Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/67278
Type: Artigo de periódico
Title: Functional characterization of a basic D49 phospholipase A(2) (LmTX-I) from the venom of the snake Lachesis muta muta (bushmaster)
Author: Damico, DCS
Bueno, LGF
Rodrigues-Simioni, L
Marangoni, S
da Cruz-Hofling, MA
Novello, JC
Abstract: The whole venom of Lachesis muta muta is preponderantly neurotoxic but moderately myotoxic on the chick biventer cervicis preparation (BCp). We have now examined these toxic activities of a basic phospholipase A(2), LmTX-I, isolated from the whole venom. LmTX-I caused a significant concentration-dependent neuromuscular blockade in the BCp. The time to produce 50% neuromuscular blockade was 14.7 +/- 0.75 min (30 mu g/ml). 23.6 +/- 0.9 min (10 mu g/ml). 34 +/- 1.7 min (2.5 mu g/ml) and 39.2 +/- 3.6 min (1 mu g/ml), (n = 5/concentration; p < 0.05). Complete blockade with all tested concentrations was not accompanied by inhibition of the response to ACh. At the highest concentration. LmTX-I (30 mu g/ml) significantly reduced contractures elicited by exogenous KCl (20 mM), increased the release of creatine kinase (1542.5 +/- 183.9 IU[L vs 442.7 +/- 39.8 IU/L for controls after 120 min, p < 0.05), and induced the appearance of degenerating muscle fibers (similar to 15%). Quantification of myonecrosis indicated 14.8 +/- 0.8 and 2.0 +/- 0.4%, with 30 and 10 mu g/ml venom concentration, respectively, against 1.07 +/- 0.4% for control preparations. The findings indicate that the basic PLA(2) present on venom from L. m. muta (LmTX-1) possesses a dominant neurotoxic action on isolated chick nerve-muscle preparations, whereas myotoxicity was mainly observed at the highest Concentration used (30 mu g/ml). These effects of LmTX-I closely reproduce the effects of the whole venom of L. m. muta in chick neuromuscular preparations. (c) 2006 Elsevier Ltd. All rights reserved.
Subject: biventer cervicis preparation
Asp49 phospholipase A2
Lachesis muta muta venom
myotoxicity
neuromuscular blockade
neurotoxicity
Country: Inglaterra
Editor: Pergamon-elsevier Science Ltd
Rights: fechado
Identifier DOI: 10.1016/j.toxicon.2006.02.007
Date Issue: 2006
Appears in Collections:Unicamp - Artigos e Outros Documentos

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