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

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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, Lunardi, Joël·2002·Journal of Biological Chemistry

DOI 10.1074/jbc.m106585200

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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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Self-citation
Proteomic analysis of redox‐ and ErbB2‐dependent changes in mammary luminal epithelial cells using cysteine‐ and lysine‐labelling two‐dimensional difference gel electrophoresis
Chan, H., Gharbi, S., Gaffney, P. R. J., Cramer, R., Waterfield, M. D., & Timms, J. F. (2005) · PROTEOMICS · doi:10.1002/pmic.200401300 · Cited by 98

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
ORCID: Rabilloud, Thierry
Heller, Manfred
Aebersold, Ruedi
Benahmed, Mohamed
Venue: Journal of Biological Chemistry
Publisher: Elsevier BV
Published: 2002-05
Volume: 277
Issue: 22
Pages: 19396-19401
ISSN: 0021-9258 (ISSN-L)
DOI: 10.1074/jbc.m106585200
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: hybrid
doi.org
Licence: cc-by
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
creativecommons.org/licenses/by/4.0/ (vor, 6728 d)
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 (medical) › 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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Proteomics Analysis of Cellular Response to Oxidative Stress

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