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 journalArticle

    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

    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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