Post-induction, stimulus-specific regulation of tumor necrosis factor mRNA expression

J Biol Chem. 2007 Apr 20;282(16):11629-38. doi: 10.1074/jbc.M611418200. Epub 2007 Feb 15.

Abstract

The tumor necrosis factor (TNF) gene is activated by multiple extracellular signals in a stimulus- and cell type-specific fashion. Based on the presence of kappaB-like DNA motifs in the region upstream of the TNF gene, some have proposed a direct role for NF-kappaB in lipopolysaccharide (LPS)-induced TNF gene transcription in cells of the monocyte/macrophage lineage. However, we have previously demonstrated a general and critical role for a minimal TNF promoter region bearing only one of the kappaB-like motifs, kappa3, which is bound by nuclear factor of activated T cell proteins in lymphocytes and fibroblasts in response to multiple stimuli and Ets proteins in LPS-stimulated macrophages. Here, in an effort to resolve these contrasting findings, we used a combination of site-directed mutagenesis of the TNF promoter, quantitative DNase I footprinting, and analysis of endogenous TNF mRNA production in response to multiple stimuli under conditions that inhibit NF-kappaB activation (using the proteasome inhibitor lactacystin and using cells lacking either functional NF-kappaB essential modulator, which is the IkappaB kinase regulatory subunit, or the Nemo gene itself). We find that TNF mRNA production in response to ionophore is NF-kappaB-independent, but inhibition of NF-kappaB activation attenuates virus- and LPS-induced TNF mRNA levels after initial induction. We conclude that induction of TNF gene transcription by virus or LPS does not depend upon NF-kappaB binding to the proximal promoter; rather, a stimulus-specific post-induction mechanism involving NF-kappaB, yet to be characterized, is involved in the maintenance of maximal TNF mRNA levels.

Publication types

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

MeSH terms

  • Acetylcysteine / analogs & derivatives
  • Acetylcysteine / pharmacology
  • Amino Acid Motifs
  • Animals
  • DNA / chemistry
  • Deoxyribonuclease I / metabolism
  • Gene Expression Regulation*
  • Humans
  • Ionophores / pharmacology
  • Lipopolysaccharides / metabolism
  • Mice
  • NF-kappa B / metabolism
  • Proteasome Inhibitors
  • Protein Structure, Tertiary
  • RNA, Messenger / metabolism*
  • Tumor Necrosis Factor-alpha / metabolism*

Substances

  • Ionophores
  • Lipopolysaccharides
  • NF-kappa B
  • Proteasome Inhibitors
  • RNA, Messenger
  • Tumor Necrosis Factor-alpha
  • lactacystin
  • DNA
  • Deoxyribonuclease I
  • Acetylcysteine