The road to advanced glycation end products: a mechanistic perspective
Abstract
Protein glycation is a slow natural process involving the chemical modification of the reactive amino and guanidine functions in amino acids by sugars and carbohydrates-derived reactive carbonyls. Its deleterious consequences are obvious in the case of long-lived proteins in aged people and are exacerbated by the high blood concentration of sugars in diabetic patients. The non-enzymatic glycation of proteins occurs through a wide range of concurrent processes comprising condensation, rearrangement, fragmentation, and oxidation reactions. Using a few well established intermediates such as Schiff base, Amadori product and reactive a-dicarbonyls as milestones and the results of in vitro glycation investigations, an overall detailed mechanistic analysis of protein glycation is presented for the first time. The pathways leading to several advanced glycation end products (AGEs) such as (carboxymethyl)lysine, pentosidine, and glucosepane are outlined, whereas other AGEs useful as potential biomarkers of glycation are only briefly mentioned. The current stage of the development of glycation inhibitors has been reviewed with an emphasis on their mechanism of action.
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HbA1c is an advanced glycation end-product of hemoglobin, a principle protein in red blood cells.
“HbA1c is an advanced glycation end-product of hemoglobin, a principle protein in red blood cells (Figure 10).”
From KDIGO 2022 Clinical Practice Guideline for Diabetes Management in Chronic Kidney Disease (2022) · cites this paper as [223]
Hyperglycemia produces glycation of proteins and other molecular structures that eventuate in permanently glycated forms termed advanced glycation end-products.
“Hyperglycemia produces glycation of proteins and other molecular structures that eventuate in permanently glycated forms termed advanced glycation end-products.”
From KDIGO 2022 Clinical Practice Guideline for Diabetes Management in Chronic Kidney Disease (2022) · cites this paper as [223]
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RAGE-mediated inflammation in patients with septic shock
Hofer, S., Uhle, F., Fleming, T. H., Hell, C., Schmoch, T., Bruckner, T. M., Weigand, M. A., & Brenner, T. (2016) · Journal of Surgical Research · doi:10.1016/j.jss.2016.01.019 · Cited by 23 · see citing works
- Authors
- Cho, S.-J., Roman, G., Yeboah, F., & Konishi, Y.
- Affiliations
- Biotechnology Research Institute (CA)
- Corresponding author
- Konishi, Y.
- ORCID
- Roman, G.
- Venue
- Current Medicinal Chemistry
- Publisher
- Bentham Science Publishers Ltd.
- Published
- 2007-06-01
- Volume
- 14
- Issue
- 15
- Pages
- 1653-1671
- ISSN
- 0929-8673 (ISSN-L)
- OpenAlex
- W2112698509
- Cited by
- 213
- References
- 0
- Citations by year
- 2026: 4 · 2025: 15 · 2024: 13 · 2023: 21 · 2022: 13 · 2021: 16 · 2020: 6 · 2019: 12 · 2018: 10 · 2017: 11 · 2016: 17 · 2015: 5 · 2014: 7 · 2013: 16 · 2012: 14
- FWCI
- 5.06
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Current Medicinal Chemistry (publishedVersion)
- PubMed (publishedVersion)
- NPARC (submittedVersion)
- Funders
- Diabetes Action Research and Education Foundation
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Clinical Biochemistry › Advanced Glycation End Products research
- Life Sciences › Agricultural and Biological Sciences › Food Science › Potato Plant Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glycosylation and Glycoproteins Research
- Keywords
- advanced glycation end products, protein glycation, glycation, Schiff base, Amadori products, α-dicarbonyl compounds, carboxymethyllysine, pentosidine, glucosepane, glycation inhibitors, diabetes mellitus, aging, reactive carbonyl compounds
- MeSH terms
- Animals, Arabinose, Glucose, Humans, Proteins, Glycation End Products, Advanced, Oxidative Stress
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