Mitochondrial oxidative stress in mice lacking the glutathione peroxidase-1 gene
Open accessAbstract
Oxidative stress resulting from mitochondrially derived reactive oxygen species (ROS) has been hypothesized to damage mitochondrial oxidative phosphorylation (OXPHOS) and to be a factor in aging and degenerative disease. If this hypothesis is correct, then genetically inactivating potential mitochondrial antioxidant enzymes such as glutathione peroxidase-1 (Gpx1; EC 1.11.1.9) should increase mitochondrial ROS production and decrease OXPHOS function. To determine the expression pattern of Gpx1, isoform-specific antibodies were generated and mutant mice were prepared in which the Gpx1 protein was substituted for by beta-galactosidase, driven by the Gpx1 promoter. These experiments revealed that Gpx1 is highly expressed in both the mitochondria and the cytosol of the liver and kidney, but poorly expressed in heart and muscle. To determine the physiological importance of Gpx1, mice lacking Gpx1 were generated by targeted mutagenesis in mouse ES cells. Homozygous mutant Gpx1(tm1Mgr) mice have 20% less body weight than normal animals and increased levels of lipid peroxides in the liver. Moreover, the liver mitochondria were found to release markedly increased hydrogen peroxide, a Gpx1 substrate, and have decreased mitochondrial respiratory control ratio and power output index. Hence, genetic inactivation of Gpx1 resulted in growth retardation, presumably due in part to reduced mitochondrial energy production as a product of increased oxidative stress.
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GPx-1 deficiency in mice augments release of oxidants from respiring mitochondria.
“Consistent with a role for GPx-1 in modulating mitochondrial oxidants, its deficiency in mice augments release of oxidants from respiring mitochondria (126).”
From Redox regulation of mitochondrial function (2012) · cites this paper as [126]
Cites
Hydroperoxide metabolism in mammalian organs.
Chance, B., Sies, H., & Boveris, A. (1979) · Physiological Reviews · doi:10.1152/physrev.1979.59.3.527 · Cited by 5,827 · see citing works
The Free Radical Theory of Aging Matures
BECKMAN, K. B., & AMES, B. N. (1998) · Physiological Reviews · doi:10.1152/physrev.1998.78.2.547 · Cited by 3,879 · see citing works
Mitochondrial diseases in man and mouse
Wallace, D. C. (1999) · Science · doi:10.1126/science.283.5407.1482 · Cited by 3,060 · see citing works
Self-citationThe mitochondrial permeability transition
Zoratti, M., & Szabó, I. (1995) · Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes · doi:10.1016/0304-4157(95)00003-a · Cited by 2,395 · see citing works
Targeted disruption of the c-src proto-oncogene leads to osteopetrosis in mice
Soriano, P. M., Montgomery, C. A., Geske, R. S., & Bradley, A. (1991) · Cell · doi:10.1016/0092-8674(91)90499-o · Cited by 1,997 · see citing works
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 · see citing works
Self-citationMitochondrial control of apoptosis
Kroemer, G., Zamzami, N., & Susín, S. A. (1997) · Immunology Today · doi:10.1016/s0167-5699(97)80014-x · Cited by 1,492 · see citing works
Friedrich, G., & Soriano, P. M. (1991) · Genes & Development · doi:10.1101/gad.5.9.1513 · Cited by 1,403 · see citing works
Bax and Adenine Nucleotide Translocator Cooperate in the Mitochondrial Control of Apoptosis
Marzo, I., Brenner, C., Zamzami, N., Jürgensmeier, J. M., Susin, S. A., Vieira, H. L. A., Prévost, M.-C., Xie, Z., Matsuyama, S., Reed, J. C., et al. (1998) · Science · doi:10.1126/science.281.5385.2027 · Cited by 1,168 · see citing works
Kamo, N., Muratsugu, M., Hongoh, R., & Kobatake, Y. (1979) · The Journal of Membrane Biology · doi:10.1007/bf01868720 · Cited by 956 · see citing works
[5] Diversity of glutathione peroxidases
Maiorino, F. M., Brigelius‐Flohé, R., Aumann, K. D., Roveri, A., Schomburg, D., & Flohé, L. (1995) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(95)52007-4 · Cited by 854 · see citing works
Sohal, R. S., Ku, H.-H., Agarwal, S., Forster, M. J., & Lal, H. (1994) · Mechanisms of Ageing and Development · doi:10.1016/0047-6374(94)90104-x · Cited by 788 · see citing works
Trounce, I. A., Kim, Y. L., Jun, A. S., & Wallace, D. C. (1996) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(96)64044-0 · Cited by 749 · see citing works
Self-citationKang, S. W., Chae, H. Z., Seo, M. S., Kim, K., Baines, I., & Rhee, S. G. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.11.6297 · Cited by 693 · see citing works
Goldstein, S., Meyerstein, D., & Czapski, G. (1993) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(93)90043-t · Cited by 679 · see citing works
Chambers, I., Frampton, J., Goldfarb, P. S., Affara, N. A., McBain, W., & Harrison, P. R. (1986) · The EMBO Journal · doi:10.1002/j.1460-2075.1986.tb04350.x · Cited by 667 · see citing works
Mitochondrial disease in mouse results in increased oxidative stress
Esposito, L., Melov, S., Panov, A. V., Cottrell, B. A., & Wallace, D. C. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.9.4820 · Cited by 637 · see citing works
Self-citationHalestrap, A. P., Woodfield, K.-Y., & Connern, C. P. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.6.3346 · Cited by 592 · see citing works
Mitochondrial disease in superoxide dismutase 2 mutant mice
Melov, S., Coskun, P., Patel, M., Tuinstra, R., Cottrell, B., Jun, A. S., Zastawny, T. H., Dizdaroglu, M., Goodman, S. I., Huang, T.-T., et al. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.3.846 · Cited by 581 · see citing works
Self-citationDetection of catalase in rat heart mitochondria.
