Vascular endothelial growth factor receptor-2-induced initial endothelial cell migration depends on the presence of the urokinase receptor

Circ Res. 2004 Jun 25;94(12):1562-70. doi: 10.1161/01.RES.0000131498.36194.6b. Epub 2004 May 6.

Abstract

The angiogenic response of endothelial cells initiated by different growth factors is accompanied by assembly of cell surface-bound proteolytic machinery as a prerequisite for focal invasion. We have shown previously how the vascular endothelial growth factor (VEGF) initiates proteolysis by activation of pro-urokinase (pro-PA) via the VEGF receptor-2 (VEGFR-2). We now show that the cell surface receptor of the uPA-system, the urokinase receptor (uPAR), is redistributed to focal adhesions at the leading edge of endothelial cells in response to VEGF. VEGF165 and VEGF-E, both interacting with VEGFR-2, but not PlGF exclusively stimulating VEGFR-1, induce within minutes internalization of uPAR via an LDL receptor-like molecule, dependent on generation of active uPA and the presence of plasminogen activator inhibitor-1 (PAI-1). uPAR seems to play a pivotal role in VEGFR-2-induced endothelial cell migration because cleavage of surface uPAR impaired the migratory response of endothelial cells toward VEGF-E, but not toward PlGF.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Cell Movement / drug effects
  • Cells, Cultured / drug effects
  • Endothelial Cells / cytology*
  • Endothelial Cells / drug effects
  • Endothelial Cells / metabolism
  • Endothelium, Vascular / cytology*
  • Endothelium, Vascular / drug effects
  • Enzyme Inhibitors / pharmacology
  • Female
  • Focal Adhesions / metabolism
  • Humans
  • Integrins / physiology
  • Matrix Metalloproteinase 2 / physiology
  • Matrix Metalloproteinases, Membrane-Associated
  • Membrane Proteins
  • Metalloendopeptidases / physiology
  • Mice
  • Mice, Inbred C57BL
  • Mice, Knockout
  • Neovascularization, Physiologic / drug effects
  • Neovascularization, Physiologic / physiology*
  • Oligodeoxyribonucleotides, Antisense / pharmacology
  • Phosphatidylinositol Diacylglycerol-Lyase
  • Plasminogen Activator Inhibitor 1 / deficiency
  • Plasminogen Activator Inhibitor 1 / genetics
  • Proteins / pharmacology
  • Receptors, Cell Surface / deficiency
  • Receptors, Cell Surface / genetics
  • Receptors, Cell Surface / physiology*
  • Receptors, Urokinase Plasminogen Activator
  • Recombinant Proteins / pharmacology
  • Vascular Endothelial Growth Factor A / pharmacology
  • Vascular Endothelial Growth Factor Receptor-2 / physiology*
  • Viral Proteins / pharmacology

Substances

  • Enzyme Inhibitors
  • Integrins
  • Membrane Proteins
  • Oligodeoxyribonucleotides, Antisense
  • PLAUR protein, human
  • Pigf protein, mouse
  • Plasminogen Activator Inhibitor 1
  • Plaur protein, mouse
  • Proteins
  • Receptors, Cell Surface
  • Receptors, Urokinase Plasminogen Activator
  • Recombinant Proteins
  • VEGF-like protein, Orf virus
  • VEGFA protein, human
  • Vascular Endothelial Growth Factor A
  • Viral Proteins
  • vascular endothelial growth factor A, mouse
  • Vascular Endothelial Growth Factor Receptor-2
  • Matrix Metalloproteinases, Membrane-Associated
  • Metalloendopeptidases
  • Matrix Metalloproteinase 2
  • Phosphatidylinositol Diacylglycerol-Lyase