow metastases. Our findings
      suggest that, in the progression of HD towards a widely disseminated disease, the
      LewisX moiety of the CD15 antigen on the tumor cells acquires a sialyl-group.
      This change may confer on the tumor cells the capacity to metastasize.
FAU - Benharroch, D
AU  - Benharroch D
AD  - Department of Pathology, Soroka University Medical Center, Beer-Sheva, Israel.
      benaroch@bgumail.bgu.ac.il
FAU - Dima, E
AU  - Dima E
FAU - Levy, A
AU  - Levy A
FAU - Ohana-Malka, O
AU  - Ohana-Malka O
FAU - Ariad, S
AU  - Ariad S
FAU - Prinsloo, I
AU  - Prinsloo I
FAU - Mejirovsky, E
AU  - Mejirovsky E
FAU - Sacks, M
AU  - Sacks M
FAU - Gopas, J
AU  - Gopas J
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Leuk Lymphoma
JT  - Leukemia & lymphoma
JID - 9007422
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Biomarkers)
RN  - 0 (Lewis X Antigen)
RN  - 0 (Sialoglycoproteins)
SB  - IM
MH  - Actuarial Analysis
MH  - Adolescent
MH  - Adult
MH  - Aged
MH  - Antibodies, Monoclonal
MH  - Biomarkers
MH  - Child
MH  - Child, Preschool
MH  - Female
MH  - Hodgkin Disease/immunology/*metabolism/pathology
MH  - Humans
MH  - Immunohistochemistry
MH  - Lewis X Antigen/*biosynthesis/immunology
MH  - Male
MH  - Middle Aged
MH  - Prognosis
MH  - Reed-Sternberg Cells/chemistry/immunology
MH  - Retrospective Studies
MH  - Sialoglycoproteins/*biosynthesis/immunology
MH  - Survival Rate
EDAT- 2000/09/07 11:00
MHDA- 2001/03/03 10:01
CRDT- 2000/09/07 11:00
PHST- 2000/09/07 11:00 [pubmed]
PHST- 2001/03/03 10:01 [medline]
PHST- 2000/09/07 11:00 [entrez]
AID - I308J009004 [pii]
AID - 10.3109/10428190009053553 [doi]
PST - ppublish
SO  - Leuk Lymphoma. 2000 Sep;39(1-2):185-94. doi: 10.3109/10428190009053553.

PMID- 9212232
OWN - NLM
STAT- MEDLINE
DCOM- 19970723
LR  - 20160303
IS  - 0020-7136 (Print)
IS  - 0020-7136 (Linking)
VI  - 72
IP  - 1
DP  - 1997 Jul 3
TI  - Immunoreactivities of polyclonal and monoclonal anti-T and anti-Tn antibodies
      with human carcinoma cells, grown in vitro and in a xenograft model.
PG  - 119-27
AB  - Human polyclonal, monospecific anti-T and -Tn antibodies were found to be
      reactive in ELISA tests with human ovarian (IGROV-1, OVCAR-3 and SKOV-3), breast 
      (SKBr-3 and T47D)- and oral (KB)-carcinoma cell lines, but less so or
      non-reactive with normal epithelia and fibroblasts. The direct binding
      radioimmunoassay, using 125I-labeled human antibodies, to the IGROV-1 cancer
      cells was inhibited by homologous unlabeled antibodies of the same concentration,
      but not by the respective immunodominant haptenic monosaccharides (Gal for T and 
      GalNAc for Tn). Rodent ascitic monoclonal anti-T (Ca3114 and Ca3741) and anti-Tn 
      (Ca3250, Ca3268 and Ca3638) antibodies were also reactive with the ovarian- and
      breast-cancer cells, as measured by FACS and ELISA tests, but to a lower extent
      than the polyclonal human antibodies. Both the monoclonal anti-T (Ca3741) and
      anti-Tn (Ca3250 and Ca3638) antibody-binding reactivities were significantly
      inhibited by the haptenic free monosaccharides. Addition of the above MAbs to
      IGROV-1 ovarian-cancer or T47D breast-cancer cells cultured in vitro resulted in 
      significant cytological change and inhibition of the viability of the tumor
      cells, but not of normal epithelial breast cells. This effect on viability was
      shown to be complement-independent, yet it was profoundly influenced by the
      concentration of the serum added to the assay medium. In vivo biodistribution of 
      the anti-T (Ca3114) and anti-Tn (Ca3638) MAbs administered i.p. to athymic
      IGROV-1 tumor-bearing CD1 female nude mice revealed higher 125I-labeled antibody 
      accumulation in the tumor xenografts and in their lung tissues, as compared with 
      other organs of the same mice tested. The above results thus suggest the
      feasibility of utilizing these antibodies in immunotherapy and drug targeting.
FAU - Avichezer, D
AU  - Avichezer D
AD  - Department of Immunology, The Weizmann Institute of Science, Rehovot, Israel.
FAU - Springer, G F
AU  - Springer GF
FAU - Schechter, B
AU  - Schechter B
FAU - Arnon, R
AU  - Arnon R
LA  - eng
GR  - CA22540/CA/NCI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Int J Cancer
JT  - International journal of cancer
JID - 0042124
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Antigens, Viral, Tumor)
RN  - 0 (CCAAT-Enhancer-Binding Proteins)
RN  - 0 (DNA-Binding Proteins)
RN  - 0 (Nuclear Proteins)
RN  - 0 (Tn antigen)
SB  - IM
EIN - Int J Cancer 1997 Sep 4;72(5):918
MH  - Animals
MH  - Antibodies, Monoclonal/*immunology
MH  - Antibody Specificity
MH  - Antigens, Tumor-Associated, Carbohydrate/*immunology
MH  - Antigens, Viral, Tumor/*immunology
MH  - Breast Neoplasms/immunology
MH  - CCAAT-Enhancer-Binding Proteins
MH  - Carcinoma/*immunology
MH  - Cell Survival
MH  - Coculture Techniques
MH  - DNA-Binding Proteins
MH  - Dose-Response Relationship, Immunologic
MH  - Enzyme-Linked Immunosorbent Assay
MH  - Female
MH  - Humans
MH  - Mice
MH  - Mice, Nude
MH  - Neoplasm Transplantation
MH  - Nuclear Proteins
MH  - Ovarian Neoplasms/immunology
MH  - Tumor Cells, Cultured
EDAT- 1997/07/03 00:00
MHDA- 2000/06/20 09:00
CRDT- 1997/07/03 00:00
PHST- 1997/07/03 00:00 [pubmed]
PHST- 2000/06/20 09:00 [medline]
PHST- 1997/07/03 00:00 [entrez]
AID - 10.1002/(SICI)1097-0215(19970703)72:1<119::AID-IJC17>3.0.CO;2-E [pii]
PST - ppublish
SO  - Int J Cancer. 1997 Jul 3;72(1):119-27.

PMID- 9712788
OWN - NLM
STAT- MEDLINE
DCOM- 19981002
LR  - 20181113
IS  - 0019-9567 (Print)
IS  - 0019-9567 (Linking)
VI  - 66
IP  - 9
DP  - 1998 Sep
TI  - Shiga toxin binds human platelets via globotriaosylceramide (Pk antigen) and a
      novel platelet glycosphingolipid.
PG  - 4355-66
AB  - Hemolytic-uremic syndrome is a clinical syndrome characterized by acute renal
      failure, microangiopathic hemolytic anemia, and thrombocytopenia that often
      follows infection by Shiga toxin- or verotoxin-producing strains of Escherichia
      coli. Because thrombocytopenia and platelet activation are hallmark features of
      hemolytic-uremic syndrome, we examined the ability of Shiga toxin to bind
      platelets by flow cytometry and high-performance thin-layer chromatography
      (HPTLC) of isolated platelet glycosphingolipids. By HPTLC, Shiga toxin was shown 
      to bind globotriaosylceramide (Gb3) and a minor platelet glycolipid with an Rf of
      0.03, band 0.03. In a survey of 20 human tissues, band 0.03 was identified only
      in platelets. In individuals, band 0.03 was expressed by 20% of donors and was
      specifically associated with increased platelet Gb3 expression. Based on
      glycosidase digestion and epitope mapping, band 0.03 was hypothesized to
      represent a novel glycosphingolipid,
      IV3-beta-Galalpha1-4galactosylglobotetraosylceramide. Based on incidence,
      structure, and association with increased Gb3 expression, band 0.03 may represent
      the antithetical Luke blood group antigen. By flow cytometry, Shiga toxin bound
      human platelets, although the amount of Shiga toxin bound varied in donors.
      Differences in Shiga toxin binding to platelet membranes did not reflect
      differences in platelet Gb3 expression. In contrast, there was a loose
      association between Shiga toxin binding and decreasing forward scatter,
      suggesting that Shiga toxin and verotoxins bind more efficiently to smaller,
      older platelets. In summary, Shiga and Shiga-like toxins may bind platelets via
      specific glycosphingolipid receptors. Such binding may contribute to the
      thrombocytopenia, platelet activation, and microthrombus formation observed in
      hemolytic-uremic syndrome.
FAU - Cooling, L L
AU  - Cooling LL
AD  - Department of Pathology, SUNY Health Science Center at Syracuse, Syracuse, New
      York, USA.
FAU - Walker, K E
AU  - Walker KE
FAU - Gille, T
AU  - Gille T
FAU - Koerner, T A
AU  - Koerner TA
LA  - eng
GR  - T32 HL007344/HL/NHLBI NIH HHS/United States
GR  - R29 HL42395/HL/NHLBI NIH HHS/United States
GR  - T32 HL07344/HL/NHLBI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Infect Immun
JT  - Infection and immunity
JID - 0246127
RN  - 0 (Antigens, Nuclear)
RN  - 0 (Bacterial Toxins)
RN  - 0 (Glycolipids)
RN  - 0 (Glycosphingolipids)
RN  - 0 (Lactosylceramides)
RN  - 0 (Nuclear Proteins)
RN  - 0 (Receptors, Cell Surface)
RN  - 0 (Shiga Toxins)
RN  - 0 (Trihexosylceramides)
RN  - 71965-57-6 (globotriaosylceramide)
RN  - EC 3.2.1.- (Glycoside Hydrolases)
SB  - IM
MH  - Antigens, Nuclear
MH  - Bacterial Toxins/*metabolism
MH  - Blood Platelets/*metabolism
MH  - Carbohydrate Sequence
MH  - Glycolipids/metabolism
MH  - Glycoside Hydrolases/metabolism
MH  - Glycosphingolipids/*metabolism
MH  - Humans
MH  - Lactosylceramides/biosynthesis
MH  - Molecular Sequence Data
MH  - Nuclear Proteins/metabolism
MH  - Phenotype
MH  - Receptors, Cell Surface/*metabolism
MH  - Shiga Toxins
MH  - Shigella dysenteriae/*metabolism
MH  - Trihexosylceramides/*metabolism
PMC - PMC108526
EDAT- 1998/08/26 00:00
MHDA- 1998/08/26 00:01
CRDT- 1998/08/26 00:00
PHST- 1998/08/26 00:00 [pubmed]
PHST- 1998/08/26 00:01 [medline]
PHST- 1998/08/26 00:00 [entrez]
PST - ppublish
SO  - Infect Immun. 1998 Sep;66(9):4355-66.

PMID- 6117281
OWN - NLM
STAT- MEDLINE
DCOM- 19811215
LR  - 20171117
IS  - 0006-291X (Print)
IS  - 0006-291X (Linking)
VI  - 100
IP  - 4
DP  - 1981 Jun
TI  - The hapten structure of a developmentally regulated glycolipid antigen (SSEA-1)
      isolated from human erythrocytes and adenocarcinoma: a preliminary note.
PG  - 1578-86
FAU - Hakomori, S
AU  - Hakomori S
FAU - Nudelman, E
AU  - Nudelman E
FAU - Levery, S
AU  - Levery S
FAU - Solter, D
AU  - Solter D
FAU - Knowles, B B
AU  - Knowles BB
LA  - eng
GR  - CA10815/CA/NCI NIH HHS/United States
GR  - CA19224/CA/NCI NIH HHS/United States
GR  - CA20026/CA/NCI NIH HHS/United States
GR  - etc.
PT  - Comparative Study
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, Non-P.H.S.
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Biochem Biophys Res Commun
JT  - Biochemical and biophysical research communications
JID - 0372516
RN  - 0 (Antigens, Neoplasm)
RN  - 0 (Glycolipids)
RN  - 0 (Haptens)
RN  - 0 (Lewis X Antigen)
SB  - IM
MH  - Adenocarcinoma/*immunology
MH  - Antigens, Neoplasm/*isolation & purification
MH  - Carbohydrate Sequence
MH  - Colonic Neoplasms/*immunology
MH  - Erythrocytes/*immunology
MH  - Glycolipids/*immunology/*isolation & purification
MH  - Haptens
MH  - Humans
MH  - Immunochemistry
MH  - Lewis X Antigen
EDAT- 1981/06/01 00:00
MHDA- 1981/06/01 00:01
CRDT- 1981/06/01 00:00
PHST- 1981/06/01 00:00 [pubmed]
PHST- 1981/06/01 00:01 [medline]
PHST- 1981/06/01 00:00 [entrez]
AID - 0006-291X(81)90699-9 [pii]
PST - ppublish
SO  - Biochem Biophys Res Commun. 1981 Jun;100(4):1578-86.

PMID- 7827324
OWN - NLM
STAT- MEDLINE
DCOM- 19950222
LR  - 20061115
IS  - 0959-4965 (Print)
IS  - 0959-4965 (Linking)
VI  - 5
IP  - 14
DP  - 1994 Sep 8
TI  - Expression of 9-O-acetylated gangliosides during development of the rat olfactory
      system.
PG  - 1755-9
AB  - The expression of 9-O-acetylated gangliosides recognized by the Jones monoclonal 
      antibody (mAb) correlates with cell migration and axonal outgrowth in the
      developing rat nervous system. We studied the expression of these gangliosides
      during the development and maturation of the rat olfactory system. Beginning on
      embryonic day 13 (E13) the olfactory epithelium and the migratory mass were
      intensely stained with Jones mAb. However, though this immunoreactivity
      disappeared from the olfactory epithelium at E19, it remained in a few fascicles 
      and some glomeruli of the newborn and adult olfactory bulbs. We concluded that
      the expression of 9-O-acetylated gangliosides by olfactory axons and/or migrating
      cells may facilitate axonal outgrowth during development and might be involved in
      the formation of new glomeruli in the mature olfactory bulb.
FAU - Mendez-Otero, R
AU  - Mendez-Otero R
AD  - Instituto de Biofisica Carlos Chagas Filho, Universidade Federal do Rio de
      Janeiro, G-Cidade Universitaria, Rio de Janeiro, Brazil.
FAU - Ramon-Cueto, A
AU  - Ramon-Cueto A
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - Neuroreport
JT  - Neuroreport
JID - 9100935
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Gangliosides)
SB  - IM
MH  - Animals
MH  - Antibodies, Monoclonal/immunology
MH  - Axons/physiology
MH  - Female
MH  - Gangliosides/*biosynthesis
MH  - Immunohistochemistry
MH  - Nerve Fibers/physiology
MH  - Olfactory Bulb/embryology/metabolism
MH  - Olfactory Mucosa/embryology/metabolism
MH  - Olfactory Pathways/embryology/metabolism
MH  - Pregnancy
MH  - Rats
MH  - Smell/*physiology
EDAT- 1994/09/08 00:00
MHDA- 1994/09/08 00:01
CRDT- 1994/09/08 00:00
PHST- 1994/09/08 00:00 [pubmed]
PHST- 1994/09/08 00:01 [medline]
PHST- 1994/09/08 00:00 [entrez]
PST - ppublish
SO  - Neuroreport. 1994 Sep 8;5(14):1755-9.

PMID- 14533679
OWN - NLM
STAT- MEDLINE
DCOM- 20031023
LR  - 20041117
IS  - 0022-3395 (Print)
IS  - 0022-3395 (Linking)
VI  - 89
IP  - 4
DP  - 2003 Aug
TI  - Mucin-type O-glycosylation in helminth parasites from major taxonomic groups:
      evidence for widespread distribution of the Tn antigen (GalNAc-Ser/Thr) and
      identification of UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase
      activity.
PG  - 709-14
AB  - This article focuses on the initiation pathway of mucin-type O-glycosylation in
      helminth parasites. The presence of the GalNAc-O-Ser/Thr structure, also known as
      Tn antigen, a truncated determinant related to aberrant glycosylation in mammal
      cells, and the activity of the UDP-GalNAc:polypeptide
      N-acetyl-galactosaminyltransferase (ppGaNTase), the enzyme responsible for its
      synthesis, were studied in species from major taxonomic groups. Tn reactivity was
      determined in extracts from Taenia hydatigena, Mesocestoides corti, Fasciola
      hepatica, Nippostrongylus brasiliensis, and Toxocara canis using the monoclonal
      antibody 83D4. The Tn determinant was revealed in all preparations, and multiple 
      patterns of Tn-bearing glycoproteins were observed by immunoblotting.
      Additionally, the first evidence that helminth parasites express ppGaNTase
      activity was obtained. This enzyme was studied in extracts from Echinococcus
      granulosus, F. hepatica, and T. canis by measuring the incorporation of
      UDP-(3H)GalNAc to both deglycosylated ovine syalomucin (dOSM) and synthetic
      peptide sequences derived from tandem repeats of human mucins. Whereas
      significant levels of ppGaNTase activity were detected in all the extracts when
      dOSM was used as a multisite acceptor, it was only observed in F. hepatica and E.
      granulosus extracts when mucin-derived peptides were used, suggesting that T.
      canis ppGaNTase enzyme(s) may represent a member of the gene family with a more
      restricted specificity for worm O-glycosylation motifs. The widespread expression
      of Tn antigen, capable of evoking both humoral and cellular immunity, strongly
      suggests that simple mucin-type O-glycosylation does not constitute an aberrant
      phenomenon in helminth parasites.
FAU - Casaravilla, Cecilia
AU  - Casaravilla C
AD  - Unidad de Biologia Parasitaria, Departamento de Biologia Celular y Molecular,
      Facultad de Ciencias, Instituto de Higiene, Av. A. Navarro 3051 CP11600,
      Montevideo, Uruguay.
FAU - Freire, Teresa
AU  - Freire T
FAU - Malgor, Ramiro
AU  - Malgor R
FAU - Medeiros, Andrea
AU  - Medeiros A
FAU - Osinaga, Eduardo
AU  - Osinaga E
FAU - Carmona, Carlos
AU  - Carmona C
LA  - eng
PT  - Journal Article
PL  - United States
TA  - J Parasitol
JT  - The Journal of parasitology
JID - 7803124
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Glycopeptides)
RN  - 0 (Glycoproteins)
RN  - 0 (Tn antigen)
RN  - EC 2.4.1.- (N-Acetylgalactosaminyltransferases)
RN  - EC 2.4.1.41 (polypeptide N-acetylgalactosaminyltransferase)
SB  - IM
MH  - Animals
MH  - Antigens, Tumor-Associated, Carbohydrate/chemistry/*metabolism
MH  - Blotting, Western
MH  - Cattle
MH  - Dogs
MH  - Echinococcus/enzymology/immunology/metabolism
MH  - Electrophoresis, Polyacrylamide Gel
MH  - Fasciola hepatica/enzymology/immunology/metabolism
MH  - Glycopeptides/metabolism
MH  - Glycoproteins/analysis
MH  - Glycosylation
MH  - Helminths/enzymology/immunology/*metabolism
MH  - Humans
MH  - Mesocestoides/enzymology/immunology/metabolism
MH  - Mice
MH  - N-Acetylgalactosaminyltransferases/*metabolism
MH  - Nippostrongylus/enzymology/immunology/metabolism
MH  - Rats
MH  - Rats, Wistar
MH  - Taenia/enzymology/immunology/metabolism
MH  - Toxocara canis/enzymology/immunology/metabolism
EDAT- 2003/10/10 05:00
MHDA- 2003/10/24 05:00
CRDT- 2003/10/10 05:00
PHST- 2003/10/10 05:00 [pubmed]
PHST- 2003/10/24 05:00 [medline]
PHST- 2003/10/10 05:00 [entrez]
AID - 10.1645/GE-2970 [doi]
PST - ppublish
SO  - J Parasitol. 2003 Aug;89(4):709-14. doi: 10.1645/GE-2970.

PMID- 19162326
OWN - NLM
STAT- MEDLINE
DCOM- 20090622
LR  - 20090306
IS  - 1872-9142 (Electronic)
IS  - 0161-5890 (Linking)
VI  - 46
IP  - 6
DP  - 2009 Mar
TI  - Characterization of murine MGL1 and MGL2 C-type lectins: distinct glycan
      specificities and tumor binding properties.
PG  - 1240-9
LID - 10.1016/j.molimm.2008.11.021 [doi]
AB  - Antigen presenting cells (APC) express a variety of pattern recognition
      receptors, including the C-type lectin receptors (CLR) that specifically
      recognize carbohydrate structures expressed on self-tissue and pathogens. The CLR
      play an important role in antigen uptake and presentation and have been shown to 
      mediate cellular interactions. The ligand specificity of the human macrophage
      galactose-type lectin (MGL) has been characterized extensively. Here, we set out 
      to determine the glycan specificity of the murine homologues, MGL1 and MGL2,
      using a glycan array. Murine MGL1 was found to be highly specific for Lewis X and
      Lewis A structures, whereas mMGL2, more similar to the human MGL, recognized
      N-acetylgalactosamine (GalNAc) and galactose, including the O-linked Tn-antigen, 
      TF-antigen and core 2. The generation of MGL1 and MGL2-Fc proteins allowed us to 
      identify ligands in lymph nodes, and MGL1-Fc additionally recognized high
      endothelial venules. Strikingly, MGL2 interacted strongly to adenocarcinoma
      cells, suggesting a potential role in tumor immunity.
FAU - Singh, Satwinder Kaur
AU  - Singh SK
AD  - Department of Molecular Cell Biology and Immunology, VU University Medical
      Center, Amsterdam, The Netherlands.
FAU - Streng-Ouwehand, Ingeborg
AU  - Streng-Ouwehand I
FAU - Litjens, Manja
AU  - Litjens M
FAU - Weelij, Danny R
AU  - Weelij DR
FAU - Garcia-Vallejo, Juan Jesus
AU  - Garcia-Vallejo JJ
FAU - van Vliet, Sandra J
AU  - van Vliet SJ
FAU - Saeland, Eirikur
AU  - Saeland E
FAU - van Kooyk, Yvette
AU  - van Kooyk Y
LA  - eng
GR  - GM62116/GM/NIGMS NIH HHS/United States
PT  - Journal Article
PT  - Research Support, N.I.H., Extramural
DEP - 20090121
PL  - England
TA  - Mol Immunol
JT  - Molecular immunology
JID - 7905289
RN  - 0 (Asialoglycoproteins)
RN  - 0 (Lectins, C-Type)
RN  - 0 (Ligands)
RN  - 0 (MGL2 protein, mouse)
RN  - 0 (Membrane Proteins)
RN  - 0 (Mgl1 protein, mouse)
RN  - 0 (Polysaccharides)
RN  - 0 (Recombinant Proteins)
SB  - IM
MH  - Adenocarcinoma/metabolism
MH  - Animals
MH  - Antigen-Presenting Cells/immunology
MH  - Asialoglycoproteins/genetics/immunology/*metabolism
MH  - Bone Marrow Cells/metabolism
MH  - Cell Line, Tumor
MH  - Cells, Cultured
MH  - Endothelium, Vascular/metabolism
MH  - Extracellular Matrix/metabolism
MH  - Lectins, C-Type/genetics/immunology/*metabolism
MH  - Ligands
MH  - Lymph Nodes/metabolism
MH  - Membrane Proteins/genetics/immunology/*metabolism
MH  - Mice
MH  - Mice, Inbred C57BL
MH  - Polysaccharides/*metabolism
MH  - Recombinant Proteins/genetics/metabolism
MH  - Skin/metabolism
EDAT- 2009/01/24 09:00
MHDA- 2009/06/23 09:00
CRDT- 2009/01/24 09:00
PHST- 2008/09/24 00:00 [received]
PHST- 2008/11/17 00:00 [revised]
PHST- 2008/11/21 00:00 [accepted]
PHST- 2009/01/24 09:00 [entrez]
PHST- 2009/01/24 09:00 [pubmed]
PHST- 2009/06/23 09:00 [medline]
AID - S0161-5890(08)00760-8 [pii]
AID - 10.1016/j.molimm.2008.11.021 [doi]
PST - ppublish
SO  - Mol Immunol. 2009 Mar;46(6):1240-9. doi: 10.1016/j.molimm.2008.11.021. Epub 2009 
      Jan 21.

PMID- 9076517
OWN - NLM
STAT- MEDLINE
DCOM- 19970627
LR  - 20181113
IS  - 0282-0080 (Print)
IS  - 0282-0080 (Linking)
VI  - 14
IP  - 1
DP  - 1997 Jan
TI  - The usefulness of anti-fucosylated antigen antibody YB-2 for diagnosis of
      hepatocellular carcinoma.
PG  - 81-7
AB  - Levels of fucosylated antigens in sera from patients with liver diseases were
      examined by a newly developed sandwich-type enzyme immuno assay with the aid of
      anti-fucosylated antigen antibody, YB-2 which reacts simultaneously with Y, Leb
      and H type 2 antigens. When the cut-off value was set arbitrarily at mean +3 SD
      values of normal, 30 (69.8%) of the 43 patients with HCC, 14 (53.8%) of the 26
      patients with liver cirrhosis (LC) and 24 (45.3%) of the 53 patients with chronic
      hepatitis (CH) were found to be positive, whereas all of the 30 samples from
      healthy controls were negative. The levels of alpha-fetoprotein (AFP) and protein
      induced by vitamin K absence or antagonist-II (PIVKA-II) in HCC were not
      correlated with those of YB-2 antigens. The positive rates of the combination
      YB-2 and AFP assay and YB-2 and PIVKA-II assay in HCC were significantly higher
      (83.7 and 86.0%, respectively) than that of the AFP and PIVKA-II combination
      (65.1%) which had been reported to be the best combination up to this time.
FAU - Nakamura, J
AU  - Nakamura J
AD  - First Department of Surgery, Gunma University School of Medicine, Maebashi,
      Japan.
FAU - Yazawa, S
AU  - Yazawa S
FAU - Hada, T
AU  - Hada T
FAU - Asao, T
AU  - Asao T
FAU - Naitoh, H
AU  - Naitoh H
FAU - Takenoshita, S
AU  - Takenoshita S
FAU - Kosaka, M
AU  - Kosaka M
FAU - Akamatsu, S
AU  - Akamatsu S
FAU - Tachikawa, T
AU  - Tachikawa T
FAU - Nagamachi, Y
AU  - Nagamachi Y
LA  - eng
PT  - Journal Article
PL  - United States
TA  - Glycoconj J
JT  - Glycoconjugate journal
JID - 8603310
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens)
RN  - 0 (Antigens, Neoplasm)
RN  - 0 (Biomarkers)
RN  - 0 (Protein Precursors)
RN  - 0 (alpha-Fetoproteins)
RN  - 53230-14-1 (acarboxyprothrombin)
RN  - 9001-26-7 (Prothrombin)
SB  - IM
MH  - Adult
MH  - Aged
MH  - Aged, 80 and over
MH  - Antibodies, Monoclonal/*analysis/*immunology
MH  - Antigens/*blood/immunology
MH  - Antigens, Neoplasm/blood/immunology
MH  - *Biomarkers
MH  - Carcinoma, Hepatocellular/*diagnosis/immunology
MH  - Female
MH  - Hepatitis/blood/immunology
MH  - Humans
MH  - Immunoassay/*methods
MH  - Liver Cirrhosis/blood/immunology
MH  - Male
MH  - Middle Aged
MH  - Protein Precursors/analysis
MH  - Prothrombin/analysis
MH  - Reference Values
MH  - Sensitivity and Specificity
MH  - alpha-Fetoproteins/analysis
EDAT- 1997/01/01 00:00
MHDA- 1997/01/01 00:01
CRDT- 1997/01/01 00:00
PHST- 1997/01/01 00:00 [pubmed]
PHST- 1997/01/01 00:01 [medline]
PHST- 1997/01/01 00:00 [entrez]
PST - ppublish
SO  - Glycoconj J. 1997 Jan;14(1):81-7.

PMID- 2521835
OWN - NLM
STAT- MEDLINE
DCOM- 19890329
LR  - 20071114
IS  - 0012-1606 (Print)
IS  - 0012-1606 (Linking)
VI  - 132
IP  - 1
DP  - 1989 Mar
TI  - A neuroectoderm-associated ganglioside participates in fibronectin
      receptor-mediated adhesion of germinal cells to fibronectin.
PG  - 212-29
AB  - Previous studies with a rat neural cell line have shown that the D1.1
      ganglioside, an O-acetylated derivative of GD3, is involved in cellular adhesion 
      to fibronectin. In vivo, D1.1 is present on germinal cells of the developing rat 
      central nervous system, but not on postmitotic cells that migrate away from the
      germinal zones. These observations suggest that D1.1 could participate in
      adhesive interactions with germinal zones and that the loss of D1.1 could be
      involved in the decision to being migration. In support of this hypothesis,
      immunofluorescence histochemistry shows that both fibronectin and fibronectin
      receptor are colocalized with D1.1 in the ventricular zones of the embryonic rat 
      brain and in the external granule cell layer of the postnatal cerebellum. Dishes 
      coated with monoclonal antibody against D1.1 were used to isolate D1.1-positive
      germinal cells from Embryonic Day 14 cerebrum and from Postnatal Day 6
      cerebellum. These cells are able to adhere to fibronectin-coated dishes by a
      mechanism that is inhibitable by a synthetic hexapeptide containing the
      arg-gly-asp cell recognition sequence of fibronectin. Adhesion is also partially 
      inhibited by antibody against fibronectin receptor and is slowed by anti-D1.1
      antibody, implicating both the receptor and the ganglioside in the adhesion
      process. During 3 days in culture these D1.1-positive, fibronectin
      receptor-positive cells exhibit a neuronal phenotype, as judged by morphology and
      staining with tetanus toxin. This further confirms the neuroepithelial origin of 
      the cells. The cells do not synthesize detectable amounts of fibronectin, thus
      leaving unidentified the source of the fibronectin seen in the germinal zones in 
      tissue sections. Immunoprecipitation experiments show that the fibronectin
      receptors present on these cells are heterodimers. Under nonreducing conditions, 
      the immunoprecipitates contain an alpha-subunit of 150-160 kDa and a beta-subunit
      of 115-125 kDa.
FAU - Stallcup, W B
AU  - Stallcup WB
AD  - Cancer Research Center, La Jolla Cancer Research Foundation, California 92037.
FAU - Pytela, R
AU  - Pytela R
FAU - Ruoslahti, E
AU  - Ruoslahti E
LA  - eng
GR  - CA28896/CA/NCI NIH HHS/United States
GR  - CA42507/CA/NCI NIH HHS/United States
GR  - NS21990/NS/NINDS NIH HHS/United States
PT  - Journal Article
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Dev Biol
JT  - Developmental biology
JID - 0372762
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Fibronectins)
RN  - 0 (Gangliosides)
RN  - 0 (Receptors, Fibronectin)
RN  - 0 (Receptors, Immunologic)
SB  - IM
MH  - Age Factors
MH  - Animals
MH  - Antibodies, Monoclonal/immunology
MH  - Brain/cytology/*embryology
MH  - *Cell Adhesion
MH  - Cell Differentiation
MH  - Cerebellum/cytology
MH  - Fibronectins/*physiology
MH  - Fluorescent Antibody Technique
MH  - Gangliosides/*physiology
MH  - Molecular Weight
MH  - Precipitin Tests
MH  - Rats
MH  - Receptors, Fibronectin
MH  - Receptors, Immunologic/*physiology
EDAT- 1989/03/01 00:00
MHDA- 1989/03/01 00:01
CRDT- 1989/03/01 00:00
PHST- 1989/03/01 00:00 [pubmed]
PHST- 1989/03/01 00:01 [medline]
PHST- 1989/03/01 00:00 [entrez]
AID - 0012-1606(89)90218-2 [pii]
PST - ppublish
SO  - Dev Biol. 1989 Mar;132(1):212-29.

PMID- 16203776
OWN - NLM
STAT- MEDLINE
DCOM- 20060208
LR  - 20151119
IS  - 1078-0432 (Print)
IS  - 1078-0432 (Linking)
VI  - 11
IP  - 19 Pt 1
DP  - 2005 Oct 1
TI  - Thomsen-Friedenreich and Tn antigens in nipple fluid: carbohydrate biomarkers for
      breast cancer detection.
PG  - 6868-71
AB  - PURPOSE: Novel biomarkers would facilitate early and accurate diagnosis of breast
      cancer. The Thomsen-Freidenreich (TF) and Tn antigens are aberrantly glycosylated
      carbohydrate cancer-associated antigens found in approximately 80% of
      adenocarcinomas. Both TF and Tn are expressed on cell-surface glycoproteins and
      glycolipids. Nipple aspirate fluid (NAF) is concentrated in secreted proteins and
      lipids from cells that give rise to cancer. The objective of this study was to
      determine if NAF from breasts with cancer contains elevated levels of TF and Tn
      compared with NAF from normal breasts. A sensitive and specific antigen capture
      immunoassay for TF and Tn detection in NAF was developed for this purpose.
      EXPERIMENTAL DESIGN: Fifty NAF samples, 25 from breasts with cancer and 25 from
      normal breasts, were examined. Antigen capture immunoassays were done on the
      samples using monoclonal antibodies that specifically recognized either TF or Tn 
      antigen in NAF. These antibodies captured serially diluted NAF samples, and the
      concentration of TF or Tn was determined by comparing absorbance values against a
      standard curve generated from standard sources of TF or Tn. RESULTS: TF and Tn
      were detected in 19 of 25 and 20 of 25 NAF samples from breasts with cancer,
      respectively, compared with 0 of 25 and 1 of 25 NAF samples from breasts without 
      cancer (P < 0.001 for both TF and Tn). In 92% of the cancerous breast NAF samples
      tested, either TF or Tn was found. CONCLUSIONS: Simultaneous measurement of TF
      and Tn in NAF may facilitate the noninvasive detection of breast cancer and
      warrants further study.
FAU - Kumar, Senthil R
AU  - Kumar SR
AD  - Department of Biochemistry, University of Missouri, Columbia, Missouri 65212,
      USA.
FAU - Sauter, Edward R
AU  - Sauter ER
FAU - Quinn, Thomas P
AU  - Quinn TP
FAU - Deutscher, Susan L
AU  - Deutscher SL
LA  - eng
PT  - Journal Article
PT  - Research Support, U.S. Gov't, Non-P.H.S.
PL  - United States
TA  - Clin Cancer Res
JT  - Clinical cancer research : an official journal of the American Association for
      Cancer Research
JID - 9502500
RN  - 0 (Antigens, Neoplasm)
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Biomarkers, Tumor)
RN  - 0 (Carbohydrates)
RN  - 0 (Tn antigen)
RN  - 3554-90-3 (Thomsen-Friedenreich antigen)
SB  - IM
MH  - Adult
MH  - Aged
MH  - Antigens, Neoplasm/metabolism
MH  - Antigens, Tumor-Associated, Carbohydrate/*biosynthesis
MH  - *Biomarkers, Tumor
MH  - Biopsy, Needle
MH  - Body Fluids/metabolism
MH  - Breast/metabolism
MH  - Breast Neoplasms/*diagnosis/*metabolism
MH  - Carbohydrates/chemistry
MH  - Enzyme-Linked Immunosorbent Assay
MH  - Female
MH  - Glycosylation
MH  - Humans
MH  - Immunoassay
MH  - Mass Screening
MH  - Middle Aged
MH  - Postmenopause
MH  - Premenopause
MH  - Recurrence
EDAT- 2005/10/06 09:00
MHDA- 2006/02/09 09:00
CRDT- 2005/10/06 09:00
PHST- 2005/10/06 09:00 [pubmed]
PHST- 2006/02/09 09:00 [medline]
PHST- 2005/10/06 09:00 [entrez]
AID - 11/19/6868 [pii]
AID - 10.1158/1078-0432.CCR-05-0146 [doi]
PST - ppublish
SO  - Clin Cancer Res. 2005 Oct 1;11(19 Pt 1):6868-71. doi:
      10.1158/1078-0432.CCR-05-0146.

PMID- 7987817
OWN - NLM
STAT- MEDLINE
DCOM- 19950110
LR  - 20151119
IS  - 0008-5472 (Print)
IS  - 0008-5472 (Linking)
VI  - 54
IP  - 24
DP  - 1994 Dec 15
TI  - Sialyl-Tn antigen expression occurs early during human mammary carcinogenesis and
      is associated with high nuclear grade and aneuploidy.
PG  - 6302-5
AB  - Sialyl-Tn (STn) antigen represents an aberrant glycosylation product of cell
      surface mucin in adenocarcinomas. We studied its expression in 40 breast
      carcinomas (35 of which included in situ carcinomas) by performing immunostaining
      with B72.3 monoclonal antibody. STn expression was observed in 50% of cases and
      was equally frequent in in situ and in invasive carcinomas. Positive STn staining
      significantly correlated with high nuclear grade (P = 0.001), aneuploidy (P <
      0.001) and high S-phase fraction (P = 0.02). No correlation was observed between 
      STn staining and age, menopausal status, presence of invasive component, or
      hormone receptor positivity. STn staining may provide an objective marker of
      dedifferentiation of breast tumors and should be investigated further for its
      prognostic value in breast cancers and as a biomarker of malignant transformation
      of breast epithelium.
FAU - Cho, S H
AU  - Cho SH
AD  - Department of Breast and Gynecologic Medical Oncology, University of Texas M. D. 
      Anderson Cancer Center, Houston 77030.
FAU - Sahin, A
AU  - Sahin A
FAU - Hortobagyi, G N
AU  - Hortobagyi GN
FAU - Hittelman, W N
AU  - Hittelman WN
FAU - Dhingra, K
AU  - Dhingra K
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Cancer Res
JT  - Cancer research
JID - 2984705R
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Biomarkers, Tumor)
RN  - 0 (sialosyl-Tn antigen)
SB  - IM
MH  - Adult
MH  - Aged
MH  - Aged, 80 and over
MH  - Antigens, Tumor-Associated, Carbohydrate/*analysis
MH  - Biomarkers, Tumor/*analysis
MH  - Breast Neoplasms/*immunology/pathology
MH  - Carcinoma in Situ/*immunology
MH  - Carcinoma, Ductal, Breast/*immunology
MH  - Female
MH  - Humans
MH  - Middle Aged
MH  - Ploidies
MH  - Retrospective Studies
EDAT- 1994/12/15 00:00
MHDA- 1994/12/15 00:01
CRDT- 1994/12/15 00:00
PHST- 1994/12/15 00:00 [pubmed]
PHST- 1994/12/15 00:01 [medline]
PHST- 1994/12/15 00:00 [entrez]
PST - ppublish
SO  - Cancer Res. 1994 Dec 15;54(24):6302-5.

PMID- 1516058
OWN - NLM
STAT- MEDLINE
DCOM- 19921008
LR  - 20071205
IS  - 0008-5472 (Print)
IS  - 0008-5472 (Linking)
VI  - 52
IP  - 18
DP  - 1992 Sep 15
TI  - Human urinary bladder carcinoma glycoconjugates expressing T-(Gal beta(1-3)GalNAc
      alpha 1-O-R) and T-like antigens: a comparative study using peanut agglutinin and
      poly- and monoclonal antibodies.
PG  - 5030-6
AB  - T- and T-like antigens on glycoproteins and glycolipids were examined in extracts
      of human urinary bladder tumors and normal tissue by Western blot analysis and
      reagent binding to thin layer chromatograms. Three different anti-T-reagents were
      used: peanut (Arachis hypogaea) lectin (PNA) and mono- and polyclonal antibodies 
      specific for T-antigen (Gal beta(1-3)GalNAc alpha 1-O-R). Immunodetection with
      the T-specific reagents in nitrocellulose replicas of bladder tumor
      glycoproteins, separated by sodium dodecyl sulfate-polyacrylamide gel
      electrophoresis, demonstrated tumor-specific T-antigen-bearing glycoproteins
      compared to normal urothelial glycoproteins. In addition, a remarkable difference
      in binding was found between the immunological reagents and PNA lectin. PNA
      showed major reactivity to a 28-kD glycoprotein extracted from tumors. Monoclonal
      anti-T-antibody (clone HH8) showed major reactivity with an M(r) 34,000
      glycoprotein, and polyclonal anti-T-antibody showed major reactivity with an M(r)
      36,000 glycoprotein. PNA agarose column affinity-purified tumor glycoproteins did
      not bind the antibodies. Glycoproteins, M(r) 28,000 and 34,000, were shown to be 
      O-linked by stepwise deglycosylation. In solid phase monosaccharide inhibition
      tests, galactose followed by N-acetyl-galactosamine were the most potent
      monosaccharides inhibiting binding to immobilized bladder tumor glycoproteins.
      None of the anti-T-reagents reacted with glycolipids extracted from tumor tissue.
      It is concluded that PNA lectin, in addition to the T-disaccharide, reacts with
      other protein-anchored carbohydrate structures in carcinomas.
FAU - Langkilde, N C
AU  - Langkilde NC
AD  - Department of Experimental Clinical Oncology, Danish Cancer Society, Aarhus.
FAU - Wolf, H
AU  - Wolf H
FAU - Clausen, H
AU  - Clausen H
FAU - Orntoft, T F
AU  - Orntoft TF
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Cancer Res
JT  - Cancer research
JID - 2984705R
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antibodies, Neoplasm)
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Disaccharides)
RN  - 0 (Glycoconjugates)
RN  - 0 (Glycoproteins)
RN  - 0 (Lectins)
RN  - 0 (Monosaccharides)
RN  - 0 (Peanut Agglutinin)
RN  - 3554-90-3 (Thomsen-Friedenreich antigen)
SB  - IM
MH  - Antibodies, Monoclonal/immunology
MH  - Antibodies, Neoplasm/immunology
MH  - Antigens, Tumor-Associated, Carbohydrate/*immunology/metabolism
MH  - Binding, Competitive
MH  - Blotting, Western
MH  - Carbohydrate Sequence
MH  - Carcinoma/*immunology
MH  - Chromatography, Affinity
MH  - Chromatography, Thin Layer
MH  - Disaccharides/chemistry/*immunology
MH  - Glycoconjugates/*immunology
MH  - Glycoproteins/chemistry/immunology
MH  - Glycosylation
MH  - Humans
MH  - Lectins/metabolism
MH  - Molecular Sequence Data
MH  - Monosaccharides/metabolism
MH  - Peanut Agglutinin
MH  - Structure-Activity Relationship
MH  - Urinary Bladder/*immunology
MH  - Urinary Bladder Neoplasms/*immunology
EDAT- 1992/09/15 00:00
MHDA- 1992/09/15 00:01
CRDT- 1992/09/15 00:00
PHST- 1992/09/15 00:00 [pubmed]
PHST- 1992/09/15 00:01 [medline]
PHST- 1992/09/15 00:00 [entrez]
PST - ppublish
SO  - Cancer Res. 1992 Sep 15;52(18):5030-6.

PMID- 8625220
OWN - NLM
STAT- MEDLINE
DCOM- 19960626
LR  - 20151119
IS  - 0008-543X (Print)
IS  - 0008-543X (Linking)
VI  - 76
IP  - 6
DP  - 1995 Sep 15
TI  - Expression of alpha-3/4-monofucosylated polylactosaminoglycan epitope, as defined
      by monoclonal antibody FW6, is a marker of the colorectal adenoma-carcinoma
      sequence.
PG  - 954-60
AB  - BACKGROUND: The expression of a distinct alpha-3/4-monofucosylated
      polylactosaminoglycan epitope, which is detected by monoclonal antibody FW6, was 
      investigated by comparative immunohistochemical analysis of colorectal tissue
      specimens exhibiting different grades of premalignant and malignant
      transformation. The presence of this peculiar epitope was compared with different
      lewis type 2 blood group antigens. METHODS: Paraffin embedded specimens from 8
      hyperplastic polyps, 46 adenomas, 27 colorectal carcinomas, and 10 corresponding 
      liver metastases were studied. Staining reactions included monoclonal antibodies 
      FW6, AM-3 (anti-sialosyl-Le(x)), LeuM1 (anti-Le(x)), and 12-4LE (anti-Le(y)) in a
      standard peroxidase-antiperoxidase method. RESULTS: Hyperplastic polyps were not 
      reactive with FW6 or LeuM1, but showed a slight binding of AM-3 and 12-4LE in
      some cases. Approximately two-thirds of the adenomatous polyps displayed a
      pronounced staining activity by AM-3, and approximately half of them revealed
      FW6, LeuM1, and 12-4LE binding. Only the expression of the FW6 (P < 0.005)
      epitope correlated with the presence of severe dysplasia. All antibodies were
      more or less reactive with colorectal carcinomas and their liver metastases, and 
      some showed correlating binding patterns. CONCLUSIONS: FW6 revealed a high
      specificity for adenomas with areas of severe epithelial dysplasia. Because this 
      monoclonal antibody also detects the great majority of carcinomas, it is
      reasonable to postulate that the alpha-3/4-monofucosylated polylactosaminoglycan 
      epitope is an important marker for malignant transformation in the colorectal
      adenoma-carcinoma sequence.
FAU - Baldus, S E
AU  - Baldus SE
AD  - Department of Pathology, University of Cologne, Germany.
FAU - Vierbuchen, M
AU  - Vierbuchen M
FAU - Hanisch, F G
AU  - Hanisch FG
FAU - Schwonzen, M
AU  - Schwonzen M
FAU - Fischer, R
AU  - Fischer R
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Cancer
JT  - Cancer
JID - 0374236
RN  - 0 (Amino Sugars)
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens, Neoplasm)
RN  - 0 (Biomarkers, Tumor)
RN  - 0 (Epitopes)
RN  - 0 (Lewis Blood-Group System)
RN  - 0 (Polysaccharides)
RN  - 0 (lactosaminoglycan)
SB  - AIM
SB  - IM
MH  - Adenoma/diagnosis/*immunology
MH  - Amino Sugars/*immunology
MH  - Antibodies, Monoclonal
MH  - Antigens, Neoplasm/*immunology
MH  - *Biomarkers, Tumor
MH  - Carcinoma/diagnosis/*immunology/pathology
MH  - Colorectal Neoplasms/diagnosis/*immunology/pathology
MH  - Epitopes
MH  - Humans
MH  - Immunoenzyme Techniques
MH  - Intestinal Polyps/diagnosis/*immunology/pathology
MH  - Lewis Blood-Group System/*immunology
MH  - Liver Neoplasms/immunology/secondary
MH  - Neoplasm Metastasis
MH  - Polysaccharides/*immunology
EDAT- 1995/09/15 00:00
MHDA- 1995/09/15 00:01
CRDT- 1995/09/15 00:00
PHST- 1995/09/15 00:00 [pubmed]
PHST- 1995/09/15 00:01 [medline]
PHST- 1995/09/15 00:00 [entrez]
PST - ppublish
SO  - Cancer. 1995 Sep 15;76(6):954-60.

PMID- 6175663
OWN - NLM
STAT- MEDLINE
DCOM- 19820624
LR  - 20181113
IS  - 0021-9738 (Print)
IS  - 0021-9738 (Linking)
VI  - 69
IP  - 5
DP  - 1982 May
TI  - Clonal expression of the Tn antigen in erythroid and granulocyte colonies and its
      application to determination of the clonality of the human megakaryocyte colony
      assay.
PG  - 1081-91
AB  - To evaluate whether exposure of Tn determinants at the surface of human
      erythrocytes, platelets, and granulocytes could arise from a somatic mutation in 
      a hemopoietic stem cell, burst-forming unit erythroid (BFU-E) colonies,
      colony-forming unit granulocyte-macrophage (CFU-GM), and colony-forming
      unit-eosinophil (CFU-Eo) were grown from a blood group O patient with a typical
      Tn syndrome displaying two distinct populations (Tn(+) and Tn(-)) of platelets,
      granulocytes, and erythrocytes. A large number of colonies was observed.
      Individual colonies were studied with a fluorescent conjugate of Helix pomatia
      agglutinin (HPA). A sizeable fraction of each of the erythroid and granulocytic
      colonies appeared to consist exclusively of either HPA-positive or HPA-negative
      cells, thereby demonstrating the clonal origin of those exhibiting the Tn marker.
      Similar results were obtained from a second patient. These findings establish
      that the HPA labeling of Tn cells is an accurate marker permitting assessment of 
      the clonality of the human megakaryocyte (MK) colony assay. For the study of MK
      cultures a double-staining procedure using the HPA lectin and a monoclonal
      antiplatelet antibody (J-15) was applied in situ to identify all MK constituting 
      a colony. Our results, obtained in studies of 133 MK colonies, provide definitive
      evidence that the human MK colony assay is clonal because all MK colonies were
      exclusively composed of Tn(+) and Tn(-) MK. Furthermore, the distribution of MK
      within a single colony was shown to be seminormal with a mean at 6 MK, isolated
      MK typically being absent in culture. Comparison of the proportion of mature
      Tn(+) cells in blood with their respective Tn(+) progenitors has also shown that 
      no proliferative advantage occurs after the commitment; because Tn
      polyagglutinability is an acquired disorder, then the expansion of the Tn(+)
      clone must occur either during the proliferative stage of the pluripotent stem
      cell or during the commitment itself. This study therefore affords evidence that 
      a blood group antigen plays a role in the differentiation of a pluripotent stem
      cell.
FAU - Vainchenker, W
AU  - Vainchenker W
FAU - Testa, U
AU  - Testa U
FAU - Deschamps, J F
AU  - Deschamps JF
FAU - Henri, A
AU  - Henri A
FAU - Titeux, M
AU  - Titeux M
FAU - Breton-Gorius, J
AU  - Breton-Gorius J
FAU - Rochant, H
AU  - Rochant H
FAU - Lee, D
AU  - Lee D
FAU - Cartron, J P
AU  - Cartron JP
LA  - eng
PT  - Case Reports
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - J Clin Invest
JT  - The Journal of clinical investigation
JID - 7802877
RN  - 0 (Agglutinins)
RN  - 0 (Antigens)
RN  - 0 (Epitopes)
RN  - 0 (Receptors, Antigen)
RN  - 0 (Tn receptor)
SB  - AIM
SB  - IM
MH  - Adult
MH  - Agglutinins/immunology
MH  - *Antigens
MH  - Cell Differentiation
MH  - Clone Cells
MH  - Colony-Forming Units Assay
MH  - Epitopes
MH  - Erythrocytes/*immunology
MH  - Fluorescent Antibody Technique
MH  - Granulocytes/*immunology
MH  - Helix (Snails)
MH  - Humans
MH  - Male
MH  - Megakaryocytes
MH  - Mutation
MH  - *Receptors, Antigen
PMC - PMC370172
EDAT- 1982/05/01 00:00
MHDA- 1982/05/01 00:01
CRDT- 1982/05/01 00:00
PHST- 1982/05/01 00:00 [pubmed]
PHST- 1982/05/01 00:01 [medline]
PHST- 1982/05/01 00:00 [entrez]
PST - ppublish
SO  - J Clin Invest. 1982 May;69(5):1081-91.

PMID- 2413456
OWN - NLM
STAT- MEDLINE
DCOM- 19851118
LR  - 20190501
IS  - 0027-8424 (Print)
IS  - 0027-8424 (Linking)
VI  - 82
IP  - 20
DP  - 1985 Oct
TI  - Blood group A cross-reacting epitope defined by monoclonal antibodies NCC-LU-35
      and -81 expressed in cancer of blood group O or B individuals: its identification
      as Tn antigen.
PG  - 7039-43
AB  - Two monoclonal antibodies, NCC-LU-35 and NCC-LU-81, have been established after
      immunization of mice with membrane preparations of human lung cancer Lu65 tumor
      xenograft cells grown in vivo and intact cells cultured in vitro, respectively.
      These two antibodies react specifically with a majority of human adenocarcinomas,
      irrespective of the host's blood group ABO status, as well as with normal tissues
      and erythrocytes of blood group A individuals. The antigenicity is associated
      with a high molecular weight mucin-like glycoprotein separated by gel filtration 
      of Lu65 tumor extracts. The epitope of the mucin-like glycoprotein has been
      identified as alpha-N-acetylgalactosaminyl residue directly linked
      O-glycosidically to serine or threonine residues of polypeptides. This epitope
      was serologically detected several years ago and given the name Tn. Our
      identification of the epitope is based on the following results: The antigen is
      sensitive to alpha-N-acetylgalactosaminidase, but not to sialidase or
      alpha-fucosidase. Various mono- and difucosyl A determinants, either type 1 or
      type 2 chain, cross-react with both antibodies. The reactivity with both
      antibodies can be created by treatment of glycophorin A of normal erythrocytes
      with sialidase followed by beta-galactosidase. N-[3H]acetylgalactosamine can be
      released by galactose oxidase/NaB3H4 treatment from the Lu65 mucin-like
      glycoprotein but not from the mucin-like glycoprotein of normal colonic mucosa
      upon reductive beta-elimination (alkaline borohydride treatment). The antigen may
      be one of the tumor-associated A cross-reacting antigens occurring in a wide
      variety of human adenocarcinomas of hosts belonging to all ABO blood groups.
FAU - Hirohashi, S
AU  - Hirohashi S
FAU - Clausen, H
AU  - Clausen H
FAU - Yamada, T
AU  - Yamada T
FAU - Shimosato, Y
AU  - Shimosato Y
FAU - Hakomori, S
AU  - Hakomori S
LA  - eng
GR  - CA19224/CA/NCI NIH HHS/United States
GR  - GM23100/GM/NIGMS NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Proc Natl Acad Sci U S A
JT  - Proceedings of the National Academy of Sciences of the United States of America
JID - 7505876
RN  - 0 (ABO Blood-Group System)
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigen-Antibody Complex)
RN  - 0 (Antigens, Neoplasm)
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Epitopes)
RN  - 0 (Glycolipids)
RN  - 0 (Glycoproteins)
RN  - 0 (Tn antigen)
SB  - IM
MH  - ABO Blood-Group System/*immunology
MH  - Animals
MH  - *Antibodies, Monoclonal
MH  - Antigen-Antibody Complex
MH  - Antigens, Neoplasm/*analysis
MH  - *Antigens, Tumor-Associated, Carbohydrate
MH  - Cell Line
MH  - Epitopes/*analysis
MH  - Glycolipids/analysis
MH  - Glycoproteins/isolation & purification
MH  - Humans
MH  - Lung Neoplasms/*immunology
MH  - Mice
MH  - Mice, Nude
MH  - Neoplasm Transplantation
MH  - Transplantation, Heterologous
PMC - PMC391305
EDAT- 1985/10/01 00:00
MHDA- 1985/10/01 00:01
CRDT- 1985/10/01 00:00
PHST- 1985/10/01 00:00 [pubmed]
PHST- 1985/10/01 00:01 [medline]
PHST- 1985/10/01 00:00 [entrez]
AID - 10.1073/pnas.82.20.7039 [doi]
PST - ppublish
SO  - Proc Natl Acad Sci U S A. 1985 Oct;82(20):7039-43. doi: 10.1073/pnas.82.20.7039.

PMID- 7734303
OWN - NLM
STAT- MEDLINE
DCOM- 19950606
LR  - 20190515
IS  - 0007-0920 (Print)
IS  - 0007-0920 (Linking)
VI  - 71
IP  - 5
DP  - 1995 May
TI  - Expression of sialyl-Tn in gastric cancer: correlation with known prognostic
      factors.
PG  - 1074-6
AB  - Sialyl-Tn (STn) is a core region carcinoma-associated carbohydrate determinant
      expressed on cancer-associated mucins. Expression of STn has been associated with
      poor prognosis in colon and ovarian cancer, independent of other prognostic
      factors such as tumour grade, stage or histological type. Recent studies have
      suggested that STn expression may be an independent prognostic variable in
      gastric cancer. We have examined 158 patients with gastric cancer using the
      antibody B72.3 (Biomira, Edmonton, Alberta, Canada). Of these, 110 patients (70%)
      expressed STn. Expression of STn did not correlate with tumour differentiation or
      the Ming classification, but expression was noted more frequently in the
      relatively good prognosis intestinal type of tumours (chi 2 = 6.9, P = 0.03).
      Conversely, early-stage cancers showed a significantly lower frequency of
      expression than more advanced cases (chi 2 = 13.75, P = 0.003). In this patient
      group, STn expression did not influence survival, and in multivariate regression 
      analysis only tumour stage and Lauren classification were found to be independent
      prognostic variables.
FAU - Miles, D W
AU  - Miles DW
AD  - Imperial Cancer Research Fund Department of Clinical Oncology, Guy's Hospital,
      London, UK.
FAU - Linehan, J
AU  - Linehan J
FAU - Smith, P
AU  - Smith P
FAU - Filipe, I
AU  - Filipe I
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - Br J Cancer
JT  - British journal of cancer
JID - 0370635
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Biomarkers, Tumor)
RN  - 0 (sialosyl-Tn antigen)
SB  - IM
MH  - Antigens, Tumor-Associated, Carbohydrate/*analysis
MH  - Biomarkers, Tumor/*analysis
MH  - Cell Membrane/chemistry
MH  - Cytoplasm/chemistry
MH  - Follow-Up Studies
MH  - Humans
MH  - Immunohistochemistry
MH  - Mucus/chemistry
MH  - Prognosis
MH  - Stomach Neoplasms/*chemistry/ultrastructure
PMC - PMC2033804
EDAT- 1995/05/01 00:00
MHDA- 1995/05/01 00:01
CRDT- 1995/05/01 00:00
PHST- 1995/05/01 00:00 [pubmed]
PHST- 1995/05/01 00:01 [medline]
PHST- 1995/05/01 00:00 [entrez]
AID - 10.1038/bjc.1995.207 [doi]
PST - ppublish
SO  - Br J Cancer. 1995 May;71(5):1074-6. doi: 10.1038/bjc.1995.207.

PMID- 8340252
OWN - NLM
STAT- MEDLINE
DCOM- 19930830
LR  - 20190512
IS  - 0910-5050 (Print)
IS  - 0910-5050 (Linking)
VI  - 84
IP  - 6
DP  - 1993 Jun
TI  - Development and characterization of a novel anti-fucosylated antigen monoclonal
      antibody YB-2 and its usefulness in the immunohistochemical diagnosis of
      colorectal cancer.
PG  - 641-8
AB  - A novel monoclonal antibody, YB-2 was obtained after immunization of mice with
      fucosylated antigens isolated from human saliva. The antibody was demonstrated to
      react with Y (Fuc alpha 1-->2Gal-beta 1-->4[Fuc alpha 1-->3]GlcNAc beta),Leb (Fuc
      alpha 1-->2Gal beta 1-->3[Fuc alpha 1-->4]GlcNAc beta) and H type 2 (Fuc alpha
      1-->2Gal-beta 1-->4GlcNAc beta) antigens, but not with H type 1 (Fuc alpha
      1-->2Gal beta 1-->3GlcNAc beta), Lea (Gal beta 1-->3[Fuc alpha 1-->4]GlcNAc
      beta), X (Gal beta 1-->4[Fuc alpha 1-->3]GlcNAc beta) or with non-fucosylated
      antigens. Inhibition assays of YB-2 antibody with such reactive antigens showed
      that YB-2 antibody preferentially reacted with Y antigen. Formalin-fixed and
      paraffin-embedded sections prepared from normal and malignant colorectal tissues 
      were examined immunohistochemically with YB-2. The positive rates of staining
      with YB-2 antibody were 88.6% in malignant and 12.0% in normal tissues. The
      expression of fucosylated antigens detected by YB-2 antibody seemed to be
      correlated with survival among patients with primary colorectal cancer.
      Therefore, YB-2 antibody could be useful as an immunochemical tool for diagnosis 
      and evaluation of the prognosis of colorectal cancer.
FAU - Yazawa, S
AU  - Yazawa S
AD  - Department of Legal Medicine, Gunma University School of Medicine, Maebashi.
FAU - Akamatsu, S
AU  - Akamatsu S
FAU - Tachikawa, T
AU  - Tachikawa T
FAU - Naito, H
AU  - Naito H
FAU - Nakamura, J
AU  - Nakamura J
FAU - Asao, T
AU  - Asao T
FAU - Nagamachi, Y
AU  - Nagamachi Y
FAU - Nakajima, T
AU  - Nakajima T
FAU - Shin, S
AU  - Shin S
FAU - Chia, D
AU  - Chia D
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - Japan
TA  - Jpn J Cancer Res
JT  - Japanese journal of cancer research : Gann
JID - 8509412
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens, Neoplasm)
SB  - IM
MH  - *Antibodies, Monoclonal/isolation & purification
MH  - Antibody Specificity
MH  - Antigens, Neoplasm/*analysis
MH  - Colorectal Neoplasms/*diagnosis/*immunology/mortality
MH  - Enzyme-Linked Immunosorbent Assay
MH  - Humans
MH  - Immunoenzyme Techniques
MH  - Survival Analysis
PMC - PMC5919324
EDAT- 1993/06/01 00:00
MHDA- 1993/06/01 00:01
CRDT- 1993/06/01 00:00
PHST- 1993/06/01 00:00 [pubmed]
PHST- 1993/06/01 00:01 [medline]
PHST- 1993/06/01 00:00 [entrez]
AID - 10.1111/j.1349-7006.1993.tb02024.x [doi]
PST - ppublish
SO  - Jpn J Cancer Res. 1993 Jun;84(6):641-8. doi: 10.1111/j.1349-7006.1993.tb02024.x.

PMID- 8621218
OWN - NLM
STAT- MEDLINE
DCOM- 19960614
LR  - 20160303
IS  - 0020-7136 (Print)
IS  - 0020-7136 (Linking)
VI  - 65
IP  - 4
DP  - 1996 Feb 8
TI  - Serological and immunochemical analysis of Lewis y (Ley) blood group antigen
      expression in epithelial ovarian cancer.
PG  - 406-12
AB  - The expression of Ley blood group antigen in epithelial ovarian cancer tissues
      and cell lines has been studied using a Ley-specific monoclonal antibody (MAb
      3S193). In ovarian cancer specimens, Ley was expressed in 75% of the 140 tumor
      specimens examined, with strong or moderate expression being observed in 56% of
      the samples. Seven of the 11 ovarian cancer cell lines studied were Ley-positive.
      Using immunochemical approaches, Ley epitopes were found to be expressed on 4
      types of carrier molecules: CA125 ovarian cancer antigen, MUC-1 mucins, lower
      m.w. glycoproteins and glycolipids. In cell lines, Ley was more commonly
      expressed on MUC-1 mucin than on CA125, whereas in tumor specimens Ley was
      commonly found on both CA125 and MUC-1. The biochemical nature of the smaller Ley
      glycoproteins was not determined, but it was shown that they were not CEA and
      LAMP-1, known Ley carriers in some other tumor types. Glycolipids carrying Ley
      epitopes were detected in both ovarian cancer cell lines and tumor specimens. The
      presence of Ley epitopes on a number of different molecular carriers, including 2
      major ovarian cancer antigens (CA125 and MUC-1), explains the high incidence of
      Ley in ovarian cancer. The high expression of Ley in ovarian cancer and the
      availability of specific murine and humanized MAbs make Ley an attractive
      candidate target for clinical studies.
FAU - Yin, B W
AU  - Yin BW
AD  - Immunology Program, Memorial Sloan-Kettering Cancer Center, New York, USA.
FAU - Finstad, C L
AU  - Finstad CL
FAU - Kitamura, K
AU  - Kitamura K
FAU - Federici, M G
AU  - Federici MG
FAU - Welshinger, M
AU  - Welshinger M
FAU - Kudryashov, V
AU  - Kudryashov V
FAU - Hoskins, W J
AU  - Hoskins WJ
FAU - Welt, S
AU  - Welt S
FAU - Lloyd, K O
AU  - Lloyd KO
LA  - eng
GR  - CA-08748/CA/NCI NIH HHS/United States
GR  - CA-33049/CA/NCI NIH HHS/United States
GR  - CA-52477/CA/NCI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Int J Cancer
JT  - International journal of cancer
JID - 0042124
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Glycolipids)
RN  - 0 (Glycoproteins)
RN  - 0 (Lewis Blood-Group System)
RN  - 0 (Lewis Y antigen)
RN  - 0 (Mucins)
SB  - IM
MH  - Antibodies, Monoclonal/immunology
MH  - Female
MH  - Glycolipids/analysis
MH  - Glycoproteins/analysis
MH  - Humans
MH  - Immunohistochemistry
MH  - Lewis Blood-Group System/*analysis
MH  - Mucins/analysis
MH  - Neoplasms, Glandular and Epithelial/*immunology
MH  - Ovarian Neoplasms/*immunology
MH  - Tumor Cells, Cultured
EDAT- 1996/02/08 00:00
MHDA- 2000/06/20 09:00
CRDT- 1996/02/08 00:00
PHST- 1996/02/08 00:00 [pubmed]
PHST- 2000/06/20 09:00 [medline]
PHST- 1996/02/08 00:00 [entrez]
AID - 10.1002/(SICI)1097-0215(19960208)65:4<406::AID-IJC2>3.0.CO;2-0 [pii]
AID - 10.1002/(SICI)1097-0215(19960208)65:4<406::AID-IJC2>3.0.CO;2-0 [doi]
PST - ppublish
SO  - Int J Cancer. 1996 Feb 8;65(4):406-12. doi:
      10.1002/(SICI)1097-0215(19960208)65:4<406::AID-IJC2>3.0.CO;2-0.

PMID- 20227685
OWN - NLM
STAT- MEDLINE
DCOM- 20100623
LR  - 20181201
IS  - 1873-426X (Electronic)
IS  - 0008-6215 (Linking)
VI  - 345
IP  - 6
DP  - 2010 Apr 19
TI  - Identification of cell-surface mannans in a virulent Helicobacter pylori strain.
PG  - 830-8
LID - 10.1016/j.carres.2010.01.022 [doi]
AB  - With the intent of contributing to a carbohydrate-based vaccine against the
      gastroduodenal pathogen, Helicobacter pylori, we report here the structure of
      cell-surface mannans obtained from a virulent strain. Unlike other wild-type
      strains, this strain was found to express in good quantities this polysaccharide 
      in vitro. Structural analysis revealed a branched mannan formed by a backbone of 
      alpha-(1-->6)-linked mannopyranosyl residues with approximately 80% branching at 
      the O-2 position. The branches were composed of O-2-linked Man residues in both
      alpha- and beta-configurations: [abstract: see text]. In addition, this strain
      also expressed cell-surface emblematic H. pylori lipopolysaccharides (LPS)
      containing partially fucosylated polyLacNAc O-chains. Affinity assays with
      polymyxin-B and concanavalin A revealed no association between the mannan and the
      LPS. The described mannans may be implicated in the mediation of host-microbial
      interactions and immunological modulation.
CI  - Copyright (c) 2010 Elsevier Ltd. All rights reserved.
FAU - Ferreira, Jose A
AU  - Ferreira JA
AD  - Departamento de Quimica, Universidade de Aveiro, Aveiro, Portugal.
FAU - Azevedo, Nuno F
AU  - Azevedo NF
FAU - Vieira, Maria Joao
AU  - Vieira MJ
FAU - Figueiredo, Ceu
AU  - Figueiredo C
FAU - Goodfellow, Brian J
AU  - Goodfellow BJ
FAU - Monteiro, Mario A
AU  - Monteiro MA
FAU - Coimbra, Manuel A
AU  - Coimbra MA
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20100216
PL  - Netherlands
TA  - Carbohydr Res
JT  - Carbohydrate research
JID - 0043535
RN  - 0 (Lipopolysaccharides)
RN  - 0 (Mannans)
RN  - 11028-71-0 (Concanavalin A)
RN  - J2VZ07J96K (Polymyxin B)
SB  - IM
MH  - Carbohydrate Sequence
MH  - Chromatography, Affinity
MH  - Concanavalin A/chemistry
MH  - Helicobacter pylori/*chemistry
MH  - Lipopolysaccharides/*chemistry
MH  - Magnetic Resonance Spectroscopy
MH  - Mannans/*chemistry
MH  - Molecular Sequence Data
MH  - Polymyxin B/chemistry
MH  - Virulence
EDAT- 2010/03/17 06:00
MHDA- 2010/06/24 06:00
CRDT- 2010/03/16 06:00
PHST- 2009/12/04 00:00 [received]
PHST- 2010/01/26 00:00 [revised]
PHST- 2010/01/29 00:00 [accepted]
PHST- 2010/03/16 06:00 [entrez]
PHST- 2010/03/17 06:00 [pubmed]
PHST- 2010/06/24 06:00 [medline]
AID - S0008-6215(10)00046-7 [pii]
AID - 10.1016/j.carres.2010.01.022 [doi]
PST - ppublish
SO  - Carbohydr Res. 2010 Apr 19;345(6):830-8. doi: 10.1016/j.carres.2010.01.022. Epub 
      2010 Feb 16.

