The DOI matches its Crossref record; 215 of the 217 references it cites were found in a registry or an index.
Glutathione peroxidases
Abstract
Background With increasing evidence that hydroperoxides are not only toxic but rather exert essential physiological functions, also hydroperoxide removing enzymes have to be re-viewed. In mammals, the peroxidases inter alia comprise the 8 glutathione peroxidases (GPx1-GPx8) so far identified.Scope of the review Since GPxs have recently been reviewed under various aspects, we here focus on novel findings considering their diverse physiological roles exceeding an antioxidant activity.Major conclusions GPxs are involved in balancing the H2O2 homeostasis in signalling cascades, e.g. in the insulin signalling pathway by GPx1; GPx2 plays a dual role in carcinogenesis depending on the mode of initiation and cancer stage; GPx3 is membrane associated possibly explaining a peroxidatic function despite low plasma concentrations of GSH; GPx4 has novel roles in the regulation of apoptosis and, together with GPx5, in male fertility. Functions of GPx6 are still unknown, and the proposed involvement of GPx7 and GPx8 in protein folding awaits elucidation.General significance Collectively, selenium-containing GPxs (GPx1-4 and 6) as well as their non-selenium congeners (GPx5, 7 and 8) became key players in important biological contexts far beyond the detoxification of hydroperoxides. This article is part of a Special Issue entitled Cellular functions of glutathione.
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In the citing paper
“the reduced glutathione (GSH)-dependent enzyme glutathione peroxidase 4 (GPX4)—which is directly targeted by RSL3—has emerged as the main endogenous inhibitor of ferroptosis by virtue of its ability to limit lipid peroxidation by catalyzing the GSH-dependent reduction of lipid hydroperoxides to lipid alcohols [547–550].”
From Molecular mechanisms of cell death: recommendations of the nomenclature committee on cell death 2018. (2018) · cites this paper as [549]
In the citing paper
“erastin triggers ferroptosis by (indirectly) affecting the catalytic cycle of GPX4 via a mechanism that involves the inhibition of the cystine/glutamate antiporter system xc− and consequent decrease in intracellular cysteine (which derives from cystine reduction in the cytoplasm) and GSH (which is synthesized from cysteine) [539, 548, 549, 551].”
From Molecular mechanisms of cell death: recommendations of the nomenclature committee on cell death 2018. (2018) · cites this paper as [549]
In the citing paper
“Glutathione depletion causes loss of cellular antioxidant capacity, as well as inhibition of glutathione-dependent enzymes, such as glutathione peroxidases [24, 25].”
From Ferroptosis: Death by Lipid Peroxidation (2016) · cites this paper as [25]
In the citing paper
“First, GPX4 is the only enzyme that can reduce lipid hydroperoxides within biological membranes [25].”
From Ferroptosis: Death by Lipid Peroxidation (2016) · cites this paper as [25]
In the citing paper
“Second, GPX4 uses glutathione as an essential cofactor for its enzymatic activity [25].”
From Ferroptosis: Death by Lipid Peroxidation (2016) · cites this paper as [25]
In the citing paper
“GPx-1 acts in the intracellular environment and maintains the physiological level of hydrogen peroxide, which is important in mitochondrial function, thiol redox homeostasis, and signal transduction (Brigelius-Flohé and Maiorino 2013).”