Radi, R., Turrens, J. F., Chang, L. Y., Bush, K. M., Crapo, J. D., & Freeman, B. A. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)54740-2 · Cited by 573 · see citing works
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 · see citing works
Costantini, P., Chernyak, B. V., Petronilli, V., & Bernardi, P. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.12.6746 · Cited by 516 · see citing works
Williams, M. D., Remmen, H. V., Conrad, C. C., Huang, T., Epstein, C. J., & Richardson, A. G. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.43.28510 · Cited by 453 · see citing works
de Haan, J. B., Bladier, C., Griffiths, P., Kelner, M. J., O’Shea, R. D., Cheung, N. S., Bronson, R. T., Silvestro, M. J., Wild, S., Zheng, S. S., et al. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.35.22528 · Cited by 450 · see citing works
Regulation of the Permeability Transition Pore in Skeletal Muscle Mitochondria
Fontaine, E. M., Eriksson, O., Ichas, F., & Bernardi, P. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.20.12662 · Cited by 347 · see citing works
Beyer, W. F., Imlay, J. A., & Fridovich, I. (1991) · Progress in nucleic acid research and molecular biology · doi:10.1016/s0079-6603(08)60843-0 · Cited by 347 · see citing works
Hyslop, P. A., & Sklar, L. A. (1984) · Analytical Biochemistry · doi:10.1016/0003-2697(84)90457-3 · Cited by 316 · see citing works
Tiana, L., Caib, Q., & Wei, H. (1998) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(98)00025-2 · Cited by 300 · see citing works
Arai, M., Imai, H., Koumura, T., Yoshida, M., Emoto, K., Umeda, M., Chiba, N., & Nakagawa, Y. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.8.4924 · Cited by 296 · see citing works
Connern, C. P., & Halestrap, A. P. (1994) · Biochemical Journal · doi:10.1042/bj3020321 · Cited by 246 · see citing works
Substrate and Site Specificity of Hydrogen Peroxide Generation in Mouse Mitochondria
Kwong, L. K., & Sohal, R. S. (1998) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1997.0489 · Cited by 236 · see citing works
Chernyak, B. V., & Bernardi, P. (1996) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1996.0623w.x · Cited by 233 · see citing works
Guide to techniques in mouse development
Wassarman, P. M., & Depamphilis, M. (1993) · Cited by 220 · see citing works
Membrane potential and surface potential in mitochondria: Uptake and binding of lipophilic cations
Rottenberg, H. (1984) · The Journal of Membrane Biology · doi:10.1007/bf01868977 · Cited by 218 · see citing works
MacGregor, G. R., Zambrowicz, B., & Soriano, P. M. (1995) · Development · doi:10.1242/dev.121.5.1487 · Cited by 209 · see citing works
Self-citationVillani, G., & Attardi, G. M. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.4.1166 · Cited by 199 · see citing works
Rat Phospholipid-hydroperoxide Glutathione Peroxidase
Thimmalapura, P., Burdsall, A., Oleksa, L. M., Chisolm, G. M., & Driscoll, D. M. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.45.26993 · Cited by 195 · see citing works
Arai, M., Imai, H., Sumi, D., Imanaka, T., Takano, T., Chiba, N., & Nakagawa, Y. (1996) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1996.1525 · Cited by 129 · see citing works
