Aminoethylcysteine ketimine decarboxylated dimer protects submitochondrial particles from lipid peroxidation at a concentration not inhibitory of electron transport

Biochem Biophys Res Commun. 1994 Nov 30;205(1):264-8. doi: 10.1006/bbrc.1994.2659.

Abstract

In contrast with other inhibitors of the NADH dehydrogenase of the respiratory chain, the decarboxylated dimer of aminoethylcysteine ketimine protects bovine heart submitochondrial particles (SMP) from the NADH-Fe(+3)-ADP-induced lipid peroxidation. This effect, measured as inhibition of malondialdehyde formation, is concentration-dependent in the range 0.02-0.2 mM. This range of concentration is not inhibitory on NADH-oxidase activity of SMP. Furthermore the dimer is able to counteract the malondialdehyde formation stimulated by the Complex I inhibitors rotenone and N-methyl-4-phenylpyridinium (MPP+).

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acids, Sulfur / pharmacology*
  • Animals
  • Antioxidants / pharmacology
  • Cattle
  • Electron Transport / drug effects
  • Free Radical Scavengers
  • Free Radicals
  • Lipid Peroxidation*
  • Mitochondria, Heart / ultrastructure
  • Submitochondrial Particles / drug effects*
  • Submitochondrial Particles / metabolism
  • Superoxides / metabolism

Substances

  • Amino Acids, Sulfur
  • Antioxidants
  • Free Radical Scavengers
  • Free Radicals
  • Superoxides
  • thialysine ketimine