Role of Oxidant Species in Aging
Abstract
Organisms are constantly exposed to many different forms of reactive oxygen species and reactive nitrogen species that damage proteins, nucleic acids, and lipids, leading to loss of biological function. The possibility that reactive oxygen/nitrogen-mediated protein damage contributes to the aging process is supported by results of many studies showing that aging is associated with the accumulation of such protein damage. Summarized here are results of studies, showing that the accumulation of,protein damage is a complex function of a multiplicity of factors that govern the intracellular levels of reactive oxygen/nitrogen species, on the one hand, and a multiplicity of factors that govern the degradation and/or repair of damaged proteins, on the other. Basic mechanisms involved in the modification of proteins by various forms of reactive oxygen/nitrogen species are also discussed.
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Protein carbonyls are protein modifications formed on side chains of proteins following the oxidation of proline, arginine, lysine, and threonine.
“Protein carbonyls, [C=O], (aldehydes or ketones) are protein modifications, formed on side chains of proteins following the oxidation of proline, arginine, lysine, and threonine.”
From Reactive Oxygen Species, Toxicity, Oxidative Stress, and Antioxidants: Chronic Diseases and Aging (2023) · cites this paper as Stadtman 2004
Protein carbonyls are structurally stable and suitable for chemical detection.
“These products are structurally stable and suitable for chemical detection (Stadtman 2004).”
From Reactive Oxygen Species, Toxicity, Oxidative Stress, and Antioxidants: Chronic Diseases and Aging (2023) · cites this paper as Stadtman 2004
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Valko, M., Rhodes, C. J., Moncol, J., Izakovic, M., & Mazur, M. (2006) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2005.12.009 · Cited by 6,680 · see citing works
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Birben, E., Şahiner, Ü. M., Saçkesen, C., ERZURUM, S. C., & Kalaycı, Ö. (2012) · World Allergy Organization Journal · doi:10.1097/wox.0b013e3182439613 · Cited by 4,960 · see citing works
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Jomova, K., Raptova, R., Alomar, S. Y., Alwasel, S. H., Nepovimova, E., Kuca, K., & Valko, M. (2023) · Archives of Toxicology · doi:10.1007/s00204-023-03562-9 · Cited by 2,638 · see citing works
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Trachootham, D., Lu, W., Ogasawara, M. A., Valle, N. R.-D., & Huang, P. (2008) · Antioxidants & Redox Signaling · doi:10.1089/ars.2007.1957 · Cited by 1,781 · see citing works
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Jan, A. T., Azam, M., Siddiqui, K., Ali, A., Choi, I., & Haq, Q. M. R. (2015) · International Journal of Molecular Sciences · doi:10.3390/ijms161226183 · Cited by 1,252 · see citing works
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Islam, M. T. (2016) · Neurological Research · doi:10.1080/01616412.2016.1251711 · Cited by 989 · see citing works
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BackgroundOxidative stress, mitochondrial dysfunction and neurodegenerative diseases; a mechanistic insight
Bhat, A. H., Dar, K. B., Anees, S., Zargar, M. A., Masood, A., Sofi, M. A., & Ganie, S. A. (2015) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2015.07.025 · Cited by 938 · see citing works
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Khansari, N., Shakiba, Y., & Mahmoudi, M. (2009) · Recent Patents on Inflammation & Allergy Drug Discovery · doi:10.2174/187221309787158371 · Cited by 922 · see citing works
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BackgroundKregel, K. C., & Zhang, H. J. (2007) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00327.2006 · Cited by 883 · see citing works
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Slimen, I. B., Najar, T., Ghram, A., Debbabi, H., Mrad, M. B., & Abderrabba, M. (2014) · International Journal of Hyperthermia · doi:10.3109/02656736.2014.971446 · Cited by 880 · see citing works
Lavie, L. (2014) · Sleep Medicine Reviews · doi:10.1016/j.smrv.2014.07.003 · Cited by 692 · see citing works
Systemic adaptation to oxidative challenge induced by regular exercise
Radak, Z., Chung, H. Y., & Goto, S. (2008) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2007.01.029 · Cited by 623 · see citing works
Oxidative stress and oxidative damage in chemical carcinogenesis
Klaunig, J. E., Wang, Z., Pu, X., & Zhou, S. (2011) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2009.11.028 · Cited by 475 · see citing works
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BackgroundRajjou, L., Lovigny, Y., Groot, S. P. C., Belghazi, M., Job, C., & Job, D. (2008) · PLANT PHYSIOLOGY · doi:10.1104/pp.108.123141 · Cited by 460 · see citing works
“Indeed, a progressive accumulation of oxidative damage of these macromolecules in aged tissues is thought to contribute to the decline in biological functions characteristic of the aged phenotype (Stadtman, 2001, 2004).”
