Insulin-like growth factor binding protein-3 induces angiogenesis through IGF-I- and SphK1-dependent mechanisms

J Thromb Haemost. 2007 Apr;5(4):835-45. doi: 10.1111/j.1538-7836.2007.02431.x. Epub 2007 Feb 9.

Abstract

Angiogenesis is critical for development and repair, and is a prominent feature of many pathological conditions. Based on evidence that insulin-like growth factor binding protein (IGFBP)-3 enhances cell motility and activates sphingosine kinase (SphK) in human endothelial cells, we have investigated whether IGFBP-3 plays a role in promoting angiogenesis. IGFBP-3 potently induced network formation by human endothelial cells on Matrigel. Moreover, it up-regulated proangiogenic genes, such as vascular endothelial growth factor (VEGF) and matrix metalloproteinases (MMP)-2 and -9. IGFBP-3 even induced membrane-type 1 MMP (MT1-MMP), which regulates MMP-2 activation. Decreasing SphK1 expression by small interfering RNA (siRNA), blocked IGFBP-3-induced network formation and inhibited VEGF, MT1-MMP but not IGF-I up-regulation. IGF-I activated SphK, leading to sphingosine-1-phosphate (S1P) formation. The IGF-I effect on SphK activity was blocked by specific inhibitors of IGF-IR, PI3K/Akt and ERK1/2 phosphorylation. The disruption of IGF-I signaling prevented the IGFBP-3 effect on tube formation, SphK activity and VEGF release. Blocking ERK1/2 signaling caused the loss of SphK activation and VEGF and IGF-I up-regulation. Finally, IGFBP-3 dose-dependently stimulated neovessel formation into subcutaneous implants of Matrigel in vivo. Thus, IGFBP-3 positively regulates angiogenesis through involvement of IGF-IR signaling and subsequent SphK/S1P activation.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Capillaries / metabolism
  • Collagen / metabolism
  • Drug Combinations
  • Endothelium, Vascular / cytology*
  • Humans
  • Insulin-Like Growth Factor Binding Protein 3 / metabolism
  • Insulin-Like Growth Factor Binding Protein 3 / physiology*
  • Insulin-Like Growth Factor I / physiology*
  • Laminin / metabolism
  • Mice
  • Mice, Inbred C57BL
  • Neovascularization, Pathologic*
  • Phosphotransferases (Alcohol Group Acceptor) / metabolism
  • Phosphotransferases (Alcohol Group Acceptor) / physiology*
  • Proteoglycans / metabolism
  • Receptor, IGF Type 1 / metabolism
  • Signal Transduction
  • Vascular Endothelial Growth Factor A / metabolism

Substances

  • Drug Combinations
  • Insulin-Like Growth Factor Binding Protein 3
  • Laminin
  • Proteoglycans
  • Vascular Endothelial Growth Factor A
  • matrigel
  • Insulin-Like Growth Factor I
  • Collagen
  • Phosphotransferases (Alcohol Group Acceptor)
  • sphingosine kinase
  • Receptor, IGF Type 1