The BioGRID | PUBLICATION VIEW

	Biochem. Biophys. Res. Commun. Apr (2000); 270(3):932-5
Role of the recombinant non-integrin platelet collagen receptor P65 on platelet activation induced by convulxin.
Francischetti IM, Chiang TM, Guimar�es JA, Bon C
Unite des Venins, Institut Pasteur, 25 rue du Dr. Roux, Paris, 75724, France. ifrancischetti@niaid.nih.gov
Abstract: Convulxin (Cvx) isolated from Crotalus durissus terrificus venom selectively binds with a high affinity to platelets and induces platelet aggregation by a mechanism that resembles that induced by collagen. Taking advantage that P65 has been recently cloned and expressed as a recombinant soluble protein (rec-P65), we examined the role of this non-integrin collagen receptor in platelet activation induced by Cvx. Rec-P65 blocked platelet adhesion to collagen-coated surfaces and inhibited platelet aggregation and ATP secretion induced by type I collagen. On the other hand, rec-P65 did not inhibit platelet aggregation and ATP secretion induced by Cvx, and it did not affect platelet adhesion to Cvx. In addition, ligand-blotting indicated that the Cvx binding to the collagen receptor GPVI was preserved in the presence of rec-P65. These observations indicate that P65 does not play a significant role in platelet activation by Cvx; in contrast, platelet response to collagen involves multiple receptors.
[PUBMED: 10772928]