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lüll Regulation of apoptosis by nitrosative stress Kim KM; Kim PK; Kwon YG; Bai SK; Nam WD; Kim YMJ Biochem Mol Biol 2002[Jan]; 35 (1): 127-33Nitrosative stress can prevent or induce apoptosis. It occurs via S-nitrosylation by the interaction of nitric oxide (NO) with the biological thiols of proteins. Cellular redox potential and non-heme iron content determine S-nitrosylation. Apoptotic cell death is inhibited by S-nitrosylation of the redox-sensitive thiol in the catalytic site of caspase family proteases, which play an essential role in the apoptotic signal cascade. Nitrosative stress can also promote apoptosis by the activation of mitochondrial apoptotic pathways, such as the release of cytochrome c, an apoptosis-inducing factor, and endonuclease G from mitochondria, as well as the suppression of NF-kB activity. In this article we reviewed the mechanisms whereby S-nitrosylation and nitrosative stress regulate the apoptotic signal cascade.|*Apoptosis[MESH]|Animals[MESH]|Caspase Inhibitors[MESH]|Cell Death[MESH]|Heme/chemistry[MESH]|Humans[MESH]|Iron/metabolism[MESH]|Mitochondria/metabolism[MESH]|Nitric Oxide/*metabolism[MESH]|Nitrogen/*metabolism[MESH]|Oxidation-Reduction[MESH]|Signal Transduction[MESH]|Sulfhydryl Compounds/chemistry[MESH] |