Dicarbonyl stress in cell and tissue dysfunction contributing to ageing and disease
Open accessAbstract
Dicarbonyl stress is the abnormal accumulation of dicarbonyl metabolites leading to increased protein and DNA modification contributing to cell and tissue dysfunction in ageing and disease. Enzymes metabolising dicarbonyls, glyoxalase 1 and aldoketo reductases, provide an efficient and stress-response enzyme defence against dicarbonyl stress. Dicarbonyl stress is produced by increased formation and/or decreased metabolism of dicarbonyl metabolites, and by exposure to exogenous dicarbonyls. It contributes to ageing, disease and activity of cytototoxic chemotherapeutic agents.
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Glyoxal is mainly formed by oxidative degradation of carbohydrates, lipids, nucleotides, and serine.
“Although the latter mechanism is non-oxidative, the reactive precursor glyoxal is mainly formed by oxidative degradation of carbohydrates, lipids, nucleotides, and serine [37].”
From Protein oxidation - Formation mechanisms, detection and relevance as biomarkers in human diseases (2021) · cites this paper as [37]
Table 1 (appearing in our copy under Closing remarks) lists lipid peroxidation, oxidative degradation of serine, monosaccharide degradation, and nucleotide degradation as sources of glyoxal. It does not say that all four pathways are oxidative or that they are collectively the main sources; it also lists degradation of glycated proteins and food and beverages. (LLM, conf=0.84)
Experimental — accuracy not yet measuredThe scavenging capacity of the glyoxalase system can be overridden by an increase in dicarbonyl formation, leading to dicarbonyl stress and enhanced AGE production.
“However, the scavenging capacity of this system can be overridden by an increase in dicarbonyl forma-tion, leading to dicarbonyl stress which results in enhanced AGE production.[70,71]”
From The Role of Dietary Advanced Glycation End Products in Metabolic Dysfunction (2021) · cites this paper as [70]
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Research works printed but not linked: 1
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“Although the latter mechanism is non-oxidative, the reactive precursor glyoxal is mainly formed by oxidative degradation of carbohydrates, lipids, nucleotides, and serine [37].”
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Self-citation
- Authors
- Rabbani, N., & Thornalley, P. J.
- Affiliations
- University Hospital Coventry (GB)
- Corresponding author
- Thornalley, Paul J.
- Venue
- Biochemical and Biophysical Research Communications
- Publisher
- Elsevier BV
- Published
- 2015-03
- Volume
- 458
- Issue
- 2
- Pages
- 221-226
- ISSN
- 0006-291X (ISSN-L)
- OpenAlex
- W2022173379
- Cited by
- 353
- References
- 48
- Citations by year
- 2026: 19 · 2025: 26 · 2024: 39 · 2023: 16 · 2022: 39 · 2021: 38 · 2020: 34 · 2019: 36 · 2018: 25 · 2017: 40 · 2016: 32 · 2015: 9
- FWCI
- 3.50
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Biochemical and Biophysical Research Communications (publishedVersion, cc-by-nc-nd)
- PubMed (publishedVersion)
- Warwick Research Archive Portal (University of Warwick) (acceptedVersion)
- Funders
- Biotechnology and Biological Sciences Research Council (BB/D006295/2, BB/D006295/1)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Clinical Biochemistry › Advanced Glycation End Products research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Aldose Reductase and Taurine
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Keywords
- dicarbonyl stress, glyoxal, methylglyoxal, protein carbonylation, DNA modification, glyoxalase I, stress response, aging, disease, anticancer agents
- MeSH terms
- Aging, Aldehydes, Cardiovascular Diseases, Deoxyglucose, Diabetes Mellitus, Glyoxal, Humans, Inflammation, Kidney Diseases, Models, Biological, Pyruvaldehyde, Stress, Physiological, Oxidative Stress
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