Cited by 393Redox biology and oxidative stressAntioxidant Activity and Oxidative StressNeutrophil, Myeloperoxidase and Oxidative Mechanisms

Proteomics Analysis of Cellular Response to Oxidative Stress

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Rabilloud, Thierry, Heller, Manfred, Gasnier, Françoise, Luche, Sylvie, Rey, Catherine, Aebersold, Ruedi, Benahmed, Mohamed, Louisot, Pierre +1 more·2002·Journal of Biological Chemistry

Abstract

The proteomics analysis reported here shows that a major cellular response to oxidative stress is the modification of several peroxiredoxins. An acidic form of the peroxiredoxins appeared to be systematically increased under oxidative stress conditions. Peroxiredoxins are enzymes catalyzing the destruction of peroxides. In doing so, a reactive cysteine in the peroxiredoxin active site is weakly oxidized (disulfide or sulfenic acid) by the destroyed peroxides. Cellular thiols (e.g. thioredoxin) are used to regenerate the peroxiredoxins to their active state. Tandem mass spectrometry was carried out to characterize the modified form of the protein produced in vivo by oxidative stress. The cysteine present in the active site was shown to be oxidized into cysteic acid, leading to an inactivated form of peroxiredoxin. This strongly suggested that peroxiredoxins behave as a dam upon oxidative stress, being both important peroxide-destroying enzymes and peroxide targets. Results obtained in a primary culture of Leydig cells challenged with tumor necrosis factor alpha suggested that this oxidized/native balance of peroxiredoxin 2 may play an active role in resistance or susceptibility to tumor necrosis factor alpha-induced apoptosis.

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  • Many mammalian 2-Cys Prxs are susceptible to overoxidation, in which the -S-OH of the oxidized Cys-active site is further oxidized to −SO2H (sulfinic acid).

    “however, many of the mammalian 2-Cys forms are susceptible to overoxidation, a process in which the –S-OH of the oxidized Cys-active site is further oxidized to −SO2H (sulfinic acid) (338, 462).”

    From Redox regulation of mitochondrial function (2012) · cites this paper as [338]

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Authors
Rabilloud, T., Heller, M., Gasnier, F., Luche, S., Rey, C., Aebersold, R., Benahmed, M., Louisot, P., & Lunardi, J.
Affiliations
  • Université Joseph Fourier (FR)
  • University of Washington (US)
  • Inserm (FR)
Corresponding author
Rabilloud, Thierry
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
2002-05
Volume
277
Issue
22
Pages
19396-19401
ISSN
0021-9258 (ISSN-L)
OpenAlex
W2069480316
Cited by
393
References
37
Citations by year
2026: 2 · 2025: 4 · 2024: 3 · 2023: 3 · 2022: 2 · 2021: 5 · 2020: 4 · 2019: 7 · 2018: 6 · 2017: 18 · 2016: 12 · 2015: 15 · 2014: 17 · 2013: 18 · 2012: 21
FWCI
11.01
Type
journal article
Language
en
Open access
Locations
  • Journal of Biological Chemistry (publishedVersion, cc-by)
  • PubMed (publishedVersion)
Funders
Centre National de la Recherche Scientifique
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
  • Health Sciences › Medicine › Biochemistry › Antioxidant Activity and Oxidative Stress
  • Life Sciences › Immunology and Microbiology › Immunology › Neutrophil, Myeloperoxidase and Oxidative Mechanisms
Keywords
peroxiredoxin, oxidative stress, peroxiredoxin 2, cysteine oxidation, sulfenic acid, cysteic acid, protein modification, thioredoxin, peroxide detoxification, Leydig cells, TNF-α, apoptosis
MeSH terms
Animals, Binding Sites, Cysteine, Humans, Oxygen, Peptides, Peroxidases, Protein Binding, Mass Spectrometry, Swine, Tumor Necrosis Factor-alpha, Apoptosis, Oxidative Stress, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization, Jurkat Cells, Peroxiredoxins, Peroxiredoxin III

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