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The Importance of Proteins in Defense Against Oxidation
Abstract
Free radicals are a normal feature of cellular oxygen metabolism. However, free radical-associated damage is an important factor in many pathological and toxicological processes. For a long time, lipid peroxidation, mediated by oxygen-derived free radicals, was probably the most extensively investigated process. From more recent studies, it has become evident that proteins are also the targets of free radicals, and this has important implication for their activity, unfolding, and degradation, as well as in cell functioning. After giving a brief overview of the key role of proteins in the overall antioxidant defense, this review examines their role as targets of oxidation reactions, taking into account the reactivity of amino acid residues and some of their oxidation products. In light of recent data, we then consider the specific role of sulfur-containing amino acids in protein degradation and their possible interplay with the reversal of limited oxidative lesions. The participation of proteins in the overall antioxidant defense is also discussed, specifically the role of metallothionein as an intracellular antioxidant and that of albumin as a circulating antioxidant.
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“Albumin is considered to be quantitatively the most important extracellular antioxidant, representing almost three‐quarters of the antioxidant capacity of plasma.92”
From Hypoalbuminemia: Pathogenesis and Clinical Significance (2019) · cites this paper as [92]
Citations
Cites
Ellman, G. L. (1959) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(59)90090-6 · Cited by 26,824
Chemistry and biochemistry of 4-hydroxynonenal, malonaldehyde and related aldehydes
Esterbauer, H., Schaur, R. J., & Zollner, H. (1991) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(91)90192-6 · Cited by 6,672
A Quantitative Assessment of Plasma Homocysteine as a Risk Factor for Vascular Disease
Boushey, C. J. (1995) · JAMA · doi:10.1001/jama.1995.03530130055028 · Cited by 3,708
Superoxide radical and superoxide dismutases
Fridovich, I. (1995) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.64.070195.000525 · Cited by 3,455
Protein Oxidation in Aging, Disease, and Oxidative Stress
Berlett, B. S., & Stadtman, E. R. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.33.20313 · Cited by 3,379
Miller, N. J., Rice-Evans, C. A., Davies, M. J., Gopinathan, V., & Milner, A. D. (1993) · Clinical Science · doi:10.1042/cs0840407 · Cited by 3,108
All About Albumin: Biochemistry, Genetics, and Medical Applications
Peters, T. (1995) · Thammasat University Digital Collections · Cited by 3,089
Advanced Glycosylation End Products in Tissue and the Biochemical Basis of Diabetic Complications
Flier, J. S., Underhill, L. H., Brownlee, M., Cerami, A., & Vlassara, H. (1988) · New England Journal of Medicine · doi:10.1056/nejm198805193182007 · Cited by 2,512
The role of lipid peroxidation and antioxidants in oxidative modification of LDL
Esterbauer, H., Gebicki, J. M., Puhl, H., & Jürgens, G. (1992) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(92)90181-f · Cited by 2,307
Antioxidants in Human Health and Disease
Halliwell, B. B. (1996) · Annual Review of Nutrition · doi:10.1146/annurev.nu.16.070196.000341 · Cited by 1,852
Research works printed but not linked: 7
- Ciorba MA, 1999, Proc Natl Acad Sci U S A, 93, 15306
- Evans MD, 1994, Am J Physiol, 266, L593
- McCully KS, 1983, Atheroscler Rev, 11, 157
- Montgomery DAD, 1962, Clin Sci, 22, 141
- Pitt BR, 1997, Am J Physiol, 273, L856
- Rosenblatt DS, 1995, New York, 3111
- Stafforini DM, 1994, J Lipid Mediat, 10, 53
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Liu, J., & Ames, B. N. (2005) · Nutritional Neuroscience · doi:10.1080/10284150500047161 · Cited by 138
Davila, M. P., Muñoz, P. M., Bolaños, J. M. G., Stout, T. A. E., Gadella, B. M., Tapia, J. A., da Silva, C. B., Ortega‐Ferrusola, C., & Peña, F. J. (2016) · Reproduction · doi:10.1530/rep-16-0409 · Cited by 137
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Bourdon, E., Loreau, N., Lagrost, L., & Blache, D. (2005) · Free Radical Research · doi:10.1080/10715760400024935 · Cited by 132
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Colombo, G., Aldini, G., Orioli, M., Giustarini, D., Gornati, R., Rossi, R., Colombo, R., Carini, M., Milzani, A., & Dalle‐Donne, I. (2009) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2806 · Cited by 70
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Altomare, A., Baron, G., Brioschi, M., Longoni, M., Riccardo, B., Edoardo, V., Tremoli, E., Carini, M., Agostoni, P., Vistoli, G., et al. (2020) · Antioxidants · doi:10.3390/antiox9050367 · Cited by 45
Montgomery, M. K., Buttemer, W. A., & Hulbert, A. J. (2012) · Experimental Gerontology · doi:10.1016/j.exger.2011.11.014 · Cited by 44
Guerreiro, G., Faverzani, J. L., Jacques, C. E. D., Marchetti, D. P., Sitta, Â., Coelho, D. D. M., Kayser, A., Kok, F., de Athayde, L. S., Manfredini, V., et al. (2018) · Journal of Cellular Biochemistry · doi:10.1002/jcb.27332 · Cited by 44
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Yones, D. A., Zaghlol, K., Abdallah, A. M., & Galal, L. (2014) · Tropical parasitology · doi:10.4103/2229-5070.145581 · Cited by 42
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Wei, L., Sui, H., Zhang, J., & Guo, Z. (2021) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2021.06.148 · Cited by 32
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Metadata
- Authors
- Bourdon, E., & Blache, D.
- Affiliations
- Inserm (FR)
- ORCID
- Bourdon, Emmanuel
- Venue
- Antioxidants & Redox Signaling
- Publisher
- SAGE Publications
- Published
- 2001-04
- Volume
- 3
- Issue
- 2
- Pages
- 293-311
- ISSN
- 1523-0864 (ISSN-L)
- 1557-7716
- OpenAlex
- W1611625030
- Cited by
- 220
- References
- 124
- Citations by year
- 2026: 5 · 2025: 8 · 2024: 9 · 2023: 12 · 2022: 9 · 2021: 13 · 2020: 12 · 2019: 6 · 2018: 18 · 2017: 6 · 2016: 15 · 2015: 13 · 2014: 14 · 2013: 13 · 2012: 8
- FWCI
- 1.28
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Antioxidants and Redox Signaling (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Institut National de la Santé et de la Recherche Médicale
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Health Sciences › Medicine › Biochemistry (medical) › Antioxidant Activity and Oxidative Stress
- Physical Sciences › Chemistry › Organic Chemistry › Free Radicals and Antioxidants
- Keywords
- protein oxidation, antioxidant defense, free radicals, lipid peroxidation, protein unfolding, protein degradation, sulfur-containing amino acids, metallothionein, albumin, oxidative damage
- MeSH terms
- Animals, Antioxidants, Oxidation-Reduction, Proteins
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