The DOI matches its Crossref record; 37 of the 37 references it cites were found in a registry or an index.
Proteomics Analysis of Cellular Response to Oxidative Stress
Open accessAbstract
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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“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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D'Autréaux, B., & Toledano, M. B. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2256 · Cited by 3,642
Structure, mechanism and regulation of peroxiredoxins
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Hydrogen peroxide sensing and signaling
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Metadata
- 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
- hybrid
- doi.org
- Licence
- 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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