Anti-inflammatory properties of histone deacetylase inhibitors: a mechanistic study

J Trauma Acute Care Surg. 2012 Feb;72(2):347-53; discussion 353-4. doi: 10.1097/TA.0b013e318243d8b2.

Abstract

Background: We have demonstrated that postshock administration of suberoylanilide hydroxamic acid (SAHA), a histone deacetylase inhibitor, can significantly improve early survival in a highly lethal model of hemorrhagic shock. As the primary insult in hemorrhagic shock is cellular hypoxia, and transcription factor hypoxia-inducible factor-1α (HIF-1α) controls proinflammatory gene expression in macrophages, we hypothesized that SAHA would attenuate the HIF-1α associated proinflammatory pathway in a hypoxic macrophage model.

Methods: Mouse macrophages were exposed to hypoxic conditions (0.5% O2, 10% CO2, and 89.5% N2) at 37°C in the presence or absence of SAHA (10 μmol/L). The cells and culture medium were harvested at 1 hour, 4 hours, and 8 hours. Sham (no hypoxia, no SAHA) served as a control. Western blots were performed to assess protein levels of prolyl hydroxylase 2 (PHD2), HIF-1α, and inducible nitric oxide synthase (iNOS) in the cells. Colorimetric biochemical assay and enzyme-linked immunosorbent assay were used to analyze the release of nitric oxide (NO) and secretion of tumor necrosis factor α (TNF-α), respectively, in the cell culture medium.

Results: Hypoxia significantly increased cellular level of HIF-1α (1 hour and 4 hours), gene transcription of iNOS (4 hours and 8 hours), iNOS protein (8 hours), NO production (8 hours), and TNF-α secretion (4 hours and 8 hours). SAHA treatment attenuated all of the above hypoxia-induced alterations in the macrophages. In addition, SAHA treatment significantly increased cellular level of PHD2, one of the upstream negative regulators of HIF-1α, at 1 hour.

Conclusions: Treatment with SAHA attenuates hypoxia-HIF-1α-inflammatory pathway in macrophages and suppresses hypoxia-induced release of proinflammatory NO and TNF-α. SAHA also causes an early increase in cellular PHD2, which provides, at least in part, a new explanation for the decrease in the HIF-1α protein levels.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Animals
  • Anti-Inflammatory Agents / pharmacology*
  • Blotting, Western
  • Cell Hypoxia
  • Cells, Cultured
  • Colorimetry
  • Enzyme-Linked Immunosorbent Assay
  • Histone Deacetylase Inhibitors / pharmacology*
  • Hydroxamic Acids / pharmacology*
  • Macrophages / drug effects*
  • Macrophages / metabolism*
  • Mice
  • Nitric Oxide / metabolism
  • Nitric Oxide Synthase Type II / metabolism
  • RNA / analysis
  • Real-Time Polymerase Chain Reaction
  • Shock, Hemorrhagic / drug therapy*
  • Tumor Necrosis Factor-alpha / metabolism
  • Vorinostat

Substances

  • Anti-Inflammatory Agents
  • Histone Deacetylase Inhibitors
  • Hydroxamic Acids
  • Tumor Necrosis Factor-alpha
  • Nitric Oxide
  • Vorinostat
  • RNA
  • Nitric Oxide Synthase Type II