PMID- 9171318
OWN - NLM
STAT- MEDLINE
DCOM- 19970721
LR  - 20061115
IS  - 0022-510X (Print)
IS  - 0022-510X (Linking)
VI  - 149
IP  - 2
DP  - 1997 Aug
TI  - Pathogenesis of the neurotoxicity caused by anti-GD2 antibody therapy.
PG  - 127-30
AB  - After treatment of melanomas with anti-GD2 monoclonal antibody (MAb) (14G2a),
      some patients develop sensorimotor demyelinating polyneuropathy with and without 
      the syndrome of inappropriate antidiuretic hormone (SIADH). To clarify what
      causes the neurotoxicity of anti-GD2 MAb, we investigated the immunohistochemical
      localization of GD2 in the human nervous system. Anti-GD2 MAb (14G2a) reacted
      with the myelin sheaths in the peripheral nerves as well as with the pituicyte
      cytoplasm in the posterior lobe of the pituitary gland. We assume that the
      binding of anti-GD2 MAb to peripheral nerve myelin and the pituicytes in the
      posterior pituitary causes sensorimotor demyelinating neuropathy and SIADH.
FAU - Yuki, N
AU  - Yuki N
AD  - Department of Biochemistry, Faculty of Medicine, Tokyo Medical and Dental
      University, Japan. yuki@dokkyomed.ac.jp
FAU - Yamada, M
AU  - Yamada M
FAU - Tagawa, Y
AU  - Tagawa Y
FAU - Takahashi, H
AU  - Takahashi H
FAU - Handa, S
AU  - Handa S
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - Netherlands
TA  - J Neurol Sci
JT  - Journal of the neurological sciences
JID - 0375403
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Neurotoxins)
RN  - 19600-01-2 (G(M2) Ganglioside)
SB  - IM
MH  - Animals
MH  - Antibodies, Monoclonal/*toxicity
MH  - Biopsy
MH  - Central Nervous System/chemistry/pathology
MH  - Demyelinating Diseases/*chemically induced/etiology/pathology
MH  - G(M2) Ganglioside/analysis/*immunology
MH  - Humans
MH  - Inappropriate ADH Syndrome/chemically induced/etiology/pathology
MH  - Melanoma/secondary/therapy
MH  - Mice
MH  - Myelin Sheath/chemistry/pathology
MH  - Neurotoxins/pharmacology
MH  - Oculomotor Nerve/chemistry/pathology
MH  - Peripheral Nervous System Diseases/*chemically induced/etiology/pathology
MH  - Pituitary Gland/chemistry/pathology
MH  - Sural Nerve/chemistry/pathology
MH  - Tibial Nerve/chemistry/pathology
MH  - Trochlear Nerve/chemistry/pathology
EDAT- 1997/08/01 00:00
MHDA- 1997/08/01 00:01
CRDT- 1997/08/01 00:00
PHST- 1997/08/01 00:00 [pubmed]
PHST- 1997/08/01 00:01 [medline]
PHST- 1997/08/01 00:00 [entrez]
AID - S0022-510X(97)05390-2 [pii]
PST - ppublish
SO  - J Neurol Sci. 1997 Aug;149(2):127-30.

PMID- 7687590
OWN - NLM
STAT- MEDLINE
DCOM- 19930824
LR  - 20160303
IS  - 0020-7136 (Print)
IS  - 0020-7136 (Linking)
VI  - 54
IP  - 6
DP  - 1993 Jul 30
TI  - Importance of E-selectin (ELAM-1) and sialyl Lewis(a) in the adhesion of
      pancreatic carcinoma cells to activated endothelium.
PG  - 972-7
AB  - Adhesion molecules involved in attachment between human pancreatic carcinoma and 
      activated endothelial cells in vitro were investigated. Basal adhesion occurred
      between 6 pancreatic carcinoma cell lines and unstimulated human umbilical vein
      endothelial cells (HUVEC), and augmented basal adhesion to activated HUVEC was
      only seen when pancreatic cancer cells expressed sialyl Lewisa (SLea) and sialyl 
      Lewisx (SLex). Activation of HUVEC with interleukin 1-beta (IL-1 beta) or tumor
      necrosis factor-alpha (TNF-alpha), but not with interferon-gamma (IFN-gamma),
      generated the augmentative basal adhesion. Dose dependence and additive effect
      were observed in augmentation of the basal adhesion induced by IL-1 beta and/or
      TNF-alpha. Increase in adhesion correlated with up-regulation of the surface
      E-selectin (or ELAM-1) on HUVEC, and was evident at both 25 degrees C and 4
      degrees C. Anti-E-selectin and anti-SLea blocked the augmented attachment,
      whereas anti-SLex, an antibody against another known ligand for E-selectin, did
      not. The collective evidence indicates that attachment between pancreas carcinoma
      cells and activated endothelial cells is regulated by cytokines such as IL-1 beta
      and TNF-alpha, and is mediated by SLea on pancreas carcinoma and E-selectin on
      endothelial cells. These molecules may be of significant importance in
      blood-borne metastasis of pancreatic carcinoma cells to inflamed sites.
FAU - Iwai, K
AU  - Iwai K
AD  - Department of Pathology, Hokkaido University School of Medicine, Sapporo, Japan.
FAU - Ishikura, H
AU  - Ishikura H
FAU - Kaji, M
AU  - Kaji M
FAU - Sugiura, H
AU  - Sugiura H
FAU - Ishizu, A
AU  - Ishizu A
FAU - Takahashi, C
AU  - Takahashi C
FAU - Kato, H
AU  - Kato H
FAU - Tanabe, T
AU  - Tanabe T
FAU - Yoshiki, T
AU  - Yoshiki T
LA  - eng
PT  - Journal Article
PL  - United States
TA  - Int J Cancer
JT  - International journal of cancer
JID - 0042124
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Cell Adhesion Molecules)
RN  - 0 (Cytokines)
RN  - 0 (E-Selectin)
RN  - 0 (Gangliosides)
RN  - 91847-18-6 (sialyl Le(a) ganglioside)
SB  - IM
MH  - Aged
MH  - Antibodies, Monoclonal
MH  - Antigens, Tumor-Associated, Carbohydrate/*physiology
MH  - Cell Adhesion/*physiology
MH  - Cell Adhesion Molecules/*physiology
MH  - Cells, Cultured
MH  - Cytokines/physiology
MH  - E-Selectin
MH  - Endothelium, Vascular/cytology/*physiopathology
MH  - Female
MH  - Gangliosides/*physiology
MH  - Humans
MH  - Male
MH  - Middle Aged
MH  - Pancreatic Neoplasms/*physiopathology
MH  - Tumor Cells, Cultured
MH  - Umbilical Veins
EDAT- 1993/07/30 00:00
MHDA- 1993/07/30 00:01
CRDT- 1993/07/30 00:00
PHST- 1993/07/30 00:00 [pubmed]
PHST- 1993/07/30 00:01 [medline]
PHST- 1993/07/30 00:00 [entrez]
PST - ppublish
SO  - Int J Cancer. 1993 Jul 30;54(6):972-7.

PMID- 1513058
OWN - NLM
STAT- MEDLINE
DCOM- 19920925
LR  - 20110727
IS  - 0021-5082 (Print)
IS  - 0021-5082 (Linking)
VI  - 47
IP  - 2
DP  - 1992 Jun
TI  - [Investigation of a new method for separation of neutrophils from a small volume 
      of human blood].
PG  - 650-7
AB  - We have already reported a neutrophil separation method for the multiple
      simultaneous measurement of neutrophil chemiluminescence. However, when the
      reported separation method was used, at least 4 ml of venous blood was needed to 
      collect enough neutrophils for chemiluminescent measurement. Because of this
      blood volume, there is a limitation on applications of the multiple simultaneous 
      method for neonates, infants, and in some clinical situations. To expand the
      application of this neutrophil chemiluminescence measurement into clinical and
      health science areas, we have developed a new method for separation of
      neutrophils from a relatively small amount of blood (500 microliters). In
      addition, the influences of remaining red blood cells and hemoglobin levels in
      the neutrophil fraction on the chemiluminescence were examined to determine the
      necessity for elimination procedures. The new separation method used a capillary 
      tube (length, 130 mm; outside diameter, 5 mm; thickness, 0.8 mm) with density
      gradient reagents (Histopaque 1077 and 1119). After centrifugal separation (500
      g, 30 min), the neutrophil fraction was isolated with 93.1 +/- 4.7% purity and
      60.6 +/- 11.1% yield. This purity and yield were comparable to or better than
      those with the previously reported method, while levels of remaining red blood
      cells and hemoglobin were about the same. Remaining red blood cells and
      hemoglobin in the neutrophil fraction acted on the chemiluminescence as a
      quencher. For the correct estimation of neutrophil chemiluminescence, elimination
      of remaining red blood cells and hemoglobin in the neutrophil fraction is
      necessary. This new neutrophil separation method is a very useful method,
      especially for cases in which available blood amounts are limited.
FAU - Kudoh, E
AU  - Kudoh E
AD  - Department of Hygiene, Hirosaki University School of Medicine.
FAU - Komatu, T
AU  - Komatu T
FAU - Nakaji, S
AU  - Nakaji S
FAU - Sugawara, K
AU  - Sugawara K
FAU - Kumae, T
AU  - Kumae T
LA  - jpn
PT  - English Abstract
PT  - Journal Article
PL  - Japan
TA  - Nihon Eiseigaku Zasshi
JT  - Nihon eiseigaku zasshi. Japanese journal of hygiene
JID - 0417457
SB  - IM
MH  - Cell Separation/*methods
MH  - Humans
MH  - Luminescent Measurements
MH  - *Neutrophils
EDAT- 1992/06/01 00:00
MHDA- 1992/06/01 00:01
CRDT- 1992/06/01 00:00
PHST- 1992/06/01 00:00 [pubmed]
PHST- 1992/06/01 00:01 [medline]
PHST- 1992/06/01 00:00 [entrez]
PST - ppublish
SO  - Nihon Eiseigaku Zasshi. 1992 Jun;47(2):650-7.

PMID- 15730515
OWN - NLM
STAT- MEDLINE
DCOM- 20050912
LR  - 20171116
IS  - 0001-2815 (Print)
IS  - 0001-2815 (Linking)
VI  - 65
IP  - 3
DP  - 2005 Mar
TI  - Epitope recognition of antibodies that define the sialomucin, endolyn (CD164), a 
      negative regulator of haematopoiesis.
PG  - 220-39
AB  - Endolyn (CD164) is a sialomucin that functions as an adhesion molecule and a
      negative regulator of CD34+ CD38- human haematopoietic precursor cell
      proliferation. The 105A5 and 103B2/9E10 CD164 monoclonal antibodies (mAbs), which
      act as surrogate ligands, recognize distinct glycosylation-dependent classes I
      and II epitopes located on domain I of the native and recombinant CD164 proteins.
      Here, we document five new CD164 mAbs, the 96 series, that rely on conformational
      integrity, but not glycosylation, of exons 2- and 3-encoded CD164 domains,
      thereby resembling the class III mAbs, N6B6 and 67D2. Although all the 96 series 
      class III mAbs labelled both the 105A5+ and 103B2/9E10+ cells, cross-competition 
      and immunoblotting studies allow them to be categorized into two distinct class
      III subgroups, i.e. the N6B6-like subgroup that only recognizes 80-100 kDa
      proteins and the 67D2-like subgroup that also recognizes a higher molecular
      weight (>220 kDa) form. To more closely define the reactivity patterns of mAbs to
      the classes I and II epitopes, the global glycosylation patterns of the soluble
      human (h) CD164 proteins were determined using lectin binding, high-performance
      liquid chromatography (HPLC) and mass spectrometry. hCD164 recombinant proteins
      bound to the lectins, Galanthus nivalis agglutinin, Datura stramonium agglutinin,
      Sambucus nigra agglutinin, Maackia amurensis agglutinin and peanut agglutinin,
      indicating the presence of high mannose and complex N-glycans, in addition to
      core 1 O-glycans (the Tn antigen) and alpha2-3 and alpha2-6 sialic acid moieties.
      Our HPLC and mass spectrometry results revealed both high mannose and complex
      N-glycosylation with various numbers of branches increasing the complexity of the
      glycosylation pattern. Most O-glycans were small, core 1 or 2 based. High levels 
      of sialylation in alpha2-3 and alpha2-6 linkages, without sialyl-Lewis X,
      indicate that the majority of these hCD164 recombinant proteins are unable to
      bind to selectins in our assay system, but may interact with Siglec molecules.
FAU - Jorgensen-Tye, B
AU  - Jorgensen-Tye B
AD  - Stem Cell Laboratory, National Blood Service and Nuffield Department of Clinical 
      Laboratory Sciences, The John Radcliffe Hospital, Headington, Oxford, UK.
FAU - Levesque, J-P
AU  - Levesque JP
FAU - Royle, L
AU  - Royle L
FAU - Doyonnas, R
AU  - Doyonnas R
FAU - Chan, J Y-H
AU  - Chan JY
FAU - Dwek, R A
AU  - Dwek RA
FAU - Rudd, P M
AU  - Rudd PM
FAU - Harvey, D J
AU  - Harvey DJ
FAU - Simmons, P J
AU  - Simmons PJ
FAU - Watt, S M
AU  - Watt SM
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - Tissue Antigens
JT  - Tissue antigens
JID - 0331072
RN  - 0 (Agglutinins)
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens, CD)
RN  - 0 (CD146 Antigen)
RN  - 0 (CD164 protein, human)
RN  - 0 (Cd164 protein, mouse)
RN  - 0 (Endolyn)
RN  - 0 (Immunodominant Epitopes)
RN  - 0 (Lectins)
RN  - 0 (Mucins)
RN  - 0 (Neural Cell Adhesion Molecules)
RN  - 0 (Recombinant Proteins)
RN  - 0 (Sialomucins)
RN  - 0 (Transcription Factors)
SB  - IM
MH  - Agglutinins/chemistry
MH  - Animals
MH  - Antibodies, Monoclonal/*immunology
MH  - Antigen-Antibody Reactions
MH  - Antigens, CD/genetics/*immunology/metabolism
MH  - CD146 Antigen
MH  - Chromatography, High Pressure Liquid
MH  - Endolyn
MH  - Epitope Mapping
MH  - Exons
MH  - Glycosylation
MH  - Hematopoiesis/physiology
MH  - Humans
MH  - Immunodominant Epitopes/*analysis
MH  - Lectins/chemistry
MH  - Mice
MH  - Mucins/*immunology
MH  - Neural Cell Adhesion Molecules/genetics/*immunology/metabolism
MH  - Recombinant Proteins/genetics/immunology
MH  - Sialomucins
MH  - Transcription Factors
EDAT- 2005/02/26 09:00
MHDA- 2005/09/13 09:00
CRDT- 2005/02/26 09:00
PHST- 2005/02/26 09:00 [pubmed]
PHST- 2005/09/13 09:00 [medline]
PHST- 2005/02/26 09:00 [entrez]
AID - TAN358 [pii]
AID - 10.1111/j.1399-0039.2005.00358.x [doi]
PST - ppublish
SO  - Tissue Antigens. 2005 Mar;65(3):220-39. doi: 10.1111/j.1399-0039.2005.00358.x.

PMID- 8842706
OWN - NLM
STAT- MEDLINE
DCOM- 19970314
LR  - 20190512
IS  - 0959-6658 (Print)
IS  - 0959-6658 (Linking)
VI  - 6
IP  - 4
DP  - 1996 Jun
TI  - Gal alpha 4Gal-binding antibodies: specificity and use for the mapping of
      glycolipids of Burkitt lymphoma and other human tumors.
PG  - 423-31
AB  - The binding of four different Gal alpha 4Gal-specific antibodies was examined
      using several natural and synthetic Gal alpha 4Gal-containing glycolipids on
      thin-layer chromatograms. One of the antibodies, MC2102, bound much better to
      galabiosylceramide (Gal alpha 4Gal beta Cer) than to the elongated structure
      globotriaosylceramide (Gal alpha 4Gal beta-4Glc beta Cer, CD77). Two antibodies, 
      38.13 and Pk002, bound best to globotriaosylceramide but cross-reacted with the
      P1 antigen (Gal alpha 4Gal beta 3GlcNAc beta 3Gal beta 4Glc beta Cer). The fourth
      antibody tested, P001, reacted most strongly with the P1 antigen but also to some
      extent with globotriaosylceramide. None of the antibodies bound to glycolipids
      with Gal alpha 4Gal placed internally in the carbohydrate chains. The synthetic
      Gal alpha 4Gal beta-bissulfone
      (3-hexadecylsulfonyl-2-hexadecylsulfonylmethylprop-1-yl) was bound by MC2102,
      Pk002, and 38.13 with a strength comparable to Gal alpha 4Gal beta Cer. A large
      number of glycolipids lacking terminal Gal alpha 4Gal were also tested, but none 
      of the antibodies bound to any of these structures. The specificity of the
      studied antibodies was used to investigate the presence of Gal alpha 4Gal
      beta-containing glycolipids in several human and animal tissues and cells and in 
      an experimental Burkitt lymphoma cell line grown in nude mice. Glycolipids were
      also isolated from a series of human tumors and several of them were, by antibody
      binding, found to contain Gal alpha 4Gal beta Cer.
FAU - Lanne, B
AU  - Lanne B
AD  - Department of Medical Biochemistry, Goteborg University, Sweden.
FAU - Jondal, M
AU  - Jondal M
FAU - Karlsson, K A
AU  - Karlsson KA
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - Glycobiology
JT  - Glycobiology
JID - 9104124
RN  - 0 (Antibodies)
RN  - 0 (Gangliosides)
RN  - 0 (Glycolipids)
RN  - 77538-38-6 (galabiosylceramide)
RN  - X2RN3Q8DNE (Galactose)
SB  - IM
MH  - Antibodies/*metabolism
MH  - *Antibody Specificity
MH  - Burkitt Lymphoma/*metabolism
MH  - Carbohydrate Sequence
MH  - Chromatography, Thin Layer
MH  - Galactose/*metabolism
MH  - Gangliosides/immunology
MH  - Glycolipids/*metabolism
MH  - Humans
MH  - Molecular Sequence Data
MH  - Neoplasms/*metabolism
MH  - Spectrometry, Mass, Fast Atom Bombardment
EDAT- 1996/06/01 00:00
MHDA- 1996/06/01 00:01
CRDT- 1996/06/01 00:00
PHST- 1996/06/01 00:00 [pubmed]
PHST- 1996/06/01 00:01 [medline]
PHST- 1996/06/01 00:00 [entrez]
AID - 10.1093/glycob/6.4.423 [doi]
PST - ppublish
SO  - Glycobiology. 1996 Jun;6(4):423-31. doi: 10.1093/glycob/6.4.423.

PMID- 1618643
OWN - NLM
STAT- MEDLINE
DCOM- 19920731
LR  - 20181113
IS  - 0301-5564 (Print)
IS  - 0301-5564 (Linking)
VI  - 97
IP  - 4
DP  - 1992 May
TI  - Immunohistochemical demonstration of glycoconjugates bearing the type 2
      chain-backbone structure in human fetal, normal and neoplastic gastrointestinal
      tract.
PG  - 303-10
AB  - Immunohistochemical distributions of carbohydrate antigens based on the type 2
      chain in normal as well as fetal and neoplastic tissues of human gastrointestinal
      tract were investigated with a monoclonal antibody (MAb) H11 (specific for type 2
      chain) alone and in combination with the two MAbs MSG15 (for alpha 2----6
      sialylated type 2 chain) and IB9 (for the alpha 2----6 sialylated type 2 chain
      and glycoproteins having NeuAc alpha 2----6Gal-NAc), and 188C1 (for short- and
      long-chain Lex antigens) and FH2 (for the long-chain Lex antigen). In the pyloric
      mucosa of secretors, the type 2 chain is oncodevelopmentally expressed, but in
      non-secretors it is detected in surface mucous cells of normal gastric mucosa.
      The alpha 2----6 sialylation, which is confined to endocrine cells of normal
      pyloric mucosa, occurs in fetal and carcinoma tissues. Irrespective of the
      secretor status, the short- and the long-chain Lex antigens can be detected in
      mature and immature glandular mucous cells of normal gastric mucosa,
      respectively; both antigens are also expressed in fetal and carcinoma tissues. In
      the colon, the type 2 chain and its alpha 2----6 sialylated counterpart are
      expressed in an oncodevelopmental manner. The short- and the long-chain Lex
      antigens are significantly enhanced in colonic carcinoma. The glycoproteins with 
      NeuAc alpha 2----6GalNAc residues appear in gastric and colonic carcinoma as well
      as intestinalized gastric mucosa and transitional mucosa. Thus, some of these
      antigens were distinctively expressed in certain epithelial cells lining the
      normal gastrointestinal tract depending on maturation and patients' secretor
      status, and some were oncodevelopmental or carcinoma-associated antigens of the
      human gastrointestinal tract.
FAU - Nakayama, J
AU  - Nakayama J
AD  - Central Clinical Laboratories, Shinshu University Hospital, Matsumoto, Japan.
FAU - Ota, H
AU  - Ota H
FAU - Katsuyama, T
AU  - Katsuyama T
FAU - Kanai, M
AU  - Kanai M
FAU - Taki, T
AU  - Taki T
FAU - Hirabayashi, Y
AU  - Hirabayashi Y
FAU - Suzuki, Y
AU  - Suzuki Y
LA  - eng
PT  - Journal Article
PL  - Germany
TA  - Histochemistry
JT  - Histochemistry
JID - 0411300
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens, Neoplasm)
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Biomarkers, Tumor)
RN  - 0 (Glycoconjugates)
RN  - 0 (Lewis Blood-Group System)
RN  - 0 (sialosyl-Tn antigen)
SB  - IM
MH  - Antibodies, Monoclonal
MH  - Antigens, Neoplasm/analysis
MH  - *Antigens, Tumor-Associated, Carbohydrate
MH  - Biomarkers, Tumor/analysis
MH  - Carbohydrate Sequence
MH  - Fetus
MH  - Gastric Mucosa/embryology/*immunology
MH  - Gastrointestinal Neoplasms/*immunology
MH  - Glycoconjugates/*analysis/immunology
MH  - Humans
MH  - Immunohistochemistry
MH  - Intestinal Mucosa/embryology/*immunology
MH  - Lewis Blood-Group System/*analysis
MH  - Molecular Sequence Data
EDAT- 1992/05/01 00:00
MHDA- 1992/05/01 00:01
CRDT- 1992/05/01 00:00
PHST- 1992/05/01 00:00 [pubmed]
PHST- 1992/05/01 00:01 [medline]
PHST- 1992/05/01 00:00 [entrez]
PST - ppublish
SO  - Histochemistry. 1992 May;97(4):303-10.

PMID- 15843572
OWN - NLM
STAT- MEDLINE
DCOM- 20050621
LR  - 20190516
IS  - 0022-1767 (Print)
IS  - 0022-1767 (Linking)
VI  - 174
IP  - 9
DP  - 2005 May 1
TI  - Antibodies against tumor cell glycolipids and proteins, but not mucins, mediate
      complement-dependent cytotoxicity.
PG  - 5706-12
AB  - One of several effector mechanisms thought to contribute to Ab efficacy against
      cancer is complement-dependent cytotoxicity (CDC). Serological analysis of a
      series of clinical trials conducted over a 10-year period suggested that six
      vaccines containing different glycolipids induced Abs mediating CDC whereas four 
      vaccines containing carbohydrate or peptide epitopes carried almost exclusively
      by mucin molecules induced Abs that did not mediate CDC. To explore this further,
      we have now compared cell surface reactivity using flow cytometry assays (FACS), 
      complement-fixing ability, and CDC activity of a panel of mAbs and immune sera
      from these trials on the same two tumor cell lines. Abs against glycolipids GM2, 
      globo H and Lewis Y, protein KSA (epithelial cell adhesion molecule, also known
      as EpCAM) and mucin Ags Tn, sialylated Tn, Thomsen Friedenreich (TF), and MUC1
      all reacted comparably by FACS with tumor cells expressing these Ags. Compared
      with the strong complement binding and CDC with Abs against glycolipids and KSA, 
      complement binding was diminished with Abs against mucin Ags and no CDC was
      detected. A major difference between these two groups of Ags is proximity to the 
      cell membrane. Glycolipids and globular glycoproteins extend less than 100 A from
      the cell membrane while mucins extend up to 5000 A. Although complement
      activation at sites remote from the cell membrane has long been known as a
      mechanism for resistance from complement lysis in bacteria, it is identified here
      for the first time as a factor which may contribute to resistance from CDC
      against cancer cells.
FAU - Ragupathi, Govind
AU  - Ragupathi G
AD  - Department of Medicine, Memorial Sloan-Kettering Cancer Center, New York City, NY
      10021, USA.
FAU - Liu, Nancy X
AU  - Liu NX
FAU - Musselli, Cristina
AU  - Musselli C
FAU - Powell, Shemeeakah
AU  - Powell S
FAU - Lloyd, Kenneth
AU  - Lloyd K
FAU - Livingston, Philip O
AU  - Livingston PO
LA  - eng
GR  - P0 1 CA33049/CA/NCI NIH HHS/United States
GR  - P0 1 CA52477/CA/NCI NIH HHS/United States
PT  - Comparative Study
PT  - Journal Article
PT  - Research Support, N.I.H., Extramural
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - J Immunol
JT  - Journal of immunology (Baltimore, Md. : 1950)
JID - 2985117R
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antibodies, Neoplasm)
RN  - 0 (Cancer Vaccines)
RN  - 0 (Complement Membrane Attack Complex)
RN  - 0 (Glycolipids)
RN  - 0 (Immune Sera)
RN  - 0 (Mucins)
RN  - 0 (Neoplasm Proteins)
RN  - 9007-36-7 (Complement System Proteins)
SB  - AIM
SB  - IM
MH  - Antibodies, Monoclonal/metabolism/toxicity
MH  - Antibodies, Neoplasm/metabolism/*physiology/toxicity
MH  - Binding Sites, Antibody
MH  - Cancer Vaccines/administration & dosage/immunology
MH  - Cell Line, Tumor
MH  - Cell Membrane/immunology/metabolism
MH  - Complement Activation/immunology
MH  - Complement Membrane Attack Complex/metabolism
MH  - Complement System Proteins/*physiology
MH  - Cytotoxicity, Immunologic/*immunology
MH  - Glycolipids/*immunology
MH  - Humans
MH  - Immune Sera/metabolism/toxicity
MH  - Mucins/*immunology
MH  - Neoplasm Proteins/*immunology
EDAT- 2005/04/22 09:00
MHDA- 2005/06/23 09:00
CRDT- 2005/04/22 09:00
PHST- 2005/04/22 09:00 [pubmed]
PHST- 2005/06/23 09:00 [medline]
PHST- 2005/04/22 09:00 [entrez]
AID - 174/9/5706 [pii]
AID - 10.4049/jimmunol.174.9.5706 [doi]
PST - ppublish
SO  - J Immunol. 2005 May 1;174(9):5706-12. doi: 10.4049/jimmunol.174.9.5706.

PMID- 2981150
OWN - NLM
STAT- MEDLINE
DCOM- 19850221
LR  - 20071114
IS  - 0008-543X (Print)
IS  - 0008-543X (Linking)
VI  - 55
IP  - 3
DP  - 1985 Feb 1
TI  - Tn, a carcinoma-associated antigen, reacts with anti-Tn of normal human sera.
PG  - 561-9
AB  - Tn antigen is the immediate precursor of the carcinoma (CA)-associated T antigen;
      both are masked in non-CA tissues. Tn antigen was detected by absorption of human
      anti-Tn antibody in 46 of 50 primary breast CAs and in all 6 metastases
      originating from Tn-positive primary CAs. Thirteen of 25 (52%) anaplastic CAs,
      but only 2 of 15 (13%) well differentiated CAs had more Tn than T; 1 anaplastic
      CA had neither antigen. Eighteen of 20 benign breast lesions had no Tn; the 2
      positive lesions were premalignant. All 19 breast CAs, studied
      immunohistochemically, reacted strongly with human polyclonal anti-Tn; benign or 
      normal glandular tissues had minimal or no reactivity. Among live cancer cell
      lines, the most malignant sublines had more Tn than T on their cell surfaces.
      Preliminary studies with rodent monoclonal anti-Tn and anti-T antibodies gave
      immunohistochemical reactivity patterns similar to those of the polyclonal
      antibodies, but the former were less sensitive in absorption tests. Tn is a CA
      marker that promises to be useful in tumor detection.
FAU - Springer, G F
AU  - Springer GF
FAU - Taylor, C R
AU  - Taylor CR
FAU - Howard, D R
AU  - Howard DR
FAU - Tegtmeyer, H
AU  - Tegtmeyer H
FAU - Desai, P R
AU  - Desai PR
FAU - Murthy, S M
AU  - Murthy SM
FAU - Felder, B
AU  - Felder B
FAU - Scanlon, E F
AU  - Scanlon EF
LA  - eng
GR  - CA 19083/CA/NCI NIH HHS/United States
GR  - CA 22540/CA/NCI NIH HHS/United States
GR  - CA 29211/CA/NCI NIH HHS/United States
GR  - etc.
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Cancer
JT  - Cancer
JID - 0374236
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens, Neoplasm)
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Antigens, Viral, Tumor)
RN  - 0 (Blood Group Antigens)
RN  - 0 (Tn antigen)
SB  - AIM
SB  - IM
MH  - Animals
MH  - Antibodies, Monoclonal/immunology
MH  - Antigen-Antibody Reactions
MH  - Antigens, Neoplasm/*immunology
MH  - *Antigens, Tumor-Associated, Carbohydrate
MH  - Antigens, Viral, Tumor/immunology
MH  - Blood Group Antigens/*immunology
MH  - Breast Neoplasms/*immunology
MH  - Carcinoma/*immunology
MH  - Carcinoma, Intraductal, Noninfiltrating/immunology
MH  - Cell Line
MH  - Female
MH  - Hemagglutination Tests
MH  - Histocytochemistry
MH  - Humans
MH  - Immunochemistry
MH  - Immunosorbent Techniques
MH  - Lymphoma/immunology
MH  - Mammary Neoplasms, Experimental/immunology
MH  - Mice
MH  - Neoplasm Metastasis
MH  - Neoplasm Recurrence, Local
MH  - Rats
EDAT- 1985/02/01 00:00
MHDA- 1985/02/01 00:01
CRDT- 1985/02/01 00:00
PHST- 1985/02/01 00:00 [pubmed]
PHST- 1985/02/01 00:01 [medline]
PHST- 1985/02/01 00:00 [entrez]
PST - ppublish
SO  - Cancer. 1985 Feb 1;55(3):561-9.

PMID- 1618644
OWN - NLM
STAT- MEDLINE
DCOM- 19920731
LR  - 20181113
IS  - 0301-5564 (Print)
IS  - 0301-5564 (Linking)
VI  - 97
IP  - 4
DP  - 1992 May
TI  - Altered expression of sialyl-Tn, Lewis antigens and carcinoembryonic antigen
      between primary and metastatic lesions of uterine cervical cancers.
PG  - 311-7
AB  - Immunohistochemical examination was performed of serial sections of 24 normal
      human adult cervical tissues and 53 human cervical carcinomas including 36 cases 
      with lymph node metastasis. For this investigation, monoclonal antibodies
      directed to Lewis-X, Lewis-Y, sialyl-dimeric Lewis-X (SDLX), sialyl-Tn (STn) and 
      carcinoembryonic antigen (CEA) were used. STn and CEA antigens were expressed
      very weakly in the normal cervical epithelium but strongly in the cancer cells,
      indicating the antigens to be oncogenic antigens of cervical squamous cell
      carcinoma. No significant difference in immunoreactivity was observed between
      primary and metastatic lesions of carcinoma or between primary lesions with and
      without metastasis. However, the expression patterns of STn and Lewis-Y antigens 
      were quite different between primary lesions and metastatic lesions. In primary
      lesions the cancer cell nests tended to be stained centrally, but in metastatic
      lesions the cancer cell nests tended to be stained peripherally. This finding may
      reflect an important role of these carbohydrate chains in the process of
      metastasis of cervical squamous cell carcinoma to regional lymph nodes.
FAU - Ogawa, H
AU  - Ogawa H
AD  - Department of Obstetrics and Gynecology, Osaka University Medical School, Japan.
FAU - Inoue, M
AU  - Inoue M
FAU - Tanizawa, O
AU  - Tanizawa O
FAU - Miyamoto, M
AU  - Miyamoto M
FAU - Sakurai, M
AU  - Sakurai M
LA  - eng
PT  - Comparative Study
PT  - Journal Article
PL  - Germany
TA  - Histochemistry
JT  - Histochemistry
JID - 0411300
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens, Neoplasm)
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Carcinoembryonic Antigen)
RN  - 0 (Lewis Blood-Group System)
RN  - 0 (sialosyl-Tn antigen)
SB  - IM
MH  - Antibodies, Monoclonal
MH  - Antigens, Neoplasm/*analysis
MH  - *Antigens, Tumor-Associated, Carbohydrate
MH  - Carcinoembryonic Antigen/*analysis
MH  - Carcinoma, Squamous Cell/*immunology/secondary
MH  - Cervix Uteri/*immunology
MH  - Female
MH  - Humans
MH  - Immunohistochemistry
MH  - Lewis Blood-Group System/*analysis
MH  - Lymphatic Metastasis
MH  - Uterine Cervical Neoplasms/*immunology
EDAT- 1992/05/01 00:00
MHDA- 1992/05/01 00:01
CRDT- 1992/05/01 00:00
PHST- 1992/05/01 00:00 [pubmed]
PHST- 1992/05/01 00:01 [medline]
PHST- 1992/05/01 00:00 [entrez]
PST - ppublish
SO  - Histochemistry. 1992 May;97(4):311-7.

PMID- 2424969
OWN - NLM
STAT- MEDLINE
DCOM- 19860731
LR  - 20180303
IS  - 0168-8278 (Print)
IS  - 0168-8278 (Linking)
VI  - 2
IP  - 3
DP  - 1986
TI  - Human hepatocellular carcinoma-associated changes of glycosphingolipids detected 
      by two monoclonal antibodies FH2 and IB9.
PG  - 430-40
AB  - The changes of minor glycosphingolipids associated with human hepatocellular
      carcinomas were studied using monoclonal antibodies. Glycosphingolipids of twelve
      patients were isolated from the tumor tissues and their adjacent cirrhotic liver 
      tissues. The immunoreactivities of glycosphingolipids with two monoclonal
      antibodies FH2 and IB9, that define x-structure (Gal beta 1-4[Fuc alpha
      1-3]GlcNAc) and sialosyl alpha 2-6galactosyl residue, respectively, were studied 
      by a solid phase enzyme-linked immunosorbent assay and a chromatogram
      immunobinding assay. X-structure was detected in the upper-phase neutral
      glycosphingolipids from both the cirrhotic liver tissues and the tumor tissues,
      but was generally expressed more strongly in the latter tissues. The thin-layer
      chromatography patterns of x-active glycosphingolipids were more complex in the
      tumor tissues. Sialosyl alpha 2-6galactosyl residue was detected in two
      ganglioside fractions. One ganglioside with faster migration on a thin-layer
      chromatogram was found in both the non-tumorous tissues and the tumor tissues.
      Another ganglioside with slower migration was more often detected in the tumor
      tissues. It was concluded that some of minor glycosphingolipids detected by
      monoclonal antibodies FH2 and IB9 could be the 'tumor-associated' antigens.
FAU - Okada, Y
AU  - Okada Y
FAU - Arima, T
AU  - Arima T
FAU - Nagashima, H
AU  - Nagashima H
FAU - Fukushi, Y
AU  - Fukushi Y
FAU - Kannagi, R
AU  - Kannagi R
FAU - Kaizu, T
AU  - Kaizu T
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - Netherlands
TA  - J Hepatol
JT  - Journal of hepatology
JID - 8503886
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Gangliosides)
RN  - 0 (Glycosphingolipids)
RN  - 0 (alpha-Fetoproteins)
SB  - IM
MH  - Antibodies, Monoclonal/*immunology
MH  - Carcinoma, Hepatocellular/*analysis
MH  - Chromatography, Thin Layer
MH  - Gangliosides/analysis
MH  - Glycosphingolipids/*analysis/immunology
MH  - Humans
MH  - Liver Neoplasms/*analysis
MH  - alpha-Fetoproteins/analysis
EDAT- 1986/01/01 00:00
MHDA- 1986/01/01 00:01
CRDT- 1986/01/01 00:00
PHST- 1986/01/01 00:00 [pubmed]
PHST- 1986/01/01 00:01 [medline]
PHST- 1986/01/01 00:00 [entrez]
AID - S0168-8278(86)80054-X [pii]
PST - ppublish
SO  - J Hepatol. 1986;2(3):430-40.

PMID- 8095932
OWN - NLM
STAT- MEDLINE
DCOM- 19930416
LR  - 20190512
IS  - 0021-924X (Print)
IS  - 0021-924X (Linking)
VI  - 113
IP  - 1
DP  - 1993 Jan
TI  - Preparation of mouse-human chimeric antibody to an embryonic carbohydrate
      antigen, Lewis Y.
PG  - 114-7
AB  - Stage-specific embryonic antigen-1 (SSEA-1) is a well-known carbohydrate antigen 
      that is specifically expressed on the surface of cancer cells as well as
      embryonic cells. In this study, starting with a previously established hybridoma 
      producing a monoclonal antibody (named H18A) to Lewis Y antigen, which is closely
      related to SSEA-1, we cloned genomic DNA encoding active variable regions both of
      heavy and light chains of the antibody. Sequence analysis showed that VH and V
      kappa genes of H18A were in the VH 7183 family and V kappa C1 family,
      respectively. A transfected cell line named HC-H18A-7 expressing a recombinant
      chimeric H18A composed of mouse-derived antigen-binding variable regions and
      human-derived constant regions was established. The chimeric H18A was purified to
      homogeneity and shown to bind purified Lewis Y antigen with the same
      dose-response curve as the original H18A. The chimeric H18A looks more promising 
      for clinical application than the original mouse-derived H18A because its
      antigenicity is expected to be reduced.
FAU - Kaneko, T
AU  - Kaneko T
AD  - Biotechnology Research Laboratory, Tosoh Corporation, Kanagawa.
FAU - Iba, Y
AU  - Iba Y
FAU - Zenita, K
AU  - Zenita K
FAU - Shigeta, K
AU  - Shigeta K
FAU - Nakano, K
AU  - Nakano K
FAU - Itoh, W
AU  - Itoh W
FAU - Kurosawa, Y
AU  - Kurosawa Y
FAU - Kannagi, R
AU  - Kannagi R
FAU - Yasukawa, K
AU  - Yasukawa K
LA  - eng
PT  - Journal Article
PL  - England
TA  - J Biochem
JT  - Journal of biochemistry
JID - 0376600
RN  - 0 (Antibodies)
RN  - 0 (Immunoglobulin Heavy Chains)
RN  - 0 (Immunoglobulin Light Chains)
RN  - 0 (Lewis Blood-Group System)
RN  - 0 (Lewis X Antigen)
RN  - 0 (Recombinant Fusion Proteins)
RN  - 9007-49-2 (DNA)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Antibodies/genetics/*immunology
MH  - Base Sequence
MH  - Carbohydrate Sequence
MH  - DNA/chemistry
MH  - Genes, Immunoglobulin
MH  - Genetic Vectors
MH  - Humans
MH  - Immunoglobulin Heavy Chains/chemistry/genetics
MH  - Immunoglobulin Light Chains/chemistry/genetics
MH  - Lewis Blood-Group System/chemistry/*immunology
MH  - Lewis X Antigen/chemistry/immunology
MH  - Mice
MH  - Molecular Sequence Data
MH  - Plasmids
MH  - Recombinant Fusion Proteins/biosynthesis/genetics/immunology
MH  - Transfection
EDAT- 1993/01/01 00:00
MHDA- 1993/01/01 00:01
CRDT- 1993/01/01 00:00
PHST- 1993/01/01 00:00 [pubmed]
PHST- 1993/01/01 00:01 [medline]
PHST- 1993/01/01 00:00 [entrez]
AID - 10.1093/oxfordjournals.jbchem.a123993 [doi]
PST - ppublish
SO  - J Biochem. 1993 Jan;113(1):114-7. doi: 10.1093/oxfordjournals.jbchem.a123993.

PMID- 1847560
OWN - NLM
STAT- MEDLINE
DCOM- 19910327
LR  - 20131121
IS  - 0041-1132 (Print)
IS  - 0041-1132 (Linking)
VI  - 31
IP  - 2
DP  - 1991 Feb
TI  - Immunochemical studies on the differential binding properties of two monoclonal
      antibodies reacting with Tn red cells.
PG  - 142-9
AB  - Two monoclonal antibodies (MoAbs), BRIC 66 (IgM) and BRIC 111 (IgG1), were
      produced by immunizing mice with ovarian cyst blood group A1 glycoprotein and Tn 
      red cells (RBCs), respectively. Their specificities were determined by
      inhibitions using Tn sialoglycoproteins (SGPs), mucins (armadillo [ASG] and ovine
      [OSG] submaxillary glycoproteins), and monosaccharides. BRIC 66 agglutinated both
      Tn and group A RBCs and reacted immunohistochemically with both the vascular
      endothelium and tumor cells from a group A adenocarcinoma, BRIC 66 was inhibited 
      by N-acetylgalactosamine (GalNAc), Tn SGPs, and mucins on both hemagglutination
      inhibition tests and radioimmunoassay. BRIC 111 agglutinated Tn RBCs only, and it
      specifically stained tumor cells from a group O patient's breast carcinoma and a 
      group A patient's adenocarcinoma. In hemagglutination inhibition tests, BRIC 111 
      was readily inhibited by Tn SGPs, only partially inhibited by GalNAc, and not
      inhibited by mucins. In a sensitive radioimmunoassay, BRIC 111 was inhibitable by
      GalNAc. Tn SGP was 2000-fold more effective as an inhibitor than the mucins (ASG 
      and desialized OSG), which contain a high content of terminal
      alpha-GalNAc-O-serine (threonine) residues. It is postulated that BRIC 66 is
      specific for terminal alpha-GalNAc units in carbohydrate chains. The exclusive
      reaction of BRIC 111 with Tn SGP indicates a combining site larger than GalNAc
      alpha-1, which probably includes amino acid residues in juxtaposition to GalNAc
      in Tn SGP. In view of its specific agglutination of Tn RBCs, BRIC 111 is a useful
      reagent for the examination of polyagglutinable RBCs.
FAU - King, M J
AU  - King MJ
AD  - Blood Group Reference Laboratory, Bristol, UK.
FAU - Parsons, S F
AU  - Parsons SF
FAU - Wu, A M
AU  - Wu AM
FAU - Jones, N
AU  - Jones N
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Transfusion
JT  - Transfusion
JID - 0417360
RN  - 0 (ABO Blood-Group System)
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens, Neoplasm)
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Glycoproteins)
RN  - 0 (Mucins)
RN  - 0 (Sialic Acids)
RN  - 0 (Sialoglycoproteins)
RN  - 0 (Tn antigen)
RN  - 10450-60-9 (Periodic Acid)
RN  - EC 3.2.1.18 (Neuraminidase)
RN  - GZP2782OP0 (N-Acetylneuraminic Acid)
RN  - KM15WK8O5T (Acetylgalactosamine)
SB  - IM
MH  - ABO Blood-Group System/immunology
MH  - Absorption
MH  - Acetylgalactosamine/pharmacology
MH  - Adenocarcinoma/immunology
MH  - Antibodies, Monoclonal/*immunology
MH  - Antigens, Neoplasm/analysis/*immunology
MH  - *Antigens, Tumor-Associated, Carbohydrate
MH  - Breast Neoplasms/immunology
MH  - Erythrocytes/*immunology
MH  - Female
MH  - Glycoproteins/immunology/pharmacology
MH  - Hemagglutination
MH  - Humans
MH  - Immunoenzyme Techniques
MH  - Mucins/pharmacology
MH  - N-Acetylneuraminic Acid
MH  - Neuraminidase/pharmacology
MH  - Ovarian Cysts/immunology
MH  - Oxidation-Reduction
MH  - Periodic Acid
MH  - Sialic Acids/immunology
MH  - Sialoglycoproteins/immunology
EDAT- 1991/02/01 00:00
MHDA- 1991/02/01 00:01
CRDT- 1991/02/01 00:00
PHST- 1991/02/01 00:00 [pubmed]
PHST- 1991/02/01 00:01 [medline]
PHST- 1991/02/01 00:00 [entrez]
PST - ppublish
SO  - Transfusion. 1991 Feb;31(2):142-9.

PMID- 9530960
OWN - NLM
STAT- MEDLINE
DCOM- 19980506
LR  - 20181113
IS  - 0282-0080 (Print)
IS  - 0282-0080 (Linking)
VI  - 15
IP  - 1
DP  - 1998 Jan
TI  - Structures of the N-linked carbohydrate of ascorbic acid oxidase from zucchini.
PG  - 79-82
AB  - The N-glycan moiety of ascorbic acid oxidase from zucchini (Cucurbita pepo) has
      been described to be a core-pentasaccharide with a xylose [D'Andrea et al. (1988)
      Glycoconjugate J 5:151-7]. Ascorbic acid oxidase is sometimes used to
      characterize antibodies directed against carbohydrate determinants on plant
      glycoproteins. To prevent misinterpretations of immunological data, the structure
      of the N-glycan of ascorbic acid oxidase has been reinvestigated. The
      oligosaccharides were released by almond N-glycosidase and analysed as their
      pyridylamino derivatives by 2D-HPLC and exoglycosidase digestions. The main
      structure resembled the typical complex plant N-glycan consisting of a
      core-pentasaccharide decorated with xylose and 3-linked fucose. The other
      abundant species lacked the fucose residue. Small amounts of these glycans
      carried a GlcNAc residue on the 6-arm. Therefore, ascorbic acid oxidase will not 
      only react with antibodies directed against the xylosylated region but also with 
      those binding to N-glycans with 3-linked fucose.
FAU - Altmann, F
AU  - Altmann F
AD  - Institut fur Chemie, Universitat fur Bodenkultur, Wien, Austria.
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Glycoconj J
JT  - Glycoconjugate journal
JID - 8603310
RN  - 0 (Glycoproteins)
RN  - 0 (Plant Proteins)
RN  - 0 (Polysaccharides)
RN  - EC 1.10.3.3 (Ascorbate Oxidase)
SB  - IM
MH  - Ascorbate Oxidase/*chemistry
MH  - Carbohydrate Sequence
MH  - Cucurbitaceae/*enzymology
MH  - Glycoproteins/*chemistry
MH  - Molecular Sequence Data
MH  - Plant Proteins/chemistry
MH  - Polysaccharides/chemistry
EDAT- 1998/04/08 00:00
MHDA- 1998/04/08 00:01
CRDT- 1998/04/08 00:00
PHST- 1998/04/08 00:00 [pubmed]
PHST- 1998/04/08 00:01 [medline]
PHST- 1998/04/08 00:00 [entrez]
PST - ppublish
SO  - Glycoconj J. 1998 Jan;15(1):79-82.

PMID- 2118368
OWN - NLM
STAT- MEDLINE
DCOM- 19901011
LR  - 20151119
IS  - 0214-6282 (Print)
IS  - 0214-6282 (Linking)
VI  - 34
IP  - 1
DP  - 1990 Mar
TI  - Regulated changes in chondroitin sulfation during embryogenesis: an
      immunohistochemical approach.
PG  - 191-204
AB  - Chondroitin sulfate proteoglycans, which represent the main class of nonfibrous
      macromolecules found in the extracellular matrix of connective tissues, have been
      implicated in the control of a variety of cell activities during ontogenesis. The
      respective contributions of the chondroitin sulfate chains and of the protein
      moiety of the proteoglycan in morphogenesis and cytodifferentiation are not
      known. In this context, monoclonal antibodies identifying specific chondroitin
      sulfate chains are interesting new tools. A panel of well characterized
      monoclonal antibodies recognizing distinct epitopes present only in chondroitin
      sulfate chains was used in conjunction with immunohistochemical techniques for
      the purpose of identifying and mapping chondroitin sulfate isoforms during
      development in the mouse and rat fetus. Expression of chondroitin sulfate
      isoforms occurred in the tissues according to specific spatio-temporal patterns, 
      suggesting that chondroitin sulfates differing in sulfation position and degree
      perform distinct functions in development.
FAU - Mark, M P
AU  - Mark MP
AD  - Institut de Biologie Medicale, INSERM-Universite Louis Pasteur, Faculte de
      Medecipe, Strasbourg, France.
FAU - Baker, J R
AU  - Baker JR
FAU - Kimata, K
AU  - Kimata K
FAU - Ruch, J V
AU  - Ruch JV
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Review
PL  - Spain
TA  - Int J Dev Biol
JT  - The International journal of developmental biology
JID - 8917470
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Chondroitin Sulfate Proteoglycans)
RN  - 0 (Proteoglycans)
RN  - 9007-27-6 (Chondroitin)
RN  - 9007-28-7 (Chondroitin Sulfates)
SB  - IM
MH  - Animals
MH  - Antibodies, Monoclonal
MH  - Chondroitin/*analogs & derivatives
MH  - Chondroitin Sulfate Proteoglycans/*physiology
MH  - Chondroitin Sulfates/*physiology
MH  - *Embryonic and Fetal Development
MH  - Fetus/cytology/physiology
MH  - Immunohistochemistry
MH  - Morphogenesis
MH  - Proteoglycans/*physiology
MH  - Rats
RF  - 62
EDAT- 1990/03/01 00:00
MHDA- 1990/03/01 00:01
CRDT- 1990/03/01 00:00
PHST- 1990/03/01 00:00 [pubmed]
PHST- 1990/03/01 00:01 [medline]
PHST- 1990/03/01 00:00 [entrez]
PST - ppublish
SO  - Int J Dev Biol. 1990 Mar;34(1):191-204.

PMID- 2429066
OWN - NLM
STAT- MEDLINE
DCOM- 19861113
LR  - 20071114
IS  - 0023-6837 (Print)
IS  - 0023-6837 (Linking)
VI  - 55
IP  - 4
DP  - 1986 Oct
TI  - Immunoanatomic distribution of blood group antigens in the human urinary tract.
      Influence of secretor status.
PG  - 444-54
AB  - Seven mouse monoclonal antibodies and the lectin from Ulex europaeus, detecting
      blood group specificities of the ABH and Lewis systems, have been used to define 
      the immunoanatomic distribution of these antigenic structures within the human
      nephron and urothelium. The reagents employed recognize the following blood group
      related antigens: A (all variants), B, H, Lewisa (Lea), Lewisb (Leb), X (Lewisx),
      Y (Lewisy) and type 1 precursor chain. We have analyzed the presence of these
      antigens in histologically normal kidney and urothelium from 22 adults and 3
      fetuses by the immunoperoxidase method. In addition, we simultaneously examined
      blood group and secretor status in 15 of the 22 adult individuals studied.
      Immunohistochemical analyses demonstrated that these antigenic systems are
      differentially expressed in cell types and domains of the human urinary tract.
      Major differences were observed in secretor as compared to nonsecretor
      individuals, mainly in the more pronounced expression of precursor, H, Leb, and Y
      antigens in secretors. In the kidney, all antigens, except X, showed enhanced
      expression in secretor individuals on epithelial cells of the collecting ducts
      and urothelium; X antigen was mainly present in the proximal tubules and portions
      of Henle's loop. The urothelium was particularly rich in blood group antigens and
      in some cases showed differential expression of Lea/X and Leb/Y on the various
      cell layers. Secretors could be divided into two groups based on the intensity
      and pattern of staining; it is suggested that this may be determined by homo- or 
      heterozygosity at the Se locus. Nonsecretor individuals lacked expression of Leb 
      and Y determinants, as well as H antigen, in the urothelium (three of four
      cases). Comparison of normal fetal and adult tissues suggest that the expression 
      of some of these antigens is related to maturation stages of the human nephron.
      These studies confirm the importance of blood group antigens as normal
      differentiation antigens. These reagents have a wide range of applications
      including typing of blood group and secretory status in body fluids and tissues, 
      studies of histogenesis and organogenesis, and analyses of neoplastic and
      non-neoplastic diseases.
FAU - Cordon-Cardo, C
AU  - Cordon-Cardo C
FAU - Lloyd, K O
AU  - Lloyd KO
FAU - Finstad, C L
AU  - Finstad CL
FAU - McGroarty, M E
AU  - McGroarty ME
FAU - Reuter, V E
AU  - Reuter VE
FAU - Bander, N H
AU  - Bander NH
FAU - Old, L J
AU  - Old LJ
FAU - Melamed, M R
AU  - Melamed MR
LA  - eng
GR  - CA-14134/CA/NCI NIH HHS/United States
GR  - CA-21445/CA/NCI NIH HHS/United States
GR  - CA-41021/CA/NCI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Lab Invest
JT  - Laboratory investigation; a journal of technical methods and pathology
JID - 0376617
RN  - 0 (ABO Blood-Group System)
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Blood Group Antigens)
RN  - 0 (Epitopes)
RN  - 0 (Glycolipids)
RN  - 0 (Glycoproteins)
RN  - 0 (Lewis Blood-Group System)
SB  - IM
MH  - ABO Blood-Group System/immunology
MH  - Antibodies, Monoclonal/immunology
MH  - Blood Group Antigens/genetics/*immunology
MH  - Epitopes/analysis
MH  - Fetus/immunology
MH  - Glycolipids/analysis
MH  - Glycoproteins/analysis
MH  - Heterozygote
MH  - Histocytochemistry
MH  - Homozygote
MH  - Humans
MH  - Kidney/*immunology
MH  - Lewis Blood-Group System/immunology
MH  - Urinary Bladder/*immunology
EDAT- 1986/10/01 00:00
MHDA- 1986/10/01 00:01
CRDT- 1986/10/01 00:00
PHST- 1986/10/01 00:00 [pubmed]
PHST- 1986/10/01 00:01 [medline]
PHST- 1986/10/01 00:00 [entrez]
PST - ppublish
SO  - Lab Invest. 1986 Oct;55(4):444-54.

PMID- 7751324
OWN - NLM
STAT- MEDLINE
DCOM- 19950622
LR  - 20181113
IS  - 0171-5216 (Print)
IS  - 0171-5216 (Linking)
VI  - 121
IP  - 4
DP  - 1995
TI  - Distribution of Tn antigen recognized by an anti-Tn monoclonal antibody (MLS128) 
      in normal and malignant tissues of the digestive tract.
PG  - 247-52
AB  - Alterations in the normal glycosylation process are often associated with
      oncogenic transformation. Using an anti-Tn monoclonal antibody, MLS128, we have
      investigated the immunohistochemical localization of Tn antigen in normal and
      malignant tissues of the digestive tract. In normal tissues, MLS128 was
      immunoreactive with the squamous epithelium of the esophagus and was weakly
      reactive with the columnar epithelia of the stomach, duodenum, colon, bile duct
      and pancreatic duct. In malignant tissues, positive immunostaining was detected
      with high frequency (75%-100%) in carcinomas of the esophagus, stomach colon,
      biliary tract and pancreas, whereas 2 of 11 (18%) hepatocellular carcinomas were 
      positive. Tn antigen was detected in the upper two-thirds of the normal squamous 
      epithelium, and was often detected in squamous cell carcinomas with cancer pearls
      (keratinization). These results suggest that the expression of Tn antigen is
      related to the differentiation of squamous epithelium, or to keratinization. In
      normal columnar epithelial cells. Tn antigen was localized mainly to the Golgi
      area. This intracellular localization was preserved in well-differentiated
      papillary adenocarcinomas of the colon, but was lost in most cases of tubular
      adenocarcinomas.
FAU - Ohshio, G
AU  - Ohshio G
AD  - Department of Surgery, Faculty of Medicine, Kyoto University, Japan.
FAU - Imamura, T
AU  - Imamura T
FAU - Imamura, M
AU  - Imamura M
FAU - Yamabe, H
AU  - Yamabe H
FAU - Sakahara, H
AU  - Sakahara H
FAU - Nakada, H
AU  - Nakada H
FAU - Yamashina, I
AU  - Yamashina I
LA  - eng
PT  - Journal Article
PL  - Germany
TA  - J Cancer Res Clin Oncol
JT  - Journal of cancer research and clinical oncology
JID - 7902060
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Tn antigen)
SB  - IM
MH  - Adenocarcinoma/chemistry/immunology
MH  - *Antibodies, Monoclonal
MH  - Antibody Specificity
MH  - Antigens, Tumor-Associated, Carbohydrate/*analysis/immunology
MH  - Carcinoma, Squamous Cell/chemistry/immunology
MH  - Digestive System/*chemistry/immunology
MH  - Digestive System Neoplasms/*chemistry/immunology/pathology
MH  - Epithelium/chemistry/immunology
MH  - Humans
MH  - Immunohistochemistry
EDAT- 1995/01/01 00:00
MHDA- 1995/01/01 00:01
CRDT- 1995/01/01 00:00
PHST- 1995/01/01 00:00 [pubmed]
PHST- 1995/01/01 00:01 [medline]
PHST- 1995/01/01 00:00 [entrez]
PST - ppublish
SO  - J Cancer Res Clin Oncol. 1995;121(4):247-52.

PMID- 8590544
OWN - NLM
STAT- MEDLINE
DCOM- 19960327
LR  - 20151119
IS  - 0278-0240 (Print)
IS  - 0278-0240 (Linking)
VI  - 12
IP  - 3
DP  - 1995 Aug
TI  - Monoclonal antibodies recognising sialyl-Tn: production and application to
      immunochemistry.
PG  - 175-86
AB  - In order to develop reagents that can detect the exposed sialyl-Tn antigen (NeuAc
      alpha 2,6GalNAc alpha 1-O-Ser/Thr) on tumour-associated mucins, we have prepared 
      monoclonal antibodies (mabs 3C2 and 3D1, both IgM) against ovine submaxillary
      mucin (OSM; > 98% of glycans as sialyl-Tn). These mabs showed strong reactivity
      with OSM and bovine submaxillary mucin (BSM; 50% of glycans as sialyl-Tn) but did
      not react with desialylated OSM or BSM. Sialic acid at 1 mg/ml did not
      significantly inhibit mab binding to OSM, suggesting that the linkage to GalNAc
      may be important for mab binding. 3C2 and 3D1 also showed similar reactivity to
      sialyl-Tn reactive mab B72.3, and detected B72.3 captured OSM in a sandwich
      ELISA. In Western blotting of mucus from a patient with a mucinous ovarian
      tumour, the mabs reacted with high molecular weight (> 200 kDa) species. In
      immunohistochemistry, these mabs showed strong reactivity with most cancers of
      the colon, lung, and stomach, and also some tumours of the ovary and breast.
      There was only limited reactivity in normal tissue from these sites. The
      antibodies should be useful reagents for the detection of the sialyl-Tn antigen
      in human cancers.
FAU - Devine, P L
AU  - Devine PL
AD  - Department of Obstetrics and Gynaecology, University of Queensland, Australia.
FAU - Birrell, G W
AU  - Birrell GW
FAU - Quin, R J
AU  - Quin RJ
FAU - Shield, P W
AU  - Shield PW
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Dis Markers
JT  - Disease markers
JID - 8604127
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Biomarkers, Tumor)
RN  - 0 (Mucins)
RN  - 0 (sialosyl-Tn antigen)
SB  - IM
MH  - Animals
MH  - Antibodies, Monoclonal/*immunology
MH  - Antibody Formation
MH  - Antigens, Tumor-Associated, Carbohydrate/*immunology
MH  - Biomarkers, Tumor
MH  - Blotting, Western
MH  - Cattle
MH  - Enzyme-Linked Immunosorbent Assay
MH  - Female
MH  - Humans
MH  - *Immunochemistry
MH  - Immunoenzyme Techniques
MH  - Mice
MH  - Mice, Inbred BALB C
MH  - Mucins/immunology
MH  - Neoplasms/immunology
MH  - Sheep
EDAT- 1995/08/01 00:00
MHDA- 1995/08/01 00:01
CRDT- 1995/08/01 00:00
PHST- 1995/08/01 00:00 [pubmed]
PHST- 1995/08/01 00:01 [medline]
PHST- 1995/08/01 00:00 [entrez]
PST - ppublish
SO  - Dis Markers. 1995 Aug;12(3):175-86.

PMID- 17537433
OWN - NLM
STAT- MEDLINE
DCOM- 20080204
LR  - 20071120
IS  - 0014-4800 (Print)
IS  - 0014-4800 (Linking)
VI  - 83
IP  - 3
DP  - 2007 Dec
TI  - Galectin-1, an endogenous lectin produced by arterial cells, binds lipoprotein(a)
      [Lp(a)] in situ: relevance to atherogenesis.
PG  - 399-404
AB  - Lipoprotein(a) [Lp(a)], a modified LDL molecule, is implicated in atherogenesis. 
      Mechanisms of the accumulation of [Lp(a)] in atherosclerotic vessels is lacking
      in literature. We sought to investigate the complementarities of the carbohydrate
      structures on Lp(a) and LDL with galectin-1(a carbohydrate binding protein) and
      whether endogenous galectin-1 binds Lp(a) in situ. We investigated T-antigen
      structures on Lp(a) and LDL by enzyme-linked lectin assay using T-antigen
      specific lectins, galectin-1 and jacalin. Both jacalin and galectin-1 bound
      strongly to Lp(a) and to a much lesser extent, to LDL. Galectin-1 recognition of 
      the lipoproteins was abolished when the O-linked sugars were selectively removed.
      Localization of endogenous galectin-1 within histological sections of human
      internal mammary artery and in vitro binding of Lp(a) to the tissues was analyzed
      by immunohistochemical staining. The Lp(a)-binding pattern was found to overlap
      with the localization of galectin-1. The poor Lp(a)-binding on inhibiting tissue 
      galectin-1 with lactose, suggested the binding of Lp(a) to galectin-1. This may
      be suggestive of a mechanism by which Lp(a) accumulates within arterial walls in 
      atherogenesis.
FAU - Chellan, Bijoy
AU  - Chellan B
AD  - Department of Biochemistry, Sree Chitra Tirunal Institute for Medical Sciences
      and Technology, Thiruvananthapuram, Kerala, 695011, India.
FAU - Narayani, Jayakumari
AU  - Narayani J
FAU - Appukuttan, Padinjaradath S
AU  - Appukuttan PS
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20070503
PL  - Netherlands
TA  - Exp Mol Pathol
JT  - Experimental and molecular pathology
JID - 0370711
RN  - 0 (Antigens, Viral, Tumor)
RN  - 0 (Galectin 1)
RN  - 0 (LGALS1 protein, human)
RN  - 0 (Lipoprotein(a))
RN  - 0 (Lipoproteins, LDL)
RN  - 0 (Plant Lectins)
RN  - 0 (jacalin)
SB  - IM
MH  - Antigens, Viral, Tumor/chemistry/metabolism
MH  - *Atherosclerosis
MH  - Galectin 1/genetics/*metabolism
MH  - Humans
MH  - Lipoprotein(a)/*metabolism
MH  - Lipoproteins, LDL/metabolism
MH  - Mammary Arteries/*cytology/metabolism
MH  - Plant Lectins/metabolism
MH  - Protein Binding
EDAT- 2007/06/01 09:00
MHDA- 2008/02/05 09:00
CRDT- 2007/06/01 09:00
PHST- 2007/02/10 00:00 [received]
PHST- 2007/04/09 00:00 [revised]
PHST- 2007/04/09 00:00 [accepted]
PHST- 2007/06/01 09:00 [pubmed]
PHST- 2008/02/05 09:00 [medline]
PHST- 2007/06/01 09:00 [entrez]
AID - S0014-4800(07)00049-4 [pii]
AID - 10.1016/j.yexmp.2007.04.004 [doi]
PST - ppublish
SO  - Exp Mol Pathol. 2007 Dec;83(3):399-404. doi: 10.1016/j.yexmp.2007.04.004. Epub
      2007 May 3.

PMID- 17457671
OWN - NLM
STAT- MEDLINE
DCOM- 20080128
LR  - 20181113
IS  - 0282-0080 (Print)
IS  - 0282-0080 (Linking)
VI  - 24
IP  - 8
DP  - 2007 Nov
TI  - The oncofetal Thomsen-Friedenreich carbohydrate antigen in cancer progression.
PG  - 411-20
AB  - The oncofetal Thomsen-Friedenreich carbohydrate antigen
      (Galbeta1-3GalNAcalpha1-Ser/Thr TF or T antigen) is a pan-carcinoma antigen
      highly expressed by about 90% of all human carcinomas. Its broad expression and
      high specificity in cancer have attracted many investigations into its potential 
      use in cancer diagnosis and immunotherapy. Over the past few years increasing
      evidence suggests that the increased TF occurrence in cancer cells may be
      functionally important in cancer progression by allowing increased
      interaction/communication of the cells with endogenous carbohydrate-binding
      proteins (lectins), particularly the members of the galactoside-binding galectin 
      family. This review focuses on the recent progress in understanding of the
      regulation and functional significance of increased TF occurrence in cancer
      progression and metastasis.
FAU - Yu, Lu-Gang
AU  - Yu LG
AD  - The Henry Wellcome Laboratory of Molecular and Cellular Gastroenterology, School 
      of Clinical Science, University of Liverpool, Liverpool, L69 3BX, UK.
      lgyu@liverpool.ac.uk
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Review
DEP - 20070425
PL  - United States
TA  - Glycoconj J
JT  - Glycoconjugate journal
JID - 8603310
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (MUC1 protein, human)
RN  - 0 (Mucin-1)
RN  - 3554-90-3 (Thomsen-Friedenreich antigen)
SB  - IM
MH  - Antigens, Tumor-Associated, Carbohydrate/*metabolism
MH  - Cell Adhesion
MH  - Cell Proliferation
MH  - Disease Progression
MH  - Endothelium/metabolism
MH  - Humans
MH  - Mucin-1/metabolism
MH  - Neoplasm Metastasis
MH  - *Neoplasms/metabolism/pathology
MH  - Neovascularization, Pathologic
RF  - 118
EDAT- 2007/04/26 09:00
MHDA- 2008/01/29 09:00
CRDT- 2007/04/26 09:00
PHST- 2006/11/13 00:00 [received]
PHST- 2007/03/23 00:00 [accepted]
PHST- 2007/03/22 00:00 [revised]
PHST- 2007/04/26 09:00 [pubmed]
PHST- 2008/01/29 09:00 [medline]
PHST- 2007/04/26 09:00 [entrez]
AID - 10.1007/s10719-007-9034-3 [doi]
PST - ppublish
SO  - Glycoconj J. 2007 Nov;24(8):411-20. doi: 10.1007/s10719-007-9034-3. Epub 2007 Apr
      25.

