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(Received for publication, May 16, 1997, and in revised form, July 8, 1997)
From the We analyzed the interaction of convulxin (Cvx), a
72-kDa protein isolated from the venom of Crotalus durissus
terrificus, with human platelets. Cvx is a potent platelet
agonist that induces an increase in the intracellular Ca2+
concentration ([Ca2+]i), granule exocytosis and
aggregation. 125I-Labeled Cvx binds specifically and
rapidly to platelets at binding sites of high and moderate affinity.
Platelets adhere to immobilized Cvx in a time-dependent but
cation-independent manner. Platelet exocytosis and aggregation induced
by Cvx were inhibited by an anti-integrin
Volume 272, Number 43,
Issue of October 24, 1997
pp. 27035-27041
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
Adhesion and Activation of Human Platelets Induced by Convulxin
Involve Glycoprotein VI and Integrin
2
1
,
,
Laboratoire de Recherche sur
l'Hémostase et la Thrombose, Faculté de Médecine
Xavier Bichat, BP 416, 75870 Paris Cedex 18, France,
Unité des Venins, Institut Pasteur, 25 rue du Dr Roux,
75724 Paris Cedex 15, France, and the ¶ Department of Internal
Medicine, Faculty of Medicine, Kyoto University, 54 Shogoin
Kawaramachi, Sakyo-Ku, Kyoto 606-01, Japan
2
1 monoclonal antibody (6F1) and by the
Fab fragments of a polyclonal anti-glycoprotein VI (GPVI) antibody.
Both the adhesion of platelets to Cvx and the Cvx-induced increase in
[Ca2+]i were inhibited by anti-GPVI Fab fragments
but not by 6F1. Ligand blotting assay showed that 125I-Cvx
binds to a 57-kDa platelet protein with an electrophoretic mobility
identical to that of GPVI. In addition, we observed the following: (i)
125I-Cvx binds to GPVI immunoprecipitated by the anti-GPVI
antibody from a platelet lysate, and (ii) Cvx inhibits the binding of
anti-GPVI IgG to GPVI. Taken together, these results demonstrate that
GPVI behaves as a Cvx receptor and that the
21 integrin appears to be involved
in the later stages of Cvx-induced platelet activation, i.e. exocytosis and aggregation.
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