PMID- 2136357
OWN - NLM
STAT- MEDLINE
DCOM- 19920911
LR - 20181113
IS - 0282-0080 (Print)
IS - 0282-0080 (Linking)
VI - 7
IP - 6
DP - 1990
TI - Pregnancy-associated changes in oligomannose oligosaccharides of human and bovine
uromodulin (Tamm-Horsfall glycoprotein).
PG - 609-24
AB - The urinary glycoprotein uromodulin (Tamm-Horsfall glycoprotein) exhibits a
pregnancy-associated ability to inhibit antigen-specific T cell proliferation,
and the activity is associated with a carbohydrate moiety [Muchmore and Decker
(1985) Science 229:479-81; Hession et al., (1987) Science 237:1479-84; Muchmore,
Shifrin and Decker (1987) J Immunol 138:2547-53]. We report here that the
Man6(7)GlcNAc2-R glycopeptides derived from uromodulin inhibit antigen-specific T
cell proliferation by 50% at 0.2-2 microM, and further studies, reported
elsewhere, confirm that oligomannose glycopeptides from other sources are also
inhibitory, with Man9GlcNAc2-R the most inhibitory of those tested [Muchmore et
al., J Leukocyte Biol (in press)]. In this work, we have extended the observation
of pregnancy-associated inhibitory activity to a second species, and have
compared the oligomannose profile of Tamm-Horsfall glycoprotein (nonpregnant)
with that of uromodulin (pregnant) derived from both human and bovine sources.
Surprisingly, there was a pregnancy-associated decrease in the total content of
oligomannose chains due predominantly to a reduction in Man5GlcNAc2-R and
Man6GlcNAc2-R. Man7GlcNAc2-R, which did not decrease with pregnancy, comprised a
significantly greater proportion of the total oligomannose chains in pregnant vs.
nonpregnant samples from both species (human; 34.6% vs. 25.9%: bovine; 14.4% vs.
7.2%).
FAU - Smagula, R M
AU - Smagula RM
AD - Department of Biochemistry, University of Maine, Orono 04469.
FAU - Van Halbeek, H
AU - Van Halbeek H
FAU - Decker, J M
AU - Decker JM
FAU - Muchmore, A V
AU - Muchmore AV
FAU - Moody, C E
AU - Moody CE
FAU - Sherblom, A P
AU - Sherblom AP
LA - eng
GR - P41-RR-05351/RR/NCRR NIH HHS/United States
GR - S07 RR07161/RR/NCRR 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 - Glycoconj J
JT - Glycoconjugate journal
JID - 8603310
RN - 0 (Mucoproteins)
RN - 0 (Oligosaccharides)
RN - 0 (Pregnancy Proteins)
RN - 0 (UMOD protein, human)
RN - 0 (Umod protein, mouse)
RN - 0 (Uromodulin)
RN - PHA4727WTP (Mannose)
SB - IM
MH - Animals
MH - Carbohydrate Sequence
MH - Cattle
MH - Cell Division
MH - Chromatography, Gel
MH - Chromatography, High Pressure Liquid
MH - Electrophoresis, Polyacrylamide Gel
MH - Female
MH - Humans
MH - Mannose/*metabolism
MH - Mice
MH - Molecular Sequence Data
MH - Mucoproteins/*metabolism/urine
MH - Oligosaccharides/*metabolism
MH - Pregnancy
MH - Pregnancy Proteins/*metabolism
MH - T-Lymphocytes/immunology
MH - Uromodulin
EDAT- 1990/01/01 00:00
MHDA- 1990/01/01 00:01
CRDT- 1990/01/01 00:00
PHST- 1990/01/01 00:00 [pubmed]
PHST- 1990/01/01 00:01 [medline]
PHST- 1990/01/01 00:00 [entrez]
PST - ppublish
SO - Glycoconj J. 1990;7(6):609-24.
PMID- 1991473
OWN - NLM
STAT- MEDLINE
DCOM- 19910313
LR - 20161017
IS - 0014-2956 (Print)
IS - 0014-2956 (Linking)
VI - 195
IP - 1
DP - 1991 Jan 1
TI - NMR investigations of the N-linked oligosaccharides at individual glycosylation
sites of human lutropin.
PG - 257-68
AB - Human lutropin or luteinizing hormone (hLH) is a heterodimeric glycoprotein,
composed of two subunits. hLH alpha (N-glycosylated at Asn52 and Asn78) and hLH
beta (N-glycosylated at Asn30). The sugar chains were liberated by hydrazinolysis
from intact hLH beta and from glycopeptides obtained after tryptic digestion of
hLH alpha, subsequently reduced and fractionated as alditols by anion-exchange
and ion-suppression amine-adsorption HPLC and identified mainly by
one-dimensional (1D) and two-dimensional (2D) 1H-NMR spectroscopy. The results
indicate predominantly diantennary. N-acetyllactosamine-type structures at all
three glycosylation sites. The oligosaccharides attached to Asn52 (hLH alpha) and
Asn30 (hLH beta) show a remarkably similar pattern, with mainly chain-terminating
4-sulphated 2-deoxy-2-N-acetylamino-D-galactose (GalNAc) and a
sulphated/sialylated structure as the major single component. However, virtually
all N-glycans on the beta subunit bear a fucose residue alpha 1-6-linked to the
proximal GlcNAc, whereas those at Asn52 (and Asn78) of the alpha subunit are
predominantly non-fucosylated. The oligosaccharides at Asn78 (hLH alpha) are
sialylated rather than sulphated and contain the unique sequence NeuAc alpha 2-6
GalNAc beta 1-4GlcNAc beta 1-2 Man alpha 1-3 as part of the majority of mono- and
disialylated compounds. The major single constituent at Asn78 has the following
structure: [formula, see text]
FAU - Weisshaar, G
AU - Weisshaar G
AD - Department of Biochemistry, University of Auckland, New Zealand.
FAU - Hiyama, J
AU - Hiyama J
FAU - Renwick, A G
AU - Renwick AG
FAU - Nimtz, M
AU - Nimtz M
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 - 7006-34-0 (Asparagine)
RN - 9002-67-9 (Luteinizing Hormone)
SB - IM
MH - Amino Acid Sequence
MH - Asparagine
MH - Carbohydrate Conformation
MH - Carbohydrate Sequence
MH - Chromatography, High Pressure Liquid
MH - Glycosylation
MH - Humans
MH - Luteinizing Hormone/*chemistry
MH - Magnetic Resonance Spectroscopy/methods
MH - Molecular Sequence Data
MH - Oligosaccharides/*chemistry/isolation & purification
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 - Eur J Biochem. 1991 Jan 1;195(1):257-68.
PMID- 3514617
OWN - NLM
STAT- MEDLINE
DCOM- 19860522
LR - 20131121
IS - 0021-9258 (Print)
IS - 0021-9258 (Linking)
VI - 261
IP - 12
DP - 1986 Apr 25
TI - Membrane glycophorins in Sta blood group erythrocytes.
PG - 5544-52
AB - Structural and immunochemical studies of glycophorins isolated from erythrocytes
of an individual homozygous for the M Sta blood group phenotype are described.
Reactivities with specific monoclonal antibodies indicated that two major M and N
glycophorins were present. The M and N Sta glycophorins were resolved by Lens
culinaris lectin affinity chromatography. The N species was not held on the
lectin but the M species, like control alpha glycophorins, was retained and could
be eluted with alpha-methylmannoside. The two proteins were present in almost
equimolar amounts. Studies of the CNBr fragments provided evidence that the
structure of M Sta glycophorin is the same as that of the usual M alpha
glycophorin but that the N Sta glycophorin is a variant. The amino-terminal
octapeptides of the M and N species were similar in amino acid and carbohydrate
composition to those isolated, respectively, from M and N alpha glycophorins. The
studies focused on CNBr glycopeptide B that, in control alpha glycophorins,
extends from amino acid residues 9 to 81. The fragment from the M species
exhibited properties identical to those of the corresponding fragment of control
alpha glycophorins in terms of size, chromatographic behavior, amino acid and
carbohydrate contents and compositions, the presence of O-glycosidically linked
saccharides and a single Asn-linked carbohydrate unit. The structures of the
O-linked units were inferred experimentally to be NeuAc(alpha 2,3)Gal-(beta
1,3)GalNAc and NeuAc(alpha 2,3)Gal(beta 1,3) [NeuAc(alpha 2,6)]GalNAc, present in
a ratio similar to that found in controls; and the Asn-linked unit also appeared
to be as in the control. The tryptic glycopeptide pattern of the M Sta
glycophorin CNBr fragment B was identical to the pattern of the corresponding
control fragment, and the composition of the tryptic peptides suggested sequence
identity with the control fragment. In contrast, the N Sta glycophorin yielded
two CNBr glycopeptides B; both contained fewer amino acid residues and virtually
lacked Man and GlcNAc, indicating the absence of the Asn-linked carbohydrate. The
much decreased levels of these carbohydrates in the intact N protein,
corroborated the latter finding. The O-glycosidic saccharides appeared similar to
those found in control alpha glycophorins. However, the tryptic glycopeptide
pattern of the variant differed from control M or N alpha glycophorins,
suggesting a deletion of a large segment of the molecule near residues 40-61
and/or a substitution of methionine for a residue upstream from residue
40.(ABSTRACT TRUNCATED AT 400 WORDS)
FAU - Blumenfeld, O O
AU - Blumenfeld OO
FAU - Adamany, A M
AU - Adamany AM
FAU - Kikuchi, M
AU - Kikuchi M
FAU - Sabo, B
AU - Sabo B
FAU - McCreary, J
AU - McCreary J
LA - eng
GR - 16389/PHS 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 (Amino Acids)
RN - 0 (Antibodies, Monoclonal)
RN - 0 (Carbohydrates)
RN - 0 (Glycophorin)
RN - 0 (MNSs Blood-Group System)
RN - 0 (Oligosaccharides)
RN - 0 (Peptide Fragments)
RN - 0 (Sialoglycoproteins)
RN - OS382OHJ8P (Cyanogen Bromide)
SB - IM
MH - Amino Acids/analysis
MH - Antibodies, Monoclonal
MH - Carbohydrates/analysis
MH - Chromatography, Affinity
MH - Chromatography, Gel
MH - Cyanogen Bromide/pharmacology
MH - Electrophoresis, Polyacrylamide Gel
MH - Erythrocyte Membrane/*analysis
MH - Glycophorin/*analysis
MH - Homozygote
MH - Humans
MH - Immunosorbent Techniques
MH - *MNSs Blood-Group System
MH - Oligosaccharides/analysis
MH - Peptide Fragments/analysis
MH - Phenotype
MH - Sialoglycoproteins/*analysis
EDAT- 1986/04/25 00:00
MHDA- 1986/04/25 00:01
CRDT- 1986/04/25 00:00
PHST- 1986/04/25 00:00 [pubmed]
PHST- 1986/04/25 00:01 [medline]
PHST- 1986/04/25 00:00 [entrez]
PST - ppublish
SO - J Biol Chem. 1986 Apr 25;261(12):5544-52.
PMID- 1388166
OWN - NLM
STAT- MEDLINE
DCOM- 19921022
LR - 20131121
IS - 0021-9258 (Print)
IS - 0021-9258 (Linking)
VI - 267
IP - 27
DP - 1992 Sep 25
TI - The asparagine-linked oligosaccharides on tissue factor pathway inhibitor
terminate with SO4-4GalNAc beta 1, 4GlcNAc beta 1,2 Mana alpha.
PG - 19140-6
AB - Tissue factor pathway inhibitor (TFPI) produced by endothelial cells contains
sulfated Asn-linked oligosaccharides. We have determined that greater than 70% of
the oligosaccharides on recombinant TFPI expressed in 293 cells terminate with
the sequence SO4-4GalNAc beta 1, 4GlcNAc beta 1, 2Man alpha. Oligosaccharides
terminating with this sequence have previously been described on lutropin,
thyrotropin, and pro-opiomelanocortin: glycoproteins synthesized in the anterior
pituitary. A GalNAc-transferase that recognizes the tripeptide motif
Pro-Xaa-Arg/Lys 6-9 residues N-terminal to Asn glycosylation sites accounts for
the specific addition of GalNAc to the oligosaccharide acceptor on these
glycoproteins, whereas a GalNAc beta 1,4GlcNAc beta 1, 2Man
alpha-4-sulfotransferase accounts for the addition of sulfate. The sulfated
oligosaccharides present on these hormones are responsible for their rapid
clearance from plasma by a receptor in hepatic reticuloendothelial cells. GalNAc-
and sulfotransferase activities with the same properties as those expressed in
the pituitary are detected at high levels in 293 cells and at lower levels in
endothelial cells. Chinese hamster ovary (CHO) cells do not contain detectable
levels of either transferase and rTFPI expressed in CHO cells does not contain
sulfated Asn-linked oligosaccharides. TFPI contains the sequence Pro-Phe-Lys, 9
residues N-terminal to the glycosylation site at position 228; this tripeptide
may act as the recognition sequence for the GalNAc-transferase. rTFPI produced by
293 cells, but not that produced by CHO cells, is bound by the receptor on
hepatic reticuloendothelial cells suggesting the sulfated structures play a role
in the biologic behavior of TFPI.
FAU - Smith, P L
AU - Smith PL
AD - Department of Pathology, Washington University School of Medicine, St. Louis,
Missouri.
FAU - Skelton, T P
AU - Skelton TP
FAU - Fiete, D
AU - Fiete D
FAU - Dharmesh, S M
AU - Dharmesh SM
FAU - Beranek, M C
AU - Beranek MC
FAU - MacPhail, L
AU - MacPhail L
FAU - Broze, G J Jr
AU - Broze GJ Jr
FAU - Baenziger, J U
AU - Baenziger JU
LA - eng
GR - R37-CA21923/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 (Acetates)
RN - 0 (Lipoproteins)
RN - 0 (Oligosaccharides)
RN - 0 (Recombinant Proteins)
RN - 0 (lipoprotein-associated coagulation inhibitor)
RN - 7006-34-0 (Asparagine)
RN - EC 2.4.1.- (Galactosyltransferases)
RN - EC 2.4.1.- (N-Acetylgalactosaminyltransferases)
RN - EC 2.4.1.- (glycoprotein hormone-specific N-acetylgalactosamine transferase)
RN - EC 2.8.2.- (CHST9 protein, human)
RN - EC 2.8.2.- (N-acetylgalactosamine-4-sulfotransferase)
RN - EC 2.8.2.- (Sulfotransferases)
RN - EC 3.2.1.52 (beta-N-Acetylhexosaminidases)
RN - Q40Q9N063P (Acetic Acid)
SB - IM
MH - Acetates/chemistry
MH - Acetic Acid
MH - Animals
MH - Asparagine/chemistry
MH - CHO Cells
MH - Carbohydrate Sequence
MH - Cricetinae
MH - Endothelium, Vascular/metabolism
MH - Galactosyltransferases/metabolism
MH - Humans
MH - Lipoproteins/*chemistry/metabolism
MH - Metabolic Clearance Rate
MH - Molecular Sequence Data
MH - N-Acetylgalactosaminyltransferases/metabolism
MH - Oligosaccharides/chemistry/metabolism
MH - Recombinant Proteins/chemistry/metabolism
MH - Sulfotransferases/metabolism
MH - beta-N-Acetylhexosaminidases/metabolism
EDAT- 1992/10/05 19:15
MHDA- 2001/03/28 10:01
CRDT- 1992/10/05 19:15
PHST- 1992/10/05 19:15 [pubmed]
PHST- 2001/03/28 10:01 [medline]
PHST- 1992/10/05 19:15 [entrez]
PST - ppublish
SO - J Biol Chem. 1992 Sep 25;267(27):19140-6.
PMID- 2226797
OWN - NLM
STAT- MEDLINE
DCOM- 19901204
LR - 20131121
IS - 0014-5793 (Print)
IS - 0014-5793 (Linking)
VI - 271
IP - 1-2
DP - 1990 Oct 1
TI - Carbohydrate structures of a human tissue plasminogen activator variant expressed
in recombinant Chinese hamster ovary cells.
PG - 14-8
AB - The carbohydrate structures of a genetically engineered human tissue plasminogen
activator variant bearing a single N-glycosylation site at Asn 448 are reported.
After isolation of the tryptic glycopeptide and liberation of the N-linked
carbohydrates by polypeptide:N-glycosidase F, 6 major oligosaccharide fractions
were separated by HPLC on NH2-bonded phase. Their structures were determined by
compositional and methylation analyses combined with fast atom bombardment mass
spectrometry. Seventy percent of the carbohydrates were of the biantennary
complex type with fucose at the proximal GlcNAc and zero, one or two alpha 2-3
linked NeuAc. The remainder were triantennary structures with one, two or three
NeuAc.
FAU - Nimtz, M
AU - Nimtz M
AD - Department of Cell Biology and Genetics, GBF-Gesellschaft fur Biotechnologische
Forschung mbH, Braunschweig, FRG.
FAU - Noll, G
AU - Noll G
FAU - Paques, E P
AU - Paques EP
FAU - Conradt, H S
AU - Conradt HS
LA - eng
PT - Journal Article
PL - England
TA - FEBS Lett
JT - FEBS letters
JID - 0155157
RN - 0 (Glycoproteins)
RN - 0 (Oligosaccharides)
RN - 0 (Recombinant Proteins)
RN - 0RH81L854J (Glutamine)
RN - 7006-34-0 (Asparagine)
RN - EC 3.4.21.- (Plasminogen Activators)
SB - IM
MH - Animals
MH - Asparagine/genetics
MH - Carbohydrate Conformation
MH - Carbohydrate Sequence
MH - Cell Line
MH - Clone Cells
MH - Cricetinae
MH - Cricetulus
MH - Genetic Variation
MH - Glutamine/genetics
MH - Glycoproteins/biosynthesis/*chemistry/genetics
MH - Glycosylation
MH - Humans
MH - Methylation
MH - Molecular Sequence Data
MH - Oligosaccharides/*chemistry
MH - Plasminogen Activators/biosynthesis/*chemistry/genetics
MH - Recombinant Proteins
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 - 0014-5793(90)80361-L [pii]
PST - ppublish
SO - FEBS Lett. 1990 Oct 1;271(1-2):14-8.
PMID- 10766826
OWN - NLM
STAT- MEDLINE
DCOM- 20000510
LR - 20131121
IS - 0021-9258 (Print)
IS - 0021-9258 (Linking)
VI - 275
IP - 16
DP - 2000 Apr 21
TI - X-ray crystal structure and characterization of halide-binding sites of human
myeloperoxidase at 1.8 A resolution.
PG - 11964-71
AB - The x-ray crystal structure of human myeloperoxidase has been extended to 1.8 A
resolution, using x-ray data recorded at -180 degrees C (r = 0.197, free r =
0.239). Results confirm that the heme is covalently attached to the protein via
two ester linkages between the carboxyl groups of Glu(242) and Asp(94) and
modified methyl groups on pyrrole rings A and C of the heme as well as a
sulfonium ion linkage between the sulfur atom of Met(243) and the beta-carbon of
the vinyl group on pyrrole ring A. In the native enzyme a bound chloride ion has
been identified at the amino terminus of the helix containing the proximal
His(336). Determination of the x-ray crystal structure of a
myeloperoxidase-bromide complex (r = 0.243, free r = 0.296) has shown that this
chloride ion can be replaced by bromide. Bromide is also seen to bind, at partial
occupancy, in the distal heme cavity, in close proximity to the distal His(95),
where it replaces the water molecule hydrogen bonded to Gln(91). The
bromide-binding site in the distal cavity appears to be the halide-binding site
responsible for shifts in the Soret band of the absorption spectrum of
myeloperoxidase. It is proposed that halide binding to this site inhibits the
enzyme by effectively competing with H(2)O(2) for access to the distal histidine,
whereas in compound I, the same site may be the halide substrate-binding site.
FAU - Fiedler, T J
AU - Fiedler TJ
AD - Department of Biochemistry and Molecular Biology, University of Miami Medical
School, Miami, Florida 33136, USA.
FAU - Davey, C A
AU - Davey CA
FAU - Fenna, R E
AU - Fenna RE
LA - eng
SI - PDB/1CXP
GR - GM 49149/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 (Bromides)
RN - 42VZT0U6YR (Heme)
RN - EC 1.11.1.7 (Peroxidase)
SB - IM
MH - Binding Sites
MH - Bromides/*metabolism
MH - Crystallography, X-Ray
MH - Dimerization
MH - Heme/analysis
MH - Humans
MH - Hydrogen Bonding
MH - Models, Chemical
MH - Models, Molecular
MH - Molecular Sequence Data
MH - Peroxidase/*chemistry
MH - Protein Conformation
EDAT- 2000/04/15 09:00
MHDA- 2000/05/16 09:00
CRDT- 2000/04/15 09:00
PHST- 2000/04/15 09:00 [pubmed]
PHST- 2000/05/16 09:00 [medline]
PHST- 2000/04/15 09:00 [entrez]
PST - ppublish
SO - J Biol Chem. 2000 Apr 21;275(16):11964-71.
PMID- 8174273
OWN - NLM
STAT- MEDLINE
DCOM- 19940607
LR - 20171128
IS - 0009-8981 (Print)
IS - 0009-8981 (Linking)
VI - 224
IP - 1
DP - 1994 Jan 14
TI - Alteration of asparagine-linked glycosylation in serum transferrin of patients
with hepatocellular carcinoma.
PG - 1-8
AB - The asparagine-linked sugar chains in serum transferrin purified from patients
with hepatocellular carcinoma (n = 13), healthy individuals (n = 5) and patients
with liver cirrhosis (n = 6) were compared. Sugar chains released with
N-glycanase from desialylated and pepsin-digested transferrin were derivatized by
reductive pyridylamination. Analysis of the sugar chains by high performance
liquid chromatography in combination with exoglycosidase digestion revealed an
increase of a biantennary complex-type sugar chain with a fucosylated trimannosyl
core; 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 in 7 of 13 cancer
patients and an increase of a sugar chain with a fucosylated trimannosyl core and
bisecting N-acetylglucosamine; 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 in one of the 13 cancer patients. Further, the
fucosylated alteration of the sugar chain was detected also in alpha
1-antitrypsin, hemopexin, alpha 1-acid glycoprotein and alpha 2-HS glycoprotein
from one of the patients with increased fucosylated transferrin.
FAU - Matsumoto, K
AU - Matsumoto K
AD - School of Pharmaceutical Sciences, Toho University, Chiba, Japan.
FAU - Maeda, Y
AU - Maeda Y
FAU - Kato, S
AU - Kato S
FAU - Yuki, H
AU - Yuki H
LA - eng
PT - Journal Article
PL - Netherlands
TA - Clin Chim Acta
JT - Clinica chimica acta; international journal of clinical chemistry
JID - 1302422
RN - 0 (Biomarkers, Tumor)
RN - 0 (Glycoproteins)
RN - 0 (Oligosaccharides)
RN - 0 (Transferrin)
RN - 7006-34-0 (Asparagine)
RN - EC 3.2.1.- (Glycoside Hydrolases)
RN - IY9XDZ35W2 (Glucose)
SB - IM
MH - Asparagine/*metabolism
MH - Biomarkers, Tumor
MH - Carbohydrate Sequence
MH - Carcinoma, Hepatocellular/*blood
MH - Chromatography, High Pressure Liquid
MH - Glucose/*metabolism
MH - Glycoproteins/analysis/metabolism
MH - Glycoside Hydrolases/chemistry
MH - Humans
MH - Hydrolysis
MH - Liver Cirrhosis/blood
MH - Liver Neoplasms/*blood
MH - Molecular Sequence Data
MH - Oligosaccharides
MH - Transferrin/*metabolism
EDAT- 1994/01/14 00:00
MHDA- 1994/01/14 00:01
CRDT- 1994/01/14 00:00
PHST- 1994/01/14 00:00 [pubmed]
PHST- 1994/01/14 00:01 [medline]
PHST- 1994/01/14 00:00 [entrez]
AID - 0009-8981(94)90115-5 [pii]
PST - ppublish
SO - Clin Chim Acta. 1994 Jan 14;224(1):1-8.
PMID- 1899031
OWN - NLM
STAT- MEDLINE
DCOM- 19910227
LR - 20071114
IS - 0006-2960 (Print)
IS - 0006-2960 (Linking)
VI - 30
IP - 3
DP - 1991 Jan 22
TI - Oligosaccharide structures present on asparagine-289 of recombinant human
plasminogen expressed in a Chinese hamster ovary cell line.
PG - 625-33
AB - The oligosaccharide structures linked to Asn289 of a recombinant (r) variant
(R561S) human plasminogen (HPg) expressed in Chinese hamster ovary (CHO) cells,
after transfection of these cells with a plasmid containing the cDNA coding for
the variant HPg, have been determined. Employing high-performance anion-exchange
liquid chromatography mapping of the oligosaccharide units cleaved from the
protein by glycopeptidase F, compared with elution positions of standard
oligosaccharides, coupled with monosaccharide compositional determinations and
analyses of sequential exoglycosidase digestions and specific lectin binding, we
find that considerable microheterogeneity in oligosaccharide structure exists at
this sole potential N-linked glycosylation site on HPg. A variety of high-mannose
structures, as well as bi-, tri-, and tetraantennary complex-type carbohydrate,
has been found, in relative amounts of 1-25% of the total oligosaccharides. The
complex-type structures contain variable amounts of sialic acid (Sia), ranging
from 0 to 5 mol/mol of oligosaccharide in the different glycan structures.
Neither hybrid-type molecules, N-acetylglucosamine bisecting oligosaccharides,
nor N-acetyllactosaminyl-repeat structures were found to be present in the
complex-type carbohydrate pool in observable amounts. Of interest, a significant
portion of the Sia exists an outer arm structures in an (alpha 2,6) linkage to
the penultimate galactose, a novel finding in CHO cell-directed
glycosylation.(ABSTRACT TRUNCATED AT 250 WORDS)
FAU - Davidson, D J
AU - Davidson DJ
AD - Department of Chemistry and Biochemistry, University of Notre Dame, Indiana
46556.
FAU - Castellino, F J
AU - Castellino FJ
LA - eng
GR - HL-13423/HL/NHLBI 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 - Biochemistry
JT - Biochemistry
JID - 0370623
RN - 0 (Oligonucleotides)
RN - 7006-34-0 (Asparagine)
RN - 9001-91-6 (Plasminogen)
RN - EC 3.2.1.21 (beta-Glucosidase)
RN - EC 3.2.1.74 (Glucan 1,4-beta-Glucosidase)
SB - IM
MH - Animals
MH - Asparagine/*genetics
MH - Carbohydrate Conformation
MH - Carbohydrate Sequence
MH - Cell Line
MH - Cricetinae
MH - Cricetulus
MH - Female
MH - Glucan 1,4-beta-Glucosidase
MH - Glycosylation
MH - Humans
MH - Hydrolysis
MH - Molecular Sequence Data
MH - Oligonucleotides/chemistry/*metabolism
MH - Ovary/*metabolism
MH - Plasminogen/biosynthesis/*genetics
MH - beta-Glucosidase
EDAT- 1991/01/22 00:00
MHDA- 1991/01/22 00:01
CRDT- 1991/01/22 00:00
PHST- 1991/01/22 00:00 [pubmed]
PHST- 1991/01/22 00:01 [medline]
PHST- 1991/01/22 00:00 [entrez]
PST - ppublish
SO - Biochemistry. 1991 Jan 22;30(3):625-33.
PMID- 8323299
OWN - NLM
STAT- MEDLINE
DCOM- 19930803
LR - 20071114
IS - 0003-9861 (Print)
IS - 0003-9861 (Linking)
VI - 304
IP - 1
DP - 1993 Jul
TI - Assignment of O-glycan attachment sites to the hinge-like regions of human
lysosomal membrane glycoproteins lamp-1 and lamp-2.
PG - 65-73
AB - The lysosomal membrane glycoproteins lamp-1 and lamp-2 are extensively
glycosylated with a variety of different carbohydrate structures of both N-linked
and O-linked type. In the present paper, we report the localization of O-linked
oligosaccharides exclusively to the hinge-like regions of lamp-1 and lamp-2
isolated from human chronic myelogenous leukemia cells. In both glycoproteins,
the O-glycans appear in clusters. In lamp-1, Thr-171, Thr-172, Ser-179, Ser-181,
and Ser-183 were fully glycosylated, whereas Ser-169 was partially glycosylated.
In lamp-2, complete glycosylation was found at Ser-167, Thr-168, Thr-172,
Thr-175, Thr-176, Thr-182, and Thr-183, and partial glycosylation at Ser-179 and
Thr-181, and possibly also at Thr-185. The amino acid sequences of these
O-glycosylation sites are consistent with the previous reports that residues at
positions -1 and +3 may influence the glycosylation reaction. Circular dichroism
and nuclear magnetic resonance spectroscopy was used for the structural
characterization of a synthetic peptide corresponding to residues 167 to 190 of
lamp-1. The results indicated that the proline-rich O-glycan acceptor region does
not adopt any typical periodic structure but differs from random-coil structure.
The circular dichroism spectrum of the peptide is, however, similar to that of
porcine submaxillary apomucin. A significant conformational variability was
observed in this region, presumably due to a slow (on the nuclear magnetic
resonance time scale) cis-trans isomerization of several proline residues. These
results, taken together, strongly suggest that a hinge region does not display
any typical ordered structure. The presence of O-glycans thus likely protects
this region from intralumenal lysosomal proteases.
FAU - Carlsson, S R
AU - Carlsson SR
AD - Department of Medical Biochemistry and Biophysics, University of Umea, Sweden.
FAU - Lycksell, P O
AU - Lycksell PO
FAU - Fukuda, M
AU - Fukuda M
LA - eng
GR - CA 48737/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 (Antigens, CD)
RN - 0 (Glycopeptides)
RN - 0 (Glycoproteins)
RN - 0 (Lysosome-Associated Membrane Glycoproteins)
RN - 0 (Membrane Glycoproteins)
RN - 0 (Polysaccharides)
SB - IM
MH - Amino Acid Sequence
MH - *Antigens, CD
MH - Circular Dichroism
MH - Glycopeptides/chemistry
MH - Glycoproteins/*chemistry
MH - Humans
MH - Lysosome-Associated Membrane Glycoproteins
MH - Magnetic Resonance Spectroscopy
MH - Membrane Glycoproteins/*chemistry/ultrastructure
MH - Molecular Sequence Data
MH - Polysaccharides/chemistry
MH - Protein Structure, Secondary
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 - S0003-9861(83)71322-6 [pii]
AID - 10.1006/abbi.1993.1322 [doi]
PST - ppublish
SO - Arch Biochem Biophys. 1993 Jul;304(1):65-73. doi: 10.1006/abbi.1993.1322.
PMID- 7451505
OWN - NLM
STAT- MEDLINE
DCOM- 19810327
LR - 20061115
IS - 0021-9258 (Print)
IS - 0021-9258 (Linking)
VI - 256
IP - 3
DP - 1981 Feb 10
TI - Structural studies of asparagine-linked sugar chains of human ceruloplasmin.
Structural characteristics of the triantennary complex type sugar chains of human
plasma glycoproteins.
PG - 1283-9
AB - The structures of the oligosaccharides released from human ceruloplasmin by
hydrazinolysis were studied by sequential exoglycosidase digestion in combination
with methylation analysis and periodate oxidation. A molecule of ceruloplasmin
was shown to have two biantennary oligosaccharides A-1 and one triantennary
oligosaccharide A-2, the structures of which are shown below. (Formula see text)
The abbreviations used are: NeuAc, N-acetylneuraminic acid; Gal, galactose;
GlcNAc, N-acetylglucosamine; Man, mannose.
FAU - Yamashita, K
AU - Yamashita K
FAU - Liang, C J
AU - Liang CJ
FAU - Funakoshi, S
AU - Funakoshi S
FAU - Kobata, A
AU - Kobata A
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 (Glycoproteins)
RN - 0 (Oligosaccharides)
RN - 7006-34-0 (Asparagine)
RN - EC 1.16.3.1 (Ceruloplasmin)
RN - EC 3.2.1.- (Glycoside Hydrolases)
SB - IM
MH - Asparagine/*analysis
MH - Carbohydrate Conformation
MH - Carbohydrate Sequence
MH - *Ceruloplasmin
MH - *Glycoproteins/urine
MH - Glycoside Hydrolases
MH - Humans
MH - Methylation
MH - Oligosaccharides/analysis
EDAT- 1981/02/10 00:00
MHDA- 1981/02/10 00:01
CRDT- 1981/02/10 00:00
PHST- 1981/02/10 00:00 [pubmed]
PHST- 1981/02/10 00:01 [medline]
PHST- 1981/02/10 00:00 [entrez]
PST - ppublish
SO - J Biol Chem. 1981 Feb 10;256(3):1283-9.
PMID- 7774715
OWN - NLM
STAT- MEDLINE
DCOM- 19950710
LR - 20111117
IS - 0014-5793 (Print)
IS - 0014-5793 (Linking)
VI - 365
IP - 1
DP - 1995 May 22
TI - Structural determination of two N-linked glycans isolated from recombinant human
lactoferrin expressed in BHK cells.
PG - 57-60
AB - A full-length cDNA coding for human lactoferrin was isolated from a mammary gland
library and the recombinant protein was expressed in BHK cells as described by
Stowell K. M. et al. [1991, Biochem. J. 276, 349-355]. Two N-linked glycans from
purified recombinant lactoferrin were released by hydrazinolysis and analyzed by
400-MHz 1H-NMR spectroscopy. The identified structures corresponded to
N-acetyllactosaminic biantennary glycans and were alpha-2,3-disialylated forms
(80%) or alpha-2,3-monosialylated (20%) forms. Moreover, 70% of total glycans
were alpha-1,6-fucosylated at the GlcNAc residue linked to asparagine. In regard
to its glycan moiety, the recombinant glycoprotein is close to native
lactoferrins from milk or leucocytes but shows specific structural features which
should be taken into account prior to in vivo and in vitro biological studies.
FAU - Legrand, D
AU - Legrand D
AD - Laboratoire de Chimie Biologique, UMR CNRS n.111, Universite des Sciences et
Technologies de Lille, Villeneuve d'Ascq, France.
FAU - Salmon, V
AU - Salmon V
FAU - Coddeville, B
AU - Coddeville B
FAU - Benaissa, M
AU - Benaissa M
FAU - Plancke, Y
AU - Plancke Y
FAU - Spik, G
AU - Spik G
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 (Monosaccharides)
RN - 0 (Polysaccharides)
RN - 0 (Recombinant Proteins)
RN - EC 3.4.21.- (Lactoferrin)
SB - IM
MH - Animals
MH - Carbohydrate Sequence
MH - Cells, Cultured
MH - Cricetinae
MH - Glycosylation
MH - Humans
MH - Lactoferrin/*chemistry/genetics
MH - Magnetic Resonance Spectroscopy
MH - Molecular Sequence Data
MH - Monosaccharides/analysis
MH - Polysaccharides/*chemistry/genetics
MH - Recombinant Proteins/chemistry
MH - Sequence Analysis
EDAT- 1995/05/22 00:00
MHDA- 1995/05/22 00:01
CRDT- 1995/05/22 00:00
PHST- 1995/05/22 00:00 [pubmed]
PHST- 1995/05/22 00:01 [medline]
PHST- 1995/05/22 00:00 [entrez]
AID - 0014-5793(95)00441-B [pii]
PST - ppublish
SO - FEBS Lett. 1995 May 22;365(1):57-60.
PMID- 7686446
OWN - NLM
STAT- MEDLINE
DCOM- 19930730
LR - 20151119
IS - 0008-5472 (Print)
IS - 0008-5472 (Linking)
VI - 53
IP - 13
DP - 1993 Jul 1
TI - Sugar chains of human cord serum alpha-fetoprotein: characteristics of N-linked
sugar chains of glycoproteins produced in human liver and hepatocellular
carcinomas.
PG - 2970-5
AB - Human serum alpha-fetoprotein (AFP) is elevated in not only hepatocellular
carcinoma (HCC) but also benign liver diseases. AFP produced in HCC and benign
liver diseases was separated into several isoforms corresponding to different
sugar chain structures by several types of lectin affinity electrophoresis, and
the HCC-specific AFP isoform was discriminated from those of benign liver
diseases. Because a small amount of HCC-specific AFP isoform was detected in cord
serum AFP, the whole sugar chain structures of human cord serum AFP were
determined, as follows: Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha
1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta
1-->4R1 and R2, Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha
2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, and
Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2
-->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2 in the
ratio of 81.6:8.9:9.5. R1 and R2 denote GlcNAc beta 1-->4GlcNAcOT (subscript OT
represents an NaB3H4-reduced oligosaccharide) and GlcNAc beta 1-->4(Fuc alpha
1-->6)GlcNAcOT, respectively, and the ratio between R1 and R2 in the respective
fractions was approximately 19:1. In contrast, the sugar chain structure of HCC
highly specific AFP isoform was found to comprise a monosialyl-biantennary sugar
chain with additional fucosylation of the proximal N-acetylglucosamine.
Fucosylation of AFP produced in fetal liver increased in inverse proportion to
the gestation period, in weeks, indicating that fucosylation of AFP in HCC may be
related to the dedifferentiation of human hepatocytes through malignant
transformation.
FAU - Yamashita, K
AU - Yamashita K
AD - Department of Biochemistry, Sasaki Institute, Tokyo, Japan.
FAU - Taketa, K
AU - Taketa K
FAU - Nishi, S
AU - Nishi S
FAU - Fukushima, K
AU - Fukushima K
FAU - Ohkura, T
AU - Ohkura 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 (Biomarkers, Tumor)
RN - 0 (Glycoproteins)
RN - 0 (Lectins)
RN - 0 (Oligosaccharides)
RN - 0 (Phytohemagglutinins)
RN - 0 (alpha-Fetoproteins)
SB - IM
MH - Biomarkers, Tumor/*analysis
MH - Carbohydrate Sequence
MH - Carcinoma, Hepatocellular/*blood/chemistry/metabolism
MH - Chromatography, Affinity
MH - Electrophoresis, Paper
MH - Fetal Blood/*chemistry
MH - Glycoproteins/biosynthesis/blood/*chemistry
MH - Humans
MH - Lectins
MH - Liver/embryology/*metabolism
MH - Liver Diseases/blood/metabolism
MH - Liver Neoplasms/*blood/chemistry/metabolism
MH - Molecular Sequence Data
MH - Oligosaccharides/biosynthesis/blood/*chemistry
MH - Phytohemagglutinins
MH - Sensitivity and Specificity
MH - alpha-Fetoproteins/*biosynthesis/metabolism
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]
PST - ppublish
SO - Cancer Res. 1993 Jul 1;53(13):2970-5.
id: 0 Error occurred: The following PMID is not available: 0
PMID- 2390069
OWN - NLM
STAT- MEDLINE
DCOM- 19900925
LR - 20181113
IS - 0264-6021 (Print)
IS - 0264-6021 (Linking)
VI - 269
IP - 3
DP - 1990 Aug 1
TI - Primary structure of glycans isolated from human leucocyte lactotransferrin.
Absence of fucose residues questions the proposed mechanism of hyposideraemia.
PG - 821-5
AB - Lactotransferrin was highly purified from lysates of human neutrophilic
leucocytes by immuno-affinity chromatography. A comparative analysis of the molar
carbohydrate compositions of human leucocyte lactotransferrin and human milk
lactotransferrin reveals that the glycans of leucocyte lactotransferrin differ
essentially by the absence of fucose residues. Structural analysis combining
methylation-mass spectrometry and 400 MHz 1H-n.m.r. spectrometry of
oligosaccharide alditols released from human leucocyte lactotransferrin shows the
presence of two disialylated and non-fucosylated biantennary glycans of the
N-acetyl-lactosaminic type. These results question a previously proposed
mechanism for hyposideraemia in which the leucocyte lactotransferrin was involved
and in which the fucose residues played a key role.
FAU - Derisbourg, P
AU - Derisbourg P
AD - Laboratoire de Chimie Biologique, Universite des Sciences et Techniques de Lille
Flandres-Artois, Villeneuve d'Ascq, France.
FAU - Wieruszeski, J M
AU - Wieruszeski JM
FAU - Montreuil, J
AU - Montreuil J
FAU - Spik, G
AU - Spik G
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 (Hydrazines)
RN - 0 (Lactoglobulins)
RN - 0 (Oligosaccharides)
RN - 0 (Polysaccharides)
RN - 28RYY2IV3F (Fucose)
RN - EC 3.4.21.- (Lactoferrin)
SB - IM
MH - Anemia, Hypochromic/blood
MH - Carbohydrate Sequence
MH - Fucose/metabolism
MH - Humans
MH - Hydrazines/metabolism
MH - Lactoferrin/*blood/isolation & purification/metabolism
MH - Lactoglobulins/*blood
MH - Leukocytes/*analysis
MH - Magnetic Resonance Spectroscopy
MH - Mass Spectrometry/methods
MH - Milk, Human/analysis
MH - Molecular Sequence Data
MH - Oligosaccharides/metabolism
MH - Polysaccharides/*blood/isolation & purification
PMC - PMC1131661
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]
PST - ppublish
SO - Biochem J. 1990 Aug 1;269(3):821-5.
PMID- 19838169
OWN - NLM
STAT- MEDLINE
DCOM- 20091203
LR - 20181113
IS - 1548-7105 (Electronic)
IS - 1548-7091 (Linking)
VI - 6
IP - 11
DP - 2009 Nov
TI - Enrichment of glycopeptides for glycan structure and attachment site
identification.
PG - 809-11
LID - 10.1038/nmeth.1392 [doi]
AB - We present a method to enrich for glycoproteins from proteomic samples.
Sialylated glycoproteins were selectively periodate-oxidized, captured on
hydrazide beads, trypsinized and released by acid hydrolysis of sialic acid
glycosidic bonds. Mass spectrometric fragment analysis allowed identification of
glycan structures, and additional fragmentation of deglycosylated ions yielded
peptide sequence information, which allowed glycan attachment site and protein
identification. We identified 36 N-linked and 44 O-linked glycosylation sites on
glycoproteins from human cerebrospinal fluid.
FAU - Nilsson, Jonas
AU - Nilsson J
AD - Department of Clinical Chemistry and Transfusion Medicine, Institute of
Biomedicine, University of Gothenburg, Sahlgrenska University Hospital,
Gothenburg, Sweden. jonas.nilsson@clinchem.gu.se
FAU - Ruetschi, Ulla
AU - Ruetschi U
FAU - Halim, Adnan
AU - Halim A
FAU - Hesse, Camilla
AU - Hesse C
FAU - Carlsohn, Elisabet
AU - Carlsohn E
FAU - Brinkmalm, Gunnar
AU - Brinkmalm G
FAU - Larson, Goran
AU - Larson G
LA - eng
PT - Journal Article
PT - Research Support, Non-U.S. Gov't
DEP - 20091018
PL - United States
TA - Nat Methods
JT - Nature methods
JID - 101215604
RN - 0 (Cerebrospinal Fluid Proteins)
RN - 0 (Glycopeptides)
RN - 0 (Glycoproteins)
RN - 0 (Polysaccharides)
RN - EC 3.5.1.52 (Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase)
SB - IM
MH - Cerebrospinal Fluid Proteins/*analysis
MH - Glycopeptides/analysis
MH - Glycoproteins/*chemistry/*isolation & purification
MH - Glycosylation
MH - Humans
MH - Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase/metabolism
MH - Polysaccharides/analysis/chemistry
MH - Proteomics
MH - Tandem Mass Spectrometry
EDAT- 2009/10/20 06:00
MHDA- 2009/12/16 06:00
CRDT- 2009/10/20 06:00
PHST- 2009/07/15 00:00 [received]
PHST- 2009/09/04 00:00 [accepted]
PHST- 2009/10/20 06:00 [entrez]
PHST- 2009/10/20 06:00 [pubmed]
PHST- 2009/12/16 06:00 [medline]
AID - nmeth.1392 [pii]
AID - 10.1038/nmeth.1392 [doi]
PST - ppublish
SO - Nat Methods. 2009 Nov;6(11):809-11. doi: 10.1038/nmeth.1392. Epub 2009 Oct 18.
PMID- 3342257
OWN - NLM
STAT- MEDLINE
DCOM- 19880330
LR - 20161126
IS - 0006-3002 (Print)
IS - 0006-3002 (Linking)
VI - 964
IP - 2
DP - 1988 Feb 17
TI - Chemical structure of neutral sugar chains isolated from human mature milk
kappa-casein.
PG - 213-20
AB - The carbohydrate chains linked to human kappa-casein from mature milk were
released by alkaline borohydride treatment as reduced oligosaccharides. The
neutral oligosaccharides of lower molecular weight were fractionated and purified
by gel filtration and preparative thin layer chromatographies. Seven neutral
oligosaccharides (a di- (0.5%), two tetra- (30.5%), two penta- (5.4%) and two
hexasaccharide alditols (10.9%] were obtained in homogeneity, and followed by
methylation analysis with gas-liquid chromatography-mass spectrometry and by
anomer analysis with 13C nuclear magnetic resonance. Their chemical structures
were identified to be Gal beta 1----3GalNAc-ol (I), Gal beta 1----3[Gal beta
1----4GlcNAc beta 1----6]GalNAc-ol (II), Gal beta 1----3[Fuc alpha 1----4GlcNAc
beta 1----6]GalNAc-ol (III), GlcNAc beta 1----3/6Gal beta 1----3[Gal beta
1----4GlcNAc beta 1----6]GalNAc-ol (IV), GlcNAc beta 1----3/6Gal beta 1----3[Fuc
alpha 1----4GlcNAc beta 1----6]GalNAc-ol (V), Fuc alpha 1----4GlcNAc beta
1----3/6Gal beta 1----3[Gal beta 1----4GlcNAc beta 1----6]GalNAc-ol (VI) and Fuc
alpha 1----4GlcNAc beta 1----3/6Gal beta 1----3[Fuc alpha 1----4GlcNAc beta
1----6]GalNAc-ol (VII). Five oligosaccharide alditols (III-VII) were the novel
carbohydrate chains of kappa-casein from mammalian milk.
