Role of the recombinant non-integrin platelet collagen receptor P65 on platelet activation induced by convulxin

Ivo M.B. Francischetti, Thomas M. Chiang, Jorge A. Guimarães, Cassian Bon

Research output: Contribution to journalArticlepeer-review

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. (C) 2000 Academic Press.

Original languageEnglish (US)
Pages (from-to)932-935
Number of pages4
JournalBiochemical and Biophysical Research Communications
Volume270
Issue number3
DOIs
StatePublished - Apr 21 2000
Externally publishedYes

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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