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Phosphorylation status and function of p53 are inversely related to protein kinase C activation

  1. Author:
    Nakamura, K.
    Sun, Y.
    Yokoyama, Y.
    Ferris, D.
    Singh, N.
    Ichikawa, T.
    Shinozuka, K.
    Kunitomo, M.
    Colburn, N.

  2. Author Address

    Nakamura K NCI, Frederick Canc Res & Dev Ctr, Gene Regulat Sect, Lab Biochem Physiol Ft Detrick, MD 21702 USA NCI, Frederick Canc Res & Dev Ctr, Gene Regulat Sect, Lab Biochem Physiol Ft Detrick, MD 21702 USA NCI, Frederick Canc Res & Dev Ctr, SAIC Ft Detrick, MD 21702 USA Warner Lambert Co, Parke Davis Pharmaceut Res Div, Dept Mol Biol Ann Arbor, MI 48105 USA Mukogawa Womens Univ, Interdisciplinary Res Inst Biosci Nishinomiya Hyogo 6638558 Japan Mukogawa Womens Univ, Fac Pharmaceut Sci, Dept Pharmacol Nishinomiya Hyogo 6638179 Japan
    1. Year: 2000
  2. Journal: Anticancer Research
    1. 20
    2. 1A
    3. Pages: 1-5
  4. Type of Article: Article
  1. Abstract:

    The role of phosphorylation in the regulation of p53 protein function is little understood We have addressed the role of protein kinase C (PKC) in the phosphorylation. Exposure to the protein kinase inhibitor, 1-(5-isoquinolinesulfonyl) -2-methylpiperazine dihydrochloride (H7) increased the phosphorylation of wild type p53 protein, