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Synergism between baltergin metalloproteinase and Ba SPII RP4 PLA2 from Bothrops alternatus venom on skeletal muscle (C2C12) cells |
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| Authors: | Soledad BustilloClaudia C Gay María E García Denegri Luis A Ponce-SotoElisa Bal de Kier Joffé Ofelia AcostaLaura C Leiva |
| Institution: | a Facultad de Ciencias Exactas y Naturales y Agrimensura, Universidad Nacional del Nordeste (UNNE), Av. Libertad 5470, CP 3400, Corrientes, Argentina b Facultad de Ciencias Veterinarias, Universidad Nacional del Nordeste (UNNE), Corrientes, Argentina c Area Investigación, Instituto de Oncología Angel H. Roffo, Buenos Aires, Argentina d Departamento de Bioquímica, Instituto de Biología, Universidade Estadual de Campinas, Campinas, SP, Brasil |
| Abstract: | Acute muscle damage, myonecrosis, is one of the main characteristics of envenoming by Bothrops genus. In this in vitro 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: 583.34 μg/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. |
| Keywords: | Bothrops alternatus Cytotoxicity Phospholipase A2 Metalloproteinase Baltergin C2C12 Synergism |
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