title: Advanced Glycation End Products: A Molecular Target for Vascular Complications in Diabetes.
abstract: A nonenzymatic reaction between reducing sugars and amino groups of proteins, lipids and nucleic acids contributes to the aging of macromolecules and subsequently alters their structural integrity and function. This process has been known to progress at an accelerated rate under hyperglycemic and/or oxidative stress conditions. Over a course of days to weeks, early glycation products undergo further reactions such as rearrangements and dehydration to become irreversibly cross-linked, fluorescent and senescent macroprotein derivatives termed advanced glycation end products (AGEs). There is a growing body of evidence indicating that interaction of AGEs with their receptor (RAGE) elicits oxidative stress generation and as a result evokes proliferative, inflammatory, thrombotic and fibrotic reactions in a variety of cells. This evidence supports AGEs' involvement in diabetes- and aging-associated disorders such as diabetic vascular complications, cancer, Alzheimer's disease and osteoporosis. Therefore, inhibition of AGE formation could be a novel molecular target for organ protection in diabetes. This report summarizes the pathophysiological role of AGEs in vascular complications in diabetes and discusses the potential clinical utility of measurement of serum levels of AGEs for evaluating organ damage in diabetes.
authors.affiliation: Department of Pathophysiology and Therapeutics of Diabetic Vascular Complications, Kurume University School of Medicine, Kurume, Japan.
authors.forename: Sho-Ichi
authors.initials: S
authors.lastname: Yamagishi
authors.affiliation: Department of Pathophysiology and Therapeutics of Diabetic Vascular Complications, Kurume University School of Medicine, Kurume, Japan.
authors.forename: Nobutaka
authors.initials: N
authors.lastname: Nakamura
authors.affiliation: Department of Pathophysiology and Therapeutics of Diabetic Vascular Complications, Kurume University School of Medicine, Kurume, Japan.|Saravio Central Institute, Oita, Japan.
authors.forename: Mika
authors.initials: M
authors.lastname: Suematsu
authors.affiliation: Saravio Central Institute, Oita, Japan.
authors.forename: Kuniyoshi
authors.initials: K
authors.lastname: Kaseda
authors.affiliation: Department of Pathophysiology and Therapeutics of Diabetic Vascular Complications, Kurume University School of Medicine, Kurume, Japan.
authors.forename: Takanori
authors.initials: T
authors.lastname: Matsui
mesh_terms: D058892:Adenosine Deaminase Inhibitors / Q000627:therapeutic use*; D000544:Alzheimer Disease / Q000150:complications / Q000188:drug therapy / Q000235:genetics / Q000473:pathology; D052157:Aptamers, Nucleotide / Q000627:therapeutic use*; D002318:Cardiovascular Diseases / Q000150:complications / Q000188:drug therapy / Q000235:genetics / Q000473:pathology; D003922:Diabetes Mellitus, Type 1 / Q000150:complications / Q000188:drug therapy* / Q000235:genetics / Q000473:pathology; D003924:Diabetes Mellitus, Type 2 / Q000150:complications / Q000188:drug therapy* / Q000235:genetics / Q000473:pathology; D003925:Diabetic Angiopathies / Q000150:complications / Q000188:drug therapy* / Q000235:genetics / Q000473:pathology; D018819:Dipeptidyl Peptidase 4 / Q000235:genetics / Q000378:metabolism; D015870:Gene Expression; D017127:Glycation End Products, Advanced / Q000037:antagonists & inhibitors* / Q000378:metabolism; D006801:Humans; D009369:Neoplasms / Q000150:complications / Q000188:drug therapy / Q000235:genetics / Q000473:pathology; D010024:Osteoporosis / Q000150:complications / Q000188:drug therapy / Q000235:genetics / Q000473:pathology; D018384:Oxidative Stress; D000067759:Receptor for Advanced Glycation End Products / Q000235:genetics / Q000378:metabolism
chemical_list: C000593871:AGER protein, human; D058892:Adenosine Deaminase Inhibitors; D052157:Aptamers, Nucleotide; D017127:Glycation End Products, Advanced; D000067759:Receptor for Advanced Glycation End Products; C042807:DPP4 protein, human; D018819:Dipeptidyl Peptidase 4