The Road to Advanced Glycation End Products: A Mechanistic Perspective

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Journal titleCurrent Medicinal Chemistry
Pages16531671; # of pages: 19
SubjectAcids; Aged; Amino Acids; analysis; Biotechnology; blood; Glucose; glycation; Glycosylation; In Vitro; pha; Protein; Proteins; Vitro
AbstractProtein glycation is a slow natural process involving the chemical modification of the reactive amino and guanidine functions in amino acids by sugars and carbohydrates-derived reactive carbonyls. Its deleterious consequences are obvious in the case of long-lived proteins in aged people and are exacerbated by the high blood concentration of sugars in diabetic patients. The non-enzymatic glycation of proteins occurs through a wide range of concurrent processes comprising condensation, rearrangement, fragmentation, and oxidation reactions. Using a few well established intermediates such as Schiff base, Amadori product and reactive a-dicarbonyls as milestones and the results of in vitro glycation investigations, an overall detailed mechanistic analysis of protein glycation is presented for the first time. The pathways leading to several advanced glycation end products (AGEs) such as (carboxymethyl)lysine, pentosidine, and glucosepane are outlined, whereas other AGEs useful as potential biomarkers of glycation are only briefly mentioned. The current stage of the development of glycation inhibitors has been reviewed with an emphasis on their mechanism of action
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AffiliationNRC Biotechnology Research Institute; National Research Council Canada
Peer reviewedNo
NRC number47556
NPARC number3540312
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Record identifier51c4eb58-ed06-4e4c-b46e-7cbcce0f223f
Record created2009-03-01
Record modified2016-05-09
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