FAU - Saito, T
AU - Saito T
AD - Laboratory of Food Hygiene, Faculty of Social Welfare, Tohoku Fukushi University,
Japan.
FAU - Itoh, T
AU - Itoh T
FAU - Adachi, S
AU - Adachi S
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 (Caseins)
RN - 0 (Oligosaccharides)
SB - IM
EIN - Biochim Biophys Acta 1988 Mar 17;964(3):391
MH - Carbohydrate Conformation
MH - Carbohydrate Sequence
MH - *Caseins
MH - Female
MH - Humans
MH - Mass Spectrometry
MH - Milk, Human/*analysis
MH - Molecular Sequence Data
MH - Oligosaccharides/*isolation & purification
EDAT- 1988/02/17 00:00
MHDA- 1988/02/17 00:01
CRDT- 1988/02/17 00:00
PHST- 1988/02/17 00:00 [pubmed]
PHST- 1988/02/17 00:01 [medline]
PHST- 1988/02/17 00:00 [entrez]
AID - 0304-4165(88)90169-9 [pii]
PST - ppublish
SO - Biochim Biophys Acta. 1988 Feb 17;964(2):213-20.
PMID- 7592613
OWN - NLM
STAT- MEDLINE
DCOM- 19951204
LR - 20161123
IS - 0021-9258 (Print)
IS - 0021-9258 (Linking)
VI - 270
IP - 41
DP - 1995 Oct 13
TI - Structural analysis of the oligosaccharides derived from glycodelin, a human
glycoprotein with potent immunosuppressive and contraceptive activities.
PG - 24116-26
AB - Glycodelin, also known as placental protein 14 (PP14) or progesterone-associated
endometrial protein (PAEP), is a human glycoprotein with potent immunosuppressive
and contraceptive activities. In this paper we report the first characterization
of glycodelin-derived oligosaccharides. Using strategies based upon fast atom
bombardment and electrospray mass spectrometry we have established that
glycodelin is glycosylated at Asn-28 and Asn-63. The Asn-28 site carries high
mannose, hybrid and complex-type structures, whereas the second site is
exclusively occupied by complex-type glycans. The major non-reducing epitopes in
the complex-type glycans are: Gal beta 1-4GlcNAc (lacNAc), GalNAc beta 1-4GlcNAc
(lacdiNAc), NeuAc alpha 2-6Gal beta 1-4GlcNAc (sialylated lacNAc), NeuAc alpha
2-6Gal beta 1-4GlcNAc (sialylated lacdiNAc), Gal beta 1-4(Fuc alpha 1-3)GlcNAc
(Lewisx), and GalNAc beta 1-4(Fuc alpha 1-3)GlcNAc (lacdiNAc analogue of Lewisx).
It is possible that the oligosaccharides bearing sialylated lacNAc or lacdiNAc
antennae may manifest immunosuppressive effects by specifically blocking adhesive
and activation-related events mediated by CD22, the human B cell associated
receptor. Oligosaccharides with fucosylated lacdiNAc antennae have previously
been shown to potently block selectin-mediated adhesions and may perform the same
function in glycodelin. The potent inhibitory effect of glycodelin on initial
human sperm-zona pellucida binding is consistent with our previous suggestion
that this cell adhesion event requires a selectin-like adhesion process. This
result also raises the possibility that a convergence between immune and gamete
recognition processes may have occurred in the types of carbohydrate ligands
recognized in the human.
FAU - Dell, A
AU - Dell A
AD - Department of Biochemistry, Imperial College of Science, Technology and Medicine,
London, United Kingdom.
FAU - Morris, H R
AU - Morris HR
FAU - Easton, R L
AU - Easton RL
FAU - Panico, M
AU - Panico M
FAU - Patankar, M
AU - Patankar M
FAU - Oehniger, S
AU - Oehniger S
FAU - Koistinen, R
AU - Koistinen R
FAU - Koistinen, H
AU - Koistinen H
FAU - Seppala, M
AU - Seppala M
FAU - Clark, G F
AU - Clark GF
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 (Contraceptive Agents)
RN - 0 (Epitopes)
RN - 0 (Glycodelin)
RN - 0 (Glycoproteins)
RN - 0 (Immunosuppressive Agents)
RN - 0 (Oligosaccharides)
RN - 0 (PAEP protein, human)
RN - 0 (Peptide Fragments)
RN - 0 (Pregnancy Proteins)
RN - OS382OHJ8P (Cyanogen Bromide)
SB - IM
MH - Amino Acid Sequence
MH - Carbohydrate Conformation
MH - Carbohydrate Sequence
MH - *Contraceptive Agents
MH - Cyanogen Bromide
MH - Epitopes/analysis/chemistry
MH - Gas Chromatography-Mass Spectrometry
MH - Glycodelin
MH - *Glycoproteins
MH - Humans
MH - *Immunosuppressive Agents
MH - Molecular Sequence Data
MH - Oligosaccharides/*chemistry/isolation & purification
MH - Peptide Fragments/chemistry
MH - Pregnancy Proteins/*chemistry
MH - Spectrometry, Mass, Fast Atom Bombardment
EDAT- 1995/10/13 00:00
MHDA- 1995/10/13 00:01
CRDT- 1995/10/13 00:00
PHST- 1995/10/13 00:00 [pubmed]
PHST- 1995/10/13 00:01 [medline]
PHST- 1995/10/13 00:00 [entrez]
PST - ppublish
SO - J Biol Chem. 1995 Oct 13;270(41):24116-26.
PMID- 24766575
OWN - NLM
STAT- MEDLINE
DCOM- 20150122
LR - 20140606
IS - 1535-3907 (Electronic)
IS - 1535-3893 (Linking)
VI - 13
IP - 6
DP - 2014 Jun 6
TI - Efficient and accurate glycopeptide identification pipeline for high-throughput
site-specific N-glycosylation analysis.
PG - 3121-9
LID - 10.1021/pr500238v [doi]
AB - Study of site-specific N-glycosylation in complex sample remains a huge
analytical challenge because protein glycosylation is structurally diverse in
post-translational modifications, resulting in an intricacy of N-glycopeptides.
Here we have developed a novel approach for high-throughput N-glycopeptide
profiling based on a network-centric algorithm for deciphering glycan
fragmentation in mass spectrometry. We performed an extensive validation and a
high-throughput N-glycosylation study on serum and identified thousands of
N-glycopeptide spectra with high confidence. The results revealed a similar level
of glycan microheterogeneity to that of conventional glycomics approach on
individual proteins and provided the unique in-depth site-specific information
that could only be studied through glycopeptide profiling.
FAU - Liu, Mingqi
AU - Liu M
AD - Department of Chemistry, Fudan University , 220 Han Dan Road, Shanghai 200433, P.
R. China.
FAU - Zhang, Yang
AU - Zhang Y
FAU - Chen, Yaohan
AU - Chen Y
FAU - Yan, Guoquan
AU - Yan G
FAU - Shen, Chengping
AU - Shen C
FAU - Cao, Jing
AU - Cao J
FAU - Zhou, Xinwen
AU - Zhou X
FAU - Liu, Xiaohui
AU - Liu X
FAU - Zhang, Lei
AU - Zhang L
FAU - Shen, Huali
AU - Shen H
FAU - Lu, Haojie
AU - Lu H
FAU - He, Fuchu
AU - He F
FAU - Yang, Pengyuan
AU - Yang P
LA - eng
PT - Journal Article
PT - Research Support, Non-U.S. Gov't
DEP - 20140508
PL - United States
TA - J Proteome Res
JT - Journal of proteome research
JID - 101128775
RN - 0 (Blood Proteins)
RN - 0 (Glycoproteins)
SB - IM
MH - Amino Acid Motifs
MH - Blood Proteins/chemistry/metabolism
MH - Carbohydrate Conformation
MH - Carbohydrate Sequence
MH - Glycoproteins/blood/*chemistry
MH - Glycosylation
MH - Humans
MH - Molecular Sequence Data
MH - Peptide Mapping
MH - *Protein Processing, Post-Translational
MH - Tandem Mass Spectrometry
EDAT- 2014/04/29 06:00
MHDA- 2015/01/23 06:00
CRDT- 2014/04/29 06:00
PHST- 2014/04/29 06:00 [entrez]
PHST- 2014/04/29 06:00 [pubmed]
PHST- 2015/01/23 06:00 [medline]
AID - 10.1021/pr500238v [doi]
PST - ppublish
SO - J Proteome Res. 2014 Jun 6;13(6):3121-9. doi: 10.1021/pr500238v. Epub 2014 May 8.
PMID- 2813359
OWN - NLM
STAT- MEDLINE
DCOM- 19891201
LR - 20181113
IS - 0027-8424 (Print)
IS - 0027-8424 (Linking)
VI - 86
IP - 20
DP - 1989 Oct
TI - Relationship between sugar chain structure and biological activity of recombinant
human erythropoietin produced in Chinese hamster ovary cells.
PG - 7819-22
AB - Two forms of erythropoietin, EPO-bi and EPO-tetra, with different biological
activities were isolated from the culture medium of a recombinant Chinese hamster
ovary cell line, B8-300, into which the human erythropoietin gene had been
introduced. EPO-bi, an unusual form, showed only one-seventh the in vivo activity
and 3 times higher in vitro activity of the previously described recombinant
human EPO (standard EPO). In contrast, EPO-tetra showed both in vivo and in vitro
activities comparable to those of the standard EPO. EPO-bi, EPO-tetra, and the
standard EPO had the same amino acid composition and immunoreactivity. However,
structural analyses of their N-linked sugar chains revealed that EPO-bi contains
the biantennary complex type as the major sugar chain, while EPO-tetra and the
standard EPO contain the tetraantennary complex type as the major sugar chain.
From examination of various preparations of recombinant human EPO, we found a
positive correlation between the in vivo activity of EPO and the ratio of
tetraantennary to biantennary oligosaccharides. These results suggest that higher
branching of the N-linked sugar chains is essential for effective expression of
in vivo biological activity of EPO.
FAU - Takeuchi, M
AU - Takeuchi M
AD - Pharmaceutical Laboratory, Kirin Brewery, Gunma, Japan.
FAU - Inoue, N
AU - Inoue N
FAU - Strickland, T W
AU - Strickland TW
FAU - Kubota, M
AU - Kubota M
FAU - Wada, M
AU - Wada M
FAU - Shimizu, R
AU - Shimizu R
FAU - Hoshi, S
AU - Hoshi S
FAU - Kozutsumi, H
AU - Kozutsumi H
FAU - Takasaki, S
AU - Takasaki S
FAU - Kobata, A
AU - Kobata A
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 (Oligosaccharides)
RN - 0 (Recombinant Proteins)
RN - 11096-26-7 (Erythropoietin)
SB - IM
MH - Animals
MH - Carbohydrate Conformation
MH - Carbohydrate Sequence
MH - Cell Line
MH - Cricetinae
MH - Cricetulus
MH - Erythropoietin/genetics/isolation & purification/*pharmacology
MH - Female
MH - Genes
MH - Humans
MH - Molecular Sequence Data
MH - Oligosaccharides/*isolation & purification
MH - Ovary
MH - Recombinant Proteins/isolation & purification/pharmacology
MH - Transfection
PMC - PMC298162
EDAT- 1989/10/01 00:00
MHDA- 1989/10/01 00:01
CRDT- 1989/10/01 00:00
PHST- 1989/10/01 00:00 [pubmed]
PHST- 1989/10/01 00:01 [medline]
PHST- 1989/10/01 00:00 [entrez]
PST - ppublish
SO - Proc Natl Acad Sci U S A. 1989 Oct;86(20):7819-22.
PMID- 9677337
OWN - NLM
STAT- MEDLINE
DCOM- 19980923
LR - 20181113
IS - 0264-6021 (Print)
IS - 0264-6021 (Linking)
VI - 333 ( Pt 3)
DP - 1998 Aug 1
TI - Glycosylation pattern of human inter-alpha-inhibitor heavy chains.
PG - 749-56
AB - Human inter-alpha-inhibitor (IalphaI) is a plasma serine-proteinase inhibitor. It
consists of three polypeptide chains covalently linked by a glycosaminoglycan
chain: a light chain named bikunin carrying the anti-proteinase activity and two
heavy chains, H1 and H2, which exhibit specific properties, e.g. they interact
with hyaluronan thus stabilizing the extracellular matrix. In this study, using
matrix-assisted laser desorption ionization-time-of-flight MS and amino acid
sequencing of tryptic peptides, we provide a detailed analysis of the
glycosylation pattern of both heavy chains. H1 carries two complex-type N-glycans
of predominantly biantennary structure linked to asparagine residues at positions
256 and 559 respectively. In contrast, the oligosaccharides attached to H2 are a
complex-type N-glycan in the N-terminal region of the protein (Asn64) and three
to four type-1 core-structure O-glycans mono- or di-sialylated, clustered in the
C-terminal region. We propose that these O-glycans might function as a
recognition signal for the H2 heavy chain. The biological implications of this
hypothesis, notably for the biosynthetic pathway of IalphaI, are discussed.
FAU - Flahaut, C
AU - Flahaut C
AD - Laboratoire de Biochimie, Faculte de Pharmacie, Universite de Lille II, Avenue du
Professeur Laguesse, B.P. 83, F-59006 Lille, France.
FAU - Capon, C
AU - Capon C
FAU - Balduyck, M
AU - Balduyck M
FAU - Ricart, G
AU - Ricart G
FAU - Sautiere, P
AU - Sautiere P
FAU - Mizon, J
AU - Mizon J
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 (Alpha-Globulins)
RN - 0 (Glycopeptides)
RN - 0 (Macromolecular Substances)
RN - 0 (Serine Proteinase Inhibitors)
RN - 39346-44-6 (inter-alpha-inhibitor)
SB - IM
MH - Alpha-Globulins/chemistry/*metabolism
MH - Amino Acid Sequence
MH - Carbohydrate Sequence
MH - Chromatography, High Pressure Liquid
MH - Glycopeptides/chemistry/metabolism
MH - Glycosylation
MH - Humans
MH - Macromolecular Substances
MH - Molecular Sequence Data
MH - Serine Proteinase Inhibitors/chemistry/*metabolism
MH - Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
PMC - PMC1219641
EDAT- 1998/07/25 00:00
MHDA- 1998/07/25 00:01
CRDT- 1998/07/25 00:00
PHST- 1998/07/25 00:00 [pubmed]
PHST- 1998/07/25 00:01 [medline]
PHST- 1998/07/25 00:00 [entrez]
PST - ppublish
SO - Biochem J. 1998 Aug 1;333 ( Pt 3):749-56.
PMID- 22678432
OWN - NLM
STAT- MEDLINE
DCOM- 20121001
LR - 20181113
IS - 1750-2799 (Electronic)
IS - 1750-2799 (Linking)
VI - 7
IP - 7
DP - 2012 Jun 7
TI - Determination of site-specific glycan heterogeneity on glycoproteins.
PG - 1285-98
LID - 10.1038/nprot.2012.062 [doi]
AB - The comprehensive analysis of protein glycosylation is a major requirement for
understanding glycoprotein function in biological systems, and is a prerequisite
for producing recombinant glycoprotein therapeutics. This protocol describes
workflows for the characterization of glycopeptides and their site-specific
heterogeneity, showing examples of the analysis of recombinant human
erythropoietin (rHuEPO), alpha1-proteinase inhibitor (A1PI) and immunoglobulin
(IgG). Glycoproteins of interest can be proteolytically digested either in
solution or in-gel after electrophoretic separation, and the (glyco)peptides are
analyzed by capillary/nano-liquid chromatography-electrospray ionization tandem
mass spectrometry (LC-ESI-MS/MS). If required, specific glycopeptide enrichment
steps, such as hydrophilic interaction liquid chromatography (HILIC), can also be
performed. Particular emphasis is placed on data interpretation and the
determination of site-specific glycan heterogeneity. The described workflow takes
approximately 3-5 d, including sample preparation and data analysis. The data
obtained from analyzing released glycans of rHuEPO and IgG, described in the
second protocol of this series (10.1038/nprot.2012.063), provide complementary
detailed glycan structural information that facilitates characterization of the
glycopeptides.
FAU - Kolarich, Daniel
AU - Kolarich D
AD - Biomolecular Frontiers Research Centre, Faculty of Science, Macquarie University,
Sydney, New South Wales, Australia.
FAU - Jensen, Pia H
AU - Jensen PH
FAU - Altmann, Friedrich
AU - Altmann F
FAU - Packer, Nicolle H
AU - Packer NH
LA - eng
PT - Journal Article
PT - Research Support, Non-U.S. Gov't
DEP - 20120607
PL - England
TA - Nat Protoc
JT - Nature protocols
JID - 101284307
RN - 0 (EPO protein, human)
RN - 0 (Glycoproteins)
RN - 0 (Polysaccharides)
RN - 11096-26-7 (Erythropoietin)
SB - IM
MH - Chromatography, Liquid/methods
MH - Electrophoresis, Polyacrylamide Gel
MH - Erythropoietin/chemistry/metabolism
MH - Glycoproteins/*chemistry/metabolism
MH - Glycosylation
MH - Humans
MH - Polysaccharides/*chemistry/metabolism
MH - Proteomics/*methods
MH - Software
MH - Tandem Mass Spectrometry/methods
EDAT- 2012/06/09 06:00
MHDA- 2012/10/02 06:00
CRDT- 2012/06/09 06:00
PHST- 2012/06/09 06:00 [entrez]
PHST- 2012/06/09 06:00 [pubmed]
PHST- 2012/10/02 06:00 [medline]
AID - nprot.2012.062 [pii]
AID - 10.1038/nprot.2012.062 [doi]
PST - epublish
SO - Nat Protoc. 2012 Jun 7;7(7):1285-98. doi: 10.1038/nprot.2012.062.
PMID- 7679920
OWN - NLM
STAT- MEDLINE
DCOM- 19930401
LR - 20181113
IS - 0007-0920 (Print)
IS - 0007-0920 (Linking)
VI - 67
IP - 3
DP - 1993 Mar
TI - Carbohydrate structures of human alpha-fetoprotein of patients with
hepatocellular carcinoma: presence of fucosylated and non-fucosylated
triantennary glycans.
PG - 486-92
AB - Chemical structures of the sugar chains of various human alpha-fetoprotein (AFP)
species with different affinity for Concanavalin A (Con A) and Lens culinaris
agglutinin (LCA) were examined by pyridylamination of their oligosaccharides and
stepwise exoglycosidase digestion. Using reversed-phase and size-fractionation
high performance liquid chromatography systems we identified six
pyridylamino-sugar chains. The Con A-reactive and LCA-nonreactive species of AFP
from patients with hepatocellular carcinoma contained a biantennary sugar chain,
and the Con A-reactive and LCA-reactive species had a biantennary one with a
fucose residue at the innermost N-acetylglucosamine residue. The Con
A-nonreactive and LCA-reactive species contained a biantennary sugar chain both
with a bisecting-N-acetylglucosamine residue at the trimannosyl core and with a
focus residue at the innermost N-acetylglucosamine residue. The Con A-nonreactive
and LCA-nonreactive species contained a fucosylated triantennary sugar chain as a
major component, and two minor components: a triantennary sugar chain and a
biantennary sugar chain with a bisecting-N-acetylglucosamine residue at the
trimannosyl core. Thus, the fucosylated and non-fucosylated triantennary sugar
chains were newly identified in human AFP. Essentially identical results were
obtained for AFP from the patient with gallbladder carcinoma which metastasizes
to the liver. These results indicate that the increment in fucosylation and
branching to form new antennae is a characteristic feature of the carbohydrate
chains of AFP from patients with neoplastic diseases of the liver.
FAU - Aoyagi, Y
AU - Aoyagi Y
AD - Department of Internal Medicine, Niigata University School of Medicine, Japan.
FAU - Suzuki, Y
AU - Suzuki Y
FAU - Igarashi, K
AU - Igarashi K
FAU - Saitoh, A
AU - Saitoh A
FAU - Oguro, M
AU - Oguro M
FAU - Yokota, T
AU - Yokota T
FAU - Mori, S
AU - Mori S
FAU - Suda, T
AU - Suda T
FAU - Isemura, M
AU - Isemura M
FAU - Asakura, H
AU - Asakura H
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 (Polysaccharides)
RN - 0 (alpha-Fetoproteins)
SB - IM
MH - Carbohydrate Conformation
MH - Carcinoma, Hepatocellular/*chemistry
MH - Chromatography, High Pressure Liquid
MH - Humans
MH - Liver Neoplasms/*chemistry
MH - Polysaccharides/analysis
MH - alpha-Fetoproteins/*chemistry/isolation & purification
PMC - PMC1968279
EDAT- 1993/03/01 00:00
MHDA- 1993/03/01 00:01
CRDT- 1993/03/01 00:00
PHST- 1993/03/01 00:00 [pubmed]
PHST- 1993/03/01 00:01 [medline]
PHST- 1993/03/01 00:00 [entrez]
PST - ppublish
SO - Br J Cancer. 1993 Mar;67(3):486-92.
PMID- 24706782
OWN - NLM
STAT- MEDLINE
DCOM- 20140624
LR - 20181113
IS - 1091-6490 (Electronic)
IS - 0027-8424 (Linking)
VI - 111
IP - 17
DP - 2014 Apr 29
TI - Expression and glycoengineering of functionally active heteromultimeric IgM in
plants.
PG - 6263-8
LID - 10.1073/pnas.1320544111 [doi]
AB - IgM antibodies are an important player of the human's innate defense mechanisms
and increasingly have gained interest as therapeutics. Although the expression of
IgM antibodies in mammalian cell culture is established, this approach remains
costly and alternative methods have not been developed yet. Plants have a proven
record for the production of therapeutically relevant recombinant proteins.
However, whether they are able to express proteins like IgM antibodies, which
range among the most complex human proteins, remains unknown so far. Here we
report the in planta generation of the functionally active monoclonal antitumor
IgM PAT-SM6 (SM6). SM6 efficiently accumulates in plant leaves and assembles
correctly into heterooligomers (pentamers and hexamers). Detailed glycosylation
analysis exhibited complex and oligomannosidic N-glycans in a site-specific
manner on human-serum IgM and on plant- and human-cell-line-produced SM6.
Moreover, extensive in planta glycoengineering allowed the generation of SM6
decorated with sialylated human-type oligosaccharides, comparable to
plasma-derived IgM. A glycosylated model of pentameric IgM exhibits different
accessibility of the glycosylation sites, explaining site-specific glycosylation.
Biochemical and biophysical properties and importantly biological activities of
plant-derived SM6 glycoforms are comparable to the human-cell-derived
counterparts. The in planta generation of one of the most complex human proteins
opens new pathways toward the production of difficult-to-express proteins for
pharmaceutical applications. Moreover, the generation of IgMs with a controlled
glycosylation pattern allows the study of the so far unknown contribution of
sugar moieties to the function of IgMs.
FAU - Loos, Andreas
AU - Loos A
AD - Department of Applied Genetics and Cell Biology, University of Natural Resources
and Life Sciences, 1190 Vienna, Austria.
FAU - Gruber, Clemens
AU - Gruber C
FAU - Altmann, Friedrich
AU - Altmann F
FAU - Mehofer, Ulrich
AU - Mehofer U
FAU - Hensel, Frank
AU - Hensel F
FAU - Grandits, Melanie
AU - Grandits M
FAU - Oostenbrink, Chris
AU - Oostenbrink C
FAU - Stadlmayr, Gerhard
AU - Stadlmayr G
FAU - Furtmuller, Paul G
AU - Furtmuller PG
FAU - Steinkellner, Herta
AU - Steinkellner H
LA - eng
SI - RefSeq/NP_653247
PT - Journal Article
PT - Research Support, Non-U.S. Gov't
DEP - 20140331
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 (Immunoglobulin M)
RN - 0 (Polysaccharides)
SB - IM
CIN - Proc Natl Acad Sci U S A. 2014 Apr 29;111(17):6124-5. PMID: 24737888
MH - Chromatography, Affinity
MH - Glycomics/*methods
MH - Glycosylation
MH - Humans
MH - Immunoglobulin M/chemistry/*metabolism
MH - Models, Molecular
MH - Plant Cells/metabolism
MH - Plant Leaves/metabolism
MH - Polysaccharides/chemistry/metabolism
MH - *Protein Multimerization
MH - Spectrometry, Mass, Electrospray Ionization
MH - Tobacco/*metabolism
PMC - PMC4035941
OTO - NOTNLM
OT - N-glycosylation
OT - recombinant biopharmaceuticals
EDAT- 2014/04/08 06:00
MHDA- 2014/06/25 06:00
CRDT- 2014/04/08 06:00
PHST- 2014/04/08 06:00 [entrez]
PHST- 2014/04/08 06:00 [pubmed]
PHST- 2014/06/25 06:00 [medline]
AID - 1320544111 [pii]
AID - 10.1073/pnas.1320544111 [doi]
PST - ppublish
SO - Proc Natl Acad Sci U S A. 2014 Apr 29;111(17):6263-8. doi:
10.1073/pnas.1320544111. Epub 2014 Mar 31.
PMID- 10731668
OWN - NLM
STAT- MEDLINE
DCOM- 20000414
LR - 20181130
IS - 0021-924X (Print)
IS - 0021-924X (Linking)
VI - 127
IP - 1
DP - 2000 Jan
TI - Characterization of the N-oligosaccharides attached to the atypical Asn-X-Cys
sequence of recombinant human epidermal growth factor receptor.
PG - 65-72
AB - The extracellular domain of human EGF receptor (sEGFR) produced by CHO cells has
been used in various biophysical studies to elucidate the molecular mechanism of
EGF-induced receptor activation. We have found that the CHO sEGFR contains one
oligosaccharide chain attached to an atypical N-glycosylation consensus sequence,
Asn(32 )-X( 33 )-Cys(34 ). The oligosaccharide structure at Asn(32 ) is a mixture
of the monosialo and asialo forms of a core fucosylated biantennary complex-type
oligosaccharide. Deletion of this atypical glycosylation site by replacement of
Asn(32 ) with lysine changed neither the expression nor function of the full
length EGFR in CHO cells. The glycosylation at Asn(32 ) in CHO sEGFR was
incomplete: 20% of Asn(32 ) remained unmodified. Thus, CHO sEGFR itself is
heterogeneous with respect to the glycosylation at Asn(32 ), which may cause
problems in biophysical studies. An attempt to remove the oligosaccharide at
Asn(32 ) enzymatically did not succeed under nondenaturing conditions. Therefore,
sEGFR with the mutation of Asn(32) -> Lys(32 )is useful for biophysical and
biochemical studies, and, particularly, for X-ray crystallography.
FAU - Sato, C
AU - Sato C
AD - Department of Structural Biology, Biomolecular Engineering Research Institute,
Furuedai Suita, Osaka 565-0874, Japan.
FAU - Kim, J H
AU - Kim JH
FAU - Abe, Y
AU - Abe Y
FAU - Saito, K
AU - Saito K
FAU - Yokoyama, S
AU - Yokoyama S
FAU - Kohda, D
AU - Kohda D
LA - eng
PT - Journal Article
PL - England
TA - J Biochem
JT - Journal of biochemistry
JID - 0376600
RN - 0 (Oligosaccharides)
RN - 0 (Recombinant Proteins)
RN - 7006-34-0 (Asparagine)
RN - EC 2.7.10.1 (ErbB Receptors)
RN - K3Z4F929H6 (Lysine)
RN - K848JZ4886 (Cysteine)
SB - IM
MH - Amino Acid Sequence
MH - Amino Acid Substitution/genetics
MH - Animals
MH - Asparagine/*chemistry/genetics/metabolism
MH - CHO Cells
MH - Carbohydrate Sequence
MH - Cricetinae
MH - Cysteine/*chemistry/genetics/metabolism
MH - ErbB Receptors/biosynthesis/*chemistry/*genetics/metabolism
MH - Glycosylation
MH - Humans
MH - Lysine/genetics/metabolism
MH - Molecular Sequence Data
MH - Oligosaccharides/*chemistry/metabolism
MH - Recombinant Proteins/biosynthesis/*chemistry/metabolism
MH - Transfection
EDAT- 2000/03/25 09:00
MHDA- 2000/04/25 09:00
CRDT- 2000/03/25 09:00
PHST- 2000/03/25 09:00 [pubmed]
PHST- 2000/04/25 09:00 [medline]
PHST- 2000/03/25 09:00 [entrez]
PST - ppublish
SO - J Biochem. 2000 Jan;127(1):65-72.
PMID- 8687384
OWN - NLM
STAT- MEDLINE
DCOM- 19960820
LR - 20181113
IS - 0264-6021 (Print)
IS - 0264-6021 (Linking)
VI - 316 ( Pt 2)
DP - 1996 Jun 1
TI - The glycosylation of Bowes melanoma tissue plasminogen activator: lectin mapping,
reaction with anti-L2/HNK-1 antibodies and the presence of sulphated/glucuronic
acid containing glycans.
PG - 427-37
AB - The glycosylation of tissue plasminogen activator (t-PA) obtained from the Bowes
melanoma cell line was re-examined using methods of serial lectin affinity
chromatography coupled with Bio-Gel P-4 gel filtration chromatography and
exoglycosidase sequencing. This study clarified an earlier discrepancy in the
literature and confirmed that the major complex N-linked glycans on Bowes t-PA
that carry sialic acid as their sole charged group are bi-antennary, core
fucosylated, with terminal N-acetylgalactosamine residues. We also report the
characterization of a series of related and previously unidentified sialylated
glycans. Further we show that Bowes t-PA expresses glucuronic acid/sulphate
containing N-linked glycans and is recognized by anti-carbohydrate L2/HNK-1
monoclonal antibodies. The presence on Bowes t-PA of glycans associated primarily
with the nervous system is consistent with its expression in a cell line of
neuroectodermal origin.
FAU - Jaques, A J
AU - Jaques AJ
AD - Biochemistry Department, Oxford University, U.K.
FAU - Opdenakker, G
AU - Opdenakker G
FAU - Rademacher, T W
AU - Rademacher TW
FAU - Dwek, R A
AU - Dwek RA
FAU - Zamze, S E
AU - Zamze SE
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 (CD57 Antigens)
RN - 0 (Epitopes)
RN - 0 (Glucuronates)
RN - 0 (Lectins)
RN - 0 (Oligosaccharides)
RN - 0 (Polysaccharides)
RN - 0 (Sialic Acids)
RN - 0 (Sulfates)
RN - 110231-93-1 (glucuronic acid 3-sulfate)
RN - EC 3.4.21.68 (Tissue Plasminogen Activator)
RN - GZP2782OP0 (N-Acetylneuraminic Acid)
SB - IM
MH - Antibodies, Monoclonal/immunology
MH - Blotting, Western
MH - CD57 Antigens/immunology
MH - Carbohydrate Sequence
MH - Chromatography, Affinity
MH - Chromatography, Gel
MH - Chromatography, Ion Exchange
MH - Electrophoresis, Paper
MH - Epitopes/chemistry
MH - Gas Chromatography-Mass Spectrometry
MH - Glucuronates/analysis
MH - Glycosylation
MH - Lectins/metabolism
MH - Melanoma, Experimental/*chemistry
MH - Molecular Sequence Data
MH - N-Acetylneuraminic Acid
MH - Oligosaccharides/analysis/chemistry
MH - Polysaccharides/*analysis
MH - Sialic Acids/metabolism
MH - Sulfates/analysis
MH - Tissue Plasminogen Activator/*chemistry/metabolism
MH - Tumor Cells, Cultured
PMC - PMC1217368
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]
PST - ppublish
SO - Biochem J. 1996 Jun 1;316 ( Pt 2):427-37.
PMID- 4091823
OWN - NLM
STAT- MEDLINE
DCOM- 19860326
LR - 20181113
IS - 0264-6021 (Print)
IS - 0264-6021 (Linking)
VI - 232
IP - 3
DP - 1985 Dec 15
TI - Comparative study of glycophorin A derived O-glycans from human Cad, Sd(a+) and
Sd(a-) erythrocytes.
PG - 813-8
AB - Glycophorin A was purified from the erythrocyte membranes of blood group Cad,
Sd(a+) and Sd(a-) donors and the oligosaccharide alditols, obtained after
alkaline borohydride degradation, separated by h.p.l.c. on an alkylamine silica
gel column, were characterized by sugar analysis. Structure determination of the
major acid components by methylation analysis, g.l.c.-m.s. and 1H-n.m.r.
indicated that the three blood group Cad red cells under study (samples Cad.,
Bui. and Des.) carry the same pentasaccharide GalNAc(beta 1-4)[NeuAc(alpha
2-3)]Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc -ol(Cad determinant) but in different
amounts. This pentasaccharide, however, was absent from glycophorin A of Sd(a+)
and Sd (a-) donors, suggesting that the Sda determinant is not associated with
glycophorins. It was calculated that glycophorin A from the original Cad donor
(Cad.) carries about 12 O-glycosidically linked pentasaccharide chains per
molecule whereas only 2-3 of these chains were present in the samples from the
two other unrelated Cad individuals (Bui. and Des.) It is well known from
quantitative agglutination studies that the proportion of red cells which can be
agglutinated by the Dolichos biflorus lectin varies from one Cad blood sample to
another. Some are completely agglutinated (Cad. donor) whereas others are only
partially agglutinated (Bui. and Des. donors) suggesting that some red cells
might not carry the Cad determinants. From the results presented above and sodium
dodecyl sulphate/polyacrylamide-gel electrophoresis studies it is suggested that
Cad red cells from Bui. and Des. do not carry a mixture of glycophorin A
molecules with or without the Cad pentasaccharides but a spectrum of glycoprotein
molecules with varying amounts of Cad determinants.
FAU - Blanchard, D
AU - Blanchard D
FAU - Capon, C
AU - Capon C
FAU - Leroy, Y
AU - Leroy Y
FAU - Cartron, J P
AU - Cartron JP
FAU - Fournet, B
AU - Fournet B
LA - eng
PT - Comparative Study
PT - Journal Article
PL - England
TA - Biochem J
JT - The Biochemical journal
JID - 2984726R
RN - 0 (Blood Group Antigens)
RN - 0 (Borohydrides)
RN - 0 (Carbohydrates)
RN - 0 (Glycophorin)
RN - 0 (Oligosaccharides)
RN - 0 (Sialoglycoproteins)
RN - 0 (Sugar Alcohols)
SB - IM
MH - *Blood Group Antigens
MH - Borohydrides
MH - Carbohydrates/analysis
MH - Chromatography, High Pressure Liquid
MH - Electrophoresis, Polyacrylamide Gel
MH - Erythrocyte Membrane/*analysis
MH - *Glycophorin/metabolism
MH - Humans
MH - Oligosaccharides/*analysis
MH - *Sialoglycoproteins/metabolism
MH - Sugar Alcohols/*analysis
PMC - PMC1152955
EDAT- 1985/12/15 00:00
MHDA- 1985/12/15 00:01
CRDT- 1985/12/15 00:00
PHST- 1985/12/15 00:00 [pubmed]
PHST- 1985/12/15 00:01 [medline]
PHST- 1985/12/15 00:00 [entrez]
PST - ppublish
SO - Biochem J. 1985 Dec 15;232(3):813-8.
PMID- 2015821
OWN - NLM
STAT- MEDLINE
DCOM- 19910523
LR - 20161017
IS - 0014-2956 (Print)
IS - 0014-2956 (Linking)
VI - 197
IP - 1
DP - 1991 Apr 10
TI - Structure determination of the glycans of human-serum alpha 1-antichymotrypsin
using 1H-NMR spectroscopy and deglycosylation by N-glycanase.
PG - 209-15
AB - alpha 1-Antichymotrypsin purified from normal human serum was separated by
affinity chromatography into th ree microheterogeneous forms on a
concanavalin-A-Sepharose column: a pass-through (peak 1), a retarded (peak 2) and
a bound form (peaks 3 + 4). For each form the asparagine-linked carbohydrate
chains were liberated as oligosaccharides by hydrazinolysis, submitted to
reduction with NaBH4 after re-N-acetylation and further separated by affinity
chromatography on a concanavalin-A-Sepharose column. The complete primary
structure of the glycans was determined by high-resolution 1H-NMR spectroscopy.
The results indicated the presence of disialyl diantennary and of trisialyl
triantennary type glycanic structures, the latter being accompanied by traces of
disialylated triantennary oligosaccharide. The N-glycanase was used for the
deglycosylation of the unfractionated alpha 1-antichymotrypsin; the successive
removal of the N-linked complex-type oligosaccharide side chains of alpha
1-antichymotrypsin was studied in the presence of detergents. From these
experiments it is concluded that alpha 1-antichymotrypsin carries four
oligosaccharide side chains. Moreover our results show that the peak 1 contains
four triantennary glycans, the peak 2 three triantennary and one diantennary
glycans while the bound peaks 3 + 4 possess, on average, about one triantennary
and three diantennary glycans per molecule. Since we showed that the peak 4
contains mostly diantennary glycans, it can be deduced that in peak 3 there are
molecules carrying two triantennary and two diantennary glycans and others
carrying one triantennary and three diantennary glycans.
FAU - Laine, A
AU - Laine A
AD - Unite 16 INSERM, Lille, France.
FAU - Hachulla, E
AU - Hachulla E
FAU - Strecker, G
AU - Strecker G
FAU - Michalski, J C
AU - Michalski JC
FAU - Wieruszeski, J M
AU - Wieruszeski JM
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 - 0 (alpha 1-Antichymotrypsin)
RN - 0 (alpha 1-Antitrypsin)
RN - 7006-34-0 (Asparagine)
RN - 7YNJ3PO35Z (Hydrogen)
RN - EC 3.5.- (Amidohydrolases)
RN - EC 3.5.1.52 (Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase)
SB - IM
MH - Amidohydrolases
MH - Asparagine
MH - Carbohydrate Conformation
MH - Carbohydrate Sequence
MH - Chromatography, Affinity
MH - Humans
MH - Hydrogen
MH - Immunoelectrophoresis, Two-Dimensional
MH - Magnetic Resonance Spectroscopy/methods
MH - Molecular Sequence Data
MH - Oligosaccharides/*chemistry/isolation & purification
MH - Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase
MH - Polysaccharides/*chemistry/isolation & purification
MH - alpha 1-Antichymotrypsin/*chemistry/isolation & purification
MH - alpha 1-Antitrypsin/chemistry/isolation & purification
EDAT- 1991/04/10 00:00
MHDA- 1991/04/10 00:01
CRDT- 1991/04/10 00:00
PHST- 1991/04/10 00:00 [pubmed]
PHST- 1991/04/10 00:01 [medline]
PHST- 1991/04/10 00:00 [entrez]
PST - ppublish
SO - Eur J Biochem. 1991 Apr 10;197(1):209-15.
PMID- 7096333
OWN - NLM
STAT- MEDLINE
DCOM- 19820917
LR - 20071114
IS - 0021-9258 (Print)
IS - 0021-9258 (Linking)
VI - 257
IP - 15
DP - 1982 Aug 10
TI - The structures and microheterogeneity of the carbohydrate chains of human plasma
ceruloplasmin. A study employing 500-MHz 1H-NMR spectroscopy.
PG - 8755-60
FAU - Endo, M
AU - Endo M
FAU - Suzuki, K
AU - Suzuki K
FAU - Schmid, K
AU - Schmid K
FAU - Fournet, B
AU - Fournet B
FAU - Karamanos, Y
AU - Karamanos Y
FAU - Montreuil, J
AU - Montreuil J
FAU - Dorland, L
AU - Dorland L
FAU - van Halbeek, H
AU - van Halbeek H
FAU - Vliegenthart, J F
AU - Vliegenthart JF
LA - eng
GR - GM-10374/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 - EC 1.16.3.1 (Ceruloplasmin)
SB - IM
MH - Carbohydrate Sequence
MH - *Ceruloplasmin
MH - Humans
MH - Magnetic Resonance Spectroscopy
EDAT- 1982/08/10 00:00
MHDA- 1982/08/10 00:01
CRDT- 1982/08/10 00:00
PHST- 1982/08/10 00:00 [pubmed]
PHST- 1982/08/10 00:01 [medline]
PHST- 1982/08/10 00:00 [entrez]
PST - ppublish
SO - J Biol Chem. 1982 Aug 10;257(15):8755-60.
PMID- 1898343
OWN - NLM
STAT- MEDLINE
DCOM- 19911021
LR - 20181113
IS - 0264-6021 (Print)
IS - 0264-6021 (Linking)
VI - 278 ( Pt 2)
DP - 1991 Sep 1
TI - Carbohydrate structure of human pancreatic elastase 1.
PG - 505-14
AB - Human pancreatic elastase 1 (E1) is a glycoprotein containing two potential
N-glycosylation sites, one of which carries a carbohydrate moiety [Wendorf,
Geyer, Sziegoleit & Linder (1989) FEBS Lett. 249, 275-278]. In order to study its
glycosylation, glycoprotein isolated from post-mortem pancreas tissue of 75
donors was digested with trypsin. Oligosaccharides were liberated from resulting
glycopeptides by treatment with
peptide-N4-(N-acetyl-beta-glycosaminyl)-asparagine amidase F, radiolabelled by
reduction with KB3H4 and separated by h.p.l.c. and gel filtration. Major
oligosaccharide alditol fractions, representing 67.8 mol% of total glycans, were
characterized by methylation analysis and sequential degradation with
exoglycosidases. The results revealed that about two-fifths of the partially
truncated, mainly biantennary, complex-type glycans found comprised blood group
A, B, Lea (or X), difucosyl A or difucosyl B determinants, which could be
assigned to lactosamine antennae linked to Man(alpha 1-3)- residues of the sugar
chains.
FAU - Wendorf, P
AU - Wendorf P
AD - Institut fur Medizinische Mikrobiologie, Universitat Giessen, Federal Republic of
Germany.
FAU - Linder, D
AU - Linder D
FAU - Sziegoleit, A
AU - Sziegoleit A
FAU - Geyer, R
AU - Geyer 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 (Glycopeptides)
RN - 0 (Oligosaccharides)
RN - 0 (Sugar Alcohols)
RN - EC 3.4.21.36 (Pancreatic Elastase)
RN - EC 3.4.21.4 (Trypsin)
SB - IM
MH - Carbohydrate Conformation
MH - Carbohydrate Sequence
MH - Chromatography, Liquid
MH - Electrophoresis, Polyacrylamide Gel
MH - Glycopeptides/metabolism
MH - Glycosylation
MH - Humans
MH - Hydrogen-Ion Concentration
MH - Methylation
MH - Molecular Sequence Data
MH - Oligosaccharides/*chemistry/metabolism
MH - Pancreas/*enzymology
MH - Pancreatic Elastase/*chemistry/isolation & purification
MH - Sugar Alcohols/chemistry
MH - Trypsin/chemistry
PMC - PMC1151374
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 - Biochem J. 1991 Sep 1;278 ( Pt 2):505-14.
PMID- 9852066
OWN - NLM
STAT- MEDLINE
DCOM- 19990126
LR - 20151119
IS - 0021-9258 (Print)
IS - 0021-9258 (Linking)
VI - 273
IP - 51
DP - 1998 Dec 18
TI - Phosphorylation and O-glycosylation sites of human chromogranin A (CGA79-439)
from urine of patients with carcinoid tumors.
PG - 34087-97
AB - Because of their water-soluble properties, chromogranins (CGs) and
chromogranin-derived fragments are released together with catecholamines from
adrenal chromaffin cells during stress situations and can be detected in the
blood by radiochemical and enzyme assays. It is well known that chromogranins can
serve as immunocytochemical markers for neuroendocrine tissues and as a
diagnostic tool for neuroendocrine tumors. In 1993, large CGA-derived fragments
have been shown to be excreted into the urine in patients with carcinoid tumors
and the present study deals with the characterization of the post-translational
modifications (phosphorylation and O-glycosylation) located along the largest
natural CGA-derived fragment CGA79-439. Using mild proteolysis of peptidic
material, high performance liquid chromatography, sequencing, and mass
spectrometry analysis, six post-translational modifications were detected along
the C-terminal CGA-derived fragment CGA79-439. Three O-linked glycosylation sites
were located in the core of the protein on Thr163, Thr165, and Thr233, consisting
in di-, tri-, and tetrasaccharides. Three phosphorylation sites were located in
the middle and C-terminal domain, on serine residues Ser200, Ser252, and Ser315.
These modified sites were compared with sequences of others species and discussed
in relation with the post-translational modifications that we have reported
previously for bovine CGA.
FAU - Gadroy, P
AU - Gadroy P
AD - INSERM, Unite 338, Biologie de la Communication Cellulaire, 67084 Strasbourg,
France.
FAU - Stridsberg, M
AU - Stridsberg M
FAU - Capon, C
AU - Capon C
FAU - Michalski, J C
AU - Michalski JC
FAU - Strub, J M
AU - Strub JM
FAU - Van Dorsselaer, A
AU - Van Dorsselaer A
FAU - Aunis, D
AU - Aunis D
FAU - Metz-Boutigue, M H
AU - Metz-Boutigue MH
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 (Biomarkers, Tumor)
RN - 0 (CHGA protein, human)
RN - 0 (Chromogranin A)
RN - 0 (Chromogranins)
RN - 0 (Glycopeptides)
RN - 0 (Peptide Fragments)
RN - 0 (Phosphopeptides)
SB - IM
MH - Amino Acid Sequence
MH - Animals
MH - Biomarkers, Tumor/urine
MH - Carcinoid Tumor/secondary/*urine
MH - Cattle
MH - Chromatography, High Pressure Liquid
MH - Chromogranin A
MH - Chromogranins/*chemistry/*metabolism/urine
MH - Glycopeptides/chemistry/isolation & purification
MH - Glycosylation
MH - Humans
MH - Liver Neoplasms/secondary/urine
MH - Molecular Sequence Data
MH - Peptide Fragments/chemistry/ultrastructure
MH - Phosphopeptides/chemistry/isolation & purification
MH - Phosphorylation
MH - *Protein Processing, Post-Translational
MH - Sequence Alignment
MH - Sequence Homology, Amino Acid
MH - Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
EDAT- 1998/12/16 00:00
MHDA- 1998/12/16 00:01
CRDT- 1998/12/16 00:00
PHST- 1998/12/16 00:00 [pubmed]
PHST- 1998/12/16 00:01 [medline]
PHST- 1998/12/16 00:00 [entrez]
PST - ppublish
SO - J Biol Chem. 1998 Dec 18;273(51):34087-97.
