Kim Ki-Mo, Kim Peter K M, Kwon Young-Guen, Bai Se-Kyung, Nam Woo-Dong, Kim Young-Myeong
Vascular System Research Center, Kangwon National University, Chunchon, Kangwon-do, Korea.
J Biochem Mol Biol. 2002 Jan 31;35(1):127-33. doi: 10.5483/bmbrep.2002.35.1.127.
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.
亚硝化应激可预防或诱导细胞凋亡。它通过一氧化氮（NO）与蛋白质的生物硫醇相互作用导致的S-亚硝基化而发生。细胞氧化还原电位和非血红素铁含量决定S-亚硝基化。胱天蛋白酶家族蛋白酶催化位点中氧化还原敏感硫醇的S-亚硝基化可抑制细胞凋亡性死亡，这些蛋白酶在凋亡信号级联反应中起重要作用。亚硝化应激还可通过激活线粒体凋亡途径促进细胞凋亡，如细胞色素c、凋亡诱导因子和核酸内切酶G从线粒体释放，以及抑制NF-κB活性。在本文中，我们综述了S-亚硝基化和亚硝化应激调节凋亡信号级联反应的机制。
