Cytokines suppress adipogenesis and PPAR-gamma function through the TAK1/TAB1/NIK cascade

Nat Cell Biol. 2003 Mar;5(3):224-30. doi: 10.1038/ncb942.

Abstract

Pluripotent mesenchymal stem cells in bone marrow differentiate into adipocytes, osteoblasts and other cells. Balanced cytodifferentiation of stem cells is essential for the formation and maintenance of bone marrow; however, the mechanisms that control this balance remain largely unknown. Whereas cytokines such as interleukin-1 (IL-1) and tumour-necrosis factor-alpha (TNF-alpha) inhibit adipogenesis, the ligand-induced transcription factor peroxisome proliferator-activated receptor-gamma (PPAR-gamma), is a key inducer of adipogenesis. Therefore, regulatory coupling between cytokine- and PPAR-gamma-mediated signals might occur during adipogenesis. Here we show that the ligand-induced transactivation function of PPAR-gamma is suppressed by IL-1 and TNF-alpha, and that this suppression is mediated through NF-kappaB activated by the TAK1/TAB1/NF-kappaB-inducing kinase (NIK) cascade, a downstream cascade associated with IL-1 and TNF-alpha signalling. Unlike suppression of the PPAR-gamma transactivation function by mitogen-activated protein kinase-induced growth factor signalling through phosphorylation of the A/B domain, NF-kappaB blocks PPAR-gamma binding to DNA by forming a complex with PPAR-gamma and its AF-1-specific co-activator PGC-2. Our results suggest that expression of IL-1 and TNF-alpha in bone marrow may alter the fate of pluripotent mesenchymal stem cells, directing cellular differentiation towards osteoblasts rather than adipocytes by suppressing PPAR-gamma function through NF-kappaB activated by the TAK1/TAB1/NIK cascade.

Publication types

  • Research Support, Non-U.S. Gov't
  • Retracted Publication

MeSH terms

  • Adaptor Proteins, Signal Transducing*
  • Adipocytes / cytology*
  • Adipocytes / drug effects
  • Animals
  • Blotting, Northern
  • Blotting, Western
  • Cell Division / physiology*
  • Cell Line
  • Chromans / pharmacology
  • Cytokines / physiology*
  • Electrophoretic Mobility Shift Assay
  • HIV Envelope Protein gp120 / physiology*
  • MAP Kinase Kinase Kinases / physiology*
  • Mice
  • NF-kappaB-Inducing Kinase
  • Plasmids
  • Precipitin Tests
  • Protein Serine-Threonine Kinases / physiology*
  • Receptors, Cytoplasmic and Nuclear / physiology*
  • Recombinant Fusion Proteins / physiology*
  • Signal Transduction
  • Thiazoles / pharmacology
  • Thiazolidinediones*
  • Transcription Factors / physiology*
  • Troglitazone

Substances

  • Adaptor Proteins, Signal Transducing
  • Chromans
  • Cytokines
  • HIV Envelope Protein gp120
  • Receptors, Cytoplasmic and Nuclear
  • Recombinant Fusion Proteins
  • TAB1 protein, human
  • Thiazoles
  • Thiazolidinediones
  • Transcription Factors
  • Protein Serine-Threonine Kinases
  • MAP Kinase Kinase Kinases
  • MAP kinase kinase kinase 7
  • Troglitazone