Transcriptional induction of rat liver apolipoprotein A-I gene expression by glucocorticoids requires the glucocorticoid receptor and a labile cell-specific protein

Eur J Biochem. 1996 Jul 15;239(2):451-9. doi: 10.1111/j.1432-1033.1996.0451u.x.

Abstract

Treatment with glucocorticoids increases the concentration of plasma high-density lipoprotein (HDL), which is inversely correlated to the development of atherosclerosis. Previously, we demonstrated that repeated administration of glucocorticoids increases apolipoprotein (apo) A-I gene expression and decreases apoA-II gene expression in rat liver. In the present study, the mechanism of glucocorticoid action on hepatic apoA-I and apoA-II expression was studied. A single injection of rats with dexamethasone increased hepatic apoA-I mRNA levels within 6 h and further increases were observed after 12 h and 24 h. In contrast, liver apoA-II mRNA levels gradually decreased after dexamethasone treatment to less than 25% control levels after 24 h. In rat primary hepatocytes and McARH8994 hepatoma cells, addition of dexamethasone increased apoA-I mRNA levels in a time-dependent and dose-dependent manner, whereas apoA-II mRNA levels were unchanged. Simultaneous addition of the glucocorticoid antagonist RU486 prevented the increase in apoA-I mRNA levels after dexamethasone treatment, which suggests that the effects of dexamethasone are mediated through the glucocorticoid receptor. Inhibition of transcription by actinomycin D and nuclear-run-on experiments in McARH8994 cells and primary hepatocytes showed that dexamethasone induced apoA-I, but not apoA-II, gene transcription. Transient-transfection assays in McARH8994 cells with a chloramphenicol acetyl transferase vector driven by the rat-apoA-I-gene promoter demonstrated that the proximal apoA-I promoter could be induced by dexamethasone, and this effect could be abolished by simultaneous treatment with RU486. However, in COS-1 cells, apoA-I promoter transcription was not induced by dexamethasone or cotransfected glucocorticoid receptor. In addition, the induction of apoA-I gene transcription by dexamethasone was blocked by the protein-synthesis inhibitor cycloheximide, which suggests the presence of a labile protein involved in apoA-I gene activation by dexamethasone. In conclusion, our results demonstrate that dexamethasone regulates rat apoA-I, but not apoA-II, gene expression through direct action on the hepatocyte. The induction of apoA-I gene transcription by dexamethasone requires the glucocorticoid receptor and a labile cell-specific protein.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Apolipoprotein A-I / biosynthesis*
  • Apolipoprotein A-II / biosynthesis*
  • Base Sequence
  • Carcinoma, Hepatocellular
  • Cell Line
  • Cell Nucleus / metabolism
  • Cells, Cultured
  • Chloramphenicol O-Acetyltransferase / biosynthesis
  • Chlorocebus aethiops
  • Cloning, Molecular
  • DNA Primers
  • Dactinomycin / pharmacology
  • Dexamethasone / pharmacology*
  • Glucocorticoids / pharmacology*
  • Kinetics
  • Liver / drug effects
  • Liver / metabolism*
  • Male
  • Mifepristone / pharmacology
  • Molecular Sequence Data
  • Polymerase Chain Reaction
  • RNA, Messenger / biosynthesis
  • Rats
  • Rats, Sprague-Dawley
  • Receptors, Glucocorticoid / drug effects
  • Receptors, Glucocorticoid / physiology*
  • Recombinant Proteins / biosynthesis
  • Transcription, Genetic* / drug effects
  • Transfection

Substances

  • Apolipoprotein A-I
  • Apolipoprotein A-II
  • DNA Primers
  • Glucocorticoids
  • RNA, Messenger
  • Receptors, Glucocorticoid
  • Recombinant Proteins
  • Dactinomycin
  • Mifepristone
  • Dexamethasone
  • Chloramphenicol O-Acetyltransferase