Umbelliferone induces changes in the structure and pharmacological activities of Bn IV, a phospholipase A(2) isoform isolated from Bothrops neuwiedi

Página do item simplificado
dc.contributor.authorToyama, Daniela de Oliveira
dc.contributor.authordos Santos Diz Filho, Eduardo Britto [UNESP]
dc.contributor.authorCavada, Benildo Sousa
dc.contributor.authorMatias da Rocha, Bruno Anderson
dc.contributor.authorBuzzo de Oliveira, Simone Cristina [UNESP]
dc.contributor.authorCotrim, Camila Aparecida [UNESP]
dc.contributor.authorGomes Soares, Veronica Cristina [UNESP]
dc.contributor.authorDelatorre, Plinio
dc.contributor.authorMarangoni, Sergio
dc.contributor.authorToyama, Marcos Hikari [UNESP]
dc.contributor.institutionUniversidade Estadual Paulista (Unesp)
dc.contributor.institutionUniv Presbiteriana Mackenzie
dc.contributor.institutionUniversidade Estadual de Campinas (UNICAMP)
dc.contributor.institutionUniversidade Federal do Ceará (UFC)
dc.contributor.institutionUniversidade Federal da Paraíba (UFPB)
dc.date.accessioned2014-05-20T13:12:23Z
dc.date.available2014-05-20T13:12:23Z
dc.date.issued2011-05-01
dc.description.abstractIn this paper was demonstrated that umbelliferone induces changes in structure and pharmacological activities of Bn IV, a lysine 49 secretory phospholipase A(2) (sPLA2) from Both tops neuwiedi. Incubation of Bn IV with umbelliferone virtually abolished platelet aggregation, edema, and myotoxicity induced by native Bn IV. The amino acid sequence of Bn IV showed high sequence similarities with other Lys49 sPLA2s from B. jararacussu (BthTx-I), B. pirajai (PrTx-I), and B. neuwiedi pauloensis (Bn SP6 and Bn SP7). This sPLA2 also has a highly conserved C-terminal amino acid sequence, which has been shown as important for the pharmacological activities of Lys49 sPLA2. Sequencing of Bn IV previously treated with umbelliferone revealed modification of S(1) and S(20). Fluorescent spectral analysis and circular dichroism (CD) studies showed that umbelliferone modified the secondary structure of this protein. Moreover, the pharmacological activity of Bn IV is driven by synergism of the C-terminal region with the a-helix motifs, which are involved in substrate binding of the Asp49 and Lys49 residues of 5PLA2 and have a direct effect on the Ca2+-independent membrane damage of some secretory snake venom PLA2. For Bn IV, these interactions are potentially important for triggering the pharmacological activity of this 5PLA2. (C) 2011 Elsevier Ltd. All rights reserved.en
dc.description.affiliationUNESP, Lab Quim Macromol, Unidade Sao Vicente, BR-11330900 Sao Vicente, SP, Brazil
dc.description.affiliationUniv Presbiteriana Mackenzie, Ctr Ciencias Biol & Saude, São Paulo, Brazil
dc.description.affiliationUniv Estadual Campinas, Dept Bioquim, Inst Biol, Campinas, SP, Brazil
dc.description.affiliationUniversidade Federal do Ceará (UFC), Dept Bioquim & Biol Mol, Fortaleza, Ceara, Brazil
dc.description.affiliationUniversidade Federal da Paraíba (UFPB), Dept Biol Mol, BR-58059900 Joao Pessoa, Paraiba, Brazil
dc.description.affiliationUnespUNESP, Lab Quim Macromol, Unidade Sao Vicente, BR-11330900 Sao Vicente, SP, 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: 06/55778-2
dc.description.sponsorshipIdFAPESP: 07/54714-3
dc.description.sponsorshipIdCNPq: 301665/2007-9
dc.format.extent851-860
dc.identifierhttp://dx.doi.org/10.1016/j.toxicon.2011.02.024
dc.identifier.citationToxicon. Oxford: Pergamon-Elsevier B.V. Ltd, v. 57, n. 6, p. 851-860, 2011.
dc.identifier.doi10.1016/j.toxicon.2011.02.024
dc.identifier.issn0041-0101
dc.identifier.lattes8573195327542061
dc.identifier.urihttp://hdl.handle.net/11449/355
dc.identifier.wosWOS:000290696900003
dc.language.isoeng
dc.publisherPergamon-Elsevier B.V. Ltd
dc.relation.ispartofToxicon
dc.relation.ispartofjcr2.352
dc.relation.ispartofsjr0,692
dc.rights.accessRightsAcesso restrito
dc.sourceWeb of Science
dc.subjectSecretory phospholipase A(2) (sPLA2)en
dc.subjectLys49 PLA2en
dc.subjectUmbelliferoneen
dc.subjectAnti-PLA2 activityen
dc.titleUmbelliferone induces changes in the structure and pharmacological activities of Bn IV, a phospholipase A(2) isoform isolated from Bothrops neuwiedien
dc.typeArtigo
dcterms.licensehttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dcterms.rightsHolderPergamon-Elsevier B.V. Ltd
unesp.author.lattes8573195327542061
unesp.campusUniversidade Estadual Paulista (Unesp), Instituto de Biociências, São Vicentept

Arquivos

Licença do Pacote
Agora exibindo 1 - 2 de 2
Nenhuma Miniatura disponível
Nome:
license.txt
Tamanho:
1.71 KB
Formato:
Item-specific license agreed upon to submission
Descrição:
Nenhuma Miniatura disponível
Nome:
license.txt
Tamanho:
1.71 KB
Formato:
Item-specific license agreed upon to submission
Descrição:

Coleções

Artigos - Ciências Biológicas - São Vicente