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Advanced protein glycosylation in diabetes and aging

M Brownlee1

  • 1Diabetes Research Center, Albert Einstein College of Medicine, Bronx, New York 10461, USA.

Annual Review of Medicine
|January 1, 1995
PubMed

Insights

Advanced glycation end products (AGEs) accumulate with age and high sugar, causing tissue damage. Inhibiting AGE formation in diabetic animals prevented complications, with human trials underway.

Area of Science:

  • Biochemistry
  • Pathophysiology
  • Endocrinology

Background:

  • Advanced glycation end products (AGEs) are formed from protein glycation.
  • AGE accumulation is linked to aging and hyperglycemia.
  • AGEs cause cellular dysfunction and tissue damage.

Purpose of the Study:

  • To investigate the role of AGEs in diabetic complications.
  • To evaluate the therapeutic potential of AGE formation inhibitors.

Main Methods:

  • Studies involved long-term diabetic animal models.
  • Pharmacologic inhibition of AGE formation was employed.
  • Assessment of various diabetic pathologies was performed.

Main Results:

  • Inhibition of AGE formation prevented diabetic retinopathy.
  • Nephropathy, neuropathy, and arterial abnormalities were also prevented.
  • These findings highlight the detrimental effects of AGEs.

Conclusions:

  • AGEs play a critical role in the pathogenesis of diabetic complications.
  • Pharmacologic inhibition of AGE formation is a promising therapeutic strategy.
  • Further clinical investigation in humans is warranted.

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