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| pubmed-article:9054388 | lifeskim:mentions | umls-concept:C1517892 | lld:lifeskim |
| pubmed-article:9054388 | lifeskim:mentions | umls-concept:C0332120 | lld:lifeskim |
| pubmed-article:9054388 | lifeskim:mentions | umls-concept:C0598002 | lld:lifeskim |
| pubmed-article:9054388 | lifeskim:mentions | umls-concept:C0208973 | lld:lifeskim |
| pubmed-article:9054388 | pubmed:issue | 11 | lld:pubmed |
| pubmed-article:9054388 | pubmed:dateCreated | 1997-4-17 | lld:pubmed |
| pubmed-article:9054388 | 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. | lld:pubmed |
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| pubmed-article:9054388 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9054388 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9054388 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:9054388 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9054388 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:9054388 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:9054388 | pubmed:author | pubmed-author:NewmanP JPJ | lld:pubmed |
| pubmed-article:9054388 | pubmed:author | pubmed-author:JacksonD EDE | lld:pubmed |
| pubmed-article:9054388 | pubmed:author | pubmed-author:WangRR | lld:pubmed |
| pubmed-article:9054388 | pubmed:author | pubmed-author:WardC MCM | lld:pubmed |
| pubmed-article:9054388 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9054388 | pubmed:day | 14 | lld:pubmed |
| pubmed-article:9054388 | pubmed:volume | 272 | lld:pubmed |
| pubmed-article:9054388 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9054388 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9054388 | pubmed:pagination | 6986-93 | lld:pubmed |
| pubmed-article:9054388 | pubmed:dateRevised | 2007-11-15 | lld:pubmed |
| pubmed-article:9054388 | pubmed:meshHeading | pubmed-meshheading:9054388-... | lld:pubmed |
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| pubmed-article:9054388 | pubmed:meshHeading | pubmed-meshheading:9054388-... | lld:pubmed |
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| pubmed-article:9054388 | pubmed:meshHeading | pubmed-meshheading:9054388-... | lld:pubmed |
| pubmed-article:9054388 | pubmed:year | 1997 | lld:pubmed |
| pubmed-article:9054388 | 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. | lld:pubmed |
| pubmed-article:9054388 | pubmed:affiliation | Blood Research Institute, Blood Center of Southeastern Wisconsin, Milwaukee, Wisconsin 53233-2121, USA. | lld:pubmed |
| pubmed-article:9054388 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:9054388 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:9054388 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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