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A collagen-like peptide stimulates tyrosine phosphorylation of syk and
phospholipase C gamma2 in platelets independent of the integrin alpha2beta1
J Asselin, JM Gibbins, M Achison, YH Lee, LF Morton, RW Farndale, MJ Barnes and SP Watson
Department of Pharmacology, University of Oxford, UK.
Activation of platelets by collagen is mediated through a tyrosine
kinase-dependent pathway that is associated with phosphorylation of the Fc
receptor gamma chain, the tyrosine kinase syk, and phospholipase C gamma2
(PLC gamma2). We recently described a collagen-related triple- helical
peptide (CRP) with the sequence GCP*(GPP*)GCP*G (single letter amino acid
code: P* = hydroxyproline; Morton et al, Biochem J306:337, 1995). The
cross-linked peptide is a potent stimulus of platelet activation but,
unlike collagen, does not support alpha2beta1-mediated, Mg2+-dependent
adhesion, suggesting that its action is independent of the integrin
alpha2beta1. This finding suggests the existence of a platelet receptor
other than alpha2beta1 that underlies activation. In the present study, we
show that CRP stimulates tyrosine phosphorylation of the same pattern of
proteins in platelets as collagen, including syk and PLC gamma2. Protein
tyrosine phosphorylation induced by CRP is not altered in the absence of
Mg2+ or the presence of monoclonal antibodies (MoAbs) to the integrin
alpha2beta1 (MoAb 6F1 and MoAb 13), conditions that prevent the interaction
of collagen with the integrin. In contrast, phosphorylation of syk and PLC
gamma2 by collagen is partially reduced by MoAb 6F1 and MoAb 13 or by
removal of Mg2+. This may reflect a direct role of alpha2beta1 in
collagen-induced signaling events or an indirect role in which the integrin
facilitates the binding of collagen to its signaling receptor. The results
show an alpha2beta1-independent pathway of platelet activation by CRP that
involves phosphorylation of syk and PLC gamma2. This pathway appears to
contribute to platelet activation by collagen.
Volume 89,
Issue 4,
pp. 1235-1242,
02/15/1997
Copyright © 1997 by The American Society of Hematology
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K. Suzuki-Inoue, Y. Ozaki, M. Kainoh, Y. Shin, Y. Wu, Y. Yatomi, T. Ohmori, T. Tanaka, K. Satoh, and T. Morita
Rhodocytin Induces Platelet Aggregation by Interacting with Glycoprotein Ia/IIa (GPIa/IIa, Integrin alpha 2beta 1). INVOLVEMENT OF GPIa/IIa-ASSOCIATED Src AND PROTEIN TYROSINE PHOSPHORYLATION
J. Biol. Chem.,
January 5, 2001;
276(2):
1643 - 1652.
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M. Achison, C. M. Elton, P. G. Hargreaves, C. G. Knight, M. J. Barnes, and R. W. Farndale
Integrin-independent Tyrosine Phosphorylation of p125fak in Human Platelets Stimulated by Collagen
J. Biol. Chem.,
January 26, 2001;
276(5):
3167 - 3174.
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V. Schulte, D. Snell, W. Bergmeier, H. Zirngibl, S. P. Watson, and B. Nieswandt
Evidence for Two Distinct Epitopes within Collagen for Activation of Murine Platelets
J. Biol. Chem.,
January 5, 2001;
276(1):
364 - 368.
[Abstract]
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A.-H. Lagrue-Lak-Hal, N. Debili, G. Kingbury, C. Lecut, J.-P. Le Couedic, J.-L. Villeval, M. Jandrot-Perrus, and W. Vainchenker
Expression and Function of the Collagen Receptor GPVI during Megakaryocyte Maturation
J. Biol. Chem.,
April 27, 2001;
276(18):
15316 - 15325.
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H. E. Tibbles, A. Vassilev, H. Wendorf, D. Schonhoff, D. Zhu, D. Lorenz, B. Waurzyniak, X.-P. Liu, and F. M. Uckun
Role of a JAK3-dependent Biochemical Signaling Pathway in Platelet Activation and Aggregation
J. Biol. Chem.,
May 18, 2001;
276(21):
17815 - 17822.
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A. Navdaev, J. M. Clemetson, J. Polgar, B. E. Kehrel, M. Glauner, E. Magnenat, T. N. C. Wells, and K. J. Clemetson
Aggretin, a Heterodimeric C-type Lectin from Calloselasma rhodostoma (Malayan Pit Viper), Stimulates Platelets by Binding to alpha 2beta 1 Integrin and Glycoprotein Ib, Activating Syk and Phospholipase Cgamma 2, but Does Not Involve the Glycoprotein VI/Fc Receptor gamma Chain Collagen Receptor
J. Biol. Chem.,
June 8, 2001;
276(24):
20882 - 20889.
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