AF4 and AF4-MLL mediate transcriptional elongation of 5-lipoxygenase mRNA by 1, 25-dihydroxyvitamin D3

Oncotarget. 2015 Sep 22;6(28):25784-800. doi: 10.18632/oncotarget.4703.

Abstract

The human 5-lipoxygenase (5-LO), encoded by the ALOX5 gene, is the key enzyme in the formation of pro-inflammatory leukotrienes. ALOX5 gene transcription is strongly stimulated by calcitriol (1α, 25-dihydroxyvitamin D3) and TGFβ (transforming growth factor-β). Here, we investigated the influence of MLL (activator of transcript initiation), AF4 (activator of transcriptional elongation) as well as of the leukemogenic fusion proteins MLL-AF4 (ectopic activator of transcript initiation) and AF4-MLL (ectopic activator of transcriptional elongation) on calcitriol/TGFβ-dependent 5-LO transcript elongation. We present evidence that the AF4 complex directly interacts with the vitamin D receptor (VDR) and promotes calcitriol-dependent ALOX5 transcript elongation. Activation of transcript elongation was strongly enhanced by the AF4-MLL fusion protein but was sensitive to Flavopiridol. By contrast, MLL-AF4 displayed no effect on transcriptional elongation. Furthermore, HDAC class I inhibitors inhibited the ectopic effects caused by AF4-MLL on transcriptional elongation, suggesting that HDAC class I inhibitors are potential therapeutics for the treatment of t(4;11)(q21;q23) leukemia.

Keywords: 5-lipoxygenase; AF4; HDAC; MLL; calcitriol.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Arachidonate 5-Lipoxygenase / biosynthesis*
  • Arachidonate 5-Lipoxygenase / genetics
  • Calcitriol / pharmacology*
  • Cyclin-Dependent Kinase 9 / antagonists & inhibitors
  • Cyclin-Dependent Kinase 9 / metabolism
  • DNA-Binding Proteins / genetics
  • DNA-Binding Proteins / metabolism*
  • Enzyme Induction
  • HEK293 Cells
  • HeLa Cells
  • Histone Deacetylase Inhibitors / pharmacology
  • Histone-Lysine N-Methyltransferase / genetics
  • Histone-Lysine N-Methyltransferase / metabolism*
  • Humans
  • Leukemia / drug therapy
  • Leukemia / enzymology*
  • Leukemia / genetics
  • Ligands
  • Myeloid-Lymphoid Leukemia Protein / genetics
  • Myeloid-Lymphoid Leukemia Protein / metabolism*
  • Nuclear Proteins / genetics
  • Nuclear Proteins / metabolism*
  • Oncogene Proteins, Fusion / genetics
  • Oncogene Proteins, Fusion / metabolism*
  • Promoter Regions, Genetic
  • Proteasome Endopeptidase Complex / metabolism
  • Proteasome Inhibitors / pharmacology
  • Protein Binding
  • Protein Kinase Inhibitors / pharmacology
  • Proteolysis
  • RNA Interference
  • RNA, Messenger / biosynthesis*
  • RNA, Messenger / genetics
  • Receptors, Calcitriol / agonists
  • Receptors, Calcitriol / metabolism
  • Transcription Elongation, Genetic / drug effects*
  • Transcriptional Elongation Factors
  • Transfection

Substances

  • DNA-Binding Proteins
  • Histone Deacetylase Inhibitors
  • KMT2A protein, human
  • Ligands
  • MLL-AF4 fusion protein, human
  • Nuclear Proteins
  • Oncogene Proteins, Fusion
  • Proteasome Inhibitors
  • Protein Kinase Inhibitors
  • RNA, Messenger
  • Receptors, Calcitriol
  • Transcriptional Elongation Factors
  • VDR protein, human
  • Myeloid-Lymphoid Leukemia Protein
  • AFF1 protein, human
  • Arachidonate 5-Lipoxygenase
  • ALOX5 protein, human
  • Histone-Lysine N-Methyltransferase
  • CDK9 protein, human
  • Cyclin-Dependent Kinase 9
  • Proteasome Endopeptidase Complex
  • Calcitriol