dc.creatorZago, E B
dc.creatorCastilho, R F
dc.creatorVercesi, A E
dc.date2000-Jul
dc.date2015-11-27T12:22:37Z
dc.date2015-11-27T12:22:37Z
dc.date.accessioned2018-03-29T00:54:16Z
dc.date.available2018-03-29T00:54:16Z
dc.identifierFebs Letters. v. 478, n. 1-2, p. 29-33, 2000-Jul.
dc.identifier0014-5793
dc.identifier
dc.identifierhttp://www.ncbi.nlm.nih.gov/pubmed/10922464
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/194559
dc.identifier10922464
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1294792
dc.descriptionAcetoacetate, an NADH oxidant, stimulated the ruthenium red-insensitive rat liver mitochondrial Ca(2+) efflux without significant release of state-4 respiration, disruption of membrane potential (Deltapsi) or mitochondrial swelling. This process is compatible with the opening of the currently designated low conductance state of the permeability transition pore (PTP) and, under our experimental conditions, was associated with a partial oxidation of the mitochondrial pyridine nucleotides. In contrast, diamide, a thiol oxidant, induced a fast mitochondrial Ca(2+) efflux associated with a release of state-4 respiration, a disruption of Deltapsi and a large amplitude mitochondrial swelling. This is compatible with the opening of the high conductance state of the PTP and was associated with extensive oxidation of pyridine nucleotides. Interestingly, the addition of carbonyl cyanide p-(trifluoromethoxy)phenylhydrazone to the acetoacetate experiment promoted a fast shift from the low to the high conductance state of the PTP. Both acetoacetate and diamide-induced mitochondrial permeabilization were inhibited by exogenous catalase. We propose that the shift from a low to a high conductance state of the PTP can be promoted by the oxidation of NADPH. This impairs the antioxidant function of the glutathione reductase/peroxidase system, strongly strengthening the state of mitochondrial oxidative stress.
dc.description478
dc.description29-33
dc.languageeng
dc.relationFebs Letters
dc.relationFEBS Lett.
dc.rightsfechado
dc.rights
dc.sourcePubMed
dc.subjectAcetoacetates
dc.subjectAnimals
dc.subjectCalcium
dc.subjectCarbonyl Cyanide P-trifluoromethoxyphenylhydrazone
dc.subjectCell Respiration
dc.subjectDiamide
dc.subjectElectric Conductivity
dc.subjectFemale
dc.subjectIntracellular Membranes
dc.subjectIon Channels
dc.subjectMembrane Potentials
dc.subjectMembrane Proteins
dc.subjectMitochondria, Liver
dc.subjectMitochondrial Membrane Transport Proteins
dc.subjectMitochondrial Swelling
dc.subjectNad
dc.subjectNadp
dc.subjectOxidants
dc.subjectOxidation-reduction
dc.subjectOxidative Stress
dc.subjectPermeability
dc.subjectRats
dc.subjectRats, Wistar
dc.subjectReactive Oxygen Species
dc.subjectSubstrate Specificity
dc.subjectSulfhydryl Reagents
dc.subjectUncoupling Agents
dc.titleThe Redox State Of Endogenous Pyridine Nucleotides Can Determine Both The Degree Of Mitochondrial Oxidative Stress And The Solute Selectivity Of The Permeability Transition Pore.
dc.typeArtículos de revistas


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