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Insulin-Like Growth Factor 1 Receptor Regulates Breast Cancer Cell Adhesion through Beta-1 Integrin.

Christopher A Galifi1, Elvan Dogan1, Luis Fernandez Almansa1

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Both insulin-like growth factor 1 (IGF-1) stimulation and knockdown of its receptor (IGF1R) increase triple-negative breast cancer (TNBC) cell adhesion. This suggests surface-bound IGF1R inhibits cell adhesion, offering insights into TNBC metastasis.

Keywords:
IGF-1IGF1Radhesionbreast cancerfibronectin. (Min.5-Max. 8)β1 integrin

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Area of Science:

  • Oncology
  • Molecular Biology
  • Cell Biology

Background:

  • The insulin-like growth factor (IGF-1/IGF1R) pathway is linked to breast cancer aggressiveness.
  • Previous attempts to inhibit this pathway in clinical trials have failed, highlighting gaps in understanding its role in triple-negative breast cancer (TNBC) metastasis.
  • Recent research suggests IGF1R influences integrin function and cancer cell adhesion dynamics.

Purpose of the Study:

  • To investigate the hypothesis that IGF1R directly regulates cancer cell adhesion.
  • To elucidate the mechanism by which IGF1R affects cell adhesion in TNBC.
  • To explore the role of IGF1R in TNBC cell adhesion to endothelial cells.

Main Methods:

  • Utilized MDA-MB-231 and Hs578T TNBC cell lines.
  • Employed siRNA-mediated knockdown of IGF1R and integrins.
  • Conducted adhesion assays, including xCELLigence E-plates, to quantify cell adhesion under various conditions (IGF-1 stimulation, IGF1R knockdown).
  • Assessed adhesion to human umbilical vein endothelial cells (HUVECs).

Main Results:

  • IGF-1 stimulation enhanced MDA-MB-231 TNBC cell adhesion, an effect reversed by an IGF1R inhibitor and a receptor internalization inhibitor.
  • Unexpectedly, IGF1R knockdown also significantly increased cell adhesion.
  • Concomitant knockdown of β1 integrin reversed the increased adhesion observed with both IGF-1 stimulation and IGF1R knockdown, indicating β1 integrin dependence.
  • Inhibition of IGF1R signaling reduced TNBC cell adhesion to HUVECs.

Conclusions:

  • Both IGF-1 stimulation and IGF1R knockdown paradoxically promote TNBC cell adhesion.
  • A proposed model suggests that surface-bound IGF1R inhibits β1 integrin function, thereby blocking cell adhesion.
  • Ligand-mediated IGF1R internalization is crucial for its effect on adhesion.
  • These findings may explain the lack of success with selective IGF1R antagonists in clinical trials.