BackgroundIndian medicinal herbs as sources of antioxidants
Ali, S. S., Kasoju, N., Luthra, A., Singh, A., Hallihosur, S., Sahu, A., & Bora, U. (2007) · Food Research International · doi:10.1016/j.foodres.2007.10.001 · Cited by 460 · see citing works
“Besides DNA ROS also attack other cellular components involving polyunsaturated fatty acid residues of phospholipids (Siems, Grune, & Esterbauer, 1995), side chains of all amino acid residues of proteins, in particular cysteine and methionine residues (Stadtman, 2004).”
BackgroundFREE RADICALS, ANTIOXIDANTS, DISEASES AND PHYTOMEDICINES: CURRENT STATUS AND FUTURE PROSPECT
Sen, S., Chakraborty, R., Sridhar, C., Reddy, Y. S., & De, B. (2010) · Cited by 378 · see citing works
Reactive oxygen species, nutrition, hypoxia and diseases: Problems solved?
Görlach, A., Dimova, E. Y., Petry, A., Martı́nez-Ruiz, A., Hernansanz‐Agustín, P., Rolo, A. P., Palmeira, C. M., & Kietzmann, T. (2015) · Redox Biology · doi:10.1016/j.redox.2015.08.016 · Cited by 351 · see citing works
Functional senescence in Drosophila melanogaster
Grotewiel, M. S., Martin, I., Bhandari, P., & Cook-Wiens, E. (2005) · Ageing Research Reviews · doi:10.1016/j.arr.2005.04.001 · Cited by 324 · see citing works
“It is possible that senescence of protein turnover might lead to the accumulation of defective proteins that in turn might influence aging (Stadtman, 2004).”
BackgroundOxidative stress, inflamm-aging and immunosenescence
Cannizzo, E. S., Clement, C. C., Sahu, R. K., Follo, C., & Santambrogio, L. (2011) · Journal of Proteomics · doi:10.1016/j.jprot.2011.06.005 · Cited by 303 · see citing works
“Protein carbonyls derive from oxidation of amino acid residues, amongwhich arginine, lysine and proline are themost targeted [79–82].”
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Das, B. C., Thapa, P., Karki, R., Schinke, C., Das, S., Kambhampati, S., Banerjee, S. K., Veldhuizen, P. J. V., Verma, A. K., Weiss, L. M., et al. (2013) · Future Medicinal Chemistry · doi:10.4155/fmc.13.38 · Cited by 279 · see citing works
Ziech, D., Franco, R., Georgakilas, A. G., Georgakila, S., Malamou‐Mitsi, V., Schoneveld, O., Pappa, A., & Panayiotidis, M. I. (2010) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2010.07.010 · Cited by 274 · see citing works
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Moulton, P. V., & Yang, W. (2012) · Journal of Environmental and Public Health · doi:10.1155/2012/472751 · Cited by 265 · see citing works
“This imbalance can result from exposure to pro-oxidant substances—ROS—present as air pollutants in the atmosphere [26, 57, 69].”
