Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/194492
Type: Artigo de periódico
Title: Inhibition Of Mitochondrial Permeability Transition By Low Ph Is Associated With Less Extensive Membrane Protein Thiol Oxidation.
Author: Teixeira, B M
Kowaltowski, A J
Castilho, R F
Vercesi, A E
Abstract: Ca2+ and inorganic phosphate-induced mitochondrial swelling and membrane protein thiol oxidation, which are associated with mitochondrial permeability transition, are inhibited by progressively decreasing the incubation medium pH between 7.2 and 6.0. Nevertheless, the detection of mitochondrial H2O2 production under these conditions is increased. Permeability transition induced by phenylarsine oxide, which promotes membrane protein thiol cross-linkage in a process independent of Ca2+ or reactive oxygen species, is also strongly inhibited in acidic incubation media. In addition, we observed that the decreased protein thiol reactivity with phenylarsine oxide or phenylarsine oxide-induced swelling at pH 6.0 is reversed by diethyl pyrocarbonate, in a hydroxylamine-sensitive manner. These results provide evidence that the inhibition of mitrochondrial permeability transition observed at lower incubation medium pH is mediated by a decrease in membrane protein thiol reactivity, related to the protonation of protein histidyl residues.
Subject: Animals
Antimycin A
Arsenicals
Calcimycin
Calcium
Carbonyl Cyanide P-trifluoromethoxyphenylhydrazone
Diethyl Pyrocarbonate
Hydrogen-ion Concentration
Hydroxylamine
Intracellular Membranes
Ionophores
Membrane Proteins
Mitochondria, Liver
Oxidation-reduction
Permeability
Rats
Rats, Wistar
Serum Albumin, Bovine
Sulfhydryl Compounds
Rights: aberto
Identifier DOI: 
Address: http://www.ncbi.nlm.nih.gov/pubmed/10841269
Date Issue: 1999
Appears in Collections:Artigos e Materiais de Revistas Científicas - Unicamp

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