PMID- 29741879
OWN - NLM
STAT- MEDLINE
DCOM- 20190404
LR - 20190404
IS - 1520-6882 (Electronic)
IS - 0003-2700 (Linking)
VI - 90
IP - 13
DP - 2018 Jul 3
TI - Reanalysis of Global Proteomic and Phosphoproteomic Data Identified a Large
Number of Glycopeptides.
PG - 8065-8071
LID - 10.1021/acs.analchem.8b01137 [doi]
AB - Protein glycosylation plays fundamental roles in many cellular processes, and
previous reports have shown dysregulation to be associated with several human
diseases, including diabetes, cancer, and neurodegenerative disorders. Despite
the vital role of glycosylation for proper protein function, the analysis of
glycoproteins has been lagged behind to other protein modifications. In this
study, we describe the reanalysis of global proteomic data from breast cancer
xenograft tissues using recently developed software package GPQuest 2.0,
revealing a large number of previously unidentified N-linked glycopeptides. More
importantly, we found that using immobilized metal affinity chromatography (IMAC)
technology for the enrichment of phosphopeptides had coenriched a substantial
number of sialoglycopeptides, allowing for a large-scale analysis of
sialoglycopeptides in conjunction with the analysis of phosphopeptides.
Collectively, combined tandem mass spectrometry (MS/MS) analyses of global
proteomic and phosphoproteomic data sets resulted in the identification of 6724
N-linked glycopeptides from 617 glycoproteins derived from two breast cancer
xenograft tissues. Next, we utilized GPQuest 2.0 for the reanalysis of global and
phosphoproteomic data generated from 108 human breast cancer tissues that were
previously analyzed by Clinical Proteomic Analysis Consortium (CPTAC). Reanalysis
of the CPTAC data set resulted in the identification of 2683 glycopeptides from
the global proteomic data set and 4554 glycopeptides from phosphoproteomic data
set, respectively. Together, 11292 N-linked glycopeptides corresponding to 1731
N-linked glycosites from 883 human glycoproteins were identified from the two
data sets. This analysis revealed an extensive number of glycopeptides hidden in
the global and enriched in IMAC-based phosphopeptide-enriched proteomic data,
information which would have remained unknown from the original study otherwise.
The reanalysis described herein can be readily applied to identify glycopeptides
from already existing data sets, providing insight into many important facets of
protein glycosylation in different biological, physiological, and pathological
processes.
FAU - Hu, Yingwei
AU - Hu Y
AUID- ORCID: 0000-0002-4629-0985
AD - Department of Pathology , Johns Hopkins University , Baltimore , Maryland 21287 ,
United States.
FAU - Shah, Punit
AU - Shah P
AD - Department of Pathology , Johns Hopkins University , Baltimore , Maryland 21287 ,
United States.
FAU - Clark, David J
AU - Clark DJ
AUID- ORCID: 0000-0003-0527-8469
AD - Department of Pathology , Johns Hopkins University , Baltimore , Maryland 21287 ,
United States.
FAU - Ao, Minghui
AU - Ao M
AD - Department of Pathology , Johns Hopkins University , Baltimore , Maryland 21287 ,
United States.
FAU - Zhang, Hui
AU - Zhang H
AUID- ORCID: 0000-0001-8726-7098
AD - Department of Pathology , Johns Hopkins University , Baltimore , Maryland 21287 ,
United States.
LA - eng
GR - U01 CA152813/CA/NCI NIH HHS/United States
GR - U24 CA210985/CA/NCI NIH HHS/United States
PT - Journal Article
PT - Research Support, N.I.H., Extramural
DEP - 20180611
PL - United States
TA - Anal Chem
JT - Analytical chemistry
JID - 0370536
RN - 0 (Glycopeptides)
RN - 0 (Phosphopeptides)
SB - IM
MH - Animals
MH - Cell Line, Tumor
MH - Cell Transformation, Neoplastic
MH - Chromatography, Affinity
MH - Female
MH - Glycopeptides/*metabolism
MH - Humans
MH - Mammary Neoplasms, Experimental/metabolism
MH - Mice
MH - Phosphopeptides/*metabolism
MH - Proteomics/*methods
PMC - PMC6440470
MID - NIHMS1014734
EDAT- 2018/05/10 06:00
MHDA- 2019/04/05 06:00
CRDT- 2018/05/10 06:00
PHST- 2018/05/10 06:00 [pubmed]
PHST- 2019/04/05 06:00 [medline]
PHST- 2018/05/10 06:00 [entrez]
AID - 10.1021/acs.analchem.8b01137 [doi]
PST - ppublish
SO - Anal Chem. 2018 Jul 3;90(13):8065-8071. doi: 10.1021/acs.analchem.8b01137. Epub
2018 Jun 11.
PMID- 1421757
OWN - NLM
STAT- MEDLINE
DCOM- 19921218
LR - 20131121
IS - 0959-6658 (Print)
IS - 0959-6658 (Linking)
VI - 2
IP - 4
DP - 1992 Aug
TI - Identification of the O-linked glycosylation site of the human transferrin
receptor.
PG - 355-9
AB - The human transferrin receptor is a glycoprotein containing three N-linked and
one O-linked glycosylation sites. Tryptic digestion of the receptor, followed by
chromatography on BioGel P-2 and reverse-phase HPLC, yields a glycopeptide (amino
acids 101-120) containing the O-linked site. Amino acid sequence analysis reveals
that the site of O-glycosylation is Thr-104. Mass spectral analysis is consistent
with the presence of a Gal-GalNAc core with predominantly two sialic acid
residues.
FAU - Hayes, G R
AU - Hayes GR
AD - Department of Biochemistry and Molecular Biology, SUNY Health Science Center,
Syracuse 13210.
FAU - Enns, C A
AU - Enns CA
FAU - Lucas, J J
AU - Lucas JJ
LA - eng
GR - GM 43111/GM/NIGMS NIH HHS/United States
GR - RR0317/RR/NCRR 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 (Glycoproteins)
RN - 0 (Peptide Fragments)
RN - 0 (Receptors, Transferrin)
RN - 2ZD004190S (Threonine)
RN - EC 3.4.21.4 (Trypsin)
SB - IM
MH - Amino Acid Sequence
MH - Binding Sites
MH - Carbohydrate Conformation
MH - Female
MH - Glycoproteins/*chemistry
MH - Glycosylation
MH - Humans
MH - Mass Spectrometry
MH - Molecular Sequence Data
MH - Peptide Fragments/chemistry
MH - Placenta/chemistry
MH - Receptors, Transferrin/*chemistry
MH - Threonine/metabolism
MH - Trypsin
EDAT- 1992/08/01 00:00
MHDA- 1992/08/01 00:01
CRDT- 1992/08/01 00:00
PHST- 1992/08/01 00:00 [pubmed]
PHST- 1992/08/01 00:01 [medline]
PHST- 1992/08/01 00:00 [entrez]
PST - ppublish
SO - Glycobiology. 1992 Aug;2(4):355-9.
PMID- 6619126
OWN - NLM
STAT- MEDLINE
DCOM- 19831123
LR - 20081121
IS - 0021-9258 (Print)
IS - 0021-9258 (Linking)
VI - 258
IP - 19
DP - 1983 Oct 10
TI - A carbohydrate structural variant of MM glycoprotein (glycophorin A).
PG - 11537-45
AB - A variant of the MM glycoprotein (glycophorin A) was isolated from erythrocyte
membranes of two individual donors, a mother (L.G.) and daughter (V.W.). This
glycoprotein was found to be a carbohydrate variant in which, for both donors,
certain O-glycosidically linked saccharides retained the core structure
consisting of NeuAc(alpha 2,3)Gal(beta 1,3)GalNAc that is common to all O-linked
saccharides of the MN glycoproteins, and, in addition, contained substituents, of
varying chain lengths, on the primary carbinol of GalNAc. These saccharides were
released from the polypeptide by beta-elimination in the presence of sodium
borohydride, and aspects of their structure were investigated by glycosidase
digestion and periodate oxidation. Thus, the smallest variant structure was
deduced to be NeuAc(alpha 2,3)Gal(beta 1,3)[GlcNAc(beta 1,6)]H2GalNAc. The
6-O-linked GlcNAc appears to serve as the focus of further chain elongation
reactions, involving alternate additions of Gal and GlcNAc residues and leading
to the formation of several homologous structures. Two such structures,
NeuAc(alpha 2,3)Gal(beta 1,3)[GlcNAc(beta 1,?) Gal(beta 1,3/4)GlcNAc(beta
1,6)]H2GalNAc and NeuAc(alpha 2,3) Gal(beta 1,3)[Gal(beta 1,3/4)GlcNAc(beta
1,6)]H2GalNAc were the predominant species present. A larger saccharide was also
isolated and its partial sequence was determined to be Gal(beta 1,3/4)GlcNAc(beta
1,?)[Gal(beta 1,3/4)Glc-NAc(beta 1,?)] Gal(beta 1,3/4)GlcNAc(beta
1,6)[NeuAc(alpha 2,3)Gal-(beta 1,3)]H2GalNAc. Because the peptide portion of
these glycoproteins contains two methionine residues, it was possible to isolate
two CNBr glycopeptides from separate regions of the molecule, and to assess the
distribution of these variant structures in the polypeptide. The saccharides were
linked to about 2-3 Ser and/or Thr residues in the donor LG glycoprotein and one
of the attachment sites was located within the CNBr glycooctapeptide representing
the NH2 terminus. Considerable heterogeneity in saccharide structure was
documented for this site, and it is likely that such heterogeneity occurs also at
other sites. The variant saccharides bear structural similarities to the core
region of O-linked saccharides of certain blood group-active mucins and ovarian
cyst secretions, and to the outer sequences of N-linked carbohydrate units (I-,
i-active) of the major glycoprotein of human erythrocytes, band 3. The structures
of the variant saccharides suggest that they may be potential precursors of H
blood group-active carbohydrates, present in varying degrees of maturity, and
attached to an integral protein of erythrocytes.
FAU - Adamany, A M
AU - Adamany AM
FAU - Blumenfeld, O O
AU - Blumenfeld OO
FAU - Sabo, B
AU - Sabo B
FAU - McCreary, J
AU - McCreary J
LA - eng
GR - GM 16389/GM/NIGMS NIH HHS/United States
GR - HL 19011/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 Biol Chem
JT - The Journal of biological chemistry
JID - 2985121R
RN - 0 (Carbohydrates)
RN - 0 (Glycophorin)
RN - 0 (Oligosaccharides)
RN - 0 (Peptide Fragments)
RN - 0 (Sialic Acids)
RN - 0 (Sialoglycoproteins)
SB - IM
MH - Carbohydrate Conformation
MH - Carbohydrate Sequence
MH - Carbohydrates/analysis
MH - Erythrocyte Membrane/*analysis
MH - Female
MH - *Genetic Variation
MH - Glycophorin/*genetics/isolation & purification
MH - Hemagglutination
MH - Humans
MH - Oligosaccharides/*isolation & purification
MH - Peptide Fragments/analysis
MH - Sialic Acids/analysis
MH - Sialoglycoproteins/*genetics
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):11537-45.
PMID- 3179269
OWN - NLM
STAT- MEDLINE
DCOM- 19881222
LR - 20061115
IS - 0006-2960 (Print)
IS - 0006-2960 (Linking)
VI - 27
IP - 15
DP - 1988 Jul 26
TI - Comparative structural study of N-linked oligosaccharides of urinary and
recombinant erythropoietins.
PG - 5646-54
AB - The structures of the N-linked oligosaccharides of the urinary erythropoietin
(u-EPO) purified from urine of aplastic anemic patients were analyzed and
compared with those for recombinant erythropoietin (r-EPO) prepared with baby
hamster kidney (BHK) cells. Asparagine-linked neutral oligosaccharides were
released from each EPO protein by N-oligosaccharide glycopeptidase (almond)
digestion. The reducing ends of the oligosaccharide chains thus obtained were
aminated with a fluorescent reagent, 2-aminopyridine, and the mixture of
pyridylamino derivatives of the oligosaccharides was separated by
high-performance liquid chromatography (HPLC) on an ODS silica column. More than
8 and 13 kinds of oligosaccharide fractions for u-EPO and r-EPO (BHK),
respectively, were completely separated by the one-step HPLC procedure. The
structure of each oligosaccharide thus isolated was analyzed by a combination of
sequential exoglycosidase digestion and another kind of HPLC with an amide-silica
column. Furthermore, high-resolution proton nuclear magnetic resonance (1H NMR)
spectroscopy and methylation analyses were carried out in the case of r-EPO
(BHK).(ABSTRACT TRUNCATED AT 250 WORDS)
FAU - Tsuda, E
AU - Tsuda E
AD - Research Institute of Life Science, Snow Brand Milk Products Company Ltd.,
Tochigi, Japan.
FAU - Goto, M
AU - Goto M
FAU - Murakami, A
AU - Murakami A
FAU - Akai, K
AU - Akai K
FAU - Ueda, M
AU - Ueda M
FAU - Kawanishi, G
AU - Kawanishi G
FAU - Takahashi, N
AU - Takahashi N
FAU - Sasaki, R
AU - Sasaki R
FAU - Chiba, H
AU - Chiba H
FAU - Ishihara, H
AU - Ishihara H
AU - et al.
LA - eng
PT - Journal Article
PT - Research Support, Non-U.S. Gov't
PL - United States
TA - Biochemistry
JT - Biochemistry
JID - 0370623
RN - 0 (Glycoproteins)
RN - 0 (Oligosaccharides)
RN - 0 (Recombinant Proteins)
RN - 11096-26-7 (Erythropoietin)
SB - IM
MH - Carbohydrate Sequence
MH - Chromatography, High Pressure Liquid
MH - Erythropoietin/*analysis/urine
MH - Glycoproteins/*analysis
MH - Magnetic Resonance Spectroscopy
MH - Mass Spectrometry
MH - Molecular Sequence Data
MH - Oligosaccharides/*analysis
MH - Recombinant Proteins/analysis
EDAT- 1988/07/26 00:00
MHDA- 1988/07/26 00:01
CRDT- 1988/07/26 00:00
PHST- 1988/07/26 00:00 [pubmed]
PHST- 1988/07/26 00:01 [medline]
PHST- 1988/07/26 00:00 [entrez]
PST - ppublish
SO - Biochemistry. 1988 Jul 26;27(15):5646-54.
PMID- 10024660
OWN - NLM
STAT- MEDLINE
DCOM- 19990323
LR - 20071115
IS - 0959-6658 (Print)
IS - 0959-6658 (Linking)
VI - 9
IP - 3
DP - 1999 Mar
TI - Structural characterization of the N-linked oligosaccharides in bile
salt-stimulated lipase originated from human breast milk.
PG - 227-34
AB - The detailed structures of N- glycans derived from bile salt-stimulated lipase
(BSSL) found in human milk were determined by combining exoglycosidase digestion
with matrix-assisted laser desorption/ionization time-of-flight mass
spectrometry. The N- glycan structures were conclusively determined in terms of
complexity and degree of fucosylation. Ion-exchange chromatography with pulsed
amperometric detection, together with mass-spectral analysis of the esterified N-
glycans, indicated the presence of monosialylated structures. The molecular mass
profile of esterified N- glycans present in BSSL further permitted the more
detailed studies through collision-induced dissociation (CID) and sequential
exoglycosidase cleavages. The N- glycan structures were elucidated to be
complex/dibranched, fucosylated/complex/dibranched,
monosialylated/complex/dibranched, and monosialylated/fucosylated/dibranched
entities.
FAU - Mechref, Y
AU - Mechref Y
AD - Department of Chemistry, Indiana University, Bloomington, IN 47405, USA.
FAU - Chen, P
AU - Chen P
FAU - Novotny, M V
AU - Novotny MV
LA - eng
GR - GM24349/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 - England
TA - Glycobiology
JT - Glycobiology
JID - 9104124
RN - 0 (Glycoproteins)
RN - 0 (Oligosaccharides)
RN - 0 (alpha-Fetoproteins)
RN - EC 3.1.1.- (bile salt-stimulated lipase)
RN - EC 3.1.1.13 (Sterol Esterase)
SB - IM
MH - Carbohydrate Sequence
MH - Female
MH - Glycoproteins/*chemistry
MH - Humans
MH - Milk, Human/*enzymology
MH - Molecular Sequence Data
MH - Oligosaccharides/*chemistry
MH - Sequence Analysis
MH - Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
MH - Sterol Esterase/*chemistry
MH - alpha-Fetoproteins/chemistry
EDAT- 1999/02/20 00:00
MHDA- 1999/02/20 00:01
CRDT- 1999/02/20 00:00
PHST- 1999/02/20 00:00 [pubmed]
PHST- 1999/02/20 00:01 [medline]
PHST- 1999/02/20 00:00 [entrez]
AID - cwc019 [pii]
PST - ppublish
SO - Glycobiology. 1999 Mar;9(3):227-34.
PMID- 6833285
OWN - NLM
STAT- MEDLINE
DCOM- 19830527
LR - 20111117
IS - 0021-9258 (Print)
IS - 0021-9258 (Linking)
VI - 258
IP - 8
DP - 1983 Apr 25
TI - Characterization of the B-chain of human plasma alpha 2HS-glycoprotein. The
complete amino acid sequence and primary structure of its heteroglycan.
PG - 4966-71
AB - alpha 2HS-Glycoprotein, a normal human plasma protein, was recently shown to
consist of two polypeptide chains. In the present study, we have separated these
two chains from one another and have elucidated the complete primary structure of
the B-chain. Employing automated Edman degradation, the polypeptide moiety of
this chain was shown to consist of 27 amino acid residues with an unequal
distribution of the neutral and charged amino acid residues. The first 20
residues are uncharged, whereas the carboxyl-terminal heptapeptide contains all
charged residues. Utilizing 500-MHz 1H-NMR spectroscopy, the carbohydrate unit
proved to be a trisaccharide consisting of sialic acid, galactose, and
N-acetylgalactosamine O-glycosidically linked to serine (residue 6). The
structure of the B-chain was found to be as follows. (formula; see text) Thus,
the molecular weight of the B-chain is 3386. Evaluation of the polypeptide chain
by the procedure of Chou and Fasman (Chou, P.Y., and Fasman, G.D. (1979) Adv.
Enzymol. 47, 45-148) predicts that the B-chain has two beta-turns. Thereby, the
carbohydrate unit which is linked to the Ser residue located in the first
beta-turn appears to be directed away from the protein. The second beta-turn
probably includes the Cys residue which links the B- to the A-chain. In agreement
with the CD analysis, the B-chain lacks beta-conformation but possesses a short
alpha-helical region.
FAU - Gejyo, F
AU - Gejyo F
FAU - Chang, J L
AU - Chang JL
FAU - Burgi, W
AU - Burgi W
FAU - Schmid, K
AU - Schmid K
FAU - Offner, G D
AU - Offner GD
FAU - Troxler, R F
AU - Troxler RF
FAU - Van Halbeek, H
AU - Van Halbeek H
FAU - Dorland, L
AU - Dorland L
FAU - Gerwig, G J
AU - Gerwig GJ
FAU - Vliegenthart, J F
AU - Vliegenthart JF
LA - eng
GR - GM-10374/GM/NIGMS NIH HHS/United States
GR - HL-13262/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 (AHSG protein, human)
RN - 0 (Blood Proteins)
RN - 0 (Macromolecular Substances)
RN - 0 (alpha-2-HS-Glycoprotein)
SB - IM
MH - Amino Acid Sequence
MH - Blood Proteins/*analysis
MH - Carbohydrate Sequence
MH - Circular Dichroism
MH - Humans
MH - Macromolecular Substances
MH - Molecular Weight
MH - alpha-2-HS-Glycoprotein
EDAT- 1983/04/25 00:00
MHDA- 1983/04/25 00:01
CRDT- 1983/04/25 00:00
PHST- 1983/04/25 00:00 [pubmed]
PHST- 1983/04/25 00:01 [medline]
PHST- 1983/04/25 00:00 [entrez]
PST - ppublish
SO - J Biol Chem. 1983 Apr 25;258(8):4966-71.
PMID- 11180632
OWN - NLM
STAT- MEDLINE
DCOM- 20010405
LR - 20071114
IS - 1076-5174 (Print)
IS - 1076-5174 (Linking)
VI - 35
IP - 12
DP - 2000 Dec
TI - Structure of the asparagine-linked sugar chains of porcine kidney and human urine
cerebroside sulfate activator protein.
PG - 1416-24
AB - The specific sugar residues and their linkages in the oligosaccharides from pig
kidney and human urine cerebroside sulfate activator proteins (saposin B),
although previously hypothesized, have been unambiguously characterized.
Exhaustive sequential exoglycosidase digestion of the trimethyl-p-aminophenyl
derivatives, followed by either matrix-assisted laser desorption/ionization
and/or mass spectrometry, was used to define the residues and their linkages. The
oligosaccharides were enzymatically released from the proteins by treatment with
peptidyl-N-glycosidase F and separated from the proteins by reversed-phase
high-performance liquid chromatography (HPLC). Reducing termini were converted to
the trimethyl-p-aminophenyl derivative and the samples were further purified by
normal-phase HPLC. The derivatized carbohydrates were then treated sequentially
with a series of exoglycosidases of defined specificity, and the products of each
digestion were examined by mass spectrometry. The pentasaccharides from pig
kidney and human urine protein were shown to be of the asparagine-linked complex
type composed of mannose-alpha 1-6-mannose-beta
1-4-N-acetylglucosamine-N-acetylglucosamine(alpha 1-6-fucose). This highly
degraded structure probably represents the final product of intra-lysosomal
exoglycosidase digestion. Oligosaccharide sequencing by specific exoglycosidase
degradation coupled with mass spectrometry is more rapid than conventional
oligosaccharide sequencing. The procedures developed will be useful for
sequencing other oligosaccharides including those from other members of the
lipid-binding protein class to which cerebroside sulfate activator belongs. (c)
2000 John Wiley & Sons, Ltd.
FAU - Faull, K F
AU - Faull KF
AD - Department of Chemistry and Biochemistry, UCLA, Los Angeles, California, 90095,
USA. faull@chem.ucla.edu
FAU - Johnson, J
AU - Johnson J
FAU - Kim, M J
AU - Kim MJ
FAU - To, T
AU - To T
FAU - Whitelegge, J P
AU - Whitelegge JP
FAU - Stevens, R L
AU - Stevens RL
FAU - Fluharty, C B
AU - Fluharty CB
FAU - Fluharty, A L
AU - Fluharty AL
LA - eng
GR - NS31271/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 Mass Spectrom
JT - Journal of mass spectrometry : JMS
JID - 9504818
RN - 0 (Glycoproteins)
RN - 0 (PSAP protein, human)
RN - 0 (Saposins)
RN - 0 (Sphingolipid Activator Proteins)
RN - 7006-34-0 (Asparagine)
SB - IM
MH - Animals
MH - Asparagine/*chemistry
MH - *Carbohydrate Conformation
MH - Chromatography, High Pressure Liquid
MH - Glycoproteins/*chemistry/urine
MH - Humans
MH - Kidney/*chemistry
MH - Molecular Structure
MH - Saposins
MH - Spectrometry, Mass, Electrospray Ionization
MH - Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
MH - Sphingolipid Activator Proteins
MH - Swine
EDAT- 2001/02/17 11:00
MHDA- 2001/04/06 10:01
CRDT- 2001/02/17 11:00
PHST- 2001/02/17 11:00 [pubmed]
PHST- 2001/04/06 10:01 [medline]
PHST- 2001/02/17 11:00 [entrez]
AID - 10.1002/1096-9888(200012)35:12<1416::AID-JMS75>3.0.CO;2-K [pii]
AID - 10.1002/1096-9888(200012)35:12<1416::AID-JMS75>3.0.CO;2-K [doi]
PST - ppublish
SO - J Mass Spectrom. 2000 Dec;35(12):1416-24. doi:
10.1002/1096-9888(200012)35:12<1416::AID-JMS75>3.0.CO;2-K.
PMID- 3935432
OWN - NLM
STAT- MEDLINE
DCOM- 19860130
LR - 20161017
IS - 0014-2956 (Print)
IS - 0014-2956 (Linking)
VI - 153
IP - 2
DP - 1985 Dec 2
TI - Structures of the major carbohydrates of natural human interleukin-2.
PG - 255-61
AB - Purified human interleukin-2 secreted by peripheral blood lymphocytes from
healthy donors was found to exist in several forms. These forms were (partially)
resolved by reversed-phase high-performance liquid chromatography and sodium
dodecyl sulfate/polyacrylamide gel electrophoresis. Two major polypeptide species
(interleukin-2 N1 and N2, 16.5 kDa) were shown to be glycosylated on the basis of
[3H]galactose/[3H]glucosamine incorporation and determination of amino sugars
after acid hydrolysis. A third component (interleukin-2 M, 14.5 kDa) represents a
nonglycosylated form. The amino acid composition and the NH2-terminal sequence of
both forms are consistent with the data deduced from the cDNA coding for
interleukin-2 after removal of a leader peptide of 20 amino acids. Carbohydrates
are O-linked to the IL-2 protein via threonine-3 of the polypeptide chain. The
oligosaccharides were released by reductive beta-elimination and were purified by
gel filtration and high-performance liquid chromatography. Applying methylation
analysis, exoglycosidase digestion and fast atom bombardment mass spectrometry
the following major carbohydrate structures were identified: N1, NeuAc(alpha
2-3)Gal(beta 1-3)GalNAc-ol; and N2, NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha
2-6)]GalNAc-ol.
FAU - Conradt, H S
AU - Conradt HS
FAU - Geyer, R
AU - Geyer R
FAU - Hoppe, J
AU - Hoppe J
FAU - Grotjahn, L
AU - Grotjahn L
FAU - Plessing, A
AU - Plessing A
FAU - Mohr, H
AU - Mohr H
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 (Amino Acids)
RN - 0 (Carbohydrates)
RN - 0 (Interleukin-2)
RN - 37H9VM9WZL (Calcimycin)
RN - 9007-49-2 (DNA)
RN - NI40JAQ945 (Tetradecanoylphorbol Acetate)
SB - IM
MH - Amino Acid Sequence
MH - Amino Acids/analysis
MH - Binding Sites
MH - Calcimycin/pharmacology
MH - Carbohydrates/blood
MH - Chromatography, Gel
MH - Chromatography, High Pressure Liquid
MH - DNA/analysis
MH - Electrophoresis, Polyacrylamide Gel
MH - Humans
MH - Interleukin-2/*analysis
MH - Lymphocytes/metabolism
MH - Mass Spectrometry
MH - Methylation
MH - Tetradecanoylphorbol Acetate/pharmacology
EDAT- 1985/12/02 00:00
MHDA- 1985/12/02 00:01
CRDT- 1985/12/02 00:00
PHST- 1985/12/02 00:00 [pubmed]
PHST- 1985/12/02 00:01 [medline]
PHST- 1985/12/02 00:00 [entrez]
PST - ppublish
SO - Eur J Biochem. 1985 Dec 2;153(2):255-61.
PMID- 2550193
OWN - NLM
STAT- MEDLINE
DCOM- 19891026
LR - 20131121
IS - 0198-0238 (Print)
IS - 0198-0238 (Linking)
VI - 8
IP - 6
DP - 1989 Jul-Aug
TI - Recombinant human erythropoietin produced by Namalwa cells.
PG - 419-27
AB - To establish a practical exogenous gene expression system in human cells, a cDNA
coding for human erythropoietin (EPO) was expressed in human B-lymphoblastoid
Namalwa cells. The Namalwa-derived recombinant EPO was purified from the culture
fluid by a simple three-step procedure. The Namalwa EPO showed an equivalent
activity in vivo to that of human urinary EPO. Oligosaccharide structure analyses
suggested that almost all N-linked oligosaccharide chains of Namalwa EPO are
shared by urinary EPO. The two major N-linked oligosaccharides of Namalwa EPO
were fucose-containing tetraantennary and fucose-containing triantennary
structures.
FAU - Yanagi, H
AU - Yanagi H
AD - Takarazuka Research Center, Sumitomo Chemical Co., Ltd., Hyogo, Japan.
FAU - Yoshima, T
AU - Yoshima T
FAU - Ogawa, I
AU - Ogawa I
FAU - Okamoto, M
AU - Okamoto M
LA - eng
PT - Journal Article
PL - United States
TA - DNA
JT - DNA (Mary Ann Liebert, Inc.)
JID - 8302432
RN - 0 (Hydroxyapatites)
RN - 0 (Oligosaccharides)
RN - 0 (Recombinant Proteins)
RN - 11096-26-7 (Erythropoietin)
RN - 9007-49-2 (DNA)
RN - 91D9GV0Z28 (Durapatite)
RN - E1UOL152H7 (Iron)
SB - IM
MH - Animals
MH - Carbohydrate Sequence
MH - Cell Line
MH - Chromatography
MH - Chromatography, Affinity
MH - Chromatography, High Pressure Liquid
MH - DNA/genetics
MH - Durapatite
MH - Erythropoietin/*genetics/metabolism/pharmacology
MH - Humans
MH - Hydroxyapatites
MH - Iron/metabolism
MH - Liver/metabolism
MH - Mice
MH - Molecular Sequence Data
MH - Molecular Weight
MH - Oligosaccharides/isolation & purification
MH - Plasmids
MH - Rats
MH - Recombinant Proteins/isolation & purification/metabolism
MH - Restriction Mapping
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 - DNA. 1989 Jul-Aug;8(6):419-27.
PMID- 8404899
OWN - NLM
STAT- MEDLINE
DCOM- 19931103
LR - 20161017
IS - 0014-2956 (Print)
IS - 0014-2956 (Linking)
VI - 216
IP - 3
DP - 1993 Sep 15
TI - Variation of the glycosylation of human pancreatic bile-salt-dependent lipase.
PG - 807-12
AB - Glycoproteins of human pancreatic juice were characterized by means of lectins
after electrophoresis and electrotransfer to nitrocellulose membranes. For the
detected glycoproteins, only a 100-kDa glycoprotein varied in the pancreatic
juice from a normal patient (i.e. without any pancreatic disorder) compared to
the pancreatic juice from a patient suffering from chronic pancreatitis. This
protein, which is the only protein in human pancreatic juice which is
O-glycosylated and N-glycosylated, was identified as the bile-salt-dependent
lipase. Among the glycosylated proteins present in human pancreatic juice, only
the glycosylation of bile-salt-dependent lipase differs between individuals. The
enzyme was isolated either from normal or pathological human pancreatic juices.
The purified variants have an identical molecular mass and amino-acid
composition. As suspected from lectin affinity studies, the oligosaccharide
composition differs between the variants. The structure of the N-linked
oligosaccharides of the variant from the pancreatic juice of a normal donor
correlated with complete processing and maturation of a complex-type N-glycan.
Alteration of the maturation process can be detected for a
bile-salt-dependent-lipase variant from a patient suffering with chronic
pancreatitis, since the carbohydrate composition is compatible with the
predominance of hybrid or high-mannose-type structures. The amount of sugar
involved in O-glycosylation associated with the peanut agglutinin reactivity
suggests the presence of 12-14 minimal Gal beta 1-->3GalNac-->T/S O-glycan
structures which are sialylated and fucosylated. The amount of sugar involved in
the O-linked oligosaccharide structure appears to be unchanged in the variants
isolated from the pathological pancreatic juice.
FAU - Mas, E
AU - Mas E
AD - INSERM U260, Faculte de Medecine, Marseille, France.
FAU - Abouakil, N
AU - Abouakil N
FAU - Roudani, S
AU - Roudani S
FAU - Franc, J L
AU - Franc JL
FAU - Montreuil, J
AU - Montreuil J
FAU - Lombardo, D
AU - Lombardo D
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 (Bile Acids and Salts)
RN - 0 (Carbohydrates)
RN - 0 (Lectins)
RN - EC 3.1.1.3 (Lipase)
SB - IM
MH - Bile Acids and Salts/*metabolism
MH - Blotting, Western
MH - Carbohydrate Sequence
MH - Carbohydrates/analysis
MH - Electrophoresis, Polyacrylamide Gel
MH - Glycosylation
MH - Humans
MH - Lectins
MH - Lipase/chemistry/*metabolism
MH - Molecular Sequence Data
MH - Pancreatic Juice/*enzymology
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 - Eur J Biochem. 1993 Sep 15;216(3):807-12.
PMID- 8416919
OWN - NLM
STAT- MEDLINE
DCOM- 19930128
LR - 20131121
IS - 0021-9258 (Print)
IS - 0021-9258 (Linking)
VI - 268
IP - 1
DP - 1993 Jan 5
TI - Structural elucidation of a variety of GalNAc-containing N-linked
oligosaccharides from human urinary kallidinogenase.
PG - 113-26
AB - Fifteen different structures of terminal GalNAc-containing N-linked
oligosaccharides from human urinary kallidinogenase have been identified. These
N-linked oligosaccharides were mostly neutral, because sialic acid content was
lower than 0.13 mol of sialic acid/mol of sugar chain, and sulfate was not
detected. The oligosaccharides were released from pepsin-digested protein by
glycoamidase A (from almond) digestion. The reducing ends of the oligosaccharide
chains were aminated with a fluorescent reagent, 2-aminopyridine. The resulting
mixture of pyridylamino derivatives of the oligosaccharides were separated by
high performance liquid chromatography on an ODS-silica column, and 15
oligosaccharides were isolated. The structure of each oligosaccharide fraction
was analyzed by two-dimensional sugar mapping, component sugar analysis, high
resolution proton nuclear magnetic resonance and methylation analysis. It was
found that each N-linked oligosaccharide associated with human urinary
kallidinogenase contains unsubstituted GalNAc residues at the nonreducing
terminal. These 15 oligosaccharides include 5 biantennary, 7 triantennary, and 3
tetraantennary oligosaccharides.
FAU - Tomiya, N
AU - Tomiya N
AD - Mie Research Laboratory, Sanwa Kagaku Kenkyusho Co. Ltd., Japan.
FAU - Awaya, J
AU - Awaya J
FAU - Kurono, M
AU - Kurono M
FAU - Hanzawa, H
AU - Hanzawa H
FAU - Shimada, I
AU - Shimada I
FAU - Arata, Y
AU - Arata Y
FAU - Yoshida, T
AU - Yoshida T
FAU - Takahashi, N
AU - Takahashi N
LA - eng
PT - Journal Article
PL - United States
TA - J Biol Chem
JT - The Journal of biological chemistry
JID - 2985121R
RN - 0 (Indicators and Reagents)
RN - 0 (Oligosaccharides)
RN - EC 3.4.21.- (Kallikreins)
RN - KM15WK8O5T (Acetylgalactosamine)
SB - IM
MH - Acetylgalactosamine/*analysis
MH - Carbohydrate Conformation
MH - Carbohydrate Sequence
MH - Chromatography
MH - Gas Chromatography-Mass Spectrometry
MH - Humans
MH - Indicators and Reagents
MH - Kallikreins/chemistry/*urine
MH - Magnetic Resonance Spectroscopy
MH - Molecular Sequence Data
MH - Oligosaccharides/*chemistry/isolation & purification
EDAT- 1993/01/05 00:00
MHDA- 1993/01/05 00:01
CRDT- 1993/01/05 00:00
PHST- 1993/01/05 00:00 [pubmed]
PHST- 1993/01/05 00:01 [medline]
PHST- 1993/01/05 00:00 [entrez]
PST - ppublish
SO - J Biol Chem. 1993 Jan 5;268(1):113-26.
PMID- 2023947
OWN - NLM
STAT- MEDLINE
DCOM- 19910531
LR - 20181113
IS - 0027-8424 (Print)
IS - 0027-8424 (Linking)
VI - 88
IP - 9
DP - 1991 May 1
TI - Characterization of a posttranslational fucosylation in the growth factor domain
of urinary plasminogen activator.
PG - 3992-6
AB - A posttranslational modification site in natural and recombinant urinary-type
plasminogen activators (urokinases; EC 3.4.21.31) has been localized to Thr-18,
in the growth factor domain of the molecule. This is the region of urinary
plasminogen activator responsible for its specific receptor binding. An unusual
carbohydrate-protein linkage, a single monosaccharide, fucose, covalently
attached directly to threonine in the peptide, is described here. The glycan
moiety and the site of modification have been identified with mass spectrometry
and confirmed by carbohydrate composition analysis, Edman degradation, and one-
and two-dimensional NMR studies. This type of modification is normally not
detected without mass spectrometry because the fucose-threonine bond is
hydrolyzed under standard acidic conditions of the amino acid analysis and Edman
sequencing. This modification may be widely found in other proteins.
FAU - Buko, A M
AU - Buko AM
AD - Analytical Research Department, Abbott Laboratories, North Chicago, IL 60064.
FAU - Kentzer, E J
AU - Kentzer EJ
FAU - Petros, A
AU - Petros A
FAU - Menon, G
AU - Menon G
FAU - Zuiderweg, E R
AU - Zuiderweg ER
FAU - Sarin, V K
AU - Sarin VK
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 (Recombinant Proteins)
RN - 28RYY2IV3F (Fucose)
RN - EC 3.4.21.73 (Urokinase-Type Plasminogen Activator)
SB - IM
MH - Amino Acid Sequence
MH - Animals
MH - Cell Line
MH - Fucose/metabolism
MH - Glycosylation
MH - Magnetic Resonance Spectroscopy
MH - Mice
MH - Molecular Sequence Data
MH - Peptide Mapping
MH - Protein Processing, Post-Translational
MH - Recombinant Proteins/metabolism
MH - Urokinase-Type Plasminogen Activator/*metabolism
PMC - PMC51579
EDAT- 1991/05/01 00:00
MHDA- 1991/05/01 00:01
CRDT- 1991/05/01 00:00
PHST- 1991/05/01 00:00 [pubmed]
PHST- 1991/05/01 00:01 [medline]
PHST- 1991/05/01 00:00 [entrez]
PST - ppublish
SO - Proc Natl Acad Sci U S A. 1991 May 1;88(9):3992-6.
PMID- 2040275
OWN - NLM
STAT- MEDLINE
DCOM- 19910709
LR - 20161017
IS - 0014-2956 (Print)
IS - 0014-2956 (Linking)
VI - 198
IP - 1
DP - 1991 May 23
TI - The conformational effects of N-glycosylation on the tailpiece from serum IgM.
PG - 131-9
AB - 1H-NMR spectroscopy has been used to study the conformation and dynamics of the
isolated tailpiece from human serum immunoglobulin M, a 22-residue peptide
containing a single asparagine glycosylation site. The peptide is isolated as a
set of glycoforms, varying only in the sequence of the oligosaccharide attached
at the glycosylation site. The oligosaccharides present have the general formula
(Man)n(GlcNAc)2, with 45% having n = 6, 45% having n = 8 and 10% having n = 7
and/or 9. They have been identified and their NMR parameters compared to those
found for the isolated oligosaccharides in free solution. The conformation and
dynamics of the peptide component have also been studied, using NOE data and
hydrogen-exchange experiments, and the results compared to those obtained from
the aglycosyl peptide of the same sequence. The presence of the peptide is found
to have no measurable effect on the conformation of the oligosaccharides.
However, the presence of oligosaccharide causes a decrease in the conformational
mobility of the backbone and sidechains of the peptide in the region of the
glycosylation site. This is proposed to result from interactions between the
oligosaccharide core and the amino acid side chains. Further, the conformation of
the N-glycosidic linkage has been shown to be both rigid and planar. Thus, the
conformational space available to an N-linked oligosaccharide in a glycoprotein
relative to the protein may depend to a large extent upon the flexibility of the
asparagine side chain. Various roles for the different glycoforms of the tail
peptide are discussed.
FAU - Wormald, M R
AU - Wormald MR
AD - Department of Biochemistry, University of Oxford, England.
FAU - Wooten, E W
AU - Wooten EW
FAU - Bazzo, R
AU - Bazzo R
FAU - Edge, C J
AU - Edge CJ
FAU - Feinstein, A
AU - Feinstein A
FAU - Rademacher, T W
AU - Rademacher TW
FAU - Dwek, R A
AU - Dwek RA
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 (Immunoglobulin M)
RN - 0 (Oligosaccharides)
SB - IM
MH - Amino Acid Sequence
MH - Carbohydrate Conformation
MH - Glycosylation
MH - Humans
MH - Immunoglobulin M/*metabolism
MH - Magnetic Resonance Spectroscopy
MH - Molecular Sequence Data
MH - Oligosaccharides/chemistry
MH - Protein Conformation
EDAT- 1991/05/23 00:00
MHDA- 1991/05/23 00:01
CRDT- 1991/05/23 00:00
PHST- 1991/05/23 00:00 [pubmed]
PHST- 1991/05/23 00:01 [medline]
PHST- 1991/05/23 00:00 [entrez]
PST - ppublish
SO - Eur J Biochem. 1991 May 23;198(1):131-9.
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- 9654101
OWN - NLM
STAT- MEDLINE
DCOM- 19980717
LR - 20161017
IS - 0014-2956 (Print)
IS - 0014-2956 (Linking)
VI - 253
IP - 2
DP - 1998 Apr 15
TI - Structural characterisation of N-linked and O-linked oligosaccharides derived
from interferon-alpha2b and interferon-alpha14c produced by Sendai-virus-induced
human peripheral blood leukocytes.
PG - 485-93
AB - We have previously isolated and partially characterised the components of a
highly purified interferon-alpha (IFN-alpha) preparation produced by
Sendai-virus-induced human peripheral blood leukocytes. Nine IFN-alpha species
were identified, and two of these were found to be glycosylated [Nyman, T. A.,
Tolo, H., Parkkinen, J. & Kalkkinen, N. (1998) Identification of nine
interferon-alpha subtypes produced by Sendai-virus-induced human peripheral blood
leukocytes, Biochem. J. 329, 295-302]. Here, we isolated the N-linked
oligosaccharides of IFN-alpha14c and the O-linked chains of IFN-alpha2b, and the
glycans were characterised by electrospray tandem mass spectrometry and by
specific glycosidase digestions monitored by matrix-assisted laser desorption
ionisation time of flight mass spectrometry. The IFN-alpha14c N-glycans were
shown to exhibit core-fucosylated biantennary glycans, with about 10% carrying an
additional alpha1,3-linked fucose unit at the antennae. The IFN-alpha2b was shown
to carry about 50% core type-1 disialyltetrasaccharides, 30% core type-1
monosialyltrisaccharides and 20% core type-2 monosialylpentasaccharides.
FAU - Nyman, T A
AU - Nyman TA
AD - Institute of Biotechnology, Protein Chemistry Laboratory, University of Helsinki,
Finland.
FAU - Kalkkinen, N
AU - Kalkkinen N
FAU - Tolo, H
AU - Tolo H
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 (Interferon-alpha)
RN - 0 (Oligosaccharides)
RN - 0 (Polysaccharides)
SB - IM
MH - Glycosylation
MH - Humans
MH - Interferon-alpha/isolation & purification/*metabolism
MH - Leukocytes, Mononuclear/*metabolism/virology
MH - Mass Spectrometry
MH - Oligosaccharides/*chemistry/isolation & purification
MH - Polysaccharides/chemistry
MH - *Respirovirus
EDAT- 1998/07/08 00:00
MHDA- 1998/07/08 00:01
CRDT- 1998/07/08 00:00
PHST- 1998/07/08 00:00 [pubmed]
PHST- 1998/07/08 00:01 [medline]
PHST- 1998/07/08 00:00 [entrez]
PST - ppublish
SO - Eur J Biochem. 1998 Apr 15;253(2):485-93.
PMID- 10764840
OWN - NLM
STAT- MEDLINE
DCOM- 20000505
LR - 20131121
IS - 0959-6658 (Print)
IS - 0959-6658 (Linking)
VI - 10
IP - 5
DP - 2000 May
TI - Unusual N-glycosylation of a recombinant human erythropoietin expressed in a
human lymphoblastoid cell line does not alter its biological properties.
PG - 511-9
AB - Erythropoietin (Epo) is a 166 amino acids protein containing three
N-glycosylation sites (Asn-24, Asn-38, and Asn-83) and 1 O- glycosylation site
(Ser-126) and involved in the regulation of the level of red blood cells. Today,
only one recombinant human Epo (rHuEpo), produced in CHO cell line, is
extensively used in therapy to cure severe anemia. The structure of the glycan
chains of this rHuEpo slightly differ of those of the urinary human Epo (uHuEpo),
considered as the natural Epo molecule. In an attempt to produce a rHuEpo as
close as possible to the uHuEpo, Epo gene was expressed in a human lymphoblastoid
cell line, named RPMI 1788. In order to fully characterize the Epo-RPMI,
structural characterizations of the protein skeleton as well as glycan chains
were undergone. As expected, the amino acid sequence of the Epo-RPMI conformed to
that of uHuEpo. Surprisingly, the structure of some N-glycan chains, as mainly
determined by ESI-MS, revealed some unusual characteristics. Thus, 80% of
N-glycans possess a bisecting GlcNAc residue, 25% bear a second fucose residue
which is present, in a large part, in a sialyl Le(x)motif, and 13% contain more
than three LacNAc repeats (up to five per molecule). Despite these unusual
structural characteristics, the data concerning the in vitro and in vivo
biological activities were not impaired when compared to Epo-CHO and uHuEpo.
FAU - Cointe, D
AU - Cointe D
AD - Laboratoire de Glycobiologie Structurale et Fonctionnelle, Unite Mixte de
Recherche du CNRS No 8576, Universite des Sciences et Technologies de Lille,
F-59655 Villeneuve d'Ascq, France.
