Linked Life Data

11520795

Source:http://linkedlifedata.com/resource/pubmed/id/11520795

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
2001-8-24
pubmed:abstractText
The functional importance of platelet endothelial cell adhesion molecule-1 (PECAM-1/CD31) in platelets is unclear. Because PECAM-1 represents a newly assigned immunoglobulin-ITIM superfamily member expressed on the surface of platelets, it was hypothesized that it may play an important regulatory role in modulating ITAM-bearing receptors such as collagen (GP)VI receptor and FcgammaRIIA. To examine the functional role of PECAM-1 in regulating platelet-collagen interactions, 2 different approaches were applied using recombinant human PECAM-1-immunoglobulin chimeras and platelets derived from PECAM-1-deficient mice. Stimulation of platelets by collagen-, (GP)VI-selective agonist, collagen-related peptide (CRP)-, and PECAM-1-immunoglobulin chimera induced tyrosine phosphorylation of PECAM-1 in a time- and dose-dependent manner. Activation of PECAM-1 directly through the addition of soluble wild-type PECAM-1-immunoglobulin chimera, but not mutant K89A PECAM-1-immunoglobulin chimera that prevents homophilic binding, was found to inhibit collagen- and CRP-induced platelet aggregation. PECAM-1-deficient platelets displayed enhanced platelet aggregation and secretion responses on stimulation with collagen and CRP, though the response to thrombin was unaffected. Under conditions of flow, human platelet thrombus formation on a collagen matrix was reduced in a dose-dependent manner by human PECAM-1-immunoglobulin chimera. Platelets derived from PECAM-1-deficient mice form larger thrombi when perfused over a collagen matrix under flow at a shear rate of 1800 seconds(-1) compared to wild-type mice. Collectively, these results indicate that PECAM-1 serves as a physiological negative regulator of platelet-collagen interactions that may function to negatively limit growth of platelet thrombi on collagen surfaces.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
AIM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0006-4971
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
98
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1456-63
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:11520795-Animals, pubmed-meshheading:11520795-Antigens, CD31, pubmed-meshheading:11520795-Blood Coagulation, pubmed-meshheading:11520795-Blood Platelets, pubmed-meshheading:11520795-Carrier Proteins, pubmed-meshheading:11520795-Collagen, pubmed-meshheading:11520795-Depression, Chemical, pubmed-meshheading:11520795-Humans, pubmed-meshheading:11520795-Infant, pubmed-meshheading:11520795-Mice, pubmed-meshheading:11520795-Mice, Knockout, pubmed-meshheading:11520795-Mutagenesis, Site-Directed, pubmed-meshheading:11520795-Peptides, pubmed-meshheading:11520795-Phosphorylation, pubmed-meshheading:11520795-Platelet Adhesiveness, pubmed-meshheading:11520795-Platelet Aggregation, pubmed-meshheading:11520795-Platelet Membrane Glycoproteins, pubmed-meshheading:11520795-Protein Processing, Post-Translational, pubmed-meshheading:11520795-Recombinant Fusion Proteins, pubmed-meshheading:11520795-Rheology, pubmed-meshheading:11520795-Serotonin
pubmed:year
2001
pubmed:articleTitle
Platelet endothelial cell adhesion molecule-1 is a negative regulator of platelet-collagen interactions.
pubmed:affiliation
Division of Haematology, Hanson Centre for Cancer Research, IMVS, Adelaide, Australia.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't