BackgroundProtein damage, repair and proteolysis
Chondrogianni, N., Petropoulos, I., Grimm, S., Georgila, K., Catalgol, B., Friguet, B., Grune, T., & Gonos, E. S. (2012) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2012.09.001 · Cited by 254 · see citing works
Mitochondrial oxidative stress, aging and caloric restriction: The protein and methionine connection
Pamplona, R., & Barja, G. (2006) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2006.01.009 · Cited by 255 · see citing works
Age-associated analysis of oxidative stress parameters in human plasma and erythrocytes
Gil, L., Siems, W., Mazurek, B., Gross, J., Schroeder, P., Voss, P., & Grune, T. (2006) · Free Radical Research · doi:10.1080/10715760600592962 · Cited by 242 · see citing works
Redox active metal-induced oxidative stress in biological systems
Jomová, K., Baroš, S., & Valko, M. (2012) · Transition Metal Chemistry · doi:10.1007/s11243-012-9583-6 · Cited by 244 · see citing works
Exercise Training Promotes SIRT1 Activity in Aged Rats
Ferrara, N., Rinaldi, B., Corbi, G., Conti, V., Stiuso, P., Boccuti, S., Rengo, G., Rossi, F., & Filippelli, A. (2007) · Rejuvenation Research · doi:10.1089/rej.2007.0576 · Cited by 238 · see citing works
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Oxidative Stress, Inflammaging, and Immunosenescence
Bauer, M. E., & la Fuente, M. D. (2013) · Elsevier eBooks · doi:10.1016/b978-0-12-397803-5.00004-6 · Cited by 229 · see citing works
Effects of Glucagon-Like Peptide-1 on Oxidative Stress and Nrf2 Signaling
Oh, Y., & Jun, H.-S. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms19010026 · Cited by 217 · 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
Oxidative stress and Alzheimer’s disease: dietary polyphenols as potential therapeutic agents
Darvesh, A. S., Carroll, R. T., Bishayee, A., Geldenhuys, W. J., & der Schyf, C. J. V. (2010) · Expert Review of Neurotherapeutics · doi:10.1586/ern.10.42 · Cited by 203 · see citing works
Iron, Ferritin, Hereditary Ferritinopathy, and Neurodegeneration
Muhoberac, B. B., & Vidal, R. (2019) · Frontiers in Neuroscience · doi:10.3389/fnins.2019.01195 · Cited by 196 · see citing works
“Additionally, modified proteins and their aggregates are associated with compromised proteasomal function inhibiting damaged protein clearance (Grune et al., 2001; Stadtman, 2004; Hipkiss, 2006; Radak et al., 2011).”
BackgroundCai, W., He, C., Zhu, L., Xue, C., Zheng, F., Striker, G. E., & Vlassara, H. (2008) · American Journal Of Pathology · doi:10.2353/ajpath.2008.080152 · Cited by 186 · see citing works
Kanti Das, T., Wati, M. R., & Fatima-Shad, K. (2014) · Archives of Neuroscience · doi:10.5812/archneurosci.20078 · Cited by 177 · see citing works
“4-hydroxy-2-nonenal (HNE) and malondialdehyde (MDA) as lipid peroxidation products are formed in mitochondria (Figure 1) (55).”
Oxidative and antioxidative mechanisms in oral cancer and precancer: A review
Choudhari, S. K., Chaudhary, M., Gadbail, A. R., Sharma, A., & Tekade, S. (2014) · Oral Oncology · doi:10.1016/j.oraloncology.2013.09.011 · Cited by 177 · see citing works
“Amino acid residue side chains are very susceptible to attack by ROS and RNS [51].”
BackgroundAntioxidants in Huntington's disease
Johri, A., & Beal, M. F. (2011) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2011.11.014 · Cited by 158 · see citing works
“The side chains of all amino acid residues of proteins, in particular cysteine and methionine residues of proteins are susceptible to oxidation by the action of ROS/reactive nitrogen species (RNS) [64].”
BackgroundOxidative stress, cellular senescence and ageing
Pole, A., Dimri, M., & Dimri, G. P. (2016) · AIMS molecular science · doi:10.3934/molsci.2016.3.300 · Cited by 158 · see citing works
Liu, J., & Ames, B. N. (2005) · Nutritional Neuroscience · doi:10.1080/10284150500047161 · Cited by 138 · see citing works
“The oxidation of methionine residues of proteins to methionine sulfoxide, which is readily reversed by the action of methionine sulfoxide reductase (Stadtman and Levine 2003, Stadtman et al. 2003), can be considered an antioxidant defense (Stadtman 2004a, b).”
