Synergism between baltergin metalloproteinase and Ba SPII RP4 PLA2 from Bothrops alternatus venom on skeletal muscle (C2C12) cells

Soledad Bustillo, Claudia C. Gay, María E. García Denegri, Luis A. Ponce-Soto, Elisa Bal de Kier Joffé, Ofelia Acosta, Laura C. Leiva

Producción científica: Contribución a una revistaArtículorevisión exhaustiva

43 Citas (Scopus)

Resumen

Acute muscle damage, myonecrosis, is one of the main characteristics of envenoming by Bothrops genus. In this invitro study we investigated the role of a metalloproteinase (baltergin) and an acidic phospholipase A2 (Ba SPII RP4) in the cytotoxicity exhibited by Bothrops alternatus venom. Baltergin metalloproteinase purified from the venom exerted a toxic effect on C2C12 myoblast cells (CC50: 583.34μg/mL) which involved morphological alterations compatible with apoptosis/anoikis. On the contrary, the most abundant PLA2 isolated from this venom did not exhibit cytotoxicity at times and doses tested. However, when myoblasts were treated with both enzymes together, synergic activity was demonstrated. Neutralization of the venom with specific antibodies (IgG anti-baltergin and IgG anti-PLA2) confirmed this synergism.

Idioma originalInglés
Páginas (desde-hasta)338-343
Número de páginas6
PublicaciónToxicon
Volumen59
N.º2
DOI
EstadoPublicada - feb. 2012
Publicado de forma externa

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