Your browser doesn't support javascript.
loading
Why myotoxin-containing snake venoms possess powerful nucleotidases?
Caccin, Paola; Pellegatti, Patrizia; Fernandez, Julián; Vono, Maria; Cintra-Francischinelli, Mariana; Lomonte, Bruno; Gutiérrez, José María; Di Virgilio, Francesco; Montecucco, Cesare.
Afiliación
  • Caccin P; Dipartimento di Scienze Biomediche, Università di Padova, and Istituto di Neuroscienze-CNR Sezione di Padova, Padova 35121, Italy.
Biochem Biophys Res Commun ; 430(4): 1289-93, 2013 Jan 25.
Article en En | MEDLINE | ID: mdl-23261426
The venom of the snake Bothrops asper causes muscle necrosis, pain and inflammation. This venom contains myotoxins which cause an increase in intracellular Ca(2+) concentration and release of K(+) and ATP from myotubes. ATP is a key danger molecule that triggers a variety of reactions, including activation of the innate immune response. Here, using ATP-luciferase bioluminescence imaging technique, we show for the first time in vivo, that the purified myotoxins induce rapid release of ATP, whilst the complete venom of B. asper does at a very small extent. This apparent contradiction is explained by the finding that the venom contains powerful nucleotidases that in vivo convert ATP into ADP, AMP and Adenosine. These findings indicate that high concentrations of adenosine are generated by the double action of the venom and provide the experimental basis to the suggestion that in situ generated adenosine plays an important role in envenomation via its hypotensive, paralyzing and anti-coagulant activities.
Asunto(s)

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Adenosina Trifosfato / Venenos de Crotálidos / Proteínas de Reptiles / Fosfolipasas A2 Grupo II / Nucleotidasas Límite: Animals Idioma: En Revista: Biochem Biophys Res Commun Año: 2013 Tipo del documento: Article País de afiliación: Italia Pais de publicación: Estados Unidos

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Adenosina Trifosfato / Venenos de Crotálidos / Proteínas de Reptiles / Fosfolipasas A2 Grupo II / Nucleotidasas Límite: Animals Idioma: En Revista: Biochem Biophys Res Commun Año: 2013 Tipo del documento: Article País de afiliación: Italia Pais de publicación: Estados Unidos