BackgroundCurtis, C. N., Landis, G. N., Folk, D. G., Wehr, N. B., Hoe, N., Waskar, M., Abdueva, D. A., Skvortsov, D., Ford, D., Luu, A., et al. (2007) · Genome biology · doi:10.1186/gb-2007-8-12-r262 · Cited by 135 · see citing works
Clinical oxidation parameters of aging
Voß, P., & Siems, W. (2006) · Free Radical Research · doi:10.1080/10715760600953859 · Cited by 134 · see citing works
“It can be concluded that the measurement of protein bound carbonyls comprise a cheap, fast and reliable method to determine oxidative stress on protein level as the oxidative damage correlates well with aging and ever though with the severity of some diseases [63,69].”
BackgroundMethod“Hypothalamic Microinflammation” Paradigm in Aging and Metabolic Diseases
Cai, D., & Khor, S. (2019) · Cell Metabolism · doi:10.1016/j.cmet.2019.05.021 · Cited by 134 · see citing works
Tahara, E. B., de Barros, M. H., de Oliveira, G. A., Netto, L. E. S., & Kowaltowski, A. J. (2006) · The FASEB Journal · doi:10.1096/fj.06-6686com · Cited by 132 · see citing works
Lipid Raft Redox Signaling: Molecular Mechanisms in Health and Disease
Jin, S., Zhou, F., Katirai, F., & Li, P. (2011) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3619 · Cited by 129 · see citing works
“In the literature, ROS, oxygen-derived species, and oxidants are used interchangeably to refer to the same substances active in a biological system (149, 369, 381).”
Influence of reactive species on the modification of biomolecules generated from the soft plasma
Attri, P., Kumar, N., Park, J. H., et al. (2015) · Scientific Reports · doi:10.1038/srep08221 · Cited by 127 · see citing works
Sell, D. R., Strauch, C., Shen, W., & Monnier, V. M. (2007) · Biochemical Journal · doi:10.1042/bj20061645 · Cited by 126 · see citing works
Pamplona, R., & Barja, G. (2007) · Ageing Research Reviews · doi:10.1016/j.arr.2007.06.002 · Cited by 126 · see citing works
Pathophysiological importance of aggregated damaged proteins
Höhn, A., Jung, T., & Grune, T. (2014) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2014.02.028 · Cited by 126 · see citing works
Clinical pharmacology and therapeutic use of antioxidant vitamins
Rodrigo, R., Guichard, C., & Charles, R. (2007) · Fundamental & Clinical Pharmacology · doi:10.1111/j.1472-8206.2006.00466.x · Cited by 124 · see citing works
Oxidized proteins: Mechanisms of removal and consequences of accumulation
Dunlop, R. A., Brunk, U. T., & Rodgers, K. J. (2009) · IUBMB Life · doi:10.1002/iub.189 · Cited by 124 · see citing works
“tionally, increased levels of oxidized proteins are observable in tissues from older animals (42), whereas caloric restriction designed to increase life-span results in a reduction in the extent of protein damage (43).”
BackgroundKnasmüller, S., Nersesyan, A., Mišík, M., Gerner, C., Mikulits, W., Ehrlich, V. A., Hoelzl, C., Szakmary, A., & Wagner, K. (2008) · British Journal of Nutrition · doi:10.1017/s0007114508965752 · Cited by 102 · see citing works
Jiang, G., Hu, Y., Liu, L., Cai, J., Peng, C., & Li, Q. (2014) · Neurochemistry International · doi:10.1016/j.neuint.2014.06.003 · Cited by 122 · see citing works
Linnane, A. W., Kios, M., & Vitetta, L. (2007) · Biogerontology · doi:10.1007/s10522-007-9096-4 · Cited by 114 · see citing works
“For considerations embracing the concept of mischievous oxidative damage to proteins as a major contributor to the aging process consult Stadtman (2004).”
