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dc.contributor.authorXimenes, Valdecir Farias [UNESP]
dc.contributor.authorKanegae, Marilia P. P.
dc.contributor.authorRissato, Sandra Regina [UNESP]
dc.contributor.authorGalhiane, Mario Sergio [UNESP]
dc.date.accessioned2014-05-20T13:24:23Z
dc.date.available2014-05-20T13:24:23Z
dc.date.issued2007-01-15
dc.identifierhttp://dx.doi.org/10.1016/j.abb.2006.11.010
dc.identifier.citationArchives of Biochemistry and Biophysics. New York: Elsevier B.V., v. 457, n. 2, p. 134-141, 2007.
dc.identifier.issn0003-9861
dc.identifier.urihttp://hdl.handle.net/11449/7534
dc.description.abstractApocynin has been used as an efficient inhibitor of the NADPH oxidase complex and its mechanism of inhibition is linked to prior activation through the action of peroxidascs. Here we studied the oxidation of apocynin catalyzed by myeloperoxidase (MPO) and activated neutrophils. We found that apocynin is easily oxidized by MPO/H2O2 or activated neutrophils and has as products dimer and trimer derivatives. Since apocynin impedes the migration of the cytosolic component p47phox to the membrane and this effect could be related to its conjugation with essential thiol groups, we studied the reactivity of apocynin and its MPO-catalyzed oxidation products with glutathione (GSH). We found that apocynin and its oxidation products do not react with GSH. However, this thiol compound was efficiently oxidized by the apocynin radical during the MPO-catalyzed oxidation. We suggest that the reactivity of apocynin radical with thiol compounds could be involved in the inhibitory effect of this methoxy-catechol on NADPH oxidase complex. (c) 2006 Elsevier B.V. All rights reserved.en
dc.format.extent134-141
dc.language.isoeng
dc.publisherElsevier B.V.
dc.relation.ispartofArchives of Biochemistry and Biophysics
dc.sourceWeb of Science
dc.subjectapocyninpt
dc.subjectmyeloperoxidasept
dc.subjectNADPH oxidasept
dc.subjectrespiratory burstpt
dc.subjecthypochlorous acidpt
dc.subjectneutrophilpt
dc.titleThe oxidation of apocynin catalyzed by myeloperoxidase: Proposal for NADPH oxidase inhibitionen
dc.typeArtigo
dcterms.licensehttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dcterms.rightsHolderElsevier B.V.
dc.contributor.institutionUniversidade Estadual Paulista (Unesp)
dc.description.affiliationUniv Estadual Paulista, Fac Ciências, Dept Quim, Bauru, SP, Brazil
dc.description.affiliationUniv Estadual Paulista, Fac Ciências Farmaceut, Dept Anal Clin, Araraquara, SP, Brazil
dc.description.affiliationUnespUniv Estadual Paulista, Fac Ciências, Dept Quim, Bauru, SP, Brazil
dc.description.affiliationUnespUniv Estadual Paulista, Fac Ciências Farmaceut, Dept Anal Clin, Araraquara, SP, Brazil
dc.identifier.doi10.1016/j.abb.2006.11.010
dc.identifier.wosWOS:000243572800002
dc.rights.accessRightsAcesso restrito
unesp.campusUniversidade Estadual Paulista (Unesp), Faculdade de Ciências Farmacêuticas, Araraquarapt
unesp.campusUniversidade Estadual Paulista (Unesp), Faculdade de Ciências, Baurupt
dc.identifier.lattes4066413997908572
dc.identifier.lattes2611597065632795
dc.identifier.lattes3612277056838097
unesp.author.lattes4066413997908572
unesp.author.lattes2611597065632795
unesp.author.lattes3612277056838097
unesp.author.orcid0000-0003-2636-3080[1]
dc.relation.ispartofjcr3.118
dc.relation.ispartofsjr1,350
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