title: Glycated Serum Albumin and AGE Receptors.
abstract: In vivo modification of proteins by molecules with reactive carbonyl groups leads to intermediate and advanced glycation end products (AGE). Glucose is a significant glycation reagent due to its high physiological concentration and poorly controlled diabetics show increased albumin glycation. Increased levels of glycated and AGE-modified albumin have been linked to diabetic complications, neurodegeneration, and vascular disease. This review discusses glycated albumin formation, structural consequences of albumin glycation on drug binding, removal of circulating AGE by several scavenger receptors, as well as AGE-induced proinflammatory signaling through activation of the receptor for AGE. Analytical methods for quantitative detection of protein glycation and AGE formation are compared. Finally, the use of glycated albumin as a novel clinical marker to monitor glycemic control is discussed and compared to glycated hemoglobin (HbA1c) as long-term indicator of glycemic status.
authors.affiliation: School of Pharmacy, North Dakota State University, Fargo, North Dakota, USA. Electronic address: stefan.vetter@ndsu.edu.
authors.forename: Stefan W
authors.initials: SW
authors.lastname: Vetter
mesh_terms: D015415:Biomarkers / Q000097:blood*; D048909:Diabetes Complications / Q000097:blood; D017127:Glycation End Products, Advanced; D006801:Humans; D000067759:Receptor for Advanced Glycation End Products / Q000378:metabolism*; D012709:Serum Albumin / Q000378:metabolism*; D000093423:Glycated Serum Albumin
chemical_list: D015415:Biomarkers; D017127:Glycation End Products, Advanced; D000067759:Receptor for Advanced Glycation End Products; D012709:Serum Albumin; D000093423:Glycated Serum Albumin
keywords: AGE; Advanced glycation end products; Amadori products; Diabetes; Fructosamine; RAGE; Receptor for advanced glycation end products; Scavenger receptors; Serum albumin