Regulation of apoptosis by nitrosative stress.

†‡ † § , || †,#, * † ‡ § || # Nitrosative 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 Snitrosylation. Apoptotic cell death is inhibited by Snitrosylation 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-κB activity. In this article we reviewed the mechanisms whereby Snitrosylation and nitrosative stress regulate the apoptotic signal cascade.