FAK is involved in invasion and metastasis of hepatocellular carcinoma

Clin Exp Metastasis. 2010 Feb;27(2):71-82. doi: 10.1007/s10585-010-9306-3. Epub 2010 Feb 24.

Abstract

Studies have shown that focal adhesion kinase (FAK) is overexpressed in several human tumors and plays an important role in tumor progression. However, the role and underlying mechanisms of FAK in hepatocellular carcinoma (HCC) progression remains to be elucidated. In this study, we examined FAK and phosphorylated FAK Tyr397 expression in a large series of HCCs. We found that both FAK and phosphorylated FAK Tyr397 were overexpressed in HCC samples and HCC cell lines. Increased FAK and phosphorylated FAK Tyr397 expressions were correlated with tumor stage, vascular invasion and intrahepatic metastasis in HCC. Furthermore, HCC cell adhesion, migration and invasion were substantially impaired by siRNA-mediated knockdown of FAK expression, whereas cell growth, apoptosis and cell cycle distribution were not affected. In addition, depletion of FAK induced a significant reduction in expressions and activities of both MMP-2 and MMP-9. Taken together, FAK contributes to invasion and metastasis of HCC partly through regulating expressions and activations of both MMP-2 and MMP-9, suggesting FAK could be a promising therapeutic target for HCC.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Base Sequence
  • Blotting, Western
  • Carcinoma, Hepatocellular / enzymology
  • Carcinoma, Hepatocellular / pathology*
  • Cell Adhesion
  • Cell Line, Tumor
  • DNA Primers
  • Down-Regulation
  • Flow Cytometry
  • Focal Adhesion Protein-Tyrosine Kinases / metabolism
  • Focal Adhesion Protein-Tyrosine Kinases / physiology*
  • Humans
  • Immunohistochemistry
  • Liver Neoplasms / enzymology
  • Liver Neoplasms / pathology*
  • Matrix Metalloproteinase 2 / metabolism
  • Matrix Metalloproteinase 9 / metabolism
  • Middle Aged
  • Neoplasm Metastasis*
  • Phosphorylation
  • Reverse Transcriptase Polymerase Chain Reaction
  • Up-Regulation

Substances

  • DNA Primers
  • Focal Adhesion Protein-Tyrosine Kinases
  • Matrix Metalloproteinase 2
  • Matrix Metalloproteinase 9