Membrane Protein Thiol Cross-linking Associated With The Permeabilization Of The Inner Mitochondrial Membrane By Ca2+ Plus Prooxidants.

dc.creatorFagian, M M
dc.creatorPereira-da-Silva, L
dc.creatorMartins, I S
dc.creatorVercesi, A E
dc.date1990-Nov
dc.date2015-11-27T12:18:15Z
dc.date2015-11-27T12:18:15Z
dc.date.accessioned2018-03-29T00:50:51Z
dc.date.available2018-03-29T00:50:51Z
dc.identifierThe Journal Of Biological Chemistry. v. 265, n. 32, p. 19955-60, 1990-Nov.
dc.identifier0021-9258
dc.identifier
dc.identifierhttp://www.ncbi.nlm.nih.gov/pubmed/2123195
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/193674
dc.identifier2123195
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1293907
dc.descriptionIn 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.
dc.description265
dc.description19955-60
dc.languageeng
dc.relationThe Journal Of Biological Chemistry
dc.relationJ. Biol. Chem.
dc.rightsfechado
dc.rights
dc.sourcePubMed
dc.subjectAnimals
dc.subjectCalcium
dc.subjectCattle
dc.subjectCell Membrane Permeability
dc.subjectDiamide
dc.subjectDithiothreitol
dc.subjectEgtazic Acid
dc.subjectElectrophoresis, Polyacrylamide Gel
dc.subjectIntracellular Membranes
dc.subjectMembrane Potentials
dc.subjectMembrane Proteins
dc.subjectMitochondria
dc.subjectMitochondria, Heart
dc.subjectMitochondria, Liver
dc.subjectNadp
dc.subjectOxidation-reduction
dc.subjectPeroxides
dc.subjectRats
dc.subjectSubmitochondrial Particles
dc.subjectSuccinates
dc.subjectSuccinic Acid
dc.subjectSulfhydryl Compounds
dc.subjectTert-butylhydroperoxide
dc.titleMembrane Protein Thiol Cross-linking Associated With The Permeabilization Of The Inner Mitochondrial Membrane By Ca2+ Plus Prooxidants.
dc.typeArtículos de revistas


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