The DOI matches its Crossref record; 101 of the 101 references it cites were found in a registry or an index.
Advanced glycation endproducts: what is their relevance to diabetic complications?
Abstract
Glycation is a major cause of spontaneous damage to proteins in physiological systems. This is exacerbated in diabetes as a consequence of the increase in glucose and other saccharides derivatives in plasma and at the sites of vascular complications. Protein damage by the formation of early glycation adducts is limited to lysine side chain and N‐terminal amino groups whereas later stage adducts, advanced glycation endproducts (AGEs), modify these and also arginine and cysteine residues. Metabolic dysfunction in vascular cells leads to the increased formation of methylglyoxal which adds disproportionately to the glycation damage in hyperglycaemia. AGE‐modified proteins undergo cellular proteolysis leading to the formation and urinary excretion of glycation free adducts. AGEs may potentiate the development of diabetic complications by activation of cell responses by AGE‐modified proteins interacting with specific cell surface receptors, activation of cell responses by AGE free adducts, impairment of protein–protein and enzyme–substrate interactions by AGE residue formation, and increasing resistance to proteolysis of extracellular matrix proteins. The formation of AGEs is suppressed by intensive glycaemic control, and may in future be suppressed by thiamine and pyridoxamine supplementation, and several other pharmacological agents. Increasing expression of enzymes of the enzymatic defence against glycation provides a novel and potentially effective future therapeutic strategy to suppress protein glycation.
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Cites
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Cited by
The glycation of albumin: Structural and functional impacts
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Pathophysiology of the Diabetic Kidney
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Inhibition of Protein Glycation by Extracts of Culinary Herbs and Spices
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Self-citation
Metadata
- Authors
- Ahmed, N., & Thornalley, P. J.
- Venue
- Diabetes, Obesity and Metabolism
- Publisher
- Wiley
- Published
- 2006-04-21
- Volume
- 9
- Issue
- 3
- Pages
- 233-245
- ISSN
- 1462-8902 (ISSN-L)
- 1463-1326
- OpenAlex
- W2138774341
- Cited by
- 371
- References
- 101
- FWCI
- 13.16
- Type
- journal article
- Language
- en
- Open access
- closed
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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