PMID- 1736686
OWN - NLM
STAT- MEDLINE
DCOM- 19920310
LR  - 20181113
IS  - 0340-2061 (Print)
IS  - 0340-2061 (Linking)
VI  - 185
IP  - 1
DP  - 1992
TI  - Normal colon of Sprague-Dawley rats. An immunohistochemical study.
PG  - 69-76
AB  - The patterns of expression of the human-tumor-associated antigens, CO17-1A,
      GA73-3, BR55-2, GICA19-9, CA50 and carcino-embryonic antigen (CEA) were studied
      in the normal colonic mucosa (the last three also in the serum) of Sprague-Dawley
      rats. Four immunohistochemically different segments were identified: caecum,
      ascending colon, transverse colon and descending colon. The immunohistochemical
      reactions of the cells at the lower part of the crypt were essential for the
      distinction of the four segments. In the caecum, the MAbs 17-1A, 73-3 and 19-9
      stained the glycocalyx of the cells of the lower part of the crypts and the Golgi
      apparatus of the intercalated cells (IC). MAb55-2 stained very weakly the
      goblet-like cells (GLC) of the lower part of the crypt of transverse colon, in
      addition to a nearly complete lack of reaction in the upper part of the crypts.
      In the ascending colon, the lower part of the crypts showed a characteristic
      diffuse staining of the intercalated cells with MAb55-2. The perinuclear and
      mucosal staining observed in the GLC of the transverse colon with MAbs 17-1A,
      73-3 and 19-9 as against the supranuclear and Golgi zone staining observed in the
      GLC/goblet cells (GC)/columnar cells (CC) of the lower part of crypts of the
      descending colon with the same MAbs, distinguished the former segment from the
      latter. The IC demonstrated by immunohistochemistry in the lower parts of the
      crypts of caecum and ascending colon appear to correspond to the replicating
      cells of the colonic crypts.
FAU - Shetye, J D
AU  - Shetye JD
AD  - Department of Pathology, Karolinska Hospital, Stockholm, Sweden.
FAU - Rubio, C A
AU  - Rubio CA
FAU - Mellstedt, H T
AU  - Mellstedt HT
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - Germany
TA  - Anat Embryol (Berl)
JT  - Anatomy and embryology
JID - 7505194
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens, Neoplasm)
SB  - IM
MH  - Animals
MH  - Antibodies, Monoclonal
MH  - Antigens, Neoplasm/*analysis
MH  - Cecum/immunology
MH  - Colon/anatomy & histology/*immunology
MH  - Immunoenzyme Techniques
MH  - Intestinal Mucosa/*immunology
MH  - Male
MH  - Rats
MH  - Rats, Inbred Strains
EDAT- 1992/01/01 00:00
MHDA- 1992/01/01 00:01
CRDT- 1992/01/01 00:00
PHST- 1992/01/01 00:00 [pubmed]
PHST- 1992/01/01 00:01 [medline]
PHST- 1992/01/01 00:00 [entrez]
PST - ppublish
SO  - Anat Embryol (Berl). 1992;185(1):69-76.

PMID- 2665633
OWN - NLM
STAT- MEDLINE
DCOM- 19890816
LR  - 20081121
IS  - 0250-7005 (Print)
IS  - 0250-7005 (Linking)
VI  - 9
IP  - 2
DP  - 1989 Mar-Apr
TI  - Immunohistochemical detection of human lung and gastric cancer antigen in human
      salivary gland tumors.
PG  - 327-39
AB  - Immunohistochemical identification of human lung and gastric carcinoma antigen
      detected with monoclonal antibodies (MoAbs) KM-93 and KM-231 respectively, was
      described in 83 salivary gland tumors, including 67 pleomorphic adenomas, 5
      adenolymphomas, 3 mucoepidermoid tumors, 6 sialadenocarcinomas, and 2 adenoid
      cystic carcinomas as well as in normal salivary glands. The binding patterns of
      these two MoAbs was compared with that of MoAb recognizing epithelial membrane
      antigen (EMA). Serous cells of normal salivary glands showed positive KM-93
      staining, whereas ductal cells were positive with KM-231, with ductal basal cells
      being characteristically so. EMA staining was confined to luminal and lateral
      borders of serous acini and ducts. Pleomorphic adenomas indicated positive
      depositions for both KM-93 and KM-231 in luminal tumor cells or luminal borders
      of tubuloductal structures. Adenolymphomas showed positive KM-231 staining in
      basal tumor cells and a positive KM-93 reaction in luminal tumor cells.
      Mucoepidermoid tumors revealed positive KM-231 staining in mucous-secreting
      cells, whereas weak KM-93 staining was found in all tumor cells.
      Sialoadenocarcinomas exhibited varying degrees of positive staining with KM-93
      and KM-231 in their neoplastic cells. Adenoid cystic carcinomas showed luminal
      staining with KM-93 and KM-231 to their neoplastic cells. Adenoid cystic
      carcinomas showed luminal staining with KM-93 and MoAb EMA. The histogenesis of
      these salivary gland tumors is discussed in terms of the immunohistochemical
      features of staining patterns obtained with MoAbs KM-93 and KM-231.
FAU - Tsuzi, T
AU  - Tsuzi T
AD  - Department of Oral and Maxillofacial Surgery, Yamaguchi University School of
      Medicine, Japan.
FAU - Shinozaki, F
AU  - Shinozaki F
FAU - Yamada, K
AU  - Yamada K
FAU - Mori, M
AU  - Mori M
LA  - eng
PT  - Journal Article
PL  - Greece
TA  - Anticancer Res
JT  - Anticancer research
JID - 8102988
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens, Neoplasm)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Mucin-1)
SB  - IM
MH  - Adenocarcinoma/*immunology
MH  - Adenoma/*immunology
MH  - Antibodies, Monoclonal/immunology
MH  - Antigens, Neoplasm/*analysis
MH  - Carcinoma/*immunology
MH  - Humans
MH  - Immunoenzyme Techniques
MH  - Lung Neoplasms/*immunology
MH  - Membrane Glycoproteins/immunology
MH  - Mucin-1
MH  - Salivary Gland Neoplasms/*immunology
MH  - Stomach Neoplasms/*immunology
EDAT- 1989/03/01 00:00
MHDA- 1989/03/01 00:01
CRDT- 1989/03/01 00:00
PHST- 1989/03/01 00:00 [pubmed]
PHST- 1989/03/01 00:01 [medline]
PHST- 1989/03/01 00:00 [entrez]
PST - ppublish
SO  - Anticancer Res. 1989 Mar-Apr;9(2):327-39.

PMID- 19815850
OWN - NLM
STAT- MEDLINE
DCOM- 20100304
LR  - 20151119
IS  - 1460-2423 (Electronic)
IS  - 0959-6658 (Linking)
VI  - 20
IP  - 2
DP  - 2010 Feb
TI  - MUC2 mucin is a major carrier of the cancer-associated sialyl-Tn antigen in
      intestinal metaplasia and gastric carcinomas.
PG  - 199-206
LID - 10.1093/glycob/cwp161 [doi]
AB  - Changes in mucin protein expression and in glycosylation are common features in
      pre-neoplastic lesions and cancer and are therefore used as cancer-associated
      markers. De novo expression of intestinal mucin MUC2 and cancer-associated
      sialyl-Tn antigen are frequently observed in intestinal metaplasia (IM) and
      gastric cancer. However, despite that these antigens often co-localize, MUC2 has 
      not been demonstrated to be a carrier of sialyl-Tn. By using the in situ
      proximity ligation assay (in situ PLA), we herein could show that MUC2 is a major
      carrier of the sialyl-Tn antigen in all IM cases and in most gastric carcinoma
      cases. The requirement by in situ PLA for the presence of both antigens in close 
      proximity increases the selectivity compared to measurement of co-localization,
      as determined by immunohistochemistry. Identification of the mucin which is the
      carrier of a carbohydrate structure offers unique advantages for future
      development of more accurate diagnostic and prognostic markers.
FAU - Conze, Tim
AU  - Conze T
AD  - Department of Genetics and Pathology, University of Uppsala, Uppsala, Sweden.
FAU - Carvalho, Ana Sofia
AU  - Carvalho AS
FAU - Landegren, Ulf
AU  - Landegren U
FAU - Almeida, Raquel
AU  - Almeida R
FAU - Reis, Celso A
AU  - Reis CA
FAU - David, Leonor
AU  - David L
FAU - Soderberg, Ola
AU  - Soderberg O
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20091008
PL  - England
TA  - Glycobiology
JT  - Glycobiology
JID - 9104124
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens, Neoplasm)
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Biomarkers, Tumor)
RN  - 0 (MUC2 protein, human)
RN  - 0 (Mucin-2)
RN  - 0 (sialosyl-Tn antigen)
SB  - IM
MH  - Antibodies, Monoclonal/immunology
MH  - Antigens, Neoplasm/biosynthesis/chemistry/*immunology
MH  - Antigens, Tumor-Associated, Carbohydrate/biosynthesis/chemistry/*immunology
MH  - Biomarkers, Tumor/biosynthesis/chemistry/*immunology
MH  - Humans
MH  - Immunohistochemistry
MH  - Intestines/*immunology/pathology
MH  - Metaplasia/*immunology/surgery
MH  - Mucin-2/biosynthesis/chemistry/*immunology
MH  - Stomach Neoplasms/*immunology/surgery
EDAT- 2009/10/10 06:00
MHDA- 2010/03/05 06:00
CRDT- 2009/10/10 06:00
PHST- 2009/10/10 06:00 [entrez]
PHST- 2009/10/10 06:00 [pubmed]
PHST- 2010/03/05 06:00 [medline]
AID - cwp161 [pii]
AID - 10.1093/glycob/cwp161 [doi]
PST - ppublish
SO  - Glycobiology. 2010 Feb;20(2):199-206. doi: 10.1093/glycob/cwp161. Epub 2009 Oct
      8.

PMID- 7767313
OWN - NLM
STAT- MEDLINE
DCOM- 19950706
LR  - 20161123
IS  - 0969-8051 (Print)
IS  - 0969-8051 (Linking)
VI  - 22
IP  - 2
DP  - 1995 Feb
TI  - Radioimmunoimaging of colon cancer xenografts with anti-Tn monoclonal antibody.
PG  - 199-203
AB  - Tn antigen is a glycosylated tumor associated antigen and a murine monoclonal
      antibody, MLS128, has been identified to react with it. The potential of MLS128
      for the radioimmunoimaging of colorectal cancer was studied. MLS128 was labeled
      with radioiodine by the chloramine-T method or indium-111 (111In) by using
      isothiocyanatobenzyl EDTA, and was injected into nude mice bearing human colon
      cancer xenografts. Radiolabeled MLS128 showed a high and specific localization in
      xenografted tumor. At 48 h after injection, the %ID/g of 125I-labeled MLS128 in
      the tumor was 34.69, whereas that of isotype matched control antibody, FLOPC21,
      was 5.58 and the tumor-to-nontumor radioactivity ratios of 125I-labeled MLS128
      reached to 4.56, 17.84 and 23.62 for the blood, liver and bone, respectively.
      111In-labeled MLS128 showed similar results. High accumulation of MLS128 in
      xenografted tumors suggested that the monoclonal antibody MLS128 is promising for
      radioimmunoimaging of colorectal cancer.
FAU - Yao, Z
AU  - Yao Z
AD  - Department of Nuclear Medicine, Faculty of Medicine, Kyoto University, Japan.
FAU - Sakahara, H
AU  - Sakahara H
FAU - Zhang, M
AU  - Zhang M
FAU - Kobayashi, H
AU  - Kobayashi H
FAU - Nakada, H
AU  - Nakada H
FAU - Yamashina, I
AU  - Yamashina I
FAU - Konishi, J
AU  - Konishi J
LA  - eng
PT  - Comparative Study
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Nucl Med Biol
JT  - Nuclear medicine and biology
JID - 9304420
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Iodine Radioisotopes)
RN  - 0 (Tn antigen)
SB  - IM
MH  - Animals
MH  - Antibodies, Monoclonal/pharmacokinetics
MH  - Antigens, Tumor-Associated, Carbohydrate/immunology
MH  - Cell Line
MH  - Colonic Neoplasms/*diagnostic imaging
MH  - Humans
MH  - Iodine Radioisotopes/pharmacokinetics
MH  - Mice/immunology
MH  - Mice, Nude
MH  - Radioimmunodetection/*methods
MH  - Radionuclide Imaging/methods
MH  - Time Factors
MH  - Tissue Distribution
MH  - Transplantation, Heterologous
MH  - Tumor Cells, Cultured
EDAT- 1995/02/01 00:00
MHDA- 1995/02/01 00:01
CRDT- 1995/02/01 00:00
PHST- 1995/02/01 00:00 [pubmed]
PHST- 1995/02/01 00:01 [medline]
PHST- 1995/02/01 00:00 [entrez]
AID - 096980519400092X [pii]
PST - ppublish
SO  - Nucl Med Biol. 1995 Feb;22(2):199-203.

PMID- 2665636
OWN - NLM
STAT- MEDLINE
DCOM- 19890816
LR  - 20061115
IS  - 0250-7005 (Print)
IS  - 0250-7005 (Linking)
VI  - 9
IP  - 2
DP  - 1989 Mar-Apr
TI  - The tumor-associated antigens BR55-2, GA73-3 and GICA 19-9 in normal and
      corresponding neoplastic human tissues, especially gastrointestinal tissues.
PG  - 395-404
AB  - Immunohistochemical analysis with a monoclonal antibody, anti-BR55-2, was carried
      out on 163 tumors with their adjacent normal tissues and on 51 normal tissues
      from various organs by the ABC method. The expression of the antigen BR55-2 was
      compared with the expression of the colorectal carcinoma (CRC) associated
      antigens, GA73-3 and GICA19-9. BR55-2 was expressed in most normal epithelial
      tissues, whereas in the colon it seems to be exclusively a tumor-associated
      antigen. MAb55-2 might be of value in studying dysplastic lesions of the colon
      and in assessing the depth of invasion of CRC. In CRC, the expression of BR55-2
      was complementary to that of GA73-3. MAb55-2 may therefore be of value in
      immunotherapy of CRC.
FAU - Shetye, J
AU  - Shetye J
AD  - Department of Pathology, Karolinska Hospital, Stockholm, Sweden.
FAU - Christensson, B
AU  - Christensson B
FAU - Rubio, C
AU  - Rubio C
FAU - Rodensjo, M
AU  - Rodensjo M
FAU - Biberfeld, P
AU  - Biberfeld P
FAU - Mellstedt, H
AU  - Mellstedt H
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - Greece
TA  - Anticancer Res
JT  - Anticancer research
JID - 8102988
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens, Neoplasm)
RN  - 0 (Antigens, Surface)
RN  - 0 (Lewis Blood-Group System)
SB  - IM
MH  - Antibodies, Monoclonal/immunology
MH  - Antigens, Neoplasm/*analysis
MH  - Antigens, Surface/analysis
MH  - Cell Differentiation
MH  - Digestive System/*immunology
MH  - Gastrointestinal Neoplasms/*immunology/pathology
MH  - Humans
MH  - Immunoenzyme Techniques
MH  - Lewis Blood-Group System/immunology
EDAT- 1989/03/01 00:00
MHDA- 1989/03/01 00:01
CRDT- 1989/03/01 00:00
PHST- 1989/03/01 00:00 [pubmed]
PHST- 1989/03/01 00:01 [medline]
PHST- 1989/03/01 00:00 [entrez]
PST - ppublish
SO  - Anticancer Res. 1989 Mar-Apr;9(2):395-404.

PMID- 8330904
OWN - NLM
STAT- MEDLINE
DCOM- 19930819
LR  - 20131121
IS  - 0171-2985 (Print)
IS  - 0171-2985 (Linking)
VI  - 187
IP  - 3-5
DP  - 1993 Apr
TI  - Lipo-oligosaccharides (LOS) of mucosal pathogens: molecular mimicry and
      host-modification of LOS.
PG  - 382-402
AB  - Immunochemical studies of the lipo-oligosaccharides (LOS) of the Gram-negative
      bacteria Neisseria gonorrhoeae and Neisseria meningitidis have revealed some
      interesting structural characteristics of these LOS that might relate to their
      roles during pathogenesis. The carbohydrate moieties of the LOS of pathogenic
      Neisseria mimic carbohydrates present in glycosphingolipids of human cells.
      Firstly, an LOS component present among a number of Neisseria species is
      antigenically and/or chemically identical to lactoneoseries glycosphingolipids
      present in human cells. The lactoneoseries LOS becomes sialylated on Neisseria
      gonorrhoeae when they are grown in the presence of cytidine
      5'-monophospho-N-acetyl-neuraminic acid (CMP-NANA), the nucleotide sugar for
      sialic acid. Examination of gonococci present in exudates from males with natural
      infection indicates that sialylation also occurs in vivo. The mechanism for this 
      process apparently involves a bacterial sialyltransferase scavenging available
      host CMP-NANA ("host-modification" of LOS) and transferring the sialic acid to
      the lactoneoserieslike LOS. Strains of N. meningitidis and Haemophilus influenzae
      also express similarly sialylated LOS suggesting that this is a common mechanism 
      of pathogenesis among these bacteria. Additional examples of LOS that mimic other
      glycosphingolipid series have been identified also and the fact that multiple
      series can be expressed in a single population of gonococci suggests that a
      diverse set of LOS can be presented to the host during infection. It is possible 
      that this diverse set of LOS serve different functions for the bacteria in
      various hosts and/or environments during infection.
FAU - Mandrell, R E
AU  - Mandrell RE
AD  - Division of Infectious Diseases, San Francisco General Hospital, University of
      California.
FAU - Apicella, M A
AU  - Apicella MA
LA  - eng
GR  - AI18384/AI/NIAID NIH HHS/United States
GR  - AI21620/AI/NIAID NIH HHS/United States
GR  - AI24616/AI/NIAID NIH HHS/United States
GR  - etc.
PT  - Journal Article
PT  - Research Support, U.S. Gov't, P.H.S.
PT  - Review
PL  - Netherlands
TA  - Immunobiology
JT  - Immunobiology
JID - 8002742
RN  - 0 (Antigens, Bacterial)
RN  - 0 (Glycosphingolipids)
RN  - 0 (Lipopolysaccharides)
RN  - 0 (Sialic Acids)
RN  - 0 (lipid-linked oligosaccharides)
RN  - 3063-71-6 (Cytidine Monophosphate N-Acetylneuraminic Acid)
RN  - GZP2782OP0 (N-Acetylneuraminic Acid)
SB  - IM
MH  - Antigens, Bacterial/immunology
MH  - Carbohydrate Sequence
MH  - Cytidine Monophosphate N-Acetylneuraminic Acid
MH  - Glycosphingolipids/chemistry
MH  - Gram-Negative Bacteria/*chemistry/pathogenicity/physiology
MH  - Gram-Negative Bacterial Infections/microbiology
MH  - Humans
MH  - Lipopolysaccharides/*chemistry/*immunology
MH  - Male
MH  - Molecular Sequence Data
MH  - Mucous Membrane/microbiology
MH  - N-Acetylneuraminic Acid
MH  - Neutrophils/immunology
MH  - Phagocytosis/immunology
MH  - Sialic Acids/chemistry
RF  - 93
EDAT- 1993/04/01 00:00
MHDA- 1993/04/01 00:01
CRDT- 1993/04/01 00:00
PHST- 1993/04/01 00:00 [pubmed]
PHST- 1993/04/01 00:01 [medline]
PHST- 1993/04/01 00:00 [entrez]
AID - S0171-2985(11)80352-9 [pii]
AID - 10.1016/S0171-2985(11)80352-9 [doi]
PST - ppublish
SO  - Immunobiology. 1993 Apr;187(3-5):382-402. doi: 10.1016/S0171-2985(11)80352-9.

PMID- 15862866
OWN - NLM
STAT- MEDLINE
DCOM- 20050825
LR  - 20131121
IS  - 0141-8130 (Print)
IS  - 0141-8130 (Linking)
VI  - 35
IP  - 5
DP  - 2005 Jun
TI  - IgA1 is the premier serum glycoprotein recognized by human galectin-1 since T
      antigen (Galbeta1-->3GalNAc-) is far superior to non-repeating N-acetyl
      lactosamine as ligand.
PG  - 269-76
AB  - Human heart galectin-1 (HHL) was separated by high pressure liquid chromatography
      from endogenous glycoproteins co-purified with it during affinity chromatography.
      These glycoproteins offered excellent ligands for HHL binding and were rich in T 
      antigen (Galbeta1-->3 GalNAc-) of O-linked oligosaccharides. In enzyme linked
      lectin assay and hemagglutination inhibition assay, human IgA1, bovine fetuin and
      other O-glycosylated T antigen-bearing glycoproteins bound to the lectin
      efficiently in contrast to single N-acetyl lactosamine (LacNAc)-bearing N-linked 
      oligosaccharides released from them and to IgG which is not O-glycosylated. HHL
      binding to IgA1 and fetuin was unaffected by removal of their N-linked
      oligosaccharides by alpha-mannosidase. When immobilized, O-glycosylated serum
      proteins but not IgG could capture HHL from its solutions. Desialylated or
      polymeric IgA1 was better inhibitor than monomeric IgA1. The findings suggest a
      possible role for galectin-1 in anchoring of microbial and cancer cells known to 
      be rich in T antigen, in high serum IgA1 turn over and in tissue sequestering of 
      IgA1 immune complexes especially after their microbial desialylation in IgA
      nephropathy and other immune complex-mediated disorders.
FAU - Sangeetha, S R
AU  - Sangeetha SR
AD  - Division of Biochemistry, Sree Chitra Tirunal Institute for Medical Sciences and 
      Technology, Thiruvananthapuram 695011, India.
FAU - Appukuttan, P S
AU  - Appukuttan PS
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20050425
PL  - Netherlands
TA  - Int J Biol Macromol
JT  - International journal of biological macromolecules
JID - 7909578
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Asialoglycoproteins)
RN  - 0 (Galectin 1)
RN  - 0 (Immunoglobulin A)
RN  - 0 (Ligands)
RN  - 0 (Oligosaccharides)
RN  - 0 (Plant Lectins)
RN  - 0 (asialo-galactosyl-acetylgalactosamine)
RN  - 0 (jacalin)
RN  - 3554-90-3 (Thomsen-Friedenreich antigen)
RN  - EC 3.2.1.18 (Neuraminidase)
RN  - EC 3.2.1.24 (alpha-Mannosidase)
RN  - KM15WK8O5T (Acetylgalactosamine)
SB  - IM
MH  - Acetylgalactosamine/analogs & derivatives/metabolism
MH  - Antigens, Tumor-Associated, Carbohydrate/immunology/*metabolism
MH  - Asialoglycoproteins/metabolism
MH  - Chromatography, Affinity
MH  - Chromatography, High Pressure Liquid
MH  - Electrophoresis, Polyacrylamide Gel
MH  - Galectin 1/chemistry/immunology/isolation & purification/*metabolism
MH  - Humans
MH  - Immunoglobulin A/immunology/*metabolism
MH  - Ligands
MH  - Neuraminidase/metabolism
MH  - Oligosaccharides/metabolism
MH  - Plant Lectins/metabolism
MH  - alpha-Mannosidase/metabolism
EDAT- 2005/05/03 09:00
MHDA- 2005/08/27 09:00
CRDT- 2005/05/03 09:00
PHST- 2004/07/22 00:00 [received]
PHST- 2005/02/26 00:00 [revised]
PHST- 2005/03/04 00:00 [accepted]
PHST- 2005/05/03 09:00 [pubmed]
PHST- 2005/08/27 09:00 [medline]
PHST- 2005/05/03 09:00 [entrez]
AID - S0141-8130(05)00053-X [pii]
AID - 10.1016/j.ijbiomac.2005.03.004 [doi]
PST - ppublish
SO  - Int J Biol Macromol. 2005 Jun;35(5):269-76. doi: 10.1016/j.ijbiomac.2005.03.004. 
      Epub 2005 Apr 25.

PMID- 7685064
OWN - NLM
STAT- MEDLINE
DCOM- 19930708
LR  - 20061115
IS  - 0148-639X (Print)
IS  - 0148-639X (Linking)
VI  - 16
IP  - 7
DP  - 1993 Jul
TI  - Localization of GM1 and GD1b antigens in the human peripheral nervous system.
PG  - 752-6
AB  - Serum antibodies against ganglioside GM1 and/or GD1b are frequently detected in
      autoimmune neuropathies such as multifocal motor neuropathy, IgM paraproteinemic 
      neuropathy and Guillain-Barre syndrome. Some of them bind to GM1 or GD1b
      monospecifically but others cross-react with both of the antigens. In order to
      investigate the respective localizations of GM1 and GD1b antigens in the human
      peripheral nervous system, an immunohistochemical study was performed using two
      mouse monoclonal antibodies, each monospecific to GM1 and GD1b. GGR12,
      monospecific to GD1b, bound to neurons in dorsal root ganglia and sympathetic
      ganglia, and some parts of the peripheral myelin, mainly the paranodal areas.
      However GMB16, monospecific to GM1, did not bind to either neurons or myelin.
      GD1b antigen present on neurons and paranodal myelin in the peripheral nervous
      system can be a target antigen of serum antibodies in autoimmune neuropathies.
      Further effort should be made to reveal the localization of GM1 antigen in the
      human peripheral nervous system.
FAU - Kusunoki, S
AU  - Kusunoki S
AD  - Department of Neurology, Faculty of Medicine, University of Tokyo, Japan.
FAU - Chiba, A
AU  - Chiba A
FAU - Tai, T
AU  - Tai T
FAU - Kanazawa, I
AU  - Kanazawa I
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Muscle Nerve
JT  - Muscle & nerve
JID - 7803146
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens)
RN  - 0 (Epitopes)
RN  - 0 (Gangliosides)
RN  - 37758-47-7 (G(M1) Ganglioside)
SB  - IM
MH  - Antibodies, Monoclonal
MH  - Antigens/*analysis
MH  - Epitopes
MH  - G(M1) Ganglioside/*analysis
MH  - Ganglia/*immunology
MH  - Gangliosides/*analysis
MH  - Humans
MH  - Peripheral Nerves/*immunology
EDAT- 1993/07/01 00:00
MHDA- 1993/07/01 00:01
CRDT- 1993/07/01 00:00
PHST- 1993/07/01 00:00 [pubmed]
PHST- 1993/07/01 00:01 [medline]
PHST- 1993/07/01 00:00 [entrez]
AID - 10.1002/mus.880160710 [doi]
PST - ppublish
SO  - Muscle Nerve. 1993 Jul;16(7):752-6. doi: 10.1002/mus.880160710.

PMID- 21057010
OWN - NLM
STAT- MEDLINE
DCOM- 20110127
LR  - 20181113
IS  - 1098-5530 (Electronic)
IS  - 0021-9193 (Linking)
VI  - 193
IP  - 2
DP  - 2011 Jan
TI  - Biochemical characterization of UDP-Gal:GlcNAc-pyrophosphate-lipid
      beta-1,4-Galactosyltransferase WfeD, a new enzyme from Shigella boydii type 14
      that catalyzes the second step in O-antigen repeating-unit synthesis.
PG  - 449-59
LID - 10.1128/JB.00737-10 [doi]
AB  - The O antigen is the outer part of the lipopolysaccharide (LPS) in the outer
      membrane of Gram-negative bacteria and contains many repeats of an
      oligosaccharide unit. It contributes to antigenic variability and is essential to
      the full function and virulence of bacteria. Shigella is a Gram-negative human
      pathogen that causes diarrhea in humans. The O antigen of Shigella boydii type 14
      consists of repeating oligosaccharide units with the structure
      [-->6-d-Galpalpha1-->4-d-GlcpAbeta1-->6-d-Galpbeta1-->4-d-Galpbeta1-->4-d-GlcpNAc
      beta1-->]n. The wfeD gene in the O-antigen gene cluster of Shigella boydii type
      14 was proposed to encode a galactosyltransferase (GalT) involved in O-antigen
      synthesis. We confirmed here that the wfeD gene product is a beta4-GalT that
      synthesizes the Galbeta1-4GlcNAcalpha-R linkage. WfeD was expressed in
      Escherichia coli, and the activity was characterized by using UDP-[(3)H]Gal as
      the donor substrate as well as the synthetic acceptor substrate
      GlcNAcalpha-pyrophosphate-(CH(2))(1)(1)-O-phenyl. The enzyme product was analyzed
      by liquid chromatography-mass spectrometry (LC-MS), high-performance liquid
      chromatography (HPLC), nuclear magnetic resonance (NMR), and galactosidase
      digestion. The enzyme was shown to be specific for the UDP-Gal donor substrate
      and required pyrophosphate in the acceptor substrate. Divalent metal ions such as
      Mn(2)(+), Ni(2)(+), and, surprisingly, also Pb(2)(+) enhanced the enzyme
      activity. Mutational analysis showed that the Glu101 residue within a DxD motif
      is essential for activity, possibly by forming the catalytic nucleophile. The
      Lys211 residue was also shown to be required for activity and may be involved in 
      the binding of the negatively charged acceptor substrate. Our study revealed that
      the beta4-GalT WfeD is a novel enzyme that has virtually no sequence similarity
      to mammalian beta4-GalT, although it catalyzes a similar reaction.
FAU - Xu, Changchang
AU  - Xu C
AD  - Department of Medicine, Queen's University, Kingston, Ontario, Canada.
FAU - Liu, Bin
AU  - Liu B
FAU - Hu, Bo
AU  - Hu B
FAU - Han, Yanfang
AU  - Han Y
FAU - Feng, Lu
AU  - Feng L
FAU - Allingham, John S
AU  - Allingham JS
FAU - Szarek, Walter A
AU  - Szarek WA
FAU - Wang, Lei
AU  - Wang L
FAU - Brockhausen, Inka
AU  - Brockhausen I
LA  - eng
GR  - R01 AA020703/AA/NIAAA NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20101105
PL  - United States
TA  - J Bacteriol
JT  - Journal of bacteriology
JID - 2985120R
RN  - 0 (Cations, Divalent)
RN  - 0 (Enzyme Activators)
RN  - 0 (Metals)
RN  - 0 (O Antigens)
RN  - 0 (Recombinant Proteins)
RN  - 2956-16-3 (Uridine Diphosphate Galactose)
RN  - EC 2.4.1.- (Galactosyltransferases)
RN  - EC 3.2.1.- (Galactosidases)
SB  - IM
MH  - Cations, Divalent/metabolism
MH  - Chromatography, Liquid
MH  - DNA Mutational Analysis
MH  - Enzyme Activators/metabolism
MH  - Escherichia coli/genetics/metabolism
MH  - Galactosidases/metabolism
MH  - Galactosyltransferases/*metabolism
MH  - Gene Expression
MH  - Magnetic Resonance Spectroscopy
MH  - Metals/metabolism
MH  - O Antigens/*metabolism
MH  - Recombinant Proteins/genetics/metabolism
MH  - Shigella boydii/*enzymology
MH  - Substrate Specificity
MH  - Uridine Diphosphate Galactose/metabolism
PMC - PMC3019819
EDAT- 2010/11/09 06:00
MHDA- 2011/01/29 06:00
CRDT- 2010/11/09 06:00
PHST- 2010/11/09 06:00 [entrez]
PHST- 2010/11/09 06:00 [pubmed]
PHST- 2011/01/29 06:00 [medline]
AID - JB.00737-10 [pii]
AID - 10.1128/JB.00737-10 [doi]
PST - ppublish
SO  - J Bacteriol. 2011 Jan;193(2):449-59. doi: 10.1128/JB.00737-10. Epub 2010 Nov 5.

PMID- 10728707
OWN - NLM
STAT- MEDLINE
DCOM- 20000411
LR  - 20181130
IS  - 0008-5472 (Print)
IS  - 0008-5472 (Linking)
VI  - 60
IP  - 5
DP  - 2000 Mar 1
TI  - Expression of sialyl 6-sulfo Lewis X is inversely correlated with conventional
      sialyl Lewis X expression in human colorectal cancer.
PG  - 1410-6
AB  - Sialyl 6-sulfo Lewis X determinant has been described recently as a major ligand 
      for L-selectin on high endothelial venules of human peripheral lymph nodes. From 
      our investigation of its distribution in human colorectal cancer tissues and
      cultured colon cancer cells, the sialyl 6-sulfo Lewis X determinant was
      preferentially expressed in the nonmalignant colonic epithelia rather than cancer
      cells (P < 0.001; n = 23). This was in contrast to the distribution of
      conventional sialyl Lewis X, which was preferentially expressed in cancer tissues
      rather than nonmalignant epithelia (P = 0.007; n = 23), indicating that
      6-sulfation predominantly occurs in nonmalignant tissues and is suppressed upon
      malignant transformation. In confirmation of this, a nonsialylated determinant
      6-sulfo Lewis X was also found to be preferentially localized in the nonmalignant
      epithelia. Significant expression of sialyl 6-sulfo Lewis X was observed in only 
      2 lines, whereas 8 were positive for conventional sialyl Lewis X, among 13
      cultured colon cancer cell lines. Transfection of cells with fucosyltransferase
      (Fuc-T) VI induced expression of sialyl 6-sulfo Lewis X, whereas transfection of 
      Fuc-T III did not, suggesting that the determinant was synthesized mainly by
      Fuc-T VI in colonic epithelia. Members of the sialic acid cyclase pathway, the
      de-N-acetyl sialyl 6-sulfo Lewis X and cyclic sialyl 6-sulfo Lewis X
      determinants, were also preferentially expressed in the nonmalignant epithelia
      rather than colonic cancer cells (P < 0.001; n = 23). Stimulation of the sialyl
      6-sulfo Lewis X-positive colon cancer cell line with a calcium ionophore
      ionomycin markedly reduced sialyl 6-sulfo Lewis X and induced cyclic sialyl
      6-sulfo Lewis X expression. These results suggested that the metabolic conversion
      of sialyl 6-sulfo Lewis X into cyclic sialyl 6-sulfo Lewis X by a
      calcium-dependent enzyme, sialic acid cyclase, as we hypothesized for human
      leukocytes previously (C. Mitsuoka et al., Proc. Natl. Acad. Sci. USA, 96:
      1597-1602, 1999), also occurs in nonmalignant colonic epithelia.
FAU - Izawa, M
AU  - Izawa M
AD  - Program of Experimental Pathology, Aichi Cancer Center, Nagoya, Japan.
FAU - Kumamoto, K
AU  - Kumamoto K
FAU - Mitsuoka, C
AU  - Mitsuoka C
FAU - Kanamori, C
AU  - Kanamori C
FAU - Kanamori, A
AU  - Kanamori A
FAU - Ohmori, K
AU  - Ohmori K
FAU - Ishida, H
AU  - Ishida H
FAU - Nakamura, S
AU  - Nakamura S
FAU - Kurata-Miura, K
AU  - Kurata-Miura K
FAU - Sasaki, K
AU  - Sasaki K
FAU - Nishi, T
AU  - Nishi T
FAU - Kannagi, R
AU  - Kannagi R
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Cancer Res
JT  - Cancer research
JID - 2984705R
RN  - 0
      (5-acetylneuraminyl-(2-3)-galactosyl-(1-4)-(fucopyranosyl-(1-3))-N-acetylglucosam
      ine)
RN  - 0 (6'-sulfated sialyl Lewis x)
RN  - 0 (Lewis X Antigen)
RN  - 0 (Ligands)
RN  - 0 (Oligosaccharides)
SB  - IM
MH  - Colorectal Neoplasms/*metabolism
MH  - Humans
MH  - Immunohistochemistry
MH  - Lewis X Antigen/*biosynthesis
MH  - Ligands
MH  - Oligosaccharides/*biosynthesis
EDAT- 2000/03/23 09:00
MHDA- 2000/04/15 09:00
CRDT- 2000/03/23 09:00
PHST- 2000/03/23 09:00 [pubmed]
PHST- 2000/04/15 09:00 [medline]
PHST- 2000/03/23 09:00 [entrez]
PST - ppublish
SO  - Cancer Res. 2000 Mar 1;60(5):1410-6.

PMID- 18667431
OWN - NLM
STAT- MEDLINE
DCOM- 20081104
LR  - 20111117
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 283
IP  - 40
DP  - 2008 Oct 3
TI  - Chondroitin 4-O-sulfotransferase-1 modulates Wnt-3a signaling through control of 
      E disaccharide expression of chondroitin sulfate.
PG  - 27333-43
LID - 10.1074/jbc.M802997200 [doi]
AB  - Wnt-3a is a ligand that activates the beta-catenin-dependent pathway in Wnt
      signaling, which is implicated in numerous physiological events such as
      morphogenesis. So far, heparan sulfate (HS) proteoglycans have been highlighted
      as a low affinity receptor for morphogens containing Wnts. Here we show the
      importance of chondroitin sulfate (CS) proteoglycans in the efficient signaling
      of Wnt-3a and the structural features of CS required for the regulation of Wnt-3a
      signaling. Wnt-3a signaling was depressed in a mouse L cell mutant, called sog9, 
      which is defective in the EXT1 gene encoding the HS-synthesizing enzyme and the
      chondroitin 4-O-sulfotransferase (C4ST-1) gene compared with parental L cells.
      The transfection of sog9 cells with C4ST-1 resulted in the recovery of Wnt-3a
      signaling, whereas the expression of EXT1 in sog9 cells could not restore Wnt-3a 
      signaling. In addition, the expression level of introduced C4ST-1 correlated with
      the recovery of Wnt-3a signaling accompanied by the increased expression of the E
      disaccharide unit of CS. Interestingly, molecular interaction analyses using
      Biacore revealed that squid CS-E (rich in the E disaccharide unit) bound strongly
      to Wnt-3a (K(d)=13.2 nm) to the same extent as heparin from bovine lung
      (K(d)=8.43 nm). In contrast, other CS isoforms as well as HS isolated from bovine
      kidney showed little binding activity to Wnt-3a. Moreover, exogenously added CS-E
      potently inhibited the accumulation of beta-catenin induced by Wnt-3a. These
      results suggest that CS-E-like structures synthesized by C4ST-1 participate in
      Wnt-3a signaling and modulate the physiological events caused by Wnt-3a signals.
FAU - Nadanaka, Satomi
AU  - Nadanaka S
AD  - Department of Biochemistry, Kobe Pharmaceutical University, Kobe 658-8558, Japan.
FAU - Ishida, Miho
AU  - Ishida M
FAU - Ikegami, Masami
AU  - Ikegami M
FAU - Kitagawa, Hiroshi
AU  - Kitagawa H
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20080730
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Disaccharides)
RN  - 0 (Wnt Proteins)
RN  - 0 (Wnt3 Protein)
RN  - 0 (Wnt3A Protein)
RN  - 0 (Wnt3a protein, mouse)
RN  - 9007-28-7 (Chondroitin Sulfates)
RN  - EC 2.4.1.- (N-Acetylglucosaminyltransferases)
RN  - EC 2.4.1.224 (exostosin-1)
RN  - EC 2.8.2.- (Sulfotransferases)
SB  - IM
MH  - Animals
MH  - Chondroitin Sulfates/*biosynthesis/genetics
MH  - Disaccharides/*biosynthesis
MH  - Gene Expression Regulation, Enzymologic/*physiology
MH  - L Cells (Cell Line)
MH  - Mice
MH  - N-Acetylglucosaminyltransferases/genetics/metabolism
MH  - Signal Transduction/*physiology
MH  - Sulfotransferases/genetics/*metabolism
MH  - Wnt Proteins/genetics/*metabolism
MH  - Wnt3 Protein
MH  - Wnt3A Protein
EDAT- 2008/08/01 09:00
MHDA- 2008/11/05 09:00
CRDT- 2008/08/01 09:00
PHST- 2008/08/01 09:00 [pubmed]
PHST- 2008/11/05 09:00 [medline]
PHST- 2008/08/01 09:00 [entrez]
AID - M802997200 [pii]
AID - 10.1074/jbc.M802997200 [doi]
PST - ppublish
SO  - J Biol Chem. 2008 Oct 3;283(40):27333-43. doi: 10.1074/jbc.M802997200. Epub 2008 
      Jul 30.

PMID- 1694801
OWN - NLM
STAT- MEDLINE
DCOM- 19900816
LR  - 20171128
IS  - 0301-4681 (Print)
IS  - 0301-4681 (Linking)
VI  - 43
IP  - 1
DP  - 1990 Mar
TI  - Chondroitin sulfates in developing mouse tooth germs. An immunohistochemical
      study with monoclonal antibodies against chondroitin-4 and chondroitin-6
      sulfates.
PG  - 37-50
AB  - The role of glycosaminoglycans and proteoglycans during ontogenesis is not known.
      The developing tooth offers a potentially important model for studies of
      structure-function relationships. In this study, we have analysed the temproal
      and spatial expression of chondroitins of differing sulfation patterns in
      embryonic molars and incisors. For this purpose, we have used monoclonal
      antibodies (Mabs) specific for unsulfated, 4-sulfated, and 6-sulfated forms of
      chondroitin in conjunction with indirect immunofluorescence or immunoperoxidase
      labeling. Unsulfated chondroitin was not detected in embryonic teeth. Chondroitin
      4- and chondroitin 6-sulfates were present in the stellate reticulum but
      otherwise they were confined to the dental mesenchyme. The 3B3 and MC21C-epitope,
      which are markers of 6-sulfated chondroitin, were uniformly distributed in the
      dental mesenchyme during the bud stage; they disappeared from the dental papilla 
      of the cusps and of the anterior region of the incisor as development proceeded. 
      These epitopes were absent from the basement membrane and from the predentin. In 
      the odontoblastic cell lineage, the 3B3 and MC21C-epitopes were detected only
      between preodontoblasts at an early stage of differentiation. The monoclonal
      antibody 2B6 served as a probe to localize chondroitin 4-sulfate. This
      glycosaminoglycan was detected as early as the dental lamina stage but its
      expression was restricted to the basement membrane of the teeth until the late
      bell stage. After the onset of cusp formation, strong staining was also observed 
      over the occlusal region of the dental papilla while the cervical region of the
      dental papilla remained 2B6-negative. Incisors at the bell stage exhibited a
      decreasing gradient of immunostaining by 2B6 from their anterior region to their 
      posterior end. The extracellular matrix surrounding preodontoblasts reacted with 
      2B6 and the predentin, produced by the odontoblasts, was also intensely labeled
      with this antibody. Comparison between immunostaining with 3B3 and 2B6, on
      consecutive sections revealed a mutually exclusive pattern of distribution of the
      corresponding epitopes during odontogenesis. Furthermore, in the continuously
      growing incisor, a striking positive correlation was found between the
      immunostaining patterns produced by 3B3 and MC21C and the mitotic indices along
      the anterior-posterior axis of the tooth. Hence, sulfation of chondroitin seems
      developmentally regulated. We postulate that changes in the sulfation pattern of 
      chondroitin might play a role in ontogenesis by locally altering the functional
      properties of the extracellular matrix.
FAU - Mark, M P
AU  - Mark MP
AD  - Institut de Biologie Medicale, INSERM-Universite Louis Pasteur, Faculte de
      Medecine, Strasbourg, France.
FAU - Baker, J R
AU  - Baker JR
FAU - Morrison, K
AU  - Morrison K
FAU - Ruch, J V
AU  - Ruch JV
LA  - eng
GR  - AR 39244/AR/NIAMS NIH HHS/United States
GR  - HL 343/HL/NHLBI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - England
TA  - Differentiation
JT  - Differentiation; research in biological diversity
JID - 0401650
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Epitopes)
RN  - 9007-27-6 (Chondroitin)
RN  - 9007-28-7 (Chondroitin Sulfates)
SB  - IM
MH  - Animals
MH  - Antibodies, Monoclonal/immunology
MH  - Chondroitin/*analogs & derivatives
MH  - Chondroitin Sulfates/immunology/*metabolism
MH  - Epitopes/immunology
MH  - Immunohistochemistry
MH  - Incisor/cytology/immunology/metabolism
MH  - Mice
MH  - Molar/cytology/immunology/metabolism
MH  - Odontogenesis
MH  - Tooth Germ/cytology/immunology/*metabolism
EDAT- 1990/03/01 00:00
MHDA- 1990/03/01 00:01
CRDT- 1990/03/01 00:00
PHST- 1990/03/01 00:00 [pubmed]
PHST- 1990/03/01 00:01 [medline]
PHST- 1990/03/01 00:00 [entrez]
AID - S0301-4681(11)60574-4 [pii]
PST - ppublish
SO  - Differentiation. 1990 Mar;43(1):37-50.

PMID- 11878808
OWN - NLM
STAT- MEDLINE
DCOM- 20020627
LR  - 20080814
IS  - 0003-2697 (Print)
IS  - 0003-2697 (Linking)
VI  - 302
IP  - 2
DP  - 2002 Mar 15
TI  - Immunoglobulin G-class mouse monoclonal antibodies to major brain gangliosides.
PG  - 276-84
AB  - Mice genetically engineered to lack complex gangliosides are improved hosts for
      raising antibodies against those gangliosides. We report the generation and
      characterization of nine immunoglobulin G (IgG)-class monoclonal antibodies
      (mAbs) raised against the four major brain gangliosides in mammals. These include
      (designated as ganglioside specificity-IgG subclass) two anti-GM1 mAbs (GM1-1,
      GM1-2b), three anti-GD1a mAbs (GD1a-1, GD1a-2a, GD1a-2b), one anti-GD1b mAb
      (GD1b-1), and three anti-GT1b mAbs (GT1b-1, GT1b-2a, GT1b-2b). Each mAb
      demonstrated high specificity, with little or no cross-reactivity with other
      major brain gangliosides. Enzyme-linked immunosorbent assay (ELISA) screening
      against 14 closely related synthetic and purified gangliosides confirmed the high
      specificity, with no significant cross-reactivity except that of the anti-GD1a
      mAbs for the closely related minor ganglioside GT1a alpha. All of the mAbs were
      useful for ELISA, TLC immunooverlay, and immunocytochemistry. Neural cells from
      wild-type rats and mice were immunostained to differing levels with the
      anti-ganglioside antibodies, whereas neural cells from mice engineered to lack
      complex gangliosides (lacking the ganglioside-specific biosynthetic enzyme
      UDP-GalNAc:GM3/GD3 N-acetylgalactosaminyltransferase) remained unstained,
      demonstrating that most of the mAbs react only with gangliosides and not with
      related structures on glycoproteins. These mAbs may provide useful tools for
      delineation of the expression and function of the major brain gangliosides and
      for probing the pathology of anti-ganglioside autoimmune diseases.
CI  - (C)2002 Elsevier Science (USA).
FAU - Schnaar, Ronald L
AU  - Schnaar RL
AD  - Department of Pharmacology and Molecular Sciences, The Johns Hopkins School of
      Medicine, 725 N. Wolfe Street, Baltimore, Maryland 21205-2185, USA.
      schnaar@jhu.edu
FAU - Fromholt, Susan E
AU  - Fromholt SE
FAU - Gong, Yanping
AU  - Gong Y
FAU - Vyas, Alka A
AU  - Vyas AA
FAU - Laroy, Wouter
AU  - Laroy W
FAU - Wayman, Dawn M
AU  - Wayman DM
FAU - Heffer-Lauc, Marija
AU  - Heffer-Lauc M
FAU - Ito, Hiromi
AU  - Ito H
FAU - Ishida, Hideharu
AU  - Ishida H
FAU - Kiso, Makoto
AU  - Kiso M
FAU - Griffin, John W
AU  - Griffin JW
FAU - Shiekh, Kazim A
AU  - Shiekh KA
LA  - eng
GR  - NS37096/NS/NINDS NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Anal Biochem
JT  - Analytical biochemistry
JID - 0370535
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (G(M3) Ganglioside)
RN  - 0 (Gangliosides)
RN  - 0 (Immunoglobulin G)
RN  - 12707-58-3 (ganglioside, GD1a)
RN  - 19553-76-5 (ganglioside, GD1b)
RN  - 59247-13-1 (trisialoganglioside GT1)
SB  - IM
MH  - Animals
MH  - Animals, Genetically Modified
MH  - Antibodies, Monoclonal/*immunology
MH  - Antigen-Antibody Reactions
MH  - Binding Sites
MH  - Cerebellum/*chemistry
MH  - G(M3) Ganglioside/immunology
MH  - Gangliosides/*immunology
MH  - Immunoglobulin G/*immunology
MH  - Immunohistochemistry/methods
MH  - Mice
EDAT- 2002/03/07 10:00
MHDA- 2002/06/28 10:01
CRDT- 2002/03/07 10:00
PHST- 2002/03/07 10:00 [pubmed]
PHST- 2002/06/28 10:01 [medline]
PHST- 2002/03/07 10:00 [entrez]
AID - 10.1006/abio.2001.5540 [doi]
AID - S000326970195540X [pii]
PST - ppublish
SO  - Anal Biochem. 2002 Mar 15;302(2):276-84. doi: 10.1006/abio.2001.5540.

PMID- 16564536
OWN - NLM
STAT- MEDLINE
DCOM- 20060620
LR  - 20061115
IS  - 0022-1759 (Print)
IS  - 0022-1759 (Linking)
VI  - 311
IP  - 1-2
DP  - 2006 Apr 20
TI  - Comprehensive analysis of monoclonal antibodies against detergent-insoluble
      membrane/lipid rafts of HL60 cells.
PG  - 106-16
AB  - Glycosphingolipids and cholesterol are principal components of plasmamembrane
      microdomains, i.e. lipid rafts. Recent studies revealed the possible presence of 
      a variety of microdomains that distinctly differ in terms of their molecular
      composition and functions. To understand their precise structures and functions, 
      we produced monoclonal antibodies (MAbs) by immunizing mice to the microdomains
      prepared from a fraction of detergent-insoluble membrane (DIM) of HL60 cells.
      Biochemical characterization of the antigen epitopes led to classification of the
      MAbs into two groups. One group consists of MAbs that react with lipids such as
      phosphatidylglucoside, lysophosphatidylinositol, and gangliosides (GM1a and
      GD1b), and the other consists of MAbs that react with proteins such as annexin I,
      aminopeptidase N and acrogranin. Immunofluorescence staining of HL60 cells with
      the MAbs, except for the MAbs that recognize lysophosphatidylinositol or annexin 
      I, resulted in patchy-like images of the cell membranes. Interestingly, MAbs
      belonging to the former group had the potential to induce cell
      proliferation/differentiation in vitro. Our MAbs against the DIM fraction of HL60
      cells can be valuable tools for the study of membrane microdomains.
FAU - Yamazaki, Yasuhiro
AU  - Yamazaki Y
AD  - Laboratory for Neural Architecture, Advanced Technology Development Group, RIKEN 
      Brain Science Institute, Wako, Saitama 351-0198, Japan.
FAU - Nagatsuka, Yasuko
AU  - Nagatsuka Y
FAU - Oshima, Eriko
AU  - Oshima E
FAU - Suzuki, Yasuo
AU  - Suzuki Y
FAU - Hirabayashi, Yoshio
AU  - Hirabayashi Y
FAU - Hashikawa, Tsutomu
AU  - Hashikawa T
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20060309
PL  - Netherlands
TA  - J Immunol Methods
JT  - Journal of immunological methods
JID - 1305440
RN  - 0 (Annexin A1)
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Gangliosides)
RN  - 0 (Glycerophospholipids)
RN  - 0 (Grn protein, mouse)
RN  - 0 (Intercellular Signaling Peptides and Proteins)
RN  - 0 (Lysophospholipids)
RN  - 0 (ganglioside GM1alpha)
RN  - 0 (lysophosphatidylinositol)
RN  - 0 (phosphatidylglucose)
RN  - 19553-76-5 (ganglioside, GD1b)
RN  - 37758-47-7 (G(M1) Ganglioside)
RN  - EC 3.4.11.7 (Glutamyl Aminopeptidase)
SB  - IM
MH  - Animals
MH  - Annexin A1/immunology
MH  - Antibodies, Monoclonal/biosynthesis/*immunology
MH  - Cell Proliferation
MH  - Fluorescent Antibody Technique
MH  - G(M1) Ganglioside/analogs & derivatives/immunology
MH  - Gangliosides/immunology
MH  - Glutamyl Aminopeptidase/immunology
MH  - Glycerophospholipids/immunology
MH  - HL-60 Cells
MH  - Humans
MH  - Hybridomas/immunology
MH  - Immunoblotting
MH  - Intercellular Signaling Peptides and Proteins/immunology
MH  - Lysophospholipids/immunology
MH  - Membrane Microdomains/chemistry/*immunology
MH  - Mice
MH  - Mice, Inbred BALB C
EDAT- 2006/03/28 09:00
MHDA- 2006/06/21 09:00
CRDT- 2006/03/28 09:00
PHST- 2005/08/02 00:00 [received]
PHST- 2005/12/13 00:00 [revised]
PHST- 2006/01/20 00:00 [accepted]
PHST- 2006/03/28 09:00 [pubmed]
PHST- 2006/06/21 09:00 [medline]
PHST- 2006/03/28 09:00 [entrez]
AID - S0022-1759(06)00035-4 [pii]
AID - 10.1016/j.jim.2006.01.019 [doi]
PST - ppublish
SO  - J Immunol Methods. 2006 Apr 20;311(1-2):106-16. doi: 10.1016/j.jim.2006.01.019.
      Epub 2006 Mar 9.

PMID- 8891271
OWN - NLM
STAT- MEDLINE
DCOM- 19970206
LR  - 20061115
IS  - 0006-8993 (Print)
IS  - 0006-8993 (Linking)
VI  - 732
IP  - 1-2
DP  - 1996 Sep 2
TI  - Immunocytochemical analysis of gangliosides in rat primary cerebellar cultures
      using specific monoclonal antibodies.
PG  - 75-86
AB  - We studied the expression of ganglioside antigens in primary cultures of rat
      cerebellum using an immunocytochemical technique with mouse monoclonal antibodies
      (MAbs) specific for various gangliosides. Twelve MAbs that specifically recognize
      each ganglioside were used. Our study revealed that there is a cell type-specific
      expression of ganglioside antigens in the primary cultures. A number of b-series 
      gangliosides were detected in the granule cells, whereas a-series gangliosides
      were not intensely expressed. GD1b was detected in the granule cells. GD2
      appeared to be present in a subset of the granule cells or a type of small
      neurons. GD3 was associated not only with the granule cells, but also with both
      astrocytes and oligodendrocytes. An O-Ac-disialoganglioside, which was suggested 
      to be O-Ac-LD1, was restrictedly detected in Purkinje cells. The other
      gangliosides were not detected clearly in these cells. These results suggest that
      several gangliosides may be useful markers for identifying cells in primary
      cultures of the rat cerebellum; particularly b-series gangliosides such as GD2
      and GD1b for the granule cells and O-Ac-LD1 for Purkinje cells.
FAU - Kawashima, I
AU  - Kawashima I
AD  - Department of Tumor Immunology, Tokyo Metropolitan Institute of Medical Science, 
      Japan.
FAU - Nagata, I
AU  - Nagata I
FAU - Tai, T
AU  - Tai T
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - Netherlands
TA  - Brain Res
JT  - Brain research
JID - 0045503
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Gangliosides)
RN  - 0 (Tetanus Toxin)
RN  - 9012-63-9 (Cholera Toxin)
RN  - EC 3.2.1.18 (Neuraminidase)
RN  - EC 3.4.21.4 (Trypsin)
SB  - IM
MH  - Animals
MH  - Animals, Newborn
MH  - Antibodies, Monoclonal
MH  - Antibody Specificity
MH  - Carbohydrate Sequence
MH  - Cells, Cultured
MH  - Cerebellum/*cytology
MH  - Cholera Toxin
MH  - Chromatography, Thin Layer
MH  - Fluorescent Antibody Technique, Indirect
MH  - Gangliosides/*analysis/chemistry
MH  - Immunohistochemistry
MH  - Mice
MH  - Molecular Sequence Data
MH  - Molecular Structure
MH  - Neuraminidase
MH  - Neurons/*cytology
MH  - Purkinje Cells/*cytology
MH  - Rats
MH  - Rats, Wistar
MH  - Sensitivity and Specificity
MH  - Tetanus Toxin
MH  - Trypsin
EDAT- 1996/09/02 00:00
MHDA- 1996/09/02 00:01
CRDT- 1996/09/02 00:00
PHST- 1996/09/02 00:00 [pubmed]
PHST- 1996/09/02 00:01 [medline]
PHST- 1996/09/02 00:00 [entrez]
AID - 0006-8993(96)00493-3 [pii]
PST - ppublish
SO  - Brain Res. 1996 Sep 2;732(1-2):75-86.

PMID- 7539400
OWN - NLM
STAT- MEDLINE
DCOM- 19950705
LR  - 20071205
IS  - 0272-457X (Print)
IS  - 0272-457X (Linking)
VI  - 14
IP  - 1
DP  - 1995 Feb
TI  - A new monoclonal antibody (A78-G/A7) to the Thomsen-Friedenreich pan-tumor
      antigen.
PG  - 37-44
AB  - A new monoclonal antibody to the Thomsen-Friedenreich (TF) antigen (or, more
      precisely, epitope; Gal beta 1-3GalNAc-) has been developed that is specific for 
      both anomeric forms of this disaccharide (TF alpha and TF beta, including related
      structures on glycolipids), and not assay restricted. We demonstrate that this
      avid antibody (A78-G/A7) is well suited for immunohistochemistry on
      paraffin-embedded and cryosectioned tissues, immunoblotting, ELISA techniques,
      and hemagglutination. Immunohistochemistry on paraffin sections does not require 
      proteolytic or microwave pretreatment. The binding characteristics of this
      antibody are largely independent of variations in pH (6.0-8.2) and temperature
      (4-37 degrees C). Immunoblotting with KG-1 (human acute myelogenous leukemia)
      cells revealed a series of TF-active glycoproteins with a main band at about 155 
      kDa. Immunoprecipitation was performed using a new technique applicable to
      IgM-type antibodies.
FAU - Karsten, U
AU  - Karsten U
AD  - Max Delbruck Center for Molecular Medicine, Berlin-Buch, Germany.
FAU - Butschak, G
AU  - Butschak G
FAU - Cao, Y
AU  - Cao Y
FAU - Goletz, S
AU  - Goletz S
FAU - Hanisch, F G
AU  - Hanisch FG
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Hybridoma
JT  - Hybridoma
JID - 8202424
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Epitopes)
RN  - 3554-90-3 (Thomsen-Friedenreich antigen)
SB  - IM
MH  - Animals
MH  - *Antibodies, Monoclonal
MH  - Antibody Specificity
MH  - Antigens, Tumor-Associated, Carbohydrate/chemistry/*immunology
MH  - Breast Neoplasms/immunology
MH  - Carbohydrate Sequence
MH  - Cell Line
MH  - Colorectal Neoplasms/immunology
MH  - Epitopes/chemistry
MH  - Female
MH  - Humans
MH  - Immunohistochemistry
MH  - Mice
MH  - Molecular Sequence Data
MH  - Tumor Cells, Cultured
EDAT- 1995/02/01 00:00
MHDA- 1995/02/01 00:01
CRDT- 1995/02/01 00:00
PHST- 1995/02/01 00:00 [pubmed]
PHST- 1995/02/01 00:01 [medline]
PHST- 1995/02/01 00:00 [entrez]
AID - 10.1089/hyb.1995.14.37 [doi]
PST - ppublish
SO  - Hybridoma. 1995 Feb;14(1):37-44. doi: 10.1089/hyb.1995.14.37.

PMID- 18662810
OWN - NLM
STAT- MEDLINE
DCOM- 20081203
LR  - 20080825
IS  - 0008-6215 (Print)
IS  - 0008-6215 (Linking)
VI  - 343
IP  - 14
DP  - 2008 Sep 22
TI  - Catfish (Clarias batrachus) serum lectin recognizes polyvalent Tn
      [alpha-D-GalpNAc1-Ser/Thr], Talpha
      [beta-D-Galp-(1-->3)-alpha-D-GalpNAc1-Ser/Thr], and II
      [beta-D-Galp(1-->4)-beta-D-GlcpNAc1-] mammalian glycotopes.
PG  - 2384-92
LID - 10.1016/j.carres.2008.06.030 [doi]
AB  - A new calcium dependent GalNAc/Gal specific lectin was isolated from the serum of
      Indian catfish, Clarias batrachus and designated as C. batrachus lectin (CBL). It
      is a disulfide-linked homodecameric lectin of 74.65kDa subunits and the
      oligomeric form is essential for its activity. Binding specificity of CBL was
      investigated by enzyme-linked lectin-sorbent assay using a series of simple
      sugars, polysaccharides, and glycoproteins. GalNAc was more potent inhibitor than
      Gal; and alpha glycosides of both were more inhibitory than their beta
      counterparts. CBL showed maximum affinity for human tumor-associated Tn-antigens 
      (GalNAcalpha1-Ser/Thr) at the molecular level and was 3.5 times higher than
      GalNAc. CBL interacted strongly with polyvalent Tn and Talpha
      (Galbeta1,3GalNAcalpha1-) as well as multivalent-II (Galbeta1,4GlcNAcbeta1-)
      antigens containing glycoproteins and intensity of inhibition was 10(3)-10(5)
      times more than monovalent ones. The overall specificity of CBL lies in the order
      of polyvalent Tn, Talpha and II>>>>monovalent Tn > or = Me-alphaGalNAc>monovalent
      Talpha> Me-betaGalNAc>Me-alphaGal>monovalent T>GalNAc>monovalent F>monovalent
      II>Me-betaGal>Gal.
FAU - Singha, Biswajit
AU  - Singha B
AD  - Department of Biological Chemistry, Indian Association for the Cultivation of
      Science, Jadavpur, Kolkata 700 032, India.
FAU - Adhya, Mausumi
AU  - Adhya M
FAU - Chatterjee, Bishnu P
AU  - Chatterjee BP
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20080708
PL  - Netherlands
TA  - Carbohydr Res
JT  - Carbohydrate research
JID - 0043535
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Glycoproteins)
RN  - 0 (Lectins)
RN  - 0 (Tn antigen)
SB  - IM
MH  - Animals
MH  - Antigens, Tumor-Associated, Carbohydrate/*chemistry/*metabolism
MH  - *Catfishes/blood
MH  - Glycoproteins/metabolism
MH  - Hemagglutination
MH  - Humans
MH  - Lectins/blood/chemistry/isolation & purification/*metabolism
MH  - Mammals
MH  - Molecular Weight
MH  - Protein Binding
MH  - Spectrometry, Mass, Electrospray Ionization
MH  - Substrate Specificity
EDAT- 2008/07/30 09:00
MHDA- 2008/12/17 09:00
CRDT- 2008/07/30 09:00
PHST- 2007/08/20 00:00 [received]
PHST- 2008/06/26 00:00 [revised]
PHST- 2008/06/28 00:00 [accepted]
PHST- 2008/07/30 09:00 [pubmed]
PHST- 2008/12/17 09:00 [medline]
PHST- 2008/07/30 09:00 [entrez]
AID - S0008-6215(08)00349-2 [pii]
AID - 10.1016/j.carres.2008.06.030 [doi]
PST - ppublish
SO  - Carbohydr Res. 2008 Sep 22;343(14):2384-92. doi: 10.1016/j.carres.2008.06.030.
      Epub 2008 Jul 8.

PMID- 11528254
OWN - NLM
STAT- MEDLINE
DCOM- 20011204
LR  - 20171101
IS  - 0030-2414 (Print)
IS  - 0030-2414 (Linking)
VI  - 61
IP  - 2
DP  - 2001
TI  - Immunoreactivity of monoclonal antibody BW835 represents a marker of progression 
      and prognosis in early gastric cancer.
PG  - 147-55
AB  - The Thomsen-Friedenreich (TF) antigen is a well-known human pan-carcinoma
      antigen. It represents a carbohydrate core disaccharide (Gal beta 1-3GalNAc)
      which is predominantly bound to mucin peptide cores. Its immunoreactivity depends
      on changes in glycosylation which lead to a reduction in the carbohydrate chain
      length and the exposure of core carbohydrates. In the present study, we
      investigated 208 gastric adenocarcinomas with respect to their
      immunohistochemical reactivity applying two monoclonal antibodies (MAbs). MAb
      specifically detecting TF antigen (A78-G/A7) and MAb BW835 were included. The
      latter reacts with a certain glycoform of the MUC1 peptide core, characterized by
      core-type glycans like TF. A78-G/A7 epitopes were detected in 68.8% and BW835
      epitopes in 57.7% of the carcinomas. BW835 immunoreactivity correlated with the
      presence of lymph node metastases. Both A78-G/A7 and BW835 staining were
      significantly stronger in tubular/papillary cancer (WHO classification) and
      intestinal-type cancer according to Lauren. In univariate survival analyses of
      all patients studied, BW835 immunoreactivity was a marker of an unfavorable
      prognosis (p < 0.05). The presence of A78-G/A7 and BW835 epitopes exerted a
      negative effect on the subgroup of pTNM stage I carcinomas. These results
      indicate that TF and MUC1-TF immunoreactivity defines a 'high-risk' subgroup of
      stage I patients in gastric cancer.
CI  - Copyright 2001 S. Karger AG, Basel
FAU - Baldus, S E
AU  - Baldus SE
AD  - Institute of Pathology, University of Cologne, Germany. s-e.baldus@uni-koeln.de
FAU - Zirbes, T K
AU  - Zirbes TK
FAU - Glossmann, J
AU  - Glossmann J
FAU - Fromm, S
AU  - Fromm S
FAU - Hanisch, F G
AU  - Hanisch FG
FAU - Monig, S P
AU  - Monig SP
FAU - Schroder, W
AU  - Schroder W
FAU - Schneider, P M
AU  - Schneider PM
FAU - Flucke, U
AU  - Flucke U
FAU - Karsten, U
AU  - Karsten U
FAU - Thiele, J
AU  - Thiele J
FAU - Holscher, A H
AU  - Holscher AH
FAU - Dienes, H P
AU  - Dienes HP
LA  - eng
PT  - Comparative Study
PT  - Evaluation Studies
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - Switzerland
TA  - Oncology
JT  - Oncology
JID - 0135054
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens, Neoplasm)
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Biomarkers, Tumor)
RN  - 0 (Epitopes)
RN  - 0 (Mucin-1)
RN  - 0 (Neoplasm Proteins)
RN  - 0 (Protein Isoforms)
RN  - 3554-90-3 (Thomsen-Friedenreich antigen)
SB  - IM
MH  - Adenocarcinoma/*chemistry/classification/mortality/pathology
MH  - Adult
MH  - Aged
MH  - Aged, 80 and over
MH  - Antibodies, Monoclonal/*immunology
MH  - Antibody Specificity
MH  - Antigens, Neoplasm/*analysis/chemistry/immunology
MH  - Antigens, Tumor-Associated, Carbohydrate/analysis/immunology
MH  - Biomarkers, Tumor/*analysis
MH  - Disease Progression
MH  - Epitopes/analysis/immunology
MH  - Female
MH  - Glycosylation
MH  - Humans
MH  - Immunoenzyme Techniques
MH  - Life Tables
MH  - Lymphatic Metastasis
MH  - Male
MH  - Middle Aged
MH  - Mucin-1/*analysis/chemistry/immunology
MH  - Multivariate Analysis
MH  - Neoplasm Proteins/*analysis/chemistry/immunology
MH  - Neoplasm Staging
MH  - Prognosis
MH  - Protein Isoforms/analysis/chemistry/immunology
MH  - Protein Processing, Post-Translational
MH  - Retrospective Studies
MH  - Risk
MH  - Stomach Neoplasms/*chemistry/mortality/pathology
MH  - Survival Analysis
EDAT- 2001/08/31 10:00
MHDA- 2002/01/05 10:01
CRDT- 2001/08/31 10:00
PHST- 2001/08/31 10:00 [pubmed]
PHST- 2002/01/05 10:01 [medline]
PHST- 2001/08/31 10:00 [entrez]
AID - 55366 [pii]
AID - 10.1159/000055366 [doi]
PST - ppublish
SO  - Oncology. 2001;61(2):147-55. doi: 10.1159/000055366.

