Please use this identifier to cite or link to this item:
|Type:||Artigo de periódico|
|Title:||Synergism between baltergin metalloproteinase and Ba SPII RP4 PLA(2) from Bothrops alternatus venom on skeletal muscle (C2C12) cells|
|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 A(2) (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 mu g/mL) which involved morphological alterations compatible with apoptosis/anoikis. On the contrary, the most abundant PLA(2) 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-PLA(2)) confirmed this synergism. (C) 2011 Elsevier Ltd. All rights reserved.|
|Editor:||Pergamon-elsevier Science Ltd|
|Citation:||Toxicon. Pergamon-elsevier Science Ltd, v. 59, n. 2, n. 338, n. 343, 2012.|
|Appears in Collections:||Unicamp - Artigos e Outros Documentos|
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.