Metabolic-epigenetic crosstalk in macrophage activation

Epigenomics. 2015 Oct;7(7):1155-64. doi: 10.2217/epi.15.71. Epub 2015 Nov 20.

Abstract

Epigenetic enzymes are emerging as crucial controllers of macrophages, innate immune cells that determine the outcome of many inflammatory diseases. Recent studies demonstrate that the activity of particular chromatin-modifying enzymes is regulated by the availability of specific metabolites like acetyl-coenzyme A, S-adenosylmethionine, α-ketoglutarate, nicotinamide adenine dinucleotide and polyamines. In this way chromatin-modifying enzymes could sense the macrophage's metabolic status and translate this into gene expression and phenotypic changes. Importantly, distinct macrophage activation subsets display particular metabolic pathways. IFNγ/lipopolysaccharide-activated macrophages (MIFNγ/LPS or M1) display high glycolysis, which directly drives their inflammatory phenotype. In contrast, oxidative mitochondrial metabolism and enhanced polyamine production are hallmarks and requirements for IL-4-induced macrophage activation (MIL-4 or M2). Here we report how epigenetics could serve as a bridge between altered macrophage metabolism, macrophage activation and disease.

Keywords: chromatin-modifying enzymes; epigenetics; histone acetylation and methylation; inflammation; macrophages; metabolism.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acetyl Coenzyme A / metabolism
  • Acetylation
  • Chromatin / chemistry
  • Chromatin / drug effects
  • Chromatin / metabolism
  • Epigenesis, Genetic*
  • Glycolysis / drug effects
  • Glycolysis / genetics
  • Histone Deacetylases / genetics
  • Histone Deacetylases / immunology
  • Histone Deacetylases / metabolism*
  • Histones / genetics
  • Histones / metabolism
  • Humans
  • Immunity, Innate
  • Interferon-gamma / pharmacology
  • Interleukin-4 / pharmacology
  • Intracellular Signaling Peptides and Proteins / genetics
  • Intracellular Signaling Peptides and Proteins / immunology
  • Intracellular Signaling Peptides and Proteins / metabolism*
  • Isoenzymes / genetics
  • Isoenzymes / immunology
  • Isoenzymes / metabolism
  • Ketoglutaric Acids / metabolism
  • Lipopolysaccharides / pharmacology
  • Macrophage Activation / drug effects
  • Macrophages / drug effects
  • Macrophages / immunology
  • Macrophages / metabolism*
  • Mixed Function Oxygenases / genetics
  • Mixed Function Oxygenases / immunology
  • Mixed Function Oxygenases / metabolism*
  • NAD / metabolism
  • Oxidative Phosphorylation / drug effects
  • Polyamines / metabolism
  • Protein-Arginine N-Methyltransferases / genetics
  • Protein-Arginine N-Methyltransferases / immunology
  • Protein-Arginine N-Methyltransferases / metabolism*
  • Proto-Oncogene Proteins / genetics
  • Proto-Oncogene Proteins / immunology
  • Proto-Oncogene Proteins / metabolism*
  • Repressor Proteins / genetics
  • Repressor Proteins / immunology
  • Repressor Proteins / metabolism*
  • S-Adenosylmethionine / metabolism

Substances

  • Chromatin
  • DMAP1 protein, human
  • Histones
  • IL4 protein, human
  • Intracellular Signaling Peptides and Proteins
  • Isoenzymes
  • Ketoglutaric Acids
  • Lipopolysaccharides
  • Polyamines
  • Proto-Oncogene Proteins
  • Repressor Proteins
  • NAD
  • Interleukin-4
  • Acetyl Coenzyme A
  • S-Adenosylmethionine
  • Interferon-gamma
  • Mixed Function Oxygenases
  • TET1 protein, human
  • PRMT2 protein, human
  • Protein-Arginine N-Methyltransferases
  • Histone Deacetylases