Structure and function of snake venom proteins affecting platelet plug formation

Toxins (Basel). 2010 Jan;2(1):10-23. doi: 10.3390/toxins2010010. Epub 2009 Dec 28.

Abstract

Many snake venom proteins have been isolated that affect platelet plug formation by interacting either with platelet integrins, membrane glycoprotein Ib (GPIb), or plasma von Willebrand factor (VWF). Among them, disintegrins purified from various snake venoms are strong inhibitors of platelet aggregation. Botrocetin and bitiscetin derived from Bothrops jararaca and Bitis arietans venom, respectively, induce VWF-dependent platelet agglutination in vitro. Several GPIb-binding proteins have also been isolated from snake venoms. In this review, we focus on the structure and function of those snake venom proteins that influence platelet plug formation. These proteins are potentially useful as reagents for the sub-diagnosis of platelet disorder or von Willebrand disease, as well as for clinical and basic research of thrombosis and hemostasis.

Keywords: disintegrin; platelet GPIb; snake venom; thrombosis; von Willebrand factor.

Publication types

  • Review

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Blood Platelets* / metabolism
  • Humans
  • Platelet Aggregation
  • Platelet Glycoprotein GPIb-IX Complex
  • Snake Venoms*
  • von Willebrand Factor

Substances

  • Platelet Glycoprotein GPIb-IX Complex
  • Snake Venoms
  • von Willebrand Factor