BackgroundHypothalamic microinflammation: a common basis of metabolic syndrome and aging
Tang, Y., Purkayastha, S., & Cai, D. (2014) · Trends in Neurosciences · doi:10.1016/j.tins.2014.10.002 · Cited by 109 · see citing works
Grimm, S., Höhn, A., Davies, K. J. A., & Grune, T. (2010) · Free Radical Research · doi:10.3109/10715762.2010.512040 · Cited by 108 · see citing works
Islets and their antioxidant defense
Acharya, J. D., & Ghaskadbi, S. (2010) · Islets · doi:10.4161/isl.2.4.12219 · Cited by 108 · see citing works
Multimarker Screening of Oxidative Stress in Aging
Syslová, K., Böhmová, A., Mikoška, M., Kuzma, M., Pelclová, D., & Kačer, P. (2014) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2014/562860 · Cited by 102 · see citing works
“Considering this, the free radical theory was modified to oxidative stress theory of aging [5, 6].”
BackgroundAmelioration of oxidant stress by the defensin lysozyme
Liu, H., Zheng, F., Cao, Q., Ren, B., Zhu, L., Striker, G. E., & Vlassara, H. (2005) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00349.2005 · Cited by 106 · see citing works
“UNDER NORMAL CONDITIONS, where the levels of reactive oxygen species (ROS) are tightly regulated and play a role in normal metabolism, the body’s antioxidant defenses are able to successfully manage nonpathological amounts of exogenous or endogenous oxidants from reactive oxygen/nitrogen species (43).”
BackgroundInfluentialMitochondrially encoded cysteine predicts animal lifespan
Moosmann, B., & Behl, C. (2007) · Aging Cell · doi:10.1111/j.1474-9726.2007.00349.x · Cited by 104 · see citing works
“Protein oxidation is thought to constitute an important trigger of the aging process (Sohal, 2002; Stadtman, 2004).”
BackgroundOxidative Stress and Carcinogenesis: Potential of Phytochemicals in Breast Cancer Therapy
Forcados, G. E., James, D. B., Sallau, A. B., Muhammad, A. I., & Mabeta, P. (2017) · Nutrition and Cancer · doi:10.1080/01635581.2017.1267777 · Cited by 104 · see citing works
Nonenzymatic posttranslational protein modifications in ageing
Šoškić, V., Groebe, K., & Schrattenholz, A. S. (2008) · Experimental Gerontology · doi:10.1016/j.exger.2007.12.001 · Cited by 101 · see citing works
Utrera, M., Morcuende, D., & Estévez, M. (2013) · LWT · doi:10.1016/j.lwt.2013.10.040 · Cited by 100 · see citing works
Samoylenko, A., Hossain, J. A., Mennerich, D., Kellokumpu, S., Hiltunen, J. K., & Kietzmann, T. (2013) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.4662 · Cited by 102 · see citing works
“The abstraction of a hydrogen atom leads to the formation of a carbon-centered radical initiating the formation of various products such as peroxyl radicals, alkyl peroxide, and alkoxyl radicals (338).”
Astaxanthin protects against MPP+-induced oxidative stress in PC12 cells via the HO-1/NOX2 axis
Ye, Q., Huang, B., Zhang, X., Zhu, Y., & Chen, X. (2012) · BMC Neuroscience · doi:10.1186/1471-2202-13-156 · Cited by 100 · see citing works
Tashiro, J., Elliot, S. J., Gerth, D. J., Xia, X., Pereira‐Simon, S., Choi, R., Catanuto, P., Shahzeidi, S., Toonkel, R. L., Shah, R. H., et al. (2015) · Translational research · doi:10.1016/j.trsl.2015.09.004 · Cited by 98 · see citing works
Age-Related Oxidative Stress Compromises Endosomal Proteostasis
Cannizzo, E. S., Clement, C. C., Morozova, K., Valdor, R., Kaushik, S., Almeida, L. N., Follo, C., Sahu, R., Cuervo, A. M., Macian, F., et al. (2012) · Cell Reports · doi:10.1016/j.celrep.2012.06.005 · Cited by 95 · see citing works
“…compartments with oxidatively damaged proteins and protein/lipid microaggregates could interfere with efficient Cell Reports 2, 136–149, July 26, 2012 ª2012 The Authors 145 endosomal proteostasis (Stadtman, 1992, 2004; Cloos and Christgau, 2004; Dunlop et al., 2008, 2009; Tyedmers et al., 2010).”