PMID- 10491017
OWN - NLM
STAT- MEDLINE
DCOM- 19991216
LR  - 20181113
IS  - 1219-4956 (Print)
IS  - 1219-4956 (Linking)
VI  - 5
IP  - 3
DP  - 1999
TI  - Identification and characterization of different subpopulations in a human lung
      adenocarcinoma cell line (A549).
PG  - 197-204
AB  - The morphology, cell growth, antigenic expression and tumorigenicity of cell
      subpopulations from the A549 lung adenocarcinoma isolated by Percoll gradient
      separation have been analysed. Four subpopulations were obtained (subpopulations 
      A, B, C and D). Immunocytochemical analysis of several antigens was performed
      with monoclonal antibodies (MAbs): MUC1 mucin (C595, HMFG1 and HMFG2), MUC5B
      (PANH2); gp230 (PANH4); carbohydrate antigens including sialyl Lewis x (KM93), Tn
      antigen (83D4), Lewis y (C14); 5, 6, 8, 17 and 19 cytokeratins and p53. The cell 
      population D tended to form cell aggregates that piled up on the monolayer
      similar to overgrowth cultures of the A549 parental cell line, whereas A, B and C
      cell subpopulations formed well spread monolayers. Both parental A549 and
      subpopulation D secreted abundant mucus. The topographic distribution and
      secretion production were correlated with tumorigenic assays since only
      subpopulation D grew in nude mice exhibiting reduced latency period; these
      characteristics correlated with the fast growth of the subpopulation D in vitro. 
      Immunocytochemical analysis demonstrated that subpopulation D showed greater
      expression of MUC1 mucin and carbohydrate antigens such as Tn antigen, sialyl
      Lewis x and Lewis y and less expression of cytokeratins, p53, MUC5B and gp230;
      conversely, subpopulations A, B and C showed the opposite antigenic profile. Our 
      results illustrate heterogeneity in the A549 cell line; subpopulations A, B and C
      retained characteristics of more differentiated adenocarcinoma while
      subpopulation D displayed features of a less differentiated tumor line.
FAU - Croce, M V
AU  - Croce MV
AD  - Universidad Nacional de la Plata, Centro de Investigaciones Inmunologicas Basicas
      y Aplicadas (CINIBA) Calle 60 y 120, La Plata, Argentina.
FAU - Colussi, A G
AU  - Colussi AG
FAU - Price, M R
AU  - Price MR
FAU - Segal-Eiras, A
AU  - Segal-Eiras A
LA  - eng
PT  - Journal Article
PL  - Netherlands
TA  - Pathol Oncol Res
JT  - Pathology oncology research : POR
JID - 9706087
RN  - 0
      (5-acetylneuraminyl-(2-3)-galactosyl-(1-4)-(fucopyranosyl-(1-3))-N-acetylglucosam
      ine)
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Oligosaccharides)
RN  - 0 (Tumor Suppressor Protein p53)
RN  - 68238-35-7 (Keratins)
SB  - IM
MH  - Adenocarcinoma/immunology/*pathology
MH  - Animals
MH  - Antibodies, Monoclonal
MH  - Cell Separation
MH  - Humans
MH  - Immunohistochemistry
MH  - Keratins/analysis
MH  - Lung Neoplasms/immunology/*pathology
MH  - Mice
MH  - Mice, Nude
MH  - Neoplasm Transplantation
MH  - Oligosaccharides/analysis
MH  - Phenotype
MH  - Time Factors
MH  - Tumor Cells, Cultured
MH  - Tumor Suppressor Protein p53/analysis
EDAT- 1999/09/22 00:00
MHDA- 1999/09/22 00:01
CRDT- 1999/09/22 00:00
PHST- 1999/09/22 00:00 [pubmed]
PHST- 1999/09/22 00:01 [medline]
PHST- 1999/09/22 00:00 [entrez]
AID - PAOR.1999.5.3.0197 [pii]
PST - ppublish
SO  - Pathol Oncol Res. 1999;5(3):197-204.

PMID- 7538976
OWN - NLM
STAT- MEDLINE
DCOM- 19950627
LR  - 20171116
IS  - 0020-7136 (Print)
IS  - 0020-7136 (Linking)
VI  - 61
IP  - 4
DP  - 1995 May 16
TI  - CD69+ and HLA-DR+ activation antigens on peripheral blood lymphocyte populations 
      in metastatic breast and ovarian cancer patients: correlations with survival
      following active specific immunotherapy.
PG  - 470-4
AB  - Lymphocyte activation markers CD69 and HLA-DR were studied in metastatic breast
      and ovarian cancer patients who received active specific immunotherapy (ASI)
      using cancer vaccines containing the synthetic tumor-associated antigen sialyl-Tn
      or the Thomsen-Friedenreich antigen conjugated to KLH plus DETOX adjuvant. Breast
      cancer patients who showed prolonged survival following ASI had lower numbers of 
      total CD69+ and CD4+CD69+ cells prior to ASI compared to patients who died.
      However, following ASI, the surviving patients showed an increase in CD69+ and
      CD4+CD69+ cells and the deceased patients showed a decrease. A greater than 50%
      increase in the percentage of cells bearing the activation marker CD69 is
      associated with an increase in survival in both ovarian and breast cancer
      patients. In the surviving breast cancer patients there was a significant
      decrease in the percentage of non-B lymphocyte HLA-DR+ (CD20-HLA-DR+) cells
      following cyclophosphamide treatment. A strong positive correlation was found
      between lymphocyte populations CD20- HLA-DR+ and CD8+CD57+, a putative suppressor
      cell population. Breast cancer patients who showed a greater than median decrease
      in CD20-HLA-DR+ lymphocytes following cyclophosphamide treatment had a survival
      advantage over patients who had less than the median decrease in the percent
      CD20-HLA-DR+ lymphocytes.
FAU - Yacyshyn, M B
AU  - Yacyshyn MB
AD  - Department of Laboratory Medicine, University of Alberta, Edmonton, Canada.
FAU - Poppema, S
AU  - Poppema S
FAU - Berg, A
AU  - Berg A
FAU - MacLean, G D
AU  - MacLean GD
FAU - Reddish, M A
AU  - Reddish MA
FAU - Meikle, A
AU  - Meikle A
FAU - Longenecker, B M
AU  - Longenecker BM
LA  - eng
PT  - Clinical Trial
PT  - Clinical Trial, Phase I
PT  - Journal Article
PL  - United States
TA  - Int J Cancer
JT  - International journal of cancer
JID - 0042124
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens, CD)
RN  - 0 (Antigens, Differentiation, T-Lymphocyte)
RN  - 0 (Antigens, Neoplasm)
RN  - 0 (CD3 Complex)
RN  - 0 (CD4 Antigens)
RN  - 0 (CD57 Antigens)
RN  - 0 (CD69 antigen)
RN  - 0 (CD8 Antigens)
RN  - 0 (HLA-DR Antigens)
RN  - 0 (Lectins, C-Type)
SB  - IM
MH  - Adenocarcinoma/*blood/mortality/*therapy
MH  - Adult
MH  - Aged
MH  - Antibodies, Monoclonal
MH  - Antigens, CD/*blood
MH  - Antigens, Differentiation, T-Lymphocyte/*blood
MH  - Antigens, Neoplasm/*blood
MH  - Breast Neoplasms/*blood/mortality/*therapy
MH  - CD3 Complex/immunology
MH  - CD4 Antigens/blood
MH  - CD57 Antigens
MH  - CD8 Antigens/blood
MH  - Female
MH  - HLA-DR Antigens/*blood
MH  - Humans
MH  - *Immunotherapy, Active
MH  - Lectins, C-Type
MH  - Lymphocyte Activation/*immunology
MH  - Lymphocyte Subsets/*immunology
MH  - Lymphocytes/*immunology
MH  - Middle Aged
MH  - Neoplasm Metastasis
MH  - Ovarian Neoplasms/*blood/mortality/*therapy
MH  - Phenotype
MH  - Sensitivity and Specificity
EDAT- 1995/05/16 00:00
MHDA- 1995/05/16 00:01
CRDT- 1995/05/16 00:00
PHST- 1995/05/16 00:00 [pubmed]
PHST- 1995/05/16 00:01 [medline]
PHST- 1995/05/16 00:00 [entrez]
PST - ppublish
SO  - Int J Cancer. 1995 May 16;61(4):470-4.

PMID- 2663606
OWN - NLM
STAT- MEDLINE
DCOM- 19890822
LR  - 20181113
IS  - 0435-1339 (Print)
IS  - 0435-1339 (Linking)
VI  - 24
IP  - 3
DP  - 1989 Jun
TI  - Immunohistochemical study of carbohydrate antigen expression in gastric
      carcinoma.
PG  - 239-45
AB  - The expression of carbohydrate antigens in malignant and non-malignant gastric
      mucosa was studied immunohistochemically using the monoclonal antibody AH6
      directed to Ley antigen, FH2 directed to Lex antigen, and FH6 directed to
      sialyl-Lex antigen. Formalin-fixed gastric tissue resected from 54 patients with 
      gastric cancer and 20 patients with gastric ulcer were tested. The incidence of
      positive cases in gastric cancer patients with each antibody was as follows:
      AH6;85%, FH2;74%, FH6;74%. The Lex antigen was expressed in 81.5% of cases
      histologically classified as undifferentiated type, and 66.7% of cases classified
      as differentiated type. It was expressed in a higher incidence in early stage
      cancer (93.3%) than in advanced stage cancer (66.7%). Sialyl-Lex antigen was
      detected in more cases of differentiated type (88.9%) than in those of
      undifferentiated type (59.3%), whereas none of 8 early cancers of
      undifferentiated type expressed the antigen. The incidence of the expression of
      Ley antigen did not differ in relation to histological type or invasiveness. Lex 
      and Ley antigens were detected in noncancerous gastric epithelium. Sialyl-Lex
      antigen was not detected in the normal fundic gland region. These results
      demonstrate that Lex antigen may be a differentiation-associated antigen, and
      sialyl-Lex antigen might be useful as a marker of differentiated cancer and an
      indication for invasion of undifferentiated cancer.
FAU - Dohi, T
AU  - Dohi T
AD  - Second Department of Internal Medicine, Osaka Medical College, Takatsuki, Japan.
FAU - Abe, K
AU  - Abe K
FAU - Ohshiba, S
AU  - Ohshiba S
LA  - eng
PT  - Journal Article
PL  - Japan
TA  - Gastroenterol Jpn
JT  - Gastroenterologia Japonica
JID - 0152744
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens, Differentiation)
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Biomarkers, Tumor)
RN  - 0 (Lewis Blood-Group System)
SB  - IM
MH  - Adult
MH  - Aged
MH  - *Antibodies, Monoclonal
MH  - Antigens, Differentiation/analysis
MH  - Antigens, Tumor-Associated, Carbohydrate/*analysis
MH  - Biomarkers, Tumor/*analysis
MH  - Gastric Mucosa/metabolism
MH  - Humans
MH  - Immunoenzyme Techniques
MH  - *Lewis Blood-Group System
MH  - Middle Aged
MH  - Stomach Neoplasms/*metabolism
EDAT- 1989/06/01 00:00
MHDA- 1989/06/01 00:01
CRDT- 1989/06/01 00:00
PHST- 1989/06/01 00:00 [pubmed]
PHST- 1989/06/01 00:01 [medline]
PHST- 1989/06/01 00:00 [entrez]
PST - ppublish
SO  - Gastroenterol Jpn. 1989 Jun;24(3):239-45.

PMID- 10992504
OWN - NLM
STAT- MEDLINE
DCOM- 20001103
LR  - 20190508
IS  - 0019-9567 (Print)
IS  - 0019-9567 (Linking)
VI  - 68
IP  - 10
DP  - 2000 Oct
TI  - Phase variation in H type I and Lewis a epitopes of Helicobacter pylori
      lipopolysaccharide.
PG  - 5928-32
AB  - Helicobacter pylori NCTC 11637 lipopolysaccharide (LPS) expresses the human blood
      group antigens Lewis x (Le(x)), Le(y), and H type I. In this report, we
      demonstrate that the H type I epitope displays high-frequency phase variation.
      One variant expressed Le(x) and Le(y) and no H type I as determined by serology; 
      this switch was reversible. Insertional mutagenesis in NCTC 11637 of JHP563 (a
      poly(C) tract containing an open reading frame homologous to
      glycosyltransferases) yielded a transformant with a serotype similar to the phase
      variant. Structural analysis of the NCTC 11637 LPS confirmed the loss of the H
      type I epitope. Sequencing of JHP563 in strains NCTC 11637, an H type I-negative 
      variant, and an H type I-positive switchback variant showed a C14 (gene on), C13 
      (gene off), and C14 tract, respectively. Inactivation of strain G27, which
      expresses Le(x), Le(y), H type I, and Le(a), yielded a transformant that
      expressed Le(x) and Le(y). We conclude that JHP563 encodes a
      beta3-galactosyltransferase involved in the biosynthesis of H type I and Le(a)
      and that phase variation in H type I is due to C-tract changes in this gene. A
      second H type I-negative variant (variant 3a) expressed Le(x) and Le(a) and had
      lost both H type I and Le(y) expression. Inactivation of HP093-HP094 resulted in 
      a transformant expressing Le(x) and lacking Le(y) and H type I. Structural
      analysis of a mutant LPS confirmed the serological data. We conclude that the
      HP093-HP094 alpha2-fucosyltransferase (alpha2-FucT) gene product is involved in
      the biosynthesis of both Le(y) and Le(x). Finally, we inactivated HP0379 in
      strain 3a. The transformant had lost both Le(x) and Le(a) expression, which
      demonstrates that the HP0379 gene product is both an alpha3- and an alpha4-FucT. 
      Our data provide understanding at the molecular level of how H. pylori is able to
      diversify in the host, a requirement likely essential for successful colonization
      and transmission.
FAU - Appelmelk, B J
AU  - Appelmelk BJ
AD  - Department of Medical Microbiology, Vrije Universiteit, Medical School, 1081 BT
      Amsterdam, The Netherlands. BJ.Appelmelk.mm@med.vu.nl
FAU - Martino, M C
AU  - Martino MC
FAU - Veenhof, E
AU  - Veenhof E
FAU - Monteiro, M A
AU  - Monteiro MA
FAU - Maaskant, J J
AU  - Maaskant JJ
FAU - Negrini, R
AU  - Negrini R
FAU - Lindh, F
AU  - Lindh F
FAU - Perry, M
AU  - Perry M
FAU - Del Giudice, G
AU  - Del Giudice G
FAU - Vandenbroucke-Grauls, C M
AU  - Vandenbroucke-Grauls CM
LA  - eng
PT  - Journal Article
PL  - United States
TA  - Infect Immun
JT  - Infection and immunity
JID - 0246127
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Epitopes)
RN  - 0 (Lewis Blood-Group System)
RN  - 0 (Lipopolysaccharides)
RN  - EC 2.4.1.- (Galactosyltransferases)
SB  - IM
EIN - Infect Immun 2000 Dec;68(12):7214
MH  - Antibodies, Monoclonal/immunology
MH  - Carbohydrate Sequence
MH  - *Epitopes
MH  - Galactosyltransferases/chemistry/genetics/metabolism
MH  - Helicobacter pylori/genetics/*immunology/metabolism
MH  - Humans
MH  - Lewis Blood-Group System/chemistry/*immunology
MH  - Lipopolysaccharides/chemistry/*classification/*immunology
MH  - Molecular Sequence Data
MH  - Mutagenesis, Insertional
MH  - Polymerase Chain Reaction
MH  - Sequence Analysis, DNA
PMC - PMC101556
EDAT- 2000/09/19 11:00
MHDA- 2001/02/28 10:01
CRDT- 2000/09/19 11:00
PHST- 2000/09/19 11:00 [pubmed]
PHST- 2001/02/28 10:01 [medline]
PHST- 2000/09/19 11:00 [entrez]
AID - 10.1128/iai.68.10.5928-5932.2000 [doi]
PST - ppublish
SO  - Infect Immun. 2000 Oct;68(10):5928-32. doi: 10.1128/iai.68.10.5928-5932.2000.

PMID- 15505370
OWN - NLM
STAT- MEDLINE
DCOM- 20050321
LR  - 20061115
IS  - 1387-2877 (Print)
IS  - 1387-2877 (Linking)
VI  - 6
IP  - 5
DP  - 2004 Oct
TI  - The potential role of tau protein O-glycosylation in Alzheimer's disease.
PG  - 489-95
AB  - Single O-linked N-acetylglucosamine (O-GlcNAc) sugar residues can compete with
      phosphate groups to occupy specific sites on certain nuclear and cytosolic
      proteins. Here we show that inhibiting cellular kinase activities resulted in
      changes in protein O-glycosylation levels in heat-stable cytoskeletal protein
      fractions derived from primary neuronal cells. As increased phosphorylation of
      the microtubule-associated protein tau is one of the pathological hallmarks of
      Alzheimer's disease and glycosylation may play an influential role in this
      process. We observed a significant decrease in the protein O-GlcNAc glycosylation
      of a tau-enriched cytoskeletal fraction generated from AD post-mortem brain
      samples as compared with control, suggesting an inverse relationship between the 
      two post-translational modifications. Finally, cells transfected with the cDNA
      coding for O-GlcNAc transferase (OGT) displayed altered tau phosphorylation
      patterns as compared with control cells, suggesting that changes in tau
      glycosylation may influence its phosphorylation state. The specificity of the
      changes in the phosphorylation of individual amino acid residues provides
      evidence for a targeted O-glycosylation of tau.
FAU - Robertson, Laura A
AU  - Robertson LA
AD  - Alzheimer's Disease Research Centre, Division of Pathology and Neuroscience,
      University of Dundee Medical School, Ninewells Hospital, Dundee DD1 9SY, UK.
FAU - Moya, Kenneth L
AU  - Moya KL
FAU - Breen, Kieran C
AU  - Breen KC
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - Netherlands
TA  - J Alzheimers Dis
JT  - Journal of Alzheimer's disease : JAD
JID - 9814863
RN  - 0 (MAPT protein, human)
RN  - 0 (Nerve Tissue Proteins)
RN  - 0 (tau Proteins)
SB  - IM
MH  - Aged
MH  - Alzheimer Disease/*metabolism/pathology
MH  - Blotting, Western
MH  - Dementia/metabolism
MH  - Frontal Lobe/metabolism/pathology
MH  - *Glycosylation
MH  - Humans
MH  - Nerve Tissue Proteins/*metabolism
MH  - Neurofibrillary Tangles/metabolism/pathology
MH  - Sensitivity and Specificity
MH  - Temporal Lobe/metabolism/pathology
MH  - tau Proteins
EDAT- 2004/10/27 09:00
MHDA- 2005/03/22 09:00
CRDT- 2004/10/27 09:00
PHST- 2004/10/27 09:00 [pubmed]
PHST- 2005/03/22 09:00 [medline]
PHST- 2004/10/27 09:00 [entrez]
PST - ppublish
SO  - J Alzheimers Dis. 2004 Oct;6(5):489-95.

PMID- 21999536
OWN - NLM
STAT- MEDLINE
DCOM- 20120203
LR  - 20111017
IS  - 1608-3040 (Electronic)
IS  - 0006-2979 (Linking)
VI  - 76
IP  - 7
DP  - 2011 Jul
TI  - Structural diversity of the core oligosaccharide domain of Pseudomonas aeruginosa
      lipopolysaccharide.
PG  - 755-60
LID - 10.1134/S0006297911070054 [doi]
AB  - Pseudomonas aeruginosa is a Gram-negative bacterium that is ubiquitous in the
      environment and generally considered to be a saprophyte, but it is also an
      important opportunistic human pathogen. Pseudomonas aeruginosa elaborates a
      variety of virulence factors, one of which is lipopolysaccharide (LPS). LPS of P.
      aeruginosa is composed of three distinct regions: lipid A, core oligosaccharide
      (OS), and the long-chain O antigen. The core OS of P. aeruginosa is composed of
      L-glycero-D-manno-heptose, 3-deoxy-D-manno-oct-2-ulosonic acid, D-galactosamine, 
      D-glucose, and L-rhamnose. Non-carbohydrate substituents are also found in the
      core OS including phosphate, 2-aminoethyl (di)phosphate, acetyl, alanyl and
      carbamoyl groups. Pseudomonas aeruginosa simultaneously synthesizes two core
      glycoforms, namely, capped and uncapped core. The capped core is covalently
      attached to an O antigen, whereas the uncapped core is devoid of O antigen.
      Although the core of P. aeruginosa LPS is relatively conserved, strain-to-strain 
      variability of its structure exists. This includes phosphorylation pattern, the
      level of O-acetylation, and the presence or absence of a fourth glucose residue
      at the distal end of the uncapped core. A number of studies have been reported on
      the structures of unique truncated core OS with unusual modifications. This
      mini-review summarizes the diversity of P. aeruginosa complete and truncated core
      OS structures published over the past fifteen years.
FAU - Kocincova, D
AU  - Kocincova D
AD  - Department of Molecular and Cellular Biology, University of Guelph, Ontario,
      Canada.
FAU - Lam, J S
AU  - Lam JS
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Review
PL  - United States
TA  - Biochemistry (Mosc)
JT  - Biochemistry. Biokhimiia
JID - 0376536
RN  - 0 (Lipid A)
RN  - 0 (Lipopolysaccharides)
RN  - 0 (O Antigens)
RN  - 0 (Oligosaccharides)
SB  - IM
MH  - Acetylation
MH  - Carbohydrate Sequence
MH  - Lipid A
MH  - Lipopolysaccharides/*chemistry
MH  - Molecular Sequence Data
MH  - O Antigens
MH  - Oligosaccharides/*chemistry/genetics
MH  - Phosphorylation
MH  - Pseudomonas aeruginosa/*chemistry/genetics
EDAT- 2011/10/18 06:00
MHDA- 2012/02/04 06:00
CRDT- 2011/10/18 06:00
PHST- 2011/10/18 06:00 [entrez]
PHST- 2011/10/18 06:00 [pubmed]
PHST- 2012/02/04 06:00 [medline]
AID - BCM76070925 [pii]
AID - 10.1134/S0006297911070054 [doi]
PST - ppublish
SO  - Biochemistry (Mosc). 2011 Jul;76(7):755-60. doi: 10.1134/S0006297911070054.

PMID- 14736333
OWN - NLM
STAT- MEDLINE
DCOM- 20040907
LR  - 20181113
IS  - 1470-8728 (Electronic)
IS  - 0264-6021 (Linking)
VI  - 379
IP  - Pt 3
DP  - 2004 May 1
TI  - Rhesus monkey gastric mucins: oligomeric structure, glycoforms and Helicobacter
      pylori binding.
PG  - 765-75
AB  - Mucins isolated from the stomach of Rhesus monkey are oligomeric glycoproteins
      with a similar mass, density, glycoform profile and tissue localization as human 
      MUC5AC and MUC6. Antibodies raised against the human mucins recognize those from 
      monkey, which thus appear to be orthologous to those from human beings. Rhesus
      monkey muc5ac and muc6 are produced by the gastric-surface epithelium and glands 
      respectively, and occur as three distinct glycoforms. The mucins are substituted 
      with the histo blood-group antigens B, Le(a) (Lewis a), Le(b), Le(x), Le(y),
      H-type-2, the Tn-antigen, the T-antigen, the sialyl-Le(x) and sialyl-Le(a)
      structures, and the expression of these determinants varies between individuals. 
      At neutral pH, Helicobacter pylori strains expressing BabA (blood-group
      antigen-binding adhesin) bind Rhesus monkey gastric mucins via the Le(b) or
      H-type-1 structures, apparently on muc5ac, as well as on a smaller putative
      mucin, and binding is inhibited by Le(b) or H-type-1 conjugates. A SabA (sialic
      acid-binding adhesin)-positive H. pylori mutant binds to sialyl-Le(x)-positive
      mucins to a smaller extent compared with the BabA-positive strains. At acidic pH,
      the microbe binds to mucins substituted by sialylated structures such as
      sialyl-Le(x) and sialylated type-2 core, and this binding is inhibited by DNA and
      dextran sulphate. Thus mucin- H. pylori binding occurs via at least three
      different mechanisms: (1) BabA-dependent binding to Le(b) and related structures,
      (2) SabA-dependent binding to sialyl-Le(x) and (3) binding through a
      charge-mediated mechanism to sialylated structures at low pH values.
FAU - Linden, Sara
AU  - Linden S
AD  - Mucosal Biology Group, Department of Cell and Molecular Biology, Biomedical
      Center, Lund University, SE-22184 Lund, Sweden.
FAU - Boren, Thomas
AU  - Boren T
FAU - Dubois, Andre
AU  - Dubois A
FAU - Carlstedt, Ingemar
AU  - Carlstedt I
LA  - eng
GR  - R01 CA082312/CA/NCI NIH HHS/United States
GR  - R01 CA082312-08/CA/NCI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - Biochem J
JT  - The Biochemical journal
JID - 2984726R
RN  - 0 (Lewis Blood-Group System)
RN  - 0 (Mucins)
RN  - 0 (Protein Isoforms)
RN  - 0 (Protein Subunits)
SB  - IM
MH  - Animals
MH  - Centrifugation, Density Gradient
MH  - Helicobacter pylori/*metabolism
MH  - Hydrogen-Ion Concentration
MH  - Lewis Blood-Group System/metabolism
MH  - *Macaca mulatta
MH  - Molecular Weight
MH  - Mucins/analysis/*chemistry/*metabolism
MH  - Organ Specificity
MH  - Protein Binding
MH  - Protein Isoforms/chemistry/metabolism
MH  - Protein Structure, Quaternary
MH  - Protein Subunits/chemistry/metabolism
MH  - Solubility
MH  - Stomach/*chemistry
PMC - PMC1224112
EDAT- 2004/01/23 05:00
MHDA- 2004/09/08 05:00
CRDT- 2004/01/23 05:00
PHST- 2004/01/15 00:00 [accepted]
PHST- 2003/12/23 00:00 [revised]
PHST- 2003/10/10 00:00 [received]
PHST- 2004/01/23 05:00 [pubmed]
PHST- 2004/09/08 05:00 [medline]
PHST- 2004/01/23 05:00 [entrez]
AID - 10.1042/BJ20031557 [doi]
AID - BJ20031557 [pii]
PST - ppublish
SO  - Biochem J. 2004 May 1;379(Pt 3):765-75. doi: 10.1042/BJ20031557.

PMID- 1918047
OWN - NLM
STAT- MEDLINE
DCOM- 19911114
LR  - 20071114
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 266
IP  - 29
DP  - 1991 Oct 15
TI  - The structural basis for pyocin resistance in Neisseria gonorrhoeae
      lipooligosaccharides.
PG  - 19303-11
AB  - Pyocin resistance in a strain of Neisseria gonorrhoeae has been found to be
      associated with structural differences in the oligosaccharide moieties of the
      gonococcal outer membrane lipooligosaccharides (LOS). N. gonorrhoeae strain 1291 
      had been treated with several pyocins, usually lethal bacteriocins produced by
      Pseudomonas aeruginosa, and a series of surviving mutants were selected. The LOS 
      of these pyocin-resistant mutants had altered electrophoretic mobilities in
      sodium dodecyl sulfate-polyacrylamide gels (Dudas, K. C., and Apicella, M. A.
      (1988) Infect. Immun. 56, 499-504). Structural analyses of the oligosaccharide
      portions of the wild-type (1291 wt) and five pyocin-resistant strains (1291a-e)
      by liquid secondary ion mass spectrometry, tandem mass spectrometry, and
      methylation analysis revealed that four of the mutant strains make
      oligosaccharides that differ from the wild-type LOS by successive saccharide
      deletions (1291a,c-e) and, in the oligosaccharide of 1291b, by the addition of a 
      terminal Gal to the 1291c structure. The composition, sequence, and linkages of
      the terminal tetrasaccharide of the wild-type LOS are the same as the
      lacto-N-neotetraose terminus of the human paragloboside (Gal beta 1----4GlcNAc
      beta 1----3Gal beta 1----4Glc-ceramide), and both glycolipids bound the same
      monoclonal antibodies O6B4/3F11 that recognize this terminal epitope. None of the
      pyocin-resistant mutants bound this antibody. The 1291b LOS bound a monoclonal
      antibody that is specific for Gal alpha 1----4Gal beta 1----4Glc-ceramide (Pk
      glycosphingolipid) and shared a common composition, sequence, and linkages with
      this latter glycosphingolipid. Organisms that bound the anti-Pk monoclone
      occurred at the rate of approximately 1/750 among the wild-type parent strain.
      This structural information supports the conclusion that treatment with pyocin
      selects for mutants with truncated LOS structures and suggests that the
      oligosaccharides contained in the LOS of the wild-type strain and 1291b mimic
      those of human glycosphingolipids.
FAU - John, C M
AU  - John CM
AD  - Department of Pharmaceutical Chemistry, University of California, San Francisco
      94143.
FAU - Griffiss, J M
AU  - Griffiss JM
FAU - Apicella, M A
AU  - Apicella MA
FAU - Mandrell, R E
AU  - Mandrell RE
FAU - Gibson, B W
AU  - Gibson BW
LA  - eng
GR  - AI21620/AI/NIAID NIH HHS/United States
GR  - AI24616/AI/NIAID NIH HHS/United States
GR  - AI8384/AI/NIAID NIH HHS/United States
GR  - etc.
PT  - Journal Article
PT  - Research Support, U.S. Gov't, Non-P.H.S.
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Ions)
RN  - 0 (Lipopolysaccharides)
RN  - 0 (Pyocins)
SB  - IM
MH  - Carbohydrate Sequence
MH  - Chromatography, High Pressure Liquid
MH  - *Drug Resistance, Microbial
MH  - Electrophoresis, Polyacrylamide Gel
MH  - Genes, Bacterial
MH  - Ions
MH  - Lipopolysaccharides/*metabolism
MH  - Mass Spectrometry
MH  - Methylation
MH  - Molecular Sequence Data
MH  - Mutation
MH  - Neisseria gonorrhoeae/*drug effects/genetics/metabolism
MH  - Pseudomonas aeruginosa/metabolism
MH  - Pyocins/*pharmacology
MH  - Radioimmunoassay
EDAT- 1991/10/15 00:00
MHDA- 1991/10/15 00:01
CRDT- 1991/10/15 00:00
PHST- 1991/10/15 00:00 [pubmed]
PHST- 1991/10/15 00:01 [medline]
PHST- 1991/10/15 00:00 [entrez]
PST - ppublish
SO  - J Biol Chem. 1991 Oct 15;266(29):19303-11.

PMID- 9250810
OWN - NLM
STAT- MEDLINE
DCOM- 19970924
LR  - 20190116
IS  - 1042-8194 (Print)
IS  - 1026-8022 (Linking)
VI  - 25
IP  - 5-6
DP  - 1997 May
TI  - Expression of sialosyl-T and disialosyl-T antigens in erythroid cells.
PG  - 403-14
AB  - Expression of T, sialosyl-T and disialosyl-T antigens on normal blood and bone
      marrow cells as well as transformed cells was examined using specific monoclonal 
      antibodies and multidimensional flow cytometry. Both anti-sialosyl-T (QSH1) and
      anti-disialosyl-T (QSH2) monoclonal antibodies aggregated erythrocytes. The
      anti-disialosyl-T antibody was specific for the erythroid lineage and did not
      react with neutrophils, monocytes or T-lymphocytes, while the anti-sialosyl-T
      antibody reacted with erythroid cells and a subset of T-lymphocytes. The
      developing erythroid cells in bone marrow showed coordinate expression of
      glycophorin A and the two carbohydrate chains, sialosyl-T and disialosyl-T.
      Analysis of neoplastic cells showed that the anti-disialosyl-T antibody only
      reacted with glycophorin A-positive blasts from erythroleukemia (FAB M6) patients
      (4/4) and one patient with chronic myeloid leukemia in erythroblastic
      transformation (CMLET). Leukemic blasts from these patients demonstrated
      coordinate quantitative expression of glycophorin A and disialosyl-T. The
      anti-sialosyl-T antibody reacted with glycophorin A-positive blasts from FAB M6
      patients (4/4) and one CMLET patient; however, the antibody also reacted with
      glycophorin A-negative blasts from one FAB M6 and the one CMLET patients and
      transformed cells from other types of leukemia. The anti-T monoclonal antibody
      (HH8) did not react with any of the other cells tested. These results indicate
      that glycophorin A and disialosyl-T expression are tightly linked during normal
      erythroid development and erythroid leukemogenesis.
FAU - Muroi, K
AU  - Muroi K
AD  - Division of Transfusion Medicine, Jichi Medical School, Minamikawachi-machi,
      Tochigi-ken, Japan.
FAU - Amemiya, Y
AU  - Amemiya Y
FAU - Sievers, E L
AU  - Sievers EL
FAU - Miura, Y
AU  - Miura Y
FAU - Hakamori, S I
AU  - Hakamori SI
FAU - Loken, M R
AU  - Loken MR
LA  - eng
GR  - CA42505/CA/NCI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PT  - Review
PL  - United States
TA  - Leuk Lymphoma
JT  - Leukemia & lymphoma
JID - 9007422
RN  - 0 (Antigens, Surface)
RN  - 0 (Glycophorin)
RN  - 0 (Mucins)
RN  - 0 (Oligosaccharides)
RN  - 0 (disialosyl-T antigen, human)
RN  - 0 (sialosyl-T antigen)
SB  - IM
MH  - Antigens, Surface/blood/*metabolism
MH  - Carbohydrate Sequence
MH  - Erythrocytes/*metabolism
MH  - Glycophorin/metabolism
MH  - Humans
MH  - Leukemia/blood/*metabolism
MH  - Molecular Sequence Data
MH  - Mucins/blood/*metabolism
MH  - Oligosaccharides/blood/*metabolism
RF  - 31
EDAT- 1997/05/01 00:00
MHDA- 1997/05/01 00:01
CRDT- 1997/05/01 00:00
PHST- 1997/05/01 00:00 [pubmed]
PHST- 1997/05/01 00:01 [medline]
PHST- 1997/05/01 00:00 [entrez]
AID - 10.3109/10428199709039027 [doi]
PST - ppublish
SO  - Leuk Lymphoma. 1997 May;25(5-6):403-14. doi: 10.3109/10428199709039027.

PMID- 6576183
OWN - NLM
STAT- MEDLINE
DCOM- 19830923
LR  - 20071114
IS  - 0027-8874 (Print)
IS  - 0027-8874 (Linking)
VI  - 71
IP  - 2
DP  - 1983 Aug
TI  - Glycosphingolipids as tumor-associated and differentiation markers.
PG  - 231-51
FAU - Hakomori, S
AU  - Hakomori S
FAU - Kannagi, R
AU  - Kannagi R
LA  - eng
GR  - CA-19224/CA/NCI NIH HHS/United States
GR  - CA-20026/CA/NCI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - J Natl Cancer Inst
JT  - Journal of the National Cancer Institute
JID - 7503089
RN  - 0 (Antigens, Neoplasm)
RN  - 0 (Blood Group Antigens)
RN  - 0 (Glycosphingolipids)
RN  - 0 (Membrane Lipids)
SB  - IM
MH  - Animals
MH  - Antigens, Neoplasm/analysis
MH  - Blood Group Antigens/immunology
MH  - Carbohydrate Conformation
MH  - Carbohydrate Sequence
MH  - Cell Line
MH  - *Cell Transformation, Neoplastic
MH  - Glycosphingolipids/*analysis/biosynthesis
MH  - Humans
MH  - Membrane Lipids/analysis
MH  - Neoplasm Metastasis
MH  - Neoplasms/*analysis/immunology/physiopathology
MH  - Oncogenes
EDAT- 1983/08/01 00:00
MHDA- 1983/08/01 00:01
CRDT- 1983/08/01 00:00
PHST- 1983/08/01 00:00 [pubmed]
PHST- 1983/08/01 00:01 [medline]
PHST- 1983/08/01 00:00 [entrez]
PST - ppublish
SO  - J Natl Cancer Inst. 1983 Aug;71(2):231-51.

PMID- 10491405
OWN - NLM
STAT- MEDLINE
DCOM- 19991013
LR  - 20181113
IS  - 0021-9738 (Print)
IS  - 0021-9738 (Linking)
VI  - 104
IP  - 6
DP  - 1999 Sep
TI  - Monoclonal antibodies raised against Guillain-Barre syndrome-associated
      Campylobacter jejuni lipopolysaccharides react with neuronal gangliosides and
      paralyze muscle-nerve preparations.
PG  - 697-708
AB  - Guillain-Barre syndrome and its variant, Miller-Fisher syndrome, are acute,
      postinfectious, autoimmune neuropathies that frequently follow Campylobacter
      jejuni enteritis. The pathogenesis is believed to involve molecular mimicry
      between sialylated epitopes on C. jejuni LPSs and neural gangliosides. More than 
      90% of Miller-Fisher syndrome cases have serum anti-GQ1b and anti-GT1a
      ganglioside antibodies that may also react with other disialylated gangliosides
      including GD3 and GD1b. Structural studies on LPS from neuropathy-associated C.
      jejuni strains have revealed GT1a-like and GD3-like core oligosaccharides. To
      determine whether this structural mimicry results in pathogenic autoantibodies,
      we immunized mice with GT1a/GD3-like C. jejuni LPS and then cloned mAb's that
      reacted with both the immunizing LPS and GQ1b/GT1a/GD3 gangliosides.
      Immunohistology demonstrated antibody binding to ganglioside-rich sites including
      motor nerve terminals. In ex vivo electrophysiological studies of nerve terminal 
      function, application of antibodies either ex vivo or in vivo via passive
      immunization induced massive quantal release of acetylcholine, followed by
      neurotransmission block. This effect was complement-dependent and associated with
      extensive deposits of IgM and C3c at nerve terminals. These data provide strong
      support for the molecular mimicry hypothesis as a mechanism for the induction of 
      cross-reactive pathogenic anti-ganglioside/LPS antibodies in postinfectious
      neuropathies.
FAU - Goodyear, C S
AU  - Goodyear CS
AD  - University Department of Neurology, Southern General Hospital, Glasgow G51 4TF,
      Scotland.
FAU - O'Hanlon, G M
AU  - O'Hanlon GM
FAU - Plomp, J J
AU  - Plomp JJ
FAU - Wagner, E R
AU  - Wagner ER
FAU - Morrison, I
AU  - Morrison I
FAU - Veitch, J
AU  - Veitch J
FAU - Cochrane, L
AU  - Cochrane L
FAU - Bullens, R W
AU  - Bullens RW
FAU - Molenaar, P C
AU  - Molenaar PC
FAU - Conner, J
AU  - Conner J
FAU - Willison, H J
AU  - Willison HJ
LA  - eng
GR  - Wellcome Trust/United Kingdom
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - J Clin Invest
JT  - The Journal of clinical investigation
JID - 7802877
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Complement C3)
RN  - 0 (Gangliosides)
RN  - 0 (Immunoglobulin M)
RN  - 0 (Lipopolysaccharides)
SB  - AIM
SB  - IM
EIN - J Clin Invest 1999 Dec;104(12):1771
MH  - Animals
MH  - Antibodies, Monoclonal/*immunology
MH  - Campylobacter jejuni/*immunology
MH  - Complement C3/physiology
MH  - Cross Reactions
MH  - Female
MH  - Gangliosides/*immunology
MH  - Immunization
MH  - Immunoglobulin M/immunology
MH  - Lipopolysaccharides/*immunology
MH  - Male
MH  - Mice
MH  - Mice, Inbred Strains
MH  - Neuromuscular Junction/*physiology
MH  - Peripheral Nerves/immunology
MH  - Polyradiculoneuropathy/*microbiology
PMC - PMC408431
EDAT- 1999/09/24 09:00
MHDA- 2000/03/04 09:00
CRDT- 1999/09/24 09:00
PHST- 1999/09/24 09:00 [pubmed]
PHST- 2000/03/04 09:00 [medline]
PHST- 1999/09/24 09:00 [entrez]
AID - 10.1172/JCI6837 [doi]
PST - ppublish
SO  - J Clin Invest. 1999 Sep;104(6):697-708. doi: 10.1172/JCI6837.

PMID- 3571288
OWN - NLM
STAT- MEDLINE
DCOM- 19870619
LR  - 20151119
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 262
IP  - 14
DP  - 1987 May 15
TI  - Monoclonal antibody detects monosialogangliosides having a sialic acid alpha
      2----3-galactosyl residue.
PG  - 6803-7
AB  - A murine monoclonal antibody (mAb), designated mAb 202, was generated using a
      human melanoma cell line, UCLASO-M14 as the immunogen. mAb 202 reacted with two
      (GM2 and GM3) of the four (GM2, GM3, GD2, and GD3) gangliosides expressed by M14.
      Several authentic monosialogangliosides, including GM4, GM3, GM2, GM1, GM1b, and 
      sialylparagloboside were then tested for their binding to 202 mAb by the immune
      adherence inhibition assay, TLC-enzyme immunostaining, and enzyme-linked
      immunosorbent assay. All showed positive binding but in varying degrees. GM4
      showed the strongest affinity. No significant differences of reactivity were
      observed between the sialic acid derivatives, N-acetyl and N-glycolyl, in these
      gangliosides. Disialogangliosides such as GD3, GD2, GD1a, and GD1b,
      trisialoganglioside GT1b, and neutral glycolipids including GlcCer, GalCer,
      LacCer, GbOs3Cer, GbOs4Cer, GgOs3Cer, GgOs4Cer, and nLcOs4Cer were all negative. 
      These results indicate that the 202 mAb detects sialyl alpha 2----3Gal residue in
      the monosialoganglioside, irrespective of the internal structure. Since GM4 is
      not expressed by M14 cells, the terminal disaccharide (sialyl alpha 2----3Gal) in
      GM3 and/or GM2 must have been the epitope responsible for the generation of the
      antibody.
FAU - Tai, T
AU  - Tai T
FAU - Sze, L
AU  - Sze L
FAU - Kawashima, I
AU  - Kawashima I
FAU - Saxton, R E
AU  - Saxton RE
FAU - Irie, R F
AU  - Irie RF
LA  - eng
GR  - CA12582/CA/NCI NIH HHS/United States
GR  - CA30647/CA/NCI NIH HHS/United States
GR  - CA42396/CA/NCI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Gangliosides)
RN  - 0 (sialogangliosides)
RN  - X2RN3Q8DNE (Galactose)
SB  - IM
MH  - *Antibodies, Monoclonal
MH  - Carbohydrate Conformation
MH  - Carbohydrate Sequence
MH  - Cell Line
MH  - Galactose/*analysis
MH  - Gangliosides/*analysis
MH  - Humans
MH  - Melanoma
EDAT- 1987/05/15 00:00
MHDA- 1987/05/15 00:01
CRDT- 1987/05/15 00:00
PHST- 1987/05/15 00:00 [pubmed]
PHST- 1987/05/15 00:01 [medline]
PHST- 1987/05/15 00:00 [entrez]
PST - ppublish
SO  - J Biol Chem. 1987 May 15;262(14):6803-7.

PMID- 687374
OWN - NLM
STAT- MEDLINE
DCOM- 19781027
LR  - 20190501
IS  - 0264-6021 (Print)
IS  - 0264-6021 (Linking)
VI  - 173
IP  - 1
DP  - 1978 Jul 1
TI  - Blood-group-I activity associated with band 3, the major intrinsic membrane
      protein of human erythrocytes.
PG  - 333-6
AB  - Affinity chromatography of radioiodinated solubilized erythrocyte stroma and of
      radioiodinated purified Band 3 on an anti-(blood-group I)-adsorbent column showed
      blood-group-I activity associated with a subpopulation of Band 3. The specificity
      of binding was confirmed by inhibition with known blood-group substances in
      radioimmunoassays.
FAU - Childs, R A
AU  - Childs RA
FAU - Feizi, T
AU  - Feizi T
FAU - Fukuda, M
AU  - Fukuda M
FAU - Hakomori, S I
AU  - Hakomori SI
LA  - eng
PT  - Journal Article
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - England
TA  - Biochem J
JT  - The Biochemical journal
JID - 2984726R
RN  - 0 (Blood Group Antigens)
RN  - 0 (I Blood-Group System)
RN  - 0 (Membrane Proteins)
SB  - IM
MH  - *Blood Group Antigens
MH  - Chromatography, Affinity
MH  - Electrophoresis, Polyacrylamide Gel
MH  - Erythrocyte Membrane/*immunology
MH  - Erythrocytes/*immunology
MH  - Humans
MH  - *I Blood-Group System
MH  - Membrane Proteins/*immunology
PMC - PMC1185778
EDAT- 1978/07/01 00:00
MHDA- 1978/07/01 00:01
CRDT- 1978/07/01 00:00
PHST- 1978/07/01 00:00 [pubmed]
PHST- 1978/07/01 00:01 [medline]
PHST- 1978/07/01 00:00 [entrez]
AID - 10.1042/bj1730333 [doi]
PST - ppublish
SO  - Biochem J. 1978 Jul 1;173(1):333-6. doi: 10.1042/bj1730333.

PMID- 9298690
OWN - NLM
STAT- MEDLINE
DCOM- 19971215
LR  - 20181113
IS  - 0282-0080 (Print)
IS  - 0282-0080 (Linking)
VI  - 14
IP  - 5
DP  - 1997 Aug
TI  - Carbohydrate-mediated cell adhesion involved in hematogenous metastasis of
      cancer.
PG  - 577-84
AB  - The carbohydrate determinants, sialyl Lewis A and sialyl Lewis X, which are
      frequently expressed on human cancer cells, serve as ligands for a cell adhesion 
      molecule of the selectin family, E-selectin, which is expressed on vascular
      endothelial cells. These carbohydrate determinants are involved in the adhesion
      of cancer cells to vascular endothelium and thus contribute to hematogenous
      metastasis of cancer. The initial adhesion mediated by these molecules triggers
      activation of integrin molecules through the action of several cytokines and
      leads to the extravasation of cancer cells. Cancer cells also produce humoral
      factors that facilitate E-selectin expression on endothelial cells. The degree of
      expression of the carbohydrate ligands at the surface of cancer cells is well
      correlated with the frequency of hematogenous metastasis and prognostic outcome
      of patients with cancers. The alteration of glycosyltransferase activities that
      leads to the enhanced expression of these carbohydrate ligands on cancer cell
      surface are currently being investigated.
FAU - Kannagi, R
AU  - Kannagi R
AD  - Molecular Pathology, Aichi Cancer Center, Nagoya, Japan.
LA  - eng
PT  - Journal Article
PT  - Review
PL  - United States
TA  - Glycoconj J
JT  - Glycoconjugate journal
JID - 8603310
RN  - 0
      (5-acetylneuraminyl-(2-3)-galactosyl-(1-4)-(fucopyranosyl-(1-3))-N-acetylglucosam
      ine)
RN  - 0 (Biomarkers, Tumor)
RN  - 0 (E-Selectin)
RN  - 0 (Lewis X Antigen)
RN  - 0 (Oligosaccharides)
RN  - 0 (P-Selectin)
RN  - 117978-16-2 (sialyl-Le(a) oligosaccharide)
RN  - EC 2.4.- (Glycosyltransferases)
SB  - IM
MH  - Animals
MH  - Biomarkers, Tumor
MH  - *Cell Adhesion
MH  - E-Selectin/*physiology
MH  - Glycosyltransferases/metabolism
MH  - Humans
MH  - Lewis X Antigen/*physiology
MH  - Models, Biological
MH  - Neoplasm Metastasis/*pathology/*physiopathology
MH  - Neoplasms/*pathology/*physiopathology
MH  - Oligosaccharides/*metabolism
MH  - P-Selectin/physiology
MH  - Prognosis
RF  - 56
EDAT- 1997/08/01 00:00
MHDA- 1997/09/23 00:01
CRDT- 1997/08/01 00:00
PHST- 1997/08/01 00:00 [pubmed]
PHST- 1997/09/23 00:01 [medline]
PHST- 1997/08/01 00:00 [entrez]
PST - ppublish
SO  - Glycoconj J. 1997 Aug;14(5):577-84.

PMID- 2716059
OWN - NLM
STAT- MEDLINE
DCOM- 19890619
LR  - 20131121
IS  - 0022-2836 (Print)
IS  - 0022-2836 (Linking)
VI  - 206
IP  - 3
DP  - 1989 Apr 5
TI  - X-ray crystal structure of the blue oxidase ascorbate oxidase from zucchini.
      Analysis of the polypeptide fold and a model of the copper sites and ligands.
PG  - 513-29
AB  - Two crystal forms of the multi-copper protein ascorbate oxidase from Zucchini
      have been analysed at 2.5 A (1 A = 0.1 nm) resolution and a model of the
      polypeptide chain and the copper ions and their ligands has been built. Crystal
      forms M2 and M1 contain a dimer of 140,000 Mr and a tetramer of 280,000 Mr,
      respectively, in the asymmetric unit. The crystallographic analysis proceeded by 
      multiple isomorphous replacement in M2 followed by solvent flattening and
      averaging about the local dyad axis. M1 was solved by Patterson search techniques
      using the M2 electron density. M1 was fourfold averaged. M1 and M2 were combined 
      and the process of averaging repeated in cycles. An atomic model was built into
      the resulting electron density map and refinement initiated. The current R values
      of M2 and M1 are 24.5% and 32.6%, respectively. Excellent stereo chemistry was
      maintained, with root-mean-square deviations of bond lengths and bond angles from
      average values of 0.02 A and 3.1 degrees, respectively. Each subunit of about 550
      amino acid residues has a globular shape with dimensions of 49 A x 53 A x 65 A.
      It is built up by three domains arranged sequentially on the polypeptide chain
      and tightly associated in space. The folding of all three domains is of a similar
      beta-barrel type. It is distantly related to plastocyanin. Each subunit has four 
      copper atoms bound as mononuclear and trinuclear species. The mononuclear copper 
      has two histidine, a cysteine, and a methionine ligand and represents the type-1 
      copper. It is located in the third domain. The trinuclear cluster has eight
      histidine ligands. It may be subdivided into a pair of copper atoms with six
      histidine ligands arranged trigonal prismatic. The pair probably represents the
      type-3 copper. The remaining copper has two histidine ligands. Its third site of 
      co-ordination is formed by the pair of copper atoms. The fourth ligand may be OH-
      represented by a small protrusion of electron density. This copper probably is
      the type-2 copper. The symmetry of the trinuclear cluster is C2 and the ligands
      are supplied symmetrically by domains 1 and 3. However, domain 1 does not contain
      a type-1 copper and lacks the characteristic ligands. The unprecedented
      trinuclear cluster probably represents the oxygen binding and electron storage
      site.
FAU - Messerschmidt, A
AU  - Messerschmidt A
AD  - Max-Planck-Institut fuer Biochemie, Martinsried, BRD.
FAU - Rossi, A
AU  - Rossi A
FAU - Ladenstein, R
AU  - Ladenstein R
FAU - Huber, R
AU  - Huber R
FAU - Bolognesi, M
AU  - Bolognesi M
FAU - Gatti, G
AU  - Gatti G
FAU - Marchesini, A
AU  - Marchesini A
FAU - Petruzzelli, R
AU  - Petruzzelli R
FAU - Finazzi-Agro, A
AU  - Finazzi-Agro A
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - J Mol Biol
JT  - Journal of molecular biology
JID - 2985088R
RN  - 0 (Ligands)
RN  - 0 (Peptides)
RN  - 789U1901C5 (Copper)
RN  - EC 1.- (Oxidoreductases)
RN  - EC 1.10.3.3 (Ascorbate Oxidase)
SB  - IM
MH  - *Ascorbate Oxidase
MH  - Binding Sites
MH  - *Copper
MH  - Ligands
MH  - Models, Molecular
MH  - Molecular Conformation
MH  - *Oxidoreductases
MH  - Peptides
MH  - Plants/enzymology
MH  - X-Ray Diffraction
EDAT- 1989/04/05 00:00
MHDA- 1989/04/05 00:01
CRDT- 1989/04/05 00:00
PHST- 1989/04/05 00:00 [pubmed]
PHST- 1989/04/05 00:01 [medline]
PHST- 1989/04/05 00:00 [entrez]
AID - 0022-2836(89)90498-1 [pii]
PST - ppublish
SO  - J Mol Biol. 1989 Apr 5;206(3):513-29.

PMID- 7846011
OWN - NLM
STAT- MEDLINE
DCOM- 19950308
LR  - 20151119
IS  - 0885-3177 (Print)
IS  - 0885-3177 (Linking)
VI  - 9
IP  - 6
DP  - 1994 Nov
TI  - Blood-group sialyl-Tn antigen is more specific than Tn as a tumor marker in the
      pancreas.
PG  - 698-702
AB  - The aim of this study was to evaluate the expression of blood group Tn and
      sialyl-Tn antigens in the pancreas to determine whether they could help to
      interpret histochemically needle biopsies obtained from the pancreas. Lectin and 
      immunohistochemistry was carried out using the biotin-labeled Vicia villosa
      agglutinin isolectin B4 and the mouse monoclonal antibody MLS102 to detect the Tn
      and sialyl-Tn blood-group antigens in the pancreas. All the pancreatic ductal
      adenocarcinomas (11/11) were positively stained by V. villosa agglutinin and
      MLS102 monoclonal antibody. None of the normals or chronic pancreatitics bound
      MLS102 monoclonal antibody. The acini of all the normals and chronic
      pancreatitics were V. villosa agglutinin positive, which was absent in the normal
      ductal cells and present only sparingly in the chronic pancreatitis ductal
      tissues (10/16). Thus, both the Tn and the sialyl-Tn blood-group antigens are
      present in pancreatic ductal tissues that have undergone malignant
      transformation. MLS102 is superior to V. villosa agglutinin in distinguishing
      malignant from normal and nonmalignant pancreatic tissues in needle biopsies.
FAU - Ching, C K
AU  - Ching CK
AD  - Medical Research Center, City Hospital, Nottingham, England.
FAU - Holmes, S W
AU  - Holmes SW
FAU - Holmes, G K
AU  - Holmes GK
FAU - Long, R G
AU  - Long RG
LA  - eng
PT  - Journal Article
PL  - United States
TA  - Pancreas
JT  - Pancreas
JID - 8608542
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Biomarkers, Tumor)
RN  - 0 (Lectins)
RN  - 0 (Plant Lectins)
RN  - 0 (Tn antigen)
RN  - 0 (Vicia lectins)
RN  - 0 (sialosyl-Tn antigen)
SB  - IM
MH  - Adenocarcinoma/*chemistry/pathology
MH  - Antibodies, Monoclonal/analysis/immunology
MH  - Antigens, Tumor-Associated, Carbohydrate/*analysis
MH  - Biomarkers, Tumor/*analysis
MH  - Biopsy, Needle
MH  - Chronic Disease
MH  - Humans
MH  - Immunohistochemistry
MH  - Lectins/analysis/immunology
MH  - Pancreas/chemistry
MH  - Pancreatic Neoplasms/*chemistry/pathology
MH  - Pancreatitis/metabolism
MH  - *Plant Lectins
EDAT- 1994/11/01 00:00
MHDA- 1994/11/01 00:01
CRDT- 1994/11/01 00:00
PHST- 1994/11/01 00:00 [pubmed]
PHST- 1994/11/01 00:01 [medline]
PHST- 1994/11/01 00:00 [entrez]
PST - ppublish
SO  - Pancreas. 1994 Nov;9(6):698-702.

PMID- 9689340
OWN - NLM
STAT- MEDLINE
DCOM- 19981013
LR  - 20151119
IS  - 0105-4538 (Print)
IS  - 0105-4538 (Linking)
VI  - 53
IP  - 6
DP  - 1998 Jun
TI  - Arizona cypress (Cupressus arizonica) pollen allergens. Identification of
      cross-reactive periodate-resistant and -sensitive epitopes with monoclonal
      antibodies.
PG  - 586-93
AB  - Species of the Cupressaceae family are a worldwide cause of respiratory
      allergies. We used monoclonal antibodies (mAbs) to investigate the presence and
      the nature of cross-reacting epitopes shared by various components within
      Cupressus arizonica pollen extract (CaE) or by CaE and pollen extract from C.
      sempervirens (CsE). mAbs were produced in mice immunized with whole CaE (4A6 and 
      5E6) or with the major allergen components (2D5). Their reactivity was
      investigated by ELISA and immunoblotting before and after CaE periodate
      treatment. Cross-reactivity was evaluated by ELISA inhibition and immunoblotting.
      mAbs 2D5 and 4A6 recognized periodate-resistant epitopes, whereas the mAb 5E6
      reacted with a periodate-sensitive determinant. The former mAbs recognized
      epitopes present on CaE major allergen and also shared by other components. mAb
      5E6 showed a spread reactivity on CaE, with exclusion of the major allergen. When
      the three mAbs were tested with CsE, a restricted pattern of reactivity to mAbs
      2D5 and 4A6 was obtained, whereas mAb 5E6 maintained a spread reactivity. The CaE
      major allergen is represented by two components recognized by human IgE and
      sharing common epitopes, as proven by mAbs reactivity. The use of these mAbs
      demonstrates that cross-reactivity within CaE components and between CaE and CsE 
      is due to the presence of periodate-sensitive as well as -resistant epitopes.
FAU - Barletta, B
AU  - Barletta B
AD  - Department of Immunology, Istituto Superiore di Sanita, Rome, Italy.
FAU - Tinghino, R
AU  - Tinghino R
FAU - Corinti, S
AU  - Corinti S
FAU - Afferni, C
AU  - Afferni C
FAU - Iacovacci, P
AU  - Iacovacci P
FAU - Mari, A
AU  - Mari A
FAU - Pini, C
AU  - Pini C
FAU - Di Felice, G
AU  - Di Felice G
LA  - eng
PT  - Journal Article
PL  - Denmark
TA  - Allergy
JT  - Allergy
JID - 7804028
RN  - 0 (Allergens)
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Epitopes)
RN  - 0 (Mitogens)
RN  - 0 (Plant Proteins)
RN  - 10450-60-9 (Periodic Acid)
RN  - 55X04QC32I (Sodium Hydroxide)
RN  - B45A1BUM4Q (metaperiodate)
SB  - IM
MH  - Allergens/*immunology/*isolation & purification
MH  - Animals
MH  - Antibodies, Monoclonal/immunology
MH  - Cross Reactions/*immunology
MH  - Enzyme-Linked Immunosorbent Assay
MH  - Epitopes/*immunology
MH  - Humans
MH  - Immunoblotting
MH  - Mice
MH  - Mitogens/pharmacology
MH  - Periodic Acid/pharmacology
MH  - Plant Proteins/drug effects/immunology
MH  - Pollen/*immunology
MH  - Sodium Hydroxide/pharmacology
MH  - Trees/*immunology
EDAT- 1998/08/05 00:00
MHDA- 1998/08/05 00:01
CRDT- 1998/08/05 00:00
PHST- 1998/08/05 00:00 [pubmed]
PHST- 1998/08/05 00:01 [medline]
PHST- 1998/08/05 00:00 [entrez]
PST - ppublish
SO  - Allergy. 1998 Jun;53(6):586-93.

PMID- 2580625
OWN - NLM
STAT- MEDLINE
DCOM- 19850619
LR  - 20051117
IS  - 0008-5472 (Print)
IS  - 0008-5472 (Linking)
VI  - 45
IP  - 6
DP  - 1985 Jun
TI  - Monoclonal antibodies to a glycolipid antigen on human neuroblastoma cells.
PG  - 2642-9
AB  - Using a somatic cell hybridization technique, four murine monoclonal antibodies
      (three immunoglobulin M and one immunoglobulin G3) were produced against a human 
      neuroblastoma cell surface glycolipid antigen. They reacted strongly with all
      human neuroblastoma tumor-containing specimens and six of eight human
      neuroblastoma cell lines. More than 98% of each neuroblastoma cell population
      possessed this surface antigen, and in the presence of complement, 100% of them
      were killed. While melanoma and osteogenic sarcoma carried this antigen, leukemia
      and most Ewing's and Wilms' tumors did not. There was no cross-reaction with 30
      normal or remission bone marrow samples and none with normal human tissues other 
      than neurons in vitro. This antigen was neuraminidase sensitive, separable on
      thin-layer chromatogram, and did not modulate after combining with the monoclonal
      antibodies. These antibodies could detect less than 0.1% tumor cells deliberately
      seeded in the bone marrow samples. Because of their unique properties, these
      monoclonal antibodies may have diagnostic and therapeutic potentials.
FAU - Cheung, N K
AU  - Cheung NK
FAU - Saarinen, U M
AU  - Saarinen UM
FAU - Neely, J E
AU  - Neely JE
FAU - Landmeier, B
AU  - Landmeier B
FAU - Donovan, D
AU  - Donovan D
FAU - Coccia, P F
AU  - Coccia PF
LA  - eng
PT  - Journal Article
PL  - United States
TA  - Cancer Res
JT  - Cancer research
JID - 2984705R
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens, Neoplasm)
RN  - 0 (Epitopes)
RN  - 0 (Glycolipids)
RN  - 9007-36-7 (Complement System Proteins)
SB  - IM
MH  - Animals
MH  - Antibodies, Monoclonal/*immunology
MH  - Antigens, Neoplasm/*immunology
MH  - Cell Line
MH  - Complement System Proteins/immunology
MH  - Cytotoxicity, Immunologic
MH  - Epitopes
MH  - Glycolipids/*immunology
MH  - Humans
MH  - Hybridomas
MH  - Mice
MH  - Mice, Inbred BALB C
MH  - Mice, Nude
MH  - Neuroblastoma/*immunology
EDAT- 1985/06/01 00:00
MHDA- 1985/06/01 00:01
CRDT- 1985/06/01 00:00
PHST- 1985/06/01 00:00 [pubmed]
PHST- 1985/06/01 00:01 [medline]
PHST- 1985/06/01 00:00 [entrez]
PST - ppublish
SO  - Cancer Res. 1985 Jun;45(6):2642-9.

PMID- 8752218
OWN - NLM
STAT- MEDLINE
DCOM- 19961003
LR  - 20071114
IS  - 0092-8674 (Print)
IS  - 0092-8674 (Linking)
VI  - 86
IP  - 4
DP  - 1996 Aug 23
TI  - The alpha(1,3)fucosyltransferase Fuc-TVII controls leukocyte trafficking through 
      an essential role in L-, E-, and P-selectin ligand biosynthesis.
PG  - 643-53
AB  - alpha(1,3)Fucosylated oligosaccharides represent components of leukocyte
      counterreceptors for E- and P-selectins and of L-selectin ligands expressed by
      lymph node high endothelial venules (HEV). The identity of the
      alpha(1,3)fucosyltransferase(s) required for their expression has been uncertain,
      as has a requirement for alpha(1,3)fucosylation in HEV L-selectin ligand
      activity. We demonstrate here that mice deficient in alpha(1,3)
      fucosyltransferase Fuc-TVII exhibit a leukocyte adhesion deficiency characterized
      by absent leukocyte E- and P-selectin ligand activity and deficient HEV
      L-selectin ligand activity. Selectin ligand deficiency is distinguished by blood 
      leukocytosis, impaired leukocyte extravasation in inflammation, and faulty
      lymphocyte homing. These observations demonstrate an essential role for Fuc-TVII 
      in E-, P-, and L-selectin ligand biosynthesis and imply that this locus can
      control leukocyte trafficking in health and disease.
FAU - Maly, P
AU  - Maly P
AD  - Howard Hughes Medical Institute, University of Michigan Medical School, Ann Arbor
      48109-0650, USA.
FAU - Thall, A
AU  - Thall A
FAU - Petryniak, B
AU  - Petryniak B
FAU - Rogers, C E
AU  - Rogers CE
FAU - Smith, P L
AU  - Smith PL
FAU - Marks, R M
AU  - Marks RM
FAU - Kelly, R J
AU  - Kelly RJ
FAU - Gersten, K M
AU  - Gersten KM
FAU - Cheng, G
AU  - Cheng G
FAU - Saunders, T L
AU  - Saunders TL
FAU - Camper, S A
AU  - Camper SA
FAU - Camphausen, R T
AU  - Camphausen RT
FAU - Sullivan, F X
AU  - Sullivan FX
FAU - Isogai, Y
AU  - Isogai Y
FAU - Hindsgaul, O
AU  - Hindsgaul O
FAU - von Andrian, U H
AU  - von Andrian UH
FAU - Lowe, J B
AU  - Lowe JB
LA  - eng
GR  - GM47455/GM/NIGMS NIH HHS/United States
PT  - Journal Article
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Cell
JT  - Cell
JID - 0413066
RN  - 0 (Antigens, Surface)
RN  - 0 (E-Selectin)
RN  - 0 (Ligands)
RN  - 0 (P-Selectin)
RN  - 126880-86-2 (L-Selectin)
RN  - EC 2.4.1.- (Fucosyltransferases)
RN  - EC 2.4.1.152 (galactoside 3-fucosyltransferase)
SB  - IM
MH  - Animals
MH  - Antigens, Surface/metabolism
MH  - Cell Adhesion
MH  - Cell Movement
MH  - Cells, Cultured
MH  - E-Selectin/*biosynthesis
MH  - Endothelium, Vascular/*physiology
MH  - Fucosyltransferases/*genetics
MH  - Glycosylation
MH  - Immunologic Techniques
MH  - L-Selectin/*biosynthesis
MH  - Leukocytosis/genetics
MH  - Ligands
MH  - Lymphocytes/*physiology
MH  - Mice
MH  - Mice, Knockout
MH  - Neutrophils/physiology
MH  - P-Selectin/*biosynthesis
MH  - Protein Processing, Post-Translational
EDAT- 1996/08/23 00:00
MHDA- 1996/08/23 00:01
CRDT- 1996/08/23 00:00
PHST- 1996/08/23 00:00 [pubmed]
PHST- 1996/08/23 00:01 [medline]
PHST- 1996/08/23 00:00 [entrez]
AID - S0092-8674(00)80137-3 [pii]
PST - ppublish
SO  - Cell. 1996 Aug 23;86(4):643-53.

PMID- 8490240
OWN - NLM
STAT- MEDLINE
DCOM- 19930611
LR  - 20190512
IS  - 0959-6658 (Print)
IS  - 0959-6658 (Linking)
VI  - 3
IP  - 2
DP  - 1993 Apr
TI  - Differential distribution of major gangliosides in rat central nervous system
      detected by specific monoclonal antibodies.
PG  - 137-46
AB  - We investigated the localization of major gangliosides in adult rat brain by an
      immunofluorescence technique with mouse monoclonal antibodies (MAbs). Five MAbs
      (GMB16, GMR17, GGR12, GMR5 and GMR13) that specifically recognize gangliosides
      GM1, GD1a, GD1b, GT1b and GQ1b, respectively, were used. We have found that there
      is a cell type-specific expression of the ganglioside in the rat central nervous 
      system. In cerebellar cortex, GM1 was expressed in myelin and some glial cells.
      GD1a was detected exclusively in the molecular layer. GD1b and GQ1b were present 
      restrictedly on the granular layer; GD1b was detected on the surface of the
      granular cell bodies, whereas GQ1b was present in the cerebellar glomerulus. GT1b
      was distributed intensely in both the molecular layer and the granular layer. In 
      cerebral cortex, GM1 was detected in some glial cells. Dense staining was limited
      to the white matter. GD1a was distributed in layers I, II/III and Va, and the
      upper part of layer VI, whereas GQ1b was localized in layers IV and Vb, and the
      lower part of layer VI. GD1b was detected beneath layer III. GT1b appeared to be 
      distributed throughout all layers. In other regions, such as hippocampal
      formation and spinal cord, the expression of the ganglioside was also highly
      localized to a specific cell type and layer.
FAU - Kotani, M
AU  - Kotani M
AD  - Tokyo Metropolitan Institute of Medical Science, Department of Tumor Immunology, 
      Japan.
FAU - Kawashima, I
AU  - Kawashima I
FAU - Ozawa, H
AU  - Ozawa H
FAU - Terashima, T
AU  - Terashima T
FAU - Tai, T
AU  - Tai T
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - Glycobiology
JT  - Glycobiology
JID - 9104124
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Fluorescent Dyes)
RN  - 0 (Gangliosides)
RN  - 9012-63-9 (Cholera Toxin)
RN  - EC 3.2.1.18 (Neuraminidase)
RN  - EC 3.4.21.4 (Trypsin)
RN  - I223NX31W9 (Fluorescein-5-isothiocyanate)
SB  - IM
MH  - Animals
MH  - *Antibodies, Monoclonal
MH  - *Brain Chemistry
MH  - Cerebellar Cortex/chemistry
MH  - Cerebral Cortex/chemistry
MH  - Cholera Toxin
MH  - Female
MH  - Fluorescein-5-isothiocyanate
MH  - *Fluorescent Antibody Technique
MH  - Fluorescent Dyes
MH  - Gangliosides/*analysis
MH  - Hippocampus/chemistry
MH  - Immunohistochemistry
MH  - Neuraminidase/pharmacology
MH  - Rats
MH  - Rats, Wistar
MH  - Spinal Cord/*chemistry
MH  - Tissue Distribution
MH  - Trypsin/pharmacology
EDAT- 1993/04/01 00:00
MHDA- 1993/04/01 00:01
CRDT- 1993/04/01 00:00
PHST- 1993/04/01 00:00 [pubmed]
PHST- 1993/04/01 00:01 [medline]
PHST- 1993/04/01 00:00 [entrez]
AID - 10.1093/glycob/3.2.137 [doi]
PST - ppublish
SO  - Glycobiology. 1993 Apr;3(2):137-46. doi: 10.1093/glycob/3.2.137.

