The use of snake venom toxins as tools to study platelet receptors for collagen and von Willebrand factor

Haemostasis
R K AndrewsS P Watson

Abstract

A large proportion of the biologically active proteins and peptides present within snake venoms interact with components of the haemostatic system to promote or inhibit the normal sequence of events that lead to clot formation. The venom proteins achieve their effects through interaction with various components of the coagulation cascade, endothelial matrix and platelets. Within the latter group, a number of venom proteins target the interaction of platelets with the major adhesive proteins, von Willebrand factor and collagen. The venom proteins bind either the adhesive protein itself or their receptors on the platelet surface, notably GP-Ib-IX-V and GPVI. This review discusses the substantial contribution that venom proteins have made to our understanding of the role of these two adhesive proteins and their receptors (excluding GPIIb-IIIa) in platelet regulation.

Citations

Mar 27, 2003·Toxicon : Official Journal of the International Society on Toxinology·Paul G GallagherJay W Fox
Aug 9, 2003·Toxicon : Official Journal of the International Society on Toxinology·Paula G Sells
Jan 9, 2010·Toxicon : Official Journal of the International Society on Toxinology·Isabelle TanjoniAna M Moura-da-Silva
Aug 4, 2011·Journal of Thrombosis and Haemostasis : JTH·R M Kini
Aug 15, 2006·Toxicon : Official Journal of the International Society on Toxinology·Daniela A P CidadeRodolpho M Albano
Aug 23, 2005·Toxicon : Official Journal of the International Society on Toxinology·Gavin D LaingYotis A Senis
Jun 1, 2005·Toxicon : Official Journal of the International Society on Toxinology·Lakshmi C WijeyewickremaRobert K Andrews
Dec 12, 2017·BioMed Research International·Bruna Barbosa de SousaFábio de Oliveira
Jul 26, 2003·The Journal of Biological Chemistry·Sachiko KanajiThomas J Kunicki
Mar 22, 2003·Blood·Bernhard Nieswandt, Steve P Watson
May 29, 2020·Journal of Medicinal Chemistry·Holly FosterRichard Foster

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