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. 2010 Jun-Jul;1797(6-7):1210-6.
doi: 10.1016/j.bbabio.2010.01.034. Epub 2010 Feb 4.

Mitochondria generated nitric oxide protects against permeability transition via formation of membrane protein S-nitrosothiols

Ana Catarina R Leite  1 , Helena C F Oliveira, Fabiane L Utino, Rafael Garcia, Luciane C Alberici, Mariana P Fernandes, Roger F Castilho, Aníbal E Vercesi
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Mitochondria generated nitric oxide protects against permeability transition via formation of membrane protein S-nitrosothiols

Ana Catarina R Leite et al. Biochim Biophys Acta. 2010 Jun-Jul.
Free article

Abstract

Mitochondria 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.

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