Regulation of apoptosis by nitrosative stress

Ki Mo Kim, Peter K.M. Kim, Young Guen Kwon, Se Kyung Bai, Woo Dong Nam, Young Myeong Kim

Research output: Contribution to journalReview articlepeer-review

62 Citations (Scopus)


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-κB activity. In this article we reviewed the mechanisms whereby S-nitrosylation and nitrosative stress regulate the apoptotic signal cascade.

Original languageEnglish
Pages (from-to)127-133
Number of pages7
JournalJournal of biochemistry and molecular biology
Issue number1
Publication statusPublished - 2002 Jan 31

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology


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