From Reactive Oxygen Species, Toxicity, Oxidative Stress, and Antioxidants: Chronic Diseases and Aging (2023) · cites this paper as Brigelius-Flohé and Maiorino 2013
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Cites
1 retracted
Xu, X., Liu, T., Zhang, A., Huo, X., Luo, Q., Chen, Z., Yu, L., Li, Q., Liu, L., Lun, Z., et al. (2012) · Infection and Immunity · doi:10.1128/iai.06295-11 · Cited by 69
RetractedSelenium: Biochemical Role as a Component of Glutathione Peroxidase
Rotruck, J. T., Pope, A. L., Ganther, H. E., Swanson, A. B., Hafeman, D. G., & Hoekstra, W. G. (1973) · Science · doi:10.1126/science.179.4073.588 · Cited by 7,815
Association of reactive oxygen species levels and radioresistance in cancer stem cells
Diehn, M., Cho, R. W., Lobo, N. A., Kalisky, T., Dorie, M. J., Kulp, A. N., Qian, D., Lam, J. S., Ailles, L. E., Wong, M., et al. (2009) · Nature · doi:10.1038/nature07733 · Cited by 2,555
Characterization of Mammalian Selenoproteomes
Kryukov, G. V., Castellano, S., Novoselov, S. V., Lobanov, A. V., Zehtab, O., Guigó, R., & Gladyshev, V. N. (2003) · Science · doi:10.1126/science.1083516 · Cited by 2,385
Oncogene-induced Nrf2 transcription promotes ROS detoxification and tumorigenesis
DeNicola, G. M., Karreth, F. A., Humpton, T. J., Gopinathan, A., Wei, C., Frese, K., Mangal, D., Yu, K. H., Yeo, C. J., Calhoun, E. S., et al. (2011) · Nature · doi:10.1038/nature10189 · Cited by 2,277
Seiler, A., Schneider, M., Förster, H., Roth, S., Wirth, E. K., Culmsee, C., Plesnila, N., Kremmer, E., Rådmark, O., Wurst, W., et al. (2008) · Cell Metabolism · doi:10.1016/j.cmet.2008.07.005 · Cited by 1,470
Glutathione peroxidase: A selenoenzyme
Flohé, L., Günzler, W. A., & Schock, H. H. (1973) · FEBS Letters · doi:10.1016/0014-5793(73)80755-0 · Cited by 1,389
Keaney, J. F., Larson, M. G., Vasan, R. S., Wilson, P. W. F., Lipinska, I., Corey, D., Massaro, J. M., Sutherland, P., Vita, J. A., & Benjamin, E. J. (2003) · Arteriosclerosis, Thrombosis, and Vascular Biology · doi:10.1161/01.atv.0000058402.34138.11 · Cited by 1,304
Lubos, E., Loscalzo, J., & Handy, D. E. (2011) · Antioxidants & Redox Signaling · doi:10.1089/ars.2010.3586 · Cited by 1,280
Tissue-specific functions of individual glutathione peroxidases
Brigelius-Flohé, R. (1999) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(99)00173-2 · Cited by 1,114
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Galluzzi, L., Vitale, I., Aaronson, S. A., Abrams, J. M., Adam, D., Agostinis, P., Alnemri, E. S., Altucci, L., Amelio, I., Andrews, D. W., et al. (2018) · Cell Death & Differentiation · doi:10.1038/s41418-017-0012-4 · Cited by 6,680
Ayala, A., Muñoz, M., & Argüelles, S. (2014) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2014/360438 · Cited by 6,837
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Yang, W. S., & Stockwell, B. R. (2016) · Trends in Cell Biology · doi:10.1016/j.tcb.2015.10.014 · Cited by 3,088
Hayes, J. D., Dinkova-Kostova, A. T., & Tew, K. D. (2020) · Cancer Cell · doi:10.1016/j.ccell.2020.06.001 · Cited by 2,654
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He, L., He, T., Farrar, S., Ji, L., Liu, T., & Ma, X. (2017) · Cellular Physiology and Biochemistry · doi:10.1159/000485089 · Cited by 2,207
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Metadata
- Authors
- Brigelius-Flohé, R., & Maiorino, M.
- Affiliations
- University of Padua (IT)
- ORCID
- Maiorino, Matilde
- Venue
- Biochimica et Biophysica Acta (BBA) - General Subjects
- Publisher
- Elsevier BV
- Published
- 2013-05
- Volume
- 1830
- Issue
- 5
- Pages
- 3289-3303
- ISSN
- 0304-4165 (ISSN-L)
- OpenAlex
- W4211158689
- Cited by
- 1,904
- References
- 217
- Citations by year
- 2026: 162 · 2025: 179 · 2024: 181 · 2023: 191 · 2022: 220 · 2021: 196 · 2020: 154 · 2019: 123 · 2018: 112 · 2017: 106 · 2016: 86 · 2015: 91 · 2014: 75 · 2013: 25
- FWCI
- 7.48
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Biochimica et Biophysica Acta (BBA) - General Subjects (publishedVersion)
- PubMed (publishedVersion)
- Padua Research Archive (University of Padova) (submittedVersion)
- Funders
- German Research Council (BR778/8-1)
- Topics
- Health Sciences › Nursing › Nutrition and Dietetics › Selenium in Biological Systems
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glutathione Transferases and Polymorphisms
- Keywords
- glutathione peroxidase, glutathione peroxidase 1, GPX2, glutathione peroxidase 3, GPX4, GPX5, GPX7, GPX8, hydrogen peroxide homeostasis, hydroperoxide detoxification, insulin signaling, carcinogenesis, apoptosis, male fertility, protein folding, glutathione
- MeSH terms
- Animals, Antioxidants, Glutathione, Glutathione Peroxidase, Humans, Hydrogen Peroxide, Oxidation-Reduction
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