Esworthy, R. S., Swiderek, K. M., Ho, Y., & Chu, F. (1998) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/s0304-4165(98)00032-4 · Cited by 108 · see citing works
Kinetic control of mitochondrial ATP synthesis
LaNoue, K. F., Jeffries, F. M. H., & Radda, G. K. (1986) · Biochemistry · doi:10.1021/bi00371a058 · Cited by 103 · see citing works
Maser, R. L., Magenheimer, B. S., & Calvet, J. P. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)47126-8 · Cited by 76 · see citing works
Immunocytochemical localization of seleno-glutathione peroxidase in the adult mouse brain
Trépanier, G., Furling, D., Puymirat, J., & Mirault, M.-É. (1996) · Neuroscience · doi:10.1016/0306-4522(96)00222-9 · Cited by 70 · see citing works
Distribution of phospholipid hydroperoxide glutathione peroxidase (PHGPx) in rat testis mitochondria
Godeas, C., Sandri, G., & Panfili, E. (1994) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/0005-2736(94)90242-9 · Cited by 67 · see citing works
Cristiano, F., de Haan, J. B., Iannello, R. C., & Kola, I. (1995) · Mechanisms of Ageing and Development · doi:10.1016/0047-6374(94)01561-y · Cited by 56 · see citing works
Mitochondrial membrane potential estimated with the correction of probe binding
Demura, M., Kamo, N., & Kobatake, Y. (1987) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/0005-2728(87)90113-7 · Cited by 34 · see citing works
Oberley, T. D., Oberley, L. W., Slattery, A. F., & Elwell, J. H. (1991) · PubMed Central · Cited by 33 · see citing works
Villani, G., Tattoli, M., Capitanio, N., Glaser, P., Papa, S., & Danchin, A. (1995) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/0005-2728(95)00112-5 · Cited by 23 · see citing works
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Cited by
Sorted by citations
Halliwell, B. (2001) · Drugs & Aging · doi:10.2165/00002512-200118090-00004 · Cited by 1,502 · see citing works
Mitochondrial metabolism of reactive oxygen species
Andreyev, A. Y., Kushnareva, Y. E., & Starkov, A. A. (2005) · Biochemistry (Moscow) · doi:10.1007/s10541-005-0102-7 · Cited by 1,336 · see citing works
Lubos, E., Loscalzo, J., & Handy, D. E. (2011) · Antioxidants & Redox Signaling · doi:10.1089/ars.2010.3586 · Cited by 1,280 · see citing works
The ADP/ATP translocator is not essential for the mitochondrial permeability transition pore
Kokoszka, J. E., Waymire, K. G., Levy, S. E., Sligh, J. E., Cai, J., Jones, D. P., MacGregor, G. R., & Wallace, D. C. (2004) · Nature · doi:10.1038/nature02229 · Cited by 1,086 · see citing works
Self-citationHydrogen peroxide in the human body
Halliwell, B., Clement, M. V., & Long, L. H. (2000) · FEBS Letters · doi:10.1016/s0014-5793(00)02197-9 · Cited by 1,075 · see citing works
Trends in oxidative aging theories
Muller, F. L., Lustgarten, M. S., Jang, Y., Richardson, A., & Van Remmen, H. (2007) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2007.03.034 · Cited by 1,053 · see citing works
Mitochondrial dysfunction as a cause of optic neuropathies
Carelli, V., Ross‐Cisneros, F. N., & Sadun, A. A. (2004) · Progress in Retinal and Eye Research · doi:10.1016/j.preteyeres.2003.10.003 · Cited by 839 · see citing works
Imai, H., & Nakagawa, Y. (2003) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)01197-8 · Cited by 763 · see citing works
Redox compartmentalization in eukaryotic cells.
