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

dc.creatorToyama, DD
dc.creatorDiz, EBD
dc.creatorCavada, BS
dc.creatorda Rocha, BAM
dc.creatorde Oliveira, SCB
dc.creatorCotrim, CA
dc.creatorSoares, VCG
dc.creatorDelatorre, P
dc.creatorMarangoni, S
dc.creatorToyama, MH
dc.date2011
dc.dateMAY
dc.date2014-07-30T19:27:49Z
dc.date2015-11-26T17:50:59Z
dc.date2014-07-30T19:27:49Z
dc.date2015-11-26T17:50:59Z
dc.date.accessioned2018-03-29T00:34:20Z
dc.date.available2018-03-29T00:34:20Z
dc.identifierToxicon. Pergamon-elsevier Science Ltd, v. 57, n. 6, n. 851, n. 860, 2011.
dc.identifier0041-0101
dc.identifierWOS:000290696900003
dc.identifier10.1016/j.toxicon.2011.02.024
dc.identifierhttp://www.repositorio.unicamp.br/jspui/handle/REPOSIP/73359
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/73359
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1289855
dc.descriptionCoordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)
dc.descriptionFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.descriptionConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.descriptionIn 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.
dc.description57
dc.description6
dc.description851
dc.description860
dc.descriptionCoordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)
dc.descriptionFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.descriptionConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.descriptionCoordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)
dc.descriptionFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.descriptionConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.descriptionFAPESP [06/55778-2, 07/54714-3]
dc.descriptionCNPq [301665/2007-9]
dc.languageen
dc.publisherPergamon-elsevier Science Ltd
dc.publisherOxford
dc.publisherInglaterra
dc.relationToxicon
dc.relationToxicon
dc.rightsfechado
dc.rightshttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dc.sourceWeb of Science
dc.subjectSecretory phospholipase A(2) (sPLA2)
dc.subjectLys49 PLA2
dc.subjectUmbelliferone
dc.subjectAnti-PLA2 activity
dc.subjectAmino-acid-sequence
dc.subjectDurissus-collilineatus Venom
dc.subjectPirajai Snake-venom
dc.subjectPlatelet-aggregation
dc.subjectPiratoxin-i
dc.subjectActivation
dc.subjectMechanisms
dc.subjectInhibition
dc.subjectFlavonoids
dc.subjectPhosphorylation
dc.titleUmbelliferone induces changes in the structure and pharmacological activities of Bn IV, a phospholipase A(2) isoform isolated from Bothrops neuwiedi
dc.typeArtículos de revistas


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