Involvement of double-stranded RNA-activated protein kinase in the synergistic activation of nuclear factor-kappaB by tumor necrosis factor-alpha and gamma-interferon in preneuronal cells

J Biol Chem. 1999 Feb 19;274(8):4801-6. doi: 10.1074/jbc.274.8.4801.

Abstract

Tumor necrosis factor-alpha (TNF-alpha) and gamma-interferon (IFN-gamma) cooperate during a variety of biological responses and ultimately synergistically enhance the expression of genes involved in immune and inflammatory responses. Recently, we demonstrated that IFN-gamma can significantly potentiate TNF-alpha-induced nuclear factor (NF)-kappaB nuclear translocation in neuronal derived and endothelial cell lines. The mechanism by which these two cytokines exert their synergistic effect on NF-kappaB involves the de novo degradation of the NF-kappaB inhibitor, IkappaBbeta. The double-stranded RNA-dependent kinase PKR is IFN-inducible and has been implicated in the activation of NF-kappaB; therefore, we examined the possibility that PKR may play a role in the synergistic activation of NF-kappaB during TNF-alpha/IFN-gamma cotreatment. The PKR inhibitor 2-aminopurine (2-AP) inhibited TNF-alpha/IFN-gamma-induced NF-kappaB nuclear translocation in neuronal derived cells but not in endothelial cells. The induced degradation of IkappaBbeta, which is normally observed upon TNF-alpha/IFN-gamma cotreatment, was blocked completely by 2-AP in neuronal derived cells. Also, 2-AP treatment or overexpression of a catalytically inactive PKR inhibited the TNF-alpha/IFN-gamma-induced synergistic activation of kappaB-dependent gene expression. Our results suggest that the signal generated by IFN-gamma during TNF-alpha/IFN-gamma cotreatment may require PKR to elicit enhanced NF-kappaB activity, and this signal may affect the stability of the IkappaBbeta protein.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • 2-Aminopurine / pharmacology
  • Animals
  • Biological Transport
  • Cell Nucleus / drug effects
  • Cell Nucleus / metabolism
  • DNA-Binding Proteins / metabolism
  • I-kappa B Proteins*
  • Interferon-gamma / pharmacology*
  • NF-kappa B / antagonists & inhibitors
  • NF-kappa B / metabolism*
  • Neurons / drug effects*
  • Neurons / enzymology
  • Neurons / metabolism
  • PC12 Cells
  • Rats
  • Tumor Necrosis Factor-alpha / pharmacology*
  • eIF-2 Kinase / metabolism*

Substances

  • DNA-Binding Proteins
  • I kappa B beta protein
  • I-kappa B Proteins
  • NF-kappa B
  • Tumor Necrosis Factor-alpha
  • 2-Aminopurine
  • Interferon-gamma
  • eIF-2 Kinase