Jararhagin and jaracetin: Novel snake venom inhibitors of the integrin collagen receptor, α2β1

Mariagrazia De Luca, Christopher M. Ward, Keizo Ohmori, Robert K. Andrews, Michael C. Berndt

Research output: Contribution to journalArticleResearchpeer-review

91 Citations (Scopus)


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 α2β1-dependent platelet adhesion to collagen, a receptor interaction mediated through a homologous A domain on the integrin α2 subunit.

Original languageEnglish
Pages (from-to)570-576
Number of pages7
JournalBiochemical and Biophysical Research Communications
Issue number2
Publication statusPublished - 1 Jan 1995
Externally publishedYes

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