Glycation Theory of Aging

In its essence, this is the same process that causes the well-known process of "caramelization" of sugar.

Proteins, in fact, can be damaged both by free-radicals and by glycation.

Glycation is a reaction by which reducing sugars become attached to proteins without the assistance of an enzyme.

The end result can quickly re-arrange atoms such that the 2-carbon (2nd carbon) of the glucose loses its two hydrogens, resulting in a carbonyl group structure called an Amadori product (a ketoamine).

Both glycation and Amadori product formation are completely reversible reactions.

But the formation of Advanced Glycation End-products (AGEs) by oxidation of Amadori products is irreversible.

AGEs in tissues increase the rate of free radical production to 50-times the rate of free-radical production by unglycated proteins, which has been associated with accelerated aging.

AGEs can be formed in the body from glycation and oxidation or can be ingested directly from browned foods or tobacco smoke.

According to research, about one third of absorbed dietary AGEs are excreted in urine and rest is presumably incorporated into body tissues.

In mammals, lens crystallines, collagen and basement membrane are most vulnerable to cross-linking and AGE formation because they are the most long-lived proteins, with a slow rate of turnover.

In terms of most active sugars for glycation, Galactose is 5 times more reactive than glucose, fructose is 8 times more reactive, deoxyglucose is 25 times more reactive, ribose is 100 times more reactive, and deoxyribose is 200 times more reactive.

In terms of anti aging measures from glycation process and AGE formation, it has been suggested in animal studies that there is correlation between high blood antioxidant levels and low levels of AGEs.

It has also been recognised that there are a group of enzymes involved in the suppression of glycation processes and repair of glycated proteins in physiological systems. These enzymes involved are (according to the Louis Camille Maillard Association): glyoxalase I, aldehyde reductases and dehydrogenases, Amadoriase and fructosamine-3-phosphokinase.

Currently, there is a continuing debate about the physiological significance of AGEs in food.

It is agreed that food is a rich source of AGEs but highly glycated proteins may not be digested efficiently.

Also, AGEs that are absorbed are probably mainly glycated amino acids or AGE free adducts which are excreted rapidly in the urine by subjects with normal renal function.

Glycation Theory of Aging - Studies

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