Go, Y., & Jones, D. P. (2008) · Biochimica et Biophysica Acta · doi:10.1016/j.bbagen.2008.01.011 · Cited by 635 · see citing works
Redox regulation of mitochondrial function
Handy, D. E., & Loscalzo, J. (2012) · Antioxidants & Redox Signaling · doi:10.1089/ars.2011.4123 · Cited by 588 · see citing works
Ribas, V., García‐Ruiz, C., & Fernández-Checa, J. C. (2014) · Frontiers in Pharmacology · doi:10.3389/fphar.2014.00151 · Cited by 572 · see citing works
Development of insulin resistance and obesity in mice overexpressing cellular glutathione peroxidase
McClung, J. P., Roneker, C. A., Mu, W., Lisk, D. J., Langlais, P., Liu, F., & Lei, X. G. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0308096101 · Cited by 536 · see citing works
Salmon, A. B., Richardson, A. G., & Pérez, V. (2009) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2009.12.015 · Cited by 444 · see citing works
Oxidative stress and mitochondrial dysfunction in neurodegenerative diseases
Trushina, E. V., & McMurray, C. T. (2007) · Neuroscience · doi:10.1016/j.neuroscience.2006.10.056 · Cited by 440 · see citing works
Paradoxical Roles of Antioxidant Enzymes: Basic Mechanisms and Health Implications
Lei, X. G., Zhu, J., Cheng, W.-H., Bao, Y., Ho, Y.-S., Reddi, A. R., Holmgren, A., & Arnér, E. S. J. (2015) · Physiological Reviews · doi:10.1152/physrev.00010.2014 · Cited by 437 · see citing works
The effects of stress and aging on glutathione metabolism
Maher, P. A. (2005) · Ageing Research Reviews · doi:10.1016/j.arr.2005.02.005 · Cited by 426 · see citing works
The significance of mitochondrial toxicity testing in drug development
Dykens, J. A., & Will, Y. (2007) · Drug Discovery Today · doi:10.1016/j.drudis.2007.07.013 · Cited by 419 · see citing works
Peroxiredoxin II is essential for sustaining life span of erythrocytes in mice
Lee, T.-H. (2003) · Blood · doi:10.1182/blood-2002-08-2548 · Cited by 420 · see citing works
Interactions between mitochondrial reactive oxygen species and cellular glucose metabolism
Liemburg-Apers, D. C., Willems, P. H. G. M., Koopman, W. J. H., & Grefte, S. (2015) · Archives of Toxicology · doi:10.1007/s00204-015-1520-y · Cited by 391 · see citing works
Graham, D., Huynh, N. N., Hamilton, C. A., Beattie, E., Smith, R. A. J., Cochemé, H. M., Murphy, M. P., & Dominiczak, A. F. (2009) · Hypertension · doi:10.1161/hypertensionaha.109.130351 · Cited by 367 · see citing works
Murphy, M. P. (2011) · Antioxidants and Redox Signaling · doi:10.1089/ars.2011.4289 · Cited by 341 · see citing works
Matés, J. M., Pérez‐Gómez, C., de Castro, I. N., Asenjo, M., & Márquez, J. (2002) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/s1357-2725(01)00143-1 · Cited by 340 · see citing works
Mitochondrial DNA repair and aging
Mandavilli, B. S., Santos, J. H., & Houten, B. V. (2002) · Mutation research. Fundamental and molecular mechanisms of mutagenesis · doi:10.1016/s0027-5107(02)00220-8 · Cited by 338 · see citing works
Mice with combined disruption of Gpx1 and Gpx2 genes have colitis
Esworthy, R. S., Aranda, R., Martı́n, M. G., Doroshow, J. H., Binder, S. W., & Chu, F. (2001) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.2001.281.3.g848 · Cited by 299 · see citing works
Genova, M. L., Ventura, B., Giuliano, G., Bovina, C., Formiggini, G., Castelli, G. P., & Lenaz, G. (2001) · FEBS Letters · doi:10.1016/s0014-5793(01)02850-2 · Cited by 297 · see citing works
Mitochondrial Management of Reactive Oxygen Species
Napolitano, G., Fasciolo, G., & Venditti, P. (2021) · Antioxidants · doi:10.3390/antiox10111824 · Cited by 296 · see citing works
The role of glutathione peroxidase-1 in health and disease
Handy, D. E., & Loscalzo, J. (2022) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2022.06.004 · Cited by 288 · see citing works
Metabolic Regulation and Function of Glutathione Peroxidase-1
Lei, X. G., Cheng, W., & McClung, J. P. (2007) · Annual Review of Nutrition · doi:10.1146/annurev.nutr.27.061406.093716 · Cited by 275 · see citing works
Peroxiredoxin 1 and its role in cell signaling
Neumann, C. A., Cao, J., & Manevich, Y. (2009) · Cell Cycle · doi:10.4161/cc.8.24.10242 · Cited by 268 · see citing works
Genetic mouse models of brain ageing and Alzheimer's disease
Bilkei‐Gorzó, A. (2013) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2013.12.009 · Cited by 244 · see citing works
Recipes for Creating Animal Models of Diabetic Cardiovascular Disease
Hsueh, W. A., Abel, E. D., Breslow, J. L., Maeda, N., Davis, R. C., Fisher, E. A. A., Dansky, H. M., McClain, D. A., McIndoe, R., Wassef, M. K., et al. (2007) · Circulation Research · doi:10.1161/01.res.0000266449.37396.1f · Cited by 219 · see citing works
Mitochondria and Reactive Oxygen Species. Which Role in Physiology and Pathology?
