The DOI matches its Crossref record; 25 of the 26 references it cites were found in a registry or an index.
The selenoprotein GPX4 is essential for mouse development and protects from radiation and oxidative damage insults
Abstract
Lipid peroxidation has been implicated in a variety of pathophysiological processes, including inflammation, atherogenesis, neurodegeneration, and the ageing process. Phospholipid hydroperoxide glutathione peroxidase (GPX4) is the only major antioxidant enzyme known to directly reduce phospholipid hydroperoxides within membranes and lipoproteins, acting in conjunction with alpha tocopherol (vitamin E) to inhibit lipid peroxidation. Here we describe the generation and characterization of GPX4-deficient mice by targeted disruption of the murine Gpx4 locus through homologous recombination in embryonic stem cells. Gpx4(-/-) embryos die in utero by midgestation (E7.5) and are associated with a lack of normal structural compartmentalization. Gpx4(+/-) mice display reduced levels of Gpx4 mRNA and protein in various tissues. Interestingly, cell lines derived from Gpx4(+/-) mice are markedly sensitive to inducers of oxidative stress, including gamma-irradiation, paraquat, tert-butylhydroperoxide, and hydrogen peroxide, as compared to cell lines derived from wild-type control littermates. Gpx4(+/-) mice also display reduced survival in response to gamma-irradiation. Our observations establish GPX4 as an essential antioxidant enzyme in mice and suggest that it performs broad functions as a component of the mammalian antioxidant network.
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In the citing paper
“Gpx4−/− mice display embryonic lethality with complete penetrance [547, 550, 587, 588].”
From Molecular mechanisms of cell death: recommendations of the nomenclature committee on cell death 2018. (2018) · cites this paper as [588]
In the citing paper
“Knockout of Gpx4 in mice caused embryonic lethality between E7.5 and E8.5, indicating an essential role of Gpx4 in mouse development [42, 43].”
From Ferroptosis: Death by Lipid Peroxidation (2016) · cites this paper as [43]
In the citing paper
“In addition, unlike the other GPx-family members, GPx-4 knockout is lethal in mice (465).”
From Redox regulation of mitochondrial function (2012) · cites this paper as [465]
In the citing paper
“Complete absence of GPx-4 is known to be lethal (465),”
From Redox regulation of mitochondrial function (2012) · cites this paper as [465]
Citations
Cites
Free radicals in biology and medicine
Gutteridge, J. M. C. (1991) · General Pharmacology The Vascular System · doi:10.1016/0306-3623(91)90478-o · Cited by 17,178
Chelex 100 as a Medium for Simple Extraction of DNA for PCR-Based Typing from Forensic Material
Walsh, P. S., Metzger, D. A., & Higuchi, R. (2013) · BioTechniques · doi:10.2144/000114018 · Cited by 5,850
Free Radicals in Biology and Medicine
Land, E. J. (1990) · International Journal of Radiation Biology · doi:10.1080/09553009014552071 · Cited by 4,871
Toxicity determined in vitro by morphological alterations and neutral red absorption
Borenfreund, E., & Puerner, J. A. (1985) · Toxicology Letters · doi:10.1016/0378-4274(85)90046-3 · Cited by 1,913
Dilated cardiomyopathy and neonatal lethality in mutant mice lacking manganese superoxide dismutase
Li, Y., Huang, T.-T., Carlson, E. J., Melov, S., Ursell, P. C., Olson, J. L., Noble, L. J., Yoshimura, M. P., Berger, C., Chan, P. H., et al. (1995) · Nature Genetics · doi:10.1038/ng1295-376 · Cited by 1,789
CLONAL GROWTH OF MAMMALIAN CELLS IN VITRO
Puck, T. T., Marcus, P. I., & Cieciura, S. J. (1956) · The Journal of Experimental Medicine · doi:10.1084/jem.103.2.273 · Cited by 1,143
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
Dual Function of the Selenoprotein PHGPx During Sperm Maturation
Ursini, F., Heim, S., Kieß, M., Maiorino, M., Roveri, A., Wissing, J. B., & Flohé, L. (1999) · Science · doi:10.1126/science.285.5432.1393 · Cited by 902
Ho, Y., Magnenat, J.-L., Bronson, R. T., Cao, J., Gargano, M. D., Sugawara, M., & Funk, C. D. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.26.16644 · Cited by 562
The role of selenium peroxidases in the protection against oxidative damage of membranes
Ursini, F., & Bindoli, A. (1987) · Chemistry and Physics of Lipids · doi:10.1016/0009-3084(87)90053-3 · Cited by 391
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Davis, C. D., & Milner, J. A. (2007) · Springer eBooks · doi:10.1007/0-387-33827-6_32 · Cited by 1
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Page, M. M. (2011) · Brock University Digital Repository (Brock University)
