Cooperative interaction of hypoxia-inducible factor-2alpha (HIF-2alpha ) and Ets-1 in the transcriptional activation of vascular endothelial growth factor receptor-2 (Flk-1)

J Biol Chem. 2003 Feb 28;278(9):7520-30. doi: 10.1074/jbc.M211298200. Epub 2002 Dec 2.

Abstract

Interactions between Ets family members and a variety of other transcription factors serve important functions during development and differentiation processes, e.g. in the hematopoietic system. Here we show that the endothelial basic helix-loop-helix PAS domain transcription factor, hypoxia-inducible factor-2alpha (HIF-2alpha) (but not its close relative HIF-1alpha), cooperates with Ets-1 in activating transcription of the vascular endothelial growth factor receptor-2 (VEGF-2) gene (Flk-1). The receptor tyrosine kinase Flk-1 is indispensable for angiogenesis, and its expression is closely regulated during development. Consistent with the hypothesis that HIF-2alpha controls the expression of Flk-1 in vivo, we show here that HIF-2alpha and Flk-1 are co-regulated in postnatal mouse brain capillaries. A tandem HIF-2alpha/Ets binding site was identified within the Flk-1 promoter that acted as a strong enhancer element. Based on the analysis of transgenic mouse embryos, these motifs are essential for endothelial cell-specific reporter gene expression. A single HIF-2alpha/Ets element conferred strong cooperative induction by HIF-2alpha and Ets-1 when fused to a heterologous promoter and was most active in endothelial cells. The physical interaction of HIF-2alpha with Ets-1 was demonstrated and localized to the HIF-2alpha carboxyl terminus and the autoinhibitory exon VII domain of Ets-1, respectively. The deletion of the DNA binding and carboxyl-terminal transactivation domains of HIF-2alpha, respectively, created dominant negative mutants that suppressed transactivation by the wild type protein and failed to synergize with Ets-1. These results suggest that the interaction between HIF-2alpha and endothelial Ets factors is required for the full transcriptional activation of Flk-1 in endothelial cells and may therefore represent a future target for the manipulation of angiogenesis.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Age Factors
  • Amino Acid Motifs
  • Animals
  • Basic Helix-Loop-Helix Transcription Factors
  • Binding Sites
  • Blotting, Western
  • Cell Differentiation
  • Cell Division
  • Cell Line
  • Cell Nucleus / metabolism
  • Dose-Response Relationship, Drug
  • Embryo, Mammalian / metabolism
  • Endothelium / cytology
  • Endothelium / metabolism
  • Exons
  • Gene Deletion
  • Gene Expression Regulation, Developmental
  • Genes, Reporter
  • Genetic Vectors
  • Glutathione Transferase / metabolism
  • Humans
  • Immunohistochemistry
  • In Situ Hybridization
  • Luciferases / metabolism
  • Mice
  • Mice, Transgenic
  • Mutagenesis, Site-Directed
  • Neovascularization, Pathologic
  • Plasmids / metabolism
  • Promoter Regions, Genetic
  • Protein Binding
  • Protein Biosynthesis
  • Protein Structure, Tertiary
  • Proto-Oncogene Protein c-ets-1
  • Proto-Oncogene Proteins / chemistry
  • Proto-Oncogene Proteins / metabolism*
  • Proto-Oncogene Proteins c-ets
  • RNA, Messenger / metabolism
  • Recombinant Fusion Proteins / metabolism
  • Time Factors
  • Trans-Activators / chemistry
  • Trans-Activators / metabolism*
  • Transcription Factors / chemistry
  • Transcription Factors / metabolism*
  • Transfection
  • Transgenes
  • Vascular Endothelial Growth Factor Receptor-2 / genetics*
  • Vascular Endothelial Growth Factor Receptor-2 / metabolism*

Substances

  • Basic Helix-Loop-Helix Transcription Factors
  • ETS1 protein, human
  • Ets1 protein, mouse
  • Proto-Oncogene Protein c-ets-1
  • Proto-Oncogene Proteins
  • Proto-Oncogene Proteins c-ets
  • RNA, Messenger
  • Recombinant Fusion Proteins
  • Trans-Activators
  • Transcription Factors
  • endothelial PAS domain-containing protein 1
  • Luciferases
  • Glutathione Transferase
  • Vascular Endothelial Growth Factor Receptor-2