The soluble extracellular domain of EphB4 (sEphB4) antagonizes EphB4-EphrinB2 interaction, modulates angiogenesis, and inhibits tumor growth

Blood. 2006 Mar 15;107(6):2330-8. doi: 10.1182/blood-2005-04-1655. Epub 2005 Dec 1.

Abstract

The receptor tyrosine kinase EphB4 and its ligand EphrinB2 play a crucial role in vascular development during embryogenesis. The soluble monomeric derivative of the extracellular domain of EphB4 (sEphB4) was designed as an antagonist of EphB4/EphrinB2 signaling. sEphB4 blocks activation of EphB4 and EphrinB2; suppresses endothelial cell migration, adhesion, and tube formation in vitro; and inhibits the angiogenic effects of various growth factors (VEGF and bFGF) in vivo. sEphB4 also inhibits tumor growth in murine tumor xenograft models. sEphB4 is thus a therapeutic candidate for vascular proliferative diseases and cancer.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Angiogenesis Inhibitors
  • Angiogenesis Modulating Agents / chemistry
  • Angiogenesis Modulating Agents / pharmacology*
  • Animals
  • Cell Adhesion / drug effects
  • Cell Line, Tumor
  • Cell Movement / drug effects
  • Cell Proliferation / drug effects
  • Cells, Cultured
  • Endothelium, Vascular / cytology
  • Ephrin-B2 / metabolism*
  • Growth Inhibitors
  • Humans
  • Mice
  • Neoplasms / blood supply
  • Neoplasms / drug therapy*
  • Neoplasms / pathology
  • Neoplasms, Experimental / drug therapy
  • Neovascularization, Pathologic / drug therapy
  • Peptide Fragments / chemistry
  • Peptide Fragments / pharmacology*
  • Protein Binding / drug effects
  • Receptor, EphB4 / metabolism*
  • Solubility

Substances

  • Angiogenesis Inhibitors
  • Angiogenesis Modulating Agents
  • Ephrin-B2
  • Growth Inhibitors
  • Peptide Fragments
  • Ephb4 protein, mouse
  • Receptor, EphB4