title: Protein glycation during aging and in cardiovascular disease.
abstract: Advanced glycation endproducts (AGEs), pathophysiological important posttranslational modifications, are formed in vivo by a non-enzymatic reaction of proteins with reactive carbohydrates and accumulate during aging. They are discussed to be responsible for degenerative diseases. Glycation modifies the structure and function of proteins, induces tissue stiffening via crosslinking and a long-lasting inflammatory response after binding to AGE-receptors. Beside the extracellular matrix, a couple of intracellular proteins are known to be glycated leading to molecular and cellular dysfunction. In the cardiovascular system, AGEs are a major cause of cardiac and vascular dysfunction. Whereas AGEs are discussed to be potential biomarkers for diseases as well as for aging, the molecular analysis of AGEs in body fluids and tissue has still to be further improved. This article is part of a Special Issue entitled: Posttranslational Protein modifications in biology and Medicine.
authors.affiliation: Department of Cardiothoracic Surgery, University Hospital Halle, Ernst-Grube Str. 40, D-06120 Halle (Saale), Germany. Electronic address: andreas.simm@uk-halle.de.
authors.forename: Andreas
authors.initials: A
authors.lastname: Simm
mesh_terms: D000375:Aging / Q000378:metabolism* / Q000473:pathology; D000818:Animals; D015415:Biomarkers / Q000378:metabolism; D002318:Cardiovascular Diseases / Q000378:metabolism* / Q000473:pathology / Q000503:physiopathology; D017127:Glycation End Products, Advanced / Q000378:metabolism*; D006801:Humans; D007249:Inflammation / Q000378:metabolism / Q000473:pathology / Q000503:physiopathology; D011499:Protein Processing, Post-Translational
chemical_list: D015415:Biomarkers; D017127:Glycation End Products, Advanced
keywords: Aging; Cardiovascular disease; Diabetes mellitus; Posttranscriptional modification; Protein glycation