Antagonism of myotoxic and paralyzing activities of bothropstoxin-I by surarnin

dc.contributor.authorde Oliveira, M.
dc.contributor.authorCavalcante, WLG
dc.contributor.authorArruda, E. Z.
dc.contributor.authorMelo, P. A.
dc.contributor.authorSilva, MDP
dc.contributor.authorGallacci, M.
dc.contributor.institutionUniversidade Estadual Paulista (Unesp)
dc.contributor.institutionUniversidade Federal do Rio de Janeiro (UFRJ)
dc.date.accessioned2014-05-20T13:49:01Z
dc.date.available2014-05-20T13:49:01Z
dc.date.issued2003-09-15
dc.description.abstractPolyanionic substances are known to inhibit the myotoxic effects of some crotalide snake venoms. Bothropstoxin-I (BthTX-I), a basic Lys49 phospholipase (PLA(2)) homologue from Bothrops jararacussu venom, besides inducing muscle damage, also promotes the blockade of both directly and indirectly evoked contractions in mouse neuromuscular preparation. In this work, we evaluated the ability of suramin, a polysulfonated naphtylurea derivative, to antagonize the myotoxic and the paralyzing activities of BthTX-I on mice neuromuscular junction in vitro. Myotoxicity was assessed by light and electronic microscopic analysis of extensor digitorum longus (EDL) muscles; paralyzing activity was evaluated through the recording of both directly and indirectly evoked contractions of phrenic-diaphragm (PD) preparations. BthTX-I (1 muM) alone, or pre-incubated with suramin (10 muM) at 37degreesC for 15 min was added to the preparations for 120 min. BthTX-I induced histological alterations typical of myonecrosis in 14.6 +/- 1.0% of EDL muscle fibers. In addition, BthTX-I blocked 50% of both directly and indirectly evoked contractions in PD preparations in 72.1 +/- 9.1 and 21.1 +/- 2.0 min, respectively. Pre-incubation with suramin abolished both the muscle-damaging and muscle-paralyzing activities of BthTX-I. Since suramin is a polyanionic substance, we suggested that its effects result from the formation of inactive acid-base complexes with BthTX-I. (C) 2003 Elsevier Ltd. All rights reserved.en
dc.description.affiliationUniv Estadual Paulista, Inst Biociencias, Dept Farmacol, BR-18618000 Botucatu, SP, Brazil
dc.description.affiliationUniv Fed Rio de Janeiro, Dept Farmacol Bas & Clin, Rio de Janeiro, Brazil
dc.description.affiliationUniv Estadual Paulista, Inst Biociencias, Dept Morfol, Botucatu, SP, Brazil
dc.description.affiliationUnespUniv Estadual Paulista, Inst Biociencias, Dept Farmacol, BR-18618000 Botucatu, SP, Brazil
dc.description.affiliationUnespUniv Estadual Paulista, Inst Biociencias, Dept Morfol, Botucatu, SP, Brazil
dc.format.extent373-379
dc.identifierhttp://dx.doi.org/10.1016/S0041-0101(03)00166-1
dc.identifier.citationToxicon. Oxford: Pergamon-Elsevier B.V., v. 42, n. 4, p. 373-379, 2003.
dc.identifier.doi10.1016/S0041-0101(03)00166-1
dc.identifier.issn0041-0101
dc.identifier.lattes9353490382598257
dc.identifier.urihttp://hdl.handle.net/11449/17450
dc.identifier.wosWOS:000186083700005
dc.language.isoeng
dc.publisherElsevier B.V.
dc.relation.ispartofToxicon
dc.relation.ispartofjcr2.352
dc.relation.ispartofsjr0,692
dc.rights.accessRightsAcesso restrito
dc.sourceWeb of Science
dc.subjectbothropstoxin-Ipt
dc.subjectsuraminpt
dc.subjectmyonecrosispt
dc.subjectmuscle paralysispt
dc.titleAntagonism of myotoxic and paralyzing activities of bothropstoxin-I by surarninen
dc.typeArtigo
dcterms.licensehttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dcterms.rightsHolderElsevier B.V.
unesp.author.lattes9353490382598257
unesp.author.orcid0000-0002-2354-636X[2]
unesp.author.orcid0000-0001-6149-4030[6]
unesp.campusUniversidade Estadual Paulista (Unesp), Instituto de Biociências, Botucatupt

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