Tags

Type your tag names separated by a space and hit enter

Diabetic threesome (hyperglycaemia, renal function and nutrition) and advanced glycation end products: evidence for the multiple-hit agent?
Proc Nutr Soc. 2008 Feb; 67(1):60-74.PN

Abstract

Complex chemical processes termed non-enzymic glycation that operate in vivo and similar chemical interactions between sugars and proteins that occur during thermal processing of food (known as the Maillard reaction) are one of the interesting examples of a potentially-harmful interaction between nutrition and disease. Non-enzymic glycation comprises a series of reactions between sugars, alpha-oxoaldehydes and other sugar derivatives and amino groups of amino acids, peptides and proteins leading to the formation of heterogeneous moieties collectively termed advanced glycation end products (AGE). AGE possess a wide range of chemical and biological properties and play a role in diabetes-related pathology as well as in several other diseases. Diabetes is, nevertheless, of particular interest for several reasons: (1) chronic hyperglycaemia provides the substrates for extracellular glycation as well as intracellular glycation; (2) hyperglycaemia-induced oxidative stress accelerates AGE formation in the process of glycoxidation; (3) AGE-modified proteins are subject to rapid intracellular proteolytic degradation releasing free AGE adducts into the circulation where they can bind to several pro-inflammatory receptors, especially receptor of AGE; (4) kidneys, which are principally involved in the excretion of free AGE adducts, might be damaged by diabetic nephropathy, which further enhances AGE toxicity because of diminished AGE clearance. Increased dietary intake of AGE in highly-processed foods may represent an additional exogenous metabolic burden in addition to AGE already present endogenously in subjects with diabetes. Finally, inter-individual genetic and functional variability in genes encoding enzymes and receptors involved in either the formation or the degradation of AGE could have important pathogenic, nutrigenomic and nutrigenetic consequences.

Authors+Show Affiliations

Department of Pathophysiology, Faculty of Medicine, Masaryk University, Komenského nám 2, 662 43 Brno, Czech Republic. kankov@med.muni.cz

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't
Review

Language

eng

PubMed ID

18234133

Citation

Kanková, Katerina. "Diabetic Threesome (hyperglycaemia, Renal Function and Nutrition) and Advanced Glycation End Products: Evidence for the Multiple-hit Agent?" The Proceedings of the Nutrition Society, vol. 67, no. 1, 2008, pp. 60-74.
Kanková K. Diabetic threesome (hyperglycaemia, renal function and nutrition) and advanced glycation end products: evidence for the multiple-hit agent? Proc Nutr Soc. 2008;67(1):60-74.
Kanková, K. (2008). Diabetic threesome (hyperglycaemia, renal function and nutrition) and advanced glycation end products: evidence for the multiple-hit agent? The Proceedings of the Nutrition Society, 67(1), 60-74. https://doi.org/10.1017/S0029665108006034
Kanková K. Diabetic Threesome (hyperglycaemia, Renal Function and Nutrition) and Advanced Glycation End Products: Evidence for the Multiple-hit Agent. Proc Nutr Soc. 2008;67(1):60-74. PubMed PMID: 18234133.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Diabetic threesome (hyperglycaemia, renal function and nutrition) and advanced glycation end products: evidence for the multiple-hit agent? A1 - Kanková,Katerina, PY - 2008/2/1/pubmed PY - 2008/8/20/medline PY - 2008/2/1/entrez SP - 60 EP - 74 JF - The Proceedings of the Nutrition Society JO - Proc Nutr Soc VL - 67 IS - 1 N2 - Complex chemical processes termed non-enzymic glycation that operate in vivo and similar chemical interactions between sugars and proteins that occur during thermal processing of food (known as the Maillard reaction) are one of the interesting examples of a potentially-harmful interaction between nutrition and disease. Non-enzymic glycation comprises a series of reactions between sugars, alpha-oxoaldehydes and other sugar derivatives and amino groups of amino acids, peptides and proteins leading to the formation of heterogeneous moieties collectively termed advanced glycation end products (AGE). AGE possess a wide range of chemical and biological properties and play a role in diabetes-related pathology as well as in several other diseases. Diabetes is, nevertheless, of particular interest for several reasons: (1) chronic hyperglycaemia provides the substrates for extracellular glycation as well as intracellular glycation; (2) hyperglycaemia-induced oxidative stress accelerates AGE formation in the process of glycoxidation; (3) AGE-modified proteins are subject to rapid intracellular proteolytic degradation releasing free AGE adducts into the circulation where they can bind to several pro-inflammatory receptors, especially receptor of AGE; (4) kidneys, which are principally involved in the excretion of free AGE adducts, might be damaged by diabetic nephropathy, which further enhances AGE toxicity because of diminished AGE clearance. Increased dietary intake of AGE in highly-processed foods may represent an additional exogenous metabolic burden in addition to AGE already present endogenously in subjects with diabetes. Finally, inter-individual genetic and functional variability in genes encoding enzymes and receptors involved in either the formation or the degradation of AGE could have important pathogenic, nutrigenomic and nutrigenetic consequences. SN - 0029-6651 UR - https://www.unboundmedicine.com/medline/citation/18234133/Diabetic_threesome__hyperglycaemia_renal_function_and_nutrition__and_advanced_glycation_end_products:_evidence_for_the_multiple_hit_agent DB - PRIME DP - Unbound Medicine ER -