Protein-bound and free UV filters in cataract lenses. The concentration of UV filters is much lower than in normal lenses

Exp Eye Res. 2007 Aug;85(2):219-25. doi: 10.1016/j.exer.2007.04.004. Epub 2007 Apr 29.

Abstract

In human cataract lenses the UV filters, 3-hydroxykynurenine glucoside (3OHKG) and kynurenine (Kyn) were found to be covalently bound to proteins and the levels in the nucleus were much higher than in the cortex. The levels of the bound UV filters in cataract nuclei were much lower than those in age-matched normal lenses. 3-Hydroxykynurenine could not be detected in cataract lenses. As with normal lenses, protein-bound 3OHKG in cataract lenses was found at the highest levels followed by Kyn. Free UV filter concentrations were also markedly reduced in cataract lenses. This feature may well contribute to the lower protein-bound levels; however, there was no clear relationship between free and bound UV filter contents when individual lenses were examined. We propose that since cysteine is a major site for UV filter binding, the well-documented oxidation of protein sulfhydryl groups during the progression of nuclear cataract may account, in part, for the pronounced decrease in bound UV filters in cataract lenses.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Aged
  • Aged, 80 and over
  • Cataract / metabolism*
  • Chromatography, High Pressure Liquid / methods
  • Eye Proteins / metabolism*
  • Glucosides / metabolism
  • Humans
  • Kynurenine / analogs & derivatives
  • Kynurenine / metabolism
  • Lens Cortex, Crystalline / metabolism
  • Lens Nucleus, Crystalline / metabolism
  • Lens, Crystalline / metabolism*
  • Middle Aged
  • Protein Binding
  • Scattering, Radiation
  • Ultraviolet Rays*

Substances

  • Eye Proteins
  • Glucosides
  • hydroxykynurenine glucoside
  • Kynurenine