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 article

54 Citations (Scopus)

Abstract

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
Volume35
Issue number1
Publication statusPublished - 2002 Jan 31

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Sulfhydryl Compounds
Oxidation-Reduction
Apoptosis Inducing Factor
Apoptosis
Caspases
Cytochromes c
Catalytic Domain
Mitochondria
Nitric Oxide
Peptide Hydrolases
Cell Death
Iron
Cell death
Chemical activation
Proteins
endonuclease G

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology

Cite this

Kim, K. M., Kim, P. K. M., Kwon, Y. G., Bai, S. K., Nam, W. D., & Kim, Y. M. (2002). Regulation of apoptosis by nitrosative stress. Journal of Biochemistry and Molecular Biology, 35(1), 127-133.
Kim, Ki Mo ; Kim, Peter K.M. ; Kwon, Young Guen ; Bai, Se Kyung ; Nam, Woo Dong ; Kim, Young Myeong. / Regulation of apoptosis by nitrosative stress. In: Journal of Biochemistry and Molecular Biology. 2002 ; Vol. 35, No. 1. pp. 127-133.
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Kim, KM, Kim, PKM, Kwon, YG, Bai, SK, Nam, WD & Kim, YM 2002, 'Regulation of apoptosis by nitrosative stress', Journal of Biochemistry and Molecular Biology, vol. 35, no. 1, pp. 127-133.

Regulation of apoptosis by nitrosative stress. / Kim, Ki Mo; Kim, Peter K.M.; Kwon, Young Guen; Bai, Se Kyung; Nam, Woo Dong; Kim, Young Myeong.

In: Journal of Biochemistry and Molecular Biology, Vol. 35, No. 1, 31.01.2002, p. 127-133.

Research output: Contribution to journalReview article

TY - JOUR

T1 - Regulation of apoptosis by nitrosative stress

AU - Kim, Ki Mo

AU - Kim, Peter K.M.

AU - Kwon, Young Guen

AU - Bai, Se Kyung

AU - Nam, Woo Dong

AU - Kim, Young Myeong

PY - 2002/1/31

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N2 - 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.

AB - 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.

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Kim KM, Kim PKM, Kwon YG, Bai SK, Nam WD, Kim YM. Regulation of apoptosis by nitrosative stress. Journal of Biochemistry and Molecular Biology. 2002 Jan 31;35(1):127-133.