Proresolving Lipid Mediators: Endogenous Modulators of Oxidative Stress
Leuti, A., Maccarrone, M., & Chiurchiù, V. (2019) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2019/8107265 · Cited by 90 · see citing works
“Even though ROS and RNS mediate many physiological functions and are deeply involved in tissue and cellular homeostasis, from inflammation and immune responses to control of cell signalling and neurotransmission, an excessive and persistent production causes massive lipid peroxidation [14], protein oxidation, and nitr…”
BackgroundLiu, G.-F., Filipović, M. R., Heinemann, F. W., & Ivanović‐Burmazović, I. (2007) · Inorganic Chemistry · doi:10.1021/ic7012039 · Cited by 88 · see citing works
Involvement of 4‐hydroxy‐2‐nonenal in pollution‐induced skin damage
Pecorelli, A., Woodby, B. L., Prieux, R., & Valacchi, G. (2019) · BioFactors · doi:10.1002/biof.1513 · Cited by 88 · see citing works
Oxidative stress in aging: Theoretical outcomes and clinical evidences in humans
del Valle, L. G. (2011) · Biomedicine & Aging Pathology · doi:10.1016/j.biomag.2011.03.001 · Cited by 85 · see citing works
Aryal, B., Jeong, J., & Rao, V. A. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1321783111 · Cited by 83 · see citing works
Ruangthai, R., & Phoemsapthawee, J. (2019) · Journal of Exercise Science & Fitness · doi:10.1016/j.jesf.2019.03.001 · Cited by 85 · see citing works
Role of free radicals in human inflammatory diseases
Biswas, S., Das, R., & Banerjee, E. R. (2017) · AIMS Biophysics · doi:10.3934/biophy.2017.4.596 · Cited by 92 · see citing works
Antioxidant Activity of Centella asiatica (Linn.) Urban: Impact of Extraction Solvent Polarity
Rahman, M., Hossain, S., Rahaman, K. A., et al. (2013) · Journal of Pharmacognosy and Phytochemistry · Cited by 80 · see citing works
Neutrophils and the Systemic Inflammatory Response Syndrome (SIRS)
Sikora, J. P., Karawani, J., & Sobczak, J. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241713469 · Cited by 87 · see citing works
Free radicals in the regulation of damage and cell death - basic mechanisms and prevention.
Silva, J. P., & Coutinho, O. P. (2010) · PubMed · Cited by 78 · see citing works
Relation of plasma protein oxidation parameters and paraoxonase activity in the ageing population
Çakatay, U., Kayalı, R., & Uzun, H. (2008) · Clinical and Experimental Medicine · doi:10.1007/s10238-008-0156-0 · Cited by 75 · see citing works
Hong, J., Chen, T., Hu, P., et al. (2014) · Journal of Functional Foods · doi:10.1016/j.jff.2014.05.014 · Cited by 72 · see citing works
Oxidative Stress and Antioxidant Defense in Plants Exposed to Metal/Metalloid Toxicity
Ali, M. A., Fahad, S., Haider, I., Ahmed, N., Ahmad, S., Hussain, S., & Arshad, M. (2019) · Wiley eBooks · doi:10.1002/9781119468677.ch15 · Cited by 88 · see citing works
Pinocembrin Attenuates 6-OHDA-induced Neuronal Cell Death Through Nrf2/ARE Pathway in SH-SY5Y Cells
Jin, X., Liu, Q., Jia, L., Li, M., & Wang, X. (2014) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-014-0128-8 · Cited by 69 · see citing works
Utrera, M., Morcuende, D., Ganhão, R., et al. (2014) · Food and Bioprocess Technology · doi:10.1007/s11947-014-1450-3 · Cited by 69 · see citing works
“The oxidative deamination by metal-catalyzed reactions of lysine residues yields to the formation of AAS (Stadtman 2004).”
