Advanced protein glycosylatlon in diabetes and aging

Michael Brownlee

Research output: Contribution to journalArticle

1042 Citations (Scopus)

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
StatePublished - 1995

Fingerprint

Advanced Glycosylation End Products
Diabetic Nephropathies
Diabetic Retinopathy
Medical problems
Glycosylation
Extracellular Matrix
Reactive Oxygen Species
Animals
Animal Models
Aging of materials
Clinical Trials
Cytokines
Sugars
Proteins
Tissue
Advanced Glycosylation End Product-Specific Receptor

Keywords

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

ASJC Scopus subject areas

  • Cell Biology
  • Medicine(all)

Cite this

Advanced protein glycosylatlon in diabetes and aging. / Brownlee, Michael.

In: Annual Review of Medicine, Vol. 46, 1995, p. 223-234.

Research output: Contribution to journalArticle

Brownlee, Michael. / Advanced protein glycosylatlon in diabetes and aging. In: Annual Review of Medicine. 1995 ; Vol. 46. pp. 223-234.
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