A Catalytically Inactive Lys49 PLA2 Isoform from Bothrops jararacussu venom that Stimulates Insulin Secretion in Pancreatic Beta Cells

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dc.contributor.authorFagundes, Fabio H. R. [UNESP]
dc.contributor.authorAparicio, Ricardo
dc.contributor.authordos Santos, Marcelo L.
dc.contributor.authorDiz Filho, Eduardo B. S. [UNESP]
dc.contributor.authorOliveira, Simone C. B. [UNESP]
dc.contributor.authorToyama, Daniela O.
dc.contributor.authorToyama, Marcos H. [UNESP]
dc.contributor.institutionUniversidade Estadual de Campinas (UNICAMP)
dc.contributor.institutionUniv Mackenzie SP
dc.contributor.institutionUniversidade Estadual Paulista (Unesp)
dc.date.accessioned2014-05-20T13:12:23Z
dc.date.available2014-05-20T13:12:23Z
dc.date.issued2011-11-01
dc.description.abstractA new secretory phospholipase A2 (sPLA2) isoform from Bothrops jararacussu venom (BjVIII) has been characterized by causing platelet aggregation, an absent activity in BthTx-I, Prtx-I and PrTx-II sPLA2s. According to our results, BjVIII also enhances insulin release by the pancreatic beta cells. The complete amino acid sequence of the new isoform was determined by Edman degradation and de novo peptide sequencing. These analyses showed a G35K amino acid modification for BjVIII in comparison with BthTx-I, PrTx-I and Prtx-II, a structural difference that has been related to the conflicting biological activities among BjVIII and other Lys49 sPLA2s. The whole set of evidences collected in this work indicates that, besides the C-terminal region and B-wing of PLA2, the calcium binding loop in BjVIII should be considered as an important region, involved in the pharmacological effects of Lys49-sPLA2 isoforms from the Bothrops genus.en
dc.description.affiliationUNICAMP SP, Inst Quim, Campinas, SP, Brazil
dc.description.affiliationUniv Mackenzie SP, Ctr Ciencias Biol & Saude, São Paulo, Brazil
dc.description.affiliationUNESP, Sao Vicente, Brazil
dc.description.affiliationUNICAMP SP, IB, Dept Bioquim, Campinas, SP, Brazil
dc.description.affiliationUnespUNESP, Sao Vicente, Brazil
dc.description.sponsorshipCoordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)
dc.description.sponsorshipFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.description.sponsorshipConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.description.sponsorshipIdFAPESP: 07/54714-3
dc.description.sponsorshipIdCNPq: 301665/2007-9
dc.format.extent1133-1139
dc.identifierhttp://eurekaselect.com/88802/article
dc.identifier.citationProtein and Peptide Letters. Sharjah: Bentham Science Publ Ltd, v. 18, n. 11, p. 1133-1139, 2011.
dc.identifier.issn0929-8665
dc.identifier.urihttp://hdl.handle.net/11449/368
dc.identifier.wosWOS:000298538600010
dc.language.isoeng
dc.publisherBentham Science Publ Ltd
dc.relation.ispartofProtein and Peptide Letters
dc.relation.ispartofjcr1.039
dc.relation.ispartofsjr0,429
dc.rights.accessRightsAcesso restrito
dc.sourceWeb of Science
dc.subjectBothrops jararacussuen
dc.subjectedman degradationen
dc.subjectinsulin secretionen
dc.subjectmass spectraen
dc.subjectpancreatic beta cellsen
dc.subjectPLA2en
dc.subjectplatelet aggregationen
dc.titleA Catalytically Inactive Lys49 PLA2 Isoform from Bothrops jararacussu venom that Stimulates Insulin Secretion in Pancreatic Beta Cellsen
dc.typeArtigo
dcterms.licensehttp://www.benthamscience.com/permission.php
dcterms.rightsHolderBentham Science Publ Ltd
unesp.campusUniversidade Estadual Paulista (Unesp), Instituto de Biociências, São Vicentept

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Artigos - Ciências Biológicas - São Vicente