Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/326433
Type: Artigo
Title: Biochemical And Functional Studies Of Coltx-i, A New Myotoxic Phospholipase A(2) Isolated From Crotalus Oreganus Lutosus (great Basin Rattlesnake) Snake Venom
Author: Almeida
J. R.; Resende
L. M.; Silva
A. G.; Ribeiro
R. I. M. A.; Stabeli
R. G.; Soares
A. M.; Calderon
L. A.; Marangoni
S.; Da Silva
S. L.
Abstract: Commonly, phospholipases A(2) (PLA(2)s) play key roles in the pathogenesis of the local tissue damage characteristic of crotaline and viperine snake envenomations. Crotalus oreganus lutosus snake venom has not been extensively studied; therefore, the characterization of its components represents a valuable biotechnological tool for studying pathophysiological processes of envenoming and for gaining a deeper understanding of its biological effects. In this study, for the first time, a basic PLA(2) myotoxin, ColTx-I, was purified from C. o. lutosus through two chromatographic steps. ColTx-I is monomeric with calculated molecular mass weight (Mw) of 14,145 Da and a primary structure closely related to basic PLA(2)s from viperid venoms. The pure enzyme has a specific activity of 15.87 +/- 0.65 nmol/min/mg at optimal conditions (pH 8.0 and 37 degrees C). ColTx-I activity was found to be dependent on Ca2+, as its substitution by other ionic species as well as the addition of chelating agents significantly reduced its phospholipase activity. In vivo, ColTx-I triggered dose-dependent inflammatory responses, measured using the paw edema model, with an increase in IL-6 levels, systemic and local myotoxicity, characterized by elevated plasma creatine kinase activity. ColTx-I induced a complex series of degenerative events associated with edema, inflammatory infiltrate and skeletal muscle necrosis. These biochemical and functional results suggest that ColTx-I, a myotoxic and inflammatory mediator, plays a relevant role in C. o. lutosus envenomation. Thus, detailed studies on its mechanism of action, such as evaluating the synergism between ColTx-I and other venom components may reveal targets for the development of more specific and effective therapies. (C) 2016 Elsevier Ltd. All rights reserved.
Subject: Snake Venom
Phospholipase A(2)
Myotoxin
Crotalus Oreganus Lutosus
Biological Activities
Editor: Pergamon-Elsevier Science LTD
Oxford
Rights: fechado
Identifier DOI: 10.1016/j.toxicon.2016.03.008
Address: http://www-sciencedirect-com.ez88.periodicos.capes.gov.br/science/article/pii/S0041010116300484
Date Issue: 2016
Appears in Collections:Unicamp - Artigos e Outros Documentos

Files in This Item:
File SizeFormat 
000379373400001.pdf3.52 MBAdobe PDFView/Open


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.