In vitro cross-linking of calf lens alpha-crystallin by malondialdehyde

Int J Pept Protein Res. 1994 Oct;44(4):342-7. doi: 10.1111/j.1399-3011.1994.tb01018.x.

Abstract

The effect of malondialdehyde on structural features of bovine alpha-crystallin has been investigated by absorption and fluorescence spectroscopy as well as by far-UV circular dichroism. Experimental evidence suggests the occurrence of intermolecular cross-linking induced by malondialdehyde. This cross-linking does not seem to affect the tryptophan environment, as suggested by intrinsic protein fluorescence. On the contrary, the time dependence of far-UV dichroic activity indicates that the cross-linking is accompanied by a secondary structure change. The formation of high molecular mass aggregates, evidence by electrophoresis in denaturing conditions, leads to irreversible alpha-crystallin aggregation due to extensive intermolecular cross-linking. Since malondialdehyde is produced in vivo as a breakdown product of lipid peroxidation the possible involvement of this molecule in the pathological mechanism of cataract formation has been briefly discussed.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Cattle
  • Chemical Phenomena
  • Chemistry, Physical
  • Circular Dichroism
  • Cross-Linking Reagents / chemistry
  • Cross-Linking Reagents / pharmacology
  • Crystallins / chemistry*
  • Crystallins / drug effects*
  • Malondialdehyde / chemistry*
  • Malondialdehyde / pharmacology*
  • Spectrometry, Fluorescence
  • Spectrophotometry, Ultraviolet

Substances

  • Cross-Linking Reagents
  • Crystallins
  • Malondialdehyde