Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/74002
Type: Artigo de periódico
Title: Synergism between baltergin metalloproteinase and Ba SPII RP4 PLA(2) from Bothrops alternatus venom on skeletal muscle (C2C12) cells
Author: Bustillo, S
Gay, CC
Denegri, MEG
Ponce-Soto, LA
Joffe, EBD
Acosta, O
Leiva, LC
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.
Subject: Bothrops alternatus
Cytotoxicity
Phospholipase A(2)
Metalloproteinase
Baltergin
C2C12
Synergism
Country: Inglaterra
Editor: Pergamon-elsevier Science Ltd
Rights: fechado
Identifier DOI: 10.1016/j.toxicon.2011.11.007
Date Issue: 2012
Appears in Collections:Artigos e Materiais de Revistas Científicas - Unicamp

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