PMID- 10393028
OWN - NLM
STAT- MEDLINE
DCOM- 19990708
LR  - 20041117
IS  - 0146-0404 (Print)
IS  - 0146-0404 (Linking)
VI  - 40
IP  - 8
DP  - 1999 Jul
TI  - Alteration of sialyl Lewis epitope expression in pterygium.
PG  - 1631-6
AB  - PURPOSE: Mucin-related antigens are abundantly expressed by the cells of the
      normal human conjunctiva. The pattern of these antigens in pterygium, and
      especially the role of Galbeta1-3GlcNAc alpha2,3-sialyltransferase (ST3Gal III), 
      sialyltransferase necessary to build the sialyl-Le(a) (Lewis(a)) antigen, were
      studied. METHODS: Immunoperoxidase staining was performed on 28 pterygia using
      different monoclonal antibodies: anti-M1 (against the peptidic core of gastric
      mucins encoded by MUC 5AC gene), anti-Le(a)(7LE), anti-sialyl Le(a)(NS 19-9), and
      anti-Le(b)(2-25LE). A serologic Lewis determination was done in 18 patients.
      ST3Gal III sialyltransferase expression was also studied in 10 healthy
      conjunctiva and 10 pterygia by reverse transcriptase-polymerase chain reaction
      (RT-PCR). Glyceraldehyde-3-phosphate-dehydrogenase was used as an endogenous
      internal control. RESULTS: First, Le(a), sialyl Le(a), and Le(b)
      immunoreactivities either decreased or were no longer detectable in pterygium
      goblet cells as opposed to normal conjunctiva. Second, unlike in pterygium, the
      Lewis immunoreactivity, which is mainly located in the surface epithelial cells
      in the normal conjunctiva, was occasionally restricted to the epithelial cells of
      the deep layers. However, M1 mucins did show an identical pattern expression in a
      normal conjunctiva and pterygium. ST3Gal III expression was significantly lower
      in pterygium (0.20+/-0.02 AU [arbitrary units]) than in normal conjunctiva
      (0.95+/-0.12 AU). CONCLUSIONS: ST3Gal III gene is less expressed in pterygium
      than in normal conjunctiva. This observation could explain the decrease of sialyl
      Le(a) expression observed in pterygium by immunohistology.
FAU - Creuzot-Garcher, C
AU  - Creuzot-Garcher C
AD  - Department of Ophthalmology, University of Burgundy, Dijon, France.
FAU - Guerzider, V
AU  - Guerzider V
FAU - Assem, M
AU  - Assem M
FAU - Bron, A M
AU  - Bron AM
FAU - Delannoy, P
AU  - Delannoy P
FAU - Bara, J
AU  - Bara J
LA  - eng
PT  - Journal Article
PL  - United States
TA  - Invest Ophthalmol Vis Sci
JT  - Investigative ophthalmology & visual science
JID - 7703701
RN  - 0 (ABO Blood-Group System)
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (DNA Primers)
RN  - 0 (Epitopes)
RN  - 0 (Gangliosides)
RN  - 0 (Lewis Blood-Group System)
RN  - 0 (Mucins)
RN  - 0 (RNA, Messenger)
RN  - 91847-18-6 (sialyl Le(a) ganglioside)
RN  - EC 2.4.99.- (Sialyltransferases)
RN  - EC 2.4.99.4 (beta-galactoside alpha-2,3-sialyltransferase)
SB  - IM
MH  - ABO Blood-Group System/metabolism
MH  - Adult
MH  - Aged
MH  - Aged, 80 and over
MH  - Antibodies, Monoclonal
MH  - Conjunctiva/cytology/metabolism
MH  - DNA Primers/chemistry
MH  - Epitopes/*metabolism
MH  - Gangliosides/metabolism
MH  - Humans
MH  - Immunoenzyme Techniques
MH  - Lewis Blood-Group System/*metabolism
MH  - Middle Aged
MH  - Mucins/*metabolism
MH  - Phenotype
MH  - Pterygium/genetics/*metabolism/pathology
MH  - RNA, Messenger/analysis
MH  - Reverse Transcriptase Polymerase Chain Reaction
MH  - Sialyltransferases/genetics/*metabolism
EDAT- 1999/07/07 00:00
MHDA- 1999/07/07 00:01
CRDT- 1999/07/07 00:00
PHST- 1999/07/07 00:00 [pubmed]
PHST- 1999/07/07 00:01 [medline]
PHST- 1999/07/07 00:00 [entrez]
PST - ppublish
SO  - Invest Ophthalmol Vis Sci. 1999 Jul;40(8):1631-6.

PMID- 12163379
OWN - NLM
STAT- MEDLINE
DCOM- 20020828
LR  - 20181113
IS  - 0002-9440 (Print)
IS  - 0002-9440 (Linking)
VI  - 161
IP  - 2
DP  - 2002 Aug
TI  - Glycosylation might provide endothelial zip codes for organ-specific leukocyte
      traffic into inflammatory sites.
PG  - 543-50
AB  - Inflammatory diseases are characterized by the leukocyte infiltration into
      tissues. L-selectin on lymphocytes and its endothelial glycosylated ligands are
      instrumental in the initiation of lymphocyte extravasation. Immunohistochemical
      stainings with monoclonal antibodies against functionally active glycan-decorated
      L-selectin ligands, ie, sialyl-Lewis x (sLex, 2F3, and HECA-452) or sulfated
      extended core 1 lactosamine (MECA-79), were performed on more than 400 specimen
      representatives for thyroiditis, myocarditis, psoriasis, vasculitis, ulcerative
      colitis, and their corresponding noninflamed tissues. The endothelial expression 
      of sLex or sulfo sLex glycans in postcapillary venules was either absent or low
      in control tissues. The de novo induction of endothelial expression of sLex or
      sulfo sLex glycans was detected in all inflamed tissues. Furthermore, each organ 
      carried its own modification of sLex or sulfo sLex glycans, ie, zip code. Our
      results suggest that these zip code glycans may provide means for organ selective
      leukocyte traffic that could be used in selective leukocyte traffic inhibition.
FAU - Renkonen, Jutta
AU  - Renkonen J
AD  - Transplantation Laboratory and Department of Pathology, Haartman Institute,
      Helsinki, Finland.
FAU - Tynninen, Olli
AU  - Tynninen O
FAU - Hayry, Pekka
AU  - Hayry P
FAU - Paavonen, Timo
AU  - Paavonen T
FAU - Renkonen, Risto
AU  - Renkonen R
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Am J Pathol
JT  - The American journal of pathology
JID - 0370502
RN  - 0 (Ligands)
RN  - 126880-86-2 (L-Selectin)
SB  - AIM
SB  - IM
MH  - Cell Movement
MH  - *Glycosylation
MH  - Humans
MH  - Immunohistochemistry
MH  - Inflammation/*metabolism/*pathology
MH  - L-Selectin/metabolism
MH  - Leukocytes/*pathology
MH  - Ligands
MH  - Organ Specificity
PMC - PMC1850742
EDAT- 2002/08/07 10:00
MHDA- 2002/08/29 10:01
CRDT- 2002/08/07 10:00
PHST- 2002/08/07 10:00 [pubmed]
PHST- 2002/08/29 10:01 [medline]
PHST- 2002/08/07 10:00 [entrez]
AID - S0002-9440(10)64210-1 [pii]
AID - 10.1016/S0002-9440(10)64210-1 [doi]
PST - ppublish
SO  - Am J Pathol. 2002 Aug;161(2):543-50. doi: 10.1016/S0002-9440(10)64210-1.

PMID- 17522109
OWN - NLM
STAT- MEDLINE
DCOM- 20080306
LR  - 20150813
IS  - 0959-6658 (Print)
IS  - 0959-6658 (Linking)
VI  - 17
IP  - 8
DP  - 2007 Aug
TI  - O-linked glycan expression during Drosophila development.
PG  - 820-7
AB  - Mucin-type O-linked glycosylation is an evolutionarily conserved protein
      modification that is essential for viability in Drosophila melanogaster. However,
      the exact role of O-glycans and the identity of the crucial apoproteins modified 
      with O-linked N-acetylgalactosamine (O-GalNAc) remain unknown. In an effort to
      elucidate the O-linked glycans expressed during Drosophila development, we have
      employed fluorescent confocal microscopy using a battery of lectins and an
      antibody specific for the GalNAcalpha-Ser/Thr structure (Tn antigen). Confocal
      microscopy provides high-resolution images of the diversity of glycans expressed 
      in many developing organ systems. In particular, O-glycans are highly expressed
      on a number of ectodermally derived tissues such as the salivary glands,
      developing gut, and the tracheal system, suggesting a role for O-glycans in cell 
      polarity and tube formation common to these organs. Additionally, O-glycans are
      found in the developing nervous system and within subregions of developing
      tissues known to be active in cell signaling events. This study provides us with 
      temporal and spatial information regarding O-glycan expression as well as a set
      of reagents for the isolation of glycoproteins from specific developmental stages
      and organ systems. This information will aid us in identifying the in vivo
      substrates of the UDP-GalNAc: polypeptide N-acetylgalactosaminyltranferases, in a
      continuing effort to define the biological role of O-linked glycoproteins during 
      development.
FAU - Tian, E
AU  - Tian E
AD  - Developmental Glycobiology Unit, NIDCR, National Institutes of Health, Building
      30, Room 426, 30 Convent Drive, MSC 4370, Bethesda, MD 20892-4370, USA.
FAU - Ten Hagen, Kelly G
AU  - Ten Hagen KG
LA  - eng
GR  - Intramural NIH HHS/United States
PT  - Journal Article
PT  - Research Support, N.I.H., Intramural
DEP - 20070523
PL  - England
TA  - Glycobiology
JT  - Glycobiology
JID - 9104124
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Lectins)
RN  - 0 (Polysaccharides)
RN  - 0 (Tn antigen)
RN  - EC 2.4.1.- (N-Acetylgalactosaminyltransferases)
SB  - IM
MH  - Animals
MH  - Antigens, Tumor-Associated, Carbohydrate/analysis/immunology
MH  - Drosophila/*embryology/growth & development/metabolism
MH  - Embryonic Development
MH  - Gene Expression Regulation, Developmental
MH  - Glycosylation
MH  - Larva/metabolism
MH  - Lectins/analysis
MH  - Microscopy, Confocal
MH  - N-Acetylgalactosaminyltransferases/metabolism
MH  - Polysaccharides/*metabolism
MH  - Proteomics
MH  - Staining and Labeling
EDAT- 2007/05/25 09:00
MHDA- 2008/03/07 09:00
CRDT- 2007/05/25 09:00
PHST- 2007/05/25 09:00 [pubmed]
PHST- 2008/03/07 09:00 [medline]
PHST- 2007/05/25 09:00 [entrez]
AID - cwm056 [pii]
AID - 10.1093/glycob/cwm056 [doi]
PST - ppublish
SO  - Glycobiology. 2007 Aug;17(8):820-7. doi: 10.1093/glycob/cwm056. Epub 2007 May 23.

PMID- 3754220
OWN - NLM
STAT- MEDLINE
DCOM- 19860512
LR  - 20131121
IS  - 0014-4827 (Print)
IS  - 0014-4827 (Linking)
VI  - 164
IP  - 1
DP  - 1986 May
TI  - An anti-carbohydrate monoclonal antibody inhibits cell-substratum adhesion of F9 
      embryonal carcinoma cells.
PG  - 49-62
AB  - A monoclonal rat IgM antibody (4C9) raised against F9 embryonal carcinoma cells
      reacted with fucosyl residues in poly-N-acetyllactosamine-type large
      carbohydrates of these cells (embryoglycan). The chemical properties and
      distribution of the antigen resembled those of SSEA-1. The monoclonal antibody
      was found to inhibit cell-substratum adhesion of F9 cells: in the presence of the
      antibody, cells grew as spherical cell aggregates on plastic dishes. When the
      antibody was added to the already spread cells, they displayed the initial sign
      of rounding up within 3 h; the rounding process was largely completed within 6 h.
      After removal of the antibody, cells resumed their normal morphology. The
      antibody could act in the presence of 2,4-dinitrophenol. In serum-free medium, F9
      cells spread on plastic dishes coated with fibronectin or with laminin, and the
      process was also inhibited by the antibody. Immuno-electronmicroscopy revealed
      that 4C9 antigen was diffusely distributed over the cell surface of F9 cells. The
      distribution of the antigen was not altered generally after culturing with the
      antibody for 6 h. Another monoclonal rat IgM antibody, which did not react with
      embryoglycan and resembled anti-Forssman, did not inhibit cell-substratum
      adhesion of F9 cells, in spite of its reactivity to the cells. Thus, a
      glycoprotein with fucosyl (poly)-N-acetyllactosamine structure appears to be
      involved in cell-substratum adhesion of F9 cells.
FAU - Nomoto, S
AU  - Nomoto S
FAU - Muramatsu, H
AU  - Muramatsu H
FAU - Ozawa, M
AU  - Ozawa M
FAU - Suganuma, T
AU  - Suganuma T
FAU - Tashiro, M
AU  - Tashiro M
FAU - Muramatsu, T
AU  - Muramatsu T
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Exp Cell Res
JT  - Experimental cell research
JID - 0373226
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Dinitrophenols)
RN  - 0 (Glycoproteins)
RN  - 0 (Polysaccharides)
RN  - 0 (embryoglycan)
RN  - 82441-98-3 (poly-N-acetyllactosamine)
RN  - Q13SKS21MN (2,4-Dinitrophenol)
SB  - IM
MH  - 2,4-Dinitrophenol
MH  - Animals
MH  - Antibodies, Monoclonal/immunology
MH  - *Cell Adhesion
MH  - Cell Line
MH  - Dinitrophenols/pharmacology
MH  - Embryonal Carcinoma Stem Cells
MH  - Glycoproteins/*physiology
MH  - Neoplastic Stem Cells/*physiology
MH  - Polysaccharides/immunology/*physiology
MH  - Teratoma
EDAT- 1986/05/01 00:00
MHDA- 1986/05/01 00:01
CRDT- 1986/05/01 00:00
PHST- 1986/05/01 00:00 [pubmed]
PHST- 1986/05/01 00:01 [medline]
PHST- 1986/05/01 00:00 [entrez]
AID - 0014-4827(86)90453-2 [pii]
PST - ppublish
SO  - Exp Cell Res. 1986 May;164(1):49-62.

PMID- 3031684
OWN - NLM
STAT- MEDLINE
DCOM- 19870515
LR  - 20190501
IS  - 0027-8424 (Print)
IS  - 0027-8424 (Linking)
VI  - 84
IP  - 8
DP  - 1987 Apr
TI  - Cell-surface antigens of melanoma recognized by human monoclonal antibodies.
PG  - 2416-20
AB  - Human monoclonal antibodies (mAbs) were derived from lymph node lymphocytes and
      peripheral blood lymphocytes (PBL) from patients with melanoma. Four methods for 
      generating human mAbs were compared: fusion with human [LICR-LON-HMy-2 (LICR-2)] 
      or mouse (NS-1) cells; transformation by Epstein-Barr virus (EBV); and EBV
      transformation followed by NS-1 fusion. NS-1 fusion with lymph node lymphocytes
      resulted in a higher number of growing hybrids than LICR-2 fusion. Virtually no
      hybrids were obtained from NS-1 or LICR-2 fusions with PBL. EBV transformed
      lymphocytes from lymph node and peripheral blood with equal efficiency, and the
      yield of proliferating cultures for antibody screening was more than 10- to
      30-fold greater than that obtained by fusion techniques. However, once
      antibody-producing cultures had been identified, stability and clonability of
      EBV-transformed cells were poorer than that of NS-1 hybrid cells. To combine the 
      strengths of both methods, cultures of EBV-transformed cells were fused with
      NS-1; and hybrid clones were isolated that showed vigorous growth, clonability,
      and stable antibody secretion. Detailed specificity analysis of the mAbs produced
      by six of these clones indicated detection of a class 1 (unique) melanoma
      antigen, a class 3 melanoma antigen, and four ganglioside antigens (GD3, GM3, and
      two other, as yet uncharacterized, heterophile antigens).
FAU - Yamaguchi, H
AU  - Yamaguchi H
FAU - Furukawa, K
AU  - Furukawa K
FAU - Fortunato, S R
AU  - Fortunato SR
FAU - Livingston, P O
AU  - Livingston PO
FAU - Lloyd, K O
AU  - Lloyd KO
FAU - Oettgen, H F
AU  - Oettgen HF
FAU - Old, L J
AU  - Old LJ
LA  - eng
GR  - CA-08748/CA/NCI NIH HHS/United States
GR  - CA-33049/CA/NCI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Proc Natl Acad Sci U S A
JT  - Proceedings of the National Academy of Sciences of the United States of America
JID - 7505876
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigen-Antibody Complex)
RN  - 0 (Antigens, Surface)
SB  - IM
MH  - Antibodies, Monoclonal
MH  - Antigen-Antibody Complex
MH  - Antigens, Surface/*analysis
MH  - Cell Line
MH  - Cell Transformation, Viral
MH  - Clone Cells
MH  - Herpesvirus 4, Human/genetics
MH  - Humans
MH  - Lymphocytes/immunology
MH  - Melanoma/*immunology
PMC - PMC304662
EDAT- 1987/04/01 00:00
MHDA- 1987/04/01 00:01
CRDT- 1987/04/01 00:00
PHST- 1987/04/01 00:00 [pubmed]
PHST- 1987/04/01 00:01 [medline]
PHST- 1987/04/01 00:00 [entrez]
AID - 10.1073/pnas.84.8.2416 [doi]
PST - ppublish
SO  - Proc Natl Acad Sci U S A. 1987 Apr;84(8):2416-20. doi: 10.1073/pnas.84.8.2416.

PMID- 2568858
OWN - NLM
STAT- MEDLINE
DCOM- 19890830
LR  - 20171116
IS  - 0006-4971 (Print)
IS  - 0006-4971 (Linking)
VI  - 74
IP  - 1
DP  - 1989 Jul
TI  - Sialyl SSEA-1 antigen as a carbohydrate marker of human natural killer cells and 
      immature lymphoid cells.
PG  - 255-61
AB  - The distribution of a carbohydrate antigen, the sialyl SSEA-1 (sialyl Lex-i), in 
      human lymphoid cells was investigated by flow cytometry with a specific
      monoclonal antibody, MoAb FH-6. We concluded that the lymphocytes positive for
      the sialyl SSEA-1 antigen present in normal peripheral blood (PB) are natural
      killer (NK) cells since the positive cells had an NK activity toward K562 cells, 
      and most of the sialyl SSEA-1+ cells were simultaneously positive for Leu-11
      (CD-16) and Leu-19. Essentially, no T and B cells, defined by Leu-4 (CD3) and
      Leu-16 (CD20), were positive for the sialyl SSEA-1 antigen in PB samples taken
      from healthy donors and patients with disorders unrelated to lymphoid
      malignancies. Among the malignant lymphoid cells, many sialylated SSEA-1+ cells
      were observed in large granular lymphocyte (LGL) leukemia cells and some acute
      lymphoblastic leukemia (ALL) blasts, but not in CLL cells or malignant lymphoma
      cells. Sialyl SSEA-1 was also positive in some cultured human lymphoid cell
      lines. We conclude that expression of the sialyl SSEA-1 antigen is strictly
      limited to a distinct population of NK cells among the mature lymphocytes in
      normal PB, but the antigen is present in a wide range of immature lymphoblasts of
      T- and B-cell lineages as well as the NK-cell lineage. The sialyl SSEA-1 antigen 
      disappears from the surface of immature lymphocytes of T- and B-cell lineages
      during the course of maturation.
FAU - Ohmori, K
AU  - Ohmori K
AD  - Department of Clinical Science and Laboratory Medicine, Kyoto University, School 
      of Medicine, Sakyoku, Japan.
FAU - Yoneda, T
AU  - Yoneda T
FAU - Ishihara, G
AU  - Ishihara G
FAU - Shigeta, K
AU  - Shigeta K
FAU - Hirashima, K
AU  - Hirashima K
FAU - Kanai, M
AU  - Kanai M
FAU - Itai, S
AU  - Itai S
FAU - Sasaoki, T
AU  - Sasaoki T
FAU - Arii, S
AU  - Arii S
FAU - Arita, H
AU  - Arita H
AU  - et al.
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Blood
JT  - Blood
JID - 7603509
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens, Differentiation)
RN  - 0 (Antigens, Neoplasm)
RN  - 0 (Glycolipids)
RN  - 0 (Lewis X Antigen)
RN  - 0 (Sialic Acids)
SB  - AIM
SB  - IM
MH  - Antibodies, Monoclonal
MH  - Antigens, Differentiation/analysis
MH  - Antigens, Neoplasm/analysis
MH  - Carbohydrate Sequence
MH  - Cell Differentiation
MH  - Flow Cytometry
MH  - Glycolipids/*immunology
MH  - Humans
MH  - Killer Cells, Natural/*immunology
MH  - Leukemia/immunology
MH  - Lewis X Antigen
MH  - Lymphocytes/classification/cytology/*immunology
MH  - Lymphoma/immunology
MH  - Molecular Sequence Data
MH  - Sialic Acids
MH  - Tumor Cells, Cultured/immunology
EDAT- 1989/07/01 00:00
MHDA- 1989/07/01 00:01
CRDT- 1989/07/01 00:00
PHST- 1989/07/01 00:00 [pubmed]
PHST- 1989/07/01 00:01 [medline]
PHST- 1989/07/01 00:00 [entrez]
PST - ppublish
SO  - Blood. 1989 Jul;74(1):255-61.

PMID- 3731131
OWN - NLM
STAT- MEDLINE
DCOM- 19860918
LR  - 20151119
IS  - 0008-5472 (Print)
IS  - 0008-5472 (Linking)
VI  - 46
IP  - 9
DP  - 1986 Sep
TI  - Comparison of T-antigen expression in normal, premalignant, and malignant human
      colonic tissue using lectin and antibody immunohistochemistry.
PG  - 4841-7
AB  - The Thomsen-Friedenreich antigen has been implicated as a cancer-associated
      antigen in some human organs including the colon. Most previous studies of
      Thomsen-Friedenreich antigen expression in the colon used peanut agglutinin (PNA)
      to identify the immunodeterminant in tissues. However, evidence from other organs
      suggests that anti-T antibodies have specificities which differ from those of
      peanut lectin. To elucidate the nature of the T-immunodeterminant in colonic
      mucosa, we compared staining by PNA to that of a polyclonal (PAb) and monoclonal 
      (MAb) anti-T antibody. PNA demonstrated the best sensitivity (91%) in cancer
      tissues but the lowest specificity (68%) in normal mucosa. Staining with MAb was 
      only 76% sensitive but 100% specific. Sensitivity and specificity of PAb were
      intermediate between PNA and MAb. MAb stained fewer adenomatous polyps than
      either PNA or PAb, but staining appeared to correlate with premalignant features 
      of the polyps. PNA-binding sites were more prevalent than either PAb or MAb in
      hyperplastic polyps. Cell cytoplasm was stained by both antibodies more often
      than by PNA. The majority of fetal colonic specimens stained with all three
      reagents suggesting that Thomsen-Friedenreich antigen may be an oncodevelopmental
      antigen in human colon. Differences in staining patterns in some tissues may be
      due to different antigenic specificities among PNA, PAb, and MAb.
FAU - Yuan, M
AU  - Yuan M
FAU - Itzkowitz, S H
AU  - Itzkowitz SH
FAU - Boland, C R
AU  - Boland CR
FAU - Kim, Y D
AU  - Kim YD
FAU - Tomita, J T
AU  - Tomita JT
FAU - Palekar, A
AU  - Palekar A
FAU - Bennington, J L
AU  - Bennington JL
FAU - Trump, B F
AU  - Trump BF
FAU - Kim, Y S
AU  - Kim YS
LA  - eng
GR  - CA14905/CA/NCI NIH HHS/United States
GR  - CP15738/CP/NCI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, U.S. Gov't, Non-P.H.S.
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Cancer Res
JT  - Cancer research
JID - 2984705R
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens, Neoplasm)
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Blood Group Antigens)
RN  - 0 (Disaccharides)
RN  - 0 (Lectins)
RN  - 0 (Oligosaccharides)
RN  - 0 (Peanut Agglutinin)
RN  - 3554-90-3 (Thomsen-Friedenreich antigen)
SB  - IM
MH  - Adenoma/immunology
MH  - Antibodies, Monoclonal
MH  - Antigens, Neoplasm/*analysis
MH  - *Antigens, Tumor-Associated, Carbohydrate
MH  - *Blood Group Antigens
MH  - Cell Differentiation
MH  - Colon/immunology
MH  - Colonic Neoplasms/*immunology
MH  - Disaccharides/*analysis
MH  - Humans
MH  - Hyperplasia/immunology
MH  - Intestinal Mucosa/immunology
MH  - Intestinal Polyps/immunology
MH  - Lectins
MH  - Oligosaccharides/immunology
MH  - Peanut Agglutinin
MH  - Precancerous Conditions/*immunology
MH  - Rectal Neoplasms/*immunology
MH  - Rectum/immunology
EDAT- 1986/09/01 00:00
MHDA- 1986/09/01 00:01
CRDT- 1986/09/01 00:00
PHST- 1986/09/01 00:00 [pubmed]
PHST- 1986/09/01 00:01 [medline]
PHST- 1986/09/01 00:00 [entrez]
PST - ppublish
SO  - Cancer Res. 1986 Sep;46(9):4841-7.

PMID- 9209886
OWN - NLM
STAT- MEDLINE
DCOM- 19970821
LR  - 20171116
IS  - 0906-6705 (Print)
IS  - 0906-6705 (Linking)
VI  - 6
IP  - 2
DP  - 1997 Apr
TI  - Expression of GD3 disialoganglioside antigen on peripheral T-lymphocytes in
      patients with disseminated malignant melanoma.
PG  - 64-9
AB  - Disialoganglioside antigens GD2 and GD3 are expressed on most melanoma cells. On 
      melanoma surrounding T-cells in immunohistological sections, disialogangliosides 
      can also be found, as well as in a small % of T-lymphocytes in peripheral blood
      from healthy persons. In order to find out if there is a difference in
      ganglioside expression on peripheral T-lymphocytes between melanoma patients and 
      healthy persons, we examined the expression of CD3 as T-lymphocytic antigen and
      GD2 or GD3 antigens, respectively, by flow cytometry. We used peripheral
      mononuclear blood cells of 12 patients with advanced disseminated malignant
      melanoma and of 12 healthy control donors. For immunostaining, murine monoclonal 
      antibodies Leu-4, 14G2a and MB3.6 were used, recognizing CD3, GD2 and GD3. GD2
      expression was found on only a low proportion of T-lymphocytes in patients and
      healthy persons (pat.: mean = 1.2% +/- 0.7%, co.: mean = 0.4% +/- 0.4%).
      Disialoganglioside antigen GD3, however, could be demonstrated on an average of
      8.4% +/- 4.6% of patients' and on 4.0% +/- 2.1% of healthy persons' T-cells.
      There is a statistically significant difference (P < 0.01) between the data of
      patients' and control group. We conclude that there is a correlation between
      advanced malignant melanoma and expression of GD3 antigen on patients' peripheral
      T-lymphocytes. The immunological relevance of our findings is discussed.
FAU - Welte, B
AU  - Welte B
AD  - Department of Dermatology, University of Tubingen, Germany.
FAU - Handgretinger, R
AU  - Handgretinger R
FAU - Rassner, G
AU  - Rassner G
FAU - Fierlbeck, G
AU  - Fierlbeck G
LA  - eng
PT  - Journal Article
PL  - Denmark
TA  - Exp Dermatol
JT  - Experimental dermatology
JID - 9301549
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens, Neoplasm)
RN  - 0 (CD3 Complex)
RN  - 0 (Gangliosides)
RN  - 62010-37-1 (ganglioside, GD3)
SB  - IM
MH  - Adolescent
MH  - Adult
MH  - Aged
MH  - Animals
MH  - Antibodies, Monoclonal/immunology
MH  - Antigens, Neoplasm/*analysis
MH  - CD3 Complex/analysis
MH  - Female
MH  - Flow Cytometry
MH  - Gangliosides/*analysis
MH  - Humans
MH  - Male
MH  - Melanoma/*immunology/pathology
MH  - Mice
MH  - Middle Aged
MH  - T-Lymphocyte Subsets/*immunology
EDAT- 1997/04/01 00:00
MHDA- 1997/04/01 00:01
CRDT- 1997/04/01 00:00
PHST- 1997/04/01 00:00 [pubmed]
PHST- 1997/04/01 00:01 [medline]
PHST- 1997/04/01 00:00 [entrez]
PST - ppublish
SO  - Exp Dermatol. 1997 Apr;6(2):64-9.

PMID- 16804430
OWN - NLM
STAT- MEDLINE
DCOM- 20060808
LR  - 20131121
IS  - 0891-3668 (Print)
IS  - 0891-3668 (Linking)
VI  - 25
IP  - 7
DP  - 2006 Jul
TI  - T-antigen activation for prediction of pneumococcus-induced hemolytic uremic
      syndrome and hemolytic anemia.
PG  - 608-10
AB  - BACKGROUND: Among the most severe complications of invasive pneumococcal
      infection are hemolytic uremic syndrome (P-HUS) and hemolytic anemia (P-HA),
      which occur when the Thomsen-Freidenreich antigen (TA) is exposed on
      erythrocytes, platelets and glomeruli. METHODS: To determine the positive
      predictive value, sensitivity, and specificity of early TA activation testing for
      P-HUS or P-HA and to compare the microbiologic features of pneumococcus isolates 
      associated or not associated with TA activation. The case records for 36 patients
      with invasive pneumococcal infection who had been tested for TA activation were
      retrospectively reviewed. Clinical and laboratory data were compared between
      patients with and without TA activation. RESULTS: Positive TA activation was 86% 
      sensitive and 57% specific for P-HUS or P-HA. The positive predictive value was
      76%. There were no between-group differences in antibiotic susceptibility of the 
      pneumococcal isolates. Pneumococcal serotype 14 was the most frequent (5/10
      isolates tested) serotype causing P-HUS. Of the 36 patients, 13 required packed
      red blood cell transfusion, 3 died, and 2 required extracorporeal membrane
      oxygenation. No patient had long-term renal sequelae. CONCLUSIONS: TA activation 
      is a reasonable predictor of P-HUS or P-HA and could be useful if tested soon
      after invasive pneumococcal disease is first diagnosed.
FAU - Huang, Daniel Tsung-Ning
AU  - Huang DT
AD  - Department of Pediatrics, Mackay Memorial Hospital, Taipei, Taiwan.
FAU - Chi, Hsin
AU  - Chi H
FAU - Lee, Hung-Chang
AU  - Lee HC
FAU - Chiu, Nan-Chang
AU  - Chiu NC
FAU - Huang, Fu-Yuan
AU  - Huang FY
LA  - eng
PT  - Journal Article
PL  - United States
TA  - Pediatr Infect Dis J
JT  - The Pediatric infectious disease journal
JID - 8701858
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Penicillins)
RN  - 3554-90-3 (Thomsen-Friedenreich antigen)
RN  - N2GI8B1GK7 (Cefotaxime)
SB  - IM
MH  - Anemia, Hemolytic/blood/immunology/*microbiology
MH  - Antigens, Tumor-Associated, Carbohydrate/blood/*immunology
MH  - Cefotaxime/pharmacology
MH  - Child
MH  - Child, Preschool
MH  - Female
MH  - Hemolytic-Uremic Syndrome/blood/immunology/*microbiology
MH  - Humans
MH  - Infant
MH  - Male
MH  - Microbial Sensitivity Tests
MH  - Penicillins/pharmacology
MH  - Pneumococcal Infections/blood/*complications/immunology/microbiology
MH  - Retrospective Studies
MH  - Sensitivity and Specificity
MH  - Streptococcus pneumoniae/drug effects/*isolation & purification
MH  - Taiwan
EDAT- 2006/06/29 09:00
MHDA- 2006/08/09 09:00
CRDT- 2006/06/29 09:00
PHST- 2006/06/29 09:00 [pubmed]
PHST- 2006/08/09 09:00 [medline]
PHST- 2006/06/29 09:00 [entrez]
AID - 10.1097/01.inf.0000223494.83542.ad [doi]
AID - 00006454-200607000-00008 [pii]
PST - ppublish
SO  - Pediatr Infect Dis J. 2006 Jul;25(7):608-10. doi:
      10.1097/01.inf.0000223494.83542.ad.

PMID- 7827404
OWN - NLM
STAT- MEDLINE
DCOM- 19950222
LR  - 20190512
IS  - 0959-6658 (Print)
IS  - 0959-6658 (Linking)
VI  - 4
IP  - 4
DP  - 1994 Aug
TI  - Carbohydrate receptor-mediated gene transfer to human T leukaemic cells.
PG  - 429-35
AB  - The mucin-type carbohydrate Tn cryptantigen (GalNAc alpha 1-O-Ser/Thr, where
      GalNAc is N-acetyl-D-galactosamine) is expressed in many carcinomas, in
      haemopoietic disorders including the Tn syndrome, and on human immunodeficiency
      virus (HIV) coat glycoproteins, but is not expressed on normal, differentiated
      cells because of the expression of a Tn-processing galactosyltransferase. Using
      Jurkat T leukaemic cells which express high levels of Tn antigen due to deficient
      Tn galactosylation, we have established the Tn antigen-mediated gene transfer and
      demonstrate the considerable efficiency of this approach. We used poly(L-lysine) 
      conjugates of the monoclonal antibody 1E3 directed against the Tn antigen to
      deliver the luciferase and beta-galactosidase reporter genes to Jurkat cells by
      receptor-mediated endocytosis. Addition of unconjugated 1E3 reduced transfection 
      efficiency in a concentration-dependent manner and incubation with free GalNAc
      abolished DNA transfer completely, indicating that gene delivery is indeed
      mediated by the Tn antigen. Pre-treatment of Jurkat cells with Vibrio cholerae
      sialidase, which uncovers additional Tn antigens, resulted in an improvement of
      gene transfection. Both human and chicken adenovirus particles attached to the
      DNA/polylysine complex strongly augmented transgene expression. When the
      beta-galactosidase (lacZ) gene was delivered to Jurkat cells by Tn-mediated
      endocytosis, up to 60% of the cells were positive in the cytochemical stain using
      5-bromo-4-chloro-3-indolyl-beta-D-galactopyranoside (X-gal) as a chromogenic
      substrate. The efficiency of the transferrin receptor-mediated DNA uptake into
      Jurkat cells was comparatively low, although these cells were shown to express
      considerable amounts of transferrin receptor. We show here that a mucin-type
      carbohydrate antigen mediates highly efficient DNA uptake by endocytosis into
      Jurkat T cells. This method represents a 50-fold improvement of Jurkat cell
      transfection efficiency over other physical gene transfer techniques. Specific
      gene delivery to primary cancer cells exhibiting Tn epitopes may especially be
      desirable in immunotherapy protocols.
FAU - Thurnher, M
AU  - Thurnher M
AD  - Institute of Physiology, University of Zurich, Switzerland.
FAU - Wagner, E
AU  - Wagner E
FAU - Clausen, H
AU  - Clausen H
FAU - Mechtler, K
AU  - Mechtler K
FAU - Rusconi, S
AU  - Rusconi S
FAU - Dinter, A
AU  - Dinter A
FAU - Birnstiel, M L
AU  - Birnstiel ML
FAU - Berger, E G
AU  - Berger EG
FAU - Cotten, M
AU  - Cotten M
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - Glycobiology
JT  - Glycobiology
JID - 9104124
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Tn antigen)
RN  - 9007-49-2 (DNA)
SB  - IM
SB  - X
GS  - lacZ
MH  - Adenoviridae/genetics
MH  - Animals
MH  - Antibodies, Monoclonal
MH  - Antigens, Tumor-Associated, Carbohydrate/*genetics/metabolism
MH  - DNA/genetics
MH  - Gene Expression
MH  - *Gene Transfer Techniques
MH  - Genes, Reporter
MH  - Genetic Therapy
MH  - Genetic Vectors
MH  - Humans
MH  - Lac Operon
MH  - Leukemia, T-Cell/*genetics
MH  - Tumor Cells, Cultured/metabolism
EDAT- 1994/08/01 00:00
MHDA- 1994/08/01 00:01
CRDT- 1994/08/01 00:00
PHST- 1994/08/01 00:00 [pubmed]
PHST- 1994/08/01 00:01 [medline]
PHST- 1994/08/01 00:00 [entrez]
AID - 10.1093/glycob/4.4.429 [doi]
PST - ppublish
SO  - Glycobiology. 1994 Aug;4(4):429-35. doi: 10.1093/glycob/4.4.429.

PMID- 2429934
OWN - NLM
STAT- MEDLINE
DCOM- 19861211
LR  - 20160303
IS  - 0020-7136 (Print)
IS  - 0020-7136 (Linking)
VI  - 38
IP  - 5
DP  - 1986 Nov 15
TI  - Monoclonal antibody immunoradiometric assay for an antigenic determinant (CA 72) 
      on a novel pancarcinoma antigen (TAG-72).
PG  - 661-9
AB  - CA 72 is a monoclonal antibody (MAb) -defined antigenic determinant expressed on 
      a pancarcinoma antigen (TAG-72) found in more than 85% of human colorectal
      carcinomas. An immunoradiometric assay has been developed using the murine MAb
      B72.3 to quantitate CA 72 in human serum. In a simultaneous immunoradiometric
      assay, the mean CA 72 concentration in 1,099 serum samples from healthy blood
      donors was 1.83 +/- 2.03 (SD) units/ml. If the upper limit of normal was set at
      10 mu/mol of serum, a value including 99% of healthy blood donors, only 4 of 101 
      serum samples (4%) from patients with benign disease were elevated, whereas 15 of
      26 (58%) and 14 of 25 (56%) of rectal and colon carcinoma patient sera,
      respectively, were positive. Serum samples from 84 benign colorectal disease
      cases were examined; of these, 0 of 28 (0%) colorectal adenoma, 1 of 39 (3%)
      ulcerative proctocolitis, 0 of 15 (0%) diverticulosis, and 0 of 2 (0%) irritable 
      bowel disease sera contained more than 10 mu/ml CA 72. At a reference value of 20
      mu/ml, 0 of 101 (0%) benign disease and 2 of 1,060 (0.2%) blood donor sera had
      elevated values, whereas 10 of 26 (38%) and 9 of 25 (36%) rectal and colon
      patient sera, respectively, remained positive. The majority of patients with
      pancreatic and ovarian cancer, and a significant fraction of stomach cancer
      patient sera, also contained elevated levels of CA 72. The ability of this assay 
      to discriminate between malignant and benign diseases suggests its further
      evaluation for monitoring and diagnosis in groups at risk for development of
      cancer.
FAU - Klug, T L
AU  - Klug TL
FAU - Sattler, M A
AU  - Sattler MA
FAU - Colcher, D
AU  - Colcher D
FAU - Schlom, J
AU  - Schlom J
LA  - eng
PT  - Journal Article
PL  - United States
TA  - Int J Cancer
JT  - International journal of cancer
JID - 0042124
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens, Neoplasm)
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Epitopes)
RN  - 0 (Glycoproteins)
RN  - 0 (tumor-associated antigen 72)
SB  - IM
MH  - Adult
MH  - Age Factors
MH  - Analysis of Variance
MH  - *Antibodies, Monoclonal
MH  - Antigens, Neoplasm/*analysis
MH  - Antigens, Tumor-Associated, Carbohydrate
MH  - Colonic Neoplasms/immunology
MH  - Epitopes/*analysis
MH  - Female
MH  - Gastrointestinal Diseases/immunology
MH  - Glycoproteins/*analysis
MH  - Humans
MH  - Male
MH  - Middle Aged
MH  - Radioimmunoassay
MH  - Rectal Neoplasms/immunology
MH  - Sex Factors
MH  - Smoking
EDAT- 1986/11/15 00:00
MHDA- 1986/11/15 00:01
CRDT- 1986/11/15 00:00
PHST- 1986/11/15 00:00 [pubmed]
PHST- 1986/11/15 00:01 [medline]
PHST- 1986/11/15 00:00 [entrez]
PST - ppublish
SO  - Int J Cancer. 1986 Nov 15;38(5):661-9.

PMID- 1672317
OWN - NLM
STAT- MEDLINE
DCOM- 19910422
LR  - 20171116
IS  - 0022-1554 (Print)
IS  - 0022-1554 (Linking)
VI  - 39
IP  - 4
DP  - 1991 Apr
TI  - Qualitative difference of subcellular localization of tumor-associated
      carbohydrate (Le(x)) antigens in renal cell carcinoma and normal kidney.
PG  - 479-84
AB  - Renal cell carcinomas are immunohistochemically positive for oligosaccharides
      with the Le(x) determinant (Gal beta 1----4[Fuc alpha 1----3]GlcNAc) and its
      derivatives, as oncofetal antigens, and their expression is closely related to a 
      better prognosis of the patients. This study was designed to clarify the
      difference in antigen localization at the ultrastructural level between renal
      cell carcinoma and normal tissues. In normal kidneys, Le(x) detected by
      monoclonal antibody (MAb) FH 2 and sialylated extended Le(x) (sialyl Le(x)-i) by 
      MAb FH 6 were identified along the plasma membrane of microvilli of proximal
      tubule epithelial cells, with occasional immunoreactivity along the basolateral
      plasma membranes. Intracellular localization was very sparse. Renal cell
      carcinoma showed localization of Le(x) and sialyl Le(x)-i antigens along the cell
      membrane and in the cytosol as aggregates or filaments. Immunoreactive materials 
      were also observed in the lumen formed among carcinoma cells. The cytosolic
      immunoreactivity, not observed in the normal kidney, was regarded as "abnormal
      cytosolic accumulation" of the antigens. This pattern was more pronounced in
      clear-cell carcinoma. Pretreatment of specimens with chloroform-methanol, which
      extracts glycolipids, decreased immunoreactivity in carcinoma tissues,
      particularly that in the cytosol. The extracts contained substances
      immunoreactive for MAb FH6. Our study has demonstrated that (a) remarkable
      changes occur in the ultrastructural localization patterns of sialyl Le(x)-i and 
      Le(x) in renal cell carcinoma and (b) considerable amounts of glycolipids are
      contained in the substances with sialyl Le(x)-i deposited in the cytosol of
      clear-cell carcinoma.
FAU - Ohtani, H
AU  - Ohtani H
AD  - Department of Pathology II, Tohoku University School of Medicine, Sendai, Japan.
FAU - Fukushi, Y
AU  - Fukushi Y
FAU - Orikasa, S
AU  - Orikasa S
FAU - Nagura, H
AU  - Nagura H
LA  - eng
PT  - Comparative Study
PT  - Journal Article
PL  - United States
TA  - J Histochem Cytochem
JT  - The journal of histochemistry and cytochemistry : official journal of the
      Histochemistry Society
JID - 9815334
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Glycolipids)
RN  - 0 (Lewis X Antigen)
RN  - 7V31YC746X (Chloroform)
RN  - Y4S76JWI15 (Methanol)
SB  - IM
MH  - Adenocarcinoma/*immunology/metabolism/pathology/ultrastructure
MH  - Antibodies, Monoclonal
MH  - Antigens, Tumor-Associated, Carbohydrate/*immunology/metabolism
MH  - Cell Membrane/immunology/metabolism/ultrastructure
MH  - Chloroform
MH  - Cryopreservation
MH  - Female
MH  - Glycolipids/immunology/metabolism
MH  - Humans
MH  - Immunohistochemistry/methods
MH  - Kidney/cytology/*immunology/metabolism/ultrastructure
MH  - Kidney Neoplasms/*immunology/metabolism/pathology/ultrastructure
MH  - Lewis X Antigen/*immunology/metabolism
MH  - Male
MH  - Methanol
MH  - Microscopy, Immunoelectron
MH  - Middle Aged
EDAT- 1991/04/01 00:00
MHDA- 1991/04/01 00:01
CRDT- 1991/04/01 00:00
PHST- 1991/04/01 00:00 [pubmed]
PHST- 1991/04/01 00:01 [medline]
PHST- 1991/04/01 00:00 [entrez]
AID - 10.1177/39.4.1672317 [doi]
PST - ppublish
SO  - J Histochem Cytochem. 1991 Apr;39(4):479-84. doi: 10.1177/39.4.1672317.

PMID- 2429933
OWN - NLM
STAT- MEDLINE
DCOM- 19861211
LR  - 20160303
IS  - 0020-7136 (Print)
IS  - 0020-7136 (Linking)
VI  - 38
IP  - 5
DP  - 1986 Nov 15
TI  - Tumor-associated glycoprotein (TAG-72) detected in adenocarcinomas and benign
      lesions of the stomach.
PG  - 643-50
AB  - Murine monoclonal antibody (MAb) B72.3, prepared against a membrane-enriched
      extract of metastatic carcinoma and reactive with a high-molecular-weight
      determinant, designated tumor-associated glycoprotein (TAG)-72, was shown to be
      reactive immunohistochemically with 97% of a variety of primary adenocarcinomas
      of the stomach (n = 40). All "early" gastric carcinomas were reactive with MAb
      B72.3, although the average percentage cellular reactivity was lower than in
      "advanced" carcinomas. TAG-72 antigen was detected in benign lesions (i.e.
      adenomatous polyps and hyperplastic polyps) with intestinal metaplasia.
      Dysplastic lesions characterized by cellular atypia, abnormal differentiation,
      and disorganized mucosal architecture demonstrated higher TAG-72 expression than 
      non-dysplastic epithelia. In contrast, normal gastric mucosa was generally
      non-reactive with MAb B72.3. Assays using serial sections of normal, benign and
      malignant gastric tissues with two MAbs (B1.1 and COL-6) directed against
      distinct epitopes of carcinoembryonic antigen (CEA) demonstrated differential
      reactivity, confirming that TAG-72 and CEA are distinct, non-coordinately
      expressed antigens. Our results suggest that TAG-72 antigen may be expressed in
      malignant and dysplastic epithelial cells, as well as in intestinalized
      epithelium of the stomach which has been closely related to subsequent carcinoma 
      development. Hence, MAb B72.3 may be a useful immunohistochemical adjunct for
      detecting early foci of adenocarcinomas and premalignant lesions of the stomach.
FAU - Ohuchi, N
AU  - Ohuchi N
FAU - Thor, A
AU  - Thor A
FAU - Nose, M
AU  - Nose M
FAU - Fujita, J
AU  - Fujita J
FAU - Kyogoku, M
AU  - Kyogoku M
FAU - Schlom, J
AU  - Schlom J
LA  - eng
PT  - Journal Article
PL  - United States
TA  - Int J Cancer
JT  - International journal of cancer
JID - 0042124
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens, Neoplasm)
RN  - 0 (Carcinoembryonic Antigen)
RN  - 0 (Epitopes)
RN  - 0 (Glycoproteins)
RN  - 0 (tumor-associated antigen 72)
SB  - IM
MH  - Adenocarcinoma/*analysis
MH  - Animals
MH  - Antibodies, Monoclonal
MH  - Antigens, Neoplasm/*analysis
MH  - Carcinoembryonic Antigen/immunology
MH  - Cross Reactions
MH  - Epitopes/analysis
MH  - Glycoproteins/*analysis
MH  - Mice
MH  - Molecular Weight
MH  - Stomach Neoplasms/*analysis
EDAT- 1986/11/15 00:00
MHDA- 1986/11/15 00:01
CRDT- 1986/11/15 00:00
PHST- 1986/11/15 00:00 [pubmed]
PHST- 1986/11/15 00:01 [medline]
PHST- 1986/11/15 00:00 [entrez]
PST - ppublish
SO  - Int J Cancer. 1986 Nov 15;38(5):643-50.

PMID- 6165896
OWN - NLM
STAT- MEDLINE
DCOM- 19810820
LR  - 20171117
IS  - 0028-0836 (Print)
IS  - 0028-0836 (Linking)
VI  - 292
IP  - 5819
DP  - 1981 Jul 9
TI  - Stage-specific embryonic antigen involves alpha 1 goes to 3 fucosylated type 2
      blood group chains.
PG  - 156-8
FAU - Gooi, H C
AU  - Gooi HC
FAU - Feizi, T
AU  - Feizi T
FAU - Kapadia, A
AU  - Kapadia A
FAU - Knowles, B B
AU  - Knowles BB
FAU - Solter, D
AU  - Solter D
FAU - Evans, M J
AU  - Evans MJ
LA  - eng
PT  - Journal Article
PL  - England
TA  - Nature
JT  - Nature
JID - 0410462
RN  - 0 (Antigens)
RN  - 0 (Blood Group Antigens)
RN  - 0 (Epitopes)
RN  - 0 (Glycolipids)
RN  - 0 (Lewis X Antigen)
RN  - 0 (Oligosaccharides)
RN  - 28RYY2IV3F (Fucose)
SB  - IM
MH  - *Antigens
MH  - Blood Group Antigens/*immunology
MH  - Carbohydrate Conformation
MH  - Carbohydrate Sequence
MH  - Epitopes
MH  - Female
MH  - Fucose/analysis
MH  - *Glycolipids
MH  - Humans
MH  - Lewis X Antigen
MH  - Meconium/immunology
MH  - Oligosaccharides/analysis
MH  - Pregnancy
MH  - Radioimmunoassay
EDAT- 1981/07/09 00:00
MHDA- 1981/07/09 00:01
CRDT- 1981/07/09 00:00
PHST- 1981/07/09 00:00 [pubmed]
PHST- 1981/07/09 00:01 [medline]
PHST- 1981/07/09 00:00 [entrez]
PST - ppublish
SO  - Nature. 1981 Jul 9;292(5819):156-8.

PMID- 7142214
OWN - NLM
STAT- MEDLINE
DCOM- 19830119
LR  - 20071114
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 257
IP  - 23
DP  - 1982 Dec 10
TI  - A monoclonal antibody-defined antigen associated with gastrointestinal cancer is 
      a ganglioside containing sialylated lacto-N-fucopentaose II.
PG  - 14365-9
AB  - Two monoclonal antibodies produced by hybridomas obtained from a mouse immunized 
      with a colorectal carcinoma cell line bind specifically to human gastrointestinal
      cancer cells. The antigen of this antibody in the carcinoma cell line, a
      monosialoganglioside, has been isolated. Its carbohydrate structure is probably
      (formula: see text). This oligosaccharide is a sialyl derivative of
      lacto-N-fucopentaose II, a hapten of the human Lea blood group antigen. About 30 
      micrograms of ganglioside is obtained from 1 g of cells, wet weight. The
      ganglioside was detected by autoradiography in lipid extracts of some carcinomas 
      and of meconium, but not in lipid extracts of normal adult tissues. Antigen was
      detected by solid phase radioimmunoassay in lipid extracts from 12 out of 21
      adenocarcinomas of the colon, from 4 out of 5 gastric adenocarcinomas, and from 4
      out of 7 pancreatic carcinomas. Antigen was not detected in lipid extracts from 5
      esophageal carcinomas or from normal colon and gastric mucosa, pancreas, kidney, 
      liver, and bone marrow.
FAU - Magnani, J L
AU  - Magnani JL
FAU - Nilsson, B
AU  - Nilsson B
FAU - Brockhaus, M
AU  - Brockhaus M
FAU - Zopf, D
AU  - Zopf D
FAU - Steplewski, Z
AU  - Steplewski Z
FAU - Koprowski, H
AU  - Koprowski H
FAU - Ginsburg, V
AU  - Ginsburg V
LA  - eng
GR  - CA-10815/CA/NCI NIH HHS/United States
GR  - CA-21124/CA/NCI NIH HHS/United States
GR  - RR-05540/RR/NCRR NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens, Neoplasm)
RN  - 0 (Gangliosides)
RN  - 0 (Oligosaccharides)
SB  - IM
MH  - Animals
MH  - *Antibodies, Monoclonal
MH  - Antigens, Neoplasm/*analysis
MH  - Cell Line
MH  - Chromatography, Thin Layer
MH  - Colonic Neoplasms/*immunology
MH  - Gangliosides/*analysis
MH  - Gas Chromatography-Mass Spectrometry
MH  - Humans
MH  - Hybridomas/immunology
MH  - Mice
MH  - Oligosaccharides/*analysis
MH  - Radioimmunoassay
EDAT- 1982/12/10 00:00
MHDA- 1982/12/10 00:01
CRDT- 1982/12/10 00:00
PHST- 1982/12/10 00:00 [pubmed]
PHST- 1982/12/10 00:01 [medline]
PHST- 1982/12/10 00:00 [entrez]
PST - ppublish
SO  - J Biol Chem. 1982 Dec 10;257(23):14365-9.

PMID- 17467335
OWN - NLM
STAT- MEDLINE
DCOM- 20071011
LR  - 20070808
IS  - 1438-4221 (Print)
IS  - 1438-4221 (Linking)
VI  - 297
IP  - 5
DP  - 2007 Sep
TI  - Lipopolysaccharide in bacterial chronic infection: insights from Helicobacter
      pylori lipopolysaccharide and lipid A.
PG  - 307-19
AB  - Lipopolysaccharides are generally considered toxic components of the
      Gram-negative bacterial outer membrane with potent immunomodulating and
      immunostimulating properties, but their contribution to adaptation of a given
      bacterial species to its microbial niche is, however, predominantly overlooked.
      Helicobacter pylori, as a cause of long-term infection in the gastroduodenal
      tract, has been proposed as a model for investigating and understanding the
      dynamics of bacterial persistence and parasitism in chronic infections. This
      review examines the structure and properties of H. pylori lipopolysaccharide and 
      its lipid A moiety, and the insights that have been gained into their
      contribution to chronic infection and pathogenesis, including evasion and
      dampening of innate immune responses.
FAU - Moran, Anthony P
AU  - Moran AP
AD  - Department of Microbiology, National University of Ireland, Galway, University
      Road, Galway, Ireland. anthony.moran@nuigalway.ie
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Review
DEP - 20070427
PL  - Germany
TA  - Int J Med Microbiol
JT  - International journal of medical microbiology : IJMM
JID - 100898849
RN  - 0 (Lipid A)
RN  - 0 (Lipopolysaccharides)
RN  - 0 (Virulence Factors)
RN  - 0 (lipopolysaccharide, Helicobacter pylori)
SB  - IM
MH  - Helicobacter Infections/*microbiology
MH  - Helicobacter pylori/chemistry/*physiology
MH  - Humans
MH  - Lipid A/*chemistry/immunology
MH  - Lipopolysaccharides/*chemistry/immunology
MH  - Virulence Factors/*chemistry/immunology/*physiology
RF  - 121
EDAT- 2007/05/01 09:00
MHDA- 2007/10/12 09:00
CRDT- 2007/05/01 09:00
PHST- 2007/05/01 09:00 [pubmed]
PHST- 2007/10/12 09:00 [medline]
PHST- 2007/05/01 09:00 [entrez]
AID - S1438-4221(07)00045-8 [pii]
AID - 10.1016/j.ijmm.2007.03.008 [doi]
PST - ppublish
SO  - Int J Med Microbiol. 2007 Sep;297(5):307-19. doi: 10.1016/j.ijmm.2007.03.008.
      Epub 2007 Apr 27.

PMID- 10365852
OWN - NLM
STAT- MEDLINE
DCOM- 19990726
LR  - 20151119
IS  - 1320-5463 (Print)
IS  - 1320-5463 (Linking)
VI  - 49
IP  - 4
DP  - 1999 Apr
TI  - Expression of sialyl-Tn, Tn and T antigens in primary liver cancer.
PG  - 325-31
AB  - Sialyl-Tn, Tn and T antigens are caused by aberrant or incomplete glycosylation
      of apomucins and are related to the aggressiveness of malignant neoplasms. Using 
      41 liver samples from patients with cholangiocarcinoma (including four with
      cirrhosis), 21 with combined hepatocellular-cholangiocellular carcinoma and 17
      with hepatocellular carcinoma, the expression of sialyl-Tn, Tn and T antigens
      were characterized immunohistochemically and the correlation with apomucin
      profiles was evaluated. The prevalence of sialyl-Tn, Tn and T antigens expression
      was 89, 95 and 51% in cholangiocarcinoma without cirrhosis; 25, 75, and 0% in
      cholangiocarcinoma with cirrhosis; 29, 90, and 48% in combined
      hepatocellular-cholangiocellular carcinoma; and 0, 12 and 6% in hepatocellular
      carcinoma, respectively. Sialyl-Tn antigen was frequently expressed in
      cholangiocarcinoma without cirrhosis compared with cholangiocarcinoma with
      cirrhosis and combined hepatocellular-cholangiocellular carcinoma (P < 0.01).
      Although sialyl-Tn expression was associated with MUC1, MUC6 and MUC7 expression,
      the expression sites among them were not identical in the individual cases. These
      data suggest that the different expressions of sialyl-Tn antigen among
      cholangiocarcinoma without cirrhosis, cholangiocarcinoma with cirrhosis and
      combined hepatocellular-cholangiocellular carcinoma may reflect the biological
      features inherent to these tumors, such as the ability of invasion.
FAU - Sasaki, M
AU  - Sasaki M
AD  - Department of Pathology (II), Kanazawa University School of Medicine, Japan.
      msasaki@scarlet.ucdavis.edu
FAU - Yamato, T
AU  - Yamato T
FAU - Nakanuma, Y
AU  - Nakanuma Y
LA  - eng
PT  - Journal Article
PL  - Australia
TA  - Pathol Int
JT  - Pathology international
JID - 9431380
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Antigens, Viral, Tumor)
RN  - 0 (Biomarkers, Tumor)
RN  - 0 (Mucins)
RN  - 0 (Tn antigen)
RN  - 0 (sialosyl-Tn antigen)
SB  - IM
MH  - Antigens, Tumor-Associated, Carbohydrate/*biosynthesis
MH  - Antigens, Viral, Tumor/*biosynthesis
MH  - Biomarkers, Tumor/biosynthesis
MH  - Carcinoma, Hepatocellular/*metabolism
MH  - Cholangiocarcinoma/*metabolism
MH  - Humans
MH  - Immunohistochemistry
MH  - Liver Cirrhosis/metabolism
MH  - Liver Neoplasms/*metabolism
MH  - Mucins/metabolism
EDAT- 1999/06/12 00:00
MHDA- 1999/06/12 00:01
CRDT- 1999/06/12 00:00
PHST- 1999/06/12 00:00 [pubmed]
PHST- 1999/06/12 00:01 [medline]
PHST- 1999/06/12 00:00 [entrez]
PST - ppublish
SO  - Pathol Int. 1999 Apr;49(4):325-31.

PMID- 6653876
OWN - NLM
STAT- MEDLINE
DCOM- 19840214
LR  - 20151119
IS  - 0012-1606 (Print)
IS  - 0012-1606 (Linking)
VI  - 100
IP  - 2
DP  - 1983 Dec
TI  - Immunohistochemical localization of two monoclonal antibody-defined carbohydrate 
      antigens during early murine embryogenesis.
PG  - 318-27
AB  - Monoclonal antibodies designated "C6" and "A5" identify cell surface
      carbohydrates shared by embryonal carcinoma cells and early mouse embryos. The
      binding of both antibodies to F9 embryonal carcinoma cells was inhibited by
      N-acetyllactosamine. While antibody C6 did not agglutinate human erythrocytes,
      antibody A5 agglutinated adult, but not fetal, erythrocytes of both type A and O,
      suggesting partial specificity for branched polylactosamine structures.
      Antibodies C6 and A5 did not label preimplantation stage embryos; however,
      labeling with both antibodies was observed following treatment of embryos with
      neuraminidase. In paraffin sections of postimplantation stage embryos, C6 and A5 
      exhibited similar yet distinct patterns of labeling, restricted primarily to the 
      luminal surfaces of ectodermal and visceral endodermal epithelia. Neuraminidase
      treatment was found to expose additional patterns of C6 and A5 labeling within
      the ectoderm and mesoderm of the postimplantation embryo, not restricted to
      periluminal surfaces. These results suggest that cell surface carbohydrates are
      modified during early embryogenesis, in part, by selective patterns of
      sialylation.
FAU - Fenderson, B A
AU  - Fenderson BA
FAU - Hahnel, A C
AU  - Hahnel AC
FAU - Eddy, E M
AU  - Eddy EM
LA  - eng
GR  - HD-06220/HD/NICHD NIH HHS/United States
GR  - HD-14054/HD/NICHD NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, Non-P.H.S.
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Dev Biol
JT  - Developmental biology
JID - 0372762
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens, Surface)
RN  - 0 (Carbohydrates)
RN  - EC 3.2.1.18 (Neuraminidase)
SB  - IM
MH  - Animals
MH  - Antibodies, Monoclonal/*immunology
MH  - Antibody Specificity
MH  - Antigens, Surface/*immunology
MH  - Carbohydrates/*immunology
MH  - Embryo, Mammalian/*immunology
MH  - Embryonic Development
MH  - Epithelium/immunology
MH  - Female
MH  - Gestational Age
MH  - Mice
MH  - Neuraminidase
MH  - Pregnancy
MH  - Teratoma/*immunology
EDAT- 1983/12/01 00:00
MHDA- 1983/12/01 00:01
CRDT- 1983/12/01 00:00
PHST- 1983/12/01 00:00 [pubmed]
PHST- 1983/12/01 00:01 [medline]
PHST- 1983/12/01 00:00 [entrez]
AID - 0012-1606(83)90226-9 [pii]
PST - ppublish
SO  - Dev Biol. 1983 Dec;100(2):318-27.

PMID- 17195076
OWN - NLM
STAT- MEDLINE
DCOM- 20070801
LR  - 20131121
IS  - 0340-7004 (Print)
IS  - 0340-7004 (Linking)
VI  - 56
IP  - 8
DP  - 2007 Aug
TI  - The C-type lectin MGL expressed by dendritic cells detects glycan changes on MUC1
      in colon carcinoma.
PG  - 1225-36
AB  - The epithelial mucin MUC1 is a high molecular weight membrane glycoprotein
      frequently overexpressed and aberrantly glycosylated in adenocarcinoma. Mucins
      normally contain high amounts of O-linked carbohydrate structures that may
      influence immune reactions to this antigen. During malignant transformation,
      certain glyco-epitopes of MUC1, such as Tn-antigen, TF-antigen and their
      sialylated forms become exposed. The role of these glycan structures in tumor
      biology is unknown, but their presence is known to correlate with poor prognosis 
      in several adenocarcinomas. We analyzed the potency of MUC1 containing
      Tn-antigens (MUC1-Tn) to target C-type lectins that function as carbohydrate
      recognition and uptake molecules on dendritic cells (DC). We identified the
      macrophage galactose type C-type lectin (MGL), expressed by both DC and
      macrophages, as the receptor for recognition and binding of MUC1-Tn. To validate 
      the occurrence of MGL-MUC1 interactions in situ, we studied the binding of MGL to
      MUC1 in primary colon carcinoma tissue. Isolation of MUC1 out of colon carcinoma 
      tissue showed strong binding activity to MGL. Interestingly, MGL binding to MUC1 
      was highly correlated to binding by the lectin Helix pomatia agglutinin (HPA),
      which is associated with poor prognosis in colorectal cancer. The detection of
      MGL positive cells in situ at the tumor site together with the modified
      glycosylation status of MUC1 to target MGL on DC suggests that MGL positive
      antigen presenting cells may play a role in tumor progression.
FAU - Saeland, Eirikur
AU  - Saeland E
AD  - Department of Molecular Cell Biology and Immunology, VU University Medical
      Center, Amsterdam, The Netherlands.
FAU - van Vliet, Sandra J
AU  - van Vliet SJ
FAU - Backstrom, Malin
AU  - Backstrom M
FAU - van den Berg, Venice C M
AU  - van den Berg VC
FAU - Geijtenbeek, Teunis B H
AU  - Geijtenbeek TB
FAU - Meijer, Gerrit A
AU  - Meijer GA
FAU - van Kooyk, Yvette
AU  - van Kooyk Y
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20061229
PL  - Germany
TA  - Cancer Immunol Immunother
JT  - Cancer immunology, immunotherapy : CII
JID - 8605732
RN  - 0 (Antigens, Neoplasm)
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Cell Adhesion Molecules)
RN  - 0 (DC-specific ICAM-3 grabbing nonintegrin)
RN  - 0 (Immunoglobulin G)
RN  - 0 (Lectins, C-Type)
RN  - 0 (MGL lectin, human)
RN  - 0 (MUC1 protein, human)
RN  - 0 (Monosaccharides)
RN  - 0 (Mucin-1)
RN  - 0 (Mucins)
RN  - 0 (Neoplasm Proteins)
RN  - 0 (Receptors, Cell Surface)
RN  - 0 (Recombinant Fusion Proteins)
RN  - 0 (Tn antigen)
RN  - KM15WK8O5T (Acetylgalactosamine)
SB  - IM
MH  - Acetylgalactosamine/pharmacology
MH  - Adenocarcinoma/immunology/*metabolism
MH  - Animals
MH  - Antigens, Neoplasm/immunology/isolation & purification/*metabolism
MH  - Antigens, Tumor-Associated, Carbohydrate/immunology/*metabolism
MH  - CHO Cells
MH  - Cell Adhesion Molecules/immunology/metabolism
MH  - Colon/chemistry/cytology
MH  - Colonic Neoplasms/immunology/*metabolism
MH  - Cricetinae
MH  - Cricetulus
MH  - Dendritic Cells/immunology/*metabolism
MH  - Endocytosis
MH  - Female
MH  - Glycosylation
MH  - Humans
MH  - Immunoglobulin G/immunology
MH  - Intestinal Mucosa/chemistry/cytology
MH  - Lectins, C-Type/immunology/*metabolism
MH  - Mice
MH  - Mice, Inbred BALB C
MH  - Monocytes/cytology
MH  - Monosaccharides/pharmacology
MH  - Mucin-1
MH  - Mucins/immunology/isolation & purification/*metabolism
MH  - Neoplasm Proteins/immunology/isolation & purification/*metabolism
MH  - Protein Binding/drug effects
MH  - Protein Processing, Post-Translational
MH  - Protein Structure, Tertiary
MH  - Receptors, Cell Surface/immunology/metabolism
MH  - Recombinant Fusion Proteins/chemistry/immunology
MH  - Tandem Repeat Sequences
EDAT- 2006/12/30 09:00
MHDA- 2007/08/02 09:00
CRDT- 2006/12/30 09:00
PHST- 2006/07/28 00:00 [received]
PHST- 2006/11/25 00:00 [accepted]
PHST- 2006/12/30 09:00 [pubmed]
PHST- 2007/08/02 09:00 [medline]
PHST- 2006/12/30 09:00 [entrez]
AID - 10.1007/s00262-006-0274-z [doi]
PST - ppublish
SO  - Cancer Immunol Immunother. 2007 Aug;56(8):1225-36. doi:
      10.1007/s00262-006-0274-z. Epub 2006 Dec 29.

