Advanced protein glycosylation in diabetes and aging

M. Brownlee

Research output: Contribution to journalReview article

1044 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)223-234
Number of pages12
JournalAnnual Review of Medicine
Volume46
DOIs
StatePublished - Jan 1 1995

    Fingerprint

Keywords

  • Advanced glycation end products
  • Aminoguanidine
  • DNA
  • Matrix
  • Mitogens
  • Receptors

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)

Cite this