Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
51
pubmed:dateCreated
1995-1-24
pubmed:abstractText
The Fc receptor for IgG in platelets was identified as the integral membrane isoform encoded by the Fc gamma RIIA gene. Functional analysis of this molecule determined that activated Fc gamma RIIA is tyrosine phosphorylated and that activation induced the physical association with the protein tyrosine kinase p72syk. Other tyrosine-phosphorylated molecules also co-immunoadsorbed with the activated receptor. Tyrosine kinase activity co-immunoadsorbing with the platelet Fc gamma R was enhanced upon activation and specifically induced the phosphorylation, on tyrosine residues, of a physically associated 72-kDa protein. These data support a model of Fc gamma receptor-mediated platelet activation where signal is transduced through inducible association of the tyrosine kinase p72syk with the low affinity Fc gamma receptor. Thrombin, a potent platelet agonist, has been shown to up-regulate the activity of the tyrosine kinase p72syk in platelets. Consequently, our findings identify a second pathway by which p72syk is activated in platelets.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
23
pubmed:volume
269
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
32435-40
pubmed:dateRevised
2011-11-2
pubmed:meshHeading
pubmed:year
1994
pubmed:articleTitle
Clustering of the platelet Fc gamma receptor induces noncovalent association with the tyrosine kinase p72syk.
pubmed:affiliation
Department of Internal Medicine, Ohio State University, Columbus 43210.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.