The novel triterpenoid 2-cyano-3,12-dioxooleana-1,9-dien-28-oic acid (CDDO) potently enhances apoptosis induced by tumor necrosis factor in human leukemia cells

J Biol Chem. 2002 May 10;277(19):16448-55. doi: 10.1074/jbc.M108974200. Epub 2002 Mar 5.

Abstract

Tumor necrosis factor (TNF) is a potent activator of the nuclear factor-kappaB (NF-kappaB) pathway that leads to up-regulation of anti-apoptotic proteins. Hence, TNF induces apoptosis in the presence of inhibitors of protein or RNA synthesis. We report that a novel triterpenoid, 2-cyano-3,12-dioxooleana-1,9,-dien-28-oic acid (CDDO) inhibits NF-kappaB-mediated gene expression at a step after translocation of activated NF-kappaB to the nucleus. This effect appears specific for the NF-kappaB pathway as CDDO does not inhibit gene expression induced by the phorbol ester 12-0-tetradecanoylphorbol-13-acetate (TPA). CDDO in combination with TNF caused a dramatic increase in apoptosis in ML-1 leukemia cells that was associated with activation of caspase-8, cleavage of Bid, translocation of Bax, cytochrome c release, and caspase-3 activation. Experiments with caspase inhibitors demonstrated that caspase-8 was an initiator of this pathway. TNF also induced a transient activation of c-Jun N-terminal kinase (JNK), which upon addition of CDDO was converted to a sustained activation. The activation of JNK was also dependent on caspase-8. Sustained activation of JNK is frequently pro-apoptotic, yet inhibition of JNK did not prevent Bax translocation or cytochrome c release, demonstrating its lack of involvement in CDDO/TNF-induced apoptosis. Apoptosis was acutely induced by CDDO/TNF in every leukemia cell line tested including those that overexpress Bcl-x(L), suggesting that the mitochondrial pathway is not required for apoptosis by this combination. These results suggest that the apoptotic potency of the CDDO/TNF combination occurs through selective inhibition of NF-kappaB-dependent anti-apoptotic proteins, bypassing potential mitochondrial resistance mechanisms, and thus may provide a basis for the development of novel approaches to the treatment of leukemia.

Publication types

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

MeSH terms

  • Apoptosis*
  • Carcinogens
  • Caspase 3
  • Caspase 8
  • Caspase 9
  • Caspases / metabolism
  • Cell Nucleus / metabolism
  • Chromatin / metabolism
  • Cytochrome c Group / metabolism
  • Cytosol / metabolism
  • DNA-Binding Proteins / metabolism
  • Dose-Response Relationship, Drug
  • Enzyme Activation
  • Gene Expression Regulation
  • Humans
  • I-kappa B Proteins*
  • Immunoblotting
  • JNK Mitogen-Activated Protein Kinases*
  • Leukemia / pathology*
  • MAP Kinase Kinase 4
  • Mitochondria / metabolism
  • Mitogen-Activated Protein Kinase Kinases / metabolism
  • NF-KappaB Inhibitor alpha
  • NF-kappa B / metabolism
  • Nitric Oxide / antagonists & inhibitors
  • Oleanolic Acid / analogs & derivatives*
  • Oleanolic Acid / chemistry*
  • Oleanolic Acid / pharmacology*
  • Protein Transport
  • Proto-Oncogene Proteins / metabolism
  • Proto-Oncogene Proteins c-bcl-2 / metabolism
  • Signal Transduction
  • Tetradecanoylphorbol Acetate
  • Time Factors
  • Tumor Cells, Cultured
  • Tumor Necrosis Factor-alpha / metabolism*
  • bcl-2-Associated X Protein
  • bcl-X Protein

Substances

  • 2-cyano-3,12-dioxoolean-1,9-dien-28-oic acid
  • BAX protein, human
  • BCL2L1 protein, human
  • Carcinogens
  • Chromatin
  • Cytochrome c Group
  • DNA-Binding Proteins
  • I-kappa B Proteins
  • NF-kappa B
  • NFKBIA protein, human
  • Proto-Oncogene Proteins
  • Proto-Oncogene Proteins c-bcl-2
  • Tumor Necrosis Factor-alpha
  • bcl-2-Associated X Protein
  • bcl-X Protein
  • NF-KappaB Inhibitor alpha
  • Nitric Oxide
  • Oleanolic Acid
  • JNK Mitogen-Activated Protein Kinases
  • MAP Kinase Kinase 4
  • Mitogen-Activated Protein Kinase Kinases
  • CASP3 protein, human
  • CASP8 protein, human
  • CASP9 protein, human
  • Caspase 3
  • Caspase 8
  • Caspase 9
  • Caspases
  • Tetradecanoylphorbol Acetate