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p38 Mitogen-activated protein kinase regulation of JB6 Cl41 cell transformation promoted by epidermal growth factor

Zhiwei He1, Yong-Yeon Cho, Guangming Liu

  • 1Hormel Institute, University of Minnesota, Austin, Minnesota 55912, USA.

The Journal of Biological Chemistry
|May 16, 2003
PubMed

Insights

The p38 MAP kinase pathway is crucial for epidermal growth factor (EGF)-induced cell transformation in JB6 cells. Inhibiting this pathway blocks cell transformation by affecting key transcription factors like ATF-2, STAT1, c-Myc, and AP-1.

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Signal Transduction

Background:

  • The role of p38 MAP kinase pathway in cell transformation is not fully understood.
  • Epidermal growth factor (EGF) is known to induce cell transformation in JB6 cells.

Purpose of the Study:

  • To investigate the role of the p38 MAP kinase pathway in EGF-induced cell transformation in JB6 cells.

Main Methods:

  • Utilized a dominant negative mutant of p38 MAP kinase (DN-p38) and SB202190, a p38 MAP kinase inhibitor.
  • Assessed the effects on EGF-promoted JB6 Cl41 cell transformation.
  • Examined the phosphorylation of ATF-2, STAT1, and c-Myc.
  • Performed gel shift assays to evaluate activator protein-1 (AP-1) DNA binding.

Main Results:

  • DN-p38 MAP kinase and SB202190 significantly inhibited EGF-induced JB6 Cl41 cell transformation.
  • DN-p38 MAP kinase reduced the phosphorylation of EGF-stimulated ATF-2 and STAT1.
  • DN-p38 MAP kinase inhibited EGF-induced phosphorylation of c-Myc.
  • DN-p38 MAP kinase dose-dependently inhibited EGF-induced AP-1 DNA binding.

Conclusions:

  • p38 MAP kinase is a key regulator of EGF-induced cell transformation in JB6 cells.
  • This regulation involves the modulation of p38 MAP kinase phosphorylation and the activation of downstream targets including c-Myc and AP-1.

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