Advanced Glycation End products (AGEs)

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Advanced Glycation End products

The role of AGEs in aging: causation or correlation
Over a dozen advanced glycation end-products (AGEs) have been identified in tissue proteins by chemical or immunological methods. Of these, about half are known to accumulate with age in collagen at a rate that correlates with the half-life of the collagen. Although AGEs in proteins are probably correlative, rather than causative, with respect to aging, they accumulate to high levels in tissues in age-related chronic diseases, such as atherosclerosis, diabetes, arthritis and neurodegenerative disease. Inhibition of AGE formation in these diseases may limit oxidative and inflammatory damage in tissues, retarding the progression of pathophysiology and improve the quality of life during aging.
Glycation and oxidation: a role in the pathogenesis of atherosclerosis
Glycoxidation is of greatest significance in long-lived proteins such as collagen. In these proteins, glycoxidation products, believed to be atherogenic, accumulate with advancing age: in diabetes, their rate of accumulation is accelerated. Inhibition of glycation, oxidation, and glycoxidation may form the basis of future antiatherogenic strategies in both diabetic and nondiabetic individuals.
Involvement of advanced glycation end-products (AGEs) in Alzheimer's disease
The advanced stage of the glycation process (one of the post-translational modifications of proteins) leads to the formation of advanced glycation end-products (AGEs) and plays an important role in the pathogenesis of angiopathy in diabetic patients. It has recently become clear that AGEs also influence physiological aging and neurodegenerative diseases such as Alzheimer's disease (AD) and amyotrophic lateral sclerosis (ALS).
Advanced glycation endproducts--role in pathology of diabetic complications
Hyperglycaemia has an important role in the pathogenesis of diabetic complications by increasing protein glycation and the gradual build-up of advanced glycation endproducts (AGEs) in body tissues. Protein glycation and AGE are accompanied by increased free radical activity that contributes towards the biomolecular damage in diabetes. This review introduces the chemistry of glycation and AGEs and examines the mechanisms by which they mediate their toxicity. The role of AGEs in the pathogenesis of retinopathy, cataract, atherosclerosis, neuropathy, nephropathy, diabetic embryopathy and impaired wound healing are considered.
Vitamins and analgesics in the prevention of collagen ageing
The ageing of connective tissues involves modifications of collagen, which are currently generating much interest amongst protein researchers. Protein glycation, a non-enzymic reaction involving sugar, appears to play a role in the evolution of age-related physical changes and diabetic complications-retinopathy, neuropathy, renal failure and atherosclerosis. Our studies show that the glycation of human corneal and scleral collagen produces increases in the collagen intermolecular spacing-these increases are similar to those we previously reported on the ageing of collagen in these tissues. The present investigation employs X-ray diffraction to look at the structural effects of various substances that are believed in inhibit protein glycation. Aspirin-like compounds and certain vitamins successfully prevented the sugar-induced molecular changes from occurring in corneal and scleral collagen, suggesting that such compounds could have a useful role in this aspect of ageing.

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