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Monitoring eIF4F Assembly by Measuring eIF4E-eIF4G Interaction in Live Cells
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The role of MNK proteins and eIF4E phosphorylation in breast cancer cell proliferation and survival

Matthew J Wheater1, Peter Wm Johnson, Jeremy P Blaydes

  • 1Southampton Cancer Research UK Centre, University of Southampton School of Medicine, MP824 Southampton General Hospital, UK.

Cancer Biology & Therapy
|August 6, 2010
PubMed

Insights

This study shows that inhibiting MNK kinase activity can reduce breast cancer cell proliferation. High levels of phosphorylated eukaryotic initiation factor 4E (eIF4E) may predict which breast cancers respond to this treatment.

Area of Science:

  • Oncology
  • Molecular Biology
  • Biochemistry

Background:

  • Eukaryotic initiation factor 4E (eIF4E) is over-expressed in many cancers, including breast cancer, and acts as an oncogene.
  • Mitogen-activated protein kinase kinases (MNKs) phosphorylate eIF4E, a modification crucial for eIF4E-dependent cell transformation.
  • Understanding the role of MNKs in breast cancer proliferation and survival is critical for therapeutic development.

Purpose of the Study:

  • To investigate the role of MNKs in the proliferation and survival of breast cancer cells.
  • To determine if MNK inhibition affects breast cancer cell growth.
  • To explore the potential of phosphorylated eIF4E as a biomarker for therapeutic response.

Main Methods:

  • Analysis of phosphorylated eIF4E levels in breast tumour samples and cell lines.
  • Treatment of breast cancer cell lines with a MNK inhibitor.
  • Assessment of cell proliferation and survival using colony formation and short-term assays.
  • Evaluation of cyclin D1 synthesis inhibition.

Main Results:

  • Phosphorylated eIF4E was detected in most breast cancer cell lines, but not all tumour samples.
  • Five out of six breast cancer cell lines with high phosphorylated eIF4E levels were sensitive to a MNK inhibitor.
  • MCF-7 cells, with low phosphorylated eIF4E, were insensitive to the MNK inhibitor.
  • MNK inhibition primarily caused cytostatic effects, potentially by inhibiting cyclin D1 synthesis.

Conclusions:

  • Breast cancer cell sensitivity to MNK inhibition correlates with baseline eIF4E phosphorylation levels.
  • A subset of breast cancers may respond to MNK kinase inhibitors.
  • Phosphorylated eIF4E can serve as a predictive biomarker for identifying responsive breast cancers.

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