BackgroundInfluentialЦубер, В. Ю., Kadamov, Y., & Lm, T. (2014) · PLoS ONE · doi:10.1371/journal.pone.0115048 · Cited by 68 · see citing works
Rationale for Antioxidant Supplementation in Sarcopenia
Cerullo, F., Gambassi, G., & Cesari, M. (2012) · Journal of Aging Research · doi:10.1155/2012/316943 · Cited by 67 · see citing works
“According to the cellular constituents attacked by the oxidative stress, lipid peroxidation [28], protein oxidation [29], and DNA damage [30] will all promote abnormalities of the cell structures incompatible with proper cell function, leading to its death.”
BackgroundAging, sex differences, and oxidative stress in human respiratory and limb muscles.
Barreiro, E., Coronell, C., Lavina, B., Ramírez-Sarmiento, A., Orozco-Levi, M., & Gea, J. (2006) · Free Radical Biology & Medicine · doi:10.1016/j.freeradbiomed.2006.05.027 · Cited by 69 · see citing works
“In fact, aging has also been attributed to a greater accumulation of deleterious effects on tissues from reactive oxygen species (ROS) compared to those normally neutralized by intracellular antioxidant defenses [9,10].”
BackgroundProtein stress and stress proteins: implications in aging and disease
Sőti, C., & Csermely, P. (2007) · Journal of Biosciences · doi:10.1007/s12038-007-0050-z · Cited by 66 · see citing works
“Similarly, while cells with proteasome inhibition may eventually escape cell cycle arrest (Bence et al 2001) and maintain normal protein turnover, age-dependent decrease in proteasome activity promotes Huntingtin aggregation (Zhou et al 2003).”
BackgroundAlexander, J. E., Colyer, A., Haydock, R., Hayek, M. G., & Park, J. (2017) · The Journals of Gerontology Series A · doi:10.1093/gerona/glx182 · Cited by 65 · see citing works
“Increased oxidative stress, resulting from an imbalance between the production and exposure to ROS and the host’s antioxidant defenses, is one proposed cause of senescence (43).”
BackgroundWong, Y. T., Gruber, J., Jenner, A. M., Ng, M. P.-E., Ruan, R., & Tay, F. E. H. (2009) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2008.12.016 · Cited by 63 · see citing works
Singh, P., Barman, B., & Thakur, M. K. (2022) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2022.944697 · Cited by 69 · see citing works
“Oxidative radical-induced damage to the protein backbone results in the formation of peroxyl radicals which ultimately cause fragmentation of the protein backbone (Stadtman, 1992, 2004; Grimm et al., 2011; Reeg and Grune, 2015).”
BackgroundScharf, B., Clement, C. C., Yodmuang, S., Urbanska, A. M., Suadicani, S. O., Aphkhazava, D., Thi, M. M., Perino, G., Hardin, J., COBELLI, N. J., et al. (2013) · Chemistry & Biology · doi:10.1016/j.chembiol.2013.06.006 · Cited by 61 · see citing works
“Cross-linkages can occur via disulfide bond formation between two oxidized cysteines or by Schiff base formation from the reaction of an amine group with a carbonyl (aldehyde or ketone) group of another protein (Oliver et al., 1987; Stadtman, 1992, 2004).”
BackgroundMale rats exhibit higher oxidative protein damage than females of the same chronological age
Kayalı, R., Çakatay, U., & Tekeli, F. (2007) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2007.03.003 · Cited by 60 · see citing works
Effect of Acupuncture on Oxidative Stress Induced by Cerebral Ischemia-Reperfusion Injury
Chen, C.-H., & Hsieh, C. (2020) · Antioxidants · doi:10.3390/antiox9030248 · Cited by 59 · see citing works
“The side chain of amino acid residues attacked by ROS may lead to the dysfunction of the protein and the enzyme, and contributing to the alteration of membrane permeability [27].”
