Inhibition of stimulus-dependent epidermal growth factor receptor and transforming growth factor-α mRNA accumulation by the protein kinase C inhibitor staurosporine

Jeffrey D. Bjorge, Jeffrey E. Kudlow, Gordon B. Mills, Andrew J. Paterson

Research output: Contribution to journalArticlepeer-review

11 Scopus citations

Abstract

The ability of staurosporine, a potent inhibitor of protein kinase C, to block certain cellular events initiated by 12-O-tetradecanoylphorbol-13-acetate (TPA) and epidermal growth factor (EGF) was examined. Treatment of MDA468 breast cancer cells with TPA decreases EGF binding to the cell surface and this effect is blocked by pretreatment with staurosporine with an IC50 of 30 nM. Either 10-9 M EGF or 100 ng/ml TPA stimulated the accumulation of both EGF receptor and TGF-α mRNA and staurosporine (50 nM) completely abolished these mRNA accumulations. Staurosporine did not block EGF-stimulated tyrosine phosphorylation of its receptor as measured by immunoblotting with anti-phos-photyrosine antibodies. The ability of staurosporine to block the mRNA responses of either EGF or TPA suggests that these two agents have common signaling pathways and it implies a role for protein kinase C in the control of EGF receptor and TGF-α expression.

Original languageEnglish (US)
Pages (from-to)404-408
Number of pages5
JournalFEBS Letters
Volume243
Issue number2
DOIs
StatePublished - Jan 30 1989
Externally publishedYes

Keywords

  • Growth factor receptor
  • Phorbol ester
  • Protein kinase C
  • Tumor promotor

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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