FAU - Beliard, R
AU - Beliard R
FAU - Jorieux, S
AU - Jorieux S
FAU - Leroy, Y
AU - Leroy Y
FAU - Glacet, A
AU - Glacet A
FAU - Verbert, A
AU - Verbert A
FAU - Bourel, D
AU - Bourel D
FAU - Chirat, F
AU - Chirat F
LA - eng
PT - Journal Article
PT - Research Support, Non-U.S. Gov't
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 (Glycopeptides)
RN - 0 (Monosaccharides)
RN - 0 (Oligosaccharides)
RN - 0 (Recombinant Proteins)
RN - 11096-26-7 (Erythropoietin)
RN - GZP2782OP0 (N-Acetylneuraminic Acid)
SB - IM
MH - Amino Acid Sequence
MH - Animals
MH - CHO Cells
MH - Cell Line
MH - Chemical Fractionation
MH - Cricetinae
MH - Erythropoietin/*chemistry/genetics/*metabolism
MH - Glycopeptides/analysis/isolation & purification
MH - Glycosylation
MH - Humans
MH - Lymphocytes/*metabolism
MH - Methylation
MH - Molecular Sequence Data
MH - Monosaccharides/analysis
MH - N-Acetylneuraminic Acid/metabolism
MH - Oligosaccharides/analysis
MH - Pharmacokinetics
MH - Recombinant Proteins
MH - Structure-Activity Relationship
EDAT- 2000/04/15 09:00
MHDA- 2000/05/16 09:00
CRDT- 2000/04/15 09:00
PHST- 2000/04/15 09:00 [pubmed]
PHST- 2000/05/16 09:00 [medline]
PHST- 2000/04/15 09:00 [entrez]
AID - cwd056 [pii]
PST - ppublish
SO - Glycobiology. 2000 May;10(5):511-9.
PMID- 2059624
OWN - NLM
STAT- MEDLINE
DCOM- 19910802
LR - 20131121
IS - 0006-2960 (Print)
IS - 0006-2960 (Linking)
VI - 30
IP - 25
DP - 1991 Jun 25
TI - Asparagine-linked oligosaccharide processing in lepidopteran insect cells.
Temporal dependence of the nature of the oligosaccharides assembled on
asparagine-289 of recombinant human plasminogen produced in baculovirus vector
infected Spodoptera frugiperda (IPLB-SF-21AE) cells.
PG - 6165-74
AB - Previous studies from this laboratory have established that lepidopteran insect
cells possess the glycosylation machinery needed to assemble N-linked
complex-type oligosaccharides on Asn289 of recombinant human plasminogen (r-HPg).
In the present paper, we show that the nature of N289-linked glycosylation of
[R561E]r-HPg expressed in Spodoptera frugiperda (IPLB-SF-21AE) cells is dependent
upon the length of time of infection of the cells with the recombinant
baculovirus/HPg-cDNA construct. At the earliest postinfection (p.i.) time period
studied, i.e., 0-20 h, virtually all (96%) of the oligosaccharides released with
glycopeptidase F from N289 of the expressed r-HPg were of the high-mannose type
and comprised nearly the full range of such structures, containing 3-9 mannose
units. At a time window of 60-96 h, p.i., essentially all of the oligosaccharides
(92% of the total) assembled on N289 of rHPg were of the biantennary,
triantennary, and tetraantennary complex classes, with varying extents of outer
arm completion. At an intermediate time period window, of 20-60 h, p.i., a
mixture of complex-type oligosaccharides, totaling approximately 77% of the
glycans, with various levels of branching and outer arm completion, and
high-mannose type of oligosaccharides, totaling approximately 23% of the glycans,
was assembled on N289 of the r-HPg produced. These studies demonstrate that
lepidopteran insect cells contain the glycosyltransferase genes required for
assembly of N-linked complex oligosaccharide and that these transferases are
utilized under proper conditions. The time dependency of the assembly of
complex-type oligosaccharides on r-HPg indicates that an activation of the
appropriate glycosyl transferases and/or transferase genes can take place. Thus,
one consequence of the infective process with the recombinant
baculovirus/HPg-cDNA construct is to alter the normal glycosylation
characteristics of insect cells and to allow complex-type oligosaccharide
processing to occur.
FAU - Davidson, D J
AU - Davidson DJ
AD - Department of Chemistry and Biochemistry, University of Notre Dame, Indiana
46556.
FAU - Castellino, F J
AU - Castellino FJ
LA - eng
GR - HL-13423/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 - Biochemistry
JT - Biochemistry
JID - 0370623
RN - 0 (Oligosaccharides)
RN - 0 (Recombinant Proteins)
RN - 7006-34-0 (Asparagine)
RN - 9001-91-6 (Plasminogen)
RN - 9007-49-2 (DNA)
RN - EC 2.4.1.- (Hexosyltransferases)
RN - EC 2.4.1.- (asparagine-N-glycosyltransferase)
RN - EC 3.2.1.- (Glycoside Hydrolases)
RN - EC 3.5.- (Amidohydrolases)
RN - EC 3.5.1.52 (Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase)
RN - PHA4727WTP (Mannose)
SB - IM
MH - Amidohydrolases/chemistry/metabolism
MH - Animals
MH - Asparagine/*metabolism
MH - Baculoviridae/genetics
MH - Carbohydrate Conformation
MH - Carbohydrate Sequence
MH - Cells, Cultured
MH - DNA/biosynthesis
MH - Gene Expression
MH - Genetic Vectors
MH - Glycoside Hydrolases/metabolism
MH - Glycosylation
MH - Hexosyltransferases/genetics
MH - Humans
MH - Hydrolysis
MH - Mannose/chemistry
MH - Molecular Sequence Data
MH - Moths/*genetics/metabolism/microbiology
MH - Oligosaccharides/*metabolism
MH - Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase
MH - Plasminogen/biosynthesis/chemistry/*genetics
MH - Recombinant Proteins
MH - Time Factors
EDAT- 1991/06/25 00:00
MHDA- 1991/06/25 00:01
CRDT- 1991/06/25 00:00
PHST- 1991/06/25 00:00 [pubmed]
PHST- 1991/06/25 00:01 [medline]
PHST- 1991/06/25 00:00 [entrez]
PST - ppublish
SO - Biochemistry. 1991 Jun 25;30(25):6165-74.
PMID- 8344278
OWN - NLM
STAT- MEDLINE
DCOM- 19930903
LR - 20161017
IS - 0014-2956 (Print)
IS - 0014-2956 (Linking)
VI - 215
IP - 1
DP - 1993 Jul 1
TI - Structural study of the oligosaccharide moieties of sphingolipid activator
proteins, saposins A, C and D obtained from the spleen of a Gaucher patient.
PG - 171-9
AB - We have determined and compared the structures of the oligosaccharide moieties of
saposin A, C and D purified from the spleen of a patient with Gaucher disease.
These saposins, together with saposin B, are small glycoproteins, derived from
separate domains of a single precursor, prosaposin, and are required for the
lysosomal hydrolysis of various sphingolipids. The characteristic features of the
oligosaccharide moieties of saposin A are (a) the predominance of a fucosylated
trimannosyl core structure and (b) the occurrence of several different
oligomannose-type and N-acetyllactosamine-type oligosaccharides. Saposin C
contains (a) a predominance of oligomannose-type oligosaccharides and
monoantennary oligosaccharides and (b) the presence of four different
oligosaccharides having bisecting N-acetylglucosamine residues (found only in
this saposin). Saposin D is distinguished by the occurrence of oligomannose-type
oligosaccharides, which comprise nearly 90% of its total oligosaccharides. The
possible reasons for the unique glycosylation of each saposin is discussed.
FAU - Ito, K
AU - Ito K
AD - Department of Neurology, Nagoya University School of Medicine, Aichi, Japan.
FAU - Takahashi, N
AU - Takahashi N
FAU - Takahashi, A
AU - Takahashi A
FAU - Shimada, I
AU - Shimada I
FAU - Arata, Y
AU - Arata Y
FAU - O'Brien, J S
AU - O'Brien JS
FAU - Kishimoto, Y
AU - Kishimoto Y
LA - eng
GR - NS-08682/NS/NINDS NIH HHS/United States
GR - NS-13559/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 - Eur J Biochem
JT - European journal of biochemistry
JID - 0107600
RN - 0 (Glycoproteins)
RN - 0 (Oligosaccharides)
RN - 0 (Saposins)
SB - IM
MH - Carbohydrate Sequence
MH - Gaucher Disease/*metabolism
MH - Glycoproteins/*chemistry
MH - Molecular Sequence Data
MH - Oligosaccharides/*chemistry
MH - Saposins
MH - Spleen/*chemistry
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]
PST - ppublish
SO - Eur J Biochem. 1993 Jul 1;215(1):171-9.
PMID- 2793860
OWN - NLM
STAT- MEDLINE
DCOM- 19891117
LR - 20060501
IS - 0021-9258 (Print)
IS - 0021-9258 (Linking)
VI - 264
IP - 29
DP - 1989 Oct 15
TI - Expression of human interleukin-2 in recombinant baby hamster kidney, Ltk-, and
Chinese hamster ovary cells. Structure of O-linked carbohydrate chains and their
location within the polypeptide.
PG - 17368-73
AB - The similarity or identity of O-glycosylation in glycoproteins from natural
sources or produced in heterologous cell lines, a central problem for the
development of many biotechnologically relevant production processes, was
examined using interleukin-2 (IL-2) as a model. Human interleukin-2 was
constitutively expressed in several mammalian cell lines in high amounts. The
recombinant proteins were purified to homogeneity and their carbohydrate
structures were analyzed. Only the NeuAc alpha 2-3Gal beta 1-3[NeuAc alpha
2-6]GalNAc oligosaccharide structure or the NeuAc alpha 2-3Gal beta 1-3GalNAc
were found in all IL-2 preparations secreted from recombinant Ltk-, Chinese
hamster ovary, and baby hamster kidney cell lines. The O-linked chains were
exclusively linked to Thr in position 3 of the polypeptide chain which is the
carbohydrate attachment site in natural human IL-2. The proportions of
O-glycosylated versus nonglycosylated forms of the protein secreted by each
recombinant cell line were independent of productivity or of cell culture
conditions. Our results show that O-glycosylated human IL-2 can be produced by
applying recombinant DNA technology in heterologous cell lines with the same type
of post-translational modification that is observed for the protein secreted from
natural T lymphocytes.
FAU - Conradt, H S
AU - Conradt HS
AD - Department of Cell Biology and Genetics, Gesellschaft fur Biotechnologische
Forschung mbH, Braunschweig, Federal Republic of Germany.
FAU - Nimtz, M
AU - Nimtz M
FAU - Dittmar, K E
AU - Dittmar KE
FAU - Lindenmaier, W
AU - Lindenmaier W
FAU - Hoppe, J
AU - Hoppe J
FAU - Hauser, H
AU - Hauser H
LA - eng
PT - Journal Article
PL - United States
TA - J Biol Chem
JT - The Journal of biological chemistry
JID - 2985121R
RN - 0 (Carbohydrates)
RN - 0 (Interleukin-2)
RN - 0 (Recombinant Proteins)
SB - IM
MH - Animals
MH - Carbohydrate Conformation
MH - Carbohydrate Sequence
MH - Carbohydrates/*analysis
MH - Cell Line
MH - Cloning, Molecular
MH - Cricetinae
MH - *Gene Expression
MH - Glycosylation
MH - Humans
MH - Interleukin-2/analysis/*genetics
MH - Plasmids
MH - Protein Processing, Post-Translational
MH - Recombinant Proteins/analysis/*genetics
MH - Transfection
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 - J Biol Chem. 1989 Oct 15;264(29):17368-73.
PMID- 1694115
OWN - NLM
STAT- MEDLINE
DCOM- 19900731
LR - 20041117
IS - 0009-9147 (Print)
IS - 0009-9147 (Linking)
VI - 36
IP - 6
DP - 1990 Jun
TI - Unique structure of glycopeptide from alpha-fetoprotein produced in human
hepatoma cell line, as determined by 1H-nuclear magnetic resonance spectroscopy.
PG - 879-82
AB - Determination of alpha-fetoprotein is used in diagnosis of tumors and neural tube
defects. A good reliable source of alpha-fetoprotein would be an obvious
advantage to the preparation of diagnostic reagents and their standardization. We
have recently developed a method for the production of alpha-fetoprotein from a
human hepatoma cell line. This method, which is suitable for scaling up, allowed
us to produce 40 g of alpha-fetoprotein from culture supernatant liquid through a
simple purification procedure. We have previously shown this protein to be
identical to alpha-fetoprotein produced from other sources. However, because the
presence of different glycoforms has been reported in alpha-fetoprotein
preparations, both from human sources and from other species, it was important to
establish the type and extent of glycosylation of alpha-fetoprotein prepared by
our method. By using 1H-NMR spectroscopy we were able to establish that our
product contains a single N-linked biantennary, fully sialylated complex-type
oligosaccharide, typical of human hepatomas.
FAU - Terrana, B
AU - Terrana B
AD - Centro Ricerche Sclavo, Siena, Italy.
FAU - Tecce, M F
AU - Tecce MF
FAU - Manetti, R
AU - Manetti R
FAU - Ceccarini, C
AU - Ceccarini C
FAU - Lamba, D
AU - Lamba D
FAU - Segre, A L
AU - Segre AL
LA - eng
PT - Journal Article
PL - United States
TA - Clin Chem
JT - Clinical chemistry
JID - 9421549
RN - 0 (Glycopeptides)
RN - 0 (Protons)
RN - 0 (alpha-Fetoproteins)
SB - IM
MH - Carcinoma, Hepatocellular/*analysis
MH - Cell Line
MH - Glycopeptides/*analysis
MH - Humans
MH - Liver Neoplasms/*analysis
MH - Magnetic Resonance Spectroscopy
MH - Protons
MH - alpha-Fetoproteins/*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]
PST - ppublish
SO - Clin Chem. 1990 Jun;36(6):879-82.
PMID- 6966283
OWN - NLM
STAT- MEDLINE
DCOM- 19800722
LR - 20061115
IS - 0021-9258 (Print)
IS - 0021-9258 (Linking)
VI - 255
IP - 9
DP - 1980 May 10
TI - Studies on the oligosaccharide chains of human alpha 1-protease inhibitor. II.
Structure of oligosaccharides.
PG - 4057-61
AB - Human alpha 1-protease inhibitor has three oligosaccharide side chains attached
to 3 separate asparaginyl residues of the protein by N-glycosyl linkages. Two of
the three asparaginyl residues link mostly to the A-type oligosaccharide chains
which consist of Man3, Gal2, (GlcNAc)4 and (NeuAc)2. One of the three asparaginyl
residues also attaches to a B-type oligosaccharide chain, which consists of Man3,
Gal3, (GlcNAc)5, and (NeuAc)3. The ratio of A-chain to B-chain in this particular
position is about 2:1. The structures of A- and B-chains of the glycoprotein were
examined by periodate oxidation, sequential glycosidase digestion, and
permethylation. The results unequivocally revealed the following structure for
A-chains. (Formula: see text). B-type oligosaccharide chains have an additional
trisaccharide, i.e. NeuAc 2 alpha leads to 3 Gal 1 beta leads to 4 GlcNAc
attached to mannose at the (a) and/or (b) position of A-type chains by a beta 1
leads to 4 linkage. The sialic acid of human alpha 1-protease inhibitor was
determined to be N-acetylneuraminic acid.
FAU - Mega, T
AU - Mega T
FAU - Lujan, E
AU - Lujan E
FAU - Yoshida, A
AU - Yoshida A
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 (Glycopeptides)
RN - 0 (Oligosaccharides)
RN - 0 (alpha 1-Antitrypsin)
SB - IM
MH - Carbohydrate Conformation
MH - Carbohydrate Sequence
MH - Glycopeptides/analysis
MH - Humans
MH - *Oligosaccharides
MH - *alpha 1-Antitrypsin
EDAT- 1980/05/10 00:00
MHDA- 1980/05/10 00:01
CRDT- 1980/05/10 00:00
PHST- 1980/05/10 00:00 [pubmed]
PHST- 1980/05/10 00:01 [medline]
PHST- 1980/05/10 00:00 [entrez]
PST - ppublish
SO - J Biol Chem. 1980 May 10;255(9):4057-61.
PMID- 6684483
OWN - NLM
STAT- MEDLINE
DCOM- 19831123
LR - 20161126
IS - 0006-3002 (Print)
IS - 0006-3002 (Linking)
VI - 760
IP - 1
DP - 1983 Oct 4
TI - Study of the carbohydrate moiety of human serum sex hormone-binding globulin.
PG - 104-10
AB - Sex hormone-binding globulin from human blood serum contains two biantennary
N-linked oligosaccharide chains of the N-acetyllactosamine type and one O-linked
oligosaccharide per one molecule of the glycoprotein. These conclusions have been
based on the results of methylation analysis of the whole glycoprotein and
investigation of the structures of its glycopeptides prepared using pronase
digestion.
FAU - Avvakumov, G V
AU - Avvakumov GV
FAU - Matveentseva, I V
AU - Matveentseva IV
FAU - Akhrem, L V
AU - Akhrem LV
FAU - Strel'chyonok, O A
AU - Strel'chyonok OA
FAU - Akhrem, A A
AU - Akhrem AA
LA - eng
PT - Journal Article
PL - Netherlands
TA - Biochim Biophys Acta
JT - Biochimica et biophysica acta
JID - 0217513
RN - 0 (Amino Acids)
RN - 0 (Carbohydrates)
RN - 0 (Glycopeptides)
RN - 0 (Sex Hormone-Binding Globulin)
RN - 11028-71-0 (Concanavalin A)
SB - IM
MH - Amino Acids/analysis
MH - Carbohydrates/analysis
MH - Chromatography, Affinity
MH - Concanavalin A
MH - Glycopeptides/analysis
MH - Humans
MH - Methylation
MH - Sex Hormone-Binding Globulin/*isolation & purification
EDAT- 1983/10/04 00:00
MHDA- 1983/10/04 00:01
CRDT- 1983/10/04 00:00
PHST- 1983/10/04 00:00 [pubmed]
PHST- 1983/10/04 00:01 [medline]
PHST- 1983/10/04 00:00 [entrez]
AID - 0304-4165(83)90130-7 [pii]
PST - ppublish
SO - Biochim Biophys Acta. 1983 Oct 4;760(1):104-10.
PMID- 6725284
OWN - NLM
STAT- MEDLINE
DCOM- 19840716
LR - 20071114
IS - 0021-9258 (Print)
IS - 0021-9258 (Linking)
VI - 259
IP - 11
DP - 1984 Jun 10
TI - The structure of the carbohydrate units of human plasma galactoglycoprotein
determined by 500-megahertz 1H NMR spectroscopy.
PG - 7151-4
AB - Human plasma galactoglycoprotein (Mr = 81,000) which was recently identified and
characterized (Schmid, K., Mao, S. K. Y., Kimura, A., Hayashi, S., and Binette ,
J. P. (1980) J. Biol. Chem. 255, 3221-3226) was found to possess an unusually
high carbohydrate content (76%) comprised of NeuAc, Gal, Man, Fuc, GalNAc, and
GlcNAc. The aim of the present investigation was to elucidate the primary
structure of the oligosaccharide units of this protein. For the study of the
O-glycosidic oligosaccharide chains, the protein was subjected to
beta-elimination and the resulting oligosaccharide preparations were analyzed by
500-MHz 1H NMR spectroscopy. The structure of the predominant glycan, a
hexasaccharide: (formula; see text) and that of a tetrasaccharide: NeuAc
alpha(2----3)Gal beta(1----3)[NeuAc alpha (2----6)]GalNAc-ol, were determined.
The protein possesses approximately 40 hexasaccharides and 3
tetrasaccharides/mol. For the isolation of its N-glycosidic oligosaccharide
chains, the protein was exhaustively digested with proteases followed by
chromatography of the desialyzed resulting glycopeptide fraction on concanavalin
A-Sepharose. 500-MHz 1H NMR spectroscopy of the obtained preparations revealed
the presence of 3 diantennary N-glycosidic chains that are extended with a Fuc
residue at the Asn-linked GlcNAc.
FAU - Akiyama, K
AU - Akiyama K
FAU - Simons, E R
AU - Simons ER
FAU - Bernasconi, P
AU - Bernasconi P
FAU - Schmid, K
AU - Schmid K
FAU - van Halbeek, H
AU - van Halbeek H
FAU - Vliegenthart, J F
AU - Vliegenthart JF
FAU - Haupt, H
AU - Haupt H
FAU - Schwick, H G
AU - Schwick HG
LA - eng
GR - GM-10374/GM/NIGMS NIH HHS/United States
GR - HL-15335/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 Biol Chem
JT - The Journal of biological chemistry
JID - 2985121R
RN - 0 (Glycoproteins)
SB - IM
MH - Carbohydrate Sequence
MH - *Glycoproteins
MH - Humans
MH - Magnetic Resonance Spectroscopy
EDAT- 1984/06/10 00:00
MHDA- 1984/06/10 00:01
CRDT- 1984/06/10 00:00
PHST- 1984/06/10 00:00 [pubmed]
PHST- 1984/06/10 00:01 [medline]
PHST- 1984/06/10 00:00 [entrez]
PST - ppublish
SO - J Biol Chem. 1984 Jun 10;259(11):7151-4.
PMID- 24841998
OWN - NLM
STAT- MEDLINE
DCOM- 20150309
LR - 20140801
IS - 1615-9861 (Electronic)
IS - 1615-9853 (Linking)
VI - 14
IP - 15
DP - 2014 Aug
TI - Comparison of sialylated N-glycopeptide levels in serum of pancreatic cancer
patients, acute pancreatitis patients, and healthy controls.
PG - 1713-23
LID - 10.1002/pmic.201300270 [doi]
AB - Serum protein glycosylation is known to be affected by pathological conditions,
including cancer and inflammatory diseases. Pancreatic cancer patients would
benefit from early diagnosis, as the disease is often detected in an advanced
stage and has poor prognosis. Searching for changes in serum protein
site-specific glycosylation could reveal novel glycoprotein biomarkers. We used
Sambucus nigra lectin affinity chromatography to enrich alpha-2,6 sialylated
tryptic N-glycopeptides from albumin-depleted sera of pancreatic cancer patients,
acute pancreatitis patients, and healthy individuals, and compared their relative
abundance using ultra performance LC-MS. Relative quantitation was done using the
spectrum processing software MZmine. Identification was performed on the
web-based tool GlycopeptideID, developed for in silico analysis of intact
N-glycopeptides. Seventeen high-abundance serum proteins, mainly acute-phase
proteins, and immunoglobulins, with total 27 N-glycosylation sites, and 62
glycoforms, were identified. Pancreatitis patient sera contained 38, and
pancreatic cancer patients sera contained 13 glycoform changes with statistical
significance (p < 0.05). In pancreatitis, up to tenfold changes were found in
some glycoforms, and in pancreatic cancer, threefold. Analysis showed that the
changes often concerned one or two, but not all, N-glycosylation sites in a
specific glycoprotein. In conclusion, the analysis shows that pancreatic cancer,
and acute pancreatitis are associated with changes in concentrations of intact
sialylated N-glycopeptides derived from acute-phase proteins, and
immunoglobulins, and that changes are site specific.
CI - (c) 2014 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
FAU - Kontro, Hilkka
AU - Kontro H
AD - Transplantation Laboratory, Haartman Institute, University of Helsinki, Helsinki,
Finland.
FAU - Joenvaara, Sakari
AU - Joenvaara S
FAU - Haglund, Caj
AU - Haglund C
FAU - Renkonen, Risto
AU - Renkonen R
LA - eng
PT - Comparative Study
PT - Journal Article
PT - Research Support, Non-U.S. Gov't
PL - Germany
TA - Proteomics
JT - Proteomics
JID - 101092707
RN - 0 (Glycopeptides)
RN - GZP2782OP0 (N-Acetylneuraminic Acid)
SB - IM
MH - Case-Control Studies
MH - Glycopeptides/*blood/*chemistry
MH - Humans
MH - N-Acetylneuraminic Acid
MH - Pancreatic Neoplasms/*blood
MH - Pancreatitis/*blood
OTO - NOTNLM
OT - Acute pancreatitis
OT - Glycoproteomics
OT - MS
OT - Pancreatic cancer
OT - Sialylation
OT - Technology
EDAT- 2014/05/21 06:00
MHDA- 2015/03/10 06:00
CRDT- 2014/05/21 06:00
PHST- 2013/07/02 00:00 [received]
PHST- 2014/04/22 00:00 [revised]
PHST- 2014/05/15 00:00 [accepted]
PHST- 2014/05/21 06:00 [entrez]
PHST- 2014/05/21 06:00 [pubmed]
PHST- 2015/03/10 06:00 [medline]
AID - 10.1002/pmic.201300270 [doi]
PST - ppublish
SO - Proteomics. 2014 Aug;14(15):1713-23. doi: 10.1002/pmic.201300270.
PMID- 2393398
OWN - NLM
STAT- MEDLINE
DCOM- 19901004
LR - 20171116
IS - 0006-291X (Print)
IS - 0006-291X (Linking)
VI - 171
IP - 1
DP - 1990 Aug 31
TI - Carbohydrate composition and presence of a fucose-protein linkage in recombinant
human pro-urokinase.
PG - 401-6
AB - A new post-translational modification site in the growth factor domain of urinary
type plasminogen activator has been identified. A glycopeptide containing the
monosaccharide, fucose, covalently linked directly to the peptide backbone has
been isolated from the tryptic digest of pro-urokinase expressed in a mouse
hybridoma cell line Sp 2/0 Ag 14. The glycopeptide was isolated by
semi-preparative reversed phase high performance liquid chromatography. The
identity of a fucose containing peptide was confirmed by carbohydrate analysis,
amino acid analysis and plasma desorption mass spectrometry (PDMS). A combination
of these methodologies showed an equimolar ratio of peptide and fucose in the
glycopeptide. This modification is not detected without mass spectrometry because
the fucose residue is hydrolyzed under standard acidic conditions of amino acid
composition and N-terminal sequence analysis. The site of attachment of fucose to
the peptide has been localized towards the N-terminus (within first 23 amino
acids) of the protein. Also, the carbohydrate composition of recombinant
pro-urokinase is reported.
FAU - Kentzer, E J
AU - Kentzer EJ
AD - PPD Analytical Research Department, Abbott Laboratories, North Chicago, Illinois
60064.
FAU - Buko, A
AU - Buko A
FAU - Menon, G
AU - Menon G
FAU - Sarin, V K
AU - Sarin VK
LA - eng
PT - Journal Article
PL - United States
TA - Biochem Biophys Res Commun
JT - Biochemical and biophysical research communications
JID - 0372516
RN - 0 (Hexoses)
RN - 0 (Peptide Fragments)
RN - 0 (Recombinant Proteins)
RN - 28RYY2IV3F (Fucose)
RN - EC 3.4.21.4 (Trypsin)
RN - EC 3.4.21.73 (Urokinase-Type Plasminogen Activator)
SB - IM
MH - Amino Acid Sequence
MH - Fucose/analysis/*metabolism
MH - Glycosylation
MH - Hexoses/analysis
MH - Humans
MH - Molecular Sequence Data
MH - Peptide Fragments/analysis
MH - Peptide Mapping
MH - Protein Processing, Post-Translational
MH - Recombinant Proteins
MH - Trypsin
MH - Urokinase-Type Plasminogen Activator/*metabolism
EDAT- 1990/08/31 00:00
MHDA- 1990/08/31 00:01
CRDT- 1990/08/31 00:00
PHST- 1990/08/31 00:00 [pubmed]
PHST- 1990/08/31 00:01 [medline]
PHST- 1990/08/31 00:00 [entrez]
AID - 0006-291X(90)91407-J [pii]
PST - ppublish
SO - Biochem Biophys Res Commun. 1990 Aug 31;171(1):401-6.
PMID- 14693913
OWN - NLM
STAT- MEDLINE
DCOM- 20041006
LR - 20181130
IS - 0959-6658 (Print)
IS - 0959-6658 (Linking)
VI - 14
IP - 3
DP - 2004 Mar
TI - Characterization of N- and O-linked glycosylation of recombinant human bile
salt-stimulated lipase secreted by Pichia pastoris.
PG - 265-74
AB - Recombinant human bile salt-stimulated lipase (hBSSL) was expressed in and
secreted by Pichia pastoris, an organism exploited for the large-scale production
of recombinant (glyco)proteins by bioprocessing technology. The 76.3-kDa
glycoprotein was associated with 75-80 Man and a small amount of GlcNAc. hBSSL
has one N-glycosylation site at Asn187, which was 38-40% occupied with a
Man(10)GlcNAc(2) structure defined previously in Pichia as the
oligosaccharide-lipid form of Man(9)GlcNAc(2) trimmed of the middle-arm terminal
alpha 1,2-Man and elongated with Man alpha 1,2Man alpha 1,6-disaccharide attached
to the lower-arm core alpha 1,3-Man (Trimble et al. [1991], J. Biol. Chem., 266,
22807-22817). The C-terminal 192 residues of hBSSL contain 16 Pro-rich
11-amino-acid repeats, which include 32 Ser/Thr residues as potential
O-glycosylation sites. Using hBSSL as a platform to study Pichia's
O-glycosylation capabilities, we found that nearly all of these sites were
occupied by mannose-containing O-glycans, whose structures, after
beta-elimination and purification, were assigned by (1)H NMR and, in some cases,
by linkage-specific exoglycosidases and methylation analysis. The most abundant
O-glycan was alpha 1,2-mannobiitol (55%), followed by alpha 1,2-mannotriitol
(16%) and mannitol (10%) and a lesser amount was alpha 1,2-mannotetraitol.
Unexpectedly, Man(5) and Man(6) O-glycans were present, which had the structure
Man beta 1,2Man beta 1,2Man alpha 1,2(Man alpha 1,2)(1,2)mannitol. Also a small
amount of a phosphorylated Man(6) O-glycan was characterized by MALDI-TOF MS
postsource decay analysis as having the reducing-end mannitol disubstituted with
a glycosidically linked phosphorylated Man and an unbranched Man(4) polymer
elongated from a different mannitol carbon. This is the first report of the
synthesis of beta-Man- and phosphate-containing O-linked constituents on
glycoproteins synthesized by P. pastoris.
FAU - Trimble, Robert B
AU - Trimble RB
AD - Wadsworth Center C-547, New York State Department of Health, PO Box 509, Albany,
NY 12201-0509, USA. trimble@wadsworth.org
FAU - Lubowski, Catherine
AU - Lubowski C
FAU - Hauer, Charles R 3rd
AU - Hauer CR 3rd
FAU - Stack, Robert
AU - Stack R
FAU - McNaughton, Lynn
AU - McNaughton L
FAU - Gemmill, Trent R
AU - Gemmill TR
FAU - Kumar, S Anand
AU - Kumar SA
LA - eng
GR - GM23900/GM/NIGMS NIH HHS/United States
PT - Journal Article
PT - Research Support, U.S. Gov't, P.H.S.
DEP - 20031223
PL - England
TA - Glycobiology
JT - Glycobiology
JID - 9104124
RN - 0 (Polysaccharides)
RN - 0 (Recombinant Proteins)
RN - 0 (Sugar Alcohols)
RN - EC 3.1.1.- (bile salt-stimulated lipase)
RN - EC 3.1.1.13 (Sterol Esterase)
SB - IM
MH - Carbohydrate Sequence
MH - Glycosylation
MH - Humans
MH - Magnetic Resonance Spectroscopy
MH - Molecular Sequence Data
MH - Phosphorylation
MH - Pichia/*metabolism
MH - Polysaccharides/*analysis/*chemistry/metabolism
MH - Recombinant Proteins/chemistry/genetics/metabolism
MH - Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
MH - Sterol Esterase/*chemistry/genetics/*metabolism
MH - Sugar Alcohols/chemistry
EDAT- 2003/12/25 05:00
MHDA- 2004/10/07 09:00
CRDT- 2003/12/25 05:00
PHST- 2003/12/25 05:00 [pubmed]
PHST- 2004/10/07 09:00 [medline]
PHST- 2003/12/25 05:00 [entrez]
AID - 10.1093/glycob/cwh036 [doi]
AID - cwh036 [pii]
PST - ppublish
SO - Glycobiology. 2004 Mar;14(3):265-74. doi: 10.1093/glycob/cwh036. Epub 2003 Dec
23.
PMID- 7780197
OWN - NLM
STAT- MEDLINE
DCOM- 19950720
LR - 20131121
IS - 0959-6658 (Print)
IS - 0959-6658 (Linking)
VI - 5
IP - 2
DP - 1995 Mar
TI - The critical glycosylation site of human transferrin receptor contains a
high-mannose oligosaccharide.
PG - 227-32
AB - The human transferrin receptor (TfR) contains three N-linked oligosaccharides and
glycosylation is required for the proper folding and function of the molecule.
Earlier studies demonstrated that the oligosaccharide at Asn-727 is vital for the
production of fully active TfR. The oligosaccharide(s) present at this site have
been analysed using a combination of site-directed mutagenesis and chemical
analysis. Wild-type TfR and mutants containing only the Asn-727 site or missing
all three sites were transfected into mouse 3T3 cells and receptors were analysed
by endo-N-acetylglucosaminidase H (Endo-H) digestion, SDS-PAGE and
immunoblotting. These studies suggested that the Asn-727 site contains
high-mannose or Endo-H-sensitive hybrid oligosaccharides. Glycosylation of
Asn-727 found in the TfR purified from human placentae was analysed by high-pH
anion-exchange chromatography with pulsed amperometric detection (HPAE-PAD) and
mass spectrometry following tryptic digestion, peptide purification via
reverse-phase high-performance liquid chromatography (RP-HPLC) and peptide
sequencing. HPAE-PAD showed the presence of a series of high-mannose
oligosaccharides. Mass spectrometry confirmed these observations, but also showed
the presence of an 80 Da anionic moiety on a fraction of the oligosaccharides.
FAU - Hayes, G R
AU - Hayes GR
AD - Department of Biochemistry and Molecular Biology, SUNY Health Science Center at
Syracuse 13210, USA.
FAU - Williams, A
AU - Williams A
FAU - Costello, C E
AU - Costello CE
FAU - Enns, C A
AU - Enns CA
FAU - Lucas, J J
AU - Lucas JJ
LA - eng
GR - DK 40608/DK/NIDDK NIH HHS/United States
GR - GM 43111/GM/NIGMS NIH HHS/United States
GR - RR00317/RR/NCRR 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 (Oligosaccharides)
RN - 0 (Receptors, Transferrin)
RN - 0 (Recombinant Proteins)
RN - 7006-34-0 (Asparagine)
RN - EC 3.2.1.- (Hexosaminidases)
RN - EC 3.2.1.96 (Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase)
RN - EC 3.4.21.4 (Trypsin)
RN - PHA4727WTP (Mannose)
SB - IM
MH - 3T3 Cells
MH - Amino Acid Sequence
MH - Animals
MH - Asparagine/analysis
MH - Binding Sites
MH - Carbohydrate Sequence
MH - Chromatography, High Pressure Liquid
MH - Electrophoresis, Polyacrylamide Gel
MH - Glycosylation
MH - Hexosaminidases
MH - Humans
MH - Mannose/*analysis
MH - Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase
MH - Mass Spectrometry
MH - Mice
MH - Molecular Sequence Data
MH - Oligosaccharides/*chemistry/isolation & purification
MH - Peptide Mapping
MH - Receptors, Transferrin/biosynthesis/*chemistry/*metabolism
MH - Recombinant Proteins/biosynthesis/chemistry/metabolism
MH - Transfection
MH - Trypsin
EDAT- 1995/03/01 00:00
MHDA- 1995/03/01 00:01
CRDT- 1995/03/01 00:00
PHST- 1995/03/01 00:00 [pubmed]
PHST- 1995/03/01 00:01 [medline]
PHST- 1995/03/01 00:00 [entrez]
PST - ppublish
SO - Glycobiology. 1995 Mar;5(2):227-32.
PMID- 6190803
OWN - NLM
STAT- MEDLINE
DCOM- 19830811
LR - 20061115
IS - 0021-9258 (Print)
IS - 0021-9258 (Linking)
VI - 258
IP - 12
DP - 1983 Jun 25
TI - Primary structure of the oligosaccharide determinant of blood group Cad
specificity.
PG - 7691-5
AB - Glycophorin A and B from Cad erythrocyte membranes are the carriers of the blood
group Cad determinants. They are characterized by a significant increase in
molecular mass, as compared to the corresponding glycophorins from control
erythrocytes (Cartron, J.-P., and Blanchard, D. (1982) Biochem. J. 207, 497-504).
Lipid-free glycophorin A, purified from Cad red cells, showed an increased GalNAc
content in comparison to blood group B, Cad-negative, control cells.
Alkaline-borohydride treatment of this Cad glycophorin A released as a
predominant species a pentasaccharide; its structure was determined, by
methylation analysis and by 500-MHz 1H-NMR studies, to be: (formula; see text)
This novel oligosaccharide inhibited strongly the hemagglutination of Cad
erythrocytes by the Dolichos biflorus lectin. It shares with the blood group Sda
determinant a terminal GalNAc beta (1 leads to 4)Gal beta (1 leads to .)
sequence.
FAU - Blanchard, D
AU - Blanchard D
FAU - Cartron, J P
AU - Cartron JP
FAU - Fournet, B
AU - Fournet B
FAU - Montreuil, J
AU - Montreuil J
FAU - van Halbeek, H
AU - van Halbeek H
FAU - Vliegenthart, J F
AU - Vliegenthart JF
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 (Blood Group Antigens)
RN - 0 (Epitopes)
RN - 0 (Glycophorin)
RN - 0 (Oligosaccharides)
RN - 0 (Sialoglycoproteins)
SB - IM
MH - Blood Group Antigens/*genetics
MH - Carbohydrate Conformation
MH - Carbohydrate Sequence
MH - Epitopes/*analysis
MH - Erythrocyte Membrane/*immunology
MH - Erythrocytes/*immunology
MH - Glycophorin/*immunology
MH - Humans
MH - Magnetic Resonance Spectroscopy
MH - Oligosaccharides/*immunology
MH - Sialoglycoproteins/*immunology
EDAT- 1983/06/25 00:00
MHDA- 1983/06/25 00:01
CRDT- 1983/06/25 00:00
PHST- 1983/06/25 00:00 [pubmed]
PHST- 1983/06/25 00:01 [medline]
PHST- 1983/06/25 00:00 [entrez]
PST - ppublish
SO - J Biol Chem. 1983 Jun 25;258(12):7691-5.
PMID- 2592374
OWN - NLM
STAT- MEDLINE
DCOM- 19900119
LR - 20171116
IS - 0021-9258 (Print)
IS - 0021-9258 (Linking)
VI - 264
IP - 35
DP - 1989 Dec 15
TI - Protein and carbohydrate structural analysis of a recombinant soluble CD4
receptor by mass spectrometry.
PG - 21286-95
AB - The primary structure of a soluble form of the CD4 receptor (sCD4) expressed in
Chinese hamster ovary cells has been confirmed by mass spectrometric peptide
mapping and and tandem mass spectrometry. These studies corroborated 95% of the
369-amino acid-long sequence and established the fidelity of translation of the
NH2 and COOH terminal including the absence of "ragged ends." The arrangement of
the three disulfide bonds in recombinant sCD4 was also established by mass
spectrometry and comparative high performance liquid chromatography mapping and
shown to be identical to that expected from previous studies of intrachain
disulfide bonding in T4 antigens derived from sheep and mouse. No other
arrangements of disulfides were detected. Carbohydrate mapping by mass
spectrometry was used to establish that both potential Asn-linked glycosylation
sites in sCD4 (Asn271 and Asn300) have oligosaccharides attached. Structural
characterization by mass spectrometry and methylation analysis of the
heterogeneous family of oligosaccharides at each of the specific attachment sites
indicates that the major components of both families of oligosaccharides have the
following biantennary structures: (Formula, see text) where m + n = 0-2, and x =
0,1. Minor carbohydrate components having three N-acetylneuraminic acid (NeuAc)
groups and an additional hexose-hexosamine unit were detected by high performance
anion-exchange chromatography.
FAU - Carr, S A
AU - Carr SA
AD - Department of Physical and Structural Chemistry, Smith Kline and French
Laboratories, King of Prussia, Pennsylvania 19406.
FAU - Hemling, M E
AU - Hemling ME
FAU - Folena-Wasserman, G
AU - Folena-Wasserman G
FAU - Sweet, R W
AU - Sweet RW
FAU - Anumula, K
AU - Anumula K
FAU - Barr, J R
AU - Barr JR
FAU - Huddleston, M J
AU - Huddleston MJ
FAU - Taylor, P
AU - Taylor P
LA - eng
GR - GM-39526-02/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 (CD4 Antigens)
RN - 0 (Peptide Fragments)
RN - 0 (Recombinant Proteins)
SB - IM
EIN - J Biol Chem 1990 Feb 25;265(6):3585
MH - Amino Acid Sequence
MH - Animals
MH - *CD4 Antigens/genetics/isolation & purification
MH - Carbohydrate Conformation
MH - Carbohydrate Sequence
MH - Cell Line
MH - Chromatography, High Pressure Liquid
MH - Gene Expression
MH - Genes
MH - Humans
MH - Mass Spectrometry
MH - Methylation
MH - Molecular Sequence Data
MH - Peptide Fragments/isolation & purification
MH - Peptide Mapping
MH - Recombinant Proteins
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 - J Biol Chem. 1989 Dec 15;264(35):21286-95.
PMID- 1456441
OWN - NLM
STAT- MEDLINE
DCOM- 19930107
LR - 20111117
IS - 0003-2697 (Print)
IS - 0003-2697 (Linking)
VI - 206
IP - 1
DP - 1992 Oct
TI - N-glycosylation site mapping of human serotransferrin by serial lectin affinity
chromatography, fast atom bombardment-mass spectrometry, and 1H nuclear magnetic
resonance spectroscopy.
PG - 53-63
AB - This report describes the N-glycosylation site mapping of human serotransferrin
(h-STF). Reduced and S-carboxymethylated h-STF was digested with trypsin or
chymotrypsin. Glycopeptides in the proteolytic digests were isolated by serial
concanavalin A (Con A), Sambucus nigra agglutinin (SNA), and Phaseolus vulgaris
leukoagglutinin (LPHA) affinity chromatography and subjected to preliminary
analysis by 1H NMR spectroscopy. The glycopeptide fractions were then
individually digested with N-glycanase. One part of the digest of each fraction
was analyzed by fast atom bombardment-mass spectrometry (FAB-MS) to identify the
peptide sequences of the glycosylation sites. The other part was used to isolate
the oligosaccharide by the corresponding lectin affinity chromatography and to
characterize the structures of the isolated oligosaccharides by 1H NMR
spectroscopy and FAB-MS. The oligosaccharides in the Con A-bound fraction were
shown to have bi-alpha(2-->6)-sialyl, diantennary structures. The SNA-bound
fraction was shown to contain trisialyl, triantennary structures. Di- and
triantennary oligosaccharides were found to occur on each of the two
N-glycosylation sites of h-STF (Asn413 and Asn611) in the ratio of approximately
85:15. The SNA-bound glycopeptides were further fractionated by LPHA affinity
chromatography. Two different oligosaccharides were characterized, namely, a
trisialyl 2,4-triantennary and a trisialyl 2,6-triantennary glycan. The ratio of
2,4-triantennary vs 2,6-triantennary oligosaccharides attached to glycosylation
site Asn413 was found to be approximately 5:1, whereas the two isomeric
triantennary oligosaccharides were found to be attached to glycosylation site
Asn611 in the ratio approximately 1:1.
FAU - Fu, D
AU - Fu D
AD - Complex Carbohydrate Research Center, University of Georgia, Athens 30602-4712.
FAU - van Halbeek, H
AU - van Halbeek H
LA - eng
GR - P01-AI-27135/AI/NIAID NIH HHS/United States
GR - P41-RR-05351/RR/NCRR NIH HHS/United States
GR - S10-RR-04720/RR/NCRR NIH HHS/United States
PT - Journal Article
PT - Research Support, U.S. Gov't, P.H.S.
PL - United States
TA - Anal Biochem
JT - Analytical biochemistry
JID - 0370535
RN - 0 (Glycopeptides)
RN - 0 (Lectins)
RN - 0 (Oligosaccharides)
RN - 0 (Transferrin)
RN - EC 3.4.21.4 (Trypsin)
SB - IM
MH - Amino Acid Sequence
MH - Binding Sites
MH - Carbohydrate Sequence
MH - Chromatography, Affinity/*methods
MH - Glycopeptides/chemistry/isolation & purification
MH - Glycosylation
MH - Humans
MH - *Lectins
MH - Magnetic Resonance Spectroscopy/methods
MH - Molecular Sequence Data
MH - Oligosaccharides/chemistry/isolation & purification
MH - Peptide Mapping
MH - Spectrometry, Mass, Fast Atom Bombardment
MH - Transferrin/*chemistry/isolation & purification/metabolism
MH - Trypsin/metabolism
EDAT- 1992/10/01 00:00
MHDA- 1992/10/01 00:01
CRDT- 1992/10/01 00:00
PHST- 1992/10/01 00:00 [pubmed]
PHST- 1992/10/01 00:01 [medline]
PHST- 1992/10/01 00:00 [entrez]
AID - S0003-2697(05)80010-7 [pii]
PST - ppublish
SO - Anal Biochem. 1992 Oct;206(1):53-63.
PMID- 8477709
OWN - NLM
STAT- MEDLINE
DCOM- 19930521
LR - 20161017
IS - 0014-2956 (Print)
IS - 0014-2956 (Linking)
VI - 213
IP - 1
DP - 1993 Apr 1
TI - Structures of sialylated oligosaccharides of human erythropoietin expressed in
recombinant BHK-21 cells.
