Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/199644
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dc.contributor.CRUESPUNIVERSIDADE DE ESTADUAL DE CAMPINASpt_BR
dc.typeArtigo de periódicopt_BR
dc.titleReactive Oxygen Species And Permeability Transition Pore In Rat Liver And Kidney Mitoplasts.pt_BR
dc.contributor.authorRonchi, Juliana Apt_BR
dc.contributor.authorVercesi, Anibal Ept_BR
dc.contributor.authorCastilho, Roger Fpt_BR
unicamp.authorJuliana A Ronchi, Departamento de Patologia Clínica, Faculdade de Ciências Médicas, Universidade Estadual de Campinas (UNICAMP), 13083-887, Campinas, SP, Brazil.pt_BR
unicamp.author.externalAnibal E Vercesi,pt
unicamp.author.externalRoger F Castilho,pt
dc.subjectAdenosine Diphosphatept_BR
dc.subjectAnimalspt_BR
dc.subjectCatalasept_BR
dc.subjectChelating Agentspt_BR
dc.subjectCyclosporinept_BR
dc.subjectEgtazic Acidpt_BR
dc.subjectEnzyme Inhibitorspt_BR
dc.subjectFemalept_BR
dc.subjectHydrogen Peroxidept_BR
dc.subjectKidneypt_BR
dc.subjectLiverpt_BR
dc.subjectMitochondria, Liverpt_BR
dc.subjectMitochondrial Membrane Transport Proteinspt_BR
dc.subjectOrgan Specificitypt_BR
dc.subjectOxidation-reductionpt_BR
dc.subjectRatspt_BR
dc.subjectRats, Wistarpt_BR
dc.subjectTert-butylhydroperoxidept_BR
dc.description.abstractMitochondrial permeability transition is typically characterized by Ca(2+) and oxidative stress-induced opening of a nonselective proteinaceous membrane pore sensitive to cyclosporin A, known as the permeability transition pore (PTP). Data from our laboratory provide evidence that the PTP is formed when inner membrane proteins aggregate as a result of disulfide cross-linking caused by thiol oxidation. Here we compared the redox properties between PTP in intact mitochondria and mitoplasts. The rat liver mitoplasts retained less than 5% and 10% of the original outer membrane markers monoamine oxidase and VDAC, respectively. Kidney mitoplasts also showed a partial depletion of hexokinase. In line with the redox nature of the PTP, mitoplasts that were more susceptible to PTP opening than intact mitochondria showed higher rates of H(2)O(2) generation and decreased matrix NADPH-dependent antioxidant activity. Mitoplast PTP was also sensitive to the permeability transition inducer tert-butyl hydroperoxide and to the inhibitors cyclosporin A, EGTA, ADP, dithiothreitol and catalase. Taken together, these data indicate that, in mitoplasts, PTP exhibits redox regulatory characteristics similar to those described for intact mitochondria.en
dc.relation.ispartofJournal Of Bioenergetics And Biomembranespt_BR
dc.relation.ispartofabbreviationJ. Bioenerg. Biomembr.pt_BR
dc.date.issued2011-Decpt_BR
dc.identifier.citationJournal Of Bioenergetics And Biomembranes. v. 43, n. 6, p. 709-15, 2011-Dec.pt_BR
dc.language.isoengpt_BR
dc.description.volume43pt_BR
dc.description.firstpage709-15pt_BR
dc.rightsfechadopt_BR
dc.sourcePubMedpt_BR
dc.identifier.issn1573-6881pt_BR
dc.identifier.doi10.1007/s10863-011-9384-1pt_BR
dc.identifier.urlhttp://www.ncbi.nlm.nih.gov/pubmed/21964737pt_BR
dc.date.available2015-11-27T13:21:55Z-
dc.date.accessioned2015-11-27T13:21:55Z-
dc.description.provenanceMade available in DSpace on 2015-11-27T13:21:55Z (GMT). No. of bitstreams: 1 pmed_21964737.pdf: 280197 bytes, checksum: 2a915521af5ad7e92503bf767f758ff0 (MD5) Previous issue date: 2011en
dc.identifier.urihttp://repositorio.unicamp.br/jspui/handle/REPOSIP/199644-
dc.identifier.idPubmed21964737pt_BR
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