Glycation of collagen in hypertriglyceridemic rats

Life Sci. 1997;60(23):2119-27. doi: 10.1016/s0024-3205(97)00221-x.

Abstract

Nonenzymatic collagen glycation and modification with lipid derived metabolites was studied in rat skin and tail tendon collagen of control and hypertriglyceridemic (HTG) rats. Age-dependent changes typical for lipid and sugar derived adducts were evaluated by measuring fluorescence of these collagens at wavelengths typical for sugar (335/385 and 370/440 nm) and lipid derived adducts (356/460 and 390/460 nm). In addition pentosidine assay (corresponding to the fluorescence parameters 335/385 nm) was performed as well. It was found that pentosidine concentration as well as fluorescence intensities in skin collagen was the same for control and HTG rats and significantly increased with age. On the other hand, no significant age-dependent changes in fluorescence intensities were observed in tail tendon collagen. Pentosidine concentration in tail tendon collagen was much lower than that in skin and it was decreased in young HTG rats compared to control ones. It increased with age, more distinctly in HTG rats than in their control counterparts, in such a way that at the age of 19 months the pentosidine levels were undistinguishible in both rat strains. Possible mechanisms underlying these results are discussed.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Arginine / analogs & derivatives
  • Arginine / metabolism
  • Collagen / metabolism*
  • Disease Models, Animal
  • Glycosylation
  • Hypertriglyceridemia / genetics
  • Hypertriglyceridemia / metabolism*
  • Lipid Peroxidation
  • Lysine / analogs & derivatives
  • Lysine / metabolism
  • Male
  • Protein Processing, Post-Translational
  • Rats
  • Rats, Wistar
  • Skin / metabolism
  • Spectrometry, Fluorescence

Substances

  • Collagen
  • Arginine
  • pentosidine
  • Lysine