PG - 39-56
AB - The native structures of the Asn-linked oligosaccharides and the O-glycans at
Ser126 of human erythropoietin expressed from recombinant BHK cells have been
elucidated. Enzymatically released N-glycans were studied by methylation
analyses, fast-atom-bombardment mass spectrometry as well as one- and
two-dimensional 1H-NMR spectrometry at 600 MHz. Many (82.7%) were found to be
tetraantennary N-acetyllactosamine-type (22.8% with one, 3.6% with two and 0.4%
with three N-acetyllactosamine repeats) being tetrasialylated (41%),
trisialylated (29.6%) and disialylated (12.2%). A few (9.7%; 4.1% 2,4-branched,
5.6%, 2,6-branched) of the chains were triantennary (5.4% trisialyl, 4.3%
disialyl) and 4.6% were of the disialyl diantennary type. Almost all of the
innermost GlcNAc residues were alpha 1-6 fucosylated and NeuAc was exclusively
alpha 2-3 linked to Gal beta 1-4GlcNAc-R; 60% of the protein was found to be
O-glycosylated at Ser126; structures were monosialylated (70%) or disialylated
(30%) forms of the Gal beta 1-3GalNAc core type. Glycosylation patterns at
individual Asn-Xaa-Thr/Ser sites were determined by analytical high-pH
anion-exchange chromatography with pulsed amperometric detection. Only
tetraantennary chains with 0-3 N-acetyllactosamine repeats were detected at Asn38
and Asn83, while almost all of the di- and triantennary oligosaccharides were
attached to Asn24. Batch analysis of different preparations of recombinant
erythropoietin revealed the high reproducibility of the production procedure.
Structures containing terminal GalNAc-GlcNAc were detected in small amounts in a
few batches.
FAU - Nimtz, M
AU - Nimtz M
AD - Department of Cell Biology and Genetics, GBF-Gesellschaft fur Biotechnologische
Forschung mbH, Braunschweig, Federal Republic of Germany.
FAU - Martin, W
AU - Martin W
FAU - Wray, V
AU - Wray V
FAU - Kloppel, K D
AU - Kloppel KD
FAU - Augustin, J
AU - Augustin J
FAU - Conradt, H S
AU - Conradt HS
LA - eng
PT - Journal Article
PL - England
TA - Eur J Biochem
JT - European journal of biochemistry
JID - 0107600
RN - 0 (Oligosaccharides)
RN - 0 (Polysaccharides)
RN - 0 (Recombinant Proteins)
RN - 0 (Sialic Acids)
RN - 11096-26-7 (Erythropoietin)
RN - GZP2782OP0 (N-Acetylneuraminic Acid)
SB - IM
MH - Amino Acid Sequence
MH - Animals
MH - Carbohydrate Sequence
MH - Cells, Cultured
MH - Chromatography, High Pressure Liquid
MH - Chromatography, Ion Exchange
MH - Cloning, Molecular
MH - Cricetinae
MH - Erythropoietin/*chemistry/genetics
MH - Glycosylation
MH - Humans
MH - Kidney/chemistry
MH - Magnetic Resonance Spectroscopy
MH - Molecular Sequence Data
MH - Molecular Structure
MH - N-Acetylneuraminic Acid
MH - Oligosaccharides/*chemistry
MH - Polysaccharides/analysis
MH - Recombinant Proteins/chemistry/genetics
MH - Sialic Acids/*chemistry
MH - Spectrometry, Mass, Fast Atom Bombardment
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 - Eur J Biochem. 1993 Apr 1;213(1):39-56.
PMID- 2049076
OWN - NLM
STAT- MEDLINE
DCOM- 19910717
LR - 20181113
IS - 0264-6021 (Print)
IS - 0264-6021 (Linking)
VI - 276 ( Pt 2)
DP - 1991 Jun 1
TI - Natural human interferon-alpha 2 is O-glycosylated.
PG - 511-8
AB - Natural human interferon alpha 2 (IFN-alpha 2) was isolated from a preparation of
partially purified human leucocyte IFN by monoclonal-antibody immunoaffinity
chromatography. The purified protein had a specific activity of 1.5 x 10(8)
i.u./mg; it was estimated to constitute 10-20% of the total antiviral activity of
leucocyte IFN. N-Terminal amino-acid-sequence analysis identified the subspecies
IFN-alpha 2b and/or IFN-alpha 2c, whereas IFN-alpha 2a was not detectable. The
structure of natural IFN-alpha 2 was found to differ from that of its recombinant
(Escherichia coli-derived) equivalent. First, reverse-phase h.p.l.c. showed that
natural IFN-alpha 2 was significantly more hydrophilic then expected. Secondly,
the apparent molecular mass of the natural protein determined by SDS/PAGE was
higher than that of recombinant IFN-alpha 2; incubation under mild alkaline
conditions known to eliminate O-linked carbohydrates resulted in a reduction of
the apparent molecular mass to that of the recombinant protein. On sequence
analysis of proteolytic peptides, Thr-106 was found to be modified. These results
suggested that Thr-106 of natural IFN-alpha 2 carries O-linked carbohydrates.
Reverse-phase h.p.l.c. as well as SDS/PAGE of natural IFN-alpha 2 showed that
glycosylation is heterogeneous. For characterization of the carbohydrate
moieties, the protein was treated with neuraminidase and/or O-glycanase and
analysed by gel electrophoresis; in addition, glycopeptides obtained by
proteinase digestion and separated by h.p.l.c. were characterized by sequence
analysis and m.s. Further information on the composition of the glycans was
obtained by monosaccharide analysis. The results indicate that natural IFN-alpha
2 contains the disaccharide galactosyl-N-acetylgalactosamine (Gal-GalNAc) linked
to Thr-106. In part of the molecules, this core carbohydrate carries
(alpha-)N-acetylneuraminic acid, whereas a disaccharide, probably
N-acetyl-lactosamine, is bound to Gal-GalNAc in another proportion of the
protein. Further glycosylation isomers are present in small amounts. As IFN-alpha
2 is the only IFN-alpha species with a threonine residue at position 106, it may
represent the only O-glycosylated human IFN-alpha protein.
FAU - Adolf, G R
AU - Adolf GR
AD - Ernst-Boehringer-Institut fur Arzneimittelforschung, Bender + Co Ges mbH, Vienna,
Austria.
FAU - Kalsner, I
AU - Kalsner I
FAU - Ahorn, H
AU - Ahorn H
FAU - Maurer-Fogy, I
AU - Maurer-Fogy I
FAU - Cantell, K
AU - Cantell K
LA - eng
PT - Journal Article
PL - England
TA - Biochem J
JT - The Biochemical journal
JID - 2984726R
RN - 0 (Antibodies, Monoclonal)
RN - 0 (Interferon Type I)
RN - 0 (Monosaccharides)
RN - 0 (Peptide Fragments)
RN - EC 3.2.1.- (Glycoside Hydrolases)
SB - IM
MH - Amino Acid Sequence
MH - Antibodies, Monoclonal
MH - Chromatography, Affinity
MH - Chromatography, High Pressure Liquid
MH - Electrophoresis, Polyacrylamide Gel
MH - Enzyme-Linked Immunosorbent Assay
MH - Glycoside Hydrolases
MH - Glycosylation
MH - Humans
MH - Interferon Type I/*chemistry/isolation & purification
MH - Molecular Sequence Data
MH - Molecular Weight
MH - Monosaccharides/analysis
MH - Peptide Fragments/isolation & purification
MH - Peptide Mapping
PMC - PMC1151121
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]
PST - ppublish
SO - Biochem J. 1991 Jun 1;276 ( Pt 2):511-8.
PMID- 7309709
OWN - NLM
STAT- MEDLINE
DCOM- 19820212
LR - 20071219
IS - 0021-924X (Print)
IS - 0021-924X (Linking)
VI - 90
IP - 4
DP - 1981 Oct
TI - Studies on the structures of the carbohydrate moiety of human prothrombin.
PG - 1023-31
AB - Human prothrombin contains three asparagine-linked sugar chains in one molecule.
The sugar chains were quantitatively liberated as radioactive oligosaccharides
from the polypeptide moiety by hydrazinolysis followed by N-acetylation and
Nab3H4 reduction. All of the oligosaccharides contain N-acetylneuraminic acid.
The neutral oligosaccharides obtained from all acidic oligosaccharides by
sialidase digestion are identical. By the combination of sequential
exoglycosidase digestion and methylation analysis, the structures of the
asparagine-linked sugar chains of human prothrombin were confirmed to be as
follows: (sequence in text).
FAU - Mizuochi, T
AU - Mizuochi T
FAU - Fujii, J
AU - Fujii J
FAU - Kisiel, W
AU - Kisiel W
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 - 9001-26-7 (Prothrombin)
RN - EC 3.2.1.- (Glycoside Hydrolases)
SB - IM
MH - Carbohydrate Sequence
MH - Chromatography, Gel
MH - Electrophoresis, Paper
MH - Glycoside Hydrolases/metabolism
MH - Humans
MH - Methylation
MH - Prothrombin/*analysis
EDAT- 1981/10/01 00:00
MHDA- 1981/10/01 00:01
CRDT- 1981/10/01 00:00
PHST- 1981/10/01 00:00 [pubmed]
PHST- 1981/10/01 00:01 [medline]
PHST- 1981/10/01 00:00 [entrez]
PST - ppublish
SO - J Biochem. 1981 Oct;90(4):1023-31.
PMID- 8223648
OWN - NLM
STAT- MEDLINE
DCOM- 19931222
LR - 20161017
IS - 0014-2956 (Print)
IS - 0014-2956 (Linking)
VI - 217
IP - 3
DP - 1993 Nov 1
TI - Expression of human interferon omega 1 in Sf9 cells. No evidence for complex-type
N-linked glycosylation or sialylation.
PG - 913-9
AB - Human interferon omega 1 (IFN-omega 1) was expressed in Spodoptera frugiperda Sf9
insect cells using the baculovirus expression system. Half of the protein
purified by immunoaffinity chromatography was shown to be N-glycosylated at the
same site as the natural IFN-omega 1. The degree of glycosylation was independent
of the expression rate. While natural IFN-omega 1 was shown to carry complex-type
oligosaccharides [Adolf, G. R., Maurer-Fogy, I., Kalsner, I. & Cantell, K. (1990)
J. Biol. Chem. 265, 9290-9295], the insect cell produced protein which was
demonstrated by lectin blot, mass spectroscopy and HPLC analysis to contain only
the core oligosaccharide. Two different structures, (Man)2(GlcNAc)2[Fuc] and
(Man)3(GlcNAc)2[Fuc] were identified. The fucosylation was identified to be
(alpha 1-6)-linked to the core saccharide. Sialic acid residues were clearly
absent. IFN-omega 1 expressed in S. frugiperda cells was shown to be partially
truncated at the C-terminus by nine residues; its antiviral activity when
glycosylated was significantly lower than the activity of IFN-omega 1 produced by
Sendai-virus-stimulated leukocytes. Circular dichroism and fluorescence
spectroscopy did not reveal any structural differences between glycosylated and
nonglycosylated IFN-omega 1. This implies the importance of a complex-type
glycosylation for the maximal biological activity of human IFN-omega 1.
FAU - Voss, T
AU - Voss T
AD - Ernst-Boehringer Institut fur Arzneimittelforschung, Department of Protein
Chemistry, Bender & Co., Vienna, Austria.
FAU - Ergulen, E
AU - Ergulen E
FAU - Ahorn, H
AU - Ahorn H
FAU - Kubelka, V
AU - Kubelka V
FAU - Sugiyama, K
AU - Sugiyama K
FAU - Maurer-Fogy, I
AU - Maurer-Fogy I
FAU - Glossl, J
AU - Glossl J
LA - eng
PT - Journal Article
PL - England
TA - Eur J Biochem
JT - European journal of biochemistry
JID - 0107600
RN - 0 (Carbohydrates)
RN - 0 (DNA Primers)
RN - 0 (Interferon Type I)
RN - 0 (Sialic Acids)
RN - 0 (interferon omega 1)
RN - GZP2782OP0 (N-Acetylneuraminic Acid)
SB - IM
MH - Animals
MH - Baculoviridae/genetics
MH - Base Sequence
MH - Carbohydrate Sequence
MH - Carbohydrates/analysis
MH - Cell Line
MH - Cells, Cultured
MH - Chromatography, High Pressure Liquid
MH - Circular Dichroism
MH - Cloning, Molecular
MH - DNA Primers
MH - Electrophoresis, Polyacrylamide Gel
MH - Glycosylation
MH - Humans
MH - Interferon Type I/*genetics/isolation & purification/metabolism
MH - Mass Spectrometry
MH - Molecular Sequence Data
MH - Moths
MH - N-Acetylneuraminic Acid
MH - Protein Conformation
MH - Sialic Acids/*metabolism
MH - Spectrometry, Fluorescence
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 - Eur J Biochem. 1993 Nov 1;217(3):913-9.
PMID- 26791533
OWN - NLM
STAT- MEDLINE
DCOM- 20161213
LR - 20161230
IS - 1535-3907 (Electronic)
IS - 1535-3893 (Linking)
VI - 15
IP - 3
DP - 2016 Mar 4
TI - N-Glycoproteomics of Human Seminal Plasma Glycoproteins.
PG - 991-1001
LID - 10.1021/acs.jproteome.5b01069 [doi]
AB - Seminal plasma aids sperm by inhibiting premature capacitation, helping in the
intracervical transport and formation of an oviductal sperm reservoir, all of
which appear to be important in the fertilization process. Epitopes such as Lewis
x and y are known to be present on seminal plasma glycoproteins, which can
modulate the maternal immune response. It is suggested by multiple studies that
seminal plasma glycoproteins play, largely undiscovered, important roles in the
process of fertilization. We have devised a strategy to analyze glycopeptides
from a complex, unknown mixture of protease-digested proteins. This analysis
provides identification of the glycoproteins, glycosylation sites, glycan
compositions, and proposed structures from the original sample. This strategy has
been applied to human seminal plasma total glycoproteins. We have elucidated
glycan compositions and proposed structures for 243 glycopeptides belonging to 73
N-glycosylation sites on 50 glycoproteins. The majority of the proposed glycan
structures were complex type (83%) followed by high-mannose (10%) and then hybrid
(7%). Most of the glycoproteins were either sialylated, fucosylated, or both.
Many Lewis x/a and y/b epitopes bearing glycans were found, suggesting
immune-modulating epitopes on multiple seminal plasma glycoproteins. The study
also shows that large scale N-glycosylation mapping is achievable with current
techniques and the depth of the analysis is roughly proportional to the
prefractionation and complexity of the sample.
FAU - Saraswat, Mayank
AU - Saraswat M
AD - Transplantation Laboratory, Haartman Institute, University of Helsinki ,
Haartmaninkatu 3, P.O. Box 21, Helsinki FI-00014, Finland.
AD - HUSLAB, Helsinki University Hospital, 00290 Helsinki, Finland.
FAU - Joenvaara, Sakari
AU - Joenvaara S
AD - Transplantation Laboratory, Haartman Institute, University of Helsinki ,
Haartmaninkatu 3, P.O. Box 21, Helsinki FI-00014, Finland.
AD - HUSLAB, Helsinki University Hospital, 00290 Helsinki, Finland.
FAU - Tomar, Anil Kumar
AU - Tomar AK
AD - Department of Biophysics, All India Institute of Medical Sciences , New Delhi
110029, India.
FAU - Singh, Sarman
AU - Singh S
AD - Division of Clinical Microbiology & Molecular Medicine, Department of Laboratory
Medicine, All India Institute of Medical Sciences , New Delhi 110029, India.
FAU - Yadav, Savita
AU - Yadav S
AD - Department of Biophysics, All India Institute of Medical Sciences , New Delhi
110029, India.
FAU - Renkonen, Risto
AU - Renkonen R
AD - Transplantation Laboratory, Haartman Institute, University of Helsinki ,
Haartmaninkatu 3, P.O. Box 21, Helsinki FI-00014, Finland.
AD - HUSLAB, Helsinki University Hospital, 00290 Helsinki, Finland.
LA - eng
PT - Journal Article
PT - Research Support, Non-U.S. Gov't
DEP - 20160204
PL - United States
TA - J Proteome Res
JT - Journal of proteome research
JID - 101128775
RN - 0 (Glycoproteins)
RN - 0 (Polysaccharides)
RN - 0 (Proteome)
SB - IM
MH - Adult
MH - Amino Acid Sequence
MH - Carbohydrate Conformation
MH - Carbohydrate Sequence
MH - Gene Ontology
MH - Glycoproteins/chemistry/*metabolism
MH - Glycosylation
MH - Humans
MH - Male
MH - Polysaccharides/chemistry/metabolism
MH - Proteome/chemistry/*metabolism
MH - Proteomics
MH - Semen/*metabolism
MH - Young Adult
OTO - NOTNLM
OT - CID-MS/MS
OT - DC-SIGN ligands
OT - GlycopeptideId
OT - HE-4
OT - Lewis x
OT - Lewis y
OT - N-glycoproteomics
OT - clusterin
OT - heparin-affinity chromatography
OT - human seminal plasma
EDAT- 2016/01/23 06:00
MHDA- 2016/12/15 06:00
CRDT- 2016/01/22 06:00
PHST- 2016/01/22 06:00 [entrez]
PHST- 2016/01/23 06:00 [pubmed]
PHST- 2016/12/15 06:00 [medline]
AID - 10.1021/acs.jproteome.5b01069 [doi]
PST - ppublish
SO - J Proteome Res. 2016 Mar 4;15(3):991-1001. doi: 10.1021/acs.jproteome.5b01069.
Epub 2016 Feb 4.
PMID- 10441114
OWN - NLM
STAT- MEDLINE
DCOM- 19990908
LR - 20061115
IS - 0006-2960 (Print)
IS - 0006-2960 (Linking)
VI - 38
IP - 32
DP - 1999 Aug 10
TI - Novel glycosylated forms of human plasma endostatin and circulating
endostatin-related fragments of collagen XV.
PG - 10217-24
AB - Circulating elongated forms of the angiogenesis inhibitor and potential
anti-cancer drug endostatin were isolated from human blood filtrate.
Immunoreactive endostatin was identified by a polyclonal rabbit antiserum raised
against an N-terminal epitope of the polypeptide and purified by consecutive
chromatographic steps and immunoblotting. N- and C-terminal sequence analyses of
the isolated molecules revealed different forms of endostatin starting with
V(117)HLRPAR. lacking the last and final three residues of the noncollagenous
domain 1 (NC-1) of collagen XVIII, respectively. These polypetides are found to
be O-glycosylated at T(125) (residue 9) with a glycan structure of the mucin type
consisting of galactose N-acetylgalactosamine and N-acetylneuraminic acid
residues. Carbohydrate analyses were performed via the semiquantitative
HPLC-electrospray ionization mass spectrometry (ESMS) technique after
exoglycosidase hydrolysis. Circulating endostatins are present as
sialoglycoprotein (22 000 and 21 841 Da +/- 0.02%) and asialoglycoprotein
structures (21 710 and 21 549 Da +/- 0.02%), while the two completely
deglycosylated forms are obtained only after enzymatic incubation. The described
glycosylated endostatins may represent intermediates in the proteolytic pathway
of the NC-1 domain of collagen XVIII resulting in bioactive endostatins.
Furthermore, immunoreactive endostatin-related C-terminal fragments of human
collagen XV are found in the hemofiltrate. These polypeptides exhibit the
N-terminal sequences P(66)HLLPPP. and Y(81)EKPALH. of the collagen XV NC-1
domain. ESMS and immunoblotting analyses reveal three glycosylated polypeptides
with a molecular mass ranging from 16 to 21 kDa. Due to the high degree of
homology between collagen XV and collagen XVIII as well as their analoqous
proteolytic processing, functional similarities of collagen XVIII- and XV-related
fragments should be revealed in future experiments.
FAU - John, H
AU - John H
AD - Lower Saxony Institute for Peptide Research (IPF), Hannover, Germany.
FAU - Preissner, K T
AU - Preissner KT
FAU - Forssmann, W G
AU - Forssmann WG
FAU - Standker, L
AU - Standker L
LA - eng
PT - Journal Article
PT - Research Support, Non-U.S. Gov't
PL - United States
TA - Biochemistry
JT - Biochemistry
JID - 0370623
RN - 0 (Collagen Type XVIII)
RN - 0 (Endostatins)
RN - 0 (Oligosaccharides)
RN - 0 (Peptide Fragments)
RN - 9007-34-5 (Collagen)
SB - IM
MH - Amino Acid Sequence
MH - Animals
MH - Blotting, Western
MH - Collagen/*blood/*chemistry/isolation & purification
MH - Collagen Type XVIII
MH - Endostatins
MH - Female
MH - Glycosylation
MH - Humans
MH - Mass Spectrometry
MH - Molecular Sequence Data
MH - Oligosaccharides/analysis
MH - Peptide Fragments/*blood/*chemistry/isolation & purification
MH - Rabbits
EDAT- 1999/08/11 00:00
MHDA- 1999/08/11 00:01
CRDT- 1999/08/11 00:00
PHST- 1999/08/11 00:00 [pubmed]
PHST- 1999/08/11 00:01 [medline]
PHST- 1999/08/11 00:00 [entrez]
AID - 10.1021/bi990787+ [doi]
AID - bi990787+ [pii]
PST - ppublish
SO - Biochemistry. 1999 Aug 10;38(32):10217-24. doi: 10.1021/bi990787+.
PMID- 8202534
OWN - NLM
STAT- MEDLINE
DCOM- 19940706
LR - 20181113
IS - 0027-8424 (Print)
IS - 0027-8424 (Linking)
VI - 91
IP - 12
DP - 1994 Jun 7
TI - Human serum amyloid P component is an invariant constituent of amyloid deposits
and has a uniquely homogeneous glycostructure.
PG - 5602-6
AB - Human serum amyloid P component (SAP) is a normal plasma protein and the
precursor of amyloid P component (AP), a universal constituent of the abnormal
tissue deposits in amyloidosis, including Alzheimer disease. We show here that
its single N-linked biantennary oligosaccharide does not display the
microheterogeneity usually characteristic of glycoproteins. The protein and the
glycan structures of AP were also invariant, their resistance to degradation
suggesting a role in persistence of amyloid deposits. Asialo-SAP was rapidly
cleared from the circulation in mice by a mechanism dependent on terminal
galactose residues and was catabolized in hepatocytes. However blockade of this
pathway did not affect the clearance of native SAP. Rapid hepatic uptake and
catabolism of human asialo-SAP in man were also directly demonstrated. The
protein and glycan homogeneity of SAP and the integrity of AP suggest that the
complete glycoprotein structure is important for the normal and the
pathophysiological functions of this molecule.
FAU - Pepys, M B
AU - Pepys MB
AD - Immunological Medicine Unit, Royal Postgraduate Medical School, Hammersmith
Hospital, London, United Kingdom.
FAU - Rademacher, T W
AU - Rademacher TW
FAU - Amatayakul-Chantler, S
AU - Amatayakul-Chantler S
FAU - Williams, P
AU - Williams P
FAU - Noble, G E
AU - Noble GE
FAU - Hutchinson, W L
AU - Hutchinson WL
FAU - Hawkins, P N
AU - Hawkins PN
FAU - Nelson, S R
AU - Nelson SR
FAU - Gallimore, J R
AU - Gallimore JR
FAU - Herbert, J
AU - Herbert J
AU - et al.
LA - eng
GR - Wellcome Trust/United Kingdom
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 (Amyloid)
RN - 0 (Asialoglycoproteins)
RN - 0 (Serum Amyloid P-Component)
SB - IM
MH - Amyloid/*chemistry
MH - Animals
MH - Asialoglycoproteins/metabolism
MH - Carbohydrate Sequence
MH - Female
MH - Humans
MH - Metabolic Clearance Rate
MH - Mice
MH - Mice, Inbred CBA
MH - Molecular Sequence Data
MH - Serum Amyloid P-Component/*chemistry/metabolism
PMC - PMC44044
EDAT- 1994/06/07 00:00
MHDA- 1994/06/07 00:01
CRDT- 1994/06/07 00:00
PHST- 1994/06/07 00:00 [pubmed]
PHST- 1994/06/07 00:01 [medline]
PHST- 1994/06/07 00:00 [entrez]
PST - ppublish
SO - Proc Natl Acad Sci U S A. 1994 Jun 7;91(12):5602-6.
PMID- 11805077
OWN - NLM
STAT- MEDLINE
DCOM- 20020517
LR - 20131121
IS - 0959-6658 (Print)
IS - 0959-6658 (Linking)
VI - 11
IP - 12
DP - 2001 Dec
TI - Structural analysis of sulfated N-linked oligosaccharides in erythropoietin.
PG - 1043-9
AB - We previously demonstrated that high-performance liquid chromatography with
electrospray ionization mass spectrometry (LC/MS) equipped with a graphitized
carbon column (GCC) is useful for the structural analysis of carbohydrates in
glycoproteins. Using LC/MS with GCC, sulfated N-linked oligosaccharides were
found in erythropoietin (EPO) expressed in baby hamster kidney cells. Sulfation
occurs in a part of the N-linked oligosaccharides in the EPO. Sulfated
monosaccharide residue in the sulfated N-linked oligosaccharide was determined by
exoglycosidase digestion followed by sugar mapping by LC/MS. The linkage position
and branch-location of the sulfate group in the tetraantennary oligosaccharide
were analyzed by (1)H-nuclear magnetic resonance. It was suggested that sulfation
occurs on the C-6 position of GlcNAc located in the GlcNAcbeta1-4Manalpha1-3
branch.
FAU - Kawasaki, N
AU - Kawasaki N
AD - Division of Biological Chemistry and Biologicals, National Institute of Health
Sciences, 1-18-1, Kamiyoga, Setagaya-ku, Tokyo 158-8501 Japan.
FAU - Haishima, Y
AU - Haishima Y
FAU - Ohta, M
AU - Ohta M
FAU - Itoh, S
AU - Itoh S
FAU - Hyuga, M
AU - Hyuga M
FAU - Hyuga, S
AU - Hyuga S
FAU - Hayakawa, T
AU - Hayakawa T
LA - eng
PT - Journal Article
PL - England
TA - Glycobiology
JT - Glycobiology
JID - 9104124
RN - 0 (Oligosaccharides)
RN - 0 (Recombinant Proteins)
RN - 0 (Sugar Alcohols)
RN - 11096-26-7 (Erythropoietin)
RN - 70FD1KFU70 (Sulfur)
RN - EC 3.2.1.- (Glycoside Hydrolases)
SB - IM
MH - Animals
MH - Carbohydrate Conformation
MH - Carbohydrate Sequence
MH - Cell Line
MH - Chromatography, Liquid
MH - Cricetinae
MH - Erythropoietin/*chemistry
MH - Glycoside Hydrolases/metabolism
MH - Humans
MH - Magnetic Resonance Spectroscopy
MH - Mass Spectrometry
MH - Molecular Sequence Data
MH - Oligosaccharides/*chemistry/isolation & purification
MH - Recombinant Proteins
MH - Spectrometry, Mass, Electrospray Ionization
MH - Sugar Alcohols/chemistry
MH - Sulfur/*chemistry
EDAT- 2002/01/24 10:00
MHDA- 2002/05/23 10:01
CRDT- 2002/01/24 10:00
PHST- 2002/01/24 10:00 [pubmed]
PHST- 2002/05/23 10:01 [medline]
PHST- 2002/01/24 10:00 [entrez]
PST - ppublish
SO - Glycobiology. 2001 Dec;11(12):1043-9.
PMID- 23345538
OWN - NLM
STAT- MEDLINE
DCOM- 20130916
LR - 20181202
IS - 1535-9484 (Electronic)
IS - 1535-9476 (Linking)
VI - 12
IP - 4
DP - 2013 Apr
TI - Glycoproteomic analysis of the secretome of human endothelial cells.
PG - 956-78
LID - 10.1074/mcp.M112.024018 [doi]
AB - Previous proteomics studies have partially unraveled the complexity of
endothelial protein secretion but have not investigated glycosylation, a key
modification of secreted and membrane proteins for cell communication. In this
study, human umbilical vein endothelial cells were kept in serum-free medium
before activation by phorbol-12-myristate-13 acetate, a commonly used
secretagogue that induces exocytosis of endothelial vesicles. In addition to 123
secreted proteins, the secretome was particularly rich in membrane proteins.
Glycopeptides were enriched by zwitterionic hydrophilic interaction liquid
chromatography resins and were either treated with PNGase F and H2(18)O or
directly analyzed using a recently developed workflow combining higher-energy
C-trap dissociation (HCD) with electron-transfer dissociation (ETD) for a hybrid
linear ion trap-orbitrap mass spectrometer. After deglycosylation with PNGase F
in the presence of H2(18)O, 123 unique peptides displayed (18)O-deamidation of
asparagine, corresponding to 86 proteins with a total of 121 glycosylation sites.
Direct glycopeptide analysis via HCD-ETD identified 131 glycopeptides from 59
proteins and 118 glycosylation sites, of which 41 were known, 51 were predicted,
and 26 were novel. Two methods were compared: alternating HCD-ETD and
HCD-product-dependent ETD. The former detected predominantly high-intensity,
multiply charged glycopeptides, whereas the latter preferentially selected
precursors with complex/hybrid glycans for fragmentation. Validation was
performed by means of glycoprotein enrichment and analysis of the input, the
flow-through, and the bound fraction. This study represents the most
comprehensive characterization of endothelial protein secretion to date and
demonstrates the potential of new HCD-ETD workflows for determining the
glycosylation status of complex biological samples.
FAU - Yin, Xiaoke
AU - Yin X
AD - The King's British Heart Foundation Centre, King's College London, London SE5
9NU, UK.
FAU - Bern, Marshall
AU - Bern M
FAU - Xing, Qiuru
AU - Xing Q
FAU - Ho, Jenny
AU - Ho J
FAU - Viner, Rosa
AU - Viner R
FAU - Mayr, Manuel
AU - Mayr M
LA - eng
GR - FS/13/2/29892/British Heart Foundation/United Kingdom
GR - British Heart Foundation/United Kingdom
GR - Department of Health/United Kingdom
PT - Journal Article
PT - Research Support, Non-U.S. Gov't
DEP - 20130123
PL - United States
TA - Mol Cell Proteomics
JT - Molecular & cellular proteomics : MCP
JID - 101125647
RN - 0 (Culture Media, Conditioned)
RN - 0 (Glycoproteins)
RN - 0 (Peptide Fragments)
RN - 0 (Proteome)
RN - NI40JAQ945 (Tetradecanoylphorbol Acetate)
SB - IM
MH - Amino Acid Sequence
MH - Carbohydrate Conformation
MH - Carbohydrate Sequence
MH - Cells, Cultured
MH - Culture Media, Conditioned
MH - Glycoproteins/chemistry/*metabolism
MH - Glycosylation
MH - Human Umbilical Vein Endothelial Cells/*metabolism
MH - Humans
MH - Molecular Sequence Data
MH - Peptide Fragments/chemistry
MH - *Protein Processing, Post-Translational
MH - Proteome/chemistry/*metabolism
MH - Tetradecanoylphorbol Acetate/pharmacology
PMC - PMC3617342
EDAT- 2013/01/25 06:00
MHDA- 2013/09/17 06:00
CRDT- 2013/01/25 06:00
PHST- 2013/01/25 06:00 [entrez]
PHST- 2013/01/25 06:00 [pubmed]
PHST- 2013/09/17 06:00 [medline]
AID - M112.024018 [pii]
AID - 10.1074/mcp.M112.024018 [doi]
PST - ppublish
SO - Mol Cell Proteomics. 2013 Apr;12(4):956-78. doi: 10.1074/mcp.M112.024018. Epub
2013 Jan 23.
PMID- 9884403
OWN - NLM
STAT- MEDLINE
DCOM- 19990210
LR - 20101118
IS - 0959-6658 (Print)
IS - 0959-6658 (Linking)
VI - 9
IP - 1
DP - 1999 Jan
TI - Glycosylation sites and site-specific glycosylation in human Tamm-Horsfall
glycoprotein.
PG - 21-30
AB - The N-glycosylation sites of human Tamm-Horsfall glycoprotein from one healthy
male donor have been characterized, based on an approach using endoproteinase
Glu-C (V-8 protease, Staphylococcus aureus ) digestion and a combination of
chromatographic techniques, automated Edman sequencing, and fast atom bombardment
mass spectrometry. Seven out of the eight potential N-glycosylation sites,
namely, Asn52, Asn56, Asn208, Asn251, Asn298, Asn372, and Asn489, turned out to
be glycosylated, and the potential glycosylation site at Asn14, being close to
the N-terminus, is not used. The carbohydrate microheterogeneity on three of the
glycosylation sites was studied in more detail by high-pH anion-exchange
chromatographic profiling and 500 MHz1H-NMR spectroscopy. Glycosylation site
Asn489 contains mainly di- and tri-charged oligosaccharides which comprise, among
others, the GalNAc4 S (beta1-4)GlcNAc terminal sequence. Only glycosylation site
Asn251 bears oligomannose-type carbohydrate chains ranging from Man5GlcNAc2to
Man8GlcNAc2, in addition to a small amount of complex-type structures. Profiling
of the carbohydrate moieties of Asn208 indicates a large heterogeneity, similar
to that established for native human Tamm-Horsfall glycoprotein, namely, multiply
charged complex-type carbohydrate structures, terminated by sulfate groups,
sialic acid residues, and/or the Sda-determinant.
FAU - van Rooijen, J J
AU - van Rooijen JJ
AD - Bijvoet Center, Department of Bio-Organic Chemistry, Utrecht University, P.O. Box
80075, NL-3508 TB Utrecht, The Netherlands.
FAU - Voskamp, A F
AU - Voskamp AF
FAU - Kamerling, J P
AU - Kamerling JP
FAU - Vliegenthart, J F
AU - Vliegenthart JF
LA - eng
PT - Journal Article
PT - Research Support, Non-U.S. Gov't
PL - England
TA - Glycobiology
JT - Glycobiology
JID - 9104124
RN - 0 (Mucoproteins)
RN - 0 (Peptide Fragments)
RN - 0 (UMOD protein, human)
RN - 0 (Uromodulin)
RN - 7006-34-0 (Asparagine)
RN - EC 3.4.21.- (Serine Endopeptidases)
RN - EC 3.4.21.19 (glutamyl endopeptidase)
SB - IM
MH - Amino Acid Sequence
MH - Asparagine/metabolism
MH - Binding Sites
MH - Carbohydrate Conformation
MH - Chromatography, Affinity
MH - Chromatography, High Pressure Liquid
MH - Glycosylation
MH - Humans
MH - Magnetic Resonance Spectroscopy
MH - Male
MH - Molecular Sequence Data
MH - Mucoproteins/*chemistry/*urine
MH - Peptide Fragments/chemistry/metabolism
MH - Sequence Analysis
MH - Serine Endopeptidases/metabolism
MH - Spectrometry, Mass, Fast Atom Bombardment
MH - Uromodulin
EDAT- 1999/01/13 00:00
MHDA- 1999/01/13 00:01
CRDT- 1999/01/13 00:00
PHST- 1999/01/13 00:00 [pubmed]
PHST- 1999/01/13 00:01 [medline]
PHST- 1999/01/13 00:00 [entrez]
AID - cwc003 [pii]
PST - ppublish
SO - Glycobiology. 1999 Jan;9(1):21-30.
PMID- 8344280
OWN - NLM
STAT- MEDLINE
DCOM- 19930903
LR - 20161017
IS - 0014-2956 (Print)
IS - 0014-2956 (Linking)
VI - 215
IP - 1
DP - 1993 Jul 1
TI - Biosynthesis and secretion of human interleukin 2 glycoprotein variants from
baculovirus-infected Sf21 cells. Characterization of polypeptides and
posttranslational modifications.
PG - 189-97
AB - Human interleukin 2 (IL-2) and human IL-2 mutant proteins, with artificially
introduced N-glycosylation or O-glycosylation sites, have been expressed in a
lepidopteran cell line (Sf21, Spodoptera frugiperda) using recombinant
baculovirus vectors. Only approximately 25% of the total recombinant IL-2 protein
synthesized by Sf21 cells was secreted into the culture medium. Significant
N-terminal truncations were detected in the secreted polypeptides (up to 85% of
the molecules). Alanine and proline were absent in the major truncated forms; the
first 3-5 amino acids were also absent in a small proportion of the purified
proteins. The introduction of potential artificial O-glycosylation peptide
sequences (..GGKAPTPPPK..), to the C-terminus or between positions 80 and 81 of
the IL-2 polypeptide chain, resulted in the secretion of unglycosylated and
O-glycosylated variant forms. Fast atom bombardment mass spectrometry,
compositional analysis and methylation analysis, of the tryptic glycopeptide
APTPPPK, revealed the presence of either GalNAc or the disaccharide Gal(beta
1-3)GalNAc as the only carbohydrate constituents attached exclusively to Thr in
this peptide, in a specific ratio for each individual IL-2 mutant protein. The
Gal(beta 1-3)GalNAc protein forms could be partially altered in vitro to
mammalian-type glycoforms by porcine liver beta-galactoside
alpha-2,3-sialyltransferase in the presence of CMP-N-acetylneuraminic acid. An
IL-2 mutant form, with an 11-amino-acid peptide of human interferon-beta at
position 4, which includes its only N-glycosylation site, had exclusively
truncated proximally fucosylated oligomannosidic glycans; Man3GlcNAc[Fuc(alpha
1-6)]GlcNAc or Man2GlcNAc[Fuc(alpha 1-6)]GlcNAc structures, in a ratio of 3:1,
were detected in the secreted proteins. No evidence was obtained for the presence
of secreted proteins with complex oligosaccharide chains, irrespective of the
cell-culture conditions used or the harvesting time, for infected cells with
recombinant baculovirus constructs.
FAU - Grabenhorst, E
AU - Grabenhorst E
AD - Department of Cell Biology and Genetics, Gesellschaft fur Biotechnologische
Forschung, Braunschweig, Germany.
FAU - Hofer, B
AU - Hofer B
FAU - Nimtz, M
AU - Nimtz M
FAU - Jager, V
AU - Jager V
FAU - Conradt, H S
AU - Conradt HS
LA - eng
PT - Journal Article
PL - England
TA - Eur J Biochem
JT - European journal of biochemistry
JID - 0107600
RN - 0 (Interleukin-2)
RN - 0 (Recombinant Proteins)
SB - IM
MH - Amino Acid Sequence
MH - Animals
MH - Baculoviridae/metabolism
MH - Carbohydrate Sequence
MH - Cell Line
MH - Glycosylation
MH - Humans
MH - Interleukin-2/*biosynthesis/chemistry/metabolism
MH - Molecular Sequence Data
MH - Moths
MH - Peptide Mapping
MH - *Protein Processing, Post-Translational
MH - Recombinant Proteins/*biosynthesis
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]
PST - ppublish
SO - Eur J Biochem. 1993 Jul 1;215(1):189-97.
PMID- 6192908
OWN - NLM
STAT- MEDLINE
DCOM- 19831021
LR - 20061115
IS - 0008-5472 (Print)
IS - 0008-5472 (Linking)
VI - 43
IP - 10
DP - 1983 Oct
TI - Sugar chain of alpha-fetoprotein produced in human yolk sac tumor.
PG - 4691-5
AB - The carbohydrate moiety of alpha-fetoprotein purified from human yolk sac tumors
grown in nude mice was quantitatively released from the polypeptide chain as
oligosaccharides by hydrazinolysis. The oligosaccharides were separated into a
neutral and two acidic oligosaccharides by paper electrophoresis. By sequential
exoglycosidase digestion in combination with per-O-methylation study and
periodate oxidation, their structures were determined to be: Gal beta 1 leads to
4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(GlcNAc beta 1 leads to 4) (Gal
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 4(Fuc alpha 1 leads to 6)GlcNAcOT, Gal beta 1 leads to
4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(GlcNAc beta 1 leads to 4) (Sia
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 4(Fuc alpha 1 leads to
6)GlcNAcOT; and Sia alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to
2Man alpha 1 leads to 6(GlcNAc beta 1 leads to 4) (Sia 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 4
GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6)GlcNAcOT, in which Gal is
galactose, GlcNac is N-acetylglucosamine, Man is mannose, Fuc is fucose, Sia is
sialic acid, and Subscript OT is the NaB3H4-reduced oligosaccharide.
FAU - Yamashita, K
AU - Yamashita K
FAU - Hitoi, A
AU - Hitoi A
FAU - Tsuchida, Y
AU - Tsuchida Y
FAU - Nishi, S
AU - Nishi S
FAU - Kobata, A
AU - Kobata A
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 (Oligosaccharides)
RN - 0 (alpha-Fetoproteins)
SB - IM
MH - Carbohydrate Sequence
MH - Electrophoresis, Paper
MH - Female
MH - Humans
MH - Mesonephroma/*analysis
MH - Oligosaccharides/analysis
MH - Ovarian Neoplasms/*analysis
MH - alpha-Fetoproteins/*analysis
EDAT- 1983/10/01 00:00
MHDA- 1983/10/01 00:01
CRDT- 1983/10/01 00:00
PHST- 1983/10/01 00:00 [pubmed]
PHST- 1983/10/01 00:01 [medline]
PHST- 1983/10/01 00:00 [entrez]
PST - ppublish
SO - Cancer Res. 1983 Oct;43(10):4691-5.
PMID- 7944531
OWN - NLM
STAT- MEDLINE
DCOM- 19941107
LR - 20181113
IS - 1468-2044 (Electronic)
IS - 0003-9888 (Linking)
VI - 71
IP - 2
DP - 1994 Aug
TI - Carbohydrate deficient glycoprotein syndrome type II: a deficiency in Golgi
localised N-acetyl-glucosaminyltransferase II.
PG - 123-7
AB - The carbohydrate deficient glycoprotein (CDG) syndromes are a family of genetic
multisystemic disorders with severe nervous system involvement. This report is on
a child with a CDG syndrome that differs from the classical picture but is very
similar to a patient reported in 1991. Both these patients are therefore
designated CDG syndrome type II. Compared with type I patients they have a more
severe psychomotor retardation but no peripheral neuropathy nor cerebellar
hypoplasia. The serum transferrin isoform pattern obtained by isoelectric
focusing showed disialotransferrin as the major fraction. The serum
disialotransferrin, studied in the present patient, contained two moles of
truncated monoantennary Sialyl-Gal-GlcNAc-Man(alpha 1-->3)[Man(alpha
1-->6)]Man(beta 1-->4)GlcNAc (beta 1-->4)GlcNAc-Asn per mole of transferrin. A
profoundly deficient activity of the Golgi enzyme N-acetylglucosaminyltransferase
II (EC 2.4.1.143) was demonstrated in fibroblasts.
FAU - Jaeken, J
AU - Jaeken J
AD - Department of Paediatrics, University Hospital Gasthuisberg, Leuven, Belgium.
FAU - Schachter, H
AU - Schachter H
FAU - Carchon, H
AU - Carchon H
FAU - De Cock, P
AU - De Cock P
FAU - Coddeville, B
AU - Coddeville B
FAU - Spik, G
AU - Spik G
LA - eng
PT - Case Reports
PT - Journal Article
PT - Research Support, Non-U.S. Gov't
PL - England
TA - Arch Dis Child
JT - Archives of disease in childhood
JID - 0372434
RN - 0 (Glycoproteins)
RN - 0 (Transferrin)
RN - EC 2.4.1.- (N-Acetylglucosaminyltransferases)
RN - EC 2.4.1.146 (beta-1,3-galactosyl-0-glycosyl-glycoprotein
beta-1,3-N-acetylglucosaminyltransferase)
SB - AIM
SB - IM
MH - Carbohydrate Metabolism, Inborn Errors/blood/*classification/enzymology
MH - Carbohydrate Sequence
MH - Child
MH - Fibroblasts/enzymology
MH - Glycoproteins/*metabolism
MH - Glycosylation
MH - Golgi Apparatus/*enzymology
MH - Humans
MH - Isoelectric Focusing
MH - Male
MH - Molecular Sequence Data
MH - N-Acetylglucosaminyltransferases/*deficiency
MH - Transferrin/analysis
PMC - PMC1029941
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]
PST - ppublish
SO - Arch Dis Child. 1994 Aug;71(2):123-7.
PMID- 2971663
OWN - NLM
STAT- MEDLINE
DCOM- 19881110
LR - 20171116
IS - 0021-9258 (Print)
IS - 0021-9258 (Linking)
VI - 263
IP - 29
DP - 1988 Oct 15
TI - Human T-lymphocyte activation is associated with changes in O-glycan
biosynthesis.
PG - 15146-50
AB - The activation of human T-lymphocytes by anti-CD3 antibodies and interleukin-2
results in a marked increase in apparent molecular weight of the major
cell-surface sialoglycoprotein. Both forms of the sialoglycoprotein were
identified as leukosialin by a monospecific antiserum, and the differences in
molecular weight were found to be due to changes in the carbohydrate structures.
Our results suggest that resting T-lymphocytes express on leukosialin the
disialotetrasaccharides NeuNAc alpha 2----3Gal beta 1----3(NeuNAc alpha
2----6)Gal-NAc-Ser/Thr, whereas activated human T-cells carry on leukosialin
exclusively the more complex structures NeuNAc alpha 2----3Gal beta 1----3(NeuNAc
alpha 2----3Gal beta 1----4GlcNAc beta 1----6)GalNAc-Ser/Thr. The radical shift
in the biosynthetic pathway of O-glycans in activated T-lymphocytes compared to
resting cells is apparently caused by a decrease of alpha 2----6
sialyltransferase activity and by the parallel dramatic stimulation of the beta
1----6GlcNAc-transferase. Since both enzymes compete for the same precursor
substrate, the coordinate changes in their activities are most likely responsible
for the complete change of the carbohydrate structures on leukosialin during the
activation of human T-lymphocytes.
FAU - Piller, F
AU - Piller F
AD - Cancer Research Center, La Jolla Cancer Research Foundation, California.
