Please use this identifier to cite or link to this item: https://repositorio.unifesp.br/handle/11600/32087
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dc.contributor.authorTrevisan-Silva, Dilza
dc.contributor.authorGremski, Luiza H. [UNIFESP]
dc.contributor.authorChaim, Olga M.
dc.contributor.authorSilveira, Rafael B. da
dc.contributor.authorMeissner, Gabriel O.
dc.contributor.authorMangili, Oldemir C.
dc.contributor.authorBarbaro, Katia C.
dc.contributor.authorGremski, Waldemiro
dc.contributor.authorVeiga, Silvio S.
dc.contributor.authorSenff-Ribeiro, Andrea
dc.date.accessioned2016-01-24T13:59:05Z-
dc.date.available2016-01-24T13:59:05Z-
dc.date.issued2010-01-01
dc.identifierhttp://dx.doi.org/10.1016/j.biochi.2009.10.003
dc.identifier.citationBiochimie. Paris: Elsevier France-editions Scientifiques Medicales Elsevier, v. 92, n. 1, p. 21-32, 2010.
dc.identifier.issn0300-9084
dc.identifier.urihttp://repositorio.unifesp.br/handle/11600/32087-
dc.description.abstractBrown spiders have a worldwide distribution, and their venom has a complex composition containing many different molecules. Herein, we report the existence of a family of astacin-like metalloprotease toxins in Loxosceles intermedia venom, as well as in the venom of different species of Loxosceles. Using a cDNA library from the L. intermedia venom gland, we cloned two novel cDNAs encoding astacin-like metalloprotease toxins, LALP2 and LALP3. Using an anti-serum against the previously described astacin-like toxin in L. intermedia venom (LALP1), we detected the presence of immunologically-related toxins in the venoms of L. intermedia, Loxosceles laeta, and Loxosceles gaucho. Zymographic experiments showed gelatinolytic activity of crude venoms of L. intermedia, L. laeta, and L. gaucho (which could be inhibited by the divalent metal chelator 1,10-phenanthroline) at electrophoretic mobilities identical to those reported for immunological cross-reactivity. Moreover, mRNAs extracted from L. laeta and L. gaucho venom glands were screened for astacin-like metalloproteases, and cDNAs obtained using LALP1-specific primers were sequenced, and their deduced amino acid sequences confirmed they were members of the astacin family with the family signatures (HEXXHXXGXXHE and MXY), LALP4 and LALP5, respectively. Sequence comparison of deduced amino acid sequences revealed that LALP2, LALP3, LALP4, and LALP5 are related to the astacin family. This study identified the existence of gene family of astacin-like toxins in the venoms of brown spiders and raises the possibility that these molecules are involved in the deleterious effects triggered by the venom. (C) 2009 Elsevier Masson SAS. All rights reserved.en
dc.description.sponsorshipSecretaria de Estado de Ciencia
dc.description.sponsorshipTecnologia e Ensino Superior (SETI) do Parana
dc.description.sponsorshipFundacao Araucaria-PR
dc.description.sponsorshipConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.description.sponsorshipFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.description.sponsorshipCoordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)
dc.format.extent21-32
dc.language.isoeng
dc.publisherElsevier B.V.
dc.relation.ispartofBiochimie
dc.rightsAcesso restrito
dc.subjectAstacin familyen
dc.subjectVenomen
dc.subjectLoxoscelesen
dc.subjectMetalloproteasesen
dc.titleAstacin-like metalloproteases are a gene family of toxins present in the venom of different species of the brown spider (genus Loxosceles)en
dc.typeArtigo
dc.rights.licensehttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dc.contributor.institutionUniv Fed Parana
dc.contributor.institutionUniversidade Federal de São Paulo (UNIFESP)
dc.contributor.institutionState Univ Ponta Grosso
dc.contributor.institutionButantan Inst
dc.contributor.institutionCatholic Univ Parana
dc.description.affiliationUniv Fed Parana, Dept Cell Biol, BR-81531990 Curitiba, Parana, Brazil
dc.description.affiliationUniversidade Federal de São Paulo, Dept Biochem, São Paulo, Brazil
dc.description.affiliationState Univ Ponta Grosso, Dept Struct Mol Biol & Genet, Ponta Grossa, Parana, Brazil
dc.description.affiliationUniv Fed Parana, Dept Physiol, BR-81531990 Curitiba, Parana, Brazil
dc.description.affiliationButantan Inst, Immunopathol Lab, São Paulo, Brazil
dc.description.affiliationCatholic Univ Parana, Hlth & Biol Sci Inst, Curitiba, Parana, Brazil
dc.description.affiliationUnifespUniversidade Federal de São Paulo, Dept Biochem, São Paulo, Brazil
dc.identifier.doi10.1016/j.biochi.2009.10.003
dc.description.sourceWeb of Science
dc.identifier.wosWOS:000273944900003
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