Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
28
pubmed:dateCreated
1994-8-17
pubmed:abstractText
Platelet adhesion to subendothelial von Willebrand factor involves receptor recognition by the platelet glycoprotein (GP) Ib-IX and initiates activation signals that contribute to primary hemostasis. We show here that GPIb-IX is specifically associated with an intracellular 29-kDa protein. The physicochemical characteristics and amino acid sequence of this protein indicate that it is identical to the human zeta-isoform 14-3-3 protein, previously characterized as a platelet phospholipase A2 (PLA2). As activation of PLA2 is an early event in GPIb-IX-mediated signaling, this result suggests that ligand occupancy of GPIb-IX may directly activate PLA2, leading to platelet activation.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
269
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
18287-90
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed:year
1994
pubmed:articleTitle
Association of a phospholipase A2 (14-3-3 protein) with the platelet glycoprotein Ib-IX complex.
pubmed:affiliation
Department of Vascular Biology, Scripps Research Institute, La Jolla, California 92037.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't