FAU - Piller, V
AU - Piller V
FAU - Fox, R I
AU - Fox RI
FAU - Fukuda, M
AU - Fukuda M
LA - eng
GR - CA33895/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 (Immune Sera)
RN - 0 (Leukosialin)
RN - 0 (Oligosaccharides)
RN - 0 (Polysaccharides)
RN - 0 (Sialoglycoproteins)
RN - 0 (UN1 sialoglycoprotein, human)
SB - IM
MH - *Antigens, CD
MH - Carbohydrate Conformation
MH - Carbohydrate Sequence
MH - Humans
MH - Immune Sera
MH - In Vitro Techniques
MH - Leukosialin
MH - *Lymphocyte Activation
MH - Molecular Sequence Data
MH - Oligosaccharides/isolation & purification
MH - Polysaccharides/*biosynthesis
MH - Sialoglycoproteins/*biosynthesis/isolation & purification
MH - T-Lymphocytes/*immunology/metabolism
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 - J Biol Chem. 1988 Oct 15;263(29):15146-50.
PMID- 8390218
OWN - NLM
STAT- MEDLINE
DCOM- 19930709
LR - 20171116
IS - 0003-9861 (Print)
IS - 0003-9861 (Linking)
VI - 303
IP - 2
DP - 1993 Jun
TI - Structural analysis on the sugar chains of human alpha 1-antitrypsin: presence of
fucosylated biantennary glycan in hepatocellular carcinoma.
PG - 281-7
AB - Chemical structures of the sugar chains of alpha 1-antitrypsin (AAT) from
patients with hepatocellular carcinoma (HCC) and from healthy individuals with a
different affinity for Lens culinaris agglutinin (LCA) were examined by
pyridylamination of their oligosaccharides and stepwise exoglycosidase digestion
in combination with reversed-phase and size-fractionation high-performance liquid
chromatography. We found that the LCA-reactive species of AAT from patients with
HCC carried both the biantennary sugar chain with a fucose residue at the
innermost N-acetylglucosamine residue, 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-PA, and the biantennary chain without a fucose residue, 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 1-4GlcNAc-PA, at a ratio of about 1:0.6. The LCA-nonreactive
species of AAT contained the biantennary sugar chain 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
1-4GlcNAc as a major component. These results indicate that a characteristic
feature of the carbohydrate chains of AAT from patients with HCC is an increment
in fucosylation.
FAU - Saitoh, A
AU - Saitoh A
AD - Department of Internal Medicine, Niigata University School of Medicine, Japan.
FAU - Aoyagi, Y
AU - Aoyagi Y
FAU - Asakura, H
AU - Asakura H
LA - eng
PT - Journal Article
PL - United States
TA - Arch Biochem Biophys
JT - Archives of biochemistry and biophysics
JID - 0372430
RN - 0 (Carbohydrates)
RN - 0 (Lectins)
RN - 0 (Plant Lectins)
RN - 0 (Polysaccharides)
RN - 0 (alpha 1-Antitrypsin)
RN - 0 (lentil lectin)
RN - 28RYY2IV3F (Fucose)
RN - EC 3.2.1.51 (alpha-L-Fucosidase)
SB - IM
MH - Carbohydrate Metabolism
MH - Carbohydrate Sequence
MH - Carbohydrates/*chemistry
MH - Carcinoma, Hepatocellular/*chemistry
MH - Chromatography, High Pressure Liquid
MH - Fucose/*metabolism
MH - Humans
MH - Lectins/metabolism
MH - Liver Neoplasms/*chemistry
MH - Molecular Sequence Data
MH - *Plant Lectins
MH - Polysaccharides/*analysis
MH - alpha 1-Antitrypsin/*chemistry/metabolism
MH - alpha-L-Fucosidase/metabolism
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 - S0003-9861(83)71284-1 [pii]
AID - 10.1006/abbi.1993.1284 [doi]
PST - ppublish
SO - Arch Biochem Biophys. 1993 Jun;303(2):281-7. doi: 10.1006/abbi.1993.1284.
PMID- 8639592
OWN - NLM
STAT- MEDLINE
DCOM- 19960715
LR - 20061115
IS - 0006-2960 (Print)
IS - 0006-2960 (Linking)
VI - 35
IP - 20
DP - 1996 May 21
TI - Amino acid sequence and carbohydrate structure of a recombinant human tissue
factor pathway inhibitor expressed in Chinese hamster ovary cells: one N-and two
O-linked carbohydrate chains are located between Kunitz domains 2 and 3 and one
N-linked carbohydrate chain is in Kunitz domain 2.
PG - 6450-9
AB - Human tissue factor pathway inhibitor is a protease inhibitor with three tandem
Kunitz-type inhibitory domains. The recombinant protein (r-hTFPI) was produced
using Chinese hamster ovary cells, and its polypeptide and carbohydrate chain
structures were analyzed. The complete amino acid sequence, composed of 276
residues, was determined using a protein sequencer after protease digestion and
it was identical to that predicted from the cDNA sequence. Among three potential
N-glycosylation sites, both Asn117 and Asn167 were fully N-glycosylated but
Asn228 was not. Thr175 was also fully O-glycosylated, but Ser174 was partially
O-glycosylated. Carbohydrate composition and mass spectrometric analyses of the
undecapeptide OG-11 (residues Leu 170approximately Leu180) showed that two
O-linked carbohydrate chains consisted of a type-1 core structure
(Gal-GalNAc-Ser/Thr) with 0-3 mol of N-acetylneuraminic acid(s). The N-linked
carbohydrate chains were analyzed by two-dimensional carbohydrate mapping
combined with sequential glycosidase digestion, after the reducing-ends of
carbohydrate residues were tagged with 2-aminopyridine and non-reducing-end
sialic acids were removed with sialidase. All the N-linked structures in r-hTFPI
were complex-type carbohydrate chains with one fucose residue attached to the
reducing-end GlcNAc and consisted of bi-, tri-, and tetraantennary carbohydrate
chains in the ratio 1.9:1.3:1.0. Fucosylated tri- and tetraantennary carbohydrate
chains with one or two N-acetyllactosaminyl repeats were also found (30% of
carbohydrate chains determined). Thus, the region between Kunitz domains 2 and 3
encoded by exon 7 was highly glycosylated by two O-linked carbohydrate chains at
Ser174 and Thr175 and one N-linked carbohydrate chain at Asn167. These results
indicated that the region is occupied by a cluster of three bulky and acidic
carbohydrate chains.
FAU - Nakahara, Y
AU - Nakahara Y
AD - Chemo-Sero-Therapeutic Research Institute, Kumamoto, Japan.
FAU - Miyata, T
AU - Miyata T
FAU - Hamuro, T
AU - Hamuro T
FAU - Funatsu, A
AU - Funatsu A
FAU - Miyagi, M
AU - Miyagi M
FAU - Tsunasawa, S
AU - Tsunasawa S
FAU - Kato, H
AU - Kato H
LA - eng
PT - Comparative Study
PT - Journal Article
PT - Research Support, Non-U.S. Gov't
PL - United States
TA - Biochemistry
JT - Biochemistry
JID - 0370623
RN - 0 (Carbohydrates)
RN - 0 (Lipoproteins)
RN - 0 (Recombinant Proteins)
RN - 0 (lipoprotein-associated coagulation inhibitor)
SB - IM
MH - Amino Acid Sequence
MH - Animals
MH - CHO Cells
MH - Carbohydrate Conformation
MH - Carbohydrate Sequence
MH - Carbohydrates/analysis
MH - Cricetinae
MH - Glycosylation
MH - Humans
MH - Lipoproteins/*chemistry/genetics
MH - Mass Spectrometry
MH - Molecular Sequence Data
MH - Molecular Structure
MH - Recombinant Proteins/chemistry/genetics
MH - Sequence Homology, Amino Acid
EDAT- 1996/05/21 00:00
MHDA- 1996/05/21 00:01
CRDT- 1996/05/21 00:00
PHST- 1996/05/21 00:00 [pubmed]
PHST- 1996/05/21 00:01 [medline]
PHST- 1996/05/21 00:00 [entrez]
AID - 10.1021/bi9524880 [doi]
AID - bi9524880 [pii]
PST - ppublish
SO - Biochemistry. 1996 May 21;35(20):6450-9. doi: 10.1021/bi9524880.
PMID- 8026573
OWN - NLM
STAT- MEDLINE
DCOM- 19940809
LR - 20061115
IS - 0014-5793 (Print)
IS - 0014-5793 (Linking)
VI - 348
IP - 1
DP - 1994 Jul 4
TI - Rapid and simple approach for the NMR resonance assignment of the carbohydrate
chains of an intact glycoprotein. Application of gradient-enhanced natural
abundance 1H-13C HSQC and HSQC-TOCSY to the alpha-subunit of human chorionic
gonadotropin.
PG - 1-6
AB - The structure assessment of an intact glycoprotein in solution requires an
extensive assignment of the carbohydrate NMR resonances. However, assignment of
homonuclear spectra is very complicated because of the severe overlap of protein
and carbohydrate signals. Application of pulsed field gradients allowed high
quality natural abundance 1H-13C HSQC and HSQC-TOCSY spectra to be recorded of
the alpha-subunit of human chorionic gonadotropin. Most carbohydrate 1H-13C
correlations appear in a distinct region between the aromatic region and the
protein C alpha-H alpha region. The enormous reduction in overlap led to fast and
unambiguous assignment of the anomeric 1H-13C correlations. Subsequently,
correlations of the monosaccharide skeleton atoms were readily assigned in the
HSQC-TOCSY spectrum.
FAU - de Beer, T
AU - de Beer T
AD - Department of Bio-Organic Chemistry, Utrecht University, The Netherlands.
FAU - van Zuylen, C W
AU - van Zuylen CW
FAU - Hard, K
AU - Hard K
FAU - Boelens, R
AU - Boelens R
FAU - Kaptein, R
AU - Kaptein R
FAU - Kamerling, J P
AU - Kamerling JP
FAU - Vliegenthart, J F
AU - Vliegenthart JF
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 (Chorionic Gonadotropin)
RN - 0 (Glycoproteins)
SB - IM
MH - Carbohydrate Sequence
MH - Chorionic Gonadotropin/*chemistry
MH - Glycoproteins/*chemistry
MH - Humans
MH - Magnetic Resonance Spectroscopy/*methods
MH - Molecular Sequence Data
EDAT- 1994/07/04 00:00
MHDA- 1994/07/04 00:01
CRDT- 1994/07/04 00:00
PHST- 1994/07/04 00:00 [pubmed]
PHST- 1994/07/04 00:01 [medline]
PHST- 1994/07/04 00:00 [entrez]
AID - 0014-5793(94)00547-8 [pii]
PST - ppublish
SO - FEBS Lett. 1994 Jul 4;348(1):1-6.
PMID- 11168369
OWN - NLM
STAT- MEDLINE
DCOM- 20010329
LR - 20171116
IS - 0014-2956 (Print)
IS - 0014-2956 (Linking)
VI - 268
IP - 2
DP - 2001 Jan
TI - A nucleotide insertion and frameshift cause albumin Kenitra, an extended and
O-glycosylated mutant of human serum albumin with two additional disulfide
bridges.
PG - 344-52
AB - Albumin Kenitra is a new type of genetic variant of human serum albumin that has
been found in two members of a family of Sephardic Jews from Kenitra (Morocco).
The slow-migrating variant and the normal protein were isolated by anion-exchange
chromatography and, after treatment with CNBr, the digests were analyzed by
two-dimensional electrophoresis in a polyacrylamide gel. The CNBr peptides of the
variant were purified by reverse-phase high performance liquid chromatography and
submitted to sequence analysis. Albumin Kenitra is peculiar because it has an
elongated polypeptide chain, 601 residues instead of 585, and its sequence is
modified beginning from residue 575. DNA structural studies showed that the
variant is caused by a single-base insertion, an adenine at nucleotide position
15 970 in the genomic sequence, which leads to a frameshift with the subsequent
translation to the first termination codon of exon 15. Mass spectrometric
analyses revealed that the four additional cysteine residues of the variant form
two new S-S bridges and showed that albumin Kenitra is partially O-glycosylated
by a monosialylated HexHexNAc structure. This oligosaccharide chain has been
located to Thr596 by amino-acid sequence analysis of the tryptic fragment
592-597.
FAU - Minchiotti, L
AU - Minchiotti L
AD - Dipartimento di Biochimica A. Castellani, Universita di Pavia, via Taramelli 3B,
I-27100 Pavia, Italy.
FAU - Campagnoli, M
AU - Campagnoli M
FAU - Rossi, A
AU - Rossi A
FAU - Cosulich, M E
AU - Cosulich ME
FAU - Monti, M
AU - Monti M
FAU - Pucci, P
AU - Pucci P
FAU - Kragh-Hansen, U
AU - Kragh-Hansen U
FAU - Granel, B
AU - Granel B
FAU - Disdier, P
AU - Disdier P
FAU - Weiller, P J
AU - Weiller PJ
FAU - Galliano, M
AU - Galliano M
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 (ALB protein, human)
RN - 0 (Codon, Terminator)
RN - 0 (Disulfides)
RN - 0 (Glycoproteins)
RN - 0 (Oligosaccharides)
RN - 0 (Peptide Fragments)
RN - 0 (Serum Albumin)
RN - JAC85A2161 (Adenine)
RN - OS382OHJ8P (Cyanogen Bromide)
RN - ZIF514RVZR (Serum Albumin, Human)
SB - IM
MH - Adenine
MH - Amino Acid Sequence
MH - Codon, Terminator
MH - Cyanogen Bromide
MH - Disulfides/chemistry
MH - Exons
MH - *Frameshift Mutation
MH - Glycoproteins/*chemistry/*genetics
MH - Humans
MH - Jews
MH - Mass Spectrometry
MH - Molecular Sequence Data
MH - Morocco
MH - Oligosaccharides/chemistry
MH - Peptide Fragments/chemistry
MH - Peptide Mapping
MH - Serum Albumin/*chemistry/*genetics
MH - Serum Albumin, Human
EDAT- 2001/02/13 11:00
MHDA- 2001/04/03 10:01
CRDT- 2001/02/13 11:00
PHST- 2001/02/13 11:00 [pubmed]
PHST- 2001/04/03 10:01 [medline]
PHST- 2001/02/13 11:00 [entrez]
AID - ejb1899 [pii]
PST - ppublish
SO - Eur J Biochem. 2001 Jan;268(2):344-52.
PMID- 2386787
OWN - NLM
STAT- MEDLINE
DCOM- 19900927
LR - 20071114
IS - 0006-2960 (Print)
IS - 0006-2960 (Linking)
VI - 29
IP - 23
DP - 1990 Jun 12
TI - Oligosaccharide processing in the expression of human plasminogen cDNA by
lepidopteran insect (Spodoptera frugiperda) cells.
PG - 5584-90
AB - A comparison has been made between the Asn289-linked oligosaccharide structures
of human plasma plasminogen and a recombinant human plasminogen, expressed in
lepidopteran insect (Spodoptera frugiperda) cells, after infection of these cells
with a recombinant baculovirus containing the entire human plasminogen cDNA.
Using anion-exchange liquid chromatography mapping of the oligosaccharide units
cleaved from the proteins by glycopeptidase F, compared with elution positions of
standard oligosaccharide structures, coupled with monosaccharide compositional
analysis, we find that the human plasma protein contained only
bisialo-biantennary complex-type carbohydrate and asialo-biantennary complex
carbohydrate, confirming earlier work published by this laboratory. The
glycosylation pattern of the insect cell expressed recombinant human plasminogen
showed considerable microheterogeneity, with identifiable high-mannose
carbohydrate (Man9GlcNAc2) and truncated high-mannose oligosaccharide
(Man5GlcNAc2, Man4GlcNAc2, and Man3GlcNAc2). Of major importance, approximately
40% of the oligosaccharide population consisted of complex carbohydrate
(bisialo-biantennary), identical in structure with that of the human plasma
protein. This is the first direct identification of complex carbohydrate in
proteins produced in insect cells and demonstrates that trimming and processing
of high-mannose carbohydrate into complex-type oligosaccharide can occur. Our
data indicate that both normal and alternate pathways exist in these cells for
incorporation and trimming of high-mannose oligosaccharides and that
mannosidases, as well as galactosyl-, hexosaminidasyl-, and sialyltransferases
are present, and/or can be induced, in these cells. From these observations, we
conclude that amino acid sequences and/or protein conformational properties can
control oligosaccharide processing events.
FAU - Davidson, D J
AU - Davidson DJ
AD - Department of Chemistry and Biochemistry, University of Notre Dame, Indiana
46556.
FAU - Fraser, M J
AU - Fraser MJ
FAU - Castellino, F J
AU - Castellino FJ
LA - eng
GR - HL-13423/HL/NHLBI NIH HHS/United States
PT - Journal Article
PT - Research Support, U.S. Gov't, P.H.S.
PL - United States
TA - Biochemistry
JT - Biochemistry
JID - 0370623
RN - 0 (Oligosaccharides)
RN - 0 (Recombinant Proteins)
RN - 9001-91-6 (Plasminogen)
RN - 9007-49-2 (DNA)
SB - IM
MH - Animals
MH - Base Sequence
MH - Carbohydrate Sequence
MH - DNA/*genetics
MH - Gene Expression
MH - Glycosylation
MH - Humans
MH - Molecular Sequence Data
MH - Moths/genetics
MH - Mutation
MH - Oligosaccharides/*metabolism
MH - Plasminogen/genetics/*metabolism
MH - Recombinant Proteins/genetics
EDAT- 1990/06/12 00:00
MHDA- 1990/06/12 00:01
CRDT- 1990/06/12 00:00
PHST- 1990/06/12 00:00 [pubmed]
PHST- 1990/06/12 00:01 [medline]
PHST- 1990/06/12 00:00 [entrez]
PST - ppublish
SO - Biochemistry. 1990 Jun 12;29(23):5584-90.
PMID- 8631363
OWN - NLM
STAT- MEDLINE
DCOM- 19960703
LR - 20161017
IS - 0014-2956 (Print)
IS - 0014-2956 (Linking)
VI - 235
IP - 1-2
DP - 1996 Jan 15
TI - O-glycosylated species of natural human tumor-necrosis factor-alpha.
PG - 431-7
AB - Tumor-necrosis factor-alpha, produced by human B-cell lymphoblastoid cell line
BALL-1, was expressed as four protein bands on SDS/PAGE analysis. It may have
been glycosylated, based on the fact that the heavier two of the four bands
disappeared after neuraminidase treatment. Sugar composition analyses revealed
that the tumor necrosis factor-alpha contained galactose, N-acetylgalactosamine
and N-acetylneuraminic acid as sugar components. To prepare sugar chains, tumor
necrosis factor-alpha was treated with alkaline borodeuteride and the
oligosaccharide-alditols liberated were fractionated by gel-filtration
chromatography on a Bio-Gel P-4 column, followed by normal-phase HPLC. Three
oligosaccharide-alditols were obtained, and the structures of two of them were
identified by methylation analysis and exoglycosidase digestion. The structures
of these oligosaccharide-alditols were Gal beta 1-3(NeuAc alpha 2-6)GalNAcol and
Gal beta 1-3GalNAcol (GalNAcol, N-acetylgalactosaminitol). The structure of the
remaining oligosaccharide-alditol was determined to be NeuAc alpha
2-3Gal1-3GalNAcol by composition and methylation analyses. About 20% of tumor
necrosis factor-alpha was found to be 0-glycosylated, based on the results of the
sugar composition and structure analyses. An amino acid sequence analysis of the
glycosylated peptides was performed after Staphylococcus aureus V8 protease
digestion of tumor necrosis factor-alpha had been completed, and it was proved
that the 0-glycosylation site of tumor necrosis factor-alpha was Ser 4.
FAU - Takakura-Yamamoto, R
AU - Takakura-Yamamoto R
AD - Fujisaki Institute, Hayashibara Biochemical Laboratories, Inc., Okayama, Japan.
FAU - Yamamoto, S
AU - Yamamoto S
FAU - Fukuda, S
AU - Fukuda S
FAU - Kurimoto, M
AU - Kurimoto M
LA - eng
PT - Journal Article
PL - England
TA - Eur J Biochem
JT - European journal of biochemistry
JID - 0107600
RN - 0 (Oligosaccharides)
RN - 0 (Peptides)
RN - 0 (Sugar Alcohols)
RN - 0 (Tumor Necrosis Factor-alpha)
SB - IM
MH - Amino Acid Sequence
MH - Carbohydrate Sequence
MH - Cell Line
MH - Glycosylation
MH - Humans
MH - Molecular Sequence Data
MH - Molecular Structure
MH - Oligosaccharides/chemistry/isolation & purification
MH - Peptides
MH - Sugar Alcohols/chemistry/isolation & purification
MH - Tumor Necrosis Factor-alpha/*chemistry/genetics/isolation & purification
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 - Eur J Biochem. 1996 Jan 15;235(1-2):431-7.
PMID- 22171320
OWN - NLM
STAT- MEDLINE
DCOM- 20120807
LR - 20181113
IS - 1535-9484 (Electronic)
IS - 1535-9476 (Linking)
VI - 11
IP - 4
DP - 2012 Apr
TI - Human urinary glycoproteomics; attachment site specific analysis of N- and
O-linked glycosylations by CID and ECD.
PG - M111.013649
LID - 10.1074/mcp.M111.013649 [doi]
AB - Urine is a complex mixture of proteins and waste products and a challenging
biological fluid for biomarker discovery. Previous proteomic studies have
identified more than 2800 urinary proteins but analyses aimed at unraveling
glycan structures and glycosylation sites of urinary glycoproteins are lacking.
Glycoproteomic characterization remains difficult because of the complexity of
glycan structures found mainly on asparagine (N-linked) or serine/threonine
(O-linked) residues. We have developed a glycoproteomic approach that combines
efficient purification of urinary glycoproteins/glycopeptides with complementary
MS-fragmentation techniques for glycopeptide analysis. Starting from clinical
sample size, we eliminated interfering urinary compounds by dialysis and
concentrated the purified urinary proteins by lyophilization. Sialylated urinary
glycoproteins were conjugated to a solid support by hydrazide chemistry and
trypsin digested. Desialylated glycopeptides, released through mild acid
hydrolysis, were characterized by tandem MS experiments utilizing collision
induced dissociation (CID) and electron capture dissociation fragmentation
techniques. In CID-MS(2), Hex(5)HexNAc(4)-N-Asn and HexHexNAc-O-Ser/Thr were
typically observed, in agreement with known N-linked biantennary complex-type and
O-linked core 1-like structures, respectively. Additional glycoforms for specific
N- and O-linked glycopeptides were also identified, e.g. tetra-antennary
N-glycans and fucosylated core 2-like O-glycans. Subsequent CID-MS(3), of
selected fragment-ions from the CID-MS(2) analysis, generated peptide specific b-
and y-ions that were used for peptide identification. In total, 58 N- and 63
O-linked glycopeptides from 53 glycoproteins were characterized with respect to
glycan- and peptide sequences. The combination of CID and electron capture
dissociation techniques allowed for the exact identification of Ser/Thr
attachment site(s) for 40 of 57 putative O-glycosylation sites. We defined 29
O-glycosylation sites which have, to our knowledge, not been previously reported.
This is the first study of human urinary glycoproteins where "intact"
glycopeptides were studied, i.e. the presence of glycans and their attachment
sites were proven without doubt.
FAU - Halim, Adnan
AU - Halim A
AD - Department of Clinical Chemistry and Transfusion Medicine, Institute of
Biomedicine, Sahlgrenska Academy at the University of Gothenburg, Sweden.
FAU - Nilsson, Jonas
AU - Nilsson J
FAU - Ruetschi, Ulla
AU - Ruetschi U
FAU - Hesse, Camilla
AU - Hesse C
FAU - Larson, Goran
AU - Larson G
LA - eng
PT - Journal Article
PT - Research Support, Non-U.S. Gov't
DEP - 20111214
PL - United States
TA - Mol Cell Proteomics
JT - Molecular & cellular proteomics : MCP
JID - 101125647
RN - 0 (Glycopeptides)
RN - 0 (Glycoproteins)
RN - GZP2782OP0 (N-Acetylneuraminic Acid)
SB - IM
MH - Chromatography, Liquid
MH - Dialysis
MH - Glycopeptides/chemistry/*urine
MH - Glycoproteins/chemistry/*urine
MH - Glycosylation
MH - Humans
MH - Male
MH - N-Acetylneuraminic Acid/chemistry
MH - Proteomics/*methods
MH - Tandem Mass Spectrometry
PMC - PMC3322569
EDAT- 2011/12/16 06:00
MHDA- 2012/08/08 06:00
CRDT- 2011/12/16 06:00
PHST- 2011/12/16 06:00 [entrez]
PHST- 2011/12/16 06:00 [pubmed]
PHST- 2012/08/08 06:00 [medline]
AID - M111.013649 [pii]
AID - 10.1074/mcp.M111.013649 [doi]
PST - ppublish
SO - Mol Cell Proteomics. 2012 Apr;11(4):M111.013649. doi: 10.1074/mcp.M111.013649.
Epub 2011 Dec 14.
PMID- 23001782
OWN - NLM
STAT- MEDLINE
DCOM- 20130506
LR - 20121127
IS - 1615-9861 (Electronic)
IS - 1615-9853 (Linking)
VI - 12
IP - 22
DP - 2012 Nov
TI - Micro- and macroheterogeneity of N-glycosylation yields size and charge isoforms
of human sex hormone binding globulin circulating in serum.
PG - 3315-27
LID - 10.1002/pmic.201200354 [doi]
AB - Human sex hormone binding globulin (hSHBG) is a serum glycoprotein central to the
transport and targeted delivery of sex hormones to steroid-sensitive tissues.
Several molecular mechanisms of action of hSHBG, including the function of its
attached glycans remain unknown. Here, we perform a detailed site-specific
characterization of the N- and O-linked glycosylation of serum-derived hSHBG.
MS-driven glycoproteomics and glycomics combined with exoglycosidase treatment
were used in a bottom-up and top-down manner to determine glycosylation sites,
site-specific occupancies and monosaccharide compositions, detailed glycan
structures, and the higher level arrangement of glycans on intact hSHBG. It was
found that serum-derived hSHBG is N-glycosylated at Asn(351) and Asn(367) with
average molar occupancies of 85.1 and 95.3%, respectively. Both sites are
occupied by the same six sialylated and partly core fucosylated bi- and
triantennary N-Glycoforms with lactosamine-type antennas of the form
(+/-NeuAcalpha6)Galbeta4GlcNAc. N-Glycoforms of Asn(367) were slightly more
branched and core fucosylated than Asn(351) N-glycoforms due probably to a more
surface-exposed glycosylation site. The N-terminal Thr(7) was fully occupied by
the two O-linked glycans NeuAcalpha3Galbeta3(NeuAcalpha6)GalNAc (where NeuAc is
N-acetylneuraminic acid and GalNAc is N-acetylgalactosamine) and
NeuAcalpha3Galbeta3GalNAc in a 1:6 molar ratio. Electrophoretic analysis of
intact hSHBG revealed size and charge heterogeneity of the isoforms circulating
in blood serum. Interestingly, the size and charge heterogeneity were shown to
originate predominantly from differential Asn(351) glycan occupancies and
N-glycan sialylation that may modulate the hSHBG activity. To date, this work
represents the most detailed structural map of the heterogeneous hSHBG
glycosylation, which is a prerequisite for investigating the functional aspects
of the hSHBG glycans.
CI - (c) 2012 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
FAU - Sumer-Bayraktar, Zeynep
AU - Sumer-Bayraktar Z
AD - Department of Chemistry and Biomolecular Sciences, Macquarie University, Sydney,
Australia.
FAU - Nguyen-Khuong, Terry
AU - Nguyen-Khuong T
FAU - Jayo, Roxana
AU - Jayo R
FAU - Chen, David D Y
AU - Chen DD
FAU - Ali, Sinan
AU - Ali S
FAU - Packer, Nicolle H
AU - Packer NH
FAU - Thaysen-Andersen, Morten
AU - Thaysen-Andersen M
LA - eng
PT - Journal Article
PT - Research Support, Non-U.S. Gov't
DEP - 20121029
PL - Germany
TA - Proteomics
JT - Proteomics
JID - 101092707
RN - 0 (Glycoproteins)
RN - 0 (Polysaccharides)
RN - 0 (Protein Isoforms)
RN - 0 (Sex Hormone-Binding Globulin)
SB - IM
MH - Amino Acid Sequence
MH - Electrophoresis, Gel, Two-Dimensional
MH - Glycomics/methods
MH - Glycoproteins/blood/*chemistry/*metabolism
MH - Glycosylation
MH - Humans
MH - Molecular Sequence Data
MH - Polysaccharides/analysis/*chemistry/*metabolism
MH - Protein Isoforms
MH - Proteomics/methods
MH - Sex Hormone-Binding Globulin/*chemistry/*metabolism
EDAT- 2012/09/25 06:00
MHDA- 2013/05/07 06:00
CRDT- 2012/09/25 06:00
PHST- 2012/08/09 00:00 [received]
PHST- 2012/08/09 00:00 [revised]
PHST- 2012/08/31 00:00 [accepted]
PHST- 2012/09/25 06:00 [entrez]
PHST- 2012/09/25 06:00 [pubmed]
PHST- 2013/05/07 06:00 [medline]
AID - 10.1002/pmic.201200354 [doi]
PST - ppublish
SO - Proteomics. 2012 Nov;12(22):3315-27. doi: 10.1002/pmic.201200354. Epub 2012 Oct
29.
PMID- 1820200
OWN - NLM
STAT- MEDLINE
DCOM- 19920803
LR - 20171116
IS - 0959-6658 (Print)
IS - 0959-6658 (Linking)
VI - 1
IP - 4
DP - 1991 Sep
TI - Site-specific N-glycosylation of human chorionic gonadotrophin--structural
analysis of glycopeptides by one- and two-dimensional 1H NMR spectroscopy.
PG - 393-404
AB - Glycopeptides representing individual N-glycosylation sites of the heterodimeric
glycoprotein hormone human chorionic gonadotrophin (hCG) were obtained from
subunits hCG alpha (N-glycosylated at Asn-52 and Asn-78) and hCG beta
(N-glycosylated at Asn-13 and Asn-30) by digestion with trypsin and chymotrypsin,
respectively. Following purification by reverse-phase HPLC and identification by
amino acid sequencing, the glycopeptides were analysed by one- and
two-dimensional 1H NMR spectroscopy. The results are summarized as follows: (i)
oligosaccharides attached to Asn-52 of hCG alpha comprised monosialylated
'monoantenary' NeuAc alpha 2-3Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3[Man alpha
1-6]Man beta 1-4GlcNAc beta 1-4GlcNAc (N1-4'), disialylated diantennary NeuAc
alpha 2-3Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3[NeuAc alpha 2-3-Gal beta
1-4GlcNAc beta 1-2Man alpha 1-6]Man beta 1-4GlcNAc beta 1-4GlcNAc (N2), and the
monosialylated hybrid-type structures NeuAc alpha 2-3Gal beta 1-4GlcNAc beta
1-2Man alpha 1-3[Man alpha 1-3Man alpha 1-6]Man beta 1-4GlcNAc beta 1-4GlcNAc
(N1-A) and NeuAc alpha 2-3Gal-beta 1-4GlcNAc beta 1-2Man alpha 1-3[Man alpha
1-3(Man alpha 1-6)Man alpha 1-6]Man beta 1-4GlcNAc beta 1-4GlcNAc (N1-AB) in a
ratio approaching 5:2:2:1; (ii) Asn-78 of hCG alpha carried N2 and N1-4' almost
exclusively (ratio approximately 3:2); (iii) both N-glycosylation sites of hCG
beta contained predominantly component N2, partially (approximately 25%) and
completely alpha 1-6-fucosylated at the N-acetylglucosamine linked to Asn-13 and
Asn-30, respectively. The distinct site-specific distribution of the
oligosaccharide structures among individual N-glycosylation sites of hCG appears
to reflect primarily the influence of the surrounding protein structure on the
substrate accessibility of the Golgi processing enzymes alpha-mannosidase II,
GlcNAc transferase II and alpha 1,6-fucosyltransferase.
FAU - Weisshaar, G
AU - Weisshaar G
AD - Department of Biochemistry, University of Auckland, New Zealand.
FAU - Hiyama, J
AU - Hiyama J
FAU - Renwick, A G
AU - Renwick AG
LA - eng
PT - Journal Article
PT - Research Support, Non-U.S. Gov't
PL - England
TA - Glycobiology
JT - Glycobiology
JID - 9104124
RN - 0 (Chorionic Gonadotropin)
RN - 0 (Glycopeptides)
RN - 0 (Macromolecular Substances)
RN - 0 (Oligosaccharides)
RN - 28RYY2IV3F (Fucose)
RN - 7006-34-0 (Asparagine)
RN - V956696549 (Acetylglucosamine)
SB - IM
MH - Acetylglucosamine/metabolism
MH - Amino Acid Sequence
MH - Asparagine/metabolism
MH - Carbohydrate Sequence
MH - Chorionic Gonadotropin/*chemistry/metabolism
MH - Fucose/metabolism
MH - Glycopeptides/*chemistry/isolation & purification
MH - Glycosylation
MH - Humans
MH - Macromolecular Substances
MH - Magnetic Resonance Spectroscopy
MH - Molecular Sequence Data
MH - Oligosaccharides/*chemistry
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 - Glycobiology. 1991 Sep;1(4):393-404.
PMID- 2110822
OWN - NLM
STAT- MEDLINE
DCOM- 19900620
LR - 20061115
IS - 0006-2960 (Print)
IS - 0006-2960 (Linking)
VI - 29
IP - 12
DP - 1990 Mar 27
TI - Characteristics of asparagine-linked sugar chains of sphingolipid activator
protein 1 purified from normal human liver and GM1 gangliosidosis (type 1) liver.
PG - 3030-9
AB - Asparagine-linked sugar chains of sphingolipid activator protein 1 (SAP-1)
purified from normal human liver and GM1 gangliosidosis (type 1) liver were
comparatively investigated. Oligosaccharides released from the two SAP-1 samples
by hydrazinolysis were fractionated by paper electrophoresis and by Aleuria
aurantia lectin-Sepharose and Bio-Gel P-4 (under 400 mesh) column chromatography.
Structures of oligosaccharides in each fraction were estimated from data on their
effective molecular sizes, behavior on immobilized lectin columns with different
carbohydrate-binding specificities, results of sequential digestion by
exoglycosidases with different aglycon specificities, and methylation analysis.
Sugar chains of SAP-1 purified from normal human liver and from GM1
gangliosidosis (type 1) liver were different from each other, although both of
them were derived from complex-type sugar chains. The sugar chains of the former
were the following eight degradation products from complex-type sugar chains by
exoglycosidases in lysosomes: Man alpha 1----6(Man alpha 1----3)Man beta
1----4GlcNAc beta 1----4GlcNAcOT, Man alpha 1----6(Man alpha 1----3)Man beta
1----4GlcNAc beta 1----4(Fuc alpha 1----6)GlcNAcOT, Man alpha 1----6Man beta
1----4GlcNAc beta 1----4GlcNAcOT, Man alpha 1----6Man beta 1----4GlcNAc beta
1----4(Fuc alpha 1----6)GlcNAcOT, Man beta 1----4GlcNAc beta 1----4GlcNAcOT, Man
beta 1----4GlcNAc beta 1----4(Fuc alpha 1----6)GlcNAcOT, GlcNAc beta
1----4GlcNAcOT, and GlcNAcOT. In contrast to these, the sugar chains of the
latter were sialylated and nonsialylated mono- to tetraantennary complex-type
sugar chains that were not fully degraded due to a metabolic defect in acid
beta-galactosidase activity.
FAU - Yamashita, K
AU - Yamashita K
AD - Department of Biochemistry, Kobe University School of Medicine, Hyogo, Japan.
FAU - Inui, K
AU - Inui K
FAU - Totani, K
AU - Totani K
FAU - Kochibe, N
AU - Kochibe N
FAU - Furukawa, M
AU - Furukawa M
FAU - Okada, S
AU - Okada S
LA - eng
PT - Journal Article
PT - Research Support, Non-U.S. Gov't
PL - United States
TA - Biochemistry
JT - Biochemistry
JID - 0370623
RN - 0 (Glycoproteins)
RN - 0 (Oligosaccharides)
RN - 0 (PSAP protein, human)
RN - 0 (Saposins)
RN - 0 (Sphingolipid Activator Proteins)
RN - 37758-47-7 (G(M1) Ganglioside)
RN - 7006-34-0 (Asparagine)
RN - EC 3.2.1.- (Glycoside Hydrolases)
RN - EC 3.2.1.18 (Neuraminidase)
SB - IM
MH - Asparagine
MH - Carbohydrate Conformation
MH - Carbohydrate Sequence
MH - Chromatography, Affinity
MH - G(M1) Ganglioside
MH - Gangliosidoses/*metabolism
MH - Glycoproteins/*isolation & purification
MH - Glycoside Hydrolases
MH - Humans
MH - Liver/*analysis
MH - Molecular Sequence Data
MH - Neuraminidase
MH - Oligosaccharides/*isolation & purification
MH - Reference Values
MH - Saposins
MH - Sphingolipid Activator Proteins
EDAT- 1990/03/27 00:00
MHDA- 1990/03/27 00:01
CRDT- 1990/03/27 00:00
PHST- 1990/03/27 00:00 [pubmed]
PHST- 1990/03/27 00:01 [medline]
PHST- 1990/03/27 00:00 [entrez]
PST - ppublish
SO - Biochemistry. 1990 Mar 27;29(12):3030-9.
PMID- 3571205
OWN - NLM
STAT- MEDLINE
DCOM- 19870601
LR - 20071219
IS - 0021-924X (Print)
IS - 0021-924X (Linking)
VI - 101
IP - 1
DP - 1987 Jan
TI - The carbohydrate moiety of human platelet glycocalicin: the structures of the
major Asn-linked sugar chains.
PG - 241-9
AB - Glycocalicin, a predominant glycoprotein on the human platelet surface, has been
purified from a platelet suspension by means of sonication, ammonium sulfate
precipitation and acid treatment followed by chromatography on columns of wheat
germ agglutinin-Sepharose and Mono Q. Asparagine-linked (N-linked)
oligosaccharides were released by hydrazinolysis, and then N-acetylated and
reduced with NaBH4 or NaB3H4. The released carbohydrate chains were found to be
of the complex-type from their interaction with immobilized lectin columns. The
structures of the two major oligosaccharide-alditols separated by ion-exchange
chromatography on a Mono Q column were investigated by means of methylation
analysis, glycosidase digestion, and Smith periodate degradation, and they were
assigned as typical di- and trisialylated complex-type oligosaccharide-alditols
with two and three peripheral chains consisting of Gal-GlcNAc sequences,
respectively.
FAU - Tsuji, T
AU - Tsuji T
FAU - Osawa, T
AU - Osawa T
LA - eng
PT - Journal Article
PL - England
TA - J Biochem
JT - Journal of biochemistry
JID - 0376600
RN - 0 (Amino Acids)
RN - 0 (Carbohydrates)
RN - 0 (Oligosaccharides)
RN - 0 (Platelet Glycoprotein GPIb-IX Complex)
RN - 0 (Platelet Membrane Glycoproteins)
RN - 0 (glycocalicin)
RN - 7006-34-0 (Asparagine)
SB - IM
MH - Amino Acids/analysis
MH - Asparagine/analysis
MH - Blood Platelets/*analysis
MH - Carbohydrates/*analysis
MH - Chromatography, Affinity
MH - Chromatography, Liquid
MH - Electrophoresis, Polyacrylamide Gel
MH - Humans
MH - Oligosaccharides/analysis
MH - Platelet Aggregation
MH - *Platelet Glycoprotein GPIb-IX Complex
MH - Platelet Membrane Glycoproteins/*blood/isolation & purification
MH - Protein Denaturation
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 - J Biochem. 1987 Jan;101(1):241-9.
PMID- 7430095
OWN - NLM
STAT- MEDLINE
DCOM- 19810126
LR - 20071114
IS - 0021-9258 (Print)
IS - 0021-9258 (Linking)
VI - 255
IP - 20
DP - 1980 Oct 25
TI - Structures of the asparagine-linked sugar chains of glycophorin A.
PG - 9713-8
AB - Glycophorin A isolated from human erythrocytes contains one asparagine-linked
sugar chain in one molecule. This sugar chain was successfully released as an
oligosaccharide fraction by hydrazinolysis. The oligosaccharide fraction was
separated into four components (N, A-1, A-2', and A-2) by paper electrophoresis.
Complete structures of the major acidic oligosaccharides (A-1 and A-2) were
elucidated by sequential exoglycosidase digestion in combination with methylation
study and periodate oxidation as follows: NeuAc alpha 2 leads to 6Gal beta 1
leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(3) [Gal beta 1 leads to
4GlcNAc beta 1 leads to to 2Man alpha 1 leads to 3(6)] (GlcNAc beta 1 leads to
4)Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6)GlcNAc 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
2Man alpha 1 leads to 3) (GlcNAc beta 1 leads to 4)Man beta 1 leads to 4GlcNAc
beta 1 leads to 4(Fuc alpha 1 leads to 6) GlcNAc. The abbreviations used are:
NeuAc, N-acetylneuraminic acid; GlcNAc, N-acetylglucosamine; Fuc, fucose.
FAU - Yoshima, H
AU - Yoshima H
FAU - Furthmayr, H
AU - Furthmayr H
FAU - Kobata, A
AU - Kobata A
LA - eng
GR - AM21714-01CO9S/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 - J Biol Chem
JT - The Journal of biological chemistry
JID - 2985121R
RN - 0 (Glycophorin)
RN - 0 (Sialoglycoproteins)
RN - 0 (Sugar Alcohols)
RN - 7006-34-0 (Asparagine)
RN - EC 3.2.1.- (Glycoside Hydrolases)
SB - IM
MH - Asparagine/*analysis
MH - Carbohydrate Conformation
MH - Carbohydrate Sequence
MH - *Glycophorin
MH - Glycoside Hydrolases
MH - Humans
MH - Protein Binding
MH - *Sialoglycoproteins
MH - Sugar Alcohols/analysis
EDAT- 1980/10/25 00:00
MHDA- 1980/10/25 00:01
CRDT- 1980/10/25 00:00
PHST- 1980/10/25 00:00 [pubmed]
PHST- 1980/10/25 00:01 [medline]
PHST- 1980/10/25 00:00 [entrez]
PST - ppublish
SO - J Biol Chem. 1980 Oct 25;255(20):9713-8.
PMID- 1468573
OWN - NLM
STAT- MEDLINE
DCOM- 19930125
LR - 20081121
IS - 0014-5793 (Print)
IS - 0014-5793 (Linking)
VI - 314
IP - 3
DP - 1992 Dec 21
TI - Human urokinase contains GalNAc beta (1-4)[Fuc alpha (1-3)]GlcNAc beta (1-2) as a
novel terminal element in N-linked carbohydrate chains.
PG - 389-94
AB - Structural analysis of enzymically released N-linked carbohydrate chains of human
urokinase (urinary-type plasminogen activator) by 1H NMR spectroscopy and FAB-MS
demonstrated that the N-linked oligosaccharides on the only N-glycosylation site
contain diantennary structures with the novel GalNAc beta (1-4) [Fuc alpha
(1-3)]GlcNAc beta (1-2) element in the upper or the lower branch.
FAU - Bergwerff, A A
AU - Bergwerff AA
AD - Bijvoet Center, Department of Bio-Organic Chemistry, Utrecht University, The
Netherlands.
FAU - Thomas-Oates, J E
AU - Thomas-Oates JE
FAU - van Oostrum, J
AU - van Oostrum J
FAU - Kamerling, J P
AU - Kamerling JP
FAU - Vliegenthart, J F
AU - Vliegenthart JF
LA - eng
PT - Journal Article
PT - Research Support, Non-U.S. Gov't
PL - England
TA - FEBS Lett
JT - FEBS letters
JID - 0155157
RN - EC 3.4.21.73 (Urokinase-Type Plasminogen Activator)
SB - IM
MH - Carbohydrate Sequence
MH - Humans
MH - Magnetic Resonance Spectroscopy
MH - Molecular Sequence Data
MH - Spectrometry, Mass, Fast Atom Bombardment
MH - Urokinase-Type Plasminogen Activator/*chemistry
EDAT- 1992/12/21 00:00
MHDA- 1992/12/21 00:01
CRDT- 1992/12/21 00:00
PHST- 1992/12/21 00:00 [pubmed]
PHST- 1992/12/21 00:01 [medline]
PHST- 1992/12/21 00:00 [entrez]
PST - ppublish
SO - FEBS Lett. 1992 Dec 21;314(3):389-94.
PMID- 10029548
OWN - NLM
STAT- MEDLINE
DCOM- 19990316
LR - 20131121
IS - 0006-2960 (Print)
IS - 0006-2960 (Linking)
VI - 38
IP - 8
DP - 1999 Feb 23
TI - X-ray crystallography and mass spectroscopy reveal that the N-lobe of human
transferrin expressed in Pichia pastoris is folded correctly but is glycosylated
on serine-32.
PG - 2535-41
AB - The ferric form of the N-lobe of human serum transferrin (Fe(III)-hTF/2N) has
been expressed at high levels in Pichia pastoris. The Fe(III)-hTF/2N was
crystallized in the space group P41212, and X-ray crystallography was used to
solve the structure of the recombinant protein at 2.5 A resolution. This
represents only the second P. pastoris-derived protein structure determined to
date, and allows the comparison of the structures of recombinant Fe(III)-hTF/2N
expressed in P. pastoris and mammalian cells with serum-derived transferrin. The
polypeptide folding pattern is essentially identical in all of the three
proteins. Mass spectroscopic analyses of P. pastoris- hTF/2N and proteolytically
derived fragments revealed glycosylation of Ser-32 with a single hexose. This
represents the first localization of an O-linked glycan in a P. pastoris-derived
protein. Because of its distance from the iron-binding site, glycosylation of
Ser-32 should not affect the iron-binding properties of hTF/2N expressed in P.
pastoris, making this an excellent expression system for the production of
hTF/2N.
