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dc.contributor.CRUESPUNIVERSIDADE DE ESTADUAL DE CAMPINASpt_BR
dc.typeArtigo de periódicopt_BR
dc.titleMembrane Protein Thiol Cross-linking Associated With The Permeabilization Of The Inner Mitochondrial Membrane By Ca2+ Plus Prooxidants.pt_BR
dc.contributor.authorFagian, M Mpt_BR
dc.contributor.authorPereira-da-Silva, Lpt_BR
dc.contributor.authorMartins, I Spt_BR
dc.contributor.authorVercesi, A Ept_BR
unicamp.authorM M Fagian, Departamento de Bioquimica, Instituto de Biologia, UNICAMP, Campinas S. P., Brazil.pt_BR
unicamp.author.externalL Pereira-da-Silva,pt
unicamp.author.externalI S Martins,pt
unicamp.author.externalA E Vercesi,pt
dc.subjectAnimalspt_BR
dc.subjectCalciumpt_BR
dc.subjectCattlept_BR
dc.subjectCell Membrane Permeabilitypt_BR
dc.subjectDiamidept_BR
dc.subjectDithiothreitolpt_BR
dc.subjectEgtazic Acidpt_BR
dc.subjectElectrophoresis, Polyacrylamide Gelpt_BR
dc.subjectIntracellular Membranespt_BR
dc.subjectMembrane Potentialspt_BR
dc.subjectMembrane Proteinspt_BR
dc.subjectMitochondriapt_BR
dc.subjectMitochondria, Heartpt_BR
dc.subjectMitochondria, Liverpt_BR
dc.subjectNadppt_BR
dc.subjectOxidation-reductionpt_BR
dc.subjectPeroxidespt_BR
dc.subjectRatspt_BR
dc.subjectSubmitochondrial Particlespt_BR
dc.subjectSuccinatespt_BR
dc.subjectSuccinic Acidpt_BR
dc.subjectSulfhydryl Compoundspt_BR
dc.subjectTert-butylhydroperoxidept_BR
dc.description.abstractIn a previous report (Macedo, D.V., Ferraz, V. L., Pereira-da-Silva, L., and Vercesi, A. E. (1988) in Integration of Mitochondrial Functions (Lemasters, J. J., et al., eds) pp. 535-542, Plenum Publishing Corp., New York), we proposed that the alterations in the inner mitochondrial membrane permeability caused by Ca2+ plus prooxidants could be the consequence of membrane protein sulfhydryl-disulfide transitions. In this study, we show that Ca2+ plus diamide, a thiol oxidant, significantly decrease the ability of beef heart submitochondrial particles to build up and sustain a membrane potential generated by succinate oxidation. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of solubilized membrane proteins indicates that these effects on the membrane potential are associated with the production of protein aggregates due to thiol cross-linking. Evidence is also presented that these protein aggregates can be produced in mitoplasts previously loaded with Ca2+ and that this is potentiated by the presence of either diamide or t-butylhydroperoxide. Furthermore, dithiothreitol, a disulfide reductant, was found to be much more effective than NAD(P)+ reductants in reversing Ca2+ efflux induced by prooxidants. It is concluded that the perturbation of the inner mitochondrial membrane caused by Ca2+ plus prooxidants is associated with protein polymerization due to thiol cross-linking, resulting in the production of high molecular mass protein aggregates.en
dc.relation.ispartofThe Journal Of Biological Chemistrypt_BR
dc.relation.ispartofabbreviationJ. Biol. Chem.pt_BR
dc.date.issued1990-Novpt_BR
dc.identifier.citationThe Journal Of Biological Chemistry. v. 265, n. 32, p. 19955-60, 1990-Nov.pt_BR
dc.language.isoengpt_BR
dc.description.volume265pt_BR
dc.description.firstpage19955-60pt_BR
dc.rightsfechadopt_BR
dc.rights.holderpt_BR
dc.sourcePubMedpt_BR
dc.identifier.issn0021-9258pt_BR
dc.identifier.doipt_BR
dc.identifier.urlhttp://www.ncbi.nlm.nih.gov/pubmed/2123195pt_BR
dc.date.available2015-11-27T12:18:15Z-
dc.date.accessioned2015-11-27T12:18:15Z-
dc.description.provenanceMade available in DSpace on 2015-11-27T12:18:15Z (GMT). No. of bitstreams: 1 pmed_2123195.pdf: 4375712 bytes, checksum: 14d1d03ed8fe9a89840f5a0e8274abf7 (MD5) Previous issue date: 1990en
dc.identifier.urihttp://repositorio.unicamp.br/jspui/handle/REPOSIP/193674-
dc.identifier.idPubmed2123195pt_BR
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