Lenaz, G. (2011) · Advances in experimental medicine and biology · doi:10.1007/978-94-007-2869-1_5 · Cited by 214 · see citing works
Zhang, Y., Ikeno, Y., Qi, W., Chaudhuri, A., Li, Y., Bokov, A., Thorpe, S. R., Baynes, J., Epstein, C. J., Richardson, A. G., et al. (2009) · The Journals of Gerontology Series A · doi:10.1093/gerona/glp132 · Cited by 206 · see citing works
The pathophysiology of mitochondrial disease as modeled in the mousePreprint
Wallace, D. C., & Fan, W. (2009) · Genes & Development · doi:10.1101/gad.1784909 · Cited by 201 · see citing works
Self-citationCellular glutathione peroxidase deficiency and endothelial dysfunction
Forgione, M. A., Weiss, N., Heydrick, S., Cap, A., Klings, E. S., Bierl, C., Eberhardt, R. T., Farber, H. W., & Loscalzo, J. (2002) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00598.2001 · Cited by 199 · see citing works
Glutathionylation of Mitochondrial Proteins
Hurd, T., Costa, N. J., Dahm, C., Beer, S. M., Brown, S. E., Filipovska, A., & Murphy, M. (2005) · Antioxidants and Redox Signaling · doi:10.1089/ars.2005.7.999 · Cited by 195 · see citing works
Mitochondrial medicine--molecular pathology of defective oxidative phosphorylation.
Fosslien, E. (2001) · PubMed · Cited by 186 · see citing works
Gispert, S., Parganlija, D., Klinkenberg, M., Dröse, S., Wittig, I., Mittelbronn, M. G. A., Grzmil, P., Koob, S., Hamann, A., Walter, M. J., et al. (2013) · Human Molecular Genetics · doi:10.1093/hmg/ddt338 · Cited by 188 · see citing works
Devarajan, A., Bourquard, N., Hama, S. Y., Navab, M., Grijalva, V. R., Morvardi, S., Clarke, C. F., Vergnes, L., Reue, K., Teiber, J. F., et al. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3430 · Cited by 185 · see citing works
Mouse models for mitochondrial disease
Wallace, D. C. (2001) · American Journal of Medical Genetics · doi:10.1002/ajmg.1393 · Cited by 178 · see citing works
Self-citationMitochondrial ROS Metabolism: Modulation by Uncoupling Proteins
Casteilla, L., Rigoulet, M., & Pénicaud, L. (2001) · IUBMB Life · doi:10.1080/15216540152845984 · Cited by 170 · see citing works
Arbogast, S., & Ferreiro, A. (2010) · Antioxidants & Redox Signaling · doi:10.1089/ars.2009.2890 · Cited by 167 · see citing works
Wei, Y., Lu, C. Y., Wei, C. Y., Ma, Y. S., & Lee, H. (2001) · PubMed · Cited by 158 · see citing works
Nrf1 Is Critical for Redox Balance and Survival of Liver Cells during Development
Chen, L., Kwong, M., Lu, R., Ginzinger, D. G., Lee, C., Leung, L., & Chan, J. Y. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.13.4673-4686.2003 · Cited by 139 · see citing works
The physiopathologic role of oxidative stress in skeletal muscle
Scicchitano, B. M., Pelosi, L., Sica, G., & Musarò, A. (2017) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2017.08.009 · Cited by 141 · see citing works
Mitochondrial Catalase and Oxidative Injury
Bai, J., & Cederbaum, A. I. (2001) · Neurosignals · doi:10.1159/000046887 · Cited by 139 · see citing works
Oelze, M. W., Kröller‐Schön, S., Steven, S., Lubos, E., Doppler, C. E. J., Hausding, M., Tobias, S., Brochhausen, C., Li, H., Torzewski, M., et al. (2013) · Hypertension · doi:10.1161/hypertensionaha.113.01602 · Cited by 136 · see citing works
The antioxidative effects of probiotic Lactobacillus casei Zhang on the hyperlipidemic rats
Zhang, Y., Du, R., Wang, L., & Zhang, H. (2010) · European Food Research and Technology · doi:10.1007/s00217-010-1255-1 · Cited by 129 · see citing works
Two Tales of Antioxidant Enzymes on β Cells and Diabetes
Lei, X. G., & Vatamaniuk, M. Z. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3416 · Cited by 130 · see citing works
Diabetes, Oxidative Stress, Nitric Oxide and Mitochondria Function
Friederich, M., Hansell, P., & Palm, F. (2009) · Current Diabetes Reviews · doi:10.2174/157339909788166800 · Cited by 126 · see citing works
Antioxidant Strategies in Respiratory Medicine
Christofidou‐Solomidou, M., & Muzykantov, V. R. (2006) · Treatments in Respiratory Medicine · doi:10.2165/00151829-200605010-00004 · Cited by 128 · see citing works
Maternal germ-line transmission of mutant mtDNAs from embryonic stem cell-derived chimeric mice
Sligh, J. E., Levy, S., Waymire, K. G., Allard, P., Dillehay, D. L., Nusinowitz, S., Heckenlively, J. R., MacGregor, G. R., & Wallace, D. C. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.250491597 · Cited by 125 · see citing works
