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Advanced glycation end products (AGEs) are proteins or lipids that become glycated as a result of exposure to sugars. [1] 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 .
Pages in category "Advanced glycation end-products" The following 8 pages are in this category, out of 8 total. This list may not reflect recent changes. A.
Sorbitol may also glycate nitrogens on proteins, such as collagen, and the products of these glycations are referred-to as AGEs - advanced glycation end-products. AGEs are thought to cause disease in the human body, one effect of which is mediated by RAGE (receptor for advanced glycation end-products) and the ensuing inflammatory responses induced.
N(6)-Carboxymethyllysine (CML), also known as N ε-(carboxymethyl)lysine, is an advanced glycation endproduct (AGE). CML has been the most used marker for AGEs in food analysis. CML has been the most used marker for AGEs in food analysis.
Schematic of the relation between an immunoglobulin and RAGE Schematic of the RAGE gene and its products. RAGE (receptor for advanced glycation endproducts), also called AGER, is a 35 kilodalton transmembrane receptor [5] of the immunoglobulin super family which was first characterized in 1992 by Neeper et al. [6] Its name comes from its ability to bind advanced glycation endproducts (), which ...
Glucosepane is a lysine-arginine protein cross-linking product and advanced glycation end product (AGE) derived from D-glucose. [1] It is an irreversible, covalent cross-link product that has been found to make intermolecular and intramolecular cross-links in the collagen of the extracellular matrix (ECM) and crystallin of the eyes. [2]
Methylglyoxal is involved in the formation of advanced glycation end products (AGEs). [4] In this process, methylglyoxal reacts with free amino groups of lysine and arginine and with thiol groups of cysteine forming AGEs. Histones are also heavily susceptible to modification by methylglyoxal and these modifications are elevated in breast cancer ...
Glycation is the non-enzymatic process responsible for many (e.g. micro and macrovascular) complications in diabetes mellitus and is implicated in some diseases and in aging. [2] [3] [4] Glycation end products are believed to play a causative role in the vascular complications of diabetes mellitus. [5]