Linked Life Data

8561798

Source:http://linkedlifedata.com/resource/pubmed/id/8561798

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1996-2-23
pubmed:abstractText
Platelet activation and aggregation induced by agonists such as thrombin are accompanied by the phosphorylation of several proteins on tyrosine. Such tyrosine phosphorylation is dependent upon activation and ligand engagement of the major integrin receptor on the surface of platelets, glycoprotein (GP) IIb-IIIa (alpha IIb beta 3), but how this is accomplished is not known. The only platelet membrane GP known to associated with non receptor tyrosine kinases is CD36 (GPIV) which forms associations with pp60Fyn, pp62Yes, and pp54/58Lyn, and antibodies directed against CD36 activate platelets in a process dependent upon GPIIb-IIIa. These and other data suggest a physical association between the two membrane GPs, IIb-IIIa and CD36. By the use of immunoprecipitation of lysates of platelets that have been surface labeled and chemically crosslinked we show here that CD36 and GPIIb-IIIa are spatially associated on the surface of resting platelets.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0006-291X
pubmed:author
pubmed:issnType
Print
pubmed:day
17
pubmed:volume
218
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
575-81
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1996
pubmed:articleTitle
CD36 is spatially associated with glycoprotein IIb-IIIa (alpha IIb beta 3) on the surface of resting platelets.
pubmed:affiliation
Cancer Research Unit, Faculty of Medicine and Health Sciences, University of Newcastle, Callaghan, New South Wales, Australia.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't