Гликоздану өнімдерінің қарттану және аурулардағы ролі

Proteins or lipids that become glycated as a result of exposure to sugars
Advanced glycation end products (AGEs) are proteins or lipids that become glycated as a result of exposure to sugars. They are a bio marker implicated in aging and the development, or worsening, of many degenerative diseases, such as diabetes, atherosclerosis, chronic kidney disease, and Alzheimer's disease.

Animal derived foods that are high in fat and protein are generally AGE rich and are prone to further AGE formation during cooking. However, only low molecular weight AGEs are absorbed through diet, and vegetarians have been found to have higher concentrations of overall AGEs compared to non vegetarians. Therefore, it is unclear whether dietary AGEs contribute to disease and aging, or whether only endogenous AGEs (those produced in the body) matter. This does not free diet from potentially negatively influencing AGE, but potentially implies that dietary AGE may deserve less attention than other aspects of diet that lead to elevated blood sugar levels and formation of AGEs. and some age related chronic diseases. They are also believed to play a causative role in the vascular complications of diabetes mellitus. AGEs arise under certain pathologic conditions, such as oxidative stress due to hyperglycemia in patients with diabetes. AGEs play a role as proinflammatory mediators in gestational diabetes as well. In the context of cardiovascular disease, AGEs can induce crosslinking of collagen, which can cause vascular stiffening and entrapment of low density lipoprotein particles (LDL) in the artery walls. AGEs can also cause glycation of LDL which can promote its oxidation. Oxidized LDL is one of the major factors in the development of atherosclerosis. Finally, AGEs can bind to RAGE (receptor for advanced glycation end products) and cause oxidative stress as well as activation of inflammatory pathways in vascular endothelial cells. cardiovascular disease, and stroke. The mechanism by which AGEs induce damage is through a process called cross linking that causes intracellular damage and apoptosis. They form photosensitizers in the crystalline lens, which has implications for cataract development. Reduced muscle function is also associated with AGEs.

AGEs have a range of pathological effects, such as: and other AGE proteins have been shown in experimental models to accumulate with time, increasing from 5 50 fold over periods of 5–20 weeks in the retina, lens and renal cortex of diabetic rats. The inhibition of AGE formation reduced the extent of nephropathy in diabetic rats. Therefore, substances that inhibit AGE formation may limit the progression of disease and may offer new tools for therapeutic interventions in the therapy of AGE mediated disease. AGEs have specific cellular receptors; the best characterized are those called RAGE. The activation of cellular RAGE on endothelium, mononuclear phagocytes, and lymphocytes triggers the generation of free radicals and the expression of inflammatory gene mediators. Such increases in oxidative stress lead to the activation of the transcription factor NF κB and promote the expression of NF κB regulated genes that have been associated with atherosclerosis. In humans, histones in the cell nucleus are richest in lysine, and therefore form the glycated protein N(6) Carboxymethyllysine (CML). The pathogenesis of this process hypothesized to activation of the nuclear factor kappa B (NF κB) following AGE binding. NF κB controls several genes which are involved in inflammation. AGEs can be detected and quantified using bioanalytical and immunological methods.