Self-citationWilkinson, S. R., Horn, D., Prathalingam, S. R., & Kelly, J. M. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m303035200 · Cited by 120 · see citing works
Age-dependent alteration in muscle regeneration: the critical role of tissue niche
Barberi, L., Scicchitano, B. M., Rossi, M. D., Bigot, A., Duguez, S., Wielgosik, A., Stewart, C., McPhee, J., Conte, M., Narici, M., et al. (2013) · Biogerontology (Dordrecht) · doi:10.1007/s10522-013-9429-4 · Cited by 128 · see citing works
Degoul, F., Sutton, A., Mansouri, A., Cepanec, C., Valla, D. C., Pessayre, D., Fromenty, B., Degott, C., & Beaugrand, M. (2001) · Gastroenterology · doi:10.1053/gast.2001.24051 · Cited by 117 · see citing works
Ohsawa, I., Nishimaki, K., Murakami, Y., Suzuki, Y., Ishikawa, M., & Ohta, S. (2008) · Journal of Neuroscience · doi:10.1523/jneurosci.4956-07.2008 · Cited by 117 · see citing works
Update on mitochondria and muscle aging: All wrong roads lead to sarcopenia
Picca, A., Calvani, R., Bossola, M., Allocca, E., Menghi, A., Pesce, V., Lezza, A. M. S., Bernabei, R., Landi, F., & Marzetti, E. (2018) · Biological Chemistry · doi:10.1515/hsz-2017-0331 · Cited by 116 · see citing works
Oxidative responses and fungal infection biology
Warris, A., & Ballou, E. R. (2018) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2018.03.004 · Cited by 111 · see citing works
Effects of Growth Hormone and Insulin-Like Growth Factor-1 on Hepatocyte Antioxidative Enzymes
Brown‐Borg, H. M., Rakoczy, S. G., Romanick, M. A., & Kennedy, M. A. (2002) · Experimental Biology and Medicine · doi:10.1177/153537020222700203 · Cited by 111 · see citing works
Role of glutathione peroxidase 1 in glucose and lipid metabolism-related diseases
Huang, J., Zhou, J., Wu, Y., Ren, F., & Lei, X. G. (2018) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.05.077 · Cited by 108 · see citing works
Mitochondrial contributions to cancer cell physiology: potential for drug development
Preston, T. J., Abadi, A., Wilson, A., & Singh, G. (2001) · Advanced Drug Delivery Reviews · doi:10.1016/s0169-409x(01)00127-2 · Cited by 106 · see citing works
de Oliveira, J., Hort, M. A., Moreira, E. L. G., Glaser, V., Ribeiro‐do‐Valle, R. M., Prediger, R. D., Farina, M., Latini, A., & Bem, A. F. D. (2011) · Neuroscience · doi:10.1016/j.neuroscience.2011.09.009 · Cited by 104 · see citing works
Adipose Tissue Proadipogenic Redox Changes in Obesity
Galinier, A., Carrière, A., Fernandez, Y., Carpéné, C., André, M., Caspar‐Bauguil, S., Thouvenot, J.-P., Périquet, B., Pénicaud, L., & Casteilla, L. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m506949200 · Cited by 104 · see citing works
Rigobello, M., Folda, A., Baldoin, M. C., Scutari, G., & Bindoli, A. (2005) · Free radical research · doi:10.1080/10715760500135391 · Cited by 103 · see citing works
Wang, Q., Zheng, Y., Dong, L., Ho, Y.-S., Guo, Z., & Wang, Y.-X. (2006) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2006.12.008 · Cited by 103 · see citing works
de Haan, J. B., Crack, P. J., Flentjar, N. J., Iannello, R. C., Hertzog, P. J., & Kola, I. (2003) · Redox Report · doi:10.1179/135100003125001378 · Cited by 102 · see citing works
New Insights Into Structure and Function of Mitochondria and Their Role in Aging and Disease
Lenaz, G., Baracca, A., Fato, R., Genova, M. L., & Solaini, G. (2006) · Antioxidants and Redox Signaling · doi:10.1089/ars.2006.8.417 · Cited by 97 · see citing works
Aging increases mitochondrial DNA damage and oxidative stress in liver of rhesus monkeys
Castro, M. D. R., Suárez, E., Kraiselburd, E., Isidro, A., de la Paz, J. L. F., Ferder, L., & Ayala‐Torres, S. (2011) · Experimental Gerontology · doi:10.1016/j.exger.2011.10.002 · Cited by 95 · see citing works
Redox Control of Neural Function: Background, Mechanisms, and Significance
Maher, P. (2006) · Antioxidants and Redox Signaling · doi:10.1089/ars.2006.8.1941 · Cited by 99 · see citing works
Oxidative stress and muscle homeostasis
Musarò, A., Fulle, S., & Fanò, G. (2010) · Current Opinion in Clinical Nutrition & Metabolic Care · doi:10.1097/mco.0b013e3283368188 · Cited by 86 · see citing works
Familial glucocorticoid deficiency: New genes and mechanisms
Meimaridou, E., Hughes, C. R., Kowalczyk, J., Guasti, L., Chapple, J. P., King, P., Chan, L. F., Clark, A., & Metherell, L. (2012) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2012.12.010 · Cited by 85 · see citing works
