Jararhagin and jaracetin: novel snake venom inhibitors of the integrin collagen receptor, alpha 2 beta 1.
M De Luca, C M Ward, K Ohmori, R K Andrews, M C Berndt
Hazel and Pip Appel Vascular Biology Laboratory, Baker Medical Research Institute, Prahran, Australia.
Biochemical and biophysical research communications 1995 Jan 17Two 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.
Citation
M De Luca, C M Ward, K Ohmori, R K Andrews, M C Berndt. Jararhagin and jaracetin: novel snake venom inhibitors of the integrin collagen receptor, alpha 2 beta 1. Biochemical and biophysical research communications. 1995 Jan 17;206(2):570-6
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PMID: 7530003
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