De Luca M, Ward C M, Ohmori K, Andrews R K, Berndt M C
Hazel and Pip Appel Vascular Biology Laboratory, Baker Medical Research Institute, Prahran, Australia.
Biochem Biophys Res Commun. 1995 Jan 17;206(2):570-6. doi: 10.1006/bbrc.1995.1081.
Two novel proteins, jararhagin and jaracetin, were purified from Bothrops jararaca viper venom. Jararhagin is a 55-kDa member of the metalloprotease-disintegrin family. Jaracetin is a 60-kDa dimer representing a differently processed form of jararhagin. Like botrocetin, a previously described viper venom protein, jararhagin and jaracetin modulated binding of von Willebrand Factor to the glycoprotein Ib-IX complex on platelets through a specific interaction with the von Willebrand Factor A1 domain. Both jararhagin and jaracetin, but not botrocetin, also blocked alpha 2 beta 1-dependent platelet adhesion to collagen, a receptor interaction mediated through a homologous A domain on the integrin alpha 2 subunit.
