Structure and Function of Snake Venom Proteins Affecting Platelet Plug Formation

Toxins

Taei Matsui¹  Jiharu Hamako² 

[1] Department of Biology, Faculty of Medical Technology, Fujita Health University School of Health Sciences, Toyoake, Aichi 470-1192, JapanDepartment of Physiology, Faculty of Medical Information Technology, Fujita Health University School of Health Sciences, Toyoake, Aichi 470-1192, Japan;

关键词: disintegrin;    snake venom;    von Willebrand factor;    platelet GPIb;    thrombosis;   

DOI  :  10.3390/toxins2010010

来源: mdpi

【 摘 要 】

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.

【 授权许可】

CC BY   
© 2010 by the authors; licensee Molecular Diversity Preservation International, Basel, Switzerland