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dc.creatorLomonte, Bruno
dc.creatorTarkowski, Andrej
dc.creatorHanson, Lars Ake
dc.date.accessioned2017-09-12T21:48:16Z
dc.date.available2017-09-12T21:48:16Z
dc.date.issued1994
dc.identifier.citationhttp://europepmc.org/abstract/med/7886694es_ES
dc.identifier.issn0041-0101
dc.identifier.urihttp://hdl.handle.net/10669/73144
dc.description.abstractThe cytotoxic activity of Bothrops asper myotoxin II, a lysine-49 phospholipase A2 isoform, on different cell types in culture, was investigated. Myotoxin II caused a dose-dependent cytolytic effect on all cell types tested, characterized by rapid release of cytoplasmic lactic dehydrogenase and drastic morphological cell alterations. Quantitative differences in the susceptibility to myotoxin II among cell types fell within a relatively narrow range, and in general, the toxin was cytolytic at concentrations of 50–100 μg/ml (3–7 μM), when assays were performed using culture medium as a diluent. Toxin activity was markedly enhanced if phosphate-buffered saline was utilized instead of medium. The cytotoxic activity of myotoxin III, an aspartate-49 isoform from the same venom, on both endothelial cells and skeletal muscle myoblasts was higher than that of myotoxin II, suggesting that, although phospholipase A2 activity is clearly not required for the induction of cell damage, it may have an enhancing role. In contrast to B. asper myotoxins, other basic phospholipases A2 with myotoxic activity in vivo (notexin from Notechis scutatus, and two enzymes isolated from Vipera russelli venom) did not affect endothelial cells and myoblasts. Pretreatment of cells with neuraminidase, tunicamycin, or protamine, did not alter their susceptibility to myotoxin II. At low temperatures (2–4°C) myotoxin II was devoid of cytolytic effect. Washing and neutralization experiments using heparin with low affinity for antithrombin or mouse monoclonal antibody MAb-3 suggest that at low temperatures myotoxin II binds very weakly to the cells, and that its normal interaction with the putative target is probably not only based on charge, but that a membrane penetration event may be required.es_ES
dc.description.sponsorshipSwedish Agency for Research Cooperation with Developing Countries//SAREC/Sueciaes_ES
dc.description.sponsorshipInternational Foundation for Science/[F/1388-2]/IFS/Sueciaes_ES
dc.language.isoen_USes_ES
dc.sourceToxicon 32(11), 1359-1369. 1994es_ES
dc.subjectvenomes_ES
dc.subjectmyotoxines_ES
dc.subjectSnake venomes_ES
dc.titleBroad cytolytic specificity of myotoxin II, a lysine-49 phospholipase A2 of Bothrops asper snake venomes_ES
dc.typeinfo:eu-repo/semantics/articlees_ES
dc.identifier.doi10.1016/0041-0101(94)90408-1
dc.description.procedenceUCR::Investigación::Unidades de Investigación::Ciencias de la Salud::Instituto Clodomiro Picado (ICP)es_ES
dc.identifier.pmid7886694


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