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Originally published In Press as doi:10.1074/jbc.M001531200 on June 27, 2000

J. Biol. Chem., Vol. 275, Issue 37, 28526-28531, September 15, 2000
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Evidence of a Role for SHP-1 in Platelet Activation by the Collagen Receptor Glycoprotein VI*

Jean-Max PasquetDagger §, Lynn QuekDagger , Sophie PasquetDagger , Alastair Poole, James R. Matthews||, Clifford Lowell**, and Steve P. WatsonDagger Dagger Dagger

From the Dagger  Department of Pharmacology, University of Oxford, Mansfield Road, Oxford OX1 3QT, United Kingdom,  Department of Pharmacology, School of Medical Sciences, University Walk, Bristol BS8 1TD, United Kingdom, || Department of Medicine, University of Wales, Tenovus Building, Heath Park, Cardiff CF4 4XX, United Kingdom, and the ** Department of Laboratory Medicine, University of California, San Francisco, California 91443-0100

The Src homology (SH)2 domain-containing protein-tyrosine phosphatase SHP-1 is tyrosine phosphorylated in platelets in response to the glycoprotein VI (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 and 70 kDa specifically associate with SHP-1 following stimulation by CRP and collagen. The tyrosine kinases Lyn, which exists as a 53 and 56-kDa doublet, and Syk were identified as major components of these bands, respectively. Kinase assays on SHP-1 immunoprecipitates performed in the 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 proteins, bound selectively to a glutathione S-transferase 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 of a functional role for SHP-1 in platelet activation by GPVI.

* This work was supported by the Wellcome Trust, the Fondation pour la Recherche Medicale, the Institut National de la Santé et de la Recherche Médicale, and by Grants DK50267 and HL54467 (to C. L.) from the National Institutes of Health.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

§ Present address: UMR 5533 CNRS, Laboratoire de Pathologie Cellulaire de l'hemostase, Hopital Cardiologique du Haut-Leveque, 33604 Pessac, France.

Dagger Dagger A British Heart Foundation Research Fellow. To whom correspondence should be addressed. Tel.: 44-1865-271592; Fax: 44-1865-2719853; E-mail: steve.watson@pharm.ox.ac.uk.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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