Advanced protein glycosylation in diabetes and aging.
Products of advanced protein glycosylation (advanced glycation end products, or AGEs) accumulate in tissues as a function of time and sugar concentration. AGEs induce permanent abnormalities in extracellular matrix component function, stimulate cytokine and reactive oxygen species production through AGE-specific receptors, and modify intracellular proteins. Pharmacologic inhibition of AGE formation in long-term diabetic animals prevents diabetic retinopathy, nephropathy, neuropathy, and arterial abnormalities in animal models. Clinical trials in humans are currently in progress.
Brownlee
M
M
Diabetes Research Center, Albert Einstein College of Medicine, Bronx, New York 10461, USA.
D000368:Aged; D000544:Alzheimer Disease / Q000503:physiopathology*; D000818:Animals; D016922:Cellular Senescence / Q000502:physiology*; D016207:Cytokines / Q000502:physiology; D003920:Diabetes Mellitus / Q000503:physiopathology*; D016326:Extracellular Matrix Proteins / Q000502:physiology; D017127:Glycation End Products, Advanced / Q000502:physiology*; D006801:Humans; D017382:Reactive Oxygen Species / Q000378:metabolism; D000067759:Receptor for Advanced Glycation End Products; D011971:Receptors, Immunologic / Q000502:physiology
D016207:Cytokines; D016326:Extracellular Matrix Proteins; D017127:Glycation End Products, Advanced; D017382:Reactive Oxygen Species; D000067759:Receptor for Advanced Glycation End Products; D011971:Receptors, Immunologic