A signaling pathway leading to metastasis is controlled by N-cadherin and the FGF receptor

Cancer Cell. 2002 Oct;2(4):301-14. doi: 10.1016/s1535-6108(02)00150-2.

Abstract

The intracellular signaling events causing tumor cells to become metastatic are not well understood. N-cadherin and FGF-2 synergistically increase migration, invasion, and secretion of extracellular proteases in breast tumor cells. Here, we define a metastatic signaling cascade activated by N-cadherin and FGF-2. In the presence of N-cadherin, FGF-2 caused sustained activation of the MAPK-ERK pathway, leading to MMP-9 gene transcription and cellular invasion. N-cadherin prevented the FGF receptor (FGFR) from undergoing ligand-induced internalization, resulting in increased FGFR-1 stability. Association of FGFR-1 with N-cadherin was mediated by the first two Ig-like domains of FGFR-1. These results suggest that protection of the FGFR-1 from ligand-induced downregulation by N-cadherin enhances receptor signaling and provides a mechanism by which tumor cells can acquire metastatic properties.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Animals
  • Cadherins / physiology*
  • Female
  • Fibroblast Growth Factor 2 / physiology*
  • Gene Expression Regulation, Enzymologic
  • Humans
  • MAP Kinase Signaling System / physiology*
  • Matrix Metalloproteinase 9 / genetics*
  • Mitogen-Activated Protein Kinase Kinases / metabolism
  • Neoplasm Metastasis
  • Receptor Protein-Tyrosine Kinases / metabolism*
  • Receptor, Fibroblast Growth Factor, Type 1
  • Receptors, Fibroblast Growth Factor / metabolism*
  • Transfection
  • Tumor Cells, Cultured

Substances

  • Cadherins
  • Receptors, Fibroblast Growth Factor
  • Fibroblast Growth Factor 2
  • FGFR1 protein, human
  • Receptor Protein-Tyrosine Kinases
  • Receptor, Fibroblast Growth Factor, Type 1
  • Mitogen-Activated Protein Kinase Kinases
  • Matrix Metalloproteinase 9