Experimental diabetes as a model of accelerated aging: Matrix collagen modifications


Stefek M., KARASU Ç.

Turkiye Klinikleri Journal of Medical Sciences, vol.29, no.SUPPL., 2009 (Journal Indexed in SCI Expanded) identifier

  • Publication Type: Article / Abstract
  • Volume: 29 Issue: SUPPL.
  • Publication Date: 2009
  • Title of Journal : Turkiye Klinikleri Journal of Medical Sciences
  • Keywords: Aging, Antioxidant, Collagen, Diabetes, Glycation

Abstract

Collagen, the main protein of the extracellular matrix, undergoes continual cross-linking during aging. In healthy individuals, this process is mediated by lysyl oxidase and proceeds slowly. In addition to physiological maturation, aging collagens are crosslinked by AGEs (advanced glycation end-products), formed by a reaction between reducing sugars and body proteins in a process of non-enzymatic glycoxidation. These pathological processes are accelerated in diabetic individuals, whose average blood glucose is higher than normal. In our studies, rat tail tendon mechanical strength was significantly enhanced for diabetic animals when compared with those of age-matched controls. Tail tendons from diabetic rats were found to contain elevated amounts of p-dimethylaminobenzaldehyde-reactive material with an absorbance spectrum characteristic of the Ehrlich chromogen. The characteristic glyco-fluorophore was elevated in tendon collagen of diabetic animals. The glycation inhibitor aminoguanidine significantly inhibited changes of all three parameters evaluated while the pyridoindole antioxidant stobadine significantly decreased only tendon mechanical strength. Copyright © 2009 by Türkiye Klinikleri.