Breakdown of the FLT3-ITD/STAT5 axis and synergistic apoptosis induction by the histone deacetylase inhibitor panobinostat and FLT3-specific inhibitors

Mol Cancer Ther. 2012 Nov;11(11):2373-83. doi: 10.1158/1535-7163.MCT-12-0129. Epub 2012 Aug 31.

Abstract

Activating mutations of the class III receptor tyrosine kinase FLT3 are the most frequent molecular aberration in acute myeloid leukemia (AML). Mutant FLT3 accelerates proliferation, suppresses apoptosis, and correlates with poor prognosis. Therefore, it is a promising therapeutic target. Here, we show that RNA interference against FLT3 with an internal tandem duplication (FLT3-ITD) potentiates the efficacy of the histone deacetylase inhibitor (HDACi) panobinostat (LBH589) against AML cells expressing FLT3-ITD. Similar to RNA interference, tyrosine kinase inhibitors (TKI; AC220/cpd.102/PKC412) in combination with LBH589 exhibit superior activity against AML cells. Median dose-effect analyses of drug-induced apoptosis rates of AML cells (MV4-11 and MOLM-13) revealed combination index (CI) values indicating strong synergism. AC220, the most potent and FLT3-specific TKI, shows highest synergism with LBH589 in the low nanomolar range. A 4-hour exposure to LBH589 + AC220 already generates more than 50% apoptosis after 24 hours. Different cell lines lacking FLT3-ITD as well as normal peripheral blood mononuclear cells are not significantly affected by LBH589 + TKI, showing the specificity of this treatment regimen. Immunoblot analyses show that LBH589 + TKI induce apoptosis via degradation of FLT3-ITD and its prosurvival target STAT5. Previously, we showed the LBH589-induced proteasomal degradation of FLT3-ITD. Here, we show that activated caspase-3 also contributes to the degradation of FLT3-ITD and that STAT5 is a direct target of this protease. Our data strongly emphasize HDACi/TKI drug combinations as promising modality for the treatment of FLT3-ITD-positive AMLs.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Apoptosis / drug effects*
  • Benzothiazoles / chemistry
  • Benzothiazoles / pharmacology
  • Caspases / metabolism
  • Cell Line
  • Drug Synergism
  • Gene Duplication*
  • Gene Knockdown Techniques
  • Histone Deacetylase Inhibitors / chemistry
  • Histone Deacetylase Inhibitors / pharmacology*
  • Humans
  • Hydroxamic Acids / chemistry
  • Hydroxamic Acids / pharmacology*
  • Indoles / chemistry
  • Indoles / pharmacology*
  • Leukemia, Myeloid, Acute / pathology
  • Panobinostat
  • Phenylurea Compounds / chemistry
  • Phenylurea Compounds / pharmacology
  • Protein Kinase Inhibitors / chemistry
  • Protein Kinase Inhibitors / pharmacology
  • Protein Stability / drug effects
  • Proteolysis / drug effects
  • STAT5 Transcription Factor / metabolism*
  • Signal Transduction / drug effects
  • Staurosporine / analogs & derivatives
  • Staurosporine / chemistry
  • Staurosporine / pharmacology
  • fms-Like Tyrosine Kinase 3 / antagonists & inhibitors*
  • fms-Like Tyrosine Kinase 3 / genetics*
  • fms-Like Tyrosine Kinase 3 / metabolism

Substances

  • Benzothiazoles
  • Histone Deacetylase Inhibitors
  • Hydroxamic Acids
  • Indoles
  • Phenylurea Compounds
  • Protein Kinase Inhibitors
  • STAT5 Transcription Factor
  • quizartinib
  • Panobinostat
  • FLT3 protein, human
  • fms-Like Tyrosine Kinase 3
  • Caspases
  • Staurosporine
  • midostaurin