Protein Oxidation in Aging and Age‐Related Diseases
Abstract
Although different theories have been proposed to explain the aging process, it is generally agreed that there is a correlation between aging and the accumulation of oxidatively damaged proteins, lipids, and nucleic acids. Oxidatively modified proteins have been shown to increase as a function of age. Studies reveal an age-related increase in the level of protein carbonyl content, oxidized methionine, protein hydrophobicity, and cross-linked and glycated proteins as well as the accumulation of less active enzymes that are more susceptible to heat inactivation and proteolytic degredation. Factors that decelerate protein oxidation also increase the life span of animals and vice versa. Furthermore, a number of age-related diseases have been shown to be associated with elevated levels of oxidatively modified proteins. The chemistry of reactive oxygen species-mediated protein modification will be discussed. The accumulation of oxidatively modified proteins may reflect deficiencies in one or more parameters of a complex function that maintains a delicate balance between the presence of a multiplicity of prooxidants, antioxidants, and repair, replacement, or elimination of biologically damaged proteins.
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Most of these pathologic conditions increase as a function of age.
“It has been shown that most of these pathologic conditions increase as a function of age, indicating that oxidation of proteins occurs simultaneously to aging and age-related diseases [[109], [110], [111]].”
From Protein oxidation - Formation mechanisms, detection and relevance as biomarkers in human diseases (2021) · cites this paper as [109]
Oxidation of proteins occurs simultaneously with aging and age-related diseases.
“It has been shown that most of these pathologic conditions increase as a function of age, indicating that oxidation of proteins occurs simultaneously to aging and age-related diseases [[109], [110], [111]].”
From Protein oxidation - Formation mechanisms, detection and relevance as biomarkers in human diseases (2021) · cites this paper as [109]
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- Authors
- Stadtman, E. R.
- Affiliations
- National Institutes of Health (US)
- Corresponding author
- Stadtman, Earl R.
- Venue
- Annals of the New York Academy of Sciences
- Publisher
- Wiley
- Published
- 2001-04
- Volume
- 928
- Issue
- 1
- Pages
- 22-38
- ISSN
- 0077-8923 (ISSN-L)
- 1749-6632
- OpenAlex
- W1975621743
- Cited by
- 660
- References
- 4
- Citations by year
- 2026: 1 · 2025: 7 · 2024: 8 · 2023: 19 · 2022: 23 · 2021: 21 · 2020: 22 · 2019: 22 · 2018: 19 · 2017: 17 · 2016: 27 · 2015: 26 · 2014: 19 · 2013: 34 · 2012: 41
- FWCI
- 3.86
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Annals of the New York Academy of Sciences (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Aging › Genetics, Aging, and Longevity in Model Organisms
- Health Sciences › Medicine › Biochemistry › Antioxidant Activity and Oxidative Stress
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Keywords
- protein oxidation, aging, age-related diseases, protein carbonylation, oxidized methionine, protein hydrophobicity, protein cross-linking, protein glycation, reactive oxygen species, antioxidants, pro-oxidants, enzyme inactivation, lifespan, oxidative damage
- MeSH terms
- Aging, Amino Acids, Animals, Antioxidants, Cross-Linking Reagents, Cysteine, Disease, Humans, Longevity, Methionine, Models, Biological, Nitric Oxide, Oxidation-Reduction, Peptides, Protein Denaturation, Proteins, Tyrosine, Oxidants, Apoptosis, Reactive Oxygen Species, Oxidative Stress, Peroxynitrous Acid, Rats
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