Cited by 245Cell death mechanisms and regulationNitric Oxide and Endothelin EffectsCardiac Ischemia and Reperfusion

Nitric Oxide Suppression of Apoptosis Occurs in Association with an Inhibition of Bcl-2 Cleavage and Cytochrome cRelease

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Kim, Young-Myeong, Kim, Tae-Hyoung, Seol, Dai-Wu, Talanian, Robert V., Billiar, Timothy R.·1998·Journal of Biological Chemistry

Abstract

It is now known that caspase-3-like protease activation can promote Bcl-2 cleavage and mitochondrial cytochrome c release and that these events can lead to further downstream caspase activation. NO has been proposed as a potent, endogenous inhibitor of caspase-3-like protease activity. Experiments were carried out to determine whether NO could interrupt Bcl-2 cleavage or cytochrome c release by the inhibition of caspase activity linking these events. NO inhibited the capacity of purified caspase-3 to cleave recombinant Bcl-2. Both Bcl-2 cleavage and cytochrome c release were inhibited in tumor necrosis factor alpha- and actinomycin D-treated MCF-7 cells exposed to NO donors. The NO-mediated inhibition of Bcl-2 cleavage and cytochrome c release occurred in association with an inhibition of apoptosis and caspase-3-like activation. Thus, NO suppresses a key step in the positive feedback amplification of apoptotic signaling by preventing Bcl-2 cleavage and cytochrome c release.

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Crossref · 10.1074/jbc.273.47.31437

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  • NO inhibits cytochrome c oxidase, decreases mitochondrial ROS formation, and limits apoptotic cytochrome c release.

    “NO is a well-characterized regulator of mitochondrial function that inhibits cytochrome c oxidase, decreases mitochondrial ROS formation, and limits apoptotic cytochrome c release [32–36].”

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Research works printed but not linked: 4

  1. Jurgensmeier, J. M., Xie, Z., Deveraux, Q., Ellerby, L., Bredesen, D., and Reed, J. C. (1998) Proc. Natl. Acad. Sci. U. S. A. 95, 4997-5002
  2. Schlesinger, P. H., Gross, A., Yin, X. M., Yamamoto, K., Saito, M., Waksman, G., and Korsmeyer, S. J. (1997) Proc. Natl. Acad. Sci. U. S. A. 94, 11357-11362
  3. Schendel, S. L., Xie, Z., Montal, M. O., Matsuyama, S., Montal, M., and Reed, J. C. (1997) Proc. Natl. Acad. Sci. U. S. A. 94, 5113-5118
  4. Clem, R. J., Cheng, E. H., Karp, C. L., Kirsch, D. G., Ueno, K., Takahashi, A., Kastan, M. B., Griffin, D. E., Earnshaw, W. C., Veliuona, M. A., and Hardwick, J. M. (1998) Proc. Natl. Acad. Sci. U. S. A. 95, 554 -559

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Authors
Kim, Y.-M., Kim, T.-H., Seol, D.-W., Talanian, R. V., & Billiar, T. R.
Affiliations
  • Kangwon National University (KR)
  • University of Pittsburgh (US)
Corresponding author
Billiar, Timothy R.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
1998-11
Volume
273
Issue
47
Pages
31437-31441
ISSN
0021-9258 (ISSN-L)
OpenAlex
W2077925191
Cited by
245
References
36
Citations by year
2024: 3 · 2023: 3 · 2022: 2 · 2021: 4 · 2020: 1 · 2019: 3 · 2017: 5 · 2016: 2 · 2015: 3 · 2014: 1 · 2013: 7 · 2012: 7
FWCI
8.04
Type
journal article
Language
en
Open access
Locations
  • Journal of Biological Chemistry (publishedVersion, cc-by)
  • PubMed (publishedVersion)
Funders
National Institute of General Medical Sciences (R01GM044100, R01 GM 44100)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
  • Health Sciences › Medicine › Physiology › Nitric Oxide and Endothelin Effects
  • Health Sciences › Medicine › Pathology and Forensic Medicine › Cardiac Ischemia and Reperfusion
Keywords
nitric oxide, apoptosis, cytochrome c release, caspase-3, caspase inhibition, mitochondrial apoptosis, MCF-7 cells, TNF-α, actinomycin D
MeSH terms
Cytochrome c Group, Dactinomycin, Enzyme Activation, Liver, Nitric Oxide, Penicillamine, Tumor Necrosis Factor-alpha, Signal Transduction, Apoptosis, Proto-Oncogene Proteins c-bcl-2, Caspase 3, Caspase Inhibitors

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