Chemical modification of proteins by lipids in diabetes.
Advanced glycation and lipoxidation end-products (AGE/ALE) increase in tissue proteins with age and at an accelerated rate in diabetes. This Review focuses on the nature and source of AGEs/ALEs and the factors affecting their formation in tissue and plasma proteins. Lipids are identified as an important source of chemical modification of proteins in diabetes, and the role of diabetes, dyslipidemia and renal disease in formation of AGEs/ALEs is reviewed. The article concludes with a discussion of ELISA assays for AGEs/ALEs and the merits of measuring AGEs/ALEs in the clinical laboratory.
Department of Chemistry and Biochemistry, Graduate Science Research Center, University of South Carolina, Columbia 29208, USA. john.baynes@sc.edu
John W
JW
Baynes
D000418:Albumins / Q000737:chemistry / Q000378:metabolism; D048909:Diabetes Complications; D003920:Diabetes Mellitus / Q000378:metabolism*; D017127:Glycation End Products, Advanced / Q000096:biosynthesis* / Q000097:blood / Q000737:chemistry; D006801:Humans; D006949:Hyperlipidemias / Q000378:metabolism; D050356:Lipid Metabolism; D015227:Lipid Peroxidation; D008084:Lipoxygenase / Q000378:metabolism
D000418:Albumins; D017127:Glycation End Products, Advanced; D008084:Lipoxygenase