Glycation-induced matrix stability in the rabbit achilles tendon

G. Kesava Reddy, Lisa Stehno-Bittel, Chukuka S. Enwemeka

Research output: Contribution to journalArticlepeer-review

84 Citations (Scopus)

Abstract

Connective tissue susceptibility to nonenzymatic glycation was examined following 0, 2, 4, 6, 8, and 10 weeks of incubating the rabbit Achilles tendon in phosphate-buffered saline containing ribose (glycated). The biomechanical integrity of the glycated tendons was then compared to control tendons incubated in phosphate-buffered saline (nonglycated) at each time interval, while the biochemical stability of both groups of tendons was determined by examining collagen extractability and the formation of pentosidine at 8 weeks. Whereas there were no significant biomechanical differences between control and glycated tendons at 0- and 2-week intervals (P > 0.05), moderately significant increases in maximum load, energy to yield, and toughness of glycated tendons were observed at 4 weeks. Beyond 4 weeks of incubation, the differences between glycated and nonglycated tendons became highly significant, as glycated tendons withstood more load and tensile stress (P < 0.01 for each variable), attained significantly higher modulus of elasticity (P < 0.01), absorbed more energy (P < 0.01), and became tougher (P < 0.01) than controls. These differences in the biomechanical indices of the effects of glycation were stable between the 6th and 10th week of glycation. The maximum increases in the biomechanical measurements as a result of glycation were 29% for maximum load, 125% for stress, 19% for strain, 106% for Young's modulus of elasticity, 14% for energy to yield, and 57% for toughness. Biochemical analysis showed a 61% reduction in the extractability of neutral salt-soluble collagen, a 48% decrease in acid-soluble collagen, and a 29% decline in pepsin-soluble collagen in glycated tendons (P < 0.01). In contrast, there was a 28% increase in the amount of insoluble collagen and significantly higher amounts of pentosidine (P < 0.01) in glycated tendons. Collectively, these biomechanical and biochemical results suggest that nonenzymatic glycation may explain the altered stability of connective tissue matrix induced by the processes of diabetes and aging.

Original languageEnglish
Pages (from-to)174-180
Number of pages7
JournalArchives of Biochemistry and Biophysics
Volume399
Issue number2
DOIs
Publication statusPublished - 15 Mar 2002
Externally publishedYes

Keywords

  • Connective tissue matrix
  • Crosslinking
  • Extractability of collagen
  • Fluorescence
  • Glycation
  • Maillard reaction
  • Pentosidine
  • Tendon biomechanics
  • Tensile strength
  • Toughness

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology

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