Mechanistic studies of advanced glycosylation end product inhibition by aminoquanidine

Diane Edelstein, Michael Brownlee

Research output: Contribution to journalArticle

294 Citations (Scopus)

Abstract

Aminoguanidine-HCI inhibits the formation of advanced glycosylation end products (AGEs) in vitro and in vivo, but the mechanism by which this occurs has not been determined. Aminoguanidine inhibited glucose-derived AGE formation on RNase A by 67-85% at aminoguanidine-glucose molar ratios of 1:5 to 1:50 without affecting the concentration of Amadori products. Fast-atom-bombardment mass spectrometry of RNase peptides incubated with glucose alone or with glucose plus aminoguanidine showed that aminoguanidine inhibited the formation of AGEs without forming an adduct with glycosylated peptide. These data suggest that the primary mechanism of aminoguanidine action is reaction with Amadori-derived fragmentation products in solution. These findings are relevant to the potential clinical use of aminoguanidine in the prevention of diabetic complications.

Original languageEnglish (US)
Pages (from-to)26-29
Number of pages4
JournalDiabetes
Volume41
Issue number1
StatePublished - Jan 1992

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Advanced Glycosylation End Products
Glucose
Fast Atom Bombardment Mass Spectrometry
Pancreatic Ribonuclease
Peptides
Diabetes Complications
Ribonucleases
pimagedine

ASJC Scopus subject areas

  • Internal Medicine
  • Endocrinology, Diabetes and Metabolism

Cite this

Mechanistic studies of advanced glycosylation end product inhibition by aminoquanidine. / Edelstein, Diane; Brownlee, Michael.

In: Diabetes, Vol. 41, No. 1, 01.1992, p. 26-29.

Research output: Contribution to journalArticle

Edelstein, D & Brownlee, M 1992, 'Mechanistic studies of advanced glycosylation end product inhibition by aminoquanidine', Diabetes, vol. 41, no. 1, pp. 26-29.
Edelstein, Diane ; Brownlee, Michael. / Mechanistic studies of advanced glycosylation end product inhibition by aminoquanidine. In: Diabetes. 1992 ; Vol. 41, No. 1. pp. 26-29.
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