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Zhang, S., Zeng, H., Luo, Y., Wang, Q., & Cheng, W. (2010) · The FASEB Journal · doi:10.1096/fasebj.24.1_supplement.lb251
Davoodi, S. (2015) · cIRcle (University of British Columbia) · doi:10.14288/1.0166263
Downey, C. M., & Jirik, F. R. (2011) · Springer eBooks · doi:10.1007/978-1-4614-1025-6_45
Vergleichende, A. F., Schmidt, J., Allgemeine, L. F., & Schmahl, W. W. (2006)
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Pathways for kidney triglyceride accumulation
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Schomburg, L., & Köhrle, J. (2012) · Wiley eBooks · doi:10.1002/9783527653058.ch9
Qian, L., Fu, H., Mou, Y., Lin, W., Ye, L., & Ji, G. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23158123
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Zhu, L., Yang, F., Wang, L., Dong, L., Huang, Z., Wang, G., Chen, G., & Li, Q. (2021) · Figshare · doi:10.6084/m9.figshare.14059396
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Feng, S., Yuan, Y., Lin, Z., Li, M., Ye, D., Shi, L., Li, D., Zhao, M., Meng, C., He, X., et al. (2024) · Figshare · doi:10.6084/m9.figshare.25255823
Zhu, L., Yang, F., Lingwei, W., Dong, L., Huang, Z., Wang, G., Chen, G., & Li, Q. (2021) · Figshare · doi:10.6084/m9.figshare.14059405
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Feng, S., Yuan, Y., Lin, Z., Li, M., Ye, D., Shi, L., Li, D., Zhao, M., Meng, C., He, X., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26683051
Feng, S., Yuan, Y., Lin, Z., Li, M., Ye, D., Shi, L., Li, D., Zhao, M., Meng, C., He, X., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26683072
Zhu, L., Yang, F., Lingwei, W., Dong, L., Huang, Z., Wang, G., Chen, G., & Li, Q. (2021) · Figshare · doi:10.6084/m9.figshare.14059369
Feng, S., Yuan, Y., Lin, Z., Li, M., Ye, D., Shi, L., Li, D., Zhao, M., Meng, C., He, X., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26683066
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Zhao, J., Zhang, S., Chen, L., Liu, X., Su, H., Chen, L., Yang, L., & Zhang, H. (2020) · Figshare · doi:10.6084/m9.figshare.13083105
Feng, S., Yuan, Y., Lin, Z., Li, M., Ye, D., Shi, L., Li, D., Zhao, M., Meng, C., He, X., et al. (2024) · Figshare · doi:10.6084/m9.figshare.25256114
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Barrett, M. S., Shrimp, J. H., Löser, A., Cheff, D. M., Cheng, Q., Kipp, A. P., Hall, M. D., & Arnér, E. S. J. (2026) · Redox Biology · doi:10.1016/j.redox.2026.104445
Lei, X., Liu, G., Duan, Y., Dong, Y., Chen, F., Li, Z., Liu, Y., & Shou, S. (2026) · Science Progress · doi:10.1177/00368504261501651
Gong, G. (2011) · OpenGrey (Institut de l'Information Scientifique et Technique)
Metadata
- Authors
- Yant, L. J., Ran, Q., Rao, L., Van Remmen, H., Shibatani, T., Belter, J. G., Motta, L., Richardson, A., & Prolla, T. A.
- Affiliations
- University of Wisconsin–Madison (US)
- The University of Texas at San Antonio Health Science Center (US)
- Corresponding author
- Prolla, Tomas A
- Venue
- Free Radical Biology and Medicine
- Publisher
- Elsevier BV
- Published
- 2003-02
- Volume
- 34
- Issue
- 4
- Pages
- 496-502
- ISSN
- 0891-5849 (ISSN-L)
- OpenAlex
- W2165072468
- Cited by
- 797
- References
- 26
- Citations by year
- 2026: 29 · 2025: 41 · 2024: 82 · 2023: 59 · 2022: 52 · 2021: 51 · 2020: 43 · 2019: 32 · 2018: 39 · 2017: 35 · 2016: 22 · 2015: 27 · 2014: 27 · 2013: 24 · 2012: 26
- FWCI
- 16.61
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Free Radical Biology and Medicine (publishedVersion)
- PubMed (publishedVersion)
- Funders
- U.S. Department of Veterans Affairs
- National Institutes of Health
- University of Texas Health Science Center at San Antonio
- National Institute on Aging (P03-AG13319, 1 P01 AG19316, P01AG019316)
- National Cancer Institute
- 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
- Health Sciences › Medicine › Biochemistry (medical) › Antioxidant Activity and Oxidative Stress
- Keywords
- GPX4, phospholipid hydroperoxide glutathione peroxidase, selenoproteins, lipid peroxidation, antioxidant enzymes, embryonic lethality, oxidative stress, gamma-irradiation sensitivity, paraquat, tert-butyl hydroperoxide, hydrogen peroxide, vitamin E, mouse development
- MeSH terms
- Phospholipid Hydroperoxide Glutathione Peroxidase, Animals, Cell Line, Embryo, Mammalian, Female, Fetal Death, Embryonic and Fetal Development, Fibroblasts, Gamma Rays, Gestational Age, Glutathione Peroxidase, Hydrogen Peroxide, Mice, Inbred C57BL, Paraquat, Pregnancy, RNA, Messenger, Blotting, Northern, Blotting, Western, Mice, Knockout, Oxidative Stress, tert-Butylhydroperoxide, In Situ Nick-End Labeling, Mice
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