Structure and Function of Snake Venom Proteins Affecting Platelet Plug Formation 英文参考文献.docVIP

Toxins 2010, 2, 10-23; doi:10.3390/toxins2010010 OPENACCESS toxins ISSN 2072-6651 /journal/toxins Review Structure and Function of Snake Venom Proteins Affecting Platelet Plug Formation Taei Matsui 1,*, Jiharu Hamako 2 and Koiti Titani 3 1 Department of Biology, Faculty of Medical Technology, Fujita Health University School of Health Sciences, Toyoake, Aichi 470-1192, Japan 2 Department of Physiology, Faculty of Medical Information Technology, Fujita Health University School of Health Sciences, Toyoake, Aichi 470-1192, Japan; E-Mail: jhamako@fujita-hu.ac.jp 3 Division of Medical Polymer Sciences, Institute for Comprehensive Medical Sciences, Fujita Health University, Toyoake, Aichi 470-1192, Japan; E-Mail: ktitani@crest.ocn.ne.jp * Author to whom correspondence should be addressed; E-Mail: tmatsui@fujita-hu.ac.jp; Tel.: +81-562-93-2594; Fax: +81-562-93-4595. Received: 1 December 2009; in revised form: 18 December 2009 / Accepted: 24 December 2009 / Published: 28 December 2009 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; snake venom; von Willebrand factor; platele