The retinoid X receptor enhances the function of the peroxisome proliferator activated receptor

Biochimie. 1993;75(3-4):251-6. doi: 10.1016/0300-9084(93)90084-6.

Abstract

The peroxisome proliferator activated receptor (PPAR) is a member of the steroid hormone receptor superfamily and is activated by a variety of non-genotoxic rodent hepatocarcinogens termed peroxisome proliferators. A key marker of peroxisome proliferator action is the peroxisomal enzyme acyl-CoA oxidase that is elevated about 10-fold in the liver of treated rodents. We have shown previously that a peroxisome proliferator response element (PPRE) is located 570 bp upstream of the rat acyl-CoA oxidase gene and that PPAR binds to it. We show here that the retinoid X receptor (RXR) is required for PPAR to bind to the PPRE and that the RXR ligand, 9-cis retinoic acid, enhances PPAR action. These results therefore suggest that retinoids may modulate the action of peroxisome proliferators.

MeSH terms

  • Acyl-CoA Oxidase
  • Animals
  • Base Sequence
  • Carcinogens
  • Cell Line
  • Molecular Sequence Data
  • Oxidoreductases / metabolism*
  • Rats
  • Receptors, Cell Surface / metabolism*
  • Receptors, Cell Surface / physiology*
  • Receptors, Cytoplasmic and Nuclear*
  • Receptors, Retinoic Acid*
  • Retinoid X Receptors
  • Transcription Factors*

Substances

  • Carcinogens
  • Receptors, Cell Surface
  • Receptors, Cytoplasmic and Nuclear
  • Receptors, Retinoic Acid
  • Retinoid X Receptors
  • Transcription Factors
  • Oxidoreductases
  • Acyl-CoA Oxidase