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 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.
Kim
Ki-Mo
KM
Vascular System Research Center, Kangwon National University, Chunchon, Kangwon-do, Korea.
Kim
Peter K M
PK
Kwon
Young-Guen
YG
Bai
Se-Kyung
SK
Nam
Woo-Dong
WD
Kim
Young-Myeong
YM
D000818:Animals; D017209:Apoptosis; D061945:Caspase Inhibitors; D016923:Cell Death; D006418:Heme / Q000737:chemistry; D006801:Humans; D007501:Iron / Q000378:metabolism; D008928:Mitochondria / Q000378:metabolism; D009569:Nitric Oxide / Q000378:metabolism*; D009584:Nitrogen / Q000378:metabolism*; D010084:Oxidation-Reduction; D015398:Signal Transduction; D013438:Sulfhydryl Compounds / Q000737:chemistry
D061945:Caspase Inhibitors; D013438:Sulfhydryl Compounds; D009569:Nitric Oxide; D006418:Heme; D007501:Iron; D009584:Nitrogen