The Thiol-specific Antioxidant Enzyme Prevents Mitochondrial Permeability Transition

作者: Alicia J. Kowaltowski , Luis E. S. Netto , Anibal E. Vercesi

DOI: 10.1074/JBC.273.21.12766

关键词:

摘要: Mitochondrial swelling and membrane protein thiol oxidation associated with mitochondrial permeability transition induced by Ca2+ inorganic phosphate are inhibited in a dose-dependent manner either catalase, the thiol-specific antioxidant enzyme (TSA), recently demonstrated to present peroxidase activity, or ebselen, selenium-containing heterocycle which also possesses activity. This inhibition of is due removal mitochondrial-generated H2O2 can easily diffuse extramitochondrial space. Whereas ebselen required presence reduced glutathione as reductant grant its protective effect, TSA was fully components. Decrease oxygen concentration reaction medium inhibits permeabilization oxidation, concentration-dependent manner. The results presented this report confirm that reactive species-dependent. possible importance an intracellular antioxidant, avoiding onset transition, discussed text.

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