Decreased molecular chaperone property of alpha-crystallins due to posttranslational modifications

Biochem Biophys Res Commun. 1995 Mar 17;208(2):675-9. doi: 10.1006/bbrc.1995.1391.

Abstract

We studied the effect of oxidation, mixed disulfide formation and glycation of alpha-crystallins on their molecular chaperone property. The ability of alpha-crystallins to protect heat-induced denaturation and aggregation of beta L-crystallin was significantly diminished by these modifications. alpha-Crystallin from senile human lenses also showed significant loss of chaperone-like property. Age-dependent increase in posttranslationally modified alpha-crystallins is the likely cause for this change.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Adolescent
  • Age Factors
  • Aged
  • Animals
  • Cattle
  • Crystallins / metabolism*
  • Disulfides
  • Humans
  • In Vitro Techniques
  • Molecular Chaperones*
  • Oxidation-Reduction
  • Protein Processing, Post-Translational

Substances

  • Crystallins
  • Disulfides
  • Molecular Chaperones