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Papers In Press, published online ahead of print June 27, 2000
Department of Pharmacology, University of Oxford, Oxford OX1 3QT
Corresponding Author: Steve.Watson{at}pharm.ox.ac.uk
The SH2 domain containing protein tyrosine phosphatase SHP-1 is tyrosine phosphorylated in platelets in response to the GPVI-selective agonist collagen related peptide (CRP), collagen and thrombin. Two major, unidentified tyrosine phosphorylated bands of 28 and 32 kDa, and a minor band of 130 kDa, coprecipitate with SHP-1 in response to all three agonists. Additionally, tyrosine phosphorylated proteins of 50-55 kDa, and 70 kDa specifically associate with SHP-1 following stimulation by CRP and collagen. The tyrosine kinase Lyn, which exists as a 53/56 kDa doublet, and Syk were identified as major components of these bands, respectively. Kinase assays on SHP-1 immunoprecipitates performed in presence of the Src family kinase inhibitor PP1 confirmed the presence of a Src kinase in CRP but not thrombin-stimulated cells. Lyn, Syk and SLP-76, along with tyrosine phosphorylated 28, 32 and 130 kDa, bound selectively to a GST protein encoding the SH2 domains of SHP-1 suggesting that this is the major site of interaction. Platelets isolated from motheaten viable mice (mev/mev) revealed the presence of a heavily tyrosine phosphorylated 26 kDa protein that was not found in wild type platelets. CRP-stimulated mev/mev platelets manifested hypophosphorylation of Syk and Lyn and reduced P-selectin expression relative to controls. These observations provide evidence for a functional role for SHP-1 in platelet activation by GPVI.
J. Biol. Chem, 10.1074/jbc.M001531200
Submitted on February 18, 2000
Revised on June 26, 2000
Accepted on June 27, 2000
Evidence for a role of SHP-1 in platelet activation by the collagen receptor GPVI
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