Highly effective combination of LSD1 (KDM1A) antagonist and pan-histone deacetylase inhibitor against human AML cells

Leukemia. 2014 Nov;28(11):2155-64. doi: 10.1038/leu.2014.119. Epub 2014 Apr 4.

Abstract

The histone demethylase LSD1 (KDM1A) demethylates mono- and di-methylated (Me2) lysine (K) 4 on histone H3. High LSD1 expression blocks differentiation and confers a poor prognosis in acute myeloid leukemia (AML). Here, treatment with the novel LSD1 antagonist SP2509 attenuated the binding of LSD1 with the corepressor CoREST, increased the permissive H3K4Me3 mark on the target gene promoters, and increased the levels of p21, p27 and CCAAT/enhancer binding protein α in cultured AML cells. In addition, SP2509 treatment or LSD1 shRNA inhibited the colony growth of AML cells. SP2509 also induced morphological features of differentiation in the cultured and primary AML blasts. SP2509 induced more apoptosis of AML cells expressing mutant NPM1 than mixed-lineage leukemia fusion oncoproteins. Treatment with SP2509 alone significantly improved the survival of immune-depleted mice following tail-vein infusion and engraftment of cultured or primary human AML cells. Co-treatment with pan-HDAC inhibitor (HDI) panobinostat (PS) and SP2509 was synergistically lethal against cultured and primary AML blasts. Compared with each agent alone, co-treatment with SP2509 and PS significantly improved the survival of the mice engrafted with the human AML cells, without exhibiting any toxicity. Collectively, these findings show that the combination of LSD1 antagonist and pan-HDI is a promising therapy warranting further testing against AML.

MeSH terms

  • Animals
  • Apoptosis / drug effects
  • Cells, Cultured
  • Co-Repressor Proteins / metabolism
  • Disease Models, Animal
  • Enzyme Inhibitors / pharmacology*
  • Female
  • Histone Acetyltransferases / antagonists & inhibitors*
  • Histone Acetyltransferases / metabolism
  • Histone Demethylases / antagonists & inhibitors*
  • Histone Demethylases / genetics
  • Histone Demethylases / metabolism
  • Histones / metabolism
  • Humans
  • Hydrazines / pharmacology*
  • Leukemia, Myeloid, Acute / drug therapy*
  • Leukemia, Myeloid, Acute / genetics
  • Leukemia, Myeloid, Acute / metabolism
  • Mice, Inbred NOD
  • Mice, SCID
  • Nerve Tissue Proteins / metabolism
  • Nucleophosmin
  • RNA, Small Interfering / genetics
  • Stem Cells / cytology
  • Sulfonamides / pharmacology*
  • Tumor Cells, Cultured
  • Xenograft Model Antitumor Assays

Substances

  • Co-Repressor Proteins
  • Enzyme Inhibitors
  • Histones
  • Hydrazines
  • NPM1 protein, human
  • Nerve Tissue Proteins
  • Npm1 protein, mouse
  • RCOR1 protein, human
  • RNA, Small Interfering
  • SP2509
  • Sulfonamides
  • Nucleophosmin
  • Histone Demethylases
  • KDM1A protein, human
  • Histone Acetyltransferases