PMID- 10854286
OWN - NLM
STAT- MEDLINE
DCOM- 20000717
LR  - 20171116
IS  - 0022-3042 (Print)
IS  - 0022-3042 (Linking)
VI  - 75
IP  - 1
DP  - 2000 Jul
TI  - High-affinity anti-ganglioside IgG antibodies raised in complex ganglioside
      knockout mice: reexamination of GD1a immunolocalization.
PG  - 404-12
AB  - Gangliosides, sialic acid-bearing glycosphingolipids, are highly enriched in the 
      vertebrate nervous system. Anti-ganglioside antibodies are associated with
      various human neuropathies, although the pathogenicity of these antibodies
      remains unproven. Testing the pathogenic role of anti-ganglioside antibodies will
      be facilitated by developing high-affinity IgG-class complement-fixing monoclonal
      anti-bodies against major brain gangliosides, a goal that has been difficult to
      achieve. In this study, mice lacking complex gangliosides were used as
      immune-naive hosts to raise anti-ganglioside antibodies. Wild-type mice and
      knockout mice with a disrupted gene for GM2/GD2 synthase
      (UDP-N-acetyl-D-galactosamine : GM3/GD3 N-acetyl-D-glactosaminyltransferase) were
      immunized with GD1a conjugated to keyhole limpet hemocyanin. The knockout mice
      produced a vigorous anti-GD1a IgG response, whereas wildtype littermates failed
      to do so. Fusion of spleen cells from an immunized knockout mouse with myeloma
      cells yielded numerous IgG anti-GD1a antibody-producing colonies. Ganglioside
      binding studies revealed two specificity classes; one colony representing each
      class was cloned and characterized. High-affinity monoclonal antibody was
      produced by each hybridoma : an IgG1 that bound nearly exclusively to GD1a and an
      IgG2b that bound GD1a, GT1b, and GT1aalpha. Both antibodies readily readily
      detected gangliosides via ELISA, TLC immune overlay, immunohistochemistry, and
      immunocytochemistry. In contrast to prior reports using anti-GD1a and anti-GT1b
      IgM class monoclonal antibodies, the new antibodies bound avidly to granule
      neurons in brain tissue sections and cell cultures. Mice lacking complex
      gangliosides are improved hosts for raising high-affinity, high-titer
      anti-ganglioside IgG antibodies for probing for the distribution and physiology
      of gangliosides and the pathophysiology of anti-ganglioside antibodies.
FAU - Lunn, M P
AU  - Lunn MP
AD  - Department of. Neurology. Pharmacology. Neuroscience, Johns Hopkins Medical
      Institutions, Baltimore, Maryland, USA.
FAU - Johnson, L A
AU  - Johnson LA
FAU - Fromholt, S E
AU  - Fromholt SE
FAU - Itonori, S
AU  - Itonori S
FAU - Huang, J
AU  - Huang J
FAU - Vyas, A A
AU  - Vyas AA
FAU - Hildreth, J E
AU  - Hildreth JE
FAU - Griffin, J W
AU  - Griffin JW
FAU - Schnaar, R L
AU  - Schnaar RL
FAU - Sheikh, K A
AU  - Sheikh KA
LA  - eng
GR  - NS37096/NS/NINDS NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - England
TA  - J Neurochem
JT  - Journal of neurochemistry
JID - 2985190R
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Gangliosides)
RN  - 0 (Immunoglobulin G)
RN  - 12707-58-3 (ganglioside, GD1a)
RN  - 9013-72-3 (Hemocyanins)
RN  - EC 2.4.1.- (N-Acetylgalactosaminyltransferases)
RN  - EC 2.4.1.41 (polypeptide N-acetylgalactosaminyltransferase)
RN  - EC 2.4.1.92 ((N-acetylneuraminyl)-galactosylglucosylceramide
      N-acetylgalactosaminyltransferase)
RN  - FV4Y0JO2CX (keyhole-limpet hemocyanin)
SB  - IM
MH  - Animals
MH  - Antibodies, Monoclonal/biosynthesis/*immunology
MH  - *Antibody Affinity
MH  - Cerebellum/cytology
MH  - Gangliosides/*analysis/*immunology
MH  - Hemocyanins/immunology
MH  - Humans
MH  - Hybridomas/immunology
MH  - Immunization
MH  - Immunoglobulin G/*immunology
MH  - Immunohistochemistry
MH  - Mice
MH  - Mice, Knockout
MH  - N-Acetylgalactosaminyltransferases/*deficiency/genetics
MH  - Neurons/chemistry
EDAT- 2000/06/15 09:00
MHDA- 2000/07/25 11:00
CRDT- 2000/06/15 09:00
PHST- 2000/06/15 09:00 [pubmed]
PHST- 2000/07/25 11:00 [medline]
PHST- 2000/06/15 09:00 [entrez]
PST - ppublish
SO  - J Neurochem. 2000 Jul;75(1):404-12.

PMID- 1306106
OWN - NLM
STAT- MEDLINE
DCOM- 19930805
LR  - 20151119
IS  - 1055-9965 (Print)
IS  - 1055-9965 (Linking)
VI  - 1
IP  - 3
DP  - 1992 Mar-Apr
TI  - Prospective study of Lewis antigen alterations in the gastric precancerous
      process.
PG  - 199-205
AB  - A prospective study with two gastric biopsies taken several years apart was
      carried out in 117 subjects with intestinal metaplasia who are of the Lewis(a-b+)
      phenotype. They are residents of a rural Andean region in Colombia displaying
      very high rates of gastric cancer. The anomalous expression of Lewis(a) antigens 
      in the metaplastic epithelium carried a significantly increased risk of colonic
      metaplasia and dysplasia. Such risk was much higher when the simultaneous
      expression of sulfomucins and Lewis(a) antigen was observed.
FAU - Torrado, J
AU  - Torrado J
AD  - Department of Anatomic Pathology, Hospital Nuestra Sra. de Aranzazu, San
      Sebastian, Spain.
FAU - Correa, P
AU  - Correa P
FAU - Ruiz, B
AU  - Ruiz B
FAU - Zavala, D
AU  - Zavala D
FAU - Bara, J
AU  - Bara J
LA  - eng
GR  - P01-CA28842/CA/NCI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Cancer Epidemiol Biomarkers Prev
JT  - Cancer epidemiology, biomarkers & prevention : a publication of the American
      Association for Cancer Research, cosponsored by the American Society of
      Preventive Oncology
JID - 9200608
RN  - 0 (Biomarkers, Tumor)
RN  - 0 (Lewis Blood-Group System)
RN  - 0 (Mucins)
RN  - 0 (sulfomucin)
SB  - IM
MH  - Adult
MH  - Aged
MH  - Biomarkers, Tumor/*genetics
MH  - Biopsy
MH  - Colombia/epidemiology
MH  - Female
MH  - Gene Expression
MH  - Humans
MH  - Immunohistochemistry
MH  - Intestinal Diseases/epidemiology/genetics/*pathology
MH  - Lewis Blood-Group System/*genetics
MH  - Male
MH  - Metaplasia
MH  - Middle Aged
MH  - Mucins/genetics
MH  - Phenotype
MH  - Precancerous Conditions/epidemiology/genetics/*pathology
MH  - Prospective Studies
MH  - Risk Factors
MH  - Rural Population
MH  - Sensitivity and Specificity
MH  - Stomach Neoplasms/epidemiology/genetics/*pathology
EDAT- 1992/03/01 00:00
MHDA- 1992/03/01 00:01
CRDT- 1992/03/01 00:00
PHST- 1992/03/01 00:00 [pubmed]
PHST- 1992/03/01 00:01 [medline]
PHST- 1992/03/01 00:00 [entrez]
PST - ppublish
SO  - Cancer Epidemiol Biomarkers Prev. 1992 Mar-Apr;1(3):199-205.

PMID- 17652409
OWN - NLM
STAT- MEDLINE
DCOM- 20071212
LR  - 20131121
IS  - 0959-6658 (Print)
IS  - 0959-6658 (Linking)
VI  - 17
IP  - 10
DP  - 2007 Oct
TI  - Structural basis for recognition of breast and colon cancer epitopes Tn antigen
      and Forssman disaccharide by Helix pomatia lectin.
PG  - 1077-83
AB  - Helix pomatia agglutinin (HPA) is a lectin that has been used extensively in
      histopathology, since its binding to tissue sections from breast and colon
      cancers is correlated with the worst prognosis for the patients. The lectin
      recognizes alpha-d-N-acetylgalactosamine (alphaGalNAc) containing epitopes which 
      are only present in cancer cell lines having a high likelihood to undergo
      metastasis, such as the HT29 cancer colon cell line. Several breast cancer cell
      lines have also been shown to be labeled, although IGROV1, an ovarian cancer cell
      line, is not. Inhibition studies, using GalNAc monosaccharides, are reported
      here, showing that the labeling is dependent upon the presence of carbohydrate
      epitopes. The crystal structures of the lectin complexed with two GalNAc
      containing epitopes associated with cancer, the Tn (alphaGalNAc-Ser) and Forssman
      (alphaGalNAc1-3GalNAc) antigens, show the lectin's specificity for GalNAc is due 
      to a particular network of hydrogen bonds. A histidine residue makes hydrophobic 
      contact with the aglycon, rationalizing the preference for GalNAc bearing an
      additional sugar or amino acid in the alpha position. These structures provide
      the molecular basis for the use of HPA in metastasis research.
FAU - Lescar, Julien
AU  - Lescar J
AD  - Centre de Recherches sur les Macromolecules Vegetales, CNRS, BP53, 38041 Grenoble
      Cedex 09, France.
FAU - Sanchez, Jean-Frederic
AU  - Sanchez JF
FAU - Audfray, Aymeric
AU  - Audfray A
FAU - Coll, Jean-Luc
AU  - Coll JL
FAU - Breton, Christelle
AU  - Breton C
FAU - Mitchell, Edward P
AU  - Mitchell EP
FAU - Imberty, Anne
AU  - Imberty A
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20070725
PL  - England
TA  - Glycobiology
JT  - Glycobiology
JID - 9104124
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Disaccharides)
RN  - 0 (Epitopes)
RN  - 0 (Helix lectin)
RN  - 0 (Lectins)
RN  - 0 (Tn antigen)
RN  - 9013-60-9 (Forssman Antigen)
RN  - KM15WK8O5T (Acetylgalactosamine)
SB  - IM
MH  - Acetylgalactosamine/metabolism
MH  - Antigens, Tumor-Associated, Carbohydrate/*chemistry/metabolism
MH  - Breast Neoplasms/*chemistry/metabolism
MH  - Colonic Neoplasms/*chemistry/metabolism
MH  - Disaccharides/*chemistry/metabolism
MH  - *Epitopes
MH  - Female
MH  - Forssman Antigen/*chemistry/metabolism
MH  - Humans
MH  - Lectins/*chemistry/metabolism
EDAT- 2007/07/27 09:00
MHDA- 2007/12/13 09:00
CRDT- 2007/07/27 09:00
PHST- 2007/07/27 09:00 [pubmed]
PHST- 2007/12/13 09:00 [medline]
PHST- 2007/07/27 09:00 [entrez]
AID - cwm077 [pii]
AID - 10.1093/glycob/cwm077 [doi]
PST - ppublish
SO  - Glycobiology. 2007 Oct;17(10):1077-83. doi: 10.1093/glycob/cwm077. Epub 2007 Jul 
      25.

PMID- 2449128
OWN - NLM
STAT- MEDLINE
DCOM- 19880304
LR  - 20131121
IS  - 0003-9861 (Print)
IS  - 0003-9861 (Linking)
VI  - 260
IP  - 1
DP  - 1988 Jan
TI  - Monoclonal antibody R24 distinguishes between different N-acetyl- and
      N-glycolylneuraminic acid derivatives of ganglioside GD3.
PG  - 51-5
AB  - Monoclonal antibody (MAb) R24 was previously shown to be directed toward
      ganglioside GD3 [Pukel, C. S., Lloyd, K. O., Travassos, L. R., Dippold, W. G.,
      Oettgen, H. F., and Old, L. J. (1982) J. Exp. Med. 155, 1133-1147]. The
      structural specificity of the MAb has now been further characterized based on
      binding to structurally related glycolipids, including four GD3 derivatives with 
      different N-acetylneuraminic acid (NeuAc) and N-glycolylneuraminic acid (NeuGc)
      substituents. Three assay systems (enzyme immunostaining on thin-layer
      chromatography, enzyme-linked immunosorbent assay, and immune adherence
      inhibition assay) were used. MAb R24 was found to react with (NeuAc-NeuAc-)GD3
      and (NeuAc-NeuGc-)GD3 but not with (NeuGc-NeuAc-)GD3 or (NeuGc-NeuGc-)GD3. These 
      results clearly indicate that the outer sialic acid (Sia) moiety of GD3 is
      crucial and must be a NeuAc residue, while the inner sialic acid is less involved
      in binding to the MAb and can be either NeuAc or NeuGc. The MAb was also found to
      cross-react weakly with two gangliosides, GT1a and GQ1b, but none of other
      gangliosides nor neutral glycolipids tested reacted. These findings suggest that 
      the epitope detected by MAb R24 is the trisaccharide structure NeuAc alpha
      2----8Sia alpha 2----3Gal-, which must be in a terminal position.
FAU - Tai, T
AU  - Tai T
AD  - Department of Oncology, Tokyo Metropolitan Institute of Medical Science, Japan.
FAU - Kawashima, I
AU  - Kawashima I
FAU - Furukawa, K
AU  - Furukawa K
FAU - Lloyd, K O
AU  - Lloyd KO
LA  - eng
GR  - CA-08748/CA/NCI NIH HHS/United States
GR  - CA-21445/CA/NCI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Arch Biochem Biophys
JT  - Archives of biochemistry and biophysics
JID - 0372430
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Epitopes)
RN  - 0 (Gangliosides)
RN  - 0 (Glycolipids)
RN  - 0 (Sialic Acids)
RN  - 62010-37-1 (ganglioside, GD3)
RN  - GZP2782OP0 (N-Acetylneuraminic Acid)
SB  - IM
MH  - Animals
MH  - Antibodies, Monoclonal/*analysis
MH  - Antigen-Antibody Reactions
MH  - Cattle
MH  - Chromatography, Thin Layer
MH  - Epitopes/immunology
MH  - Gangliosides/*immunology
MH  - Glycolipids/immunology
MH  - Humans
MH  - Leukocyte Adherence Inhibition Test
MH  - Mice
MH  - N-Acetylneuraminic Acid
MH  - Sialic Acids/*immunology
EDAT- 1988/01/01 00:00
MHDA- 1988/01/01 00:01
CRDT- 1988/01/01 00:00
PHST- 1988/01/01 00:00 [pubmed]
PHST- 1988/01/01 00:01 [medline]
PHST- 1988/01/01 00:00 [entrez]
AID - 0003-9861(88)90423-7 [pii]
PST - ppublish
SO  - Arch Biochem Biophys. 1988 Jan;260(1):51-5.

PMID- 2139874
OWN - NLM
STAT- MEDLINE
DCOM- 19900613
LR  - 20071115
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 265
IP  - 14
DP  - 1990 May 15
TI  - Sialylpentaosylceramide detected with anti-GM2 monoclonal antibody. Structural
      characterization and complementary expression with GM2 in gastric cancer and
      normal gastric mucosa.
PG  - 7880-5
AB  - The ganglioside fraction of human gastric mucosa was analyzed with a newly
      established anti-GM2 monoclonal antibody KM531. Using this antibody, accumulation
      of GM2 was observed in all of four cases of gastric carcinoma. In all ganglioside
      fractions extracted from normal gastric mucosa obtained from eight cases of
      peptic ulcer GM2 itself was not detected, but three kinds of glycolipid showing
      slower mobility than GM2 on thin-layer plates were detected by immunostaining
      with KM531. These glycolipids were assigned as NGM-1, -2, and -3. They were
      completely lost in all carcinoma tissues and in non-cancerous gastric mucosa from
      two cases of gastric cancer, and they were also not detected in the ganglioside
      fraction of small or large intestine. Of these glycolipids, the major one, NGM-1,
      was isolated from the pooled ganglioside fraction of normal gastric mucosa
      obtained from cases of peptic ulcer. The structure was determined by proton
      nuclear magnetic resonance, negative ion fast atom bombardment-mass spectrometry,
      gas chromatography-mass spectrometry, and treatment with exoglycosidases and mild
      acid hydrolysis. The structure was GalNAc beta 1----4(NeuAc alpha 2----3) Gal
      beta 1----4GlcNAc beta 1----3 Gal beta 1----4Glc beta 1----1Cer, which has the
      same terminal sequence as GM2 but has internal neolacto series structure. This
      epitope was previously identified as Cad blood group antigen. The decrease of
      this glycolipid and the increase of GM2 was considered to be a cancer-associated 
      change in gastric mucosa.
FAU - Dohi, T
AU  - Dohi T
AD  - Division of Clinical Biochemistry, National Medical Center, Tokyo, Japan.
FAU - Ohta, S
AU  - Ohta S
FAU - Hanai, N
AU  - Hanai N
FAU - Yamaguchi, K
AU  - Yamaguchi K
FAU - Oshima, M
AU  - Oshima M
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Gangliosides)
RN  - 19600-01-2 (G(M2) Ganglioside)
RN  - 97708-84-4 (NGM-1)
RN  - EC 3.2.1.52 (beta-N-Acetylhexosaminidases)
SB  - IM
MH  - Antibodies, Monoclonal
MH  - Carbohydrate Conformation
MH  - Carbohydrate Sequence
MH  - G(M2) Ganglioside/*analogs & derivatives/*analysis
MH  - Gangliosides/*analysis
MH  - Gas Chromatography-Mass Spectrometry
MH  - Gastric Mucosa/*analysis
MH  - Humans
MH  - Magnetic Resonance Spectroscopy
MH  - Mass Spectrometry
MH  - Molecular Sequence Data
MH  - Stomach Neoplasms/*analysis
MH  - Stomach Ulcer/metabolism
MH  - beta-N-Acetylhexosaminidases/metabolism
EDAT- 1990/05/15 00:00
MHDA- 1990/05/15 00:01
CRDT- 1990/05/15 00:00
PHST- 1990/05/15 00:00 [pubmed]
PHST- 1990/05/15 00:01 [medline]
PHST- 1990/05/15 00:00 [entrez]
PST - ppublish
SO  - J Biol Chem. 1990 May 15;265(14):7880-5.

PMID- 6498849
OWN - NLM
STAT- MEDLINE
DCOM- 19850103
LR  - 20071114
IS  - 0008-5472 (Print)
IS  - 0008-5472 (Linking)
VI  - 44
IP  - 12 Pt 1
DP  - 1984 Dec
TI  - Detection of ganglioside GD2 in tumor tissues and sera of neuroblastoma patients.
PG  - 5914-20
AB  - A murine monoclonal antibody (monoclonal antibody 126) produced against cultured 
      human neuroblastoma cells (LAN-1) was found to be specifically directed to a
      disialoganglioside (GD2) antigen preferentially expressed on both cell lines and 
      tissues derived from melanoma and neuroblastoma. In enzyme-linked immunosorbent
      assays, monoclonal antibody 126 failed to react with leukemic and lymphoblastoid 
      cells as well as with a variety of carcinoma and sarcoma cell lines.
      Immunohistological analysis by the immunoperoxidase technique revealed strong
      reactivity of monoclonal antibody 126 with frozen and formaldehyde-fixed
      neuroblastoma and melanoma tissues. Tissues from patients with glioma or with
      small cell cancer of the lung showed faint staining, whereas those from
      individuals with sarcoma, lymphoma, and a variety of other neoplasms proved to be
      negative. Sera of neuroblastoma patients showed significantly elevated GD2 levels
      compared to normal children (p less than 0.001) and children with other tumors (p
      less than 0.001) as determined by a quantitative competitive enzyme-linked
      immunosorbent assay. Furthermore, the GD2 serum level of one neuroblastoma
      patient, when followed serially, was found to correlate with progression of
      disease, suggesting the potential usefulness of this assay for the diagnosis and 
      monitoring of neuroblastoma.
FAU - Schulz, G
AU  - Schulz G
FAU - Cheresh, D A
AU  - Cheresh DA
FAU - Varki, N M
AU  - Varki NM
FAU - Yu, A
AU  - Yu A
FAU - Staffileno, L K
AU  - Staffileno LK
FAU - Reisfeld, R A
AU  - Reisfeld RA
LA  - eng
GR  - 1F32 CA07544-01/CA/NCI NIH HHS/United States
GR  - CA28420/CA/NCI NIH HHS/United States
PT  - Comparative Study
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Cancer Res
JT  - Cancer research
JID - 2984705R
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Gangliosides)
RN  - 65988-71-8 (ganglioside, GD2)
SB  - IM
MH  - Antibodies, Monoclonal
MH  - Cell Line
MH  - Enzyme-Linked Immunosorbent Assay
MH  - Gangliosides/*analysis/blood
MH  - Humans
MH  - Neoplasms/analysis
MH  - Neuroblastoma/*analysis/blood/pathology
EDAT- 1984/12/01 00:00
MHDA- 1984/12/01 00:01
CRDT- 1984/12/01 00:00
PHST- 1984/12/01 00:00 [pubmed]
PHST- 1984/12/01 00:01 [medline]
PHST- 1984/12/01 00:00 [entrez]
PST - ppublish
SO  - Cancer Res. 1984 Dec;44(12 Pt 1):5914-20.

PMID- 1627599
OWN - NLM
STAT- MEDLINE
DCOM- 19920817
LR  - 20161126
IS  - 0006-3002 (Print)
IS  - 0006-3002 (Linking)
VI  - 1117
IP  - 1
DP  - 1992 Jul 21
TI  - Generation of one set of monoclonal antibodies specific for a-pathway
      ganglio-series gangliosides.
PG  - 97-103
AB  - We established five murine monoclonal antibodies (MAbs) specific for a-pathway
      ganglio-series gangliosides by immunizing C3H/HeN mice with these purified
      gangliosides adsorbed to Salmonella minnesota, followed by fusion with mouse
      myeloma cells. The binding specificities of these MAbs were determined by
      enzyme-linked immunosorbent assay and immunostaining on thin-layer chromatogram. 
      These five MAbs, designated GMR6, GMB28, GMB16, GMR17, and GMR11 reacted strongly
      with the gangliosides GM3, GM2, GM1, GD1a, and GT1a, respectively, that were used
      as immunogens. Three MAbs, GMB28 (anti-GM2), GMB16 (anti-GM1), and GMR11
      (anti-GT1a) showed highly restricted binding specificities, reacting only with
      the immunizing ganglioside. None of the other various authentic gangliosides or
      neutral glycolipids was recognized. On the other hand, the other two MAbs, GMR6
      (anti-GM3) and GMR17 (anti-GD1a) exhibited broader specificities. MAb GMR6
      cross-reacted with GM4, GM1b, GD1a, GT1b, and IV3NeuAc alpha-nLc4Cer. MAb GMR17
      also reacted with GM1b and GT1b. Neither GMR6 nor GMR17 reacted with other
      gangliosides or neutral glycolipids tested. Using these MAbs, we determined the
      expression of these gangliosides, especially GM1, GD1a, and GT1a on mouse, rat
      and human leukemia cells. GM1 and GD1a were expressed on some leukemia cells,
      whereas GT1a was not detected in these cells.
FAU - Kotani, M
AU  - Kotani M
AD  - Tokyo Metropolitan Institute of Medical Science, Department of Tumor Immunology, 
      Japan.
FAU - Ozawa, H
AU  - Ozawa H
FAU - Kawashima, I
AU  - Kawashima I
FAU - Ando, S
AU  - Ando S
FAU - Tai, T
AU  - Tai T
LA  - eng
PT  - Comparative Study
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - Netherlands
TA  - Biochim Biophys Acta
JT  - Biochimica et biophysica acta
JID - 0217513
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Gangliosides)
RN  - 0 (Glycolipids)
RN  - 0 (Immunoglobulin Isotypes)
SB  - IM
MH  - Animals
MH  - Antibodies, Monoclonal/immunology/*isolation & purification
MH  - Carbohydrate Sequence
MH  - Enzyme-Linked Immunosorbent Assay
MH  - Gangliosides/analysis/*immunology
MH  - Glycolipids/analysis/*immunology
MH  - Humans
MH  - Hybridomas/immunology
MH  - Immunoenzyme Techniques
MH  - Immunoglobulin Isotypes/*immunology
MH  - Mice
MH  - Mice, Inbred Strains
MH  - Molecular Sequence Data
MH  - Rats
MH  - Tumor Cells, Cultured/chemistry
EDAT- 1992/07/21 00:00
MHDA- 1992/07/21 00:01
CRDT- 1992/07/21 00:00
PHST- 1992/07/21 00:00 [pubmed]
PHST- 1992/07/21 00:01 [medline]
PHST- 1992/07/21 00:00 [entrez]
AID - 0304-4165(92)90168-T [pii]
PST - ppublish
SO  - Biochim Biophys Acta. 1992 Jul 21;1117(1):97-103.

PMID- 1618769
OWN - NLM
STAT- MEDLINE
DCOM- 19920806
LR  - 20071114
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 267
IP  - 18
DP  - 1992 Jun 25
TI  - O-acetylated gangliosides in bovine buttermilk. Characterization of 7-O-acetyl,
      9-O-acetyl, and 7,9-di-O-acetyl GD3.
PG  - 12632-8
AB  - Three O-acetylated gangliosides, G1, G2, and G3, were purified from bovine
      buttermilk by using chloroform/methanol extraction, Folch partitioning,
      chromatography on DEAE-Sephadex A-25, and Iatrobeads columns. The final yields of
      gangliosides G1, G2, and G3 were 2 mg, 37 mg, and 40 mg per 1.7 kg of the
      buttermilk powder, respectively. On the basis of immunostaining on high
      performance thin layer chromatography with specific monoclonal antibodies, mild
      alkaline treatment, gas-liquid chromatographic analysis, fast atom bombardment
      mass spectrometry, and proton nuclear magnetic resonance studies, G1 and G2 are
      characterized as O-acetylated GD3 and G3 as O-acetylated GT3, and the structures 
      of these gangliosides are as follows: [formula: see text] The major fatty acids
      of these gangliosides were C18:0, C22:0, C23:0, and C24:0, and the long chain
      base was C18-sphingosine.
FAU - Ren, S
AU  - Ren S
AD  - Department of Biochemistry and Molecular Biophysics, Medical College of Virginia,
      Virginia Commonwealth University, Richmond 23298.
FAU - Scarsdale, J N
AU  - Scarsdale JN
FAU - Ariga, T
AU  - Ariga T
FAU - Zhang, Y
AU  - Zhang Y
FAU - Klein, R A
AU  - Klein RA
FAU - Hartmann, R
AU  - Hartmann R
FAU - Kushi, Y
AU  - Kushi Y
FAU - Egge, H
AU  - Egge H
FAU - Yu, R K
AU  - Yu RK
LA  - eng
GR  - NS 26994/NS/NINDS NIH HHS/United States
GR  - NS-11853/NS/NINDS NIH HHS/United States
GR  - NS-23102/NS/NINDS NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Gangliosides)
RN  - 8029-34-3 (Butter)
SB  - IM
MH  - Acetylation
MH  - Animals
MH  - Antibodies, Monoclonal/immunology
MH  - Butter/*analysis
MH  - Carbohydrate Sequence
MH  - Chromatography, Thin Layer
MH  - Gangliosides/*analysis/chemistry/immunology
MH  - Mass Spectrometry
MH  - Milk/*analysis
MH  - Molecular Sequence Data
MH  - Molecular Structure
EDAT- 1992/06/25 00:00
MHDA- 1992/06/25 00:01
CRDT- 1992/06/25 00:00
PHST- 1992/06/25 00:00 [pubmed]
PHST- 1992/06/25 00:01 [medline]
PHST- 1992/06/25 00:00 [entrez]
PST - ppublish
SO  - J Biol Chem. 1992 Jun 25;267(18):12632-8.

PMID- 1121486
OWN - NLM
STAT- MEDLINE
DCOM- 19750621
LR  - 20071102
IS  - 0037-9727 (Print)
IS  - 0037-9727 (Linking)
VI  - 148
IP  - 2
DP  - 1975 Feb
TI  - Subcellular location of human parathyroid hormone immunoreactive peptides and
      preliminary evidence for a precursor to human PTH-1 (38545).
PG  - 387-92
FAU - Wong, E T
AU  - Wong ET
FAU - Lindall, A W
AU  - Lindall AW
LA  - eng
PT  - Journal Article
PL  - United States
TA  - Proc Soc Exp Biol Med
JT  - Proceedings of the Society for Experimental Biology and Medicine. Society for
      Experimental Biology and Medicine (New York, N.Y.)
JID - 7505892
RN  - 0 (Parathyroid Hormone)
RN  - 0 (Peptides)
SB  - IM
MH  - Cell Fractionation
MH  - Chromatography, Gel
MH  - Humans
MH  - Microsomes/metabolism
MH  - Molecular Weight
MH  - Parathyroid Glands/*metabolism/ultrastructure
MH  - Parathyroid Hormone/immunology/*metabolism
MH  - Peptides/isolation & purification/*metabolism
MH  - Radioimmunoassay
EDAT- 1975/02/01 00:00
MHDA- 1975/02/01 00:01
CRDT- 1975/02/01 00:00
PHST- 1975/02/01 00:00 [pubmed]
PHST- 1975/02/01 00:01 [medline]
PHST- 1975/02/01 00:00 [entrez]
PST - ppublish
SO  - Proc Soc Exp Biol Med. 1975 Feb;148(2):387-92.

PMID- 18824562
OWN - NLM
STAT- MEDLINE
DCOM- 20090213
LR  - 20081127
IS  - 1460-2423 (Electronic)
IS  - 0959-6658 (Linking)
VI  - 18
IP  - 12
DP  - 2008 Dec
TI  - Identification of the Drosophila core 1 beta1,3-galactosyltransferase gene that
      synthesizes T antigen in the embryonic central nervous system and hemocytes.
PG  - 1094-104
LID - 10.1093/glycob/cwn094 [doi]
AB  - T antigen (Galbeta1-3GalNAcalpha1-Ser/Thr), the well-known tumor-associated
      antigen, is a core 1 mucin-type O-glycan structure that is synthesized by core 1 
      beta1,3-galactosyltransferase (C1beta3GalT), which transfers Gal from UDP-Gal to 
      Tn antigen (GalNAcalpha1-Ser/Thr). Three putative C1beta3GalTs have been
      identified in Drosophila. However, although all three are expressed in embryos,
      their roles during embryogenesis have not yet been clarified. In this study, we
      used P-element inserted mutants to show that CG9520, one of the three putative
      C1beta3GalTs, synthesizes T antigen expressed on the central nervous system (CNS)
      during embryogenesis. We also found that T antigen was expressed on a subset of
      the embryonic hemocytes. CG9520 mutant embryos showed the loss of T antigens on
      the CNS and on a subset of hemocytes. Then, the loss of T antigens was rescued by
      precise excision of the P-element inserted into the CG9520 gene. Our data
      demonstrate that T antigens expressed on the CNS and on a subset of hemocytes are
      synthesized by CG9520 in the Drosophila embryo. In addition, we found that the
      number of circulating hemocytes was reduced in third instar larvae of CG9520
      mutant. We, therefore, named the CG9520 gene Drosophila core 1
      beta1,3-galactosyltransferase 1 because it is responsible for the synthesis and
      function of T antigen in vivo.
FAU - Yoshida, Hideki
AU  - Yoshida H
AD  - Department of Bioinformatics, Laboratory of Cell Biology, Faculty of Engineering,
      Soka University, 1-236 Tangi-cho, Hachioji, Tokyo 192-8577.
FAU - Fuwa, Takashi J
AU  - Fuwa TJ
FAU - Arima, Mikiko
AU  - Arima M
FAU - Hamamoto, Hiroshi
AU  - Hamamoto H
FAU - Sasaki, Norihiko
AU  - Sasaki N
FAU - Ichimiya, Tomomi
AU  - Ichimiya T
FAU - Osawa, Ken-Ichi
AU  - Osawa K
FAU - Ueda, Ryu
AU  - Ueda R
FAU - Nishihara, Shoko
AU  - Nishihara S
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20080929
PL  - England
TA  - Glycobiology
JT  - Glycobiology
JID - 9104124
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Drosophila Proteins)
RN  - 3554-90-3 (Thomsen-Friedenreich antigen)
RN  - EC 2.4.1.- (Galactosyltransferases)
RN  - EC 2.4.1.- (core 1 beta1,3-galactosyltransferase, Drosophila)
SB  - IM
MH  - Animals
MH  - Antigens, Tumor-Associated, Carbohydrate/*biosynthesis/immunology
MH  - Central Nervous System/metabolism
MH  - Drosophila/*embryology/*enzymology/genetics
MH  - Drosophila Proteins/*genetics
MH  - Embryo, Nonmammalian/enzymology
MH  - Galactosyltransferases/*genetics
MH  - Hemocytes/*metabolism
MH  - Histocytochemistry
MH  - Mutation
MH  - Phylogeny
EDAT- 2008/10/01 09:00
MHDA- 2009/02/14 09:00
CRDT- 2008/10/01 09:00
PHST- 2008/10/01 09:00 [pubmed]
PHST- 2009/02/14 09:00 [medline]
PHST- 2008/10/01 09:00 [entrez]
AID - cwn094 [pii]
AID - 10.1093/glycob/cwn094 [doi]
PST - ppublish
SO  - Glycobiology. 2008 Dec;18(12):1094-104. doi: 10.1093/glycob/cwn094. Epub 2008 Sep
      29.

PMID- 1674292
OWN - NLM
STAT- MEDLINE
DCOM- 19910618
LR  - 20171116
IS  - 0145-2126 (Print)
IS  - 0145-2126 (Linking)
VI  - 15
IP  - 4
DP  - 1991
TI  - Expression of CD15 as predictor of relapse in children with acute lymphoblastic
      leukemia of the pre-B type.
PG  - 189-94
AB  - Pre-B acute lymphoblastic leukemia (ALL) was diagnosed in 37 children
      morphologically, histochemically, and by immunophenotyping by flow cytometry. In 
      all patients the leukemic blasts expressed HLA-DR and CD19 (Leu-12). In 10
      patients 20% or more of the blast cells expressed a myeloid antigen: CD15
      (Leu-M1) in seven, CD33 (My9) in two and CD13 (My7) in one patient. All 37
      children achieved complete remission, but eight relapsed. Relapse occurred in six
      of seven patients with CD15-positive blasts, but in only two of 27 patients with 
      CD15-negative blasts (p = 0.0003). Thus, the occurrence of CD15 on the blasts of 
      children with pre-B ALL shows a remarkable association with a high risk of
      relapse, and these patients should therefore be considered to belong to the
      high-risk group regardless of other prognostic factors.
FAU - Lenkei, R
AU  - Lenkei R
AD  - Department of Immunology, National Bacteriological Laboratory, Stockholm, Sweden.
FAU - Bjork, O
AU  - Bjork O
FAU - Ost, A
AU  - Ost A
FAU - Biberfeld, P
AU  - Biberfeld P
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - Leuk Res
JT  - Leukemia research
JID - 7706787
RN  - 0 (Antigens, CD)
RN  - 0 (Antigens, Differentiation)
RN  - 0 (Antigens, Differentiation, Myelomonocytic)
RN  - 0 (Antigens, Neoplasm)
RN  - 0 (Lewis X Antigen)
RN  - EC 3.4.24.11 (Neprilysin)
SB  - IM
MH  - Adolescent
MH  - Antigens, CD/*metabolism
MH  - Antigens, Differentiation/*metabolism
MH  - Antigens, Differentiation, Myelomonocytic/*metabolism
MH  - Antigens, Neoplasm/metabolism
MH  - Child
MH  - Child, Preschool
MH  - Female
MH  - Humans
MH  - Immunophenotyping
MH  - Infant
MH  - Infant, Newborn
MH  - Lewis X Antigen
MH  - Male
MH  - Neprilysin
MH  - Precursor B-Cell Lymphoblastic Leukemia-Lymphoma/*immunology/pathology
MH  - Precursor Cell Lymphoblastic Leukemia-Lymphoma/*immunology/pathology
MH  - Prognosis
EDAT- 1991/01/01 00:00
MHDA- 1991/01/01 00:01
CRDT- 1991/01/01 00:00
PHST- 1991/01/01 00:00 [pubmed]
PHST- 1991/01/01 00:01 [medline]
PHST- 1991/01/01 00:00 [entrez]
PST - ppublish
SO  - Leuk Res. 1991;15(4):189-94.

PMID- 16413042
OWN - NLM
STAT- MEDLINE
DCOM- 20060509
LR  - 20131121
IS  - 0031-9422 (Print)
IS  - 0031-9422 (Linking)
VI  - 67
IP  - 4
DP  - 2006 Feb
TI  - Isolation and characterisation of a Salvia bogotensis seed lectin specific for
      the Tn antigen.
PG  - 347-55
AB  - A lectin was isolated and characterised from Salvia bogotensis seeds. Removal of 
      the abundant pigments and polysaccharides, which are present in seeds, was an
      essential step in its purification. Several procedures were assayed and the best 
      suited, including Pectinex treatment, DEAE-cellulose and affinity chromatography,
      led to a protein being obtained amounting to 18-20mg/100g seeds having high
      specific agglutination activity (SAA). The lectin specifically agglutinated human
      Tn erythrocytes and was inhibited by 37mM GalNAc, 0.019mM ovine submaxillary
      mucin (OSM) or 0.008mM asialo bovine submaxillary mucin (aBSM). Enzyme-linked
      lectinosorbent assay (ELLSA) revealed strong binding to aOSM and aBSM,
      corroborating Tn specificity, whereas no binding to fetuin or asialo fetuin was
      observed. The lectin's monomer MW (38,702Da), amino acid composition, pI,
      carbohydrate content, deglycosylated form MW, thermal stability and Ca(2+) and
      Mn(2+) requirements were determined. Evidence of the existence of two glycoforms 
      was obtained. The lectin's specificity and high affinity for the Tn antigen,
      commonly found in tumour cells, makes this protein a useful tool for
      immunohistochemical and cellular studies.
FAU - Vega, Nohora
AU  - Vega N
AD  - Biochemistry Laboratory, Chemistry Department, Universidad Nacional de Colombia, 
      Bogota, Colombia.
FAU - Perez, Gerardo
AU  - Perez G
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20060118
PL  - England
TA  - Phytochemistry
JT  - Phytochemistry
JID - 0151434
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Asialoglycoproteins)
RN  - 0 (Lectins)
RN  - 0 (Mucins)
RN  - 0 (Plant Extracts)
RN  - 0 (Tn antigen)
RN  - 0 (Transferrin)
RN  - 0 (alpha-Fetoproteins)
RN  - 0 (asialotransferrins)
RN  - 42Z2K6ZL8P (Manganese)
RN  - KM15WK8O5T (Acetylgalactosamine)
RN  - SY7Q814VUP (Calcium)
SB  - IM
MH  - Acetylgalactosamine/metabolism
MH  - Animals
MH  - Antigens, Tumor-Associated, Carbohydrate/*metabolism
MH  - Asialoglycoproteins/metabolism
MH  - Calcium/pharmacology
MH  - Carbohydrate Sequence
MH  - Cattle
MH  - Hemagglutination
MH  - Humans
MH  - Hydrogen-Ion Concentration
MH  - Lectins/genetics/*isolation & purification/*metabolism
MH  - Manganese/pharmacology
MH  - Molecular Sequence Data
MH  - Molecular Weight
MH  - Mucins/metabolism
MH  - Plant Extracts/chemistry
MH  - Salvia/*chemistry
MH  - Seeds/*chemistry
MH  - Submandibular Gland/metabolism
MH  - Temperature
MH  - Transferrin/analogs & derivatives/metabolism
MH  - alpha-Fetoproteins/metabolism
EDAT- 2006/01/18 09:00
MHDA- 2006/05/10 09:00
CRDT- 2006/01/18 09:00
PHST- 2005/08/12 00:00 [received]
PHST- 2005/09/30 00:00 [revised]
PHST- 2005/11/23 00:00 [accepted]
PHST- 2006/01/18 09:00 [pubmed]
PHST- 2006/05/10 09:00 [medline]
PHST- 2006/01/18 09:00 [entrez]
AID - S0031-9422(05)00668-0 [pii]
AID - 10.1016/j.phytochem.2005.11.028 [doi]
PST - ppublish
SO  - Phytochemistry. 2006 Feb;67(4):347-55. doi: 10.1016/j.phytochem.2005.11.028. Epub
      2006 Jan 18.

PMID- 1828263
OWN - NLM
STAT- MEDLINE
DCOM- 19910710
LR  - 20151119
IS  - 0022-1767 (Print)
IS  - 0022-1767 (Linking)
VI  - 146
IP  - 12
DP  - 1991 Jun 15
TI  - Immunoprecipitation of membrane proteins from rat basophilic leukemia cells by
      the antiganglioside monoclonal antibody AA4.
PG  - 4271-7
AB  - In previous studies, mAb AA4 inhibited IgE binding, induced rapid morphologic
      changes, and blocked histamine release in rat basophilic leukemia (RBL-2H3)
      cells. It bound to two novel derivatives of ganglioside GD1b (Ag I and Ag II)
      that appear to be present only in rat mast cells. The present study demonstrates 
      the importance of gangliosides Ag I and Ag II for binding of mAb AA4 to intact
      cells. We also investigated the presence of gangliosides Ag I and Ag II and
      proteins immunoprecipitated with mAb AA4 in the parental and four variant cell
      lines. In comparison with the parental RBL-2H3, two variant cell lines had very
      low (0.5% and 2.0%) and two others had intermediate levels (9% and 18%) of
      125I-AA4 binding. mAb AA4 inhibited 125I-IgE binding to the parental RBL-2H3
      cells and to only one variant with intermediate amounts of gangliosides Ag I and 
      Ag II. Therefore, there are variations in the proximity of these gangliosides to 
      the high affinity IgE receptor (Fc epsilon RI) among different cell lines. mAb
      AA4 immunoprecipitated proteins of 50 to 60, 120, and 135 kDa from 125I-surface
      labeled cells. These were different from the subunits of Fc epsilon RI. The
      amount of gangliosides Ag I and Ag II in cell extracts correlated with the number
      of mAb AA4 binding sites on the cell surface and with the quantity of proteins
      precipitated from the different cell lines. Thus, these membrane proteins appear 
      to be associated with gangliosides Ag I and Ag II. The binding of mAb AA4 to the 
      surface gangliosides could induce intracellular changes through transmembrane
      signaling by these proteins.
FAU - Stephan, V
AU  - Stephan V
AD  - Clinical Immunology Section, National Institute of Dental Research, National
      Institutes of Health, Bethesda, MD 20892.
FAU - Guo, N
AU  - Guo N
FAU - Ginsburg, V
AU  - Ginsburg V
FAU - Siraganian, R P
AU  - Siraganian RP
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - J Immunol
JT  - Journal of immunology (Baltimore, Md. : 1950)
JID - 2985117R
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens, Differentiation, B-Lymphocyte)
RN  - 0 (Gangliosides)
RN  - 0 (Iodine Radioisotopes)
RN  - 0 (Membrane Proteins)
RN  - 0 (Receptors, Fc)
RN  - 0 (Receptors, IgE)
RN  - 37341-29-0 (Immunoglobulin E)
RN  - EC 3.2.1.18 (Neuraminidase)
SB  - AIM
SB  - IM
MH  - Animals
MH  - Antibodies, Monoclonal/*immunology
MH  - Antigens, Differentiation, B-Lymphocyte/immunology
MH  - Gangliosides/analysis/*immunology
MH  - Immunoglobulin E/metabolism
MH  - Iodine Radioisotopes
MH  - Leukemia, Basophilic, Acute/*metabolism
MH  - Membrane Proteins/*analysis/immunology
MH  - Mice
MH  - Neuraminidase/pharmacology
MH  - *Precipitin Tests
MH  - Rats
MH  - Receptors, Fc/immunology
MH  - Receptors, IgE
EDAT- 1991/06/15 00:00
MHDA- 1991/06/15 00:01
CRDT- 1991/06/15 00:00
PHST- 1991/06/15 00:00 [pubmed]
PHST- 1991/06/15 00:01 [medline]
PHST- 1991/06/15 00:00 [entrez]
PST - ppublish
SO  - J Immunol. 1991 Jun 15;146(12):4271-7.

PMID- 3498891
OWN - NLM
STAT- MEDLINE
DCOM- 19871105
LR  - 20151119
IS  - 0027-2507 (Print)
IS  - 0027-2507 (Linking)
VI  - 54
IP  - 5
DP  - 1987 Jun
TI  - A new monoclonal-antibody-defined tumor marker (KMO1) for pancreatic carcinoma.
PG  - 393-400
FAU - Ohyanagi, H
AU  - Ohyanagi H
FAU - Saitoh, Y
AU  - Saitoh Y
FAU - Okumura, S
AU  - Okumura S
FAU - Ishida, T
AU  - Ishida T
FAU - Uesaka, K
AU  - Uesaka K
FAU - Ishida, H
AU  - Ishida H
FAU - Yamamoto, M
AU  - Yamamoto M
FAU - Uemura, Y
AU  - Uemura Y
FAU - Kano, Y
AU  - Kano Y
FAU - Suyama, T
AU  - Suyama T
LA  - eng
PT  - Comparative Study
PT  - Journal Article
PL  - United States
TA  - Mt Sinai J Med
JT  - The Mount Sinai journal of medicine, New York
JID - 0241032
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Biomarkers, Tumor)
SB  - IM
MH  - *Antibodies, Monoclonal
MH  - Biomarkers, Tumor/*analysis/immunology
MH  - Cell Line
MH  - Hemagglutination Tests/methods
MH  - Immunohistochemistry
MH  - Pancreatic Neoplasms/*immunology
EDAT- 1987/06/01 00:00
MHDA- 1987/06/01 00:01
CRDT- 1987/06/01 00:00
PHST- 1987/06/01 00:00 [pubmed]
PHST- 1987/06/01 00:01 [medline]
PHST- 1987/06/01 00:00 [entrez]
PST - ppublish
SO  - Mt Sinai J Med. 1987 Jun;54(5):393-400.

PMID- 7487355
OWN - NLM
STAT- MEDLINE
DCOM- 19951212
LR  - 20131121
IS  - 0004-069X (Print)
IS  - 0004-069X (Linking)
VI  - 42
IP  - 3
DP  - 1994
TI  - Structural and immunochemical studies on O-specific polysaccharide of Proteus
      penneri strain 14.
PG  - 209-15
AB  - The complete structure of the O-antigen of Proteus penneri strain 14, containing 
      D-alanine and L-alanine was established using methylation, solvolysis with
      anhydrous hydrogen fluoride, partial acid hydrolysis, 1H- and 13C-NMR
      spectroscopy. The role of partial structures of the pentasaccharide repeating
      unit in manifesting serological specificity and cross-reactivity of this strain
      with some other bacteria is discussed.
FAU - Sidorczyk, Z
AU  - Sidorczyk Z
AD  - Institute of Microbiology and Immunology, University of Lodz, Poland.
FAU - Swierzko, A
AU  - Swierzko A
FAU - Vinogradov, E V
AU  - Vinogradov EV
FAU - Knirel, Y A
AU  - Knirel YA
FAU - Shashkov, A S
AU  - Shashkov AS
LA  - eng
PT  - Journal Article
PL  - Switzerland
TA  - Arch Immunol Ther Exp (Warsz)
JT  - Archivum immunologiae et therapiae experimentalis
JID - 0114365
RN  - 0 (O Antigens)
RN  - OF5P57N2ZX (Alanine)
SB  - IM
MH  - Alanine/chemistry
MH  - Animals
MH  - Carbohydrate Conformation
MH  - Carbohydrate Sequence
MH  - Cross Reactions
MH  - Magnetic Resonance Spectroscopy
MH  - Molecular Sequence Data
MH  - O Antigens/*chemistry/immunology
MH  - Proteus/*chemistry/immunology
MH  - Rabbits
MH  - Stereoisomerism
EDAT- 1994/01/01 00:00
MHDA- 1994/01/01 00:01
CRDT- 1994/01/01 00:00
PHST- 1994/01/01 00:00 [pubmed]
PHST- 1994/01/01 00:01 [medline]
PHST- 1994/01/01 00:00 [entrez]
PST - ppublish
SO  - Arch Immunol Ther Exp (Warsz). 1994;42(3):209-15.

PMID- 1873810
OWN - NLM
STAT- MEDLINE
DCOM- 19910923
LR  - 20071114
IS  - 0008-5472 (Print)
IS  - 0008-5472 (Linking)
VI  - 51
IP  - 17
DP  - 1991 Sep 1
TI  - Anti-GM2 monoclonal antibodies induce necrosis in GM2-rich cultures of a human
      glioma cell line.
PG  - 4643-8
AB  - The effects of four anti-GM2 monoclonal antibodies (DMAb-1, DMAb-2, DMAb-3, and
      DMAb-5) were studied on spheroid cultures from a human glioma cell line (D-54 MG)
      that is known to express high levels of GM2. The spheroids developed central
      necrosis 48 h after antibody exposures at concentrations greater than 6
      micrograms/ml. No necrosis was found with antibodies that had been absorbed with 
      GM2 prior to exposure or with unrelated cytotoxic antibodies.
      Immunohistochemistry showed that the necrosis started shortly after the
      antibodies were evenly distributed throughout the spheroids. Light and
      transmission electron microscopy revealed that a small portion of the cells,
      mainly in the periphery of the spheroids, was unaffected by antibody exposure.
      New monolayer cultures established from antibody-treated cells expressed a 50%
      lower GM2 content as shown by flow cytometry and determination of ganglioside
      content throughout at least 12 passages. Thus, the GM2-rich D-54 MG cell line has
      subpopulations of cells with lower GM2 content. Spheroids obtained from this
      subpopulation developed only minor necrosis after antibody treatment. These
      results show that GM2 antibodies cause severe necrosis of GM2-containing glioma
      cells in vitro, but the effect depends on the concentration of antigen, and a
      threshold number of GM2 molecules is required.
FAU - Bjerkvig, R
AU  - Bjerkvig R
AD  - Department of Pathology, Gade Institute, University of Bergen, Norway.
FAU - Engebraaten, O
AU  - Engebraaten O
FAU - Laerum, O D
AU  - Laerum OD
FAU - Fredman, P
AU  - Fredman P
FAU - Svennerholm, L
AU  - Svennerholm L
FAU - Vrionis, F D
AU  - Vrionis FD
FAU - Wikstrand, C J
AU  - Wikstrand CJ
FAU - Bigner, D D
AU  - Bigner DD
LA  - eng
GR  - CA 11898/CA/NCI NIH HHS/United States
GR  - CA 32672/CA/NCI NIH HHS/United States
GR  - NS 20023/NS/NINDS NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Cancer Res
JT  - Cancer research
JID - 2984705R
RN  - 0 (Antibodies, Monoclonal)
RN  - 19600-01-2 (G(M2) Ganglioside)
SB  - IM
MH  - Antibodies, Monoclonal/*pharmacology
MH  - Cell Survival
MH  - G(M2) Ganglioside/analysis/*immunology
MH  - Glioma/chemistry/*pathology/ultrastructure
MH  - Humans
MH  - Microscopy, Electron
MH  - Microscopy, Fluorescence
MH  - Necrosis
MH  - Tumor Cells, Cultured/chemistry/pathology
EDAT- 1991/09/01 00:00
MHDA- 1991/09/01 00:01
CRDT- 1991/09/01 00:00
PHST- 1991/09/01 00:00 [pubmed]
PHST- 1991/09/01 00:01 [medline]
PHST- 1991/09/01 00:00 [entrez]
PST - ppublish
SO  - Cancer Res. 1991 Sep 1;51(17):4643-8.

PMID- 13367419
OWN - NLM
STAT- MEDLINE
DCOM- 20020501
LR  - 20181201
IS  - 0022-1767 (Print)
IS  - 0022-1767 (Linking)
VI  - 77
IP  - 3
DP  - 1956 Sep
TI  - A study of the cellular distribution of Forssman antigen in various species.
PG  - 198-212
FAU - LEDUC, E H
AU  - LEDUC EH
FAU - TANAKA, N
AU  - TANAKA N
LA  - eng
PT  - Journal Article
PL  - United States
TA  - J Immunol
JT  - Journal of immunology (Baltimore, Md. : 1950)
JID - 2985117R
RN  - 0 (Antigens)
RN  - 9013-60-9 (Forssman Antigen)
SB  - OM
MH  - *Antigens
MH  - *Forssman Antigen
OID - CLML: 5731:13562
OTO - NLM
OT  - *ANTIGENS
EDAT- 1956/09/01 00:00
MHDA- 1956/09/01 00:01
CRDT- 1956/09/01 00:00
PHST- 1956/09/01 00:00 [pubmed]
PHST- 1956/09/01 00:01 [medline]
PHST- 1956/09/01 00:00 [entrez]
PST - ppublish
SO  - J Immunol. 1956 Sep;77(3):198-212.

PMID- 17693575
OWN - NLM
STAT- MEDLINE
DCOM- 20080324
LR  - 20080228
IS  - 1472-4146 (Electronic)
IS  - 0021-9746 (Linking)
VI  - 61
IP  - 3
DP  - 2008 Mar
TI  - Small bowel gastric metaplasia: a report of three cases in children.
PG  - 382-4
AB  - AIMS: To report three children displaying gastric metaplasia antral pyloric type 
      of the small bowel mucosa. METHODS: Analysis of clinical, histopathological and
      immunohistochemical data. RESULTS: The first patient was a 14-year-old girl with 
      history of chronic intestinal pseudo-obstruction and chronic jejunitis; the
      second patient was a 6-year-old girl with a long-lasting jejunostomy; and the
      third patient was a 5-year-old girl with ileal-rectal anastomosis. The foci of
      gastric metaplasia were obvious with H&E-stained sections. The cells at the
      gastric metaplasia mucosa proved to be MUC-1 and sialyl-Tn positive by
      immunohistochemistry and they were in a pattern that was different from that of
      the adjacent mucosa; the cells were autofluorescent in H&E-stained sections.
      CONCLUSIONS: Gastric metaplasia of the small bowel mucosa in these cases seems to
      have resulted from chronic inflammation and persistent regenerative activity.
      This has rarely been reported outside Crohn disease, and if ever in children.
FAU - Drut, R
AU  - Drut R
AD  - Department of Pathology, Superiora Sor Maria Ludovica Children's Hospital, La
      Plata, Argentina. patologi@netverk.com.ar
FAU - Altamirano, E
AU  - Altamirano E
LA  - eng
PT  - Case Reports
PT  - Journal Article
PT  - Review
DEP - 20070810
PL  - England
TA  - J Clin Pathol
JT  - Journal of clinical pathology
JID - 0376601
SB  - AIM
SB  - IM
MH  - Adolescent
MH  - Anastomosis, Surgical
MH  - Child
MH  - Female
MH  - Humans
MH  - Ileostomy
MH  - Inflammation
MH  - Intestinal Mucosa/immunology/*pathology
MH  - Intestinal Pseudo-Obstruction/immunology/pathology
MH  - *Intestine, Small
MH  - Metaplasia
MH  - Precancerous Conditions/immunology/*pathology
MH  - Pyloric Antrum/immunology/*pathology
MH  - Staining and Labeling
MH  - Time Factors
RF  - 6
EDAT- 2007/08/19 09:00
MHDA- 2008/03/25 09:00
CRDT- 2007/08/19 09:00
PHST- 2007/08/19 09:00 [pubmed]
PHST- 2008/03/25 09:00 [medline]
PHST- 2007/08/19 09:00 [entrez]
AID - jcp.2007.049841 [pii]
AID - 10.1136/jcp.2007.049841 [doi]
PST - ppublish
SO  - J Clin Pathol. 2008 Mar;61(3):382-4. doi: 10.1136/jcp.2007.049841. Epub 2007 Aug 
      10.

PMID- 2167157
OWN - NLM
STAT- MEDLINE
DCOM- 19900927
LR  - 20151119
IS  - 0008-5472 (Print)
IS  - 0008-5472 (Linking)
VI  - 50
IP  - 17
DP  - 1990 Sep 1
TI  - Gangliosides and sialoglycoproteins carrying a rare blood group antigen
      determinant, Cad, associated with human cancers as detected by specific
      monoclonal antibodies.
PG  - 5497-503
AB  - Two murine monoclonal antibodies, 2A3D2 and 2D11E2 (both IgM), which are directed
      to the gangliosides and sialoglycoproteins related to a rare blood group antigen,
      Cad, were obtained by using a ganglioside mixture prepared from human
      hepatocellular carcinoma cells (PLC/PRF/5) as the immunogen. These two monoclonal
      antibodies detected multiple ganglioside antigens present in the PLC/PRF/5 cells,
      and the major antigenic ganglioside was characterized as IV4GalNAc beta-GD1a,
      which has the carbohydrate structure GalNAc beta 1----4(NeuAc alpha 2----3)Gal
      beta 1----3GalNAc beta 1---- 4(NeuAc alpha 2----3)Gal beta 1----Cer. The two
      antibodies also reacted with GM2 (GalNAc beta 1----4[NeuAc alpha 2----3]Gal beta 
      1----4Glc beta 1----Cer) and a Cad-active lactoseries ganglioside (IV4GalNAc
      beta-sialosylparagloboside, GalNAc beta 1----4[NeuAc alpha 2----3]Gal beta
      1----4GlcNAc beta 1---- 3Gal beta 1----4Glc beta 1----Cer), which have
      carbohydrate structures related to IV4GalNAc beta-GD1a. Beside gangliosides, both
      antibodies recognized the carbohydrate determinant carried by glycophorin A on
      very rare Cad-positive human RBC; the structure of which is GalNAc beta
      1----4(NeuAc alpha 2----3)Gal beta 1----3(NeuAc alpha 2---- 6)GalNAc alpha
      1----Ser/Thr. From these findings, it is clear that monoclonal antibodies 2A3D2
      and 2D11E2 both recognize the nonreduced carbohydrate terminus composed of three 
      sugar residues, GalNac beta 1----4(NeuAc alpha 2----3)Gal beta 1----R, and are
      useful for detecting the Cad-related antigen in cells and tissues. By using these
      monoclonal antibodies, it was revealed that many cultured human hepatocellular
      carcinoma cell lines and cancer tissues taken from patients with hepatocellular
      carcinoma contain both Cad-active glycoprotein antigens and related gangliosides,
      while normal liver tissues contain no appreciable amount of either species of
      antigen. The Cad-active glycoprotein antigens in cultured human hepatocellular
      carcinoma cells appeared as triplet bands having molecular weights of 92,000,
      75,000, and 61,000, under either reducing or nonreducing conditions in sodium
      dodecyl sulfate-polyacrylamide gel electrophoresis. Essentially the same triplet 
      proteins were observed in as many as 4 of 9 cases (44%) of cancer tissue from
      patients with hepatocellular carcinoma, but not in neighboring cirrhotic tissues 
      or normal livers tissues. These results suggest that the rare blood group antigen
      Cad is associated with human cancers, especially hepatocellular carcinoma.
FAU - Hiraiwa, N
AU  - Hiraiwa N
AD  - Department of Clinical Science and Laboratory, Kyoto University, Japan.
FAU - Tsuyuoka, K
AU  - Tsuyuoka K
FAU - Li, Y T
AU  - Li YT
FAU - Tanaka, M
AU  - Tanaka M
FAU - Seno, T
AU  - Seno T
FAU - Okubo, Y
AU  - Okubo Y
FAU - Fukuda, Y
AU  - Fukuda Y
FAU - Imura, H
AU  - Imura H
FAU - Kannagi, R
AU  - Kannagi R
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Cancer Res
JT  - Cancer research
JID - 2984705R
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Blood Group Antigens)
RN  - 0 (Gangliosides)
RN  - 0 (Sialoglycoproteins)
SB  - IM
MH  - Animals
MH  - Antibodies, Monoclonal
MH  - Blood Group Antigens/*immunology
MH  - Blotting, Western
MH  - Carbohydrate Conformation
MH  - Carbohydrate Sequence
MH  - Carcinoma, Hepatocellular/*immunology
MH  - Erythrocytes/immunology
MH  - Gangliosides/*analysis
MH  - Humans
MH  - Immunohistochemistry
MH  - Liver/immunology
MH  - Liver Neoplasms/*immunology
MH  - Mice
MH  - Mice, Nude
MH  - Molecular Sequence Data
MH  - Molecular Weight
MH  - Sialoglycoproteins/*analysis
MH  - Transplantation, Heterologous
MH  - Tumor Cells, Cultured/*immunology
EDAT- 1990/09/01 00:00
MHDA- 1990/09/01 00:01
CRDT- 1990/09/01 00:00
PHST- 1990/09/01 00:00 [pubmed]
PHST- 1990/09/01 00:01 [medline]
PHST- 1990/09/01 00:00 [entrez]
PST - ppublish
SO  - Cancer Res. 1990 Sep 1;50(17):5497-503.

PMID- 78708
OWN - NLM
STAT- MEDLINE
DCOM- 19780828
LR  - 20170913
IS  - 0006-291X (Print)
IS  - 0006-291X (Linking)
VI  - 81
IP  - 4
DP  - 1978 Apr 28
TI  - Blood group i and I activities of "lacto-N-norhexaosylceramide" and its
      analogues: the structural requirements for i-specificities.
PG  - 1286-93
FAU - Niemann, H
AU  - Niemann H
FAU - Watanabe, K
AU  - Watanabe K
FAU - Hakomori, S
AU  - Hakomori S
LA  - eng
PT  - Journal Article
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Biochem Biophys Res Commun
JT  - Biochemical and biophysical research communications
JID - 0372516
RN  - 0 (Blood Group Antigens)
RN  - 0 (Epitopes)
RN  - 0 (Glycosphingolipids)
RN  - 0 (I Blood-Group System)
RN  - 0 (Isoantibodies)
SB  - IM
MH  - *Blood Group Antigens
MH  - Epitopes
MH  - Glycosphingolipids/*blood/immunology
MH  - Hemagglutination Inhibition Tests
MH  - Humans
MH  - *I Blood-Group System
MH  - Isoantibodies
MH  - Structure-Activity Relationship
EDAT- 1978/04/28 00:00
MHDA- 1978/04/28 00:01
CRDT- 1978/04/28 00:00
PHST- 1978/04/28 00:00 [pubmed]
PHST- 1978/04/28 00:01 [medline]
PHST- 1978/04/28 00:00 [entrez]
AID - 0006-291X(78)91275-5 [pii]
PST - ppublish
SO  - Biochem Biophys Res Commun. 1978 Apr 28;81(4):1286-93.

PMID- 16391846
OWN - NLM
STAT- MEDLINE
DCOM- 20060601
LR  - 20151119
IS  - 1021-335X (Print)
IS  - 1021-335X (Linking)
VI  - 15
IP  - 2
DP  - 2006 Feb
TI  - Study of the expression of Tn antigen in different types of human breast cancer
      cells using VVA-B4 lectin.
PG  - 305-10
AB  - VVA-B4 lectin was used to investigate the differences in Tn antigen expression in
      tissues of different types of human breast cancer (benign lesions, carcinoma in
      situ, invasive carcinoma) and in normal tissues neighboring lobular carcinoma.
      Locations in which Tn antigen was expressed were identified using the
      avidin-biotin-peroxidase labeling system. Tissues collected during cosmetic
      procedures and classified as normal were completely negative, except for one
      case. Benign proliferative changes including fibroadenoma, apocrine and
      cylindrical metaplasia showed a very weak positive reaction, although strongly
      positive cells were also observed. The reaction in non-invasive cases of atypical
      hyperplasia was diversified depending on site. Intralobular hyperplasia was
      characterized by a particularly high percentage of labeled cells. A majority (up 
      to 80%) of ductal and lobular carcinoma in situ showed very strong or moderate
      staining. In invasive cancers, there were conspicuous differences between stage
      of cancer development and tendency towards a decrease in intensely labeled cell
      count in the most advanced stages. In normal tissues in the direct neighborhood
      of carcinoma in situ, the cytoplasm of 40% of cells was strongly labeled.
      However, the findings for normal tissues in the close vicinity of invasive cancer
      were the most surprising, since there was either no or only very weak positive
      reaction. It can be concluded that glycosylation modifications during
      carcinogenesis, as demonstrated by the presence of Tn epitope, develop very
      early, before any destructive changes in proliferation/apoptosis or cell
      differentiation become discernible.
FAU - Konska, G
AU  - Konska G
AD  - Department of Pharmaceutical Botany, Collegium Medicum, Jagiellonian University, 
      ul. Medyczna 9, 30-688 Cracow, Poland.
FAU - Guerry, M
AU  - Guerry M
FAU - Caldefie-Chezet, F
AU  - Caldefie-Chezet F
FAU - De Latour, M
AU  - De Latour M
FAU - Guillot, J
AU  - Guillot J
LA  - eng
PT  - Comparative Study
PT  - Journal Article
PL  - Greece
TA  - Oncol Rep
JT  - Oncology reports
JID - 9422756
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Biomarkers, Tumor)
RN  - 0 (Lectins)
RN  - 0 (Tn antigen)
SB  - IM
MH  - Antigens, Tumor-Associated, Carbohydrate/*biosynthesis
MH  - Biomarkers, Tumor/*analysis
MH  - Breast Neoplasms/*metabolism/pathology
MH  - Carcinoma in Situ/metabolism/pathology
MH  - Carcinoma, Ductal, Breast/metabolism/pathology
MH  - Carcinoma, Intraductal, Noninfiltrating/metabolism/pathology
MH  - Cell Transformation, Neoplastic/*metabolism
MH  - Female
MH  - Fibroadenoma/metabolism/pathology
MH  - Humans
MH  - Hyperplasia/metabolism/pathology
MH  - Immunohistochemistry
MH  - *Lectins
MH  - Precancerous Conditions/metabolism/pathology
EDAT- 2006/01/05 09:00
MHDA- 2006/06/02 09:00
CRDT- 2006/01/05 09:00
PHST- 2006/01/05 09:00 [pubmed]
PHST- 2006/06/02 09:00 [medline]
PHST- 2006/01/05 09:00 [entrez]
PST - ppublish
SO  - Oncol Rep. 2006 Feb;15(2):305-10.

PMID- 10570420
OWN - NLM
STAT- MEDLINE
DCOM- 20000104
LR  - 20081121
IS  - 0008-543X (Print)
IS  - 0008-543X (Linking)
VI  - 86
IP  - 10
DP  - 1999 Nov 15
TI  - Mucin core protein expression in extrahepatic bile duct carcinoma is associated
      with metastases to the liver and poor prognosis.
PG  - 1966-75
AB  - BACKGROUND: Curative resection does not guarantee long term survival for the
      patient with extrahepatic bile duct carcinoma because of the possibility of
      metastases to the liver (LM). Expression of mucin core protein-1 (MUC1),
      sialyl-Le(x), and sialosyl-Tn in bile duct carcinoma was determined and compared 
      with LM and prognosis. METHODS: Immunohistochemical expression of MUC1,
      sialyl-Le(x), and sialosyl-Tn in 73 extrahepatic bile duct tumors was analyzed
      using the DF3, FH6, and TKH2 monoclonal antibodies, respectively. Scoring was
      based on the percentage of immunoreactive cells: negative, low expression (</=25%
      immunoreactive cells), and high expression (>25%). RESULTS: High expression of
      MUC1, sialyl-Le(x), and sialosyl-Tn was observed in 68.5%, 34.2%, and 54.8%,
      respectively. of 73 cases. Patients with tumors showing high expression of MUC1
      had a higher rate of LM (48.9%) and a significantly shorter survival period
      (median survival time, 17.8 months) compared with patients with tumors showing
      low (incidence of LM, 9.1%; median survival time, >100 months) or negative
      (incidence of LM, 11.1%; median survival time, 52.9 months) expression of MUC1 (P
      < 0.01). However, the survival period of patients with tumors showing high, low, 
      or negative expression of sialyl-Le(x) or of sialosyl-Tn did not differ
      significantly. High MUC1 expression correlated with LM by logistic regression
      analysis and emerged as an independent prognostic factor in stepwise multivariate
      analysis. CONCLUSIONS: The results of the current study demonstrate that high
      expression of MUC1 correlates with LM and poor outcome in patients with
      extrahepatic bile duct carcinoma.
CI  - Copyright 1999 American Cancer Society.
FAU - Takao, S
AU  - Takao S
AD  - First Department of Surgery, Kagoshima University School of Medicine, Kagoshima, 
      Japan.
FAU - Uchikura, K
AU  - Uchikura K
FAU - Yonezawa, S
AU  - Yonezawa S
FAU - Shinchi, H
AU  - Shinchi H
FAU - Aikou, T
AU  - Aikou T
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Cancer
JT  - Cancer
JID - 0374236
RN  - 0
      (5-acetylneuraminyl-(2-3)-galactosyl-(1-4)-(fucopyranosyl-(1-3))-N-acetylglucosam
      ine)
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Glycoproteins)
RN  - 0 (MUC1 tandem repeat peptide)
RN  - 0 (Mucin-1)
RN  - 0 (Neoplasm Proteins)
RN  - 0 (Oligosaccharides)
RN  - 0 (Peptide Fragments)
RN  - 0 (sialosyl-Tn antigen)
SB  - AIM
SB  - IM
MH  - Adult
MH  - Aged
MH  - Aged, 80 and over
MH  - Antigens, Tumor-Associated, Carbohydrate/biosynthesis
MH  - Bile Duct Neoplasms/*metabolism
MH  - Glycoproteins/biosynthesis
MH  - Humans
MH  - Liver Neoplasms/*secondary
MH  - Logistic Models
MH  - Middle Aged
MH  - Mucin-1/*biosynthesis
MH  - Neoplasm Proteins/*biosynthesis
MH  - Oligosaccharides/biosynthesis
MH  - Peptide Fragments/*biosynthesis
MH  - Prognosis
MH  - Retrospective Studies
EDAT- 1999/11/26 00:00
MHDA- 1999/11/26 00:01
CRDT- 1999/11/26 00:00
PHST- 1999/11/26 00:00 [pubmed]
PHST- 1999/11/26 00:01 [medline]
PHST- 1999/11/26 00:00 [entrez]
AID - 10.1002/(SICI)1097-0142(19991115)86:10<1966::AID-CNCR13>3.0.CO;2-M [pii]
PST - ppublish
SO  - Cancer. 1999 Nov 15;86(10):1966-75.

PMID- 19473117
OWN - NLM
STAT- MEDLINE
DCOM- 20091105
LR  - 20131121
IS  - 1470-8728 (Electronic)
IS  - 0264-6021 (Linking)
VI  - 421
IP  - 2
DP  - 2009 Jun 26
TI  - FAM20B is a kinase that phosphorylates xylose in the glycosaminoglycan-protein
      linkage region.
PG  - 157-62
LID - 10.1042/BJ20090474 [doi]
AB  - 2-O-phosphorylation of xylose has been detected in the glycosaminoglycan-protein 
      linkage region, GlcAbeta1-3Galbeta1-3Galbeta1-4Xylbeta1-O-Ser, of proteoglycans. 
      Recent mutant analyses in zebrafish suggest that xylosyltransferase I and FAM20B,
      a protein of unknown function that shows weak similarity to a Golgi kinase
      encoded by four-jointed, operate in a linear pathway for proteoglycan production.
      In the present study, we identified FAM20B as a kinase that phosphorylates the
      xylose residue in the linkage region. Overexpression of FAM20B increased the
      amount of both chondroitin sulfate and heparan sulfate in HeLa cells, whereas the
      RNA interference of FAM20B resulted in a reduction of their amount in the cells. 
      Gel-filtration analysis of the glycosaminoglycan chains synthesized in the
      overexpressing cells revealed that the glycosaminoglycan chains had a similar
      length to those in mock-transfected cells. These results suggest that FAM20B
      regulates the number of glycosaminoglycan chains by phosphorylating the xylose
      residue in the glycosaminoglycan-protein linkage region of proteoglycans.
FAU - Koike, Toshiyasu
AU  - Koike T
AD  - Department of Biochemistry, Kobe Pharmaceutical University, Higashinada-ku, Kobe 
      658-8558, Japan.
FAU - Izumikawa, Tomomi
AU  - Izumikawa T
FAU - Tamura, Jun-Ichi
AU  - Tamura J
FAU - Kitagawa, Hiroshi
AU  - Kitagawa H
LA  - eng
SI  - GENBANK/AB480690
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20090626
PL  - England
TA  - Biochem J
JT  - The Biochemical journal
JID - 2984726R
RN  - 0 (DNA, Complementary)
RN  - 0 (Glycosaminoglycans)
RN  - A1TA934AKO (Xylose)
RN  - EC 2.7.- (Phosphotransferases)
SB  - IM
MH  - Animals
MH  - COS Cells
MH  - Cercopithecus aethiops
MH  - Chromatography, Gel
MH  - DNA, Complementary/metabolism
MH  - Glycosaminoglycans/*metabolism
MH  - HeLa Cells
MH  - Humans
MH  - Molecular Sequence Data
MH  - Phosphorylation
MH  - Phosphotransferases/genetics/*metabolism
MH  - RNA Interference
MH  - Transfection
MH  - Xylose/*metabolism
EDAT- 2009/05/29 09:00
MHDA- 2009/11/06 06:00
CRDT- 2009/05/29 09:00
PHST- 2009/05/29 09:00 [entrez]
PHST- 2009/05/29 09:00 [pubmed]
PHST- 2009/11/06 06:00 [medline]
AID - BJ20090474 [pii]
AID - 10.1042/BJ20090474 [doi]
PST - epublish
SO  - Biochem J. 2009 Jun 26;421(2):157-62. doi: 10.1042/BJ20090474.

PMID- 9261148
OWN - NLM
STAT- MEDLINE
DCOM- 19970915
LR  - 20190508
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 272
IP  - 34
DP  - 1997 Aug 22
TI  - Lewis X biosynthesis in Helicobacter pylori. Molecular cloning of an
      alpha(1,3)-fucosyltransferase gene.
PG  - 21349-56
AB  - The lipopolysaccharide of certain strains of Helicobacter pylori was recently
      shown to contain the Lewis X (Lex) trisaccharide (Galbeta-1,
      4-(Fucalpha(1,3))-GlcNAc). Lex is an oncofetal antigen which appears on human
      gastric epithelium, and its mimicry by carbohydrate structures on the surface of 
      H. pylori may play an important part in the interaction of this pathogen with its
      host. Potential roles for bacterial Lex in mucosal adhesion, immune evasion, and 
      autoantibody induction have been proposed (Moran, A. P., Prendergast, M. M., and 
      Appelmelk, B. J. (1996) FEMS Immunol. Med. Microbiol. 16, 105-115). In mammals,
      the final step of Lex biosynthesis is the alpha(1,3)-fucosylation of GlcNAc in a 
      terminal Galbeta(1-->4)GlcNAc unit, and a corresponding
      GDP-fucose:N-acetylglucosaminyl alpha(1,3) fucosyltransferase (alpha(1,3)-Fuc-T) 
      activity was recently discovered in H. pylori extracts. We used part of a human
      alpha(1, 3)-Fuc-T amino acid sequence to search an H. pylori genomic data base
      for related sequences. Using a probe based upon weakly matching data base
      sequences, we retrieved clones from a plasmid library of H. pylori DNA. DNA
      sequence analysis of the library clones revealed a gene which we have named fucT,
      encoding a protein with localized homology to the human alpha(1,3)-Fuc-Ts. We
      have demonstrated that fucT encodes an active Fuc-T enzyme by expressing the gene
      in Escherichia coli. The recombinant enzyme shows a strong preference for type 2 
      (e.g. LacNAc) over type 1 (e.g. lacto-N-biose) acceptors in vitro. Certain
      residues in a short segment of the H. pylori protein are completely conserved
      throughout the alpha(1,3)-Fuc-T family, defining an alpha(1,3)-Fuc-T motif which 
      may be of use in identifying new fucosyltransferase genes.
FAU - Martin, S L
AU  - Martin SL
AD  - Glycobiology Unit, GlaxoWellcome Medicines Research Centre, Stevenage, Herts SG1 
      2NY, United Kingdom. slm17885@ggr.co.uk
FAU - Edbrooke, M R
AU  - Edbrooke MR
FAU - Hodgman, T C
AU  - Hodgman TC
FAU - van den Eijnden, D H
AU  - van den Eijnden DH
FAU - Bird, M I
AU  - Bird MI
LA  - eng
SI  - GENBANK/AF006039
PT  - Journal Article
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (DNA, Bacterial)
RN  - 0 (Lewis X Antigen)
RN  - EC 2.4.1.- (Fucosyltransferases)
RN  - EC 2.4.1.152 (galactoside 3-fucosyltransferase)
SB  - IM
MH  - Amino Acid Sequence
MH  - Base Sequence
MH  - Cloning, Molecular
MH  - Consensus Sequence
MH  - DNA, Bacterial/genetics
MH  - Fucosyltransferases/*genetics/metabolism
MH  - *Genes, Bacterial
MH  - Helicobacter pylori/*enzymology/*genetics
MH  - Lewis X Antigen/*biosynthesis
MH  - Molecular Sequence Data
MH  - Sequence Alignment
MH  - Sequence Homology, Amino Acid
MH  - Substrate Specificity
EDAT- 1997/08/22 00:00
MHDA- 1997/08/22 00:01
CRDT- 1997/08/22 00:00
PHST- 1997/08/22 00:00 [pubmed]
PHST- 1997/08/22 00:01 [medline]
PHST- 1997/08/22 00:00 [entrez]
AID - 10.1074/jbc.272.34.21349 [doi]
PST - ppublish
SO  - J Biol Chem. 1997 Aug 22;272(34):21349-56. doi: 10.1074/jbc.272.34.21349.

PMID- 1692349
OWN - NLM
STAT- MEDLINE
DCOM- 19900614
LR  - 20181113
IS  - 0022-538X (Print)
IS  - 0022-538X (Linking)
VI  - 64
IP  - 6
DP  - 1990 Jun
TI  - Inhibition of human immunodeficiency virus (HIV) infection in vitro by
      anticarbohydrate monoclonal antibodies: peripheral glycosylation of HIV envelope 
      glycoprotein gp120 may be a target for virus neutralization.
PG  - 2833-40
AB  - Carbohydrate structures are often involved in the initial adhesion of pathogens
      to target cells. In the present study, a panel of anticarbohydrate monoclonal
      antibodies (MAbs) was tested for their ability to inhibit in vitro human
      immunodeficiency virus infectivity. MAbs against three different N- and O-linked 
      carbohydrate epitopes (LeY, A1, and sialyl-Tn) were able to block infection by
      cell-free virus as well as inhibit syncytium formation. Inhibition of virus
      infectivity was independent of virus strain (HTLVIIIB or patient isolate
      SSI-002), the cell line used for virus propagation (H9 or MT4), and the cell type
      used as the infection target (MT4, PMC, or selected T4 lymphocytes). Inhibition
      was observed when viruses were preincubated with MAbs but not when cells were
      preincubated with MAbs before inoculation, and the MAbs were shown to precipitate
      125I-labeled gp120. The MAbs therefore define carbohydrate structures expressed
      by the viral envelope glycoprotein gp120, indicating that glycans of the viral
      envelope are possible targets for immunotherapy or vaccine development or both.
FAU - Hansen, J E
AU  - Hansen JE
AD  - Department of Infectious Diseases, Hvidovre Hospital, Denmark.
FAU - Clausen, H
AU  - Clausen H
FAU - Nielsen, C
AU  - Nielsen C
FAU - Teglbjaerg, L S
AU  - Teglbjaerg LS
FAU - Hansen, L L
AU  - Hansen LL
FAU - Nielsen, C M
AU  - Nielsen CM
FAU - Dabelsteen, E
AU  - Dabelsteen E
FAU - Mathiesen, L
AU  - Mathiesen L
FAU - Hakomori, S I
AU  - Hakomori SI
FAU - Nielsen, J O
AU  - Nielsen JO
LA  - eng
GR  - CA42505/CA/NCI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - J Virol
JT  - Journal of virology
JID - 0113724
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Epitopes)
RN  - 0 (HIV Envelope Protein gp120)
SB  - IM
SB  - X
MH  - *Antibodies, Monoclonal
MH  - Carbohydrate Conformation
MH  - Carbohydrate Sequence
MH  - Cell Line
MH  - Enzyme-Linked Immunosorbent Assay
MH  - Epitopes/immunology
MH  - Fluorescent Antibody Technique
MH  - Giant Cells/immunology
MH  - HIV/immunology/*physiology
MH  - HIV Envelope Protein gp120/*immunology
MH  - HIV-1/immunology/physiology
MH  - Humans
MH  - Molecular Sequence Data
MH  - T-Lymphocytes/immunology
MH  - *Virus Replication
PMC - PMC249465
EDAT- 1990/06/01 00:00
MHDA- 1990/06/01 00:01
CRDT- 1990/06/01 00:00
PHST- 1990/06/01 00:00 [pubmed]
PHST- 1990/06/01 00:01 [medline]
PHST- 1990/06/01 00:00 [entrez]
PST - ppublish
SO  - J Virol. 1990 Jun;64(6):2833-40.

PMID- 3510728
OWN - NLM
STAT- MEDLINE
DCOM- 19860321
LR  - 20151119
IS  - 0008-5472 (Print)
IS  - 0008-5472 (Linking)
VI  - 46
IP  - 3
DP  - 1986 Mar
TI  - Expression of Lewisa, Lewisb, X, and Y blood group antigens in human colonic
      tumors and normal tissue and in human tumor-derived cell lines.
PG  - 1553-61
AB  - Serological and immunopathological analysis of the expression of Lea, Leb, X, and
      Y blood group antigens on cell lines and tissues was performed using a panel of
      mouse monoclonal antibodies. The distribution of the antigens was determined on
      155 malignant tumor cell lines of various types and 10 short term cultures of
      normal fibroblasts and kidney cells. Among colon cancers, all four blood group
      antigens were expressed on the majority of cell lines. On lung, breast, bladder, 
      and ovarian cancer cell lines, X and Y antigens were the main specificities
      found, whereas few of the renal and hematopoietic tumor cell lines demonstrated
      any of the four blood group antigens. No blood group antigens could be detected
      on astrocytoma or melanoma cell lines. The expression of the antigens was also
      analyzed on frozen sections of colon carcinoma and adjacent normal colon tissue
      from 42 patients using the immunoperoxidase method. Lea and X were detected
      throughout the normal colon and on most colonic tumors. In poorly differentiated 
      colon cancer and in metastatic cancer, decrease of Lea antigen was observed. Leb 
      and Y expression was observed in only 20-45% of normal tissue samples but in
      almost all colonic carcinoma tissues. A selected number of tumor and normal
      specimens from patients whose secretor status was known were examined in more
      detail. Both the staining of the tissues and the reactivity of blood group
      glycolipids from the same specimens were determined. These studies confirmed the 
      above findings and demonstrated the unexpected ability of tumors of nonsecretors 
      to express Leb and/or Y antigens. In such individuals, in whom the expression of 
      Leb and Y antigens in normal tissues is absent or minimal, these antigens provide
      possible targets for immunodiagnosis and therapy.
FAU - Sakamoto, J
AU  - Sakamoto J
FAU - Furukawa, K
AU  - Furukawa K
FAU - Cordon-Cardo, C
AU  - Cordon-Cardo C
FAU - Yin, B W
AU  - Yin BW
FAU - Rettig, W J
AU  - Rettig WJ
FAU - Oettgen, H F
AU  - Oettgen HF
FAU - Old, L J
AU  - Old LJ
FAU - Lloyd, K O
AU  - Lloyd KO
LA  - eng
GR  - CA-08478/CA/NCI NIH HHS/United States
GR  - CA-34039/CA/NCI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Cancer Res
JT  - Cancer research
JID - 2984705R
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens, Neoplasm)
RN  - 0 (Blood Group Antigens)
RN  - 0 (Glycolipids)
RN  - 0 (Lewis Blood-Group System)
SB  - IM
MH  - Antibodies, Monoclonal
MH  - Antigens, Neoplasm/*analysis
MH  - Blood Group Antigens/*immunology
MH  - Cell Line
MH  - Colon/*immunology
MH  - Colonic Neoplasms/*immunology
MH  - Fluorescent Antibody Technique
MH  - Glycolipids/immunology
MH  - Humans
MH  - Immunoenzyme Techniques
MH  - Intestinal Mucosa/immunology
MH  - Lewis Blood-Group System/*immunology
EDAT- 1986/03/01 00:00
MHDA- 1986/03/01 00:01
CRDT- 1986/03/01 00:00
PHST- 1986/03/01 00:00 [pubmed]
PHST- 1986/03/01 00:01 [medline]
PHST- 1986/03/01 00:00 [entrez]
PST - ppublish
SO  - Cancer Res. 1986 Mar;46(3):1553-61.

PMID- 1346716
OWN - NLM
STAT- MEDLINE
DCOM- 19920318
LR  - 20171116
IS  - 0029-7844 (Print)
IS  - 0029-7844 (Linking)
VI  - 79
IP  - 3
DP  - 1992 Mar
TI  - Sialyl-Tn, sialyl-Lewis Xi, CA 19-9, CA 125, carcinoembryonic antigen, and tissue
      polypeptide antigen in differentiating ovarian cancer from benign tumors.
PG  - 434-40
AB  - Serum sialyl-Tn, sialyl-Lewis Xi, CA 19-9, CA 125, carcinoembryonic antigen
      (CEA), and tissue polypeptide antigen were measured in 65 women with early-stage 
      ovarian cancer (45 stage I and 20 stage II cases) and 317 with benign pelvic
      masses. As a single assay, sialyl-Tn showed the best sensitivity and specificity,
      46 and 92%, respectively. CA 19-9 detected the greatest number of cancer patients
      but had the lowest specificity. The combination of sialyl-Tn, CA 125, tissue
      polypeptide antigen, and CEA seemed to perform the best, with a sensitivity and
      specificity of 71 and 76%, respectively. The combination of sialyl-Tn, CA 125,
      and tissue polypeptide antigen gave similar results and may be more
      cost-effective. However, one-fifth of the patients with early-stage cancer still 
      showed up as false negatives even with use of the six markers in combination.
      Approaches other than serum assay alone will be needed to detect all malignant
      pelvic masses at an early stage.
FAU - Inoue, M
AU  - Inoue M
AD  - Department of Obstetrics and Gynecology, Osaka University Medical School, Japan.
FAU - Fujita, M
AU  - Fujita M
FAU - Nakazawa, A
AU  - Nakazawa A
FAU - Ogawa, H
AU  - Ogawa H
FAU - Tanizawa, O
AU  - Tanizawa O
LA  - eng
PT  - Journal Article
PL  - United States
TA  - Obstet Gynecol
JT  - Obstetrics and gynecology
JID - 0401101
RN  - 0 (Antigens, Neoplasm)
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Biomarkers, Tumor)
RN  - 0 (Carcinoembryonic Antigen)
RN  - 0 (Lewis X Antigen)
RN  - 0 (Peptides)
RN  - 0 (Tissue Polypeptide Antigen)
RN  - 0 (sialosyl-Tn antigen)
SB  - AIM
SB  - IM
MH  - Antigens, Neoplasm/*analysis
MH  - Antigens, Tumor-Associated, Carbohydrate/analysis
MH  - Biomarkers, Tumor/*analysis
MH  - Carcinoembryonic Antigen/analysis
MH  - Diagnosis, Differential
MH  - Female
MH  - Humans
MH  - Lewis X Antigen/analysis
MH  - Ovarian Neoplasms/*diagnosis/pathology
MH  - Peptides/analysis
MH  - Sensitivity and Specificity
MH  - Tissue Polypeptide Antigen
EDAT- 1992/03/01 00:00
MHDA- 1992/03/01 00:01
CRDT- 1992/03/01 00:00
PHST- 1992/03/01 00:00 [pubmed]
PHST- 1992/03/01 00:01 [medline]
PHST- 1992/03/01 00:00 [entrez]
PST - ppublish
SO  - Obstet Gynecol. 1992 Mar;79(3):434-40.

PMID- 7949653
OWN - NLM
STAT- MEDLINE
DCOM- 19941212
LR  - 20190512
IS  - 0959-6658 (Print)
IS  - 0959-6658 (Linking)
VI  - 4
IP  - 3
DP  - 1994 Jun
TI  - Two different glycosyltransferase defects that result in GalNAc alpha-O-peptide
      (Tn) expression.
PG  - 267-79
AB  - This study shows for the first time that different glycosyltransferase defects in
      the biosynthesis of O-linked oligosaccharides give rise to the same GalNAc
      alpha-O-Ser/Thr determinant on Tn erythrocytes and colorectal carcinoma cells.
      The O-linked oligosaccharides isolated from the glycophorins of Tn erythrocytes
      contained predominantly alpha-N-acetylgalactosamine-O-Ser/Thr (Tn antigen) and
      sialyl-Tn. A marked reduction in normal sialylated oligosaccharides was also
      observed. Monoclonal antibody BRIC 111 raised against Tn erythrocytes reacted
      with both Tn erythrocytes and colorectal carcinoma tissues. Weak staining was
      detected in the supranuclear area and at the surface membranes in normal
      colorectal cells, but was absent from goblet cell vesicles. An increase in
      supranuclear staining over controls was found in tumour tissue and in the
      majority of resection margin specimens. The highest levels of staining were
      present in transitional mucosa, adjacent to the tumours where goblet vesicles
      were also positive. Glycosylation defects in the same patients were further
      studied by determination of the activity of glycosyltransferases in mucosal
      tissue from control and cancer patients. The reduction in or loss of beta 1-3
      N-acetylglucosaminyl transferase activity to GalNAc-peptide in asialo-ovine
      submaxillary gland glycoprotein was detected by direct assay and by isolation of 
      the oligosaccharides from the incubation products. No differences in
      N-acetylglucosaminyl-, galactosyl- or sialyl-transfer to Gal beta 1-3GalNAc in
      antifreeze glycoprotein or in sialyl transferase to asialo-ovine submaxillary
      gland glycoprotein were detected. Our study shows that the GalNAc alpha-O-Ser/Thr
      determinant on Tn erythrocytes and in colorectal carcinoma results from different
      glycosyltransferase defects in separate biosynthetic pathways for haematopoietic 
      and epithelial tissues.
FAU - King, M J
AU  - King MJ
AD  - International Blood Group Reference Laboratory, Bristol, UK.
FAU - Chan, A
AU  - Chan A
FAU - Roe, R
AU  - Roe R
FAU - Warren, B F
AU  - Warren BF
FAU - Dell, A
AU  - Dell A
FAU - Morris, H R
AU  - Morris HR
FAU - Bartolo, D C
AU  - Bartolo DC
FAU - Durdey, P
AU  - Durdey P
FAU - Corfield, A P
AU  - Corfield AP
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - Glycobiology
JT  - Glycobiology
JID - 9104124
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Glycoproteins)
RN  - 0 (Oligosaccharides)
RN  - 0 (Tn antigen)
RN  - EC 2.4.- (Glycosyltransferases)
SB  - IM
MH  - Antigens, Tumor-Associated, Carbohydrate/*analysis/blood
MH  - Blotting, Western
MH  - Carbohydrate Conformation
MH  - Carbohydrate Sequence
MH  - Colorectal Neoplasms/*immunology
MH  - Erythrocyte Membrane/immunology
MH  - Erythrocytes/*immunology
MH  - Glycoproteins/analysis
MH  - Glycosyltransferases/*deficiency
MH  - Humans
MH  - Immunohistochemistry
MH  - Molecular Sequence Data
MH  - Oligosaccharides/biosynthesis/chemistry
MH  - Spectrometry, Mass, Fast Atom Bombardment
MH  - Tumor Cells, Cultured
EDAT- 1994/06/01 00:00
MHDA- 1994/06/01 00:01
CRDT- 1994/06/01 00:00
PHST- 1994/06/01 00:00 [pubmed]
PHST- 1994/06/01 00:01 [medline]
PHST- 1994/06/01 00:00 [entrez]
AID - 10.1093/glycob/4.3.267 [doi]
PST - ppublish
SO  - Glycobiology. 1994 Jun;4(3):267-79. doi: 10.1093/glycob/4.3.267.

PMID- 7485559
OWN - NLM
STAT- MEDLINE
DCOM- 19951212
LR  - 20171213
IS  - 0002-9513 (Print)
IS  - 0002-9513 (Linking)
VI  - 269
IP  - 4 Pt 2
DP  - 1995 Oct
TI  - Recognition of consensus CHO structure in ligands for selectins by novel antibody
      against sialyl Lewis X.
PG  - H1282-7
AB  - The selectins (L, E, and P) play an important role in the earliest events of the 
      inflammatory response, leading to the "rolling" phenomenon. All selectins react
      with sialyl Lewis X (SLex) in vitro, possibly suggesting that their ligands have 
      a consensus structure. 2H5 is a monoclonal antibody against SLex that blocks
      L-selectin-mediated adhesion. 2H5 inhibited adhesion of HL-60 cells to P- and
      E-selectin-producing COS cells in vitro and immunoprecipitated a P-selectin
      glycoprotein ligand-1-like glycoprotein from HL-60 cell lysate, suggesting that
      it recognizes a functional consensus structure on the ligands for all selectins. 
      2H5 reacted not only with human but also with rat and mouse neutrophils. 2H5 is
      the first antibody against SLex that recognizes neutrophils of nonhuman mammals. 
      The carbohydrate structure recognized by 2H5 was present not only on high
      endothelial venules of rat lymphoid organs but also on the endothelial cells of
      nonlymphoid organs. Furthermore, administration of the antibody markedly
      inhibited L- and P-selectin-mediated neutrophil rolling and adhesion in rat
      mesenteric venules in vivo. These results provide evidence for the presence of a 
      consensus carbohydrate structure on the ligands for all selectins. The consensus 
      structure thus has the potential to serve as a therapeutic target.
FAU - Tamatani, T
AU  - Tamatani T
AD  - Pharmaceutical Basic Research Laboratories, Japan Tobacco, Yokohama, Japan.
FAU - Suematsu, M
AU  - Suematsu M
FAU - Tezuka, K
AU  - Tezuka K
FAU - Hanzawa, N
AU  - Hanzawa N
FAU - Tsuji, T
AU  - Tsuji T
FAU - Ishimura, Y
AU  - Ishimura Y
FAU - Kannagi, R
AU  - Kannagi R
FAU - Toyoshima, S
AU  - Toyoshima S
FAU - Homma, M
AU  - Homma M
LA  - eng
PT  - Journal Article
PL  - United States
TA  - Am J Physiol
JT  - The American journal of physiology
JID - 0370511
RN  - 0
      (5-acetylneuraminyl-(2-3)-galactosyl-(1-4)-(fucopyranosyl-(1-3))-N-acetylglucosam
      ine)
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Glycoproteins)
RN  - 0 (Lewis X Antigen)
RN  - 0 (Ligands)
RN  - 0 (Oligosaccharides)
RN  - 0 (Selectins)
RN  - 820484N8I3 (Histamine)
SB  - IM
MH  - Animals
MH  - *Antibodies, Monoclonal/immunology/pharmacology
MH  - *Carbohydrate Sequence
MH  - Cell Adhesion/drug effects
MH  - *Consensus Sequence
MH  - Endothelium, Vascular/cytology/metabolism
MH  - Glycoproteins/metabolism
MH  - HL-60 Cells
MH  - Histamine/pharmacology
MH  - Humans
MH  - Lewis X Antigen/immunology
MH  - Ligands
MH  - Male
MH  - Mice
MH  - Neutrophils/metabolism
MH  - Oligosaccharides/*immunology
MH  - Precipitin Tests
MH  - Rats
MH  - Rats, Inbred WKY
MH  - Selectins/*metabolism
EDAT- 1995/10/01 00:00
MHDA- 1995/10/01 00:01
CRDT- 1995/10/01 00:00
PHST- 1995/10/01 00:00 [pubmed]
PHST- 1995/10/01 00:01 [medline]
PHST- 1995/10/01 00:00 [entrez]
AID - 10.1152/ajpheart.1995.269.4.H1282 [doi]
PST - ppublish
SO  - Am J Physiol. 1995 Oct;269(4 Pt 2):H1282-7. doi:
      10.1152/ajpheart.1995.269.4.H1282.

PMID- 15701648
OWN - NLM
STAT- MEDLINE
DCOM- 20050623
LR  - 20181113
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 280
IP  - 16
DP  - 2005 Apr 22
TI  - Potent glycan inhibitors of myelin-associated glycoprotein enhance axon outgrowth
      in vitro.
PG  - 16305-10
AB  - Myelin-associated glycoprotein (MAG, Siglec-4) is one of several endogenous axon 
      regeneration inhibitors that limit recovery from central nervous system injury
      and disease. Molecules that block such inhibitors may enhance axon regeneration
      and functional recovery. MAG, a member of the Siglec family of sialic
      acid-binding lectins, binds to sialoglycoconjugates on axons and particularly to 
      gangliosides GD1a and GT1b, which may mediate some of the inhibitory effects of
      MAG. In a prior study, we identified potent monovalent sialoside inhibitors of
      MAG using a novel screening platform. In the current study, the most potent of
      these were tested for their ability to reverse MAG-mediated inhibition of axon
      outgrowth from rat cerebellar granule neurons in vitro. Monovalent sialoglycans
      enhanced axon regeneration in proportion to their MAG binding affinities. The
      most potent glycoside was disialyl T antigen
      (NeuAcalpha2-3Galbeta1-3[NeuAcalpha2-6]GalNAc-R), followed by 3-sialyl T antigen 
      (NeuAcalpha2-3Galbeta1-3GalNAc-R), structures expressed on O-linked glycoproteins
      as well as on gangliosides. Prior studies indicated that blocking gangliosides
      reversed MAG inhibition. In the current study, blocking O-linked glycoprotein
      sialylation with benzyl-alpha-GalNAc had no effect. The ability to reverse MAG
      inhibition with monovalent glycosides encourages further exploration of glycans
      and glycan mimetics as blockers of MAG-mediated axon outgrowth inhibition.
FAU - Vyas, Alka A
AU  - Vyas AA
AD  - Department of Pharmacology, The Johns Hopkins School of Medicine, Baltimore,
      Maryland 21205, USA.
FAU - Blixt, Ola
AU  - Blixt O
FAU - Paulson, James C
AU  - Paulson JC
FAU - Schnaar, Ronald L
AU  - Schnaar RL
LA  - eng
GR  - R01 NS037096/NS/NINDS NIH HHS/United States
GR  - GM60938/GM/NIGMS NIH HHS/United States
GR  - NS37096/NS/NINDS NIH HHS/United States
PT  - Journal Article
PT  - Research Support, N.I.H., Extramural
PT  - Research Support, U.S. Gov't, P.H.S.
DEP - 20050208
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Ligands)
RN  - 0 (Myelin-Associated Glycoprotein)
RN  - 0 (Polysaccharides)
RN  - GZP2782OP0 (N-Acetylneuraminic Acid)
SB  - IM
MH  - Animals
MH  - Axons/*physiology
MH  - Cerebellum/metabolism
MH  - Ligands
MH  - Myelin-Associated Glycoprotein/*antagonists & inhibitors
MH  - N-Acetylneuraminic Acid/metabolism
MH  - Polysaccharides/*metabolism
MH  - Rats
PMC - PMC1852507
MID - NIHMS13381
EDAT- 2005/02/11 09:00
MHDA- 2005/06/24 09:00
CRDT- 2005/02/11 09:00
PHST- 2005/02/11 09:00 [pubmed]
PHST- 2005/06/24 09:00 [medline]
PHST- 2005/02/11 09:00 [entrez]
AID - M500250200 [pii]
AID - 10.1074/jbc.M500250200 [doi]
PST - ppublish
SO  - J Biol Chem. 2005 Apr 22;280(16):16305-10. doi: 10.1074/jbc.M500250200. Epub 2005
      Feb 8.

PMID- 7503987
OWN - NLM
STAT- MEDLINE
DCOM- 19940104
LR  - 20051117
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 268
IP  - 34
DP  - 1993 Dec 5
TI  - Binding of the O-antigen of Shigella dysenteriae type 1 and 26 related synthetic 
      fragments to a monoclonal IgM antibody.
PG  - 25797-802
AB  - Shigella dysenteriae type 1 possesses an O-antigen whose repeating unit is
      -->3)-alpha-L-Rhap-(1-->3)-alpha-L-Rhap-(1-->2)-alpha-D-Galp -(1-->3)-alpha-D-
      GlcpNAc-(1-->, where Rhap is rhamnopyranosyl, Galp is galactopyranosyl, and Glcp 
      is glucopyranosyl. Using ligand-induced protein fluorescence change, we have
      measured the affinities of a monoclonal murine IgM for 26 fragments of, or
      related to, the structure of the O-polysaccharide and of the IgM Fab for the
      intact O-specific bacterial polysaccharide. Synthetic saccharides used were
      methyl glycosides to ensure an anomerically defined pyranosyl ring conformation. 
      The galactosyl residue is the only monosaccharide of the antigenic epitope that
      shows quantifiable binding: approximately 3.0 kcal/mol of binding free energy,
      depending on the structure and conformation of the fragment it is a part of.
      Addition of an alpha-(1-->2)-linked rhamnosyl residue increases the free energy
      of binding significantly. We propose this
      rhamnopyranosyl-alpha-(1-->2)-galactopyranosyl disaccharide to be the basic
      determinant of the Shigella O-polysaccharide. Further extension (by linkages as
      in the natural antigen) of this oligosaccharidic ligand toward the upstream end
      (in an oligo- (or poly-)saccharide, such as A-->B-->C-->D-->E-->m, where A, B, C,
      D, and E are sugars and m is any moiety, such as methyl, we define A as the
      glycosyl- or upstream terminus, and E as the glycoside- or downstream terminus)
      by rhamnosyl and N-acetylglucosaminyl moieties improves the binding only
      minimally. The antibody is quite specific for the
      rhamnosyl-alpha-(1-->2)-galactosyl sequence but less so for the nature of the
      attachment to the galactosyl residue on the downstream side. Measurements using
      IgM Fab and the intact O-specific polysaccharide show that the antibody can bind 
      internal segments on the antigen chain. The free energy of binding of this
      antibody for the disaccharide determinant varies from -delta G of 4.7 to 5.1
      kcal/mol, depending on its flanking residues.
FAU - Pavliak, V
AU  - Pavliak V
AD  - National Institute of Diabetes and Digestive and Kidney Diseases, National
      Institutes of Health, Bethesda, Maryland 20892.
FAU - Nashed, E M
AU  - Nashed EM
FAU - Pozsgay, V
AU  - Pozsgay V
FAU - Kovac, P
AU  - Kovac P
FAU - Karpas, A
AU  - Karpas A
FAU - Chu, C
AU  - Chu C
FAU - Schneerson, R
AU  - Schneerson R
FAU - Robbins, J B
AU  - Robbins JB
FAU - Glaudemans, C P
AU  - Glaudemans CP
LA  - eng
PT  - Journal Article
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigen-Antibody Complex)
RN  - 0 (Immunoglobulin Fab Fragments)
RN  - 0 (Immunoglobulin M)
RN  - 0 (O Antigens)
RN  - 0 (Oligosaccharides)
RN  - 0 (Polysaccharides, Bacterial)
SB  - IM
MH  - Animals
MH  - Antibodies, Monoclonal/isolation & purification/*metabolism
MH  - Antigen-Antibody Complex
MH  - Carbohydrate Conformation
MH  - Carbohydrate Sequence
MH  - Chromatography, Affinity
MH  - Electrophoresis, Polyacrylamide Gel
MH  - Immunoglobulin Fab Fragments/isolation & purification/metabolism
MH  - Immunoglobulin M/isolation & purification/*metabolism
MH  - Kinetics
MH  - Mice
MH  - Mice, Inbred BALB C/immunology
MH  - Molecular Sequence Data
MH  - Molecular Weight
MH  - O Antigens
MH  - Oligosaccharides/chemical synthesis/chemistry/*metabolism
MH  - Polysaccharides, Bacterial/chemistry/immunology/*metabolism
MH  - Shigella dysenteriae/classification/*immunology
MH  - Thermodynamics
EDAT- 1993/12/05 00:00
MHDA- 1993/12/05 00:01
CRDT- 1993/12/05 00:00
PHST- 1993/12/05 00:00 [pubmed]
PHST- 1993/12/05 00:01 [medline]
PHST- 1993/12/05 00:00 [entrez]
PST - ppublish
SO  - J Biol Chem. 1993 Dec 5;268(34):25797-802.

PMID- 6667675
OWN - NLM
STAT- MEDLINE
DCOM- 19840329
LR  - 20181113
IS  - 0261-4189 (Print)
IS  - 0261-4189 (Linking)
VI  - 2
IP  - 12
DP  - 1983
TI  - The glycosidic antigen recognised by a novel monoclonal antibody, 75.12, is
      developmentally regulated on mouse embryonal carcinoma cells.
PG  - 2217-22
AB  - Monoclonal antibody 75.12 raised against the human ovarian teratocarcinoma cell
      line PA1 detects a 'Y' or iso-leb glycosidic structure. Using the 75.12 antibody 
      we have established that the Y antigen is expressed on some but not all mouse
      embryonal carcinoma (EC) lines. The Y or 75.12 antigen-positive EC cell lines F9 
      and PCC4 cease to express the antigen after differentiation induced with retinoic
      acid and this decreased expression parallels the morphological differentiation of
      the EC cells. These results support not only the idea that carbohydrate
      structures present on embryonic cells undergo marked alteration during
      differentiation, but also that established mouse EC cells may differ in their
      differentiation states.
FAU - Blaineau, C
AU  - Blaineau C
FAU - Le Pendu, J
AU  - Le Pendu J
FAU - Arnaud, D
AU  - Arnaud D
FAU - Connan, F
AU  - Connan F
FAU - Avner, P
AU  - Avner P
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - EMBO J
JT  - The EMBO journal
JID - 8208664
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigen-Antibody Complex)
RN  - 0 (Antigens, Neoplasm)
RN  - 0 (Oligosaccharides)
SB  - IM
MH  - Animals
MH  - *Antibodies, Monoclonal
MH  - Antigen-Antibody Complex
MH  - Antigens, Neoplasm
MH  - Blastocyst/immunology
MH  - Carbohydrate Conformation
MH  - Carbohydrate Sequence
MH  - Cell Line
MH  - Embryonal Carcinoma Stem Cells
MH  - Female
MH  - Fetus/immunology
MH  - Humans
MH  - Male
MH  - Mice
MH  - Morula/immunology
MH  - Neoplasms/immunology
MH  - Neoplastic Stem Cells/*immunology
MH  - Oligosaccharides/chemical synthesis
MH  - Stem Cells/*immunology
MH  - Teratoma/*immunology
PMC - PMC555437
EDAT- 1983/01/01 00:00
MHDA- 1983/01/01 00:01
CRDT- 1983/01/01 00:00
PHST- 1983/01/01 00:00 [pubmed]
PHST- 1983/01/01 00:01 [medline]
PHST- 1983/01/01 00:00 [entrez]
PST - ppublish
SO  - EMBO J. 1983;2(12):2217-22.

PMID- 3614206
OWN - NLM
STAT- MEDLINE
DCOM- 19870901
LR  - 20071114
IS  - 0161-5890 (Print)
IS  - 0161-5890 (Linking)
VI  - 24
IP  - 1
DP  - 1987 Jan
TI  - A monoclonal antibody with reactivity to asialo GM1 and murine natural killer
      cells.
PG  - 57-65
AB  - A monoclonal antibody (MAb) was prepared by the fusion of murine SP2-O myeloma
      cells with BALB/cByJ spleen cells that were immunized with the glycolipid asialo 
      GM1 adsorbed to naked Salmonella. The specificity of the IgM antibody obtained
      was defined using various glycolipids, cell extracts and saccharides in ELISA
      assays and thin-layer chromatography (TLC) immunoblots. The non-reducing terminal
      galactose is the immunodominant residue for this antibody; however, there is
      undetectable reactivity to free galactose, galactosylceramide or compounds with
      an alpha-linked galactose. The SH-34 antibody specifically lyses asialo
      GM1-expressing macrophages in the presence of complement and removes NK cells in 
      vitro from spleen cell populations. When the specificity of the MAb was compared 
      to that of a commercially available rabbit antiserum to asialo GM1, it was found 
      that both cross-reacted with GM1 and asialo GM3 at high antibody concns; however,
      the MAb did not bind asialo GM2 while the rabbit antiserum showed substantial
      reactivity to this glycolipid. It is anticipated that this MAb will be useful for
      the study of murine and rat natural killer cells.
FAU - Solomon, F R
AU  - Solomon FR
FAU - Higgins, T J
AU  - Higgins TJ
LA  - eng
GR  - S07-RR-05415-24/RR/NCRR NIH HHS/United States
PT  - Journal Article
PT  - Research Support, U.S. Gov't, Non-P.H.S.
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - England
TA  - Mol Immunol
JT  - Molecular immunology
JID - 7905289
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Glycolipids)
RN  - 0 (Glycosphingolipids)
RN  - 37758-47-7 (G(M1) Ganglioside)
RN  - 71012-19-6 (asialo GM1 ganglioside)
RN  - 9007-36-7 (Complement System Proteins)
SB  - IM
MH  - Animals
MH  - Antibodies, Monoclonal/*immunology
MH  - Antibody Specificity
MH  - Binding, Competitive
MH  - Chromatography, Thin Layer
MH  - Complement System Proteins/immunology
MH  - Cytotoxicity, Immunologic
MH  - Enzyme-Linked Immunosorbent Assay
MH  - Female
MH  - *G(M1) Ganglioside
MH  - Glycolipids/immunology
MH  - Glycosphingolipids/*immunology
MH  - Killer Cells, Natural/*immunology
MH  - Male
MH  - Mice
MH  - Mice, Inbred BALB C
MH  - Mice, Inbred CBA
EDAT- 1987/01/01 00:00
MHDA- 1987/01/01 00:01
CRDT- 1987/01/01 00:00
PHST- 1987/01/01 00:00 [pubmed]
PHST- 1987/01/01 00:01 [medline]
PHST- 1987/01/01 00:00 [entrez]
PST - ppublish
SO  - Mol Immunol. 1987 Jan;24(1):57-65.

PMID- 11125284
OWN - NLM
STAT- MEDLINE
DCOM- 20010222
LR  - 20180213
IS  - 1010-4283 (Print)
IS  - 1010-4283 (Linking)
VI  - 22
IP  - 2
DP  - 2001 Mar-Apr
TI  - Prognostic value of serum sialyl Lewis(a), sialyl Lewis(x) and sialyl Tn antigens
      in blood from the tumor drainage vein of colorectal cancer patients.
PG  - 115-22
AB  - The serum levels of sialyl Lewis(a) (CA19-9), sialyl Lewis(x) (SLX), sialyl Tn
      (STN) and carcinoembryonic antigen (CEA) in peripheral venous blood and tumor
      drainage venous blood of colorectal cancer patients were examined to determine
      their value as prognostic factors after surgery. Blood samples were obtained from
      the peripheral vein and from the tumor drainage vein from 124 colorectal cancer
      patients during surgical excision of the tumor. The patients were divided into
      high-antigen and low-antigen groups for each antigen in each location. Serum
      levels of SLX, STN and CEA in tumor drainage venous blood (d-SLX, d-STN and
      d-CEA, respectively) were significantly higher than in peripheral venous blood
      (p-SLX, p-STN and p-CEA, respectively). The survival time after surgery for
      patients with high d-SLX or d-CEA levels and low levels of the same antigen in
      peripheral venous blood was significantly shorter than the survival time for
      those patients with low levels of antigen at both sites (p = 0.0003 or p =
      0.0406, respectively). Cox's regression analysis revealed that a high d-SLX or
      high d-CEA level was an independent prognostic variable for patient survival. In 
      conclusion, determining d-SLX or d-CEA is more useful than p-SLX or p-CEA in
      predicting the outcome for colorectal cancer patients.
CI  - Copyright 2001 S. Karger AG, Basel
FAU - Nakagoe, T
AU  - Nakagoe T
AD  - First Department of Surgery, Nagasaki University School of Medicine, Nagasaki,
      Japan. nakagoe@net.nagasaki-u.ac.jp
FAU - Sawai, T
AU  - Sawai T
FAU - Tsuji, T
AU  - Tsuji T
FAU - Jibiki, M
AU  - Jibiki M
FAU - Ohbatake, M
AU  - Ohbatake M
FAU - Nanashima, A
AU  - Nanashima A
FAU - Yamaguchi, H
AU  - Yamaguchi H
FAU - Yasutake, T
AU  - Yasutake T
FAU - Ayabe, H
AU  - Ayabe H
FAU - Arisawa, K
AU  - Arisawa K
LA  - eng
PT  - Journal Article
PL  - United States
TA  - Tumour Biol
JT  - Tumour biology : the journal of the International Society for Oncodevelopmental
      Biology and Medicine
JID - 8409922
RN  - 0
      (5-acetylneuraminyl-(2-3)-galactosyl-(1-4)-(fucopyranosyl-(1-3))-N-acetylglucosam
      ine)
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (CA-19-9 Antigen)
RN  - 0 (Carcinoembryonic Antigen)
RN  - 0 (Oligosaccharides)
RN  - 0 (sialosyl-Tn antigen)
SB  - IM
MH  - Adult
MH  - Aged
MH  - Aged, 80 and over
MH  - Antigens, Tumor-Associated, Carbohydrate/*blood
MH  - CA-19-9 Antigen/*blood
MH  - Carcinoembryonic Antigen/blood
MH  - Colorectal Neoplasms/*blood/*blood supply/*diagnosis/surgery
MH  - Disease-Free Survival
MH  - Female
MH  - Humans
MH  - Male
MH  - Middle Aged
MH  - Oligosaccharides/*blood
MH  - Prognosis
MH  - Regression Analysis
MH  - Time Factors
MH  - Treatment Outcome
EDAT- 2000/12/23 11:00
MHDA- 2001/03/03 10:01
CRDT- 2000/12/23 11:00
PHST- 2000/12/23 11:00 [pubmed]
PHST- 2001/03/03 10:01 [medline]
PHST- 2000/12/23 11:00 [entrez]
AID - 50605 [pii]
AID - 10.1159/000050605 [doi]
PST - ppublish
SO  - Tumour Biol. 2001 Mar-Apr;22(2):115-22. doi: 10.1159/000050605.

PMID- 1988363
OWN - NLM
STAT- MEDLINE
DCOM- 19910225
LR  - 20160303
IS  - 0020-7136 (Print)
IS  - 0020-7136 (Linking)
VI  - 47
IP  - 2
DP  - 1991 Jan 21
TI  - Blood group and blood-group-related antigens in normal pancreas and pancreas
      cancer: enhanced expression of precursor type 1, Tn and sialyl-Tn in pancreas
      cancer.
PG  - 180-7
AB  - Expression of blood-group antigens A, B, Le(a), sialyl-Le(a) (sLe(a)), Le(b),
      Le(x), Le(y), precursor type I, Tn and sialyl-Tn (sTn) was examined in
      non-neoplastic pancreas (n = 37) and pancreas cancer (n = 21) using mouse
      monoclonal antibodies (MAbs). Immunohistochemical assays were performed on
      sections of paraffin-embedded tissues using the avidin-biotin complex method. In 
      normal pancreas, antibodies detecting Le(a), sLe(a) and Tn reacted with ductal
      epithelium, and antibodies detecting A and B reacted with acini and ducts,
      independently of secretor status. Le(x) was weakly expressed in ducts and acini, 
      and sTn could not be detected in normal pancreas. Expression of Le(b), Le(y) and 
      precursor type I was regulated by secretor status: Le(b) and Le(y) were expressed
      in ducts of secretor and Le(a-b-) individuals, but not in ducts of non-secretors;
      precursor type I was weakly expressed in acini and ducts of non-secretors and
      Le(a-b-) individuals, and was absent in acini and ducts of secretors. The
      following alterations in the expression of blood-group antigens were observed in 
      pancreas cancer: (1) enhanced expression of Le(x), Tn and sTn; (2) enhanced
      expression of precursor type I independently of secretor status; (3) loss of
      regulation of Le(b) by the secretor gene; (4) decreased expression of Le(y). The 
      weak expression of precursor type I. Tn and sTn in non-neoplastic pancreas, and
      their stronger expression in pancreas cancer, suggests that up-regulation of
      their expression is associated with malignant transformation of pancreatic duct
      cells.
FAU - Schuessler, M H
AU  - Schuessler MH
AD  - Memorial Sloan-Kettering Cancer Center, New York, NY 10021.
FAU - Pintado, S
AU  - Pintado S
FAU - Welt, S
AU  - Welt S
FAU - Real, F X
AU  - Real FX
FAU - Xu, M
AU  - Xu M
FAU - Melamed, M R
AU  - Melamed MR
FAU - Lloyd, K O
AU  - Lloyd KO
FAU - Oettgen, H F
AU  - Oettgen HF
LA  - eng
GR  - CA-08748/CA/NCI NIH HHS/United States
GR  - CA-33049/CA/NCI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Int J Cancer
JT  - International journal of cancer
JID - 0042124
RN  - 0 (ABO Blood-Group System)
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens, Neoplasm)
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Biomarkers, Tumor)
RN  - 0 (Blood Group Antigens)
RN  - 0 (Lewis Blood-Group System)
RN  - 0 (Tn antigen)
RN  - 0 (sialosyl-Tn antigen)
SB  - IM
MH  - ABO Blood-Group System/immunology
MH  - Antibodies, Monoclonal/immunology
MH  - Antigens, Neoplasm/*analysis
MH  - *Antigens, Tumor-Associated, Carbohydrate
MH  - Biomarkers, Tumor/*analysis
MH  - Blood Group Antigens/*immunology
MH  - Humans
MH  - Immunoenzyme Techniques
MH  - Lewis Blood-Group System/immunology
MH  - Pancreas/*immunology
MH  - Pancreatic Neoplasms/*immunology
EDAT- 1991/01/21 00:00
MHDA- 1991/01/21 00:01
CRDT- 1991/01/21 00:00
PHST- 1991/01/21 00:00 [pubmed]
PHST- 1991/01/21 00:01 [medline]
PHST- 1991/01/21 00:00 [entrez]
PST - ppublish
SO  - Int J Cancer. 1991 Jan 21;47(2):180-7.

PMID- 9257857
OWN - NLM
STAT- MEDLINE
DCOM- 19970828
LR  - 20171116
IS  - 0022-1767 (Print)
IS  - 0022-1767 (Linking)
VI  - 159
IP  - 4
DP  - 1997 Aug 15
TI  - Expression of leukocyte fucosyltransferases regulates binding to E-selectin:
      relationship to previously implicated carbohydrate epitopes.
PG  - 1917-29
AB  - E-selectin is a carbohydrate-binding endothelial cell adhesion molecule that
      reportedly interacts with several related sialylated and fucosylated
      carbohydrates. The activity of leukocyte alpha1,3-fucosyltransferases (FucT-IV or
      FucT-VII) is an essential step in the synthesis of E-selectin ligands. Using a
      panel of stably transfected hemopoietic cell lines, we have investigated the role
      of alpha1,3-fucosyltransferases in generating E-selectin ligands, and the
      relationship between adhesion to E-selectin and expression of mAb-defined
      carbohydrates. Expression of FucT-VII was always sufficient for binding to E- and
      P-selectin, while the ability of FucT-IV to construct E-selectin ligands varied
      among different cell types. Furthermore, FucT-IV was unable to support any
      binding to P-selectin in a lymphoid cell line, even when expressed at levels
      equivalent to those in myeloid cells. FucT-IV expression generated high levels of
      surface Le(x)/CD15 and CDw65, whereas expression of FucT-VII correlated with a
      subset of mAb-defined sialyl Lewis X (sLex)-like structures. FucT-IV-associated
      epitopes were present on both binding and nonbinding cells, whereas all cells
      that expressed FucT-VII-associated epitopes bound E-selectin. However, treatment 
      of HL60 cells with neuraminidase destroyed FucT-VII-associated epitopes at a
      faster rate than E-selectin binding sites. Surface expression of a subset of
      mAb-defined sLex-like carbohydrates is therefore a good marker for high levels of
      FucT-VII activity, but these carbohydrates are not themselves required for
      recognition of E-selectin.
FAU - Wagers, A J
AU  - Wagers AJ
AD  - Department of Microbiology and Immunology, Northwestern Medical School, Chicago, 
      IL 60611, USA.
FAU - Stoolman, L M
AU  - Stoolman LM
FAU - Kannagi, R
AU  - Kannagi R
FAU - Craig, R
AU  - Craig R
FAU - Kansas, G S
AU  - Kansas GS
LA  - eng
GR  - AI33189/AI/NIAID NIH HHS/United States
GR  - HL31963/HL/NHLBI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, Non-P.H.S.
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - J Immunol
JT  - Journal of immunology (Baltimore, Md. : 1950)
JID - 2985117R
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (E-Selectin)
RN  - 0 (Epitopes)
RN  - 0 (Lewis X Antigen)
RN  - 0 (P-Selectin)
RN  - 0 (RNA, Messenger)
RN  - EC 2.4.1.- (Fucosyltransferases)
RN  - EC 2.4.1.152 (galactoside 3-fucosyltransferase)
SB  - AIM
SB  - IM
MH  - Animals
MH  - Antibodies, Monoclonal/immunology
MH  - COS Cells
MH  - E-Selectin/*metabolism
MH  - *Epitopes
MH  - Fucosyltransferases/genetics/immunology/*physiology
MH  - Humans
MH  - Leukocytes/*enzymology
MH  - Lewis X Antigen/*immunology
MH  - P-Selectin/metabolism
MH  - RNA, Messenger/analysis
MH  - Tumor Cells, Cultured
EDAT- 1997/08/15 00:00
MHDA- 1997/08/15 00:01
CRDT- 1997/08/15 00:00
PHST- 1997/08/15 00:00 [pubmed]
PHST- 1997/08/15 00:01 [medline]
PHST- 1997/08/15 00:00 [entrez]
PST - ppublish
SO  - J Immunol. 1997 Aug 15;159(4):1917-29.

PMID- 12995288
OWN - NLM
STAT- MEDLINE
DCOM- 20030501
LR  - 20181201
IS  - 0040-1374 (Print)
IS  - 0040-1374 (Linking)
VI  - 7
IP  - 80
DP  - 1952 May
TI  - [The new ophthalmologic hospital in Djeddah (Arabia)].
PG  - 33
FAU - RULE, L
AU  - RULE L
LA  - und
PT  - Journal Article
TT  - Le nouvel hopital ophthalmologique de Djeddah (Arabie).
PL  - France
TA  - Tech Hosp Med Soc Sanit
JT  - Techniques hospitalieres, medico-sociales et sanitaires
JID - 21120470R
SB  - OM
MH  - Arabia
MH  - *Hospitals
MH  - Humans
MH  - *Ophthalmology
OID - CLML: 5323:19729:256:385
OTO - NLM
OT  - *HOSPITALS
OT  - *OPHTHALMOLOGY
EDAT- 1952/05/01 00:00
MHDA- 1952/05/01 00:01
CRDT- 1952/05/01 00:00
PHST- 1952/05/01 00:00 [pubmed]
PHST- 1952/05/01 00:01 [medline]
PHST- 1952/05/01 00:00 [entrez]
PST - ppublish
SO  - Tech Hosp Med Soc Sanit. 1952 May;7(80):33.

PMID- 2960671
OWN - NLM
STAT- MEDLINE
DCOM- 19871228
LR  - 20071114
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 262
IP  - 32
DP  - 1987 Nov 15
TI  - Synthesis of type 1 and 2 lacto series glycolipid antigens in human colonic
      adenocarcinoma and derived cell lines is due to activation of a normally
      unexpressed beta 1----3N-acetylglucosaminyltransferase.
PG  - 15649-58
AB  - Human colonic adenocarcinoma tissue and derived cell lines have been
      characterized by an abundance of different type 1 and 2 lacto series glycolipid
      antigens which are either low or not found in normal colonic mucosa. The
      enzymatic basis for the expression of contrasting glycolipid compositions between
      adenocarcinomas and normal colonic mucosa, as well as between derived cell lines,
      has been studied. The following results were of particular interest. (i) Abundant
      activities of beta 1----4galactosyltransferase associated with synthesis of both 
      lactosylceramide and lactoneotetraosylceramide, beta 1----3galactosyltransferase 
      for synthesis of lactotetraosylceramide, and an alpha 1----3/4fucosyltransferase 
      responsible for synthesis of Lex and Lea antigens were found in normal colonic
      mucosa or in a normal mucosal epithelial cell line HCMC, or in both. Variable
      levels of these activities were found in adenocarcinoma tissues and in various
      established adenocarcinoma cell lines. In striking contrast, significant activity
      of a beta 1----3N-acetylglucosaminyltransferase responsible for synthesis of
      lactotriaosylceramide (Lc3) was found in various cases of colonic adenocarcinoma 
      and cell lines, but was undetectable in normal colonic epithelial cells. (ii) In 
      situ transfer of galactose to Lc3 was performed on histologic sections by
      preincubation of the tissue with acceptor glycolipid followed by incubation with 
      UDP-galactose. The biosynthesized glycolipid was revealed by indirect
      immunofluorescence with the monoclonal antibody 1B2 which defines
      lactoneotetraosylceramide antigen. In these studies, histologic sections prepared
      from frozen normal proximal colon tissue were shown to lack native type 2 chain
      structures. However, transfer of galactose from UDP-galactose could be
      demonstrated in the epithelial cells of normal proximal colon after incorporation
      of Lc3 into the membranes, indicating the ability of normal colonic epithelial
      cells to synthesize type 2 chain core structures if the precursor Lc3 is
      available. In contrast, adenocarcinoma tissues showed significant native
      immunofluorescence with the antibody. These data suggest that an accumulation of 
      both type 1 and 2 chain lacto series glycolipids with alpha 1----3- or alpha
      1----4fucosyl substitution in human adenocarcinoma is due to enhanced beta
      1----3N-acetylglucosaminyltransferase rather than enhancement of other enzymes.
      This enzyme may play a key role in regulating the level of various types of lacto
      series tumor-associated antigens with the lacto type 1 or 2 chain.
FAU - Holmes, E H
AU  - Holmes EH
AD  - Pacific Northwest Research Foundation, Seattle, Washington 98104.
FAU - Hakomori, S
AU  - Hakomori S
FAU - Ostrander, G K
AU  - Ostrander GK
LA  - eng
GR  - CA41521/CA/NCI NIH HHS/United States
GR  - CA42505/CA/NCI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Glycolipids)
RN  - 0 (Lewis Blood-Group System)
RN  - EC 2.4.1.- (Glucosyltransferases)
RN  - EC 2.4.1.- (N-Acetylglucosaminyltransferases)
RN  - EC 2.4.1.- (glycosphingolipid beta1-3-N-acetylglucosaminyltransferase)
SB  - IM
MH  - Adenocarcinoma/*analysis
MH  - Carbohydrate Sequence
MH  - Cell Line
MH  - Chromatography, High Pressure Liquid
MH  - Chromatography, Thin Layer
MH  - Colonic Neoplasms/*analysis
MH  - Enzyme Activation
MH  - Fluorescent Antibody Technique
MH  - Glucosyltransferases/*metabolism
MH  - Glycolipids/*biosynthesis
MH  - Humans
MH  - Lewis Blood-Group System
MH  - *N-Acetylglucosaminyltransferases
EDAT- 1987/11/15 00:00
MHDA- 1987/11/15 00:01
CRDT- 1987/11/15 00:00
PHST- 1987/11/15 00:00 [pubmed]
PHST- 1987/11/15 00:01 [medline]
PHST- 1987/11/15 00:00 [entrez]
PST - ppublish
SO  - J Biol Chem. 1987 Nov 15;262(32):15649-58.

PMID- 11447138
OWN - NLM
STAT- MEDLINE
DCOM- 20011025
LR  - 20190513
IS  - 0959-6658 (Print)
IS  - 0959-6658 (Linking)
VI  - 11
IP  - 7
DP  - 2001 Jul
TI  - Cell surface-expressed Thomsen-Friedenreich antigen in colon cancer is
      predominantly carried on high molecular weight splice variants of CD44.
PG  - 587-92
AB  - Increased mucosal expression of TF, the Thomsen-Friedenreich oncofetal blood
      group antigen (galactose beta1-3 N-acetylgalactosamine alpha-) occurs in colon
      cancer and colitis. This allows binding of TF-specific lectins, such as peanut
      agglutinin (PNA), which is mitogenic to the colorectal epithelium. To identify
      the cell surface TF-expressing glycoprotein(s), HT29 and Caco2 colon cancer cells
      were surface-labeled with Na[(125)I] and subjected to PNA-agarose affinity
      purification and electrophoresis. Proteins, approximately 110-180 kDa, present in
      HT29 but not Caco2 were identified by Western blotting as high molecular weight
      splice variants of CD44 (CD44v). Selective removal of TF antigen by Streptococcus
      pneumoniae endo-alpha-N-acetylgalactosaminidase substantially reduced PNA binding
      to CD44v. Immunoprecipitated CD44v from HT29 cell extracts also expressed
      sialyl-Tn (sialyl 2-6 N-acetylgalactosaminealpha-). Incubation of PNA 15
      microg/ml with HT29 cells caused no additional proliferative effect in the
      presence of anti-CD44v6 mAb. In colon cancer tissue extracts (N = 3) PNA bound to
      CD44v but not to standard CD44. These data show that CD44v is a major PNA-binding
      glycoprotein in colon cancer cells. Because CD44 high molecular weight splice
      variants are present in colon cancer and inflammatory bowel disease tissue but
      are absent from normal mucosa, these results may also explain the increased PNA
      reactivity in colon cancer and inflammatory bowel disease. The coexpression of
      oncofetal carbohydrate antigens TF and sialyl-Tn on CD44 splice variants provides
      a link between cancer-associated changes in glycosylation and CD44 splicing, both
      of which correlate with increased metastatic potential.
FAU - Singh, R
AU  - Singh R
AD  - Department of Medicine, University of Liverpool, Daulby Street, Liverpool L69
      3GA, UK.
FAU - Campbell, B J
AU  - Campbell BJ
FAU - Yu, L G
AU  - Yu LG
FAU - Fernig, D G
AU  - Fernig DG
FAU - Milton, J D
AU  - Milton JD
FAU - Goodlad, R A
AU  - Goodlad RA
FAU - FitzGerald, A J
AU  - FitzGerald AJ
FAU - Rhodes, J M
AU  - Rhodes JM
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - Glycobiology
JT  - Glycobiology
JID - 9104124
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens, Surface)
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Hyaluronan Receptors)
RN  - 0 (Peptide Nucleic Acids)
RN  - 3554-90-3 (Thomsen-Friedenreich antigen)
SB  - IM
MH  - Antibodies, Monoclonal/immunology
MH  - Antigens, Surface/*immunology
MH  - Antigens, Tumor-Associated, Carbohydrate/*immunology
MH  - Colonic Neoplasms/*immunology/pathology
MH  - HT29 Cells
MH  - Humans
MH  - Hyaluronan Receptors/chemistry/genetics/*immunology/metabolism
MH  - Molecular Weight
MH  - Peptide Nucleic Acids/metabolism
EDAT- 2001/07/12 10:00
MHDA- 2001/10/26 10:01
CRDT- 2001/07/12 10:00
PHST- 2001/07/12 10:00 [pubmed]
PHST- 2001/10/26 10:01 [medline]
PHST- 2001/07/12 10:00 [entrez]
AID - 10.1093/glycob/11.7.587 [doi]
PST - ppublish
SO  - Glycobiology. 2001 Jul;11(7):587-92. doi: 10.1093/glycob/11.7.587.

PMID- 2448435
OWN - NLM
STAT- MEDLINE
DCOM- 19880322
LR  - 20151119
IS  - 0270-6474 (Print)
IS  - 0270-6474 (Linking)
VI  - 8
IP  - 2
DP  - 1988 Feb
TI  - Developmental regulation of ganglioside antigens recognized by the JONES
      antibody.
PG  - 580-92
AB  - The JONES monoclonal antibody has been immunocytochemically associated with
      regions of the developing rat brain where cell and axon migrations are occurring 
      (Mendez-Otero et al., 1986, 1988). In the present study the antigens recognized
      by the JONES antibody were analyzed in a variety of brain regions and at
      developmental ages selected to correspond to the preceding immunocytochemical
      observations. In accordance with earlier results from retina, JONES binding could
      not be detected in SDS gels from developing brain. Binding of the antibody was,
      however, prominent in chloroform/methanol extracts of the same tissues, and it
      was completely removed from tissue sections by brief chloroform/methanol
      form/methanol treatment. Enzymatic analyses of chloroform/methanol extracts
      indicated that the JONES epitope was sensitive to neuraminidase but insensitive
      to proteases. Overlay assays on developed high-performance thin-layer
      chromatographic plates (HPTLC) indicate that in all regions the JONES epitope
      resides on 2 or 3 ganglioside bands, depending on the age examined. These bands
      migrate between ganglioside standards GD 1a and GM2 on HPTLC plates and have been
      designated GJ1, GJ2, and GJ3, with the higher number designating the more rapidly
      migrating species. Occasionally, additional bands migrating in the range of
      polysialogangliosides were observed. The pattern of expression of GJ species was 
      studied in forebrain, retina, and cerebellar tissue taken from embryonic day 18
      (E18), postnatal day 0 (P0), P7, P14, and adult animals. Both region-specific
      differences in the relative prominence of each band and stage-specific
      differences in the total amount of the JONES gangliosides were detected. The
      stage-specific differences in the amount of JONES antigens are well correlated
      with the developmental periods of maximal cell migration in each region. While
      the JONES gangliosides are most prominent in forebrain before birth, in they are 
      most prominent during the first 2 postnatal weeks. In cerebellum, JONES antigen
      expression is more pronounced during the 2 periods of cell migration in this
      tissue. In retina, the more rapidly migrating GJ3 band was the most prominent
      band at all stages examined, and this same band is retained in the adult. In
      cerebellum and forebrain GJ3 is also the most pronounced band during development.
      However, in contrast to the retina, the more slowly migrating GJ1 band is
      retained in adult forebrain and cerebellum. A variety of non-brain tissues have
      also been examined for the presence of the JONES antigens.(ABSTRACT TRUNCATED AT 
      400 WORDS)
FAU - Schlosshauer, B
AU  - Schlosshauer B
AD  - Department of Biology, Yale University, New Haven, Connecticut 06511.
FAU - Blum, A S
AU  - Blum AS
FAU - Mendez-Otero, R
AU  - Mendez-Otero R
FAU - Barnstable, C J
AU  - Barnstable CJ
FAU - Constantine-Paton, M
AU  - Constantine-Paton M
LA  - eng
GR  - GM07739/GM/NIGMS NIH HHS/United States
GR  - NS 20483/NS/NINDS NIH HHS/United States
GR  - R07015/PHS HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, Non-P.H.S.
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - J Neurosci
JT  - The Journal of neuroscience : the official journal of the Society for
      Neuroscience
JID - 8102140
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Epitopes)
RN  - 0 (Gangliosides)
SB  - IM
MH  - Animals
MH  - *Antibodies, Monoclonal
MH  - *Brain Chemistry
MH  - Cell Movement
MH  - Epitopes/*analysis
MH  - Gangliosides/*immunology
MH  - Rats
MH  - Rats, Inbred Strains
MH  - Retina/analysis
EDAT- 1988/02/01 00:00
MHDA- 1988/02/01 00:01
CRDT- 1988/02/01 00:00
PHST- 1988/02/01 00:00 [pubmed]
PHST- 1988/02/01 00:01 [medline]
PHST- 1988/02/01 00:00 [entrez]
PST - ppublish
SO  - J Neurosci. 1988 Feb;8(2):580-92.

PMID- 11724906
OWN - NLM
STAT- MEDLINE
DCOM- 20020117
LR  - 20170214
IS  - 0022-1554 (Print)
IS  - 0022-1554 (Linking)
VI  - 49
IP  - 12
DP  - 2001 Dec
TI  - Altered GalNAc-alpha-2,6-sialylation compartments for mucin-associated sialyl-Tn 
      antigen in colorectal adenoma and adenocarcinoma.
PG  - 1581-92
AB  - Sialyl-Tn (STn), a mucin-associated disaccharide antigen carried by apomucins
      such as MUC2, plays an important role in tumor biology. However, little is known 
      about the subcellular localization and compartments involved in STn synthesis. In
      this study we used immunoelectron microscopy to localize STn and MUC2 apomucin in
      human colorectal tissues. MUC2 apomucin was localized predominantly in the rough 
      endoplasmic reticulum (RER) in normal colorectal mucosa (n=6), colorectal adenoma
      (n=8), and colorectal adenocarcinoma (n=10). STn, recognized by monoclonal
      antibody TKH2, was not readily detectable in normal colorectal mucosa but becomes
      manifest in both trans-Golgi apparatus and mucin droplets in colorectal adenoma. 
      In colorectal adenocarcinoma, STn was localized not only in late but also in
      early Golgi compartments, and particularly in some RER lumens. Furthermore,
      electron microscopic in situ hybridization revealed that gold particles
      representing MUC2 mRNA are primarily localized over the RER. Our findings
      indicate that in colorectal adenoma STn sialylation takes place in the
      trans-Golgi apparatus, whereas in colorectal cancer STn sialylation occurs in all
      the Golgi compartments and in the RER.
FAU - Wang, F
AU  - Wang F
AD  - Department of Pathology, Kagoshima University Faculty of Medicine, Kagoshima,
      Japan.
FAU - Goto, M
AU  - Goto M
FAU - Kim, Y S
AU  - Kim YS
FAU - Higashi, M
AU  - Higashi M
FAU - Imai, K
AU  - Imai K
FAU - Sato, E
AU  - Sato E
FAU - Yonezawa, S
AU  - Yonezawa S
LA  - eng
GR  - CA24321/CA/NCI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, Non-P.H.S.
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - J Histochem Cytochem
JT  - The journal of histochemistry and cytochemistry : official journal of the
      Histochemistry Society
JID - 9815334
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Apoproteins)
RN  - 0 (Biomarkers, Tumor)
RN  - 0 (MUC2 protein, human)
RN  - 0 (Mucin-2)
RN  - 0 (Mucins)
RN  - 0 (Neoplasm Proteins)
RN  - 0 (RNA, Messenger)
RN  - 0 (sialosyl-Tn antigen)
SB  - IM
MH  - Adenocarcinoma/*metabolism
MH  - Adenoma/*metabolism
MH  - Antigens, Tumor-Associated, Carbohydrate/biosynthesis/*metabolism
MH  - Apoproteins/genetics/*metabolism
MH  - Biomarkers, Tumor
MH  - Cell Compartmentation
MH  - Colon/metabolism
MH  - Colorectal Neoplasms/*metabolism
MH  - Humans
MH  - Intestinal Mucosa/metabolism
MH  - Microscopy, Immunoelectron
MH  - Mucin-2
MH  - Mucins/genetics/*metabolism
MH  - Neoplasm Proteins/*metabolism
MH  - Precancerous Conditions/metabolism
MH  - RNA, Messenger/metabolism
MH  - Rectum/metabolism
EDAT- 2001/11/29 10:00
MHDA- 2002/01/18 10:01
CRDT- 2001/11/29 10:00
PHST- 2001/11/29 10:00 [pubmed]
PHST- 2002/01/18 10:01 [medline]
PHST- 2001/11/29 10:00 [entrez]
AID - 10.1177/002215540104901212 [doi]
PST - ppublish
SO  - J Histochem Cytochem. 2001 Dec;49(12):1581-92. doi: 10.1177/002215540104901212.

PMID- 16809438
OWN - NLM
STAT- MEDLINE
DCOM- 20061201
LR  - 20071115
IS  - 0959-6658 (Print)
IS  - 0959-6658 (Linking)
VI  - 16
IP  - 10
DP  - 2006 Oct
TI  - Use of lectins for probing differentiated human embryonic stem cells for
      carbohydrates.
PG  - 981-90
AB  - The carbohydrates present on the surface of differentiated human embryonic stem
      cells (hESCs) are not yet well established. Here, we have employed a panel of
      lectins and several anti-carbohydrate antibodies to determine the carbohydrates
      that are present at day 12 of hESC differentiation as embryoid bodies (EBs). On
      the basis of staining with fluorescein-labeled lectins, we have determined the
      presence of both terminal and internally linked alpha-d-mannopyranosyl groups,
      poly-N-acetyllactosaminyl chains, both alpha2,3- and alpha2,6-linked
      N-acetylneuraminic acid (Neu5Ac), alpha1,6-linked l-fucosyl, and
      beta-D-galactosyl groups, and more specifically, the T, Tn, and sialyl-Tn
      antigens. However, no alpha1,2-linked l-fucosyl, terminal nonreducing
      alpha-D-galactosyl, N-acetyl-beta-D-glucosaminyl, nor
      N-acetyl-alpha-D-galactosaminyl groups were found by this approach. We also
      established the presence of Neu5Acalpha2,3/2,6-Galbeta1,4 GlcNAc-terminated
      chains on the surfaces of 12-day-old EBs, as indicated by the great enhancement
      of staining by Erythrina cristagalli agglutinin (ECA) after treatment with
      neuraminidase. In each case, inhibition of binding by a haptenic sugar or
      treatment with neuraminidase was used to eliminate the possibility of nonspecific
      binding of the lectins. A comparison with undifferentiated cell staining revealed
      an increase in alpha2,3-linked Neu5Ac as well as a change to exclusively
      alpha1,6-linked l-fucose upon differentiation.
FAU - Wearne, Kimberly A
AU  - Wearne KA
AD  - Department of Biological Chemistry, University of Michigan, Ann Arbor, MI 48109, 
      USA.
FAU - Winter, Harry C
AU  - Winter HC
FAU - O'Shea, Katherine
AU  - O'Shea K
FAU - Goldstein, Irwin J
AU  - Goldstein IJ
LA  - eng
GR  - GM29470/GM/NIGMS NIH HHS/United States
GR  - P20GM069985/GM/NIGMS NIH HHS/United States
PT  - Comparative Study
PT  - Journal Article
PT  - Research Support, N.I.H., Extramural
DEP - 20060629
PL  - England
TA  - Glycobiology
JT  - Glycobiology
JID - 9104124
RN  - 0 (Carbohydrates)
RN  - 0 (Plant Lectins)
SB  - IM
MH  - Carbohydrates/*analysis
MH  - *Cell Differentiation
MH  - Embryo, Mammalian/cytology
MH  - Embryonic Induction
MH  - Embryonic Stem Cells/chemistry/*cytology
MH  - Fluorescent Antibody Technique/methods
MH  - Humans
MH  - Plant Lectins/*pharmacology
EDAT- 2006/07/01 09:00
MHDA- 2006/12/09 09:00
CRDT- 2006/07/01 09:00
PHST- 2006/07/01 09:00 [pubmed]
PHST- 2006/12/09 09:00 [medline]
PHST- 2006/07/01 09:00 [entrez]
AID - cwl019 [pii]
AID - 10.1093/glycob/cwl019 [doi]
PST - ppublish
SO  - Glycobiology. 2006 Oct;16(10):981-90. doi: 10.1093/glycob/cwl019. Epub 2006 Jun
      29.

PMID- 18561742
OWN - NLM
STAT- MEDLINE
DCOM- 20080806
LR  - 20161020
IS  - 0884-6812 (Linking)
VI  - 30
IP  - 2
DP  - 2008 Apr
TI  - Expression of MUC1 and sialyl-Tn in benign prostatic glands, high-grade prostate 
      intraepithelial neoplasia and malignant prostatic glands: a preliminary study.
PG  - 71-7
AB  - OBJECTIVE: To postulate a possible role of MUC1 and sialylated mucins (sTn) in
      prostate malignancy. STUDY DESIGN: One sample histologic paraffin block of 24
      radical prostatectomies was selected for presence of both benign and malignant
      glands; 17 samples also included PIN. Serial cuts were stained with MUC1 and sTn 
      mouse monoclonal antibodies. Description and percentage of cell expression for
      MUC1 and sTn antibodies were obtained by light microscopy. RESULTS: MUC1
      immunostaining was more often positive for neoplastic cells, progressively from
      benign (4.7+/-5.3%) to PIN (27.1+/-19.7%) and malignant glands (34.5+/-28.4%).
      The same observation was made for sTn, respectively, from 3.9+/-4.9% to
      54.8+/-26.1% and 62.8+/-25.6%. Both antibodies showed a statistical difference
      between benign glands and PIN or malignant glands but not between PIN and
      malignant. CONCLUSION: MUC1 and sTn were expressed more intensely in PIN and
      malignant prostate glands than in benign glands. sTn seemed more specific in
      favor of cell malignancy.
FAU - Garbar, Christian
AU  - Garbar C
AD  - Department of Pathology, Free University of Brussels, Brussels, Belgium.
      christian.garbar@uzbrussel.be
FAU - Mascaux, Corinne
AU  - Mascaux C
FAU - Wespes, Eric
AU  - Wespes E
LA  - eng
PT  - Journal Article
PL  - United States
TA  - Anal Quant Cytol Histol
JT  - Analytical and quantitative cytology and histology
JID - 8506819
RN  - 0 (MUC1 protein, human)
RN  - 0 (Mucin-1)
RN  - 0 (Sialomucins)
SB  - IM
MH  - Humans
MH  - Immunohistochemistry
MH  - Male
MH  - Mucin-1/*metabolism
MH  - Neoplasm Staging
MH  - Prostate/metabolism
MH  - Prostatic Intraepithelial Neoplasia/metabolism/*pathology
MH  - Prostatic Neoplasms/metabolism/*pathology
MH  - Sialomucins/*metabolism
EDAT- 2008/06/20 09:00
MHDA- 2008/08/07 09:00
CRDT- 2008/06/20 09:00
PHST- 2008/06/20 09:00 [pubmed]
PHST- 2008/08/07 09:00 [medline]
PHST- 2008/06/20 09:00 [entrez]
PST - ppublish
SO  - Anal Quant Cytol Histol. 2008 Apr;30(2):71-7.

PMID- 7780013
OWN - NLM
STAT- MEDLINE
DCOM- 19950720
LR  - 20190512
IS  - 0006-3363 (Print)
IS  - 0006-3363 (Linking)
VI  - 52
IP  - 4
DP  - 1995 Apr
TI  - Monoclonal antibody directed to Le(y) oligosaccharide inhibits implantation in
      the mouse.
PG  - 903-12
AB  - We investigated the role of carbohydrates in blastocyst attachment to the uterine
      epithelium. Le(y) (Fuc alpha 1-->2Gal beta 1-->4[Fuc alpha 1-->3] GlcNAc) was
      localized by indirect immunofluorescence to the surface of the mouse blastocyst
      and uterine epithelium. Western blot analysis showed that Le(y) is carried on
      many uterine glycoproteins in both pregnant and nonpregnant females; however, new
      species were detected on Day 4 postcoitum (p.c.) coincident with the onset of
      uterine receptivity. The function of Le(y) in implantation was tested by
      injecting monoclonal antibody (mAb) directly into the uterine lumen on Days 3-5
      p.c. The effects of intrauterine injections on implantation were scored by
      comparing the number of viable embryos to the number of CL on Day 10 p.c.
      Injection of purified anti-Le(y) IgM into the uterine lumen on the afternoon of
      Day 4 significantly inhibited implantation. This effect was dose-dependent and
      was obtained during a narrow time window, from 87 to 93 h p.c. Inhibition of
      implantation was not observed in contralateral uterine horns injected with
      saline, nor was it observed in uterine horns injected with other
      anti-carbohydrate mAbs. We conclude that binding of anti-Le(y) to the blastocyst 
      or luminal epithelium masks a ligand involved in implantation. Although the
      mechanism of inhibition is unknown, we show that Le(y) can interact with another 
      oligosaccharide (H) that has been described as a possible uterine ligand for
      blastocyst attachment. We hypothesize that Le(y) and H form
      carbohydrate-carbohydrate interactions that promote close apposition of cell
      surface membranes during an early step in implantation.
FAU - Zhu, Z M
AU  - Zhu ZM
AD  - Department of Pathology, Anatomy, and Cell Biology, Jefferson Medical College
      Thomas Jefferson University, Philadelphia, Pennsylvania 19107, USA.
FAU - Kojima, N
AU  - Kojima N
FAU - Stroud, M R
AU  - Stroud MR
FAU - Hakomori, S
AU  - Hakomori S
FAU - Fenderson, B A
AU  - Fenderson BA
LA  - eng
GR  - CA42505/CA/NCI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Biol Reprod
JT  - Biology of reproduction
JID - 0207224
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens, Differentiation)
RN  - 0 (Immunoglobulin M)
RN  - 0 (Lewis Blood-Group System)
RN  - 0 (Lewis X Antigen)
RN  - 0 (Lewis Y antigen)
SB  - IM
MH  - Animals
MH  - Antibodies, Monoclonal/administration & dosage/*pharmacology
MH  - Antigens, Differentiation/analysis
MH  - Blastocyst/physiology
MH  - Carbohydrate Sequence
MH  - Embryo Implantation/drug effects/*physiology
MH  - Female
MH  - Fluorescent Antibody Technique
MH  - Immunoglobulin M/administration & dosage/pharmacology
MH  - *Lewis Blood-Group System
MH  - Lewis X Antigen/analysis/immunology/*physiology
MH  - Mice
MH  - Molecular Sequence Data
MH  - Uterus/chemistry/immunology
EDAT- 1995/04/01 00:00
MHDA- 1995/04/01 00:01
CRDT- 1995/04/01 00:00
PHST- 1995/04/01 00:00 [pubmed]
PHST- 1995/04/01 00:01 [medline]
PHST- 1995/04/01 00:00 [entrez]
AID - 10.1095/biolreprod52.4.903 [doi]
PST - ppublish
SO  - Biol Reprod. 1995 Apr;52(4):903-12. doi: 10.1095/biolreprod52.4.903.

PMID- 3390832
OWN - NLM
STAT- MEDLINE
DCOM- 19880824
LR  - 20071114
IS  - 0008-5472 (Print)
IS  - 0008-5472 (Linking)
VI  - 48
IP  - 15
DP  - 1988 Aug 1
TI  - Immunoglobulin G3 monoclonal antibody directed to Tn antigen (tumor-associated
      alpha-N-acetylgalactosaminyl epitope) that does not cross-react with blood group 
      A antigen.
PG  - 4361-7
AB  - An IgG3 monoclonal antibody (CU-1) directed to the Tn glycoprotein antigen, which
      does not cross-react with blood group A antigen, has been established after
      immunization of mice with a purified Tn antigen, followed by selection of
      hybridomas secreting antibodies with the desired specificity. The antibody
      binding with Tn antigen was inhibited by monosaccharide N-acetylgalactosamine (a 
      mixture of alpha and beta anomers) and specifically by
      p-nitrophenyl-alpha-D-N-acetylgalactosaminide but not by
      p-nitrophenyl-beta-D-N-acetylgalactosaminide, and the antibody binding was
      competitively inhibited by an IgM anti-Tn antibody NCC-LU-81. The antibody was
      not reactive with blood group A antigen, in contrast to previously reported
      anti-Tn antibodies which showed various degrees of cross-reactivity.
      Immunoperoxidase staining of various tumors and normal tissues with CU-1 showed a
      strong preferential or specific staining of sections from various cancer tissues 
      over normal counterpart tissues, except for goblet cells in colon and some
      mammary gland epithelia. The positive staining in cancer and normal tissues was
      independent of the blood group ABH status of the host. Among various human cell
      lines tested, a number of cancer cell lines showed various degrees of antibody
      binding activity, although the binding did not correlate with the
      pathohistological type of the tumor cell lines. The intensity of antibody binding
      to cells was not proportional to the susceptibility of cells to the
      antibody-dependent cytotoxicity.
FAU - Takahashi, H K
AU  - Takahashi HK
AD  - Department of Biochemical Oncology, Fred Hutchinson Cancer Research Center,
      Seattle, Washington 98104.
FAU - Metoki, R
AU  - Metoki R
FAU - Hakomori, S
AU  - Hakomori S
LA  - eng
GR  - CA42505/CA/NCI NIH HHS/United States
GR  - FO5 TW03783/TW/FIC NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Cancer Res
JT  - Cancer research
JID - 2984705R
RN  - 0 (ABO Blood-Group System)
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens, Neoplasm)
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Glycolipids)
RN  - 0 (Immunoglobulin G)
RN  - 0 (Tn antigen)
SB  - IM
MH  - ABO Blood-Group System/*immunology
MH  - Animals
MH  - *Antibodies, Monoclonal
MH  - Antibody-Dependent Cell Cytotoxicity
MH  - Antigens, Neoplasm/*immunology
MH  - *Antigens, Tumor-Associated, Carbohydrate
MH  - Cell Line
MH  - Cross Reactions
MH  - Glycolipids/immunology
MH  - Humans
MH  - *Immunoglobulin G
MH  - Immunohistochemistry
MH  - Mice
EDAT- 1988/08/01 00:00
MHDA- 1988/08/01 00:01
CRDT- 1988/08/01 00:00
PHST- 1988/08/01 00:00 [pubmed]
PHST- 1988/08/01 00:01 [medline]
PHST- 1988/08/01 00:00 [entrez]
PST - ppublish
SO  - Cancer Res. 1988 Aug 1;48(15):4361-7.

PMID- 1851822
OWN - NLM
STAT- MEDLINE
DCOM- 19910626
LR  - 20170210
IS  - 0732-183X (Print)
IS  - 0732-183X (Linking)
VI  - 9
IP  - 6
DP  - 1991 Jun
TI  - Clinical evaluation of circulating serum sialyl Tn antigen levels in patients
      with epithelial ovarian cancer.
PG  - 983-7
AB  - Sialyl Tn antigen (NeuAc alpha 2----6GalNac alpha 1----0-Ser/Thr [STN]) with
      antigenic specificity in the core structure of mucin-type carbohydrate chains has
      been determined. In the present study, we evaluated the clinical significance of 
      this new carbohydrate antigen, STN, in patients with epithelial ovarian cancer.
      With the use of a radioimmunoassay developed to detect STN antigen in serum,
      elevated (greater than or equal to 32.6 U/mL) antigen levels were observed in
      50.0% of patients with ovarian cancer. In contrast, 3.8% of healthy individuals
      had STN antigen levels greater than or equal to 32.6 U/mL. In 9.6% of patients
      with benign gynecologic diseases and 0% of pregnant women, there were elevated
      levels of STN antigen. There was a significant difference (P less than .001) in
      STN antigen levels between patients with ovarian cancer and patients with benign 
      gynecologic diseases, pregnant women, or the controls. The mean +/- SD for all
      evaluated samples of ovarian cancer was 109.2 +/- 146.8 U/mL. Both the mean
      values and the positive rate increased as the stage advanced. Classified
      according to the histologic type, the highest positive rate (61.0%) was observed 
      in mucinous adenocarcinoma. The usefulness of STN antigen as a circulating tumor 
      marker in ovarian cancer was estimated as follows: sensitivity 50.0%, specificity
      93.5%, positive predictive value 72.2%, negative predictive value 84.7%, and
      diagnostic value 46.8%. Serum STN antigen levels were elevated in 12 of 33
      patients with ovarian cancer who had serum CA 125 antigen levels less than 35
      U/mL. While CA 125 antigen levels were elevated in 74.6% and STN antigen levels
      were elevated in 50.0% of the same population, the use of both assays indicated
      the sensitivity of detection of 83.8% in the population studied.
FAU - Kobayashi, H
AU  - Kobayashi H
AD  - Department of Obstetrics and Gynecology, Hamamatsu University School of Medicine,
      Shizuoka, Japan.
FAU - Terao, T
AU  - Terao T
FAU - Kawashima, Y
AU  - Kawashima Y
LA  - eng
PT  - Journal Article
PL  - United States
TA  - J Clin Oncol
JT  - Journal of clinical oncology : official journal of the American Society of
      Clinical Oncology
JID - 8309333
RN  - 0 (Antigens, Neoplasm)
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Biomarkers, Tumor)
RN  - 0 (sialosyl-Tn antigen)
SB  - IM
MH  - Adenocarcinoma/immunology
MH  - Adenocarcinoma, Mucinous/immunology
MH  - Adult
MH  - Antigens, Neoplasm/*blood
MH  - Antigens, Tumor-Associated, Carbohydrate/blood
MH  - Biomarkers, Tumor/*blood
MH  - Carcinoma, Basal Cell/immunology
MH  - Cystadenocarcinoma/immunology
MH  - Endometriosis/immunology
MH  - Female
MH  - Humans
MH  - Middle Aged
MH  - Neoplasm Staging
MH  - Ovarian Neoplasms/*immunology/pathology
MH  - Predictive Value of Tests
MH  - Radioimmunoassay
MH  - Sensitivity and Specificity
EDAT- 1991/06/01 00:00
MHDA- 1991/06/01 00:01
CRDT- 1991/06/01 00:00
PHST- 1991/06/01 00:00 [pubmed]
PHST- 1991/06/01 00:01 [medline]
PHST- 1991/06/01 00:00 [entrez]
AID - 10.1200/JCO.1991.9.6.983 [doi]
PST - ppublish
SO  - J Clin Oncol. 1991 Jun;9(6):983-7. doi: 10.1200/JCO.1991.9.6.983.

PMID- 7544402
OWN - NLM
STAT- MEDLINE
DCOM- 19950926
LR  - 20061115
IS  - 0022-510X (Print)
IS  - 0022-510X (Linking)
VI  - 130
IP  - 1
DP  - 1995 May
TI  - Ganglioside-like epitopes of lipopolysaccharides from Campylobacter jejuni (PEN
      19) in three isolates from patients with Guillain-Barre syndrome.
PG  - 112-6
AB  - Sera from patients with Guillain-Barre syndrome (GBS) frequently have anti-GM1
      antibody. We earlier showed that an lipopolysaccharides (LPS) from Campylobacter 
      jejuni (PEN 19) isolated from a GBS patient has a GM1 ganglioside-like structure.
      Aspinall et al. (Biochemistry, 61 (1994) 335-337) reported that OH 4382 has an
      LPS that bears a CD3 ganglioside-like structure and that OH 4384 has an LPS that 
      bears a GT1a-like structure; both strains were isolated from patients with GBS.
      They also suggested a GM1-like structure is present in the LPSs from OH 4384, but
      failed to show the presence in the LPSs from OH 4382. To clarify the pathogenesis
      of GBS after infection by C. jejuni (PEN 19), we investigated the carbohydrate
      structures of the three strains by thin-layer chromatography immunostaining with 
      cholera toxin and monoclonal anti-ganglioside antibodies. We found that both OH
      4382 and OH 4384 have an LPS with the GM1 epitope as well as one with the GT1a or
      GD3 epitope.
FAU - Yuki, N
AU  - Yuki N
AD  - Department of Biochemistry, Faculty of Medicine, Tokyo Medical and Dental
      University, Japan.
FAU - Handa, S
AU  - Handa S
FAU - Tai, T
AU  - Tai T
FAU - Takahashi, M
AU  - Takahashi M
FAU - Saito, K
AU  - Saito K
FAU - Tsujino, Y
AU  - Tsujino Y
FAU - Taki, T
AU  - Taki T
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - Netherlands
TA  - J Neurol Sci
JT  - Journal of the neurological sciences
JID - 0375403
RN  - 0 (Antibodies, Bacterial)
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Epitopes)
RN  - 0 (Gangliosides)
RN  - 0 (Lipopolysaccharides)
RN  - 37758-47-7 (G(M1) Ganglioside)
RN  - 9012-63-9 (Cholera Toxin)
SB  - IM
MH  - Antibodies, Bacterial/*analysis/isolation & purification
MH  - Antibodies, Monoclonal/analysis
MH  - Campylobacter jejuni/*immunology
MH  - Carbohydrate Sequence
MH  - Cholera Toxin/immunology
MH  - Chromatography, Thin Layer
MH  - Epitopes/*analysis
MH  - G(M1) Ganglioside/immunology
MH  - Gangliosides/*immunology
MH  - Humans
MH  - Lipopolysaccharides/analysis/*immunology
MH  - Molecular Sequence Data
MH  - Polyradiculoneuropathy/*immunology
EDAT- 1995/05/01 00:00
MHDA- 1995/05/01 00:01
CRDT- 1995/05/01 00:00
PHST- 1995/05/01 00:00 [pubmed]
PHST- 1995/05/01 00:01 [medline]
PHST- 1995/05/01 00:00 [entrez]
AID - 0022-510X(95)00045-4 [pii]
PST - ppublish
SO  - J Neurol Sci. 1995 May;130(1):112-6.

PMID- 16547942
OWN - NLM
STAT- MEDLINE
DCOM- 20060726
LR  - 20071205
IS  - 0021-9541 (Print)
IS  - 0021-9541 (Linking)
VI  - 208
IP  - 1
DP  - 2006 Jul
TI  - Elevated Golgi pH in breast and colorectal cancer cells correlates with the
      expression of oncofetal carbohydrate T-antigen.
PG  - 167-74
AB  - Altered glycosylation has turned out to be a universal feature of cancer cells,
      and in many cases, to correlate with altered expression or localization of
      relevant glycosyltransferases. However, no such correlation exists between
      observed enzymatic changes and the expression of the oncofetal
      Thomsen-Friedenreich (T)-antigen, a core 1 (Gal-beta1 --> 3-GalNAc-ser/thr)
      carbohydrate structure. Here we report that T-antigen expression, instead,
      correlates with elevated Golgi pH in cancer cells. Firstly, using a
      Golgi-targeted green fluorescent protein (GT-EGFP) as a probe, we show that the
      medial/trans-Golgi pH (pHG) in a high proportion of breast (MCF-7) and colorectal
      (HT-29, SW-48) cancer cells is significantly more alkaline (pHG > or = 6.75) than
      that of control cells (pHG 5.9-6.5). The pH gradient between the cytoplasm and
      the Golgi lumen is also markedly reduced in MCF-7 cells, suggesting a Golgi
      acidification defect. Secondly, we show that T-antigen expression is highly
      sensitive to changes in Golgi pH, as only a 0.2 pH unit increase was sufficient
      to increase T-antigen expression in control cells. Thirdly, we found that
      T-antigen expressing MCF-7 cells have 0.3 pH units more alkaline Golgi pH than
      non-expressing MCF-7 cells. Fourthly, in all cell types examined, we observed
      significant correlation between the number of T-antigen expressing cells and
      cells with a markedly elevated Golgi pH (pHG > or = 6.75). Consistent with these 
      observations in cultured cells, cells in solid tumors also heterogenously
      expressed the T-antigen. Thus, elevated Golgi pH appears to be directly linked to
      T-antigen expression in cancer cells, but it may also act as a more general
      factor for altered glycosylation in cancer by affecting the distribution of
      Golgi-localized glycosyltransferases.
CI  - Copyright 2006 Wiley-Liss, Inc.
FAU - Rivinoja, Antti
AU  - Rivinoja A
AD  - Department of Biochemistry, University of Oulu, Linnanmaa, Oulu, Finland.
FAU - Kokkonen, Nina
AU  - Kokkonen N
FAU - Kellokumpu, Ilmo
AU  - Kellokumpu I
FAU - Kellokumpu, Sakari
AU  - Kellokumpu S
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - J Cell Physiol
JT  - Journal of cellular physiology
JID - 0050222
RN  - 0 (Antigens, Neoplasm)
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Polysaccharides)
RN  - 0 (oncofetal antigens)
RN  - 3554-90-3 (Thomsen-Friedenreich antigen)
RN  - EC 2.4.- (Glycosyltransferases)
SB  - IM
MH  - Antigens, Neoplasm/analysis/genetics/*physiology
MH  - Antigens, Tumor-Associated, Carbohydrate/analysis/genetics/*physiology
MH  - Breast Neoplasms/chemistry/pathology/*physiopathology
MH  - Cell Line, Tumor
MH  - Colorectal Neoplasms/chemistry/pathology/*physiopathology
MH  - Flow Cytometry
MH  - Gene Expression Regulation, Neoplastic
MH  - Glycosylation
MH  - Glycosyltransferases/analysis
MH  - Golgi Apparatus/enzymology/*physiology
MH  - Humans
MH  - Hydrogen-Ion Concentration
MH  - Immunohistochemistry
MH  - Microscopy, Fluorescence
MH  - Polysaccharides/metabolism
EDAT- 2006/03/21 09:00
MHDA- 2006/07/27 09:00
CRDT- 2006/03/21 09:00
PHST- 2006/03/21 09:00 [pubmed]
PHST- 2006/07/27 09:00 [medline]
PHST- 2006/03/21 09:00 [entrez]
AID - 10.1002/jcp.20653 [doi]
PST - ppublish
SO  - J Cell Physiol. 2006 Jul;208(1):167-74. doi: 10.1002/jcp.20653.

PMID- 7521878
OWN - NLM
STAT- MEDLINE
DCOM- 19941011
LR  - 20171116
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 269
IP  - 37
DP  - 1994 Sep 16
TI  - The P-selectin glycoprotein ligand from human neutrophils displays sialylated,
      fucosylated, O-linked poly-N-acetyllactosamine.
PG  - 23318-27
AB  - We previously demonstrated that P-selectin binds with high affinity to a trace,
      homodimeric glycoprotein ligand on human myeloid cells. The ligand carries the
      sialyl Lewis x (sLe(x)) epitope, a limited number of N-linked glycans, and
      clustered, sialylated O-linked glycans. In this study we demonstrate that the
      polypeptide component of this ligand is identical to that of P-selectin
      glycoprotein ligand-1 (PSGL-1), a molecule recently identified by expression
      cloning from a human myeloid cell cDNA library. We have examined the effects of
      glycosidases on purified, radioiodinated PSGL-1 from human neutrophils to further
      characterize the structure and function of the attached oligosaccharides. We
      found that PSGL-1 had poly-N-acetyllactosamine, only some of which could be
      removed with endo-beta-galactosidase. The majority of the Le(x) and sLe(x)
      structures were on endo-beta-galactosidase-sensitive chains.
      Peptide:N-glycosidase F (PNGaseF) treatment removed at least two of the three
      possible N-linked oligosaccharides from PSGL-1. Expression of Le(x) and sLe(x)
      was not detectably altered by PNGaseF digestion, indicating that these structures
      were primarily on O-linked poly-N-acetyllactosamine.
      Endo-beta-galactosidase-treated PSGL-1 retained the ability to bind to
      P-selectin, suggesting that some of the oligosaccharides recognized by P-selectin
      were either on enzyme-resistant poly-N-acetyllactosamine or on chains which lack 
      poly-N-acetyllactosamine. PNGaseF treatment did not affect the ability of PSGL-1 
      to bind to P-selectin, demonstrating that the oligosaccharides required for
      P-selectin recognition are O-linked. PSGL-1 also bound to E-selectin, but with at
      least 50-fold lower affinity than to P-selectin. These data suggest that PSGL-1
      from human neutrophils displays complex, sialylated, and fucosylated O-linked
      poly-N-acetyllactosamine that promote high affinity binding to P-selectin, but
      not to E-selectin.
FAU - Moore, K L
AU  - Moore KL
AD  - Department of Medicine, University of Oklahoma Health Sciences Center, Oklahoma
      City.
FAU - Eaton, S F
AU  - Eaton SF
FAU - Lyons, D E
AU  - Lyons DE
FAU - Lichenstein, H S
AU  - Lichenstein HS
FAU - Cummings, R D
AU  - Cummings RD
FAU - McEver, R P
AU  - McEver RP
LA  - eng
GR  - CA 37626/CA/NCI NIH HHS/United States
GR  - HL 45510/HL/NHLBI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, Non-P.H.S.
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Cell Adhesion Molecules)
RN  - 0 (E-Selectin)
RN  - 0 (Glycoproteins)
RN  - 0 (Immune Sera)
RN  - 0 (Oligodeoxyribonucleotides)
RN  - 0 (Oligosaccharides)
RN  - 0 (P-Selectin)
RN  - 0 (Peptides)
RN  - 0 (Platelet Membrane Glycoproteins)
RN  - 0 (Polysaccharides)
RN  - 0 (Sialic Acids)
RN  - 28RYY2IV3F (Fucose)
RN  - 82441-98-3 (poly-N-acetyllactosamine)
RN  - EC 3.2.1.- (Glycoside Hydrolases)
RN  - GZP2782OP0 (N-Acetylneuraminic Acid)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Base Sequence
MH  - CHO Cells
MH  - Carbohydrate Sequence
MH  - Cell Adhesion Molecules/*metabolism
MH  - Cricetinae
MH  - E-Selectin
MH  - Fucose/*metabolism
MH  - Glycoproteins/metabolism
MH  - Glycoside Hydrolases/metabolism
MH  - Humans
MH  - Immune Sera
MH  - Molecular Sequence Data
MH  - N-Acetylneuraminic Acid
MH  - Neutrophils/*metabolism
MH  - Oligodeoxyribonucleotides
MH  - Oligosaccharides/metabolism
MH  - P-Selectin
MH  - Peptides/immunology/metabolism
MH  - Platelet Membrane Glycoproteins/*metabolism
MH  - Polysaccharides/chemistry/*metabolism
MH  - Sialic Acids/*metabolism
EDAT- 1994/09/16 00:00
MHDA- 1994/09/16 00:01
CRDT- 1994/09/16 00:00
PHST- 1994/09/16 00:00 [pubmed]
PHST- 1994/09/16 00:01 [medline]
PHST- 1994/09/16 00:00 [entrez]
PST - ppublish
SO  - J Biol Chem. 1994 Sep 16;269(37):23318-27.

PMID- 7683697
OWN - NLM
STAT- MEDLINE
DCOM- 19930604
LR  - 20181113
IS  - 0021-9738 (Print)
IS  - 0021-9738 (Linking)
VI  - 91
IP  - 5
DP  - 1993 May
TI  - Persistent repression of a functional allele can be responsible for
      galactosyltransferase deficiency in Tn syndrome.
PG  - 2103-10
AB  - A human hematopoietic disorder designated as Tn syndrome or permanent mixed-field
      polyagglutinability has been ascribed to a stem cell mutation leading to a
      specific deficiency of UDP-Gal:GalNAc alpha 1-O-Ser/Thr beta 1-3
      galactosyltransferase (beta 3 Gal-T) activity in affected cells. To test for the 
      possibility that an allele of the beta 3Gal-T gene might be repressed instead of 
      mutated, we have investigated whether 5-azacytidine or sodium n-butyrate, both
      inducers of gene expression, would reactivate expression of beta 3Gal-T in cloned
      enzyme-deficient T cells derived from a patient affected by the Tn syndrome. Flow
      cytometry revealed that a single treatment induced de novo expression of the
      Thomsen-Friedenreich antigen (Gal beta 1-3GalNAc-R), the product of beta 3Gal-T
      activity. In addition, a sialylated epitope on CD43 (leukosialin), which is
      present on normal but not on beta 3Gal-T-deficient T cells, was also reexpressed.
      Although no beta 3Gal-T activity was detectable in untreated Tn syndrome T cells,
      after exposure to 5-azaC,beta 3Gal-T activity reached nearly normal values. Both 
      agents failed to reactivate beta 3Gal-T in Jurkat T leukemic cells, which also
      lack beta 3Gal-T activity. These data demonstrate that Tn syndrome T cells
      contain an intact beta 3Gal-T gene copy and that the enzyme deficiency in this
      patient is due to a persistent and complete but reversible repression of a
      functional allele. In contrast, the cause of beta 3Gal-T deficiency appears to be
      different in Jurkat T cells.
FAU - Thurnher, M
AU  - Thurnher M
AD  - Institute of Physiology, University of Zurich, Switzerland.
FAU - Rusconi, S
AU  - Rusconi S
FAU - Berger, E G
AU  - Berger EG
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - J Clin Invest
JT  - The Journal of clinical investigation
JID - 7802877
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Butyrates)
RN  - 0 (Tn antigen)
RN  - 107-92-6 (Butyric Acid)
RN  - EC 2.4.1.- (Galactosyltransferases)
RN  - EC 2.4.1.122 (glycoprotein-N-acetylgalactosamine 3-beta-galactosyltransferase)
RN  - M801H13NRU (Azacitidine)
SB  - AIM
SB  - IM
MH  - Alleles
MH  - Antigens, Tumor-Associated, Carbohydrate/genetics/*metabolism
MH  - Azacitidine/pharmacology
MH  - Butyrates/pharmacology
MH  - Butyric Acid
MH  - Carbohydrate Sequence
MH  - Clone Cells
MH  - Enzyme Repression
MH  - Galactosyltransferases/*deficiency/*genetics/metabolism
MH  - Hematologic Diseases/*enzymology/genetics
MH  - Humans
MH  - Kinetics
MH  - Molecular Sequence Data
MH  - Syndrome
MH  - T-Lymphocytes/drug effects/*enzymology/immunology
MH  - Tumor Cells, Cultured
PMC - PMC288210
EDAT- 1993/05/01 00:00
MHDA- 1993/05/01 00:01
CRDT- 1993/05/01 00:00
PHST- 1993/05/01 00:00 [pubmed]
PHST- 1993/05/01 00:01 [medline]
PHST- 1993/05/01 00:00 [entrez]
AID - 10.1172/JCI116434 [doi]
PST - ppublish
SO  - J Clin Invest. 1993 May;91(5):2103-10. doi: 10.1172/JCI116434.

PMID- 15168731
OWN - NLM
STAT- MEDLINE
DCOM- 20040629
LR  - 20181113
IS  - 0262-0898 (Print)
IS  - 0262-0898 (Linking)
VI  - 21
IP  - 2
DP  - 2004
TI  - Antigenic differences between metastatic cells in bone marrow and primary tumours
      and the anti-MUC1 humoral immune response induced in breast cancer patients.
PG  - 139-47
AB  - The dissemination of a malignant neoplasia is a complex process, which requires a
      set of molecules that remains unknown. It has been suggested that mucins and
      their carbohydrate-associated antigens may be implicated in tumour spreading
      which may be also influenced by an anti-MUC1 immune response. In this pilot
      study, we report the pattern of carbohydrate and peptidic MUC1-associated
      epitopes on carcinoma cells isolated from bone marrow (BM), taking into account
      primary tumour histopathologic features. We also bring information about the
      anti-MUC1 humoral response in these patients. Seventeen patients with invasive
      breast carcinoma were included. A sample of the primary tumour, a serum sample
      and a BM aspirate were obtained from each patient. Clinical features studied were
      tumour size, number of metastatic nodes, histological type and disease stage.
      Standard immunohistochemistry was performed with antigenic retrieval using
      different monoclonal antibodies (MAbs): anti carbohydrate antigens: Lewis x
      (KM380), sLewis x (KM93), Lewis y (C14) and Tn, anti-MUC1 peptide core MAbs:
      C595, HMFG2 and SM3, anti-cytokeratins, anti-protoncogenes ErbB2 and ErbB3 (IgG) 
      MAbs and also anti-CD34 and anti-CD45 MAbs. ELISA techniques were employed to
      study circulating MUC1 as well as free and complexed anti-MUC1 antibodies.
      Immunohistochemical results showed that carbohydrate antigenic expression
      increases in BM neoplastic cells compared to the original tumours. However, we
      were not able to demonstrate that a humoral immune response to MUC1 has been
      induced in these patients. Finally, the employed procedures allow the selective
      immortalisation of micrometastatic carcinoma cells since short-term cell lines
      were established.
FAU - Croce, M V
AU  - Croce MV
AD  - Centro de Investigaciones Inmunologicas Basicas y Aplicadas, Facultad de Ciencias
      Medicas, UNLP La Plata, Argentina.
FAU - Isla-Larrain, M
AU  - Isla-Larrain M
FAU - Tur, R
AU  - Tur R
FAU - Rabassa, M E
AU  - Rabassa ME
FAU - Segal-Eiras, A
AU  - Segal-Eiras A
LA  - eng
PT  - Comparative Study
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - Netherlands
TA  - Clin Exp Metastasis
JT  - Clinical & experimental metastasis
JID - 8409970
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antibodies, Neoplasm)
RN  - 0 (Antigens, Neoplasm)
RN  - 0 (Epitopes)
RN  - 0 (Mucin-1)
RN  - 0 (Neoplasm Proteins)
RN  - 0 (Oligosaccharides)
RN  - 0 (Peptides)
SB  - IM
MH  - Antibodies, Monoclonal/immunology
MH  - Antibodies, Neoplasm/biosynthesis/blood/*immunology
MH  - Antibody Specificity
MH  - Antigens, Neoplasm/biosynthesis/genetics/*immunology
MH  - Bone Marrow/*immunology
MH  - Breast Neoplasms/blood/*immunology/pathology
MH  - Carcinoma, Ductal/immunology/pathology
MH  - Carcinoma, Intraductal, Noninfiltrating/immunology/pathology
MH  - Carcinoma, Lobular/immunology/pathology
MH  - Carcinoma, Papillary/immunology/pathology
MH  - Cell Line, Tumor
MH  - Epitopes/immunology
MH  - Female
MH  - Gene Expression Regulation, Neoplastic
MH  - Humans
MH  - Mucin-1/*immunology
MH  - Neoplasm Proteins/immunology
MH  - Neoplastic Stem Cells/*immunology
MH  - Oligosaccharides/immunology
MH  - Peptides/immunology
MH  - Pilot Projects
EDAT- 2004/06/01 05:00
MHDA- 2004/06/30 05:00
CRDT- 2004/06/01 05:00
PHST- 2004/06/01 05:00 [pubmed]
PHST- 2004/06/30 05:00 [medline]
PHST- 2004/06/01 05:00 [entrez]
PST - ppublish
SO  - Clin Exp Metastasis. 2004;21(2):139-47.

PMID- 8623771
OWN - NLM
STAT- MEDLINE
DCOM- 19960620
LR  - 20190512
IS  - 0002-9173 (Print)
IS  - 0002-9173 (Linking)
VI  - 105
IP  - 5
DP  - 1996 May
TI  - Expression of mucin carbohydrate antigens (T, Tn and sialyl Tn) and MUC-1 gene
      product in intraductal papillary-mucinous neoplasm of the pancreas.
PG  - 613-20
AB  - Aberrant or incomplete glycosylation of mucins results in expression of T, Tn,
      and sialyl-Tn (STn) antigens in various malignant neoplasms. MUC-1 gene product
      (a mucin core protein of mammary type) is known to alter or overexpress in
      several malignant tumors. However, expression of these mucin-related antigens has
      rarely been examined in intraductal papillary-mucinous neoplasm (IPN) of the
      pancreas. The authors examined immunohistochemically the expression of these
      antigens and MUC-1 gene product in nine IPN. In normal pancreas (n = 5),
      pancreatic ducts did not express T, Tn, or STn antigens, but expressed MUC-1 gene
      product. Among the nine IPNs, two (22%) expressed T antigen, nine (100%)
      expressed Tn antigen, and seven (78%) expressed STn antigen. MUC-1 gene product
      was expressed in nine (100%) IPNs. In invasive ductal adenocarcinoma of the
      pancreas (n = 6), all cases showed strong expression of Tn and STn antigens and
      the MUC-1 gene product, but expressed no T antigen. The expression of these
      antigens and MUC-1 gene product was focal in IPN, whereas it was diffuse in
      invasive ductal adenocarcinoma of the pancreas. These data suggest that aberrant 
      or incomplete glycosylation occurs in epithelial mucins of IPN, that IPN is a
      borderline or low grade malignant neoplasm in terms of mucin-related antigen
      expression, and that mucin core protein (MUC-1 gene product) does not alter
      during pancreatic ductal carcinogenesis.
FAU - Terada, T
AU  - Terada T
AD  - Second Department of Pathology, Kanazawa University School of Medicine, Japan.
FAU - Nakanuma, Y
AU  - Nakanuma Y
LA  - eng
PT  - Journal Article
PL  - England
TA  - Am J Clin Pathol
JT  - American journal of clinical pathology
JID - 0370470
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Mucin-1)
RN  - 0 (Mucins)
RN  - 0 (Neoplasm Proteins)
SB  - AIM
SB  - IM
MH  - Adenocarcinoma, Papillary/genetics/metabolism/*pathology
MH  - Aged
MH  - Aged, 80 and over
MH  - Antigens, Tumor-Associated, Carbohydrate/*biosynthesis
MH  - Cystadenoma, Mucinous/genetics/metabolism/*pathology
MH  - Humans
MH  - Immunohistochemistry
MH  - Male
MH  - Middle Aged
MH  - Mucin-1/*biosynthesis
MH  - Mucins/*biosynthesis/genetics
MH  - Neoplasm Proteins/*biosynthesis
MH  - Pancreatic Neoplasms/genetics/metabolism/*pathology
EDAT- 1996/05/01 00:00
MHDA- 1996/05/01 00:01
CRDT- 1996/05/01 00:00
PHST- 1996/05/01 00:00 [pubmed]
PHST- 1996/05/01 00:01 [medline]
PHST- 1996/05/01 00:00 [entrez]
AID - 10.1093/ajcp/105.5.613 [doi]
PST - ppublish
SO  - Am J Clin Pathol. 1996 May;105(5):613-20. doi: 10.1093/ajcp/105.5.613.

PMID- 7850810
OWN - NLM
STAT- MEDLINE
DCOM- 19950314
LR  - 20131121
IS  - 0008-5472 (Print)
IS  - 0008-5472 (Linking)
VI  - 55
IP  - 4
DP  - 1995 Feb 15
TI  - Characterization of the major sialyl-Lex-positive mucins present in colon, colon 
      carcinoma, and sera of patients with colorectal cancer.
PG  - 928-33
AB  - The expression of the mucin-bound sialyl-Lewisx epitope is increased in the
      tissue of most colorectal carcinomas and in the sera of about 30% of tumor
      patients. In colon cancer, a portion of the sialyl-Lex groups detectable with the
      monoclonal antibody AM-3 is located on MUC1 (C. Hanski et al., Cancer Res., 53:
      4082-4088, 1993). In order to characterize the major colon carcinoma-associated
      sialyl-Lex-positive glycoprotein components, the tissue- and serum-derived
      antigens were investigated. The buoyant densities of the sialyl-Lewisx-positive
      antigens from tumor and normal colonic tissues and from sera of patients with
      colon carcinoma and healthy donors correspond to that of mucins (1.40 g/ml). The 
      sialyl-Lex-positive mucins purified from both tissues elute under nonreducing
      conditions in the void volume of a Sepharose CL-2B column, indicating a molecular
      mass more than 2 x 10(7) daltons. They yield in immunoblot after SDS gel
      electrophoresis under reducing conditions a main band at an apparent M(r)
      880,000. Radioactive labeling revealed that the band at M(r) 880,000 is the major
      protein component in sialyl-Lewisx-positive mucins both from tumor and normal
      colonic tissue. In sera of colon carcinoma patients, the sialyl-Lex moiety is
      also detectable mainly on a M(r) 880,000 glycoprotein band and, additionally, on 
      a M(r) 140,000 molecule as well as on alpha 1-acid glycoprotein. Sera from
      healthy donors exhibited only a sialyl-Lex-positive glycoprotein with the
      apparent M(r) 140,000. Sandwich ELISA as well as immunoblots of mucins purified
      from the colon carcinoma cell line LS174T indicated that the sialyl-Lex moiety
      migrating in the M(r) 880,000 band is located on MUC2 protein core. Together,
      these data suggest that sialyl-Lex antigen in colon, colon carcinoma, and the
      sera of patients with this tumor is located on the MUC2 molecule, consisting of
      several subunits with an apparent M(r) 880,000, linked via disulfide bridges. The
      increase of sialyl-Lex expression in colon carcinomas appears to be mainly due to
      a more frequent transfer of sialyl-Lex moieties onto the mucin core in tumor
      tissue.
FAU - Hanski, C
AU  - Hanski C
AD  - Klinikum Benjamin Franklin der Freien Universitat Berlin, Department of
      Gastroenterology, Germany.
FAU - Hanski, M L
AU  - Hanski ML
FAU - Zimmer, T
AU  - Zimmer T
FAU - Ogorek, D
AU  - Ogorek D
FAU - Devine, P
AU  - Devine P
FAU - Riecken, E O
AU  - Riecken EO
LA  - eng
PT  - Comparative Study
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Cancer Res
JT  - Cancer research
JID - 2984705R
RN  - 0
      (5-acetylneuraminyl-(2-3)-galactosyl-(1-4)-(fucopyranosyl-(1-3))-N-acetylglucosam
      ine)
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Mucins)
RN  - 0 (Oligosaccharides)
RN  - 368GB5141J (Sodium Dodecyl Sulfate)
SB  - IM
MH  - Antibodies, Monoclonal
MH  - Antigens, Tumor-Associated, Carbohydrate/*analysis/*blood/immunology
MH  - Chromatography
MH  - Colon/*chemistry/immunology
MH  - Colonic Neoplasms/*blood/*chemistry
MH  - Colorectal Neoplasms/*blood/*chemistry
MH  - Electrophoresis
MH  - Humans
MH  - Immunoblotting
MH  - Molecular Weight
MH  - Mucins/*analysis/*blood/immunology
MH  - Oligosaccharides/*analysis/*blood/immunology
MH  - Sodium Dodecyl Sulfate
EDAT- 1995/02/15 00:00
MHDA- 1995/02/15 00:01
CRDT- 1995/02/15 00:00
PHST- 1995/02/15 00:00 [pubmed]
PHST- 1995/02/15 00:01 [medline]
PHST- 1995/02/15 00:00 [entrez]
PST - ppublish
SO  - Cancer Res. 1995 Feb 15;55(4):928-33.

PMID- 15791836
OWN - NLM
STAT- MEDLINE
DCOM- 20060518
LR  - 20181113
IS  - 1672-0733 (Print)
IS  - 1672-0733 (Linking)
VI  - 24
IP  - 6
DP  - 2004
TI  - The comparative study on ultrastructure and immunohistochemistry in AFP negative 
      and positive hepatocellular carcinoma.
PG  - 547-9, 559
AB  - SUMMARY: To comparatively investigate ultrastructural characteristics and
      expressions of AFP (alpha-fetoprotein) and Tn (Thomsen-Friedenreich-related
      antigen) protein in AFP negative (AFP-) and AFP positive (AFP+) primary
      hepatocellular carcinoma. Fourty-three cases of AFP- and AFP+ hepatocellular
      carcinoma (HCC) tissues and five cases of normal liver tissues were divided into 
      three groups: control group (normal liver tissue, n=5); AFP+ HCC group (the serum
      AFP level was higher than 10 ng/ml, n = 22); AFP- HCC group (the serum AFP level 
      was lower than 10 ng/ml, n=21). The ultrastructural morphology was studied by
      transmission electron microscopy, the expressions of AFP and Tn protein were
      detected by immunohistochemistry and cell image analysis. 1. The
      immunohistochemical study showed that (1) the expression intensity and positive
      rate of Tn protein in AFP- HCC group were markedly higher than that in AFP+ HCC
      group (P<0.01); (2) The expression intensity of AFP in AFP- HCC group was lower
      than that in AFP+ HCC group (P<0.01). 2. The transmission electron microscopy
      demonstrated that some AFP- HCC cells linked closely with each other, others
      dispersed loosely just as cultured cells, the remarkable morphologic features in 
      AFP- HCC cells were simple organelles, but they were abundant in the free
      polyribosomes. In AFP+ HCC group, all the HCC cells linked closely together and
      were rich organelles in their cytoplasm, especially the rough endoplasmic
      reticula. In addition, mitochondria and Golgi complex were obviously observed.
      (1) The AFP and Tn protein had discrepancy distribution in AFP- and AFP+ HCC
      tissues, Tn protein may be one of the early diagnostic indicators in AFP- HCC;
      (2) The synthetic locations of the AFP and Tn protein were different in
      hepatocarcinoma cells by ultrastructural observation.
FAU - Zheng, Meirong
AU  - Zheng M
AD  - Department of Ultrastructural Pathology, Tongji Medical College, Huazhong
      University of Science and Technology, Wuhan 430030, China.
FAU - Ruan, Youbing
AU  - Ruan Y
FAU - Yang, Mulan
AU  - Yang M
FAU - Guan, Yang
AU  - Guan Y
FAU - Wu, Zhongbi
AU  - Wu Z
LA  - eng
PT  - Comparative Study
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - China
TA  - J Huazhong Univ Sci Technolog Med Sci
JT  - Journal of Huazhong University of Science and Technology. Medical sciences = Hua 
      zhong ke ji da xue xue bao. Yi xue Ying De wen ban = Huazhong keji daxue xuebao. 
      Yixue Yingdewen ban
JID - 101169627
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Biomarkers, Tumor)
RN  - 0 (Tn antigen)
RN  - 0 (alpha-Fetoproteins)
SB  - IM
MH  - Antigens, Tumor-Associated, Carbohydrate/*biosynthesis/genetics
MH  - *Biomarkers, Tumor
MH  - Carcinoma, Hepatocellular/metabolism/*ultrastructure
MH  - Female
MH  - Humans
MH  - Immunohistochemistry
MH  - Liver Neoplasms/metabolism/*ultrastructure
MH  - Male
MH  - Tumor Cells, Cultured
MH  - alpha-Fetoproteins/*biosynthesis/genetics
EDAT- 2005/03/29 09:00
MHDA- 2006/05/19 09:00
CRDT- 2005/03/29 09:00
PHST- 2005/03/29 09:00 [pubmed]
PHST- 2006/05/19 09:00 [medline]
PHST- 2005/03/29 09:00 [entrez]
PST - ppublish
SO  - J Huazhong Univ Sci Technolog Med Sci. 2004;24(6):547-9, 559.

PMID- 15033940
OWN - NLM
STAT- MEDLINE
DCOM- 20050331
LR  - 20171116
IS  - 0959-6658 (Print)
IS  - 0959-6658 (Linking)
VI  - 14
IP  - 5
DP  - 2004 May
TI  - Specificity of IgG and IgE antibodies against plant and insect glycoprotein
      glycans determined with artificial glycoforms of human transferrin.
PG  - 457-66
AB  - Cross-reactive carbohydrate determinants of plants are essentially a mixture of
      N-glycans containing beta1,2-xylose and core alpha1,3-fucose, the latter also
      found in insect glycoproteins. To determine the relative contributions of these
      two sugar residues to antibody binding, we prepared an array of glycomodified
      forms of human apo-transferrin. Using core-alpha1, 3-fucosyltransferase (EC
      2.4.1.214) and beta1,2-xylosyltransferase (EC 2.4.2.38) recombinantly expressed
      in Pichia pastoris and suitable glycosidases, glycoforms containing either only
      fucose (MMF), only xylose (MMX), both (MMXF), or neither (MM) linked to the
      common pentasaccharide core were generated. Additional glycoforms were obtained
      by enzymatic removal of the alpha1,3-linked mannosyl residue. These transferrin
      glycoforms served to define the binding specificity of antibodies in western
      blot, ELISA, and inhibition ELISA. Rabbit anti-horseradish peroxidase serum bound
      to both the fucosylated (MMF) and the xylosylated (MMX) glycoforms. Inhibition
      studies indicated two independent highly specific populations reacting with
      either of the two epitopes. In contrast, the monoclonal antibody YZ1/2.23 appears
      to recognize a larger structure including both the fucosyl and the xylosyl
      residue. The mannose-deficient glycoform was a poorer inhibitor for both
      antibodies. Terminal GlcNAc residues prevented antibody binding. Rabbit anti-bee 
      venom serum reacted with fucosylated forms (MMF and MMXF) only. Experiments with 
      sera from allergic patients suggest that glycomodified human transferrin,
      especially the MMXF glycoform, is a suitable reagent for the detection of
      antibodies against cross-reactive carbohydrate determinants. Within the panel
      studied, several sera contained high levels of fucose-reactive IgE but only a few
      sera showed any binding to MMX-transferrin.
FAU - Bencurova, Monika
AU  - Bencurova M
AD  - Glycobiology Division, Institute of Chemistry, University of Natural Resources
      and Applied Life Sciences (Universitat fur Bodenkultur), Muthgasse 18, A-1190,
      Vienna, Austria.
FAU - Hemmer, Wolfgang
AU  - Hemmer W
FAU - Focke-Tejkl, Margarete
AU  - Focke-Tejkl M
FAU - Wilson, Iain B H
AU  - Wilson IB
FAU - Altmann, Friedrich
AU  - Altmann F
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20040319
PL  - England
TA  - Glycobiology
JT  - Glycobiology
JID - 9104124
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Apoproteins)
RN  - 0 (Bee Venoms)
RN  - 0 (Epitopes)
RN  - 0 (Glycoproteins)
RN  - 0 (Immunoglobulin G)
RN  - 0 (Insect Proteins)
RN  - 0 (Plant Proteins)
RN  - 0 (Polysaccharides)
RN  - 0 (Transferrin)
RN  - 0 (apotransferrin)
RN  - 28RYY2IV3F (Fucose)
RN  - 37341-29-0 (Immunoglobulin E)
RN  - A1TA934AKO (Xylose)
SB  - IM
MH  - Animals
MH  - Antibodies, Monoclonal/immunology
MH  - Apoproteins/*immunology
MH  - Bee Venoms/immunology
MH  - Enzyme-Linked Immunosorbent Assay
MH  - Epitopes/immunology
MH  - Fucose/metabolism
MH  - Glycoproteins/*immunology
MH  - Humans
MH  - Immunoglobulin E/*immunology
MH  - Immunoglobulin G/*immunology
MH  - Insect Proteins/immunology
MH  - Pichia
MH  - Plant Proteins/immunology
MH  - Polysaccharides/*immunology
MH  - Rabbits
MH  - Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
MH  - Transferrin/*immunology
MH  - Xylose/metabolism
EDAT- 2004/03/23 05:00
MHDA- 2005/04/01 09:00
CRDT- 2004/03/23 05:00
PHST- 2004/03/23 05:00 [pubmed]
PHST- 2005/04/01 09:00 [medline]
PHST- 2004/03/23 05:00 [entrez]
AID - 10.1093/glycob/cwh058 [doi]
AID - cwh058 [pii]
PST - ppublish
SO  - Glycobiology. 2004 May;14(5):457-66. doi: 10.1093/glycob/cwh058. Epub 2004 Mar
      19.

PMID- 16824489
OWN - NLM
STAT- MEDLINE
DCOM- 20060913
LR  - 20061115
IS  - 0006-291X (Print)
IS  - 0006-291X (Linking)
VI  - 347
IP  - 1
DP  - 2006 Aug 18
TI  - Evidence that Agaricus bisporus agglutinin (ABA) has dual sugar-binding
      specificity.
PG  - 215-20
AB  - Agaricus bisporus agglutinin (ABA) is known as a useful lectin to detect
      T-antigen (Core1) disaccharide (Galbeta1-3GalNAcalpha) and related O-linked
      glycans. However, a recent X-ray crystallographic study revealed the presence of 
      another intrinsic sugar-binding site, i.e., for GlcNAc. To confirm this
      possibility, detailed analysis was performed using two advanced methods: lectin
      microarray and frontal affinity chromatography (FAC). In the lectin microarray,
      intense signals were observed on ABA spots for both N-glycanase-treated and
      O-glycanase/beta1-4galactosidase-treated Cy3-labeled asialofetuin. This indicates
      substantial affinity for both O-linked and agalactosylated (GlcNAc-exposed)
      N-linked glycans. A further approach by FAC using 20 pNP and 130
      PA-oligosaccharides demonstrated that ABA bound to Core1 (K(d) = 3.4 x 10(-6) M) 
      and Core2 (1.9 x 10(-5) M) but not to Core3 and Core6 O-linked glycans. It also
      showed substantial affinity to mono-, bi-, and tri-antennary agalactosylated
      complex-type N-linked glycans (K(d) > 1.8 x 10(-5) M). These results establish
      ABA as a lectin having dual sugar-binding sites with distinct specificity, i.e., 
      for Gal-exposed O-linked glycans and GlcNAc-exposed N-linked glycans.
FAU - Nakamura-Tsuruta, Sachiko
AU  - Nakamura-Tsuruta S
AD  - Glycostructure Analysis Team, Research Center for Glycoscience, National
      Institute of Advanced Industrial Science and Technology, AIST Tsukuba Central 2, 
      Ibaraki, Japan.
FAU - Kominami, Junko
AU  - Kominami J
FAU - Kuno, Atsushi
AU  - Kuno A
FAU - Hirabayashi, Jun
AU  - Hirabayashi J
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20060621
PL  - United States
TA  - Biochem Biophys Res Commun
JT  - Biochemical and biophysical research communications
JID - 0372516
RN  - 0 (Agaricus lectins)
RN  - 0 (Agglutinins)
RN  - 0 (Carbohydrates)
RN  - 0 (Lectins)
SB  - IM
MH  - Agglutinins/*chemistry
MH  - Binding Sites
MH  - Carbohydrates/*chemistry
MH  - Evidence-Based Medicine
MH  - Lectins/*chemistry
MH  - Protein Binding
MH  - *Protein Interaction Mapping
EDAT- 2006/07/11 09:00
MHDA- 2006/09/14 09:00
CRDT- 2006/07/11 09:00
PHST- 2006/06/12 00:00 [received]
PHST- 2006/06/13 00:00 [accepted]
PHST- 2006/07/11 09:00 [pubmed]
PHST- 2006/09/14 09:00 [medline]
PHST- 2006/07/11 09:00 [entrez]
AID - S0006-291X(06)01370-2 [pii]
AID - 10.1016/j.bbrc.2006.06.073 [doi]
PST - ppublish
SO  - Biochem Biophys Res Commun. 2006 Aug 18;347(1):215-20. doi:
      10.1016/j.bbrc.2006.06.073. Epub 2006 Jun 21.

PMID- 19261632
OWN - NLM
STAT- MEDLINE
DCOM- 20090505
LR  - 20151119
IS  - 0300-9858 (Print)
IS  - 0300-9858 (Linking)
VI  - 46
IP  - 2
DP  - 2009 Mar
TI  - Tumor-associated carbohydrate antigens: Sialyl Lea and T/Tn antigens in canine
      mammary tumors.
PG  - 222-6
LID - 10.1354/vp.46-2-222 [doi]
AB  - Twenty-eight canine mammary tubulopapillary carcinomas and 14 simple adenomas
      were studied by immunohistochemistry for the expressions of the tumor-associated 
      carbohydrate antigens. Sialyl Le(a) was detected in 71.42% of the malignant and
      92.84% of the benign tumors. Staining with anti-T and anti-Tn monoclonal
      antibodies revealed that 85.70% of the tubulopapillary carcinomas expressed T and
      Tn antigens. In contrast, 50% of the adenomas did not express T antigen, and
      42.85% of them were only weakly stained for this carbohydrate structure. In the
      case of Tn antigen, the majority (57.14%) of samples was weakly stained, and no
      binding was observed in 35.71% of the analyzed specimens. Comparison of average
      values of reaction intensity (IRS) scale for malignant versus benign tumors by
      the Mann-Whitney U-test revealed a significant relationship between T and Tn
      antigens expression and type (malignant vs. benign) mammary tumors. Based on the 
      results obtained, it is suggested that each of the studied antigens can be
      treated as a tumor-associated antigen of canine mammary tumors. However, only the
      T and Tn antigens seem to be associated with malignant transformation of mammary 
      gland cells and to be of potential value as diagnostic markers.
FAU - Nowak, M
AU  - Nowak M
AD  - Department of Biochemistry, Pharmacology and Toxicology, Faculty of Veterinary
      Medicine, University of Environmental and Life Sciences, ul. Norwida 31, 50-357
      Wroclaw, Poland.
FAU - Madej, J
AU  - Madej J
FAU - Dziegiel, P
AU  - Dziegiel P
FAU - Lopuszynski, W
AU  - Lopuszynski W
FAU - Rodo, A
AU  - Rodo A
FAU - Ugorski, M
AU  - Ugorski M
LA  - eng
PT  - Journal Article
PL  - United States
TA  - Vet Pathol
JT  - Veterinary pathology
JID - 0312020
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Biomarkers, Tumor)
RN  - 0 (Gangliosides)
RN  - 0 (sialosyl-Tn antigen)
RN  - 91847-18-6 (sialyl Le(a) ganglioside)
SB  - IM
MH  - Adenoma/metabolism/veterinary
MH  - Animals
MH  - Antigens, Tumor-Associated, Carbohydrate/*metabolism
MH  - Biomarkers, Tumor/metabolism
MH  - Carcinoma/classification/metabolism/veterinary
MH  - Dog Diseases/*metabolism/pathology
MH  - Dogs
MH  - Female
MH  - Gangliosides/*metabolism
MH  - Mammary Glands, Animal/cytology/metabolism
MH  - Mammary Neoplasms, Animal/*metabolism/pathology
EDAT- 2009/03/06 09:00
MHDA- 2009/05/06 09:00
CRDT- 2009/03/06 09:00
PHST- 2009/03/06 09:00 [entrez]
PHST- 2009/03/06 09:00 [pubmed]
PHST- 2009/05/06 09:00 [medline]
AID - 46/2/222 [pii]
AID - 10.1354/vp.46-2-222 [doi]
PST - ppublish
SO  - Vet Pathol. 2009 Mar;46(2):222-6. doi: 10.1354/vp.46-2-222.

PMID- 8609376
OWN - NLM
STAT- MEDLINE
DCOM- 19960529
LR  - 20151119
IS  - 0022-1554 (Print)
IS  - 0022-1554 (Linking)
VI  - 44
IP  - 2
DP  - 1996 Feb
TI  - Concurrent immunohistochemical staining of tumor-infiltrating lymphocytes and
      carcinoma-associated T (Thomsen-Friedenreich)/Tn antigens in human breast
      carcinoma.
PG  - 187-91
AB  - The composition of tumor-infiltrating lymphocytes (TIL) often reflects the host's
      immune response to the tumor. To study the relationship of TIL and
      carcinoma-associated T/Tn antigens in breast carcinoma, a straightforward
      concurrent immunoenzyme staining procedure was developed. Fresh tissue was
      directly fixed in a zinc-based fixative to preserve lymphocyte markers and then
      routinely embedded in paraffin. The TIL subtypes in the sections were identified 
      in the first immunostaining cycle by reaction with a monoclonal antibody (MAb) to
      lymphocyte markers CD3, CD4, CD8, CD19, or CD56, followed by a modified
      avidin-biotin procedure and diaminobenzidine tetrahydrochloride-H2O2 for color
      development. This was followed by paraformaldehyde fixation to block antibody
      crossreactivity. The T and Tn antigens on carcinoma cells were then demonstrated 
      in a second staining cycle by reaction with an MAb against T or Tn antigen,
      followed by an indirect immunoalkaline phosphatase procedure and corresponding
      substrate systems for color development. The distinguishable brown color for TIL 
      and blue or red color for T or Tn antigen enabled us to identify the TIL subsets 
      and to describe their relations with T/Tn antigen expression in situ. This
      approach may contribute to better understanding of the patients' immune defenses 
      against their tumor and aid in prognostication.
FAU - Wang, B L
AU  - Wang BL
AD  - Heather M. Bligh Cancer Research Laboratories, Chicago Medical School, IL 60064, 
      USA.
FAU - Springer, G F
AU  - Springer GF
FAU - Kaufman, M W
AU  - Kaufman MW
LA  - eng
GR  - CA 22540/CA/NCI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - J Histochem Cytochem
JT  - The journal of histochemistry and cytochemistry : official journal of the
      Histochemistry Society
JID - 9815334
RN  - 0 (Antigens, CD)
RN  - 0 (Antigens, Tumor-Associated, Carbohydrate)
RN  - 0 (Biomarkers)
RN  - 0 (Tn antigen)
RN  - 3554-90-3 (Thomsen-Friedenreich antigen)
SB  - IM
MH  - Antigens, CD/classification/immunology
MH  - Antigens, Tumor-Associated, Carbohydrate/*immunology
MH  - Biomarkers
MH  - Breast Neoplasms/*immunology/pathology
MH  - Carbohydrate Sequence
MH  - Female
MH  - Humans
MH  - Immunoenzyme Techniques
MH  - Lymphocytes, Tumor-Infiltrating/*immunology
MH  - Molecular Sequence Data
EDAT- 1996/02/01 00:00
MHDA- 1996/02/01 00:01
CRDT- 1996/02/01 00:00
PHST- 1996/02/01 00:00 [pubmed]
PHST- 1996/02/01 00:01 [medline]
PHST- 1996/02/01 00:00 [entrez]
PST - ppublish
SO  - J Histochem Cytochem. 1996 Feb;44(2):187-91.