Mechanistic target of rapamycin inhibition extends cellular lifespan in dendritic cells by preserving mitochondrial function

J Immunol. 2014 Sep 15;193(6):2821-30. doi: 10.4049/jimmunol.1302498. Epub 2014 Aug 8.

Abstract

TLR-mediated activation of dendritic cells (DCs) is associated with a metabolic transition in which mitochondrial oxidative phosphorylation is inhibited by endogenously synthesized NO and the cells become committed to glucose and aerobic glycolysis for survival. We show that inhibition of mechanistic target of rapamycin (mTOR) extends the lifespan of TLR-activated DCs by inhibiting the induction of NO production, thereby allowing the cells to continue to use their mitochondria to generate ATP, and allowing them the flexibility to use fatty acids or glucose as nutrients to fuel core metabolism. These data provide novel mechanistic insights into how mTOR modulates DC metabolism and cellular longevity following TLR activation and provide an explanation for previous findings that mTOR inhibition enhances the efficacy of DCs in autologous vaccination.

Publication types

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

MeSH terms

  • Adenosine Triphosphate / biosynthesis
  • Animals
  • Cells, Cultured
  • Cellular Senescence / immunology
  • Dendritic Cells / immunology
  • Dendritic Cells / metabolism*
  • Fatty Acids / metabolism
  • Glucose / metabolism
  • Glycolysis
  • Lipopolysaccharides
  • Mice
  • Mice, Inbred C57BL
  • Mitochondria / metabolism*
  • Nitric Oxide / metabolism
  • Nitric Oxide Synthase Type II / biosynthesis
  • Nitric Oxide Synthase Type II / genetics
  • Nitric Oxide Synthase Type II / metabolism*
  • Oxidative Phosphorylation
  • Protein Biosynthesis
  • TOR Serine-Threonine Kinases / antagonists & inhibitors*
  • Toll-Like Receptors / immunology*
  • Transcription, Genetic
  • Vaccination

Substances

  • Fatty Acids
  • Lipopolysaccharides
  • Toll-Like Receptors
  • Nitric Oxide
  • Adenosine Triphosphate
  • Nitric Oxide Synthase Type II
  • Nos2 protein, mouse
  • mTOR protein, mouse
  • TOR Serine-Threonine Kinases
  • Glucose