Suppression of complex I gene expression induces optic neuropathy
Qi, X., Lewin, A. S., Hauswirth, W. W., & Guy, J. R. (2003) · Annals of Neurology · doi:10.1002/ana.10426 · Cited by 82 · see citing works
Generation of Reactive Oxygen Species by Mitochondrial Complex I: Implications in Neurodegeneration
Fato, R., Bergamini, C., Leoni, S., Strocchi, P., & Lenaz, G. (2008) · Neurochemical Research · doi:10.1007/s11064-008-9747-0 · Cited by 79 · see citing works
Reactive oxygen and nitrogen species during viral infections
Molteni, C. G., Principi, N., & Esposito, S. (2014) · Free Radical Research · doi:10.3109/10715762.2014.945443 · Cited by 79 · see citing works
Santiago, A. P. S. A., Chaves, E. A., de Oliveira, M. F., & Galina, A. (2008) · Biochimie · doi:10.1016/j.biochi.2008.06.013 · Cited by 80 · see citing works
Mitochondrial defects in neurodegenerative disease
Wallace, D. C. (2001) · Mental Retardation and Developmental Disabilities Research Reviews · doi:10.1002/mrdd.1023 · Cited by 77 · see citing works
Self-citationHirano, M., Davidson, M. M., & DiMauro, S. (2001) · Current Opinion in Cardiology · doi:10.1097/00001573-200105000-00008 · Cited by 77 · see citing works
Interactions of Mitochondrial Thiols with Nitric Oxide
Costa, N. J., Dahm, C., Hurrell, F., Taylor, E. R., & Murphy, M. (2003) · Antioxidants and Redox Signaling · doi:10.1089/152308603322110878 · Cited by 71 · see citing works
Kapnick, S. M., Pacheco, S. E., & McGuire, P. J. (2017) · Metabolism · doi:10.1016/j.metabol.2017.11.010 · Cited by 73 · see citing works
Subudhi, U., & Chainy, G. B. N. (2009) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2009.11.004 · Cited by 74 · see citing works
Targeting Endothelial Dysfunction in Vascular Complications Associated with Diabetes
Sharma, A., Bernatchez, P. N., & de Haan, J. B. (2011) · International Journal of Vascular Medicine · doi:10.1155/2012/750126 · Cited by 74 · see citing works
Kulak, M. V., Cyr, A. R., Woodfield, G. W., Bogachek, M. V., Spanheimer, P. M., Li, T., Price, D. H., Domann, F. E., & Weigel, R. J. (2012) · Oncogene · doi:10.1038/onc.2012.400 · Cited by 73 · see citing works
Chen, L. (2005) · World Journal of Gastroenterology · doi:10.3748/wjg.v11.i37.5795 · Cited by 78 · see citing works
de Haan, J. B., Bladier, C., Lotfi-Miri, M., Taylor, J. M., Hutchinson, P. E., Crack, P. J., Hertzog, P. J., & Kola, I. (2003) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2003.10.020 · Cited by 73 · see citing works
Ding, W., Wang, L., Zhang, J., Ke, W., Zhou, J., Jiexu, Z., Guo, X., & Long, R. (2017) · Journal of Functional Foods · doi:10.1016/j.jff.2017.06.008 · Cited by 71 · see citing works
Merry, T. L., Tran, M., Stathopoulos, M., Wiede, F., Fam, B. C., Dodd, G. T., Clarke, I. J., Watt, M. J., Andrikopoulos, S., & Tiganis, T. (2013) · Antioxidants and Redox Signaling · doi:10.1089/ars.2013.5428 · Cited by 69 · see citing works
Catalytic Antioxidants in the Kidney
Hong, Y. A., & Park, C. W. (2021) · Antioxidants · doi:10.3390/antiox10010130 · Cited by 68 · see citing works
In Vivo Antioxidant Role of Glutathione Peroxidase: Evidence from Knockout Mice
Lei, X. G. (2002) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(02)47021-8 · Cited by 67 · see citing works
The role of reactive oxygen species in the pathogenesis and treatment of retinal diseases
Chan, T., Wilkinson‐Berka, J. L., Deliyanti, D., Hunter, D., Fung, A. T.-C., Liew, G., & White, A. J. R. (2020) · Experimental Eye Research · doi:10.1016/j.exer.2020.108255 · Cited by 66 · see citing works
Zhang, L., Zeng, H., & Cheng, W. (2018) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.05.067 · Cited by 66 · see citing works
Glutathione peroxidase 1 protects mitochondria against hypoxia/reoxygenation damage in mouse hearts
Thu, V. T., Kim, H. K., Ha, S. H., Yoo, J. Y., Park, W. S., Kim, N., Oh, G. T., & Han, J. (2010) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/s00424-010-0811-7 · Cited by 65 · see citing works
Wentzel, P., Gäreskog, M., & Eriksson, U. J. (2008) · Diabetes · doi:10.2337/db08-0830 · Cited by 63 · see citing works
Hormetic and regulatory effects of lipid peroxidation mediators in pancreatic beta cells
Maulucci, G., Daniel, B., Cohen, O., Avrahami, Y., & Sasson, S. (2016) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2016.03.001 · Cited by 63 · see citing works
Disulphide formation on mitochondrial protein thiols.
