Both focal adhesion kinase and c-Ras are required for the enhanced matrix metalloproteinase 9 secretion by fibronectin in ovarian cancer cells

Cancer Res. 1998 Mar 1;58(5):900-3.

Abstract

Cell adhesion to the extracellular matrix appears to trigger a cascade of intracellular signalings. We have shown previously that treatment of ovarian cancer cells with peritoneal conditioned medium or purified fibronectin (FN) activated matrix metalloproteinase 9 secretion and, thereby, cancer cell invasion. By use of antisense oligonucleotides to focal adhesion kinase (FAK) and a dominant-negative mutant of ras (S17Nras), we found that both FAK and c-Ras were required for the activation of matrix metalloproteinase 9 secretion by FN. In addition, both antisense oligonucleotides to FAK and S17Nras inhibited mitogen-activated protein kinase activation by FN treatment, suggesting the involvement of mitogen-activated protein kinase in the FN-dependent signaling.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cell Adhesion Molecules / metabolism*
  • Collagenases / metabolism*
  • Female
  • Fibronectins / pharmacology*
  • Focal Adhesion Kinase 1
  • Focal Adhesion Protein-Tyrosine Kinases
  • Genes, ras
  • Humans
  • Matrix Metalloproteinase 9
  • Oligonucleotides, Antisense
  • Ovarian Neoplasms / metabolism*
  • Protein-Tyrosine Kinases / metabolism*
  • Signal Transduction / drug effects*
  • Tumor Cells, Cultured
  • ras Proteins / metabolism*

Substances

  • Cell Adhesion Molecules
  • Fibronectins
  • Oligonucleotides, Antisense
  • Protein-Tyrosine Kinases
  • Focal Adhesion Kinase 1
  • Focal Adhesion Protein-Tyrosine Kinases
  • PTK2 protein, human
  • Collagenases
  • Matrix Metalloproteinase 9
  • ras Proteins