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rdf:type | |
lifeskim:mentions |
umls-concept:C0005821,
umls-concept:C0007577,
umls-concept:C0032176,
umls-concept:C0037083,
umls-concept:C0081939,
umls-concept:C0085536,
umls-concept:C0178539,
umls-concept:C0208973,
umls-concept:C0225336,
umls-concept:C0332120,
umls-concept:C0376315,
umls-concept:C0439855,
umls-concept:C0598002,
umls-concept:C1145667,
umls-concept:C1335280,
umls-concept:C1517892,
umls-concept:C1704666,
umls-concept:C1706044,
umls-concept:C1710082
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pubmed:issue |
11
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pubmed:dateCreated |
1997-4-17
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pubmed:abstractText |
Platelet/endothelial cell adhesion molecule-1 (PECAM-1) is a homophilic adhesion receptor that mediates leukocyte/endothelial cell interactions that take place during transendothelial migration. Recent reports have shown that the binding of certain anti-PECAM-1 antibodies results in up-regulation of integrin function on the surface of leukocytes and platelets, suggesting that PECAM-1 may be capable of transmitting information into the cell following its engagement. PECAM-1 isolated from resting or activated but nonaggregated platelets was phosphorylated predominantly on serine residues; however, PECAM-1 derived from activated, aggregated platelets was strongly phosphorylated on tyrosine. Synthetic tyrosine-phosphorylated peptides derived from five different regions within the cytoplasmic domain of PECAM-1 were screened for their ability to associate with cytoplasmic signaling molecules. The protein-tyrosine phosphatase SHP-2 was found to interact specifically with two different PECAM-1 phosphopeptides containing highly conserved phosphatase-binding motifs on PECAM-1 with the sequences VQpY663TEV and TVpY686SEV. More important, SHP-2 bound not only PECAM-1 phosphopeptides, but also became associated with full-length cellular PECAM-1 during the platelet aggregation process, and this interaction was mediated by the amino-terminal Src homology 2 domains of the phosphatase. Since SHP-2 normally serves as a positive regulator of signal transduction, its association with activated PECAM-1 suggests a number of potential mechanisms by which PECAM-1 engagement might be coupled to integrin activation in vascular cells.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
14
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pubmed:volume |
272
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
6986-93
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:9054388-Amino Acid Sequence,
pubmed-meshheading:9054388-Antigens, CD31,
pubmed-meshheading:9054388-Humans,
pubmed-meshheading:9054388-Integrins,
pubmed-meshheading:9054388-Molecular Sequence Data,
pubmed-meshheading:9054388-Platelet Aggregation,
pubmed-meshheading:9054388-Protein Tyrosine Phosphatases,
pubmed-meshheading:9054388-Signal Transduction
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pubmed:year |
1997
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pubmed:articleTitle |
The protein-tyrosine phosphatase SHP-2 binds platelet/endothelial cell adhesion molecule-1 (PECAM-1) and forms a distinct signaling complex during platelet aggregation. Evidence for a mechanistic link between PECAM-1- and integrin-mediated cellular signaling.
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pubmed:affiliation |
Blood Research Institute, Blood Center of Southeastern Wisconsin, Milwaukee, Wisconsin 53233-2121, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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