Advanced protein glycosylation in diabetes and aging

Annu Rev Med. 1995;46:223-34. doi: 10.1146/annurev.med.46.1.223.

Abstract

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.

Publication types

  • Review

MeSH terms

  • Aged
  • Alzheimer Disease / physiopathology*
  • Animals
  • Cellular Senescence / physiology*
  • Cytokines / physiology
  • Diabetes Mellitus / physiopathology*
  • Extracellular Matrix Proteins / physiology
  • Glycation End Products, Advanced / physiology*
  • Humans
  • Reactive Oxygen Species / metabolism
  • Receptor for Advanced Glycation End Products
  • Receptors, Immunologic / physiology

Substances

  • Cytokines
  • Extracellular Matrix Proteins
  • Glycation End Products, Advanced
  • Reactive Oxygen Species
  • Receptor for Advanced Glycation End Products
  • Receptors, Immunologic