A histone deacetylation-dependent mechanism for transcriptional repression of the gap junction gene cx43 in prostate cancer cells

Prostate. 2006 Aug 1;66(11):1151-61. doi: 10.1002/pros.20451.

Abstract

Background: The connexin 43 gene (cx43, GJA1) mediates gap junctional intercellular communication (GJIC), which regulates tissue homeostasis. cx43 is frequently downregulated in prostate cancer. We investigated the role of a histone deacetylase (HDAC)-dependent mechanism in the transcriptional repression of cx43 in a panel of prostate cancer cells.

Methods: The impact of Trichostatin A (TSA), an inhibitor of HDAC, on exogenous and endogenous cx43 gene transcription was examined by the luciferase assay, Northern blot, nuclear run-on, Western blot, and chromatin immunoprecipitation assays.

Results: Trichostatin A induces transcription of cx43 gene and GJIC. The co-activator p300/CBP synergizes with TSA for cx43 promoter activation. We identified a promoter region where cooperation between Ap1 and Sp1 elements was essential for TSA-induced cx43 transcription. TSA increased the level of hyperacetylated histones bound to cx43 promoter.

Conclusion: Our results highlight the potential utility of inhibitors of HDAC to restore cx43 gene expression in prostate cancer.

Publication types

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

MeSH terms

  • Acetylation
  • Animals
  • Blotting, Northern
  • Blotting, Western
  • Cell Line, Tumor
  • Connexin 43 / genetics*
  • Down-Regulation*
  • Enzyme Inhibitors / pharmacology
  • Histone Deacetylase Inhibitors
  • Histone Deacetylases / physiology*
  • Histones / metabolism
  • Humans
  • Hydroxamic Acids / pharmacology
  • Immunosorbent Techniques
  • Male
  • Mice
  • NIH 3T3 Cells
  • Promoter Regions, Genetic / genetics
  • Prostatic Neoplasms / genetics*
  • Reverse Transcriptase Polymerase Chain Reaction
  • Transcription, Genetic* / drug effects
  • Transfection

Substances

  • Connexin 43
  • Enzyme Inhibitors
  • Histone Deacetylase Inhibitors
  • Histones
  • Hydroxamic Acids
  • trichostatin A
  • Histone Deacetylases