Peroxiredoxin functions as a peroxidase and a regulator and sensor of local peroxides
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Peroxiredoxins (Prxs) contain an active site cysteine that is sensitive to oxidation by H(2)O(2). Mammalian cells express six Prx isoforms that are localized to various cellular compartments. The oxidized active site cysteine of Prx can be reduced by a cellular thiol, thus enabling Prx to function as a locally constrained peroxidase. Regulation of Prx via phosphorylation in response to extracellular signals allows the local accumulation of H(2)O(2) and thereby enables its messenger function. The fact that the oxidation state of the active site cysteine of Prx can be transferred to other proteins that are less intrinsically susceptible to H(2)O(2) also allows Prx to function as an H(2)O(2) sensor.
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Based on conserved redox-sensitive Cys residues among multiple isoforms, many Prx enzymes could be oxidatively-modified and inactivated, contributing to elevated oxidative stress.
“Based on the conserved redox-sensitive Cys residues among the multiple isoforms [47], [48], [49], many Prx enzymes could be also oxidatively-modified and inactivated, contributing to elevated levels of oxidative stress.”
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Orr, W. C., Radyuk, S. N., & Sohal, R. S. (2013) · Antioxidants & Redox Signaling · doi:10.1089/ars.2012.5002 · Cited by 55 · see citing works
Frijhoff, J., Dagnell, M., Augsten, M., Beltrami, E., Giorgio, M., & Östman, A. (2014) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.12.022 · Cited by 43 · see citing works
Kritsiligkou, P., Rand, J. D., Weids, A. J., Wang, X., Kershaw, C. J., & Grant, C. M. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.001824 · Cited by 36 · see citing works
- Authors
- Rhee, S. G., Woo, H. A., Kil, I. S., & Bae, S. H.
- Affiliations
- Ewha Womans University (KR)
- Corresponding author
- Rhee, Sue Goo
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2012-02
- Volume
- 287
- Issue
- 7
- Pages
- 4403-4410
- ISSN
- 0021-9258 (ISSN-L)
- PMC
- PMC3281607
- OpenAlex
- W2089818796
- Cited by
- 603
- References
- 88
- Citations by year
- 2026: 34 · 2025: 39 · 2024: 25 · 2023: 41 · 2022: 35 · 2021: 35 · 2020: 40 · 2019: 31 · 2018: 40 · 2017: 60 · 2016: 57 · 2015: 59 · 2014: 59 · 2013: 32 · 2012: 15
- FWCI
- 3.11
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Research Foundation
- National Research Foundation of Korea
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Life Sciences › Immunology and Microbiology › Immunology › Neutrophil, Myeloperoxidase and Oxidative Mechanisms
- Health Sciences › Nursing › Nutrition and Dietetics › Selenium in Biological Systems
- Keywords
- peroxiredoxin, peroxidase activity, hydrogen peroxide, thiol reduction, phosphorylation, redox regulation
- MeSH terms
- Animals, Cysteine, Humans, Hydrogen Peroxide, Isoenzymes, Peroxidase, Oxidation-Reduction, Phosphorylation, Second Messenger Systems, Catalytic Domain, Peroxiredoxins
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
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