The role of NF-kappa B in TNF-related apoptosis-inducing ligand (TRAIL)-induced apoptosis of melanoma cells

J Immunol. 2001 May 1;166(9):5337-45. doi: 10.4049/jimmunol.166.9.5337.

Abstract

Previous studies have shown that activation of NF-kappaB can inhibit apoptosis induced by a number of stimuli. It is also known that TNF-related apoptosis-inducing ligand (TRAIL) can activate NF-kappaB through the death receptors TRAIL-R1 and TRAIL-R2, and decoy receptor TRAIL-R4. In view of these findings, we have investigated the extent to which activation of NF-kappaB may account for the variable responses of melanoma lines to apoptosis induced by TRAIL and other TNF family members. Pretreatment of the melanoma lines with the proteasome inhibitor N-acetyl-L-leucinyl-L-leucinyl-L-norleucinal (LLnL), which is known to inhibit activation of NF-kappaB, was shown to markedly increase apoptosis in 10 of 12 melanoma lines with death receptors for TRAIL. The specificity of results for inhibition of NF-kappaB activation was supported by an increase of TRAIL-induced apoptosis in melanoma cells transfected with a degradation-resistant IkappaBalpha. Furthermore, studies with NF-kappaB reporter constructs revealed that the resistance of melanoma lines to TRAIL-induced apoptosis was correlated to activation of NF-kappaB in response to TRAIL. TRAIL-resistant sublines that were generated by intermittent exposure to TRAIL were shown to have high levels of activated NF-kappaB, and resistance to TRAIL could be reversed by LLnL and by the superrepressor form of IkappaBalpha. Therefore, these results suggest that activation of NF-kappaB by TRAIL plays an important role in resistance of melanoma cells to TRAIL-induced apoptosis and further suggest that inhibitors of NF-kappaB may be useful adjuncts in clinical use of TRAIL against melanoma.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Apoptosis / drug effects
  • Apoptosis / genetics
  • Apoptosis / immunology*
  • Apoptosis Regulatory Proteins
  • CD40 Ligand / physiology
  • Cell Culture Techniques
  • Cell Nucleus / immunology
  • Cell Nucleus / metabolism
  • Cysteine Endopeptidases / metabolism
  • Cytoplasm / immunology
  • Cytoplasm / metabolism
  • DNA-Binding Proteins / genetics
  • DNA-Binding Proteins / physiology
  • Fas Ligand Protein
  • Genes, Reporter / immunology
  • Humans
  • I-kappa B Proteins*
  • Immunity, Innate / drug effects
  • Immunity, Innate / genetics
  • Ligands
  • Melanoma / enzymology
  • Melanoma / immunology*
  • Melanoma / pathology*
  • Membrane Glycoproteins / antagonists & inhibitors
  • Membrane Glycoproteins / physiology*
  • Multienzyme Complexes / antagonists & inhibitors
  • Multienzyme Complexes / metabolism
  • NF-KappaB Inhibitor alpha
  • NF-kappa B / antagonists & inhibitors
  • NF-kappa B / genetics
  • NF-kappa B / metabolism
  • NF-kappa B / physiology*
  • Proteasome Endopeptidase Complex
  • Repressor Proteins / physiology
  • TNF-Related Apoptosis-Inducing Ligand
  • Tumor Cells, Cultured
  • Tumor Necrosis Factor-alpha / antagonists & inhibitors
  • Tumor Necrosis Factor-alpha / physiology*

Substances

  • Apoptosis Regulatory Proteins
  • DNA-Binding Proteins
  • FASLG protein, human
  • Fas Ligand Protein
  • I-kappa B Proteins
  • Ligands
  • Membrane Glycoproteins
  • Multienzyme Complexes
  • NF-kappa B
  • NFKBIA protein, human
  • Repressor Proteins
  • TNF-Related Apoptosis-Inducing Ligand
  • TNFSF10 protein, human
  • Tumor Necrosis Factor-alpha
  • NF-KappaB Inhibitor alpha
  • CD40 Ligand
  • Cysteine Endopeptidases
  • Proteasome Endopeptidase Complex