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Recent Progress in Advanced Glycation and Diabetic Vascular Disease: Role of Advanced Glycation End Product Receptors

Helen Vlassara, Richard Bucala

Open publisher page 117 citations

Abstract

Advanced glycosylation end products (AGEs) form principally from the rearrangement of early glycation products, i.e., Amadori products, which produce a class of stable moieties that possess distinctive chemical crosslinking and biological properties. It has been generally believed that proteins with half-lives of longer than a few weeks are most susceptible to advanced glycosylation and that the highest levels of AGEs occur on proteins that comprise the long-lived structural components of connective tissue matrix and basement membrane.

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What this paper is about

Advanced glycosylation end products (AGEs) form principally from the rearrangement of early glycation products, i.e., Amadori products, which produce a class of stable moieties that possess distinctive chemical crosslinking and biological properties. It has been generally believed that proteins with half-lives of longer than a few weeks are most susceptible to advanced glycosylation and that the highest levels of AGEs occur on proteins that comprise the long-lived structural components of connective tissue matrix and basement membrane.

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Available abstract

Advanced glycosylation end products (AGEs) form principally from the rearrangement of early glycation products, i.e., Amadori products, which produce a class of stable moieties that possess distinctive chemical crosslinking and biological properties. It has been generally believed that proteins with half-lives of longer than a few weeks are most susceptible to advanced glycosylation and that the highest levels of AGEs occur on proteins that comprise the long-lived structural components of connective tissue matrix and basement membrane.

Key concepts: Glycation, Amadori rearrangement, Advanced glycation end-product, Glycosylation, Chemistry, Receptor, Biochemistry, Lysine

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