Hurd, T., Filipovska, A., Costa, N. J., Dahm, C., & Murphy, M. P. (2005) · Biochemical Society Transactions · doi:10.1042/bst0331390 · Cited by 70 · see citing works
Glutathione-peroxidase-1 null muscle progenitor cells are globally defective
Lee, S., Shin, H. S., Shireman, P. K., Vasilaki, A., Remmen, H. V., & CSETE, M. E. (2006) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2006.07.005 · Cited by 61 · see citing works
Iqbal, M., Cawthon, D. L., Wideman, R. F., Jr., & Bottje, W. G. (2001) · Poultry Science · doi:10.1093/ps/80.5.656 · Cited by 59 · see citing works
Zhao, C., Tan, Y.-C., Wong, W.-C., Sem, X., Zhang, H., Han, H., Ong, S.-M., Wong, K.-L., Yeap, W.-H., Sze, S. K., et al. (2010) · Cell Death and Disease · doi:10.1038/cddis.2010.69 · Cited by 57 · see citing works
Braidy, N., Selvaraju, S., Essa, M., Vaishnav, R., Al-Adawi, S., Al-Asmi, A., Al‐Senawi, H., Alobaidy, A. A. A., Lakhtakia, R., & Guillemin, G. (2013) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2013/685909 · Cited by 65 · see citing works
Control of Redox State and Redox Signaling by Neural Antioxidant Systems
Lewerenz, J., & Maher, P. A. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3600 · Cited by 57 · see citing works
Lei, X. G., & Cheng, W. (2005) · Journal of Nutrition · doi:10.1093/jn/135.10.2295 · Cited by 57 · see citing works
- Authors
- Esposito, L. A., Kokoszka, J. E., Waymire, K. G., Cottrell, B., MacGregor, G. R., & Wallace, D. C.
- Affiliations
- Emory University (US)
- Corresponding author
- Wallace, Douglas C.
- Venue
- Free Radical Biology and Medicine
- Publisher
- Elsevier BV
- Published
- 2000-03
- Volume
- 28
- Issue
- 5
- Pages
- 754-766
- ISSN
- 0891-5849 (ISSN-L)
- PMC
- PMC3049813
- OpenAlex
- W2002860741
- Cited by
- 228
- References
- 47
- Citations by year
- 2026: 5 · 2025: 3 · 2024: 3 · 2023: 5 · 2022: 5 · 2021: 4 · 2020: 9 · 2019: 5 · 2018: 11 · 2017: 7 · 2016: 5 · 2015: 3 · 2014: 8 · 2013: 10 · 2012: 6
- FWCI
- 5.43
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Free Radical Biology and Medicine (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institute on Aging (AG-13154, R01AG013154)
- National Institute of General Medical Sciences (T32GM008490)
- National Institute of Neurological Disorders and Stroke (NS-21328, R01NS021328)
- Eunice Kennedy Shriver National Institute of Child Health and Human Development (HD-36437, R01HD036437)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Health Sciences › Nursing › Nutrition and Dietetics › Selenium in Biological Systems
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Keywords
- glutathione peroxidase 1, mitochondrial oxidative stress, reactive oxygen species, oxidative phosphorylation, hydrogen peroxide, lipid peroxidation, growth retardation, liver mitochondria, respiratory control ratio, mitochondrial energy production, tissue-specific gene expression
- MeSH terms
- Glutathione Peroxidase GPX1, Animals, Base Sequence, Female, Free Radicals, Glutathione Peroxidase, Hydrogen Peroxide, Male, Mice, Inbred C57BL, Mitochondria, Mitochondria, Heart, Mitochondria, Liver, Oxygen Consumption, Pregnancy, DNA Primers, Mice, Knockout, Oxidative Stress, Mice, In Vitro Techniques
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