BackgroundPark, S. W., Lee, C. H., Lee, J. G., Kim, L. W., Shin, B. S., Lee, B. J., & Kim, Y. H. (2011) · Neuroscience Research · doi:10.1016/j.neures.2011.01.004 · Cited by 59 · see citing works
“Excessive accumulation of ROS and inefficiency of the antioxidant enzyme system can damage DNA and induce lipid peroxidation and protein modification, causing cellular dysfunction and even apoptosis (Lohr and Browning, 1995; Stadtman, 2004).”
Vlassara, H., Uribarri, J., Ferrucci, L., Cai, W., Torreggiani, M., Post, J. B., Zheng, F., & Striker, G. E. (2009) · Seminars in Nephrology · doi:10.1016/j.semnephrol.2009.07.013 · Cited by 59 · see citing works
“These data highlighted the following: (1) there is considerable heterogeneity in the presence and degree of renal function decline in aging; (2) the measurement of glomerular filtration rate in aging needs further refinement; (3) dietary AGEs are significant contributors to the nascent AGE pool of healthy persons; (4)…”
BackgroundOxidative stress—implications, source and its prevention
Kaur, R., Kaur, J., Mahajan, J., Kumar, R., & Arora, S. (2013) · Environmental Science and Pollution Research · doi:10.1007/s11356-013-2251-3 · Cited by 59 · see citing works
Should Red Wine Be Considered a Functional Food?
Yoo, Y. J., Saliba, A. J., & Prenzler, P. D. (2010) · Comprehensive Reviews in Food Science and Food Safety · doi:10.1111/j.1541-4337.2010.00125.x · Cited by 56 · see citing works
“Adapted from Erdman and others (2007).”
BackgroundInfluentialRole of Protein Carbonylation in Skeletal Muscle Mass Loss Associated with Chronic Conditions
Barreiro, E. (2016) · Proteomes · doi:10.3390/proteomes4020018 · Cited by 56 · see citing works
Li, P., & Zhang, Y. (2013) · Handbook of experimental pharmacology · doi:10.1007/978-3-7091-1511-4_9 · Cited by 55 · see citing works
“Therefore, in general, redox signaling is often referred to as the signaling induced by ROS (Halliwell and Cross 1994; Stadtman 2004; Tang et al. 2002).”
Oxidative Stress in Aging: Advances in Proteomic Approaches
Ortuño‐Sahagún, D., Pallàs, M., & Rojas-Mayorquín, A. E. (2014) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2014/573208 · Cited by 55 · see citing works
“ROS increase oxidative stress [13–15] and reactive nitrogen species (RNS) yield nitrosative stress [15].”
- Authors
- Stadtman, E. R.
- Affiliations
- National Institutes of Health (US)
- Corresponding author
- Stadtman, Earl R.
- Venue
- Current Medicinal Chemistry
- Publisher
- Bentham Science Publishers Ltd.
- Published
- 2004-05-01
- Volume
- 11
- Issue
- 9
- Pages
- 1105-1112
- ISSN
- 0929-8673 (ISSN-L)
- OpenAlex
- W2030135352
- Cited by
- 368
- References
- 0
- Citations by year
- 2026: 1 · 2025: 6 · 2024: 6 · 2023: 4 · 2022: 14 · 2021: 20 · 2020: 21 · 2019: 13 · 2018: 13 · 2017: 18 · 2016: 16 · 2015: 22 · 2014: 26 · 2013: 35 · 2012: 29
- FWCI
- 5.09
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Current Medicinal Chemistry (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Aging › Genetics, Aging, and Longevity in Model Organisms
- Health Sciences › Medicine › Biochemistry › Antioxidant Activity and Oxidative Stress
- Keywords
- aging, reactive oxygen species, reactive nitrogen species, protein damage, protein oxidation, protein degradation, protein repair, lipid peroxidation, nucleic acid damage
- MeSH terms
- Aging, Amino Acids, Animals, Humans, Nitric Oxide, Oxidation-Reduction, Peptides, Proteins, Reactive Oxygen Species, Oxidative Stress, Reactive Nitrogen Species, Peroxynitrous Acid
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