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dc.typeArtigo de periódicopt_BR
dc.titleMitochondria Generated Nitric Oxide Protects Against Permeability Transition Via Formation Of Membrane Protein S-nitrosothiols.pt_BR
dc.contributor.authorLeite, Ana Catarina Rpt_BR
dc.contributor.authorOliveira, Helena C Fpt_BR
dc.contributor.authorUtino, Fabiane Lpt_BR
dc.contributor.authorGarcia, Rafaelpt_BR
dc.contributor.authorAlberici, Luciane Cpt_BR
dc.contributor.authorFernandes, Mariana Ppt_BR
dc.contributor.authorCastilho, Roger Fpt_BR
dc.contributor.authorVercesi, Aníbal Ept_BR
unicamp.authorAna Catarina R Leite, Departamento de Fisiologia e Biofísica, Universidade Estadual de Campinas, UNICAMP, Campinas, SP, Brazil.pt_BR C F Oliveira,pt L Utino,pt Garcia,pt C Alberici,pt P Fernandes,pt F Castilho,ptíbal E Vercesi,pt
dc.subjectEnzyme Inhibitorspt_BR
dc.subjectIn Vitro Techniquespt_BR
dc.subjectMembrane Potential, Mitochondrialpt_BR
dc.subjectMitochondria, Liverpt_BR
dc.subjectMitochondrial Membrane Transport Proteinspt_BR
dc.subjectMitochondrial Swellingpt_BR
dc.subjectNg-nitroarginine Methyl Esterpt_BR
dc.subjectNitric Oxidept_BR
dc.subjectNitric Oxide Donorspt_BR
dc.subjectNitric Oxide Synthasept_BR
dc.subjectRats, Wistarpt_BR
dc.description.abstractMitochondria generated nitric oxide (NO) regulates several cell functions including energy metabolism, cell cycling, and cell death. Here we report that the NO synthase inhibitors (L-NAME, L-NNA and L-NMMA) administered either in vitro or in vivo induce Ca2+-dependent mitochondrial permeability transition (MPT) in rat liver mitochondria via a mechanism independent on changes in the energy state of the organelle. MPT was determined by the occurrence of cyclosporin A sensitive mitochondrial membrane potential disruption followed by mitochondrial swelling and Ca2+ release. In in vitro experiments, the effect of NOS inhibitors was dose-dependent (1 to 50 microM). In addition to cyclosporin A, L-NAME-induced MPT was sensitive to Mg2+ plus ATP, EGTA, and to a lower degree, to catalase and dithiothreitol. In contrast to L-NAME, its isomer D-NAME did not induce MPT. L-NAME-induced MPT was associated with a significant decrease in both the rate of NO generation and the content of mitochondrial S-nitrosothiol. Acute and chronic in vivo treatment with L-NAME also promoted MPT and decreased the content of mitochondrial S-nitrosothiol. SNAP (a NO donor) prevented L-NAME mediated MPT and reversed the decrease in the rate of NO generation and in the content of S-nitrosothiol. We propose that S-nitrosylation of critical membrane protein thiols by NO protects against MPT.en
dc.relation.ispartofBiochimica Et Biophysica Actapt_BR
dc.relation.ispartofabbreviationBiochim. Biophys. Actapt_BR
dc.identifier.citationBiochimica Et Biophysica Acta. v. 1797, n. 6-7, p. 1210-6pt_BR
dc.rights.holderCopyright © 2010 Elsevier B.V. All rights reserved.pt_BR
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