Bendazac prevents cyanate binding to soluble lens proteins and cyanate-induced phase-separation opacities in vitro: a possible mechanism by which bendazac could delay cataract

Exp Eye Res. 1986 Dec;43(6):973-9. doi: 10.1016/0014-4835(86)90075-8.

Abstract

The reaction of lens proteins with cyanate (carbamylation) causes many changes seen in human cataract including disruption of the protein conformations. Bendazac, a putative anti-cataract drug, decreases the binding of cyanate to lens proteins and prevents the cyanate-induced elevation of the phase separation temperature in incubated rat lenses. Its major metabolite, 5-hydroxybendazac, also inhibits the binding of cyanate to lens proteins even when it is present only during a pre-incubation period. The metabolite is more effective than the parent compound.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Aspirin / pharmacology
  • Cattle
  • Crystallins / metabolism*
  • Cyanates / antagonists & inhibitors*
  • Indazoles / pharmacology*
  • Protein Binding / drug effects
  • Pyrazoles / pharmacology*
  • Rats
  • Rats, Inbred Strains
  • Temperature

Substances

  • Crystallins
  • Cyanates
  • Indazoles
  • Pyrazoles
  • 5-hydroxybendazac
  • bendazac
  • potassium cyanate
  • Aspirin