PMID- 10556798
OWN - NLM
STAT- MEDLINE
DCOM- 19991223
LR  - 20180423
IS  - 0014-2980 (Print)
IS  - 0014-2980 (Linking)
VI  - 29
IP  - 11
DP  - 1999 Nov
TI  - The sialoadhesin CD33 is a myeloid-specific inhibitory receptor.
PG  - 3440-9
AB  - Activating and inhibitory receptors act in concert to regulate cellular
      activation. Inhibitory receptors are characterized by the presence of a
      characteristic sequence known as an immunoreceptor tyrosine-based inhibitory
      motif (ITIM) in their cytoplasmic tail. Phosphorylated ITIM serve as docking
      sites for the SH2-containing phosphatases which then inhibit signal transduction.
      CD33 is a member of the immunoglobulin superfamily and contains two
      immunoglobulin-like domains, a transmembrane region and a cytoplasmic tail that
      has two potential ITIM sequences. CD33 expression is restricted to cells of
      myelomonocytic lineage. The precise function of CD33 is unknown although it is a 
      lectin that binds sialic acid residues in N- and O-glycans on cell surfaces.
      Co-immunoprecipitation studies demonstrate that CD33 associates with the
      SH2-containing tyrosine phosphatase SHP-1 in monocytes. The proximal ITIM is
      necessary and sufficient for SHP-1 binding which is mediated by the aminoterminal
      SH2 domain. Treatment of SHP-1 with a phosphopeptide representing the proximal
      CD33 ITIM results in increased SHP-1 enzymatic activity. CD33 exerts an
      inhibitory effect on tyrosine phosphorylation and Ca(2+) mobilization when
      co-engaged with the activating FcgammaRI receptor. This data indicates that CD33 
      is an inhibitory receptor that may regulate FcgammaRI signal transduction.
FAU - Ulyanova, T
AU  - Ulyanova T
AD  - Howard Hughes Medical Institute, Department of Pathology, Washington University
      School of Medicine, St. Louis, USA.
FAU - Blasioli, J
AU  - Blasioli J
FAU - Woodford-Thomas, T A
AU  - Woodford-Thomas TA
FAU - Thomas, M L
AU  - Thomas ML
LA  - eng
GR  - GM56455/GM/NIGMS NIH HHS/United States
PT  - Journal Article
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - Germany
TA  - Eur J Immunol
JT  - European journal of immunology
JID - 1273201
RN  - 0 (Antigens, CD)
RN  - 0 (Antigens, Differentiation, Myelomonocytic)
RN  - 0 (CD33 protein, human)
RN  - 0 (Cd33 protein, mouse)
RN  - 0 (Cell Adhesion Molecules)
RN  - 0 (Intracellular Signaling Peptides and Proteins)
RN  - 0 (Receptors, IgG)
RN  - 0 (Sialic Acid Binding Ig-like Lectin 3)
RN  - 42HK56048U (Tyrosine)
RN  - EC 3.1.3.48 (PTPN11 protein, human)
RN  - EC 3.1.3.48 (PTPN6 protein, human)
RN  - EC 3.1.3.48 (Protein Tyrosine Phosphatase, Non-Receptor Type 11)
RN  - EC 3.1.3.48 (Protein Tyrosine Phosphatase, Non-Receptor Type 6)
RN  - EC 3.1.3.48 (Protein Tyrosine Phosphatases)
RN  - EC 3.1.3.48 (Ptpn11 protein, mouse)
RN  - EC 3.1.3.48 (Ptpn6 protein, mouse)
RN  - EC 3.1.3.48 (SH2 Domain-Containing Protein Tyrosine Phosphatases)
SB  - IM
MH  - Animals
MH  - Antigens, CD/genetics/*metabolism
MH  - Antigens, Differentiation, Myelomonocytic/genetics/*metabolism
MH  - Binding Sites
MH  - Cell Adhesion Molecules/genetics/*metabolism
MH  - Cells, Cultured
MH  - Enzyme Activation
MH  - HL-60 Cells
MH  - Humans
MH  - Intracellular Signaling Peptides and Proteins
MH  - Mice
MH  - Protein Tyrosine Phosphatase, Non-Receptor Type 11
MH  - Protein Tyrosine Phosphatase, Non-Receptor Type 6
MH  - Protein Tyrosine Phosphatases/genetics/*metabolism
MH  - Receptors, IgG/*metabolism
MH  - SH2 Domain-Containing Protein Tyrosine Phosphatases
MH  - Sialic Acid Binding Ig-like Lectin 3
MH  - Tyrosine/metabolism
MH  - U937 Cells
MH  - src Homology Domains
EDAT- 1999/11/11 00:00
MHDA- 1999/11/11 00:01
CRDT- 1999/11/11 00:00
PHST- 1999/11/11 00:00 [pubmed]
PHST- 1999/11/11 00:01 [medline]
PHST- 1999/11/11 00:00 [entrez]
AID - 10.1002/(SICI)1521-4141(199911)29:11<3440::AID-IMMU3440>3.0.CO;2-C [doi]
PST - ppublish
SO  - Eur J Immunol. 1999 Nov;29(11):3440-9. doi:
      10.1002/(SICI)1521-4141(199911)29:11<3440::AID-IMMU3440>3.0.CO;2-C.