Increased liver-specific catalase activity in transgenic mice

DNA Cell Biol. 1996 Aug;15(8):625-30. doi: 10.1089/dna.1996.15.625.

Abstract

Catalase is the major peroxisomal H2O2-detoxifying enzyme and is thought to be critical in maintaining low H2O2 levels within a cell. It has been proposed that increased H2O2 levels may be involved in oxidative DNA damage and tumor promotion induced by peroxisome proliferators and other xenobiotics. To develop a mouse model system to address this issue, we have generated transgenic mice that exhibit a three- to four-fold increase in liver catalase levels. The activities of fatty acyl coenzyme A (CoA) oxidase and lauric acid hydroxylase were unchanged in transgenic mice, demonstrating that elevated catalase levels did not alter the activity of these other peroxisome proliferator-induced enzymes that produce active oxygen. These mice should help elucidate the role of H2O2 in cellular events mediated by peroxisome proliferators and other xenobiotics.

Publication types

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

MeSH terms

  • Acyl-CoA Oxidase
  • Animals
  • Base Sequence
  • Catalase / genetics
  • Catalase / metabolism*
  • Cytochrome P-450 CYP4A
  • Cytochrome P-450 Enzyme System / metabolism
  • DNA / analysis
  • Gene Expression
  • Genetic Vectors / genetics
  • Globins / genetics
  • Humans
  • Liver / enzymology*
  • Mice
  • Mice, Transgenic
  • Mixed Function Oxygenases / metabolism
  • Molecular Sequence Data
  • Organ Specificity
  • Oxidoreductases / metabolism
  • RNA, Messenger / analysis
  • alpha-Fetoproteins / genetics

Substances

  • RNA, Messenger
  • alpha-Fetoproteins
  • Globins
  • DNA
  • Cytochrome P-450 Enzyme System
  • Mixed Function Oxygenases
  • Oxidoreductases
  • Catalase
  • Cytochrome P-450 CYP4A
  • Acyl-CoA Oxidase