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Tumor necrosis factor-induced activation and increased tyrosine phosphorylation of mitogen-activated protein (MAP)

I Vietor1, P Schwenger, W Li

  • 1Department of Microbiology, New York University Medical Center, New York 10016.

The Journal of Biological Chemistry
|September 5, 1993
PubMed

Insights

Tumor necrosis factor (TNF) rapidly activates mitogen-activated protein kinase (MAPK) in human cells. This signaling pathway is crucial for mediating TNF

Area of Science:

  • Cellular and Molecular Biology
  • Immunology
  • Signal Transduction

Background:

  • Tumor necrosis factor (TNF) is a cytokine influencing cell growth and differentiation.
  • TNF triggers increased serine/threonine phosphorylation of cellular proteins.
  • Kinases responsible for TNF-induced phosphorylation remain largely unidentified.

Purpose of the Study:

  • To investigate the role of mitogen-activated protein kinase (MAPK) in TNF signaling.
  • To identify kinases activated by TNF in human diploid FS-4 cells.

Main Methods:

  • Assessed MAPK activity by myelin basic protein phosphorylation and electrophoretic mobility shifts.
  • Measured tyrosine phosphorylation of MAPK using 32P labeling and immunoprecipitation.
  • Utilized immunoblotting with phosphotyrosine antibodies to detect protein phosphorylation.

Main Results:

  • TNF treatment induced rapid, transient MAPK activation in FS-4 cells.
  • MAPK activation correlated with increased tyrosine phosphorylation of pp42 and pp44 MAPK.
  • No other proteins showed significant increases in tyrosine phosphorylation after TNF treatment.

Conclusions:

  • MAPK activation is a key early event in TNF-induced signaling.
  • The pp42 and pp44 MAPK isoforms are specifically activated by TNF.
  • MAPK activation is likely integral to TNF receptor-mediated cellular responses.

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