Regulation of the HIF-1alpha stability by histone deacetylases

Oncol Rep. 2007 Mar;17(3):647-51.

Abstract

Histone deacetylase inhibitors (HDACIs) are currently in clinical trials partly due to their potent anti-angiogenic effects. However, the detailed mechanism of their action is unclear. Here, we observed that several HDACIs (TSA, SB, Apicidin, and VPA) dramatically decreased HIF-1alpha protein level and transcriptional activity of HIF-1 in human and mouse tumor cell lines. Furthermore, class I HDACs, HDAC1 and 3 enhanced HIF-1alpha stability and HIF-1 transactivation function in hypoxic conditions. In addition, immunoprecipitation and in vitro binding assays revealed that HDAC1 and 3 directly bind to the oxygen-dependent degradation domain of HIF-1alpha. Collectively, these results suggest that HDAC1 and 3 are considered as a positive regulator of HIF-1alpha stability via direct interaction and may play an important role in HIF-1-induced tumor angiogenesis.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Blotting, Western
  • Cell Line, Tumor
  • Enzyme Inhibitors / pharmacology*
  • HeLa Cells
  • Histone Deacetylase Inhibitors*
  • Histone Deacetylases / drug effects*
  • Humans
  • Hydroxamic Acids / pharmacology
  • Hypoxia-Inducible Factor 1, alpha Subunit / drug effects
  • Hypoxia-Inducible Factor 1, alpha Subunit / metabolism*
  • Immunoprecipitation
  • Mice
  • Peptides, Cyclic / pharmacology
  • Reverse Transcriptase Polymerase Chain Reaction
  • Transcriptional Activation / drug effects
  • Valproic Acid / pharmacology

Substances

  • Enzyme Inhibitors
  • HIF1A protein, human
  • Histone Deacetylase Inhibitors
  • Hydroxamic Acids
  • Hypoxia-Inducible Factor 1, alpha Subunit
  • Peptides, Cyclic
  • apicidin
  • trichostatin A
  • Valproic Acid
  • Histone Deacetylases