FAU - Bewley, M C
AU - Bewley MC
AD - Institute of Molecular Biosciences, College of Sciences, Massey University,
Palmerston North, New Zealand.
FAU - Tam, B M
AU - Tam BM
FAU - Grewal, J
AU - Grewal J
FAU - He, S
AU - He S
FAU - Shewry, S
AU - Shewry S
FAU - Murphy, M E
AU - Murphy ME
FAU - Mason, A B
AU - Mason AB
FAU - Woodworth, R C
AU - Woodworth RC
FAU - Baker, E N
AU - Baker EN
FAU - MacGillivray, R T
AU - MacGillivray RT
LA - eng
SI - PDB/1B3E
GR - R01 DK 21739/DK/NIDDK NIH HHS/United States
GR - R01 DK 35533/DK/NIDDK NIH HHS/United States
GR - R01 HD 20859/HD/NICHD 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 - Biochemistry
JT - Biochemistry
JID - 0370623
RN - 0 (Ferric Compounds)
RN - 0 (Peptide Fragments)
RN - 0 (Recombinant Proteins)
RN - 0 (Transferrin)
RN - 452VLY9402 (Serine)
SB - IM
MH - Animals
MH - Cell Line
MH - Cricetinae
MH - Crystallization
MH - Crystallography, X-Ray
MH - Ferric Compounds/chemistry
MH - Glycosylation
MH - Humans
MH - Kidney/cytology
MH - Mass Spectrometry
MH - Models, Molecular
MH - Peptide Fragments/*chemistry/genetics/metabolism
MH - Pichia/*genetics
MH - *Protein Folding
MH - Recombinant Proteins/biosynthesis/*chemistry/metabolism
MH - Serine/genetics/*metabolism
MH - Transferrin/*chemistry/genetics/metabolism
EDAT- 1999/02/25 00:00
MHDA- 1999/02/25 00:01
CRDT- 1999/02/25 00:00
PHST- 1999/02/25 00:00 [pubmed]
PHST- 1999/02/25 00:01 [medline]
PHST- 1999/02/25 00:00 [entrez]
AID - 10.1021/bi9824543 [doi]
AID - bi9824543 [pii]
PST - ppublish
SO - Biochemistry. 1999 Feb 23;38(8):2535-41. doi: 10.1021/bi9824543.
PMID- 16321355
OWN - NLM
STAT- MEDLINE
DCOM- 20060602
LR - 20061115
IS - 0003-2697 (Print)
IS - 0003-2697 (Linking)
VI - 348
IP - 2
DP - 2006 Jan 15
TI - Site-specific N-glycosylation analysis of human plasma ceruloplasmin using liquid
chromatography with electrospray ionization tandem mass spectrometry.
PG - 259-68
AB - Ceruloplasmin has ferroxidase activity and plays an essential role in iron
metabolism. In this study, a site-specific glycosylation analysis of human
ceruloplasmin (CP) was carried out using reversed-phase high-performance liquid
chromatography with electrospray ionization tandem mass spectrometry
(LC-ESI-MS/MS). A tryptic digest of carboxymethylated CP was subjected to
LC-ESI-MS/MS. Product ion spectra acquired data-dependently were used for both
distinction of the glycopeptides from the peptides using the carbohydrate B-ions,
such as m/z 204 (HexNAc) and m/z 366 (HexHexNAc), and identification of the
peptide moiety of the glycopeptide based on the presence of the b- and y-series
ions derived from the peptide. Oligosaccharide composition was deduced from the
molecular weight calculated from the observed mass of the glycopeptide and
theoretical mass of the peptide. Of the seven potential N-glycosylation sites,
four (Asn119, Asn339, Asn378, and Asn743) were occupied by a sialylated
biantennary or triantennary oligosaccharide with fucose residues (0, 1, or 2). A
small amount of sialylated tetraantennary oligosaccharide was detected.
Exoglycosidase digestion suggested that fucose residues were linked to reducing
end GlcNAc in biantennary oligosaccharides and to reducing end and/or alpha1-3 to
outer arms GlcNAc in triantennary oligosaccharides and that roughly one of the
antennas in triantennary oligosaccharides was alpha2-3 sialylated and
occasionally alpha1-3 fucosylated at GlcNAc.
FAU - Harazono, Akira
AU - Harazono A
AD - National Institute of Health Sciences, Division of Biological Chemistry and
Biologicals, 1-18-1 Kami-yoga, Tokyo 158-8501, Japan. harazono@nihs.go.jp
FAU - Kawasaki, Nana
AU - Kawasaki N
FAU - Itoh, Satsuki
AU - Itoh S
FAU - Hashii, Noritaka
AU - Hashii N
FAU - Ishii-Watabe, Akiko
AU - Ishii-Watabe A
FAU - Kawanishi, Toru
AU - Kawanishi T
FAU - Hayakawa, Takao
AU - Hayakawa T
LA - eng
PT - Journal Article
PT - Research Support, Non-U.S. Gov't
DEP - 20051110
PL - United States
TA - Anal Biochem
JT - Analytical biochemistry
JID - 0370535
RN - 0 (Glycopeptides)
RN - 0 (Oligosaccharides)
RN - 7006-34-0 (Asparagine)
RN - EC 1.16.3.1 (Ceruloplasmin)
RN - EC 3.4.21.4 (Trypsin)
SB - IM
MH - Amino Acid Sequence
MH - Asparagine/*analysis/metabolism
MH - Ceruloplasmin/*analysis/chemistry/metabolism
MH - Chromatography, High Pressure Liquid/*methods
MH - Glycopeptides/*analysis
MH - Glycosylation
MH - Humans
MH - Molecular Sequence Data
MH - Oligosaccharides/analysis
MH - Peptide Mapping
MH - Spectrometry, Mass, Electrospray Ionization/*methods
MH - Trypsin/chemistry
EDAT- 2005/12/03 09:00
MHDA- 2006/06/03 09:00
CRDT- 2005/12/03 09:00
PHST- 2005/06/08 00:00 [received]
PHST- 2005/10/10 00:00 [revised]
PHST- 2005/10/18 00:00 [accepted]
PHST- 2005/12/03 09:00 [pubmed]
PHST- 2006/06/03 09:00 [medline]
PHST- 2005/12/03 09:00 [entrez]
AID - S0003-2697(05)00769-4 [pii]
AID - 10.1016/j.ab.2005.10.036 [doi]
PST - ppublish
SO - Anal Biochem. 2006 Jan 15;348(2):259-68. doi: 10.1016/j.ab.2005.10.036. Epub 2005
Nov 10.
PMID- 2513186
OWN - NLM
STAT- MEDLINE
DCOM- 19900131
LR - 20161017
IS - 0014-2956 (Print)
IS - 0014-2956 (Linking)
VI - 186
IP - 1-2
DP - 1989 Dec 8
TI - Carbohydrate structure of recombinant human uterine tissue plasminogen activator
expressed in mouse epithelial cells.
PG - 273-86
AB - Recombinant human uterine tissue plasminogen activator (tPA), in part
metabolically labeled with [6-3H]glucosamine or [35S]sulfate, was isolated from
mouse epithelial cells (C127). Oligosaccharides present were liberated by
treatment of tryptic glycopeptides with endo-beta-N-acetylglucosaminidase H or
peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidase F and fractionated by
high-performance liquid chromatography. The glycans were characterized by
digestion with exoglycosidases, methylation analysis and, in part, by acetolysis
and 1H-NMR spectroscopy. Glycopeptides comprising individual glycosylation sites
were identified by N-terminal amino acid sequencing. The results demonstrate that
recombinant tPA from C127 cells carries at Asn117 oligomannosidic glycans with
5-8 mannose residues as well as small amounts of hybrid-type species. Asn184 is
only partially glycosylated and substituted by fucosylated triantennary and small
amounts of diantennary N-acetyllactosaminic glycans. Likewise, Asn448 carries
predominantly fucosylated triantennary species, in addition to, small amounts of
diantennary and tetraantennary oligosaccharides. As a characteristic feature,
part of the triantennary glycans at Asn184 and Asn448 contain additional
Gal(alpha 1-3) substituents and/or sulfate groups linked to position six of
beta-galactosyl residues forming NeuAc(alpha 2-3)[HO3S-6]Gal(beta 1-4) units.
Oligosaccharides attached to Asn448 are almost completely substituted by (alpha
2-3)- or (alpha 2-6)-linked sialic acid residues and carry the majority of
sulfate groups present. Glycans at Asn184 were found to be less sialylated and
sulfated.
FAU - Pfeiffer, G
AU - Pfeiffer G
AD - Biochemisches Institut am Klinikum, Universitat Giessen, FRG.
FAU - Schmidt, M
AU - Schmidt M
FAU - Strube, K H
AU - Strube KH
FAU - Geyer, R
AU - Geyer R
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 (Asialoglycoproteins)
RN - 0 (Glycopeptides)
RN - 0 (Oligosaccharides)
RN - 0 (Recombinant Proteins)
RN - EC 3.4.21.68 (Tissue Plasminogen Activator)
SB - IM
MH - Amino Acid Sequence
MH - Animals
MH - Asialoglycoproteins/isolation & purification
MH - Carbohydrate Conformation
MH - Female
MH - Glycopeptides/isolation & purification
MH - Humans
MH - Methylation
MH - Mice
MH - Oligosaccharides/isolation & purification
MH - Recombinant Proteins
MH - *Tissue Plasminogen Activator
MH - Uterus
EDAT- 1989/12/08 00:00
MHDA- 1989/12/08 00:01
CRDT- 1989/12/08 00:00
PHST- 1989/12/08 00:00 [pubmed]
PHST- 1989/12/08 00:01 [medline]
PHST- 1989/12/08 00:00 [entrez]
PST - ppublish
SO - Eur J Biochem. 1989 Dec 8;186(1-2):273-86.
PMID- 8384526
OWN - NLM
STAT- MEDLINE
DCOM- 19930423
LR - 20041117
IS - 0008-6215 (Print)
IS - 0008-6215 (Linking)
VI - 239
DP - 1993 Feb 1
TI - An improved approach to the analysis of the structure of small oligosaccharides
of glycoproteins: application to the O-linked oligosaccharides from human
glycophorin A.
PG - 35-50
AB - Treatment of purified human glycophorin A with alkaline borohydride cleaved the
oligosaccharide side chains to yield alditol derivatives that were separated by
gel filtration into three mixtures of low molecular weight compounds. Each
mixture was oxidised with periodate, and the products were reduced with
borohydride and analysed after acetylation or methylation by GLC-MS and FABMS.
The resulting data allowed the monosaccharide sequence and linkage positions to
be assigned to each component of the mixtures. The anomeric configuration was
determined by 1H NMR spectroscopy of the intact fractions. The structures of a
desialylated tetrasaccharide, two monosialylated trisaccharides, and five other
minor products were defined.
FAU - Krotkiewski, H
AU - Krotkiewski H
AD - Ludwik Hirszfeld Institute of Immunology and Experimental Therapy, Polish Academy
of Sciences, Wroclaw.
FAU - Lisowska, E
AU - Lisowska E
FAU - Nilsson, G
AU - Nilsson G
FAU - Gronberg, G
AU - Gronberg G
FAU - Nilsson, B
AU - Nilsson B
LA - eng
PT - Journal Article
PL - Netherlands
TA - Carbohydr Res
JT - Carbohydrate research
JID - 0043535
RN - 0 (Blood Group Antigens)
RN - 0 (Borohydrides)
RN - 0 (Glycophorin)
RN - 0 (Oligosaccharides)
RN - 10450-60-9 (Periodic Acid)
SB - IM
MH - Acetylation
MH - Blood Group Antigens/chemistry
MH - Borohydrides
MH - Carbohydrate Sequence
MH - Erythrocytes/chemistry
MH - Glycophorin/*chemistry
MH - Humans
MH - Magnetic Resonance Spectroscopy
MH - Methylation
MH - Molecular Sequence Data
MH - Oligosaccharides/*chemistry/isolation & purification
MH - Oxidation-Reduction
MH - Periodic Acid
MH - Spectrometry, Mass, Fast Atom Bombardment
MH - Stereoisomerism
EDAT- 1993/02/01 00:00
MHDA- 1993/02/01 00:01
CRDT- 1993/02/01 00:00
PHST- 1993/02/01 00:00 [pubmed]
PHST- 1993/02/01 00:01 [medline]
PHST- 1993/02/01 00:00 [entrez]
AID - 0008-6215(93)84201-G [pii]
PST - ppublish
SO - Carbohydr Res. 1993 Feb 1;239:35-50.
PMID- 7068558
OWN - NLM
STAT- MEDLINE
DCOM- 19820614
LR - 20111117
IS - 0021-924X (Print)
IS - 0021-924X (Linking)
VI - 91
IP - 1
DP - 1982 Jan
TI - Structural study of the sugar chains of human lactoferrin: finding of four novel
complex-type asparagine-linked sugar chains.
PG - 143-55
AB - Human lactoferrin contains 2 asparagine-linked sugar chains in 1 molecule. These
sugar chains were released as oligosaccharides by hydrazinolysis from two
lactoferrin samples of different races. The two oligosaccharide fractions gave
exactly the same fractionation pattern upon paper electrophoresis and Bio-Gel P-4
column chromatography after sialidase digestion. A structural study of the
oligosaccharides obtained from the two samples by sequential exoglycosidase
digestion in combination with methylation analysis also gave the same results
indicating that there is no racial difference both in quality and quantity of the
sugar chain moiety of lactoferrin. In addition to the two acidic sugar chains,
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 4GlcNAc beta 1 leads to 2Man
alpha 1 leads to 3)Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1
leads to 6)GlucNAc and Gal beta 1 leads to 4(Fuc alpha 1 leads to 3)GlcNAc beta 1
leads to 1Man alpha 1 leads to 6(NeuAc alpha 2 leads to 6Gal beta 1 leads 4GlcNAc
beta 1 leads to 2Man alpha 1 leads to 3)Man beta 1 leads to 4GlcNAc beta 1 leads
to 4(Fuc alpha 1 leads to 6)GlcNAc, and two novel acidic sugar chains, Gal beta 1
leads to 4(Fuc alpha 1 leads to 3)GlcNAc beta 1 leads to Man alpha 1 leads to
6(NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 3Gal 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 4(Fuc alpha 1 leads to 6(GlcNAc and Gal beta 1 leads to
4(Fuc alpha 1 leads to 3)GlcNAc beta 1 leads to 3Gal 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 4(Fuc alpha 1 leads to 6)GlcNAc, were found to occur in human
lactoferrin.
FAU - Matsumoto, A
AU - Matsumoto A
FAU - Yoshima, H
AU - Yoshima H
FAU - Takasaki, S
AU - Takasaki S
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 (Hydrazines)
RN - 0 (Lactoglobulins)
RN - 0 (Oligosaccharides)
RN - 0 (Sialic Acids)
RN - 7006-34-0 (Asparagine)
RN - EC 3.4.21.- (Lactoferrin)
SB - IM
MH - *Asian Continental Ancestry Group
MH - Asparagine
MH - Carbohydrate Conformation
MH - Carbohydrate Sequence
MH - Chromatography, Gel
MH - Electrophoresis, Paper
MH - *European Continental Ancestry Group
MH - Humans
MH - Hydrazines
MH - *Lactoferrin
MH - *Lactoglobulins
MH - Milk, Human/*analysis
MH - Oligosaccharides
MH - Sialic Acids
EDAT- 1982/01/01 00:00
MHDA- 1982/01/01 00:01
CRDT- 1982/01/01 00:00
PHST- 1982/01/01 00:00 [pubmed]
PHST- 1982/01/01 00:01 [medline]
PHST- 1982/01/01 00:00 [entrez]
PST - ppublish
SO - J Biochem. 1982 Jan;91(1):143-55.
PMID- 11738084
OWN - NLM
STAT- MEDLINE
DCOM- 20020110
LR - 20171116
IS - 0006-3002 (Print)
IS - 0006-3002 (Linking)
VI - 1550
IP - 1
DP - 2001 Nov 26
TI - The glycan structure of albumin Redhill, a glycosylated variant of human serum
albumin.
PG - 20-6
AB - Although human serum albumin is synthesized without carbohydrate, glycosylated
variants of the protein can be found. We have determined the structure of the
glycan bound to the double-mutant albumin Redhill (-1 Arg, 320 Ala-->Thr). The
oligosaccharide was released from the protein using anhydrous hydrazine, and its
structure was investigated using neuraminidase and a reagent array analysis
method, which is based on the use of specific exoglycosidases. The glycan was
shown to be a disialylated biantennary complex type oligosaccharide N-linked to
318 Asn. However, a minor part (11 mol%) of the glycan was without sialic acid.
The structure is principally the same as that of glycans bound to two other types
of glycosylated albumin variants. Glycosylation can affect, for example, the
fatty acid binding properties of albumin. Taking the present information into
account, it is apparent that different effects on binding are caused not by
different glycan structures but by different locations of attachment, with the
possible addition of local conformational changes in the protein molecule.
FAU - Kragh-Hansen, U
AU - Kragh-Hansen U
AD - Department of Medical Biochemistry, The University of Aarhus, Denmark.
ukh@biokemi.au.dk
FAU - Donaldson, D
AU - Donaldson D
FAU - Jensen, P H
AU - Jensen PH
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 (Hydrazines)
RN - 0 (Ligands)
RN - 0 (Oligosaccharides)
RN - 0 (Peptide Fragments)
RN - 0 (Polysaccharides)
RN - 0 (Serum Albumin)
RN - 0 (albumin Redhill)
RN - 27RFH0GB4R (hydrazine)
RN - EC 3.2.1.- (Glycoside Hydrolases)
RN - EC 3.2.1.18 (Neuraminidase)
RN - GZP2782OP0 (N-Acetylneuraminic Acid)
RN - OS382OHJ8P (Cyanogen Bromide)
RN - ZIF514RVZR (Serum Albumin, Human)
SB - IM
MH - Carbohydrate Sequence
MH - Cyanogen Bromide
MH - Glycoside Hydrolases
MH - Glycosylation
MH - Heterozygote
MH - Humans
MH - Hydrazines
MH - Ligands
MH - Molecular Conformation
MH - Molecular Sequence Data
MH - N-Acetylneuraminic Acid/chemistry
MH - Neuraminidase
MH - Oligosaccharides/chemistry/isolation & purification
MH - Oxidation-Reduction
MH - Peptide Fragments/isolation & purification
MH - Polysaccharides/*chemistry
MH - Serum Albumin/*chemistry/genetics
MH - Serum Albumin, Human
EDAT- 2001/12/12 10:00
MHDA- 2002/01/11 10:01
CRDT- 2001/12/12 10:00
PHST- 2001/12/12 10:00 [pubmed]
PHST- 2002/01/11 10:01 [medline]
PHST- 2001/12/12 10:00 [entrez]
AID - S0167-4838(01)00264-3 [pii]
PST - ppublish
SO - Biochim Biophys Acta. 2001 Nov 26;1550(1):20-6.
PMID- 10988252
OWN - NLM
STAT- MEDLINE
DCOM- 20010109
LR - 20181130
IS - 0959-6658 (Print)
IS - 0959-6658 (Linking)
VI - 10
IP - 9
DP - 2000 Sep
TI - Characterization of the carbohydrate chains of the secreted form of the human
epidermal growth factor receptor.
PG - 901-17
AB - The human epidermal growth factor receptor (EGFR) is a transmembrane glycoprotein
having 11 potential N-glycosylation sites in its extracellular domain.
N-Glycosylation is needed for proper membrane insertion, EGF binding and receptor
functioning. The human epidermoid carcinoma A431 cell line secretes a soluble 105
kDa glycoprotein (sEGFR) that represents the extracellular domain of the
membrane-bound form, and its glycosylation pattern has been investigated. After
liberation of the oligosaccharides from sEGFR with PNGase F, the glycans were
fractionated along different routes, including Concanavalin A affinity
chromatography, anion-exchange chromatography, HPLC and high-pH anion-exchange
chromatography. The oligosaccharide fractions were characterized by 500- and
600-MHz 1H-NMR spectroscopy and mass spectrometry (FAB, ESI, and MALDI-TOF). The
oligomannose-type glycans range from Man5GlcNAc2 to Man8GlcNAc2 and account for
17% of the total carbohydrate moiety. Furthermore, di-, tri'- and tetraantennary
complex-type structures are present, both neutral and (alpha2-3)-sialylated (up
to tetrasialo), comprising 24 and 59%, respectively, of the total carbohydrate
moiety. In this study, 32 new complex-type glycans are characterized containing
the Le(x), Le(Y), and sialyl-Le(x) determinants, the bloodgroup A and H antigens,
as well as the ALe(Y) determinant. This first comprehensive glycosylation study
on a human nonrecombinant receptor shows the immense heterogeneity of the
glycosylation of sEGFR.
FAU - Stroop, C J
AU - Stroop CJ
AD - Bijvoet Center, Department of Bio-Organic Chemistry, Utrecht University, The
Netherlands.
FAU - Weber, W
AU - Weber W
FAU - Gerwig, G J
AU - Gerwig GJ
FAU - Nimtz, M
AU - Nimtz M
FAU - Kamerling, J P
AU - Kamerling JP
FAU - Vliegenthart, J F
AU - Vliegenthart JF
LA - eng
PT - Journal Article
PL - England
TA - Glycobiology
JT - Glycobiology
JID - 9104124
RN - 0 (Membrane Glycoproteins)
RN - 0 (Oligosaccharides)
RN - EC 2.7.10.1 (ErbB Receptors)
RN - EC 3.5.- (Amidohydrolases)
RN - EC 3.5.1.52 (Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase)
SB - IM
MH - Amidohydrolases/metabolism
MH - Carbohydrate Conformation
MH - Carbohydrate Sequence
MH - Chromatography, Affinity
MH - Chromatography, High Pressure Liquid
MH - Chromatography, Ion Exchange
MH - ErbB Receptors/*chemistry/genetics/isolation & purification/*metabolism
MH - Glycosylation
MH - Humans
MH - Magnetic Resonance Spectroscopy
MH - Membrane Glycoproteins/*chemistry/genetics/isolation & purification/*metabolism
MH - Methylation
MH - Molecular Sequence Data
MH - Oligosaccharides/*analysis/*chemistry/metabolism
MH - Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase
MH - Solubility
MH - Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
MH - Tumor Cells, Cultured
EDAT- 2000/09/16 11:00
MHDA- 2001/02/28 10:01
CRDT- 2000/09/16 11:00
PHST- 2000/09/16 11:00 [pubmed]
PHST- 2001/02/28 10:01 [medline]
PHST- 2000/09/16 11:00 [entrez]
PST - ppublish
SO - Glycobiology. 2000 Sep;10(9):901-17.
PMID- 24279413
OWN - NLM
STAT- MEDLINE
DCOM- 20140714
LR - 20171220
IS - 1520-6882 (Electronic)
IS - 0003-2700 (Linking)
VI - 86
IP - 1
DP - 2014 Jan 7
TI - Computational framework for identification of intact glycopeptides in complex
samples.
PG - 453-63
LID - 10.1021/ac402338u [doi]
AB - Glycosylation is an important protein modification that involves enzymatic
attachment of sugars to amino acid residues. Understanding the structure of these
sugars and the effects of glycosylation are vital for developing indicators of
disease development and progression. Although computational methods based on mass
spectrometric data have proven to be effective in monitoring changes in the
glycome, developing such methods for the glycoproteome are challenging, largely
due to the inherent complexity in simultaneously studying glycan structures with
their corresponding glycosylation sites. This paper introduces a computational
framework for identifying intact N-linked glycopeptides, i.e. glycopeptides with
N-linked glycans attached to their glycosylation sites, in complex proteome
samples. Scoring algorithms are presented for tandem mass spectra of
glycopeptides resulting from collision-induced dissociation (CID), higher-energy
C-trap dissociation (HCD), and electron transfer dissociation (ETD) fragmentation
modes. An empirical false-discovery rate estimation method, based on a
target-decoy search approach, is derived for assigning confidence. The power of
our method is further enhanced when multiple data sets are pooled together to
increase identification confidence. Using this framework, 103 highly confident
N-linked glycopeptides from 53 sites across 33 glycoproteins were identified in
complex human serum proteome samples using conventional proteomic platforms with
standard depletion of the 7-most abundant proteins. These results indicate that
our method is ready to be used for characterizing site-specific protein
glycosylation in complex samples.
FAU - Mayampurath, Anoop
AU - Mayampurath A
AD - School of Informatics & Computing, Indiana University , Bloomington, Indiana
47408, United States.
FAU - Yu, Chuan-Yih
AU - Yu CY
FAU - Song, Ehwang
AU - Song E
FAU - Balan, Jagadheshwar
AU - Balan J
FAU - Mechref, Yehia
AU - Mechref Y
FAU - Tang, Haixu
AU - Tang H
LA - eng
GR - 1R01GM093322-03/GM/NIGMS 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.
DEP - 20131210
PL - United States
TA - Anal Chem
JT - Analytical chemistry
JID - 0370536
RN - 0 (Glycopeptides)
SB - IM
MH - Amino Acid Sequence
MH - Animals
MH - Cattle
MH - Computational Biology/*methods
MH - Glycopeptides/analysis/*blood/*genetics
MH - Humans
MH - Molecular Sequence Data
MH - Swine
EDAT- 2013/11/28 06:00
MHDA- 2014/07/16 06:00
CRDT- 2013/11/28 06:00
PHST- 2013/11/28 06:00 [entrez]
PHST- 2013/11/28 06:00 [pubmed]
PHST- 2014/07/16 06:00 [medline]
AID - 10.1021/ac402338u [doi]
PST - ppublish
SO - Anal Chem. 2014 Jan 7;86(1):453-63. doi: 10.1021/ac402338u. Epub 2013 Dec 10.
PMID- 11676606
OWN - NLM
STAT- MEDLINE
DCOM- 20011231
LR - 20171116
IS - 1046-5928 (Print)
IS - 1046-5928 (Linking)
VI - 23
IP - 2
DP - 2001 Nov
TI - Determination of carbohydrate structures N-linked to soluble CD154 and
characterization of the interactions of CD40 with CD154 expressed in Pichia
pastoris and Chinese hamster ovary cells.
PG - 301-10
AB - CD40-CD154 (CD40 ligand) interactions are essential for the development of
protective immunity. Previous studies have described the CD40 binding site as a
shallow groove formed between two monomers of CD154. However, these studies have
not examined the structure or biological function of the carbohydrate on CD154.
Human CD154 contains a single N-linked glycosylation site at asparagine 240. We
have characterized the interactions between CD40 and soluble (s) CD154 in which
sCD154 contains different types of carbohydrates. Detailed carbohydrate analysis
revealed high-mannose structures on sCD154 purified from Pichia pastoris, whereas
CD154 purified from Chinese hamster ovary E1A contained heterogeneous populations
of complex carbohydrates. sCD154 purified from either system was trimeric, it
bound to CD40 with similar affinities of 10-30 nM, and it functionally induced
CD69 and CD95 expression on primary B cells. Together, these results indicate
that the presence of varied types of N-linked glycans on asparagine 240 of CD154
does not play a significant role in the CD40-CD154 interactions.
CI - Copyright 2001 Academic Press.
FAU - Khandekar, S S
AU - Khandekar SS
AD - Department of Protein Biochemistry, SmithKline Beecham Pharmaceuticals, King of
Prussia, Pennsylvania 19406, USA.
FAU - Silverman, C
AU - Silverman C
FAU - Wells-Marani, J
AU - Wells-Marani J
FAU - Bacon, A M
AU - Bacon AM
FAU - Birrell, H
AU - Birrell H
FAU - Brigham-Burke, M
AU - Brigham-Burke M
FAU - DeMarini, D J
AU - DeMarini DJ
FAU - Jonak, Z L
AU - Jonak ZL
FAU - Camilleri, P
AU - Camilleri P
FAU - Fishman-Lobell, J
AU - Fishman-Lobell J
LA - eng
PT - Journal Article
PL - United States
TA - Protein Expr Purif
JT - Protein expression and purification
JID - 9101496
RN - 0 (CD40 Antigens)
RN - 0 (Carbohydrates)
RN - 0 (Recombinant Proteins)
RN - 147205-72-9 (CD40 Ligand)
RN - 7006-34-0 (Asparagine)
RN - PHA4727WTP (Mannose)
SB - IM
MH - Animals
MH - Asparagine/chemistry
MH - B-Lymphocytes/immunology
MH - CD40 Antigens/*chemistry/genetics/immunology/metabolism
MH - CD40 Ligand/*chemistry/genetics/immunology/metabolism
MH - CHO Cells
MH - Carbohydrate Conformation
MH - Carbohydrate Metabolism
MH - Carbohydrates/*chemistry
MH - Cells, Cultured
MH - Cloning, Molecular
MH - Cricetinae
MH - Humans
MH - Mannose/chemistry/metabolism
MH - Pichia/genetics
MH - Protein Binding
MH - Recombinant Proteins/chemistry/genetics/metabolism
MH - Solubility
EDAT- 2001/10/26 10:00
MHDA- 2002/01/05 10:01
CRDT- 2001/10/26 10:00
PHST- 2001/10/26 10:00 [pubmed]
PHST- 2002/01/05 10:01 [medline]
PHST- 2001/10/26 10:00 [entrez]
AID - 10.1006/prep.2001.1501 [doi]
AID - S1046-5928(01)91501-3 [pii]
PST - ppublish
SO - Protein Expr Purif. 2001 Nov;23(2):301-10. doi: 10.1006/prep.2001.1501.
PMID- 10929010
OWN - NLM
STAT- MEDLINE
DCOM- 20000907
LR - 20161025
IS - 0959-6658 (Print)
IS - 0959-6658 (Linking)
VI - 10
IP - 8
DP - 2000 Aug
TI - N-glycan patterns of human transferrin produced in Trichoplusia ni insect cells:
effects of mammalian galactosyltransferase.
PG - 837-47
AB - The N-glycans of human serum transferrin produced in Trichopulsia ni cells were
analyzed to examine N-linked oligosaccharide processing in insect cells.
Metabolic radiolabeling of the intra- and extracellular protein fractions
revealed the presence of multiple transferrin glycoforms with molecular weights
lower than that observed for native human transferrin. Consequently, the N-glycan
structures of transferrin in the culture medium were determined using
three-dimensional high performance liquid chromatography. The attached
oligosaccharides included high mannose, paucimannosidic, and hybrid structures
with over 50% of these structures containing one fucose, alpha(1,6)-, or two
fucoses, alpha(1,6)- and alpha(1,3)-, linked to the Asn-linked
N-acetylglucosamine. Neither sialic acid nor galactose was detected on any of the
N-glycans. However, when transferrin was coexpressed with
beta(1,4)-galactosyltransferase three additional galactose-containing hybrid
oligosaccharides were obtained. The galactose attachments were exclusive to the
alpha(1, 3)-mannose branch and the structures varied by the presence of zero,
one, or two attached fucose residues. Furthermore, the presence of the
galactosyltransferase appeared to reduce the number of paucimannosidic
structures, which suggests that galactose attachment inhibits the ability of
hexosaminidase activity to remove the terminal N-acetylglucosamine. The ability
to promote galactosylation and reduce paucimannosidic N-glycans suggests that the
oligosaccharide processing pathway in insect cells may be manipulated to mimic
more closely that of mammalian cells.
FAU - Ailor, E
AU - Ailor E
AD - Department of Chemical Engineering, The Johns Hopkins University, Baltimore, MD
21218, USA.
FAU - Takahashi, N
AU - Takahashi N
FAU - Tsukamoto, Y
AU - Tsukamoto Y
FAU - Masuda, K
AU - Masuda K
FAU - Rahman, B A
AU - Rahman BA
FAU - Jarvis, D L
AU - Jarvis DL
FAU - Lee, Y C
AU - Lee YC
FAU - Betenbaugh, M J
AU - Betenbaugh MJ
LA - eng
GR - R01 GM049734/GM/NIGMS NIH HHS/United States
PT - Journal Article
PL - England
TA - Glycobiology
JT - Glycobiology
JID - 9104124
RN - 0 (DNA Primers)
RN - 0 (Polysaccharides)
RN - 0 (Recombinant Proteins)
RN - 0 (Transferrin)
RN - 11089-65-9 (Tunicamycin)
RN - EC 2.4.1.- (Galactosyltransferases)
SB - IM
MH - Animals
MH - Base Sequence
MH - Carbohydrate Conformation
MH - Carbohydrate Sequence
MH - Chromatography, High Pressure Liquid
MH - DNA Primers
MH - Galactosyltransferases/*metabolism
MH - Humans
MH - Molecular Sequence Data
MH - Moths/*cytology
MH - Polysaccharides/*metabolism
MH - Recombinant Proteins/chemistry/genetics/metabolism
MH - Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
MH - Transferrin/chemistry/genetics/*metabolism
MH - Tunicamycin/pharmacology
EDAT- 2000/08/06 11:00
MHDA- 2000/09/09 11:01
CRDT- 2000/08/06 11:00
PHST- 2000/08/06 11:00 [pubmed]
PHST- 2000/09/09 11:01 [medline]
PHST- 2000/08/06 11:00 [entrez]
PST - ppublish
SO - Glycobiology. 2000 Aug;10(8):837-47.
PMID- 12151713
OWN - NLM
STAT- MEDLINE
DCOM- 20021107
LR - 20181113
IS - 0282-0080 (Print)
IS - 0282-0080 (Linking)
VI - 18
IP - 7
DP - 2001 Jul
TI - N-glycosylation potential of maize: the human lactoferrin used as a model.
PG - 519-27
AB - In order to determine the N-glycosylation potential of maize, a monocotyledon
expression system for the production of recombinant glycoproteins, human
lactoferrin was used as a model. The human lactoferrin coding sequence was
inserted into the pUC18 plasmid under control of the wheat glutenin promoter.
Maize was stably transformed and recombinant lactoferrin was purified from the
fourth generation seeds. Glycosylation was analysed by gas chromatography, lectin
detection, glycosidase digestions and mass spectrometry. The results indicated
that both N-glycosylation sites of recombinant lactoferrin are mainly substituted
by typical plant paucimannose-type glycans, with beta1,2-xylose and
alpha1,3-linked fucose at the proximal N-acetylglucosamine, and that complex-type
glycans with Lewis(a) determinants are not present in maize recombinant
lactoferrin.
FAU - Samyn-Petit, B
AU - Samyn-Petit B
AD - Meristem Therapeutics, 8 rue des Freres Lumiere, 63100 Clermont-Ferrand, France.
FAU - Gruber, V
AU - Gruber V
FAU - Flahaut, C
AU - Flahaut C
FAU - Wajda-Dubos, J P
AU - Wajda-Dubos JP
FAU - Farrer, S
AU - Farrer S
FAU - Pons, A
AU - Pons A
FAU - Desmaizieres, G
AU - Desmaizieres G
FAU - Slomianny, M C
AU - Slomianny MC
FAU - Theisen, M
AU - Theisen M
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 (Recombinant Proteins)
RN - EC 3.4.21.- (Lactoferrin)
SB - IM
MH - Blotting, Western
MH - Glycosylation
MH - Humans
MH - Lactoferrin/*metabolism
MH - Models, Chemical
MH - Recombinant Proteins/metabolism
MH - Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
MH - Zea mays/*metabolism
EDAT- 2002/08/02 10:00
MHDA- 2002/11/26 04:00
CRDT- 2002/08/02 10:00
PHST- 2002/08/02 10:00 [pubmed]
PHST- 2002/11/26 04:00 [medline]
PHST- 2002/08/02 10:00 [entrez]
PST - ppublish
SO - Glycoconj J. 2001 Jul;18(7):519-27.
PMID- 9449027
OWN - NLM
STAT- MEDLINE
DCOM- 19980320
LR - 20181113
IS - 1355-008X (Print)
IS - 1355-008X (Linking)
VI - 7
IP - 1
DP - 1997 Aug
TI - Carbohydrate and peptide structure of the alpha- and beta-subunits of human
chorionic gonadotropin from normal and aberrant pregnancy and choriocarcinoma.
PG - 15-32
AB - Human chorionic gonadotropin (hCG), purified from the urine of 14 individuals
with normal pregnancy, diabetic pregnancy, hydatidiform mole, or choriocarcinoma,
plus two hCG standard preparations, was examined for concurrent peptide-sequence
and asparagine (N)- and serine (O)-linked carbohydrate heterogeneity.
Protein-sequence analysis was used to measure amino-terminal heterogeneity and
the "nicking" of internal peptide bonds. The use of high-pH anion-exchange
chromatography coupled with the increased sensitivity of pulsed amperometric
detection (HPAE/PAD) revealed that distinct proportions of both hCG alpha- and
beta-subunits from normal and aberrant pregnancy are hyperglycosylated, and that
it is the extent of the specific subunit hyperglycosylation that significantly
increases in malignant disease. Peptide-bond nicking was restricted to a single
linkage (beta 47-48) in normal and diabetic pregnancy, but occurred at two sites
in standard preparations, at three sites in hydatidiform mole, and at three sites
in choriocarcinoma beta-subunit. In the carbohydrate moiety, alpha-subunit from
normal pregnancy hCG contained nonfucosylated, mono- and biantennary N-linked
structures (49.3 and 36.7%, means); fucosylated biantennary and triantennary
oligosaccharides were also identified (7.3 and 6.9%). In choriocarcinoma
alpha-subunit, the level of fucosylated biantennary increased, offset by a
parallel decrease in the predominant biantennary structure of normal pregnancy (P
< 0.0001). The beta-subunit from normal pregnancy hCG contained fucosylated and
nonfucosylated biantennary N-linked structures; however, mono- and triantennary
oligosaccharides were also identified (4.6 and 13.7%). For O-linked glycans, in
beta-subunit from normal pregnancy, disaccharide-core structure predominated,
whereas tetrasaccharide-core structure was also detected (15.6%). A trend was
demonstrated in beta-subunit: the proportions of the nonpredominating N- and
O-linked oligosaccharides increased stepwise from normal pregnancy to
hydatidiform mole to choriocarcinoma. The increases were: for monoantennary
oligosaccharide, 4.6 to 6.8 to 11.2%; for triantennary, 13.7 to 26.7 to 51.5%
and, for O-linked tetrasaccharide-core structure, 15.6 to 23.0 to 74.8%. For hCG
from individual diabetic pregnancy, the principal N-linked structure (34.7%) was
consistent with a biantennary oligosaccharide previously reported only in
carcinoma; and sialylation of both N- and O-linked antennae was significantly
decreased compared to that of normal pregnancy. Taken collectively, the
distinctive patterns of subunit-specific, predominant oligosaccharides appear to
reflect the steric effect of local protein structure during glycosylation
processes. The evidence of alternative or "hyperbranched" glycoforms on both
alpha- and beta-subunits, seen at low levels in normal pregnancy and at increased
or even predominant levels in malignant disease, suggests alternative substrate
accessibility for Golgi processing enzymes, alpha 1,6 fucosyltransferase and
N-acetylglucosaminyltransferase IV, in distinct proportions of subunit molecules.
FAU - Elliott, M M
AU - Elliott MM
AD - Department of Obstetrics and Gynecology, Yale University School of Medicine, New
Haven, CT 06510, USA.
FAU - Kardana, A
AU - Kardana A
FAU - Lustbader, J W
AU - Lustbader JW
FAU - Cole, L A
AU - Cole LA
LA - eng
GR - CA-44131/CA/NCI NIH HHS/United States
GR - HD-15454/HD/NICHD NIH HHS/United States
PT - Journal Article
PT - Research Support, U.S. Gov't, P.H.S.
PL - United States
TA - Endocrine
JT - Endocrine
JID - 9434444
RN - 0 (Carbohydrates)
RN - 0 (Chorionic Gonadotropin, beta Subunit, Human)
RN - 0 (Glycoprotein Hormones, alpha Subunit)
RN - 0 (Oligosaccharides)
RN - 0 (Peptides)
SB - IM
MH - Amino Acid Sequence
MH - Carbohydrate Sequence
MH - Carbohydrates/*chemistry
MH - Choriocarcinoma/chemistry/*urine
MH - Chorionic Gonadotropin, beta Subunit, Human/isolation & purification/*urine
MH - Female
MH - Glycoprotein Hormones, alpha Subunit/isolation & purification/*urine
MH - Humans
MH - Hydatidiform Mole/chemistry/urine
MH - Hydrogen Bonding
MH - Hydrolysis
MH - Molecular Sequence Data
MH - Oligosaccharides/chemistry
MH - Peptides/*chemistry
MH - Pregnancy/*urine
MH - Pregnancy Complications, Neoplastic/*urine
MH - Pregnancy in Diabetics/urine
MH - Uterine Neoplasms/chemistry/*urine
EDAT- 1997/08/01 00:00
MHDA- 1998/02/04 00:01
CRDT- 1997/08/01 00:00
PHST- 1997/08/01 00:00 [pubmed]
PHST- 1998/02/04 00:01 [medline]
PHST- 1997/08/01 00:00 [entrez]
AID - 10.1007/BF02778058 [doi]
PST - ppublish
SO - Endocrine. 1997 Aug;7(1):15-32. doi: 10.1007/BF02778058.
PMID- 1482348
OWN - NLM
STAT- MEDLINE
DCOM- 19930208
LR - 20170913
IS - 0006-291X (Print)
IS - 0006-291X (Linking)
VI - 189
IP - 3
DP - 1992 Dec 30
TI - Hepatocyte growth factor is linked by O-glycosylated oligosaccharide on the alpha
chain.
PG - 1329-35
AB - The glycosylation site and the structure of O-glycosylated oligosaccharide of
recombinant human HGF were investigated. N-acetylgalactosamine (GalNAc) in the
alpha chain suggested the presence of O-glycosylated oligosaccharide. Sugar
analysis and amino acid sequence analysis of peptide fragments produced by
limited degradation revealed that O-glycosylated oligosaccharide linked to Thr445
of the alpha chain. The molecular weight of the oligosaccharide was determined
with ion spray mass spectrometry. From these studies, the structure of the
O-glycosylated oligosaccharide on the alpha chain of HGF was concluded as
[formula: see text].
FAU - Shimizu, N
AU - Shimizu N
AD - Pharmaceuticals Research Center, Toyobo Co. Ltd., Otsu, Japan.
FAU - Hara, H
AU - Hara H
FAU - Sogabe, T
AU - Sogabe T
FAU - Sakai, H
AU - Sakai H
FAU - Ihara, I
AU - Ihara I
FAU - Inoue, H
AU - Inoue H
FAU - Nakamura, T
AU - Nakamura T
FAU - Shimizu, S
AU - Shimizu S
LA - eng
PT - Journal Article
PL - United States
TA - Biochem Biophys Res Commun
JT - Biochemical and biophysical research communications
JID - 0372516
RN - 0 (Macromolecular Substances)
RN - 0 (Monosaccharides)
RN - 0 (Oligosaccharides)
RN - 0 (Peptide Fragments)
RN - 0 (Recombinant Proteins)
RN - 67256-21-7 (Hepatocyte Growth Factor)
RN - K3Z4F929H6 (Lysine)
RN - K848JZ4886 (Cysteine)
SB - IM
MH - Amino Acid Sequence
MH - Carbohydrate Conformation
MH - Carbohydrate Sequence
MH - Cysteine
MH - Glycosylation
MH - Hepatocyte Growth Factor/*chemistry
MH - Humans
MH - Lysine
MH - Macromolecular Substances
MH - Molecular Sequence Data
MH - Monosaccharides/analysis
MH - Oligosaccharides/*chemistry
MH - Peptide Fragments/chemistry/isolation & purification
MH - Recombinant Proteins/chemistry
EDAT- 1992/12/30 00:00
MHDA- 1992/12/30 00:01
CRDT- 1992/12/30 00:00
PHST- 1992/12/30 00:00 [pubmed]
PHST- 1992/12/30 00:01 [medline]
PHST- 1992/12/30 00:00 [entrez]
AID - 0006-291X(92)90219-B [pii]
PST - ppublish
SO - Biochem Biophys Res Commun. 1992 Dec 30;189(3):1329-35.
PMID- 8323280
OWN - NLM
STAT- MEDLINE
DCOM- 19930803
LR - 20101118
IS - 0003-9861 (Print)
IS - 0003-9861 (Linking)
VI - 304
IP - 1
DP - 1993 Jul
TI - N-linked sugar chain structure of recombinant human lymphotoxin produced by CHO
cells: the functional role of carbohydrate as to its lectin-like character and
clearance velocity.
PG - 144-53
AB - Recombinant human lymphotoxin (rhLT) produced by CHO cells transfected with human
LT genomic DNA was purified to homogeneity, but approximately 5% of the molecules
were devoid of the last two amino terminal residues. A peptide N-glycosylated at
Asn62 (Tr-45) and one partially O-glycosylated at Thr7 (Tr-14) on cleavage with
trypsin were separated by reverse phase HPLC. The N-linked sugar chains of Tr-45
were released quantitatively as oligosaccharides on hydrazinolysis (100 degrees
C, 8 h), followed by N-acetylation. After being reduced with either NaB3H4 or
NaB2H4, their structures were determined by a combination of serial lectin
affinity chromatography, exoglycosidase digestion, and methylation analysis:
82.7% of the sugar chains occur as biantennary complex-type sugar chains, the
remainder being C-2 and C-2,4/C-2,6 branched triantennary, and C-2,4 and C-2,6
branched tetraantennary complex-type sugar chains with a fucosylated mannose
core. Their sialic acid residues occur only as the Neu5Ac alpha 2-->3Gal group.
The clearance velocity from the bloodstream dramatically increased with
desialylation, and rhLT tends to have accumulated in the kidney, indicating that
there may exist other mechanisms for clearance from the circulation besides the
galactose-binding protein in hepatocytes and the filtration system of the kidney.
Desialylated rhLT showed a lectin-like binding character to uromodulin similar to
that of tumor necrosis factor, although intact rhLT did not. The interaction
between desialylated rhLT and uromodulin was inhibited by N,N'-diacetylchitobiose
and [Man alpha 1-->6(Man alpha 1-->3)Man alpha 1-->6](Man alpha 1-->2Man alpha
1-->3)Man beta 1-->4GlcNAc beta 1-->4GlcNAc-->Asn. These results indicate that
the lectin-like domain of rhLT is exposed on its desialylation.
FAU - Fukushima, K
AU - Fukushima K
AD - Department of Biochemistry, Sasaki Institute, Tokyo, Japan.
FAU - Watanabe, H
AU - Watanabe H
FAU - Takeo, K
AU - Takeo K
FAU - Nomura, M
AU - Nomura M
FAU - Asahi, T
AU - Asahi T
FAU - Yamashita, K
AU - Yamashita K
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 (Glycoproteins)
RN - 0 (Lymphotoxin-alpha)
RN - 0 (Mucoproteins)
RN - 0 (Oligosaccharides)
RN - 0 (Recombinant Proteins)
RN - 0 (UMOD protein, human)
RN - 0 (Uromodulin)
SB - IM
MH - Amino Acid Sequence
MH - Animals
MH - CHO Cells
MH - Carbohydrate Sequence
MH - Chromatography, High Pressure Liquid
MH - Cricetinae
MH - Glycoproteins/*chemistry
MH - Humans
MH - Lymphotoxin-alpha/*chemistry/pharmacokinetics
MH - Metabolic Clearance Rate
MH - Methylation
MH - Molecular Sequence Data
MH - Molecular Structure
MH - Mucoproteins/metabolism
MH - Oligosaccharides/chemistry
MH - Protein Binding
MH - Rats
MH - Recombinant Proteins/chemistry/pharmacokinetics
MH - Structure-Activity Relationship
MH - Uromodulin
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 - S0003-9861(83)71332-9 [pii]
AID - 10.1006/abbi.1993.1332 [doi]
PST - ppublish
SO - Arch Biochem Biophys. 1993 Jul;304(1):144-53. doi: 10.1006/abbi.1993.1332.
PMID- 10861392
OWN - NLM
STAT- MEDLINE
DCOM- 20000901
LR - 20061115
IS - 0006-3592 (Print)
IS - 0006-3592 (Linking)
VI - 69
IP - 2
DP - 2000 Jul 20
TI - Metabolic shifts do not influence the glycosylation patterns of a recombinant
fusion protein expressed in BHK cells.
PG - 129-39
AB - BHK-21 cells expressing a human IgG-IL2 fusion protein, with potential
application in tumor-targeted therapy, were grown under different nutrient
conditions in a continuous system for a time period of 80 days. At very
low-glucose (< 0.5 mM) or glutamine (< 0. 2 mM) concentrations, a shift toward an
energetically more efficient metabolism was observed. Cell-specific productivity
was maintained under metabolically shifted growth conditions and at the same time
an almost identical intracellular ATP content, obtained by in vivo (31)P NMR
experiments, was observed. No significant differences in the oligosaccharide
structures were detected from the IgG-IL2 fusion protein preparations obtained by
growing cells under the different metabolic states. By using oligosaccharide
mapping and MALDI/TOF-MS, only neutral diantennary oligosaccharides with or
without core alpha1-6-linked fucose were detected that carried no, one or two
beta1-4-linked galactose. Although the O-linked oligosaccharide structures that
are present in the IL2 moiety of the protein were studied with less detail, the
data obtained from the hydrazinolysis procedure point to the presence of the
classical NeuAcalpha2-3Galbeta1-3GalNAc structure. Here, it is shown that under
different defined cellular metabolic states, the quality of a recombinant product
in terms of O- and N-linked oligosaccharides is stable, even after a prolonged
cultivation period. Moreover, unaffected intracellular ATP levels under the
different metabolic states were observed.
CI - Copyright 2000 John Wiley & Sons, Inc.
FAU - Cruz, H J
AU - Cruz HJ
AD - IBET/ITQB- Instituto de Biologia Experimental e Tecnologica / Instituto de
Tecnologia Quimica e Biologica, Apartado 12, P-2781-901 Oeiras, Portugal.
FAU - Peixoto, C M
AU - Peixoto CM
FAU - Nimtz, M
AU - Nimtz M
FAU - Alves, P M
AU - Alves PM
FAU - Dias, E M
AU - Dias EM
FAU - Moreira, J L
AU - Moreira JL
FAU - Carrondo, M J
AU - Carrondo MJ
LA - eng
PT - Journal Article
PT - Research Support, Non-U.S. Gov't
PL - United States
TA - Biotechnol Bioeng
JT - Biotechnology and bioengineering
JID - 7502021
RN - 0 (Immunoglobulin G)
RN - 0 (Interleukin-2)
RN - 0 (Oligosaccharides)
RN - 0 (Recombinant Fusion Proteins)
SB - IM
MH - Animals
MH - Biotechnology
MH - Carbohydrate Sequence
MH - Cell Line
MH - Cricetinae
MH - Energy Metabolism
MH - Gene Expression
MH - Glycosylation
MH - Humans
MH - Immunoglobulin G/chemistry/genetics/metabolism
MH - Interleukin-2/chemistry/genetics/metabolism
MH - Magnetic Resonance Spectroscopy
MH - Molecular Sequence Data
MH - Oligosaccharides/chemistry
MH - Recombinant Fusion Proteins/chemistry/genetics/*metabolism
MH - Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
EDAT- 2000/06/22 10:00
MHDA- 2000/09/09 11:01
CRDT- 2000/06/22 10:00
PHST- 2000/06/22 10:00 [pubmed]
PHST- 2000/09/09 11:01 [medline]
PHST- 2000/06/22 10:00 [entrez]
AID - 10.1002/(SICI)1097-0290(20000720)69:2<129::AID-BIT2>3.0.CO;2-5 [pii]
PST - ppublish
SO - Biotechnol Bioeng. 2000 Jul 20;69(2):129-39.
PMID- 2065054
OWN - NLM
STAT- MEDLINE
DCOM- 19910812
LR - 20071114
IS - 0006-2960 (Print)
IS - 0006-2960 (Linking)
VI - 30
IP - 27
DP - 1991 Jul 9
TI - Structures of the asparagine-289-linked oligosaccharides assembled on recombinant
human plasminogen expressed in a Mamestra brassicae cell line (IZD-MBO503).
PG - 6689-96
AB - In this report, we have fortified and extended a previous investigation
[Davidson, D. J., Fraser, M. J., & Castellino, F. J. (1990) Biochemistry 29,
5584-5590] in which we demonstrated for the first time that lepidopteran insect
(Spodoptera frugiperda) cells (IPLB-SF-21AE) were capable of assembling N-linked
complex oligosaccharide on a human protein (plasminogen), the cDNA of which had
been inserted into these cells via recombinant DNA technology with a baculovirus
vector. In order to investigate whether a more general capability of lepidopteran
insect cells to produce complex oligosaccharide existed, and to identify the
chemical nature of the types of oligosaccharides that such insect cells were able
to assemble, we have infected Mamestra brassicae (IZD-MBO503) cells for 48 h with
a recombinant (r) baculovirus containing the [R561E]human plasminogen (HPg) cDNA
and characterized the nature of the glycopeptidase F (GF) released N-linked
oligosaccharides contained on Asn289 of the r-HPg expressed by these cells. We
found that approximately 63% of the total N-linked oligosaccharides were of the
complex type, with bisialo-biantennary (28%), asialo-biantennary (7%),
fucosylated bisialo-biantennary (25%), and fucosylated asialo-biantennary (3%)
oligosaccharides representing the major complex-type carbohydrate species. The
remainder of the oligosaccharides were of the high-mannose type, with
(mannose)9(N-acetylglucosamine)2 (22%), (mannose)5(N-acetylglucosamine)2 (13%),
and (mannose)3(N-acetylglucosamine)2 (2%) representing the major oligosaccharides
observed.(ABSTRACT TRUNCATED AT 250 WORDS)
FAU - Davidson, D J
AU - Davidson DJ
AD - Department of Chemistry and Biochemistry, University of Notre Dame, Indiana
46556.
FAU - Castellino, F J
AU - Castellino FJ
LA - eng
GR - HL-13423/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 - Biochemistry
JT - Biochemistry
JID - 0370623
RN - 0 (Oligosaccharides)
RN - 0 (Recombinant Proteins)
RN - 7006-34-0 (Asparagine)
RN - 9001-91-6 (Plasminogen)
RN - 9007-49-2 (DNA)
SB - IM
MH - Animals
MH - Asparagine/*chemistry
MH - Baculoviridae/genetics
MH - Carbohydrate Sequence
MH - Cell Line
MH - Chromatography, High Pressure Liquid
MH - DNA/genetics
MH - Electrophoresis, Polyacrylamide Gel
MH - Genes, Viral
MH - Glycosylation
MH - Humans
MH - Lepidoptera/cytology
MH - Molecular Sequence Data
MH - Oligosaccharides/*chemistry
MH - Plasminogen/*chemistry/genetics
MH - Recombinant Proteins/chemistry/genetics
EDAT- 1991/07/09 00:00
MHDA- 1991/07/09 00:01
CRDT- 1991/07/09 00:00
PHST- 1991/07/09 00:00 [pubmed]
PHST- 1991/07/09 00:01 [medline]
PHST- 1991/07/09 00:00 [entrez]
PST - ppublish
SO - Biochemistry. 1991 Jul 9;30(27):6689-96.
PMID- 2403553
OWN - NLM
STAT- MEDLINE
DCOM- 19900202
LR - 20131121
IS - 0021-9258 (Print)
IS - 0021-9258 (Linking)
VI - 265
IP - 1
DP - 1990 Jan 5
TI - Human transferrin receptor contains O-linked oligosaccharides.
PG - 114-25
AB - We have investigated the oligosaccharides in the human transferrin receptor from
three different cell lines. During our studies on the structures of the N-linked
oligosaccharides of the receptor, we discovered that the receptor contains
O-linked oligosaccharides. This report describes the isolation and
characterization of these O-linked oligosaccharides. Three different human cell
lines--K562, A431, and BeWo--were grown in media containing either [2-3H] mannose
or [6-3H]glucosamine. The newly synthesized and radiolabeled transferrin
receptors were purified by immunoprecipitation from cell extracts and sodium
dodecyl sulfate-polyacrylamide gel electrophoresis. The receptor was
proteolytically digested or treated directly with mild base/borohydride. The
released radiolabeled glycopeptides and oligosaccharides were separated by a
variety of chromatographic techniques, and their structures were analyzed. The
transferrin receptor from all three cell types contains O-linked oligosaccharides
that are released from peptide by mild base/borohydride treatment. The receptor
from K562 cells contains at least one O-linked oligosaccharide having two sialic
acid residues and a core structure of the disaccharide
galactose-N-acetyl-galactosamine. In contrast, the O-linked oligosaccharides in
the transferring receptors from both A431 and BeWo cell lines are not as highly
sialylated and were identified as both the neutral disaccharide
galactose-N-acetylgalactosamine and the neutral monosaccharide
N-acetylgalactosamine. In addition, the receptors from all three cell lines
contain both complex-type and high mannose-type N-linked oligosaccharides. The
complex-type chains in the receptor from A431 cells have properties of blood
group A antigens, whereas oligosaccharides in receptors from both BeWo and K562
cells lack these properties. These results are interesting since both A431 and
BeWo cells, but not K562 cells, are positive for blood group A antigens. Thus,
our results demonstrate that the human transferrin receptor contains O-linked
oligosaccharides and that there are differences in the structures of both the
O-linked and complex-type N-linked oligosaccharides on the receptors synthesized
by different cell types.
FAU - Do, S I
AU - Do SI
AD - Department of Biochemistry, University of Georgia, Athens 30602.
FAU - Enns, C
AU - Enns C
FAU - Cummings, R D
AU - Cummings RD
LA - eng
GR - CA37626-04/CA/NCI NIH HHS/United States
GR - DK40608/DK/NIDDK 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 (Borohydrides)
RN - 0 (Oligosaccharides)
RN - 0 (Receptors, Transferrin)
RN - 0 (Sialic Acids)
RN - GZP2782OP0 (N-Acetylneuraminic Acid)
RN - KM15WK8O5T (Acetylgalactosamine)
RN - N08U5BOQ1K (Glucosamine)
RN - PHA4727WTP (Mannose)
RN - X2RN3Q8DNE (Galactose)
SB - IM
MH - Acetylgalactosamine/analysis
MH - Borohydrides
MH - Carbohydrate Conformation
MH - Chromatography, Affinity
MH - Galactose/analysis
MH - Glucosamine/metabolism
MH - Humans
MH - Hydrogen-Ion Concentration
MH - Immunosorbent Techniques
MH - Mannose/analysis/metabolism
MH - N-Acetylneuraminic Acid
MH - Oligosaccharides/*isolation & purification
MH - Receptors, Transferrin/*analysis
MH - Sialic Acids/analysis
MH - Tumor Cells, Cultured
EDAT- 1990/01/05 00:00
MHDA- 1990/01/05 00:01
CRDT- 1990/01/05 00:00
PHST- 1990/01/05 00:00 [pubmed]
PHST- 1990/01/05 00:01 [medline]
PHST- 1990/01/05 00:00 [entrez]
PST - ppublish
SO - J Biol Chem. 1990 Jan 5;265(1):114-25.
PMID- 8142896
OWN - NLM
STAT- MEDLINE
DCOM- 19940502
LR - 20181113
IS - 0961-8368 (Print)
IS - 0961-8368 (Linking)
VI - 3
IP - 1
DP - 1994 Jan
TI - Structural analysis and localization of the carbohydrate moieties of a soluble
human interferon gamma receptor produced in baculovirus-infected insect cells.
PG - 30-8
AB - A soluble form of the human interferon gamma receptor that is required for the
identification of interferon gamma antagonists was expressed in
baculovirus-infected insect cells. The protein carried N-linked carbohydrate and
showed a heterogeneity on denaturing polyacrylamide gels. We investigated the
utilization of the potential sites for N-linked glycosylation and the structure
of the carbohydrate moieties of this soluble receptor. Amino acid sequence
analysis and ion spray mass spectrometry revealed that of the five potential
sites for N-linked glycosylation, Asn17 and Asn69 were always utilized, whereas
Asn62 and Asn162 were utilized in approximately one-third of the protein
population. Asn223 was never found to be glycosylated. The soluble receptor was
treated with N-glycosidase F and the oligosaccharides released were analyzed by
matrix-assisted laser desorption mass spectrometry, which showed that the protein
carried six types of short carbohydrate chains. The predominant species was a
hexasaccharide of molecular mass 1,039, containing a fucose subunit linked to the
proximal N-acetylglucosamine residue: [formula: see text]
FAU - Manneberg, M
AU - Manneberg M
AD - Department of Biology, F. Hoffmann-La Roche Ltd., Pharmaceutical Research-New
Technologies, Basel, Switzerland.
FAU - Friedlein, A
AU - Friedlein A
FAU - Kurth, H
AU - Kurth H
FAU - Lahm, H W
AU - Lahm HW
FAU - Fountoulakis, M
AU - Fountoulakis M
LA - eng
PT - Journal Article
PL - United States
TA - Protein Sci
JT - Protein science : a publication of the Protein Society
JID - 9211750
RN - 0 (Carbohydrates)
RN - 0 (Receptors, Interferon)
RN - 0 (Recombinant Proteins)
SB - IM
MH - Amino Acid Sequence
MH - Animals
MH - Baculoviridae/*genetics
MH - Carbohydrate Conformation
MH - Carbohydrate Sequence
MH - Carbohydrates/analysis/*chemistry
MH - Chromatography, High Pressure Liquid
MH - Genetic Vectors
MH - Glycosylation
MH - Humans
MH - Molecular Sequence Data
MH - *Moths
MH - Receptors, Interferon/*chemistry/genetics
MH - Recombinant Proteins/chemistry
PMC - PMC2142480
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 - 10.1002/pro.5560030105 [doi]
PST - ppublish
SO - Protein Sci. 1994 Jan;3(1):30-8. doi: 10.1002/pro.5560030105.
PMID- 10704524
OWN - NLM
STAT- MEDLINE
DCOM- 20000317
LR - 20071114
IS - 0959-6658 (Print)
IS - 0959-6658 (Linking)
VI - 10
IP - 3
DP - 2000 Mar
TI - Human alpha-N-acetylgalactosaminidase: site occupancy and structure of N-linked
oligosaccharides.
PG - 251-61
AB - Human alpha-N-acetylgalactosaminidase (alpha-GalNAc; also known as
alpha-galactosidase B) is the lysosomal exoglycohydrolase that cleaves
alpha-N-acetylgalactosaminyl moieties in glycoconjugates. Mutagenesis studies
indicated that the first five (N124, N177, N201, N359, and N385) of the six
potential N-glycosylation sites were occupied. Site 3 occupancy was important for
enzyme function and stability. Characterization of the N-linked oligosaccharide
structures on the secreted enzyme overexpressed in Chinese hamster ovary cells
revealed highly heterogeneous structures consisting of complex (approximately
53%), hybrid (approximately 12%), and high mannose-type (approximately 33%)
oligosaccharides. The complex structures were mono-, bi-, 2,4-tri-, 2,6-tri-, and
tetraantennary, among which the biantennary structures were most predominant
(approximately 53%). Approximately 80% of the complex oligo-saccharides had a
core-region fucose and 50% of the complex oligosaccharides were sialylated
exclusively with alpha-2,3-linked sialic acid residues. The majority of hybrid
type oligo-saccharides were GalGlcNAcMan(6)GlcNAc-Fuc(0-1)GlcNAc. Approximately
54% of the hybrid oligosaccharide were phosphorylated and one-third of these
structures were further sialylated, the latter representing unique phosphorylated
and sialylated structures. Of the high mannose oligosaccharides,
Man(5-7)GlcNAc(2) were the predominant species (approximately 90%) and about 50%
of the high mannose oligosaccharides were phosphorylated, exclusively as
monoesters whose positions were determined. Comparison of the oligosaccharide
structures of alpha-GalNAc and alpha-galactosidase A, an evolutionary-related and
highly homologous exoglycosidase, indicated that alpha-GalNAc had more completed
complex chains, presumably due to differences in enzyme structure/domains, rate
of biosynthesis, and/or aggregation of the overexpressed recombinant enzymes.
FAU - Ohta, M
AU - Ohta M
AD - Department of Biotechnology, Fukuyama University, Fukuyama, Hiroshima 729-0292,
Japan,
FAU - Ohnishi, T
AU - Ohnishi T
FAU - Ioannou, Y A
AU - Ioannou YA
FAU - Hodgson, M E
AU - Hodgson ME
FAU - Matsuura, F
AU - Matsuura F
FAU - Desnick, R J
AU - Desnick RJ
LA - eng
GR - 5 R01 DK34045/DK/NIDDK NIH HHS/United States
GR - M01 RR00071/RR/NCRR NIH HHS/United States
GR - P30 HD28822/HD/NICHD 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 (Oligosaccharides)
RN - 0 (sialooligosaccharides)
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 - Animals
MH - COS Cells
MH - Carbohydrate Conformation
MH - Carbohydrate Sequence
MH - Chromatography, Affinity
MH - Hexosaminidases/*chemistry/genetics/metabolism
MH - Humans
MH - Molecular Sequence Data
MH - Mutagenesis, Site-Directed
MH - Oligosaccharides/*chemistry/metabolism
MH - alpha-N-Acetylgalactosaminidase
EDAT- 2000/03/08 09:00
MHDA- 2000/03/25 09:00
CRDT- 2000/03/08 09:00
PHST- 2000/03/08 09:00 [pubmed]
PHST- 2000/03/25 09:00 [medline]
PHST- 2000/03/08 09:00 [entrez]
AID - cwd024 [pii]
PST - ppublish
SO - Glycobiology. 2000 Mar;10(3):251-61.
PMID- 8053566
OWN - NLM
STAT- MEDLINE
DCOM- 19940907
LR - 20061115
IS - 0003-2697 (Print)
IS - 0003-2697 (Linking)
VI - 218
IP - 1
DP - 1994 Apr
TI - Site-specific characterization of glycoprotein carbohydrates by exoglycosidase
digestion and laser desorption mass spectrometry.
PG - 34-46
AB - A rapid and sensitive method for sequencing oligosaccharides has been developed,
using matrix-assisted laser desorption mass spectrometry to monitor the digestion
of glycopeptides by specific exoglycosidases. Recombinant human tissue inhibitor
of metalloproteinases (TIMP), which has two glycosylation sites, has been
characterized to illustrate this new approach for obtaining site-specific
information. Glycopeptides which span residues Asn30 and Asn78 were generated by
tryptic digestion of 1 nmol of TIMP and separated by reverse-phase
high-performance liquid chromatography. The oligosaccharide composition of the
glycoforms was inferred from the observed mass shifts following digestion by
peptide-N-glycosidase F. Composition and sequence were then elucidated by
digestion with specific exoglycosidases, using a total of 200 pmol of each
glycopeptide. Glycopeptides from well-characterized proteins, fetuin, alpha
1-acid glycoprotein, and tissue plasminogen activator were also analyzed to
confirm exoglycosidase specificity for glycopeptides and establish the
quantitative significance of the relative intensities of peaks in the mass
spectra. Both TIMP glycosylation sites exhibited extensive heterogeneity
comprising mainly fucosylated complex oligosaccharides, but in different
proportions. The Asn78 site also contained 4.4% nonfucosylated mannose (Man4)
oligosaccharide. The merits and limitations of this approach as a universal
method for oligosaccharide analysis are discussed.
FAU - Sutton, C W
AU - Sutton CW
AD - Finnigan MAT Ltd., Paradise, Hemel Hempstead, Hertfordshire, United Kingdom.
FAU - O'Neill, J A
AU - O'Neill JA
FAU - Cottrell, J S
AU - Cottrell JS
LA - eng
PT - Journal Article
PL - United States
TA - Anal Biochem
JT - Analytical biochemistry
JID - 0370535
RN - 0 (Glycopeptides)
RN - 0 (Glycoproteins)
RN - 0 (Oligosaccharides)
RN - 0 (Tissue Inhibitor of Metalloproteinases)
RN - EC 3.2.1.- (Glycoside Hydrolases)
RN - EC 3.4.24.- (Metalloendopeptidases)
RN - EC 3.5.- (Amidohydrolases)
RN - EC 3.5.1.52 (Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase)
SB - IM
MH - Amidohydrolases
MH - Amino Acid Sequence
MH - Carbohydrate Sequence
MH - Glycopeptides/*analysis
MH - Glycoproteins/*analysis
MH - *Glycoside Hydrolases
MH - Lasers
MH - Mass Spectrometry/*methods
MH - Metalloendopeptidases/*antagonists & inhibitors
MH - Molecular Sequence Data
MH - Molecular Weight
MH - Oligosaccharides/analysis
MH - Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase
MH - Sensitivity and Specificity
MH - Substrate Specificity
MH - Tissue Inhibitor of Metalloproteinases
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 - S0003269784711389 [pii]
PST - ppublish
SO - Anal Biochem. 1994 Apr;218(1):34-46.
PMID- 29671580
OWN - NLM
STAT- In-Process
LR - 20190228
IS - 1520-6882 (Electronic)
IS - 0003-2700 (Linking)
VI - 90
IP - 10
DP - 2018 May 15
TI - Site-Specific Profiling of Serum Glycoproteins Using N-Linked Glycan and
Glycosite Analysis Revealing Atypical N-Glycosylation Sites on Albumin and
alpha-1B-Glycoprotein.
PG - 6292-6299
LID - 10.1021/acs.analchem.8b01051 [doi]
AB - Most serum proteins are N-linked glycosylated, and therefore the glycoproteomic
profiling of serum is essential for characterization of serum proteins. In this
study, we profiled serum N-glycoproteome by our recently developed
N-glycoproteomic method using solid-phase extraction of N-linked glycans and
glycosite-containing peptides (NGAG) coupled with LC-MS/MS and site-specific
glycosylation analysis using GPQuest software. Our data indicated that half of
identified N-glycosites were modified by at least two glycans, with a majority of
them being sialylated. Specifically, 3/4 of glycosites were modified by
biantennary N-glycans and 1/3 of glycosites were modified by triantennary
sialylated N-glycans. In addition, two novel atypical glycosites (with N-X-V
motif) were identified and validated from albumin and alpha-1B-glycoprotein. The
widespread presence of these two glycosites among individuals was further
confirmed by individual serum analyses.
FAU - Sun, Shisheng
AU - Sun S
AUID- ORCID: 0000-0002-7242-7164
AD - College of Life Science , Northwest University , Xi'an , Shaanxi Province 710069
, China.
AD - Department of Pathology , Johns Hopkins University , Baltimore , Maryland 21287 ,
United States.
FAU - Hu, Yingwei
AU - Hu Y
AUID- ORCID: 0000-0002-4629-0985
AD - Department of Pathology , Johns Hopkins University , Baltimore , Maryland 21287 ,
United States.
FAU - Jia, Li
AU - Jia L
AD - College of Life Science , Northwest University , Xi'an , Shaanxi Province 710069
, China.
FAU - Eshghi, Shadi Toghi
AU - Eshghi ST
AD - Department of Pathology , Johns Hopkins University , Baltimore , Maryland 21287 ,
United States.
FAU - Liu, Yang
AU - Liu Y
AD - Department of Pathology , Johns Hopkins University , Baltimore , Maryland 21287 ,
United States.
FAU - Shah, Punit
AU - Shah P
AD - Department of Pathology , Johns Hopkins University , Baltimore , Maryland 21287 ,
United States.
FAU - Zhang, Hui
AU - Zhang H
AUID- ORCID: 0000-0001-8726-7098
AD - Department of Pathology , Johns Hopkins University , Baltimore , Maryland 21287 ,
United States.
LA - eng
GR - U01 CA152813/CA/NCI NIH HHS/United States
GR - U24 CA210985/CA/NCI NIH HHS/United States
GR - R21 AI122382/AI/NIAID NIH HHS/United States
PT - Journal Article
PT - Research Support, Non-U.S. Gov't
PT - Research Support, N.I.H., Extramural
DEP - 20180501
PL - United States
TA - Anal Chem
JT - Analytical chemistry
JID - 0370536
EDAT- 2018/04/20 06:00
MHDA- 2018/04/20 06:00
CRDT- 2018/04/20 06:00
PHST- 2018/04/20 06:00 [pubmed]
PHST- 2018/04/20 06:00 [medline]
PHST- 2018/04/20 06:00 [entrez]
AID - 10.1021/acs.analchem.8b01051 [doi]
PST - ppublish
SO - Anal Chem. 2018 May 15;90(10):6292-6299. doi: 10.1021/acs.analchem.8b01051. Epub
2018 May 1.
PMID- 7620335
OWN - NLM
STAT- MEDLINE
DCOM- 19950830
LR - 20181113
IS - 0282-0080 (Print)
IS - 0282-0080 (Linking)
VI - 12
IP - 2
DP - 1995 Apr
TI - Identification of the oligosaccharide structures of human coagulation factor X
activation peptide at each glycosylation site.
PG - 173-81
AB - Human blood coagulation factor X has two N-linked oligosaccharides at Asn39 and
Asn49 residues and two O-linked oligosaccharides at Thr17 and Thr29 residues in
the region of the factor X activation peptide (XAP) which is cleaved off during
its activation by factor IXa. We determined the structure of oligosaccharides in
the XAP region of human factor X. Four glycopeptides each containing a
glycosylation site were isolated by digestion of XAP with endoproteinase Asp-N
followed by reversed-phase HPLC. N-linked oligosaccharides released from the
glycopeptides by glycoamidase A digestion were derivatized with 2-aminopyridine.
Pyridylamino(PA)-oligosaccharides were separated by HPLC into neutral and sialyl
oligosaccharides using an anion-exchange column. Structures of oligosaccharides
and their contents at each glycosylation site were determined by a
two-dimensional sugar mapping method. The contents of the neutral
oligosaccharides at Asn39 and Asn49 residues were 32.5% and 30.0%, respectively.
Six neutral and twelve monosialyl oligosaccharides isolated from both N-linked
glycosylation sites showed similar elution profiles composed of bi-, tri- and
tetra-antennary complex type oligosaccharides. The predominant component in
neutral oligosaccharides was biantennary without a fucose residue. Two major
monosialyl oligosaccharides were also biantennary without fucose and with a
Neu5Ac alpha 2-->6 residue. In addition, the structures of O-linked
oligosaccharides at Thr17 and Thr29 residues were suggested to be disialylated
Gal beta 3GalNAc sequences by their component analyses.
FAU - Nakagawa, H
AU - Nakagawa H
AD - GlycoLab, Nakano Vinegar Co. Ltd, Aichi, Japan.
FAU - Takahashi, N
AU - Takahashi N
FAU - Fujikawa, K
AU - Fujikawa K
FAU - Kawamura, Y
AU - Kawamura Y
FAU - Iino, M
AU - Iino M
FAU - Takeya, H
AU - Takeya H
FAU - Ogawa, H
AU - Ogawa H
FAU - Suzuki, K
AU - Suzuki K
LA - eng
PT - Journal Article
PL - United States
TA - Glycoconj J
JT - Glycoconjugate journal
JID - 8603310
RN - 0 (Oligosaccharides)
RN - 0 (Peptides)
RN - 0 (Sialic Acids)
RN - 7006-34-0 (Asparagine)
RN - 9001-29-0 (Factor X)
RN - EC 3.4.- (Endopeptidases)
RN - EC 3.4.24.- (Metalloendopeptidases)
RN - EC 3.4.24.33 (endoproteinase Asp-N)
RN - GZP2782OP0 (N-Acetylneuraminic Acid)
SB - IM
MH - Asparagine/chemistry
MH - Carbohydrate Conformation
MH - Carbohydrate Sequence
MH - Chromatography, High Pressure Liquid
MH - Endopeptidases/metabolism
MH - Factor X/*chemistry
MH - Glycosylation
MH - Humans
MH - Metalloendopeptidases
MH - Molecular Sequence Data
MH - N-Acetylneuraminic Acid
MH - Oligosaccharides/analysis/*chemistry
MH - Peptides/chemistry
MH - Sialic Acids/chemistry
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]
PST - ppublish
SO - Glycoconj J. 1995 Apr;12(2):173-81.
PMID- 2033371
OWN - NLM
STAT- MEDLINE
DCOM- 19910626
LR - 20181113
IS - 0022-1007 (Print)
IS - 0022-1007 (Linking)
VI - 173
IP - 6
DP - 1991 Jun 1
TI - Altered O-glycan synthesis in lymphocytes from patients with Wiskott-Aldrich
syndrome.
PG - 1501-10
AB - The only molecular defect reported for the X-linked immunodeficiency
Wiskott-Aldrich syndrome (WAS) is the abnormal electrophoretic behavior of the
major T lymphocyte sialoglycoprotein CD43. Since the 70 to 80 O-linked
carbohydrate chains of CD43 are known to influence markedly its electrophoretic
mobility, we analyzed the structure and the biosynthesis of O-glycans of CD43 in
lymphocytes from patients with WAS. Immunofluorescence analysis with the
carbohydrate dependent anti-CD43 antibody T305 revealed that in 10 out of the 12
WAS patients tested increased numbers of T lymphocytes carry on CD43 an epitope
which on normal lymphocytes is expressed only after activation. Other activation
antigens were absent from WAS lymphocytes. Western blots of WAS cell lysates
displayed a high molecular mass form of CD43 which reacted with the T305 antibody
and which could be found on in vivo activated lymphocytes but was absent from
normal unstimulated lymphocytes. To examine the O-glycan structures, carbohydrate
labeled CD43 was immunoprecipitated and the released oligosaccharides identified.
WAS lymphocyte CD43 was found to carry predominantly the branched structure
NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----3Gal beta 1----4G1cNAc beta
1----6) GalNAcOH whereas normal lymphocytes carry the structure NeuNAc alpha
2----3Gal beta 1----3 (NeuNAc alpha 2----6) GalNAcOH. Only after activation
NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta
1----6) GalNAcOH becomes the principal oligosaccharide on CD43 from normal
lymphocytes. Analyzing the six glycosyltransferases involved in the biosynthesis
of these O-glycan structures it was found that in WAS lymphocytes high levels of
beta 1----6 N-acetyl-glucosaminyl transferase are responsible for the expression
of NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----3Gal beta 1----4GlcNAc
beta 1----6) GalNAcOH on CD43. The gene responsible for WAS has not yet been
identified but the results presented in this study suggest that the primary
defect in WAS may affect a gene which is involved in the regulation of
O-glycosylation.
FAU - Piller, F
AU - Piller F
AD - La Jolla Cancer Research Foundation, California 92037.
FAU - Le Deist, F
AU - Le Deist F
FAU - Weinberg, K I
AU - Weinberg KI
FAU - Parkman, R
AU - Parkman R
FAU - Fukuda, M
AU - Fukuda M
LA - eng
GR - CA-33895/CA/NCI 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 (Leukosialin)
RN - 0 (Oligosaccharides)
RN - 0 (Sialoglycoproteins)
RN - 0 (UN1 sialoglycoprotein, human)
RN - EC 2.4.1.- (Hexosyltransferases)
SB - IM
MH - Antigens, CD/chemistry/*metabolism
MH - Carbohydrate Sequence
MH - Flow Cytometry
MH - Glycosylation
MH - Hexosyltransferases/metabolism
MH - Humans
MH - Leukosialin
MH - Lymphocyte Activation
MH - Lymphocyte Subsets/chemistry
MH - Lymphocytes/*metabolism
MH - Molecular Sequence Data
MH - Molecular Weight
MH - Oligosaccharides/chemistry
MH - Protein Processing, Post-Translational
MH - Sialoglycoproteins/chemistry/*metabolism
MH - Wiskott-Aldrich Syndrome/*metabolism
PMC - PMC2190829
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]
PST - ppublish
SO - J Exp Med. 1991 Jun 1;173(6):1501-10.
PMID- 2943741
OWN - NLM
STAT- MEDLINE
DCOM- 19861023
LR - 20171116
IS - 0021-9258 (Print)
IS - 0021-9258 (Linking)
VI - 261
IP - 27
DP - 1986 Sep 25
TI - Structural variations of O-linked oligosaccharides present in leukosialin
isolated from erythroid, myeloid, and T-lymphoid cell lines.
PG - 12787-95
AB - Structures of O-linked oligosaccharides of leukosialin isolated from K562
erythroid, HL-60 promyelocytic, and HSB-2 T-lymphoid cell lines were examined.
Leukosialin was isolated by specific immunoprecipitation from cells which were
metabolically labeled with [3H]glucosamine, and glycopeptides were isolated after
Pronase digestion. O-Linked oligosaccharides were released by alkaline
borohydride treatment, and the structures of purified oligosaccharides were
elucidated by specific exoglycosidase digestion, Smith degradation, and
methylation anaylsis. Oligosaccharides from K562 cells were found to be GalNAcOH,
Gal beta 1----3GalNAcOH, NeuNAc alpha 2----6GalNAcOH, NeuNAc alpha 2----3Gal beta
1----3GalNAcOH, Gal beta 1----3(NeuNAc alpha 2----6)GalNAcOH, and NeuNAc alpha
2----3Gal beta 1----3(NeuNAc alpha 2----6)GalNAcOH. On the other hand,
oligosaccharides from HL-60 and HSB-2 cells were found to be NeuNAc alpha
2----3Gal beta 1----3GalNAcOH, NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta
1----6(Gal beta 1----3)GalNAcOH, Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha
2----3)Gal beta 1----3)GalNAcOH, and NeuNAc alpha 2----3Gal beta 1----4GlcNAc
beta 1----6(NeuNAc alpha 2----3Gal beta 1----3)GalNAcOH. These results clearly
indicate that leukosialin can be differently glycosylated with O-linked chains,
and each erythroid or myeloid (and T-lymphoid) cell line expresses a
characteristic set of O-linked oligosaccharides which differ in core structures
as well as in sialylation.
FAU - Carlsson, S R
AU - Carlsson SR
FAU - Sasaki, H
AU - Sasaki H
FAU - Fukuda, M
AU - Fukuda M
LA - eng
GR - CA 33000/CA/NCI NIH HHS/United States
GR - R01 CA 33895/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 (Antigens, CD)
RN - 0 (Leukosialin)
RN - 0 (Oligosaccharides)
RN - 0 (Sialoglycoproteins)
RN - 0 (UN1 sialoglycoprotein, human)
RN - EC 3.4.24.- (Pronase)
RN - N08U5BOQ1K (Glucosamine)
SB - IM
MH - *Antigens, CD
MH - Carbohydrate Conformation
MH - Cell Line
MH - Chromatography, Gel
MH - Electrophoresis, Polyacrylamide Gel
MH - Erythrocytes/*analysis
MH - Glucosamine/metabolism
MH - Humans
MH - Leukemia, Myeloid, Acute/*metabolism
MH - Leukosialin
MH - Oligosaccharides/*analysis
MH - Pronase/metabolism
MH - Sialoglycoproteins/*analysis
MH - T-Lymphocytes/*analysis
EDAT- 1986/09/25 00:00
MHDA- 1986/09/25 00:01
CRDT- 1986/09/25 00:00
PHST- 1986/09/25 00:00 [pubmed]
PHST- 1986/09/25 00:01 [medline]
PHST- 1986/09/25 00:00 [entrez]
PST - ppublish
SO - J Biol Chem. 1986 Sep 25;261(27):12787-95.
PMID- 7841792
OWN - NLM
STAT- MEDLINE
DCOM- 19950309
LR - 20181113
IS - 0282-0080 (Print)
IS - 0282-0080 (Linking)
VI - 11
IP - 3
DP - 1994 Jun
TI - Characterization of a single glycosylated asparagine site on a glycopeptide using
solid-phase Edman degradation.
PG - 180-6
AB - The characterization of site-specific glycosylation is traditionally dependent on
the availability of suitable proteolytic cleavage sites between each glycosylated
residue, so that peptides containing individual glycosylation sites are
recovered. In the case of heavily glycosylated domains such as the O-glycosylated
mucins, which have no available protease sites, this approach is not possible.
Here we introduce a new method to gain site-specific compositional data on the
oligosaccharides attached to a single amino acid. Using a model glycopeptide from
a mutant human albumin Casebrook, glycosylated PTH-Asn was recovered after
sequential solid-phase Edman degradation, subjected to acid hydrolysis and the
sugars were identified by high performance anion exchange chromatography with
pulsed amperometric detection. The PTH-Asn(Sac) derivative was further
characterized by ionspray mass spectrometry. Comparison between an endoproteinase
Glu-C glycopeptide and a tryptic glycopeptide showed that the oligosaccharide
attached to Asn494 was stable after at least 10 cycles of Edman degradation.
FAU - Gooley, A A
AU - Gooley AA
AD - Macquarie University Centre for Analytical Biotechnology (MUCAB), Sydney, NSW,
Australia.
FAU - Pisano, A
AU - Pisano A
FAU - Packer, N H
AU - Packer NH
FAU - Ball, M
AU - Ball M
FAU - Jones, A
AU - Jones A
FAU - Alewood, P F
AU - Alewood PF
FAU - Redmond, J W
AU - Redmond JW
FAU - Williams, K L
AU - Williams KL
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 (Glycopeptides)
RN - 0 (Oligosaccharides)
RN - 0 (Serum Albumin)
RN - 6158TKW0C5 (Phenytoin)
RN - 7006-34-0 (Asparagine)
SB - IM
MH - Amino Acid Sequence
MH - Asparagine/chemistry/*metabolism
MH - Carbohydrate Sequence
MH - Chromatography, High Pressure Liquid
MH - Chromatography, Ion Exchange
MH - Glycopeptides/chemistry/*metabolism
MH - Glycosylation
MH - Humans
MH - Mass Spectrometry
MH - Molecular Sequence Data
MH - Oligosaccharides/metabolism
MH - Phenytoin/analogs & derivatives
MH - Serum Albumin/metabolism
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):180-6.
PMID- 8460945
OWN - NLM
STAT- MEDLINE
DCOM- 19930423
LR - 20061115
IS - 0003-9861 (Print)
IS - 0003-9861 (Linking)
VI - 301
IP - 2
DP - 1993 Mar
TI - Structures of mucin-type sugar chains on human erythropoietins purified from
urine and the culture medium of recombinant Chinese hamster ovary cells.
PG - 375-8
AB - Less is known about the mucin-type sugar chains attached to human erythropoietin
as compared with N-linked sugar chains which structures and function have been
well studied. In this study, we purified urinary human erythropoietin from three
independent groups of aplastic anemia patients, and analyzed the structures of
mucin-type sugar chains as well as that obtained from recombinant human
erythropoietin produced by Chinese hamster ovary cells. Unlike the N-linked sugar
chains, the mucin-type sugar chains are totally different between the urinary and
the recombinant erythropoietins. All of the three independent samples of urinary
erythropoietin contained oligosaccharides with the structures of +/- Neu5Ac alpha
2-->6GalNAc, while recombinant human erythropoietin contained those with the
structures of Neu5Ac alpha 2-->3Gal beta 1-->3(Neu5Ac alpha 2-->6)GalNAc, Neu5Ac
alpha 2-->3Gal beta 1-->3GalNAc, and Gal beta 1-->3(Neu5Ac alpha 2-->6)GalNAc.
FAU - Inoue, N
AU - Inoue N
AD - Pharmaceutical Laboratory of Kirin Brewery Co. Ltd., Gumma, Japan.
FAU - Takeuchi, M
AU - Takeuchi M
FAU - Asano, K
AU - Asano K
FAU - Shimizu, R
AU - Shimizu R
FAU - Takasaki, S
AU - Takasaki S
FAU - Kobata, A
AU - Kobata A
LA - eng
PT - Comparative Study
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 (Mucins)
RN - 0 (Oligosaccharides)
RN - 0 (Recombinant Proteins)
RN - 11096-26-7 (Erythropoietin)
SB - IM
MH - Anemia, Aplastic
MH - Animals
MH - CHO Cells
MH - Carbohydrate Sequence
MH - Cricetinae
MH - Erythropoietin/*chemistry/genetics/urine
MH - Humans
MH - Molecular Sequence Data
MH - Mucins/*chemistry/genetics/urine
MH - Oligosaccharides/*chemistry/isolation & purification
MH - Recombinant Proteins/chemistry
MH - Urine/chemistry
EDAT- 1993/03/01 00:00
MHDA- 1993/03/01 00:01
CRDT- 1993/03/01 00:00
PHST- 1993/03/01 00:00 [pubmed]
PHST- 1993/03/01 00:01 [medline]
PHST- 1993/03/01 00:00 [entrez]
AID - S0003-9861(83)71158-6 [pii]
AID - 10.1006/abbi.1993.1158 [doi]
PST - ppublish
SO - Arch Biochem Biophys. 1993 Mar;301(2):375-8. doi: 10.1006/abbi.1993.1158.
PMID- 8407880
OWN - NLM
STAT- MEDLINE
DCOM- 19931112
LR - 20121115
IS - 0021-924X (Print)
IS - 0021-924X (Linking)
VI - 114
IP - 1
DP - 1993 Jul
TI - Structural study of the N-linked oligosaccharides of hepatocyte growth factor by
two-dimensional sugar mapping.
PG - 76-82
AB - The structures of the N-linked oligosaccharides on recombinant human hepatocyte
growth factor (rh-HGF) expressed by Chinese hamster ovary (CHO) cells were
studied by two-dimensional sugar mapping. The oligosaccharides released from the
glycopeptides by peptide: N-glycosidase F (PNGase F) treatment were tagged with
2-aminopyridine at the reducing ends. The alpha-chain was linked by biantennary,
triantennary, and tetraantennary oligosaccharides, but the dominant
oligosaccharides linking the beta-chain were biantennary (> 85%). There was no
significant difference in oligosaccharide structures between the two
glycosylation sites on each chain, that is, Asn263 and Asn371 on the alpha-chain,
and Asn535 and Asn622 on the beta-chain. The linkage of sialic acid to the
non-reducing terminal galactose was identified as NeuAc alpha(2-3) by 1H-NMR
spectrometry. The structures of the N-linked oligosaccharides from rat HGF were
also studied. Triantennary oligosaccharides were obtained from the alpha-chain
and a biantennary oligosaccharide was obtained from the beta-chain. This result
indicates that the alpha-chain is also linked by higher branched oligosaccharides
than the beta-chain in rat HGF.
FAU - Hara, H
AU - Hara H
AD - Pharmaceuticals Research Center of Toyobo Co., Ltd., Otsu.
FAU - Nakae, Y
AU - Nakae Y
FAU - Sogabe, T
AU - Sogabe T
FAU - Ihara, I
AU - Ihara I
FAU - Ueno, S
AU - Ueno S
FAU - Sakai, H
AU - Sakai H
FAU - Inoue, H
AU - Inoue H
FAU - Shimizu, S
AU - Shimizu S
FAU - Nakamura, T
AU - Nakamura T
FAU - Shimizu, N
AU - Shimizu N
LA - eng
PT - Journal Article
PL - England
TA - J Biochem
JT - Journal of biochemistry
JID - 0376600
RN - 0 (Aminopyridines)
RN - 0 (Oligosaccharides)
RN - 0 (Recombinant Proteins)
RN - 67256-21-7 (Hepatocyte Growth Factor)
RN - WSX981HEWU (alpha-aminopyridine)
SB - IM
MH - Aminopyridines/chemistry
MH - Animals
MH - CHO Cells
MH - Carbohydrate Conformation
MH - Carbohydrate Sequence
MH - Chromatography, High Pressure Liquid
MH - Cricetinae
MH - Cricetulus
MH - Hepatocyte Growth Factor/*chemistry
MH - Liver/*chemistry
MH - Molecular Sequence Data
MH - Oligosaccharides/*chemistry
MH - Rats
MH - Recombinant Proteins/chemistry
MH - Spectrometry, Fluorescence
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]
PST - ppublish
SO - J Biochem. 1993 Jul;114(1):76-82.