Antiangiogenic effect by SU5416 is partly attributable to inhibition of Flt-1 receptor signaling

Mol Cancer Ther. 2002 Mar;1(5):295-302.

Abstract

Interaction between vascular endothelial growth factor (VEGF) and its cognate receptors, KDR/Flk-1 and Flt-1, of vascular endothelial cells is expected to induce an angiogenesis "switch" in tumors and other angiogenesis-associated diseases. SU5416, a selective inhibitor of the KDR/Flk-1 tyrosine kinase, is known to be a potent inhibitor of tumor angiogenesis. In this study, we first observed that SU5416 inhibited Flt-1 tyrosine kinase activity at similar doses, in addition to inhibiting KDR/Flk-1 tyrosine kinase activity in response to VEGF. SU5416 inhibited cell migration of human vascular endothelial cells expressing both Flt-1 and KDR in response to VEGF and also inhibited the cell migration in response to placenta growth factor (PIGF), a specific ligand for Flt-1. Chemotaxis of monocytes expressing only Flt-1 was also inhibited by SU5416 in a dose-dependent manner. Moreover, SU5416 was found to inhibit tyrosine kinase of Flt-1 in response to PIGF in vitro. And angiogenesis induced by PIGF in a Matrigel plug assay was inhibited by administration of SU5416. The antiangiogenic effects by this VEGF receptor-targeting compound appeared to be mediated through interference not only with KDR/Flk-1 but also with Flt-1. Cell migration of vascular endothelial cells and monocytic cells through Flt-1, thus, might play a key role in VEGF-induced tumor angiogenesis in concert with KDR/Flk-1.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • 3T3 Cells
  • Angiogenesis Inhibitors / pharmacology*
  • Animals
  • Cell Movement / drug effects
  • Cells, Cultured
  • Chemotaxis
  • Collagen / pharmacology
  • DNA, Complementary / metabolism
  • Dose-Response Relationship, Drug
  • Drug Combinations
  • Endothelium, Vascular / cytology
  • Extracellular Matrix Proteins / metabolism*
  • Humans
  • Immunoblotting
  • Indoles / pharmacology*
  • Laminin / pharmacology
  • Male
  • Mice
  • Monocytes / metabolism
  • Myosin Heavy Chains
  • Neovascularization, Pathologic
  • Nonmuscle Myosin Type IIB
  • Phosphorylation
  • Placenta Growth Factor
  • Pregnancy Proteins / metabolism
  • Protein-Tyrosine Kinases / antagonists & inhibitors
  • Protein-Tyrosine Kinases / metabolism
  • Proteoglycans / pharmacology
  • Pyrroles / pharmacology*
  • Transfection
  • Vascular Endothelial Growth Factor Receptor-1
  • Vascular Endothelial Growth Factor Receptor-2 / metabolism

Substances

  • Angiogenesis Inhibitors
  • DNA, Complementary
  • Drug Combinations
  • Extracellular Matrix Proteins
  • Indoles
  • Laminin
  • PGF protein, human
  • Pgf protein, mouse
  • Pregnancy Proteins
  • Proteoglycans
  • Pyrroles
  • matrigel
  • Placenta Growth Factor
  • Semaxinib
  • Collagen
  • FLT1 protein, human
  • Flt1 protein, mouse
  • Protein-Tyrosine Kinases
  • Vascular Endothelial Growth Factor Receptor-1
  • Vascular Endothelial Growth Factor Receptor-2
  • Nonmuscle Myosin Type IIB
  • nonmuscle myosin type IIB heavy chain
  • Myosin Heavy Chains