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Extracellular matrix protein fibronectin induces matrix metalloproteinases in human prostate adenocarcinoma cells

Sekhar Pal1, Kirat Kumar Ganguly, Amitava Chatterjee

  • 1Department of Receptor Biology and Tumor Metastasis, Chittaranjan National Cancer Institute , Kolkata , India.

Cell Communication & Adhesion
|September 20, 2013
PubMed

Insights

Prostate cancer cells interacting with fibronectin (FN) increase matrix metalloproteinases (MMPs) via specific signaling pathways. Blocking α5 integrin inhibits this MMP upregulation, suggesting a therapeutic target.

Area of Science:

  • Oncology
  • Cell Biology
  • Biochemistry

Background:

  • Extracellular protease activity, particularly matrix metalloproteinases (MMPs), is elevated in tumor cells.
  • Understanding tumor cell-extracellular matrix (ECM) interactions is crucial for cancer research.

Purpose of the Study:

  • To investigate the effect of human prostate adenocarcinoma PC-3 cell interaction with fibronectin (FN) on MMP expression.
  • To elucidate the signaling pathways involved in FN-induced MMP upregulation.

Main Methods:

  • PC-3 cells were cultured on FN-coated surfaces.
  • α5 integrin blockade, siRNA, and inhibitor studies were employed.
  • Phosphorylation, nuclear translocation, surface expression, and cell migration were analyzed.

Main Results:

  • FN coating upregulated MMP-9 and MMP-1 expression in PC-3 cells.
  • This upregulation was blocked by inhibiting α5 integrin.
  • Signaling pathways involving focal adhesion kinase (FAK), phosphatidyl-inositol-3-kinase (PI-3K), Akt, and nuclear factor-kappaB (NF-κB) were implicated.
  • FN treatment enhanced FAK, PI3K, and Akt phosphorylation, NF-κB nuclear translocation, CD-44 expression, and cell migration.

Conclusions:

  • PC-3 cell binding to FN, potentially via α5β1 integrin, triggers signaling cascades leading to MMP-9 and MMP-1 upregulation.
  • CD-44 may play a role in modulating MMP-9 activity.

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