Histone deacetylase 3 is an epigenomic brake in macrophage alternative activation

Genes Dev. 2011 Dec 1;25(23):2480-8. doi: 10.1101/gad.175950.111.

Abstract

Macrophages, a key cellular component of inflammation, become functionally polarized in a signal- and context-specific manner. Th2 cytokines such as interleukin 4 (IL-4) polarize macrophages to a state of alternative activation that limits inflammation and promotes wound healing. Alternative activation is mediated by a transcriptional program that is influenced by epigenomic modifications, including histone acetylation. Here we report that macrophages lacking histone deacetylase 3 (HDAC3) display a polarization phenotype similar to IL-4-induced alternative activation and, furthermore, are hyperresponsive to IL-4 stimulation. Throughout the macrophage genome, HDAC3 deacetylates histone tails at regulatory regions, leading to repression of many IL-4-regulated genes characteristic of alternative activation. Following exposure to Schistosoma mansoni eggs, a model of Th2 cytokine-mediated disease that is limited by alternative activation, pulmonary inflammation was ameliorated in mice lacking HDAC3 in macrophages. Thus, HDAC3 functions in alternative activation as a brake whose release could be of benefit in the treatment of multiple inflammatory diseases.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Epigenesis, Genetic*
  • Histone Deacetylases / genetics*
  • Histone Deacetylases / metabolism
  • Interleukin-4 / genetics
  • Interleukin-4 / metabolism
  • Macrophage Activation / genetics*
  • Macrophages / immunology
  • Macrophages / metabolism*
  • Mice
  • Mice, Inbred Strains
  • Pneumonia / enzymology
  • Pneumonia / immunology
  • Pneumonia / parasitology
  • Schistosoma mansoni
  • Th2 Cells / immunology
  • Th2 Cells / metabolism

Substances

  • Interleukin-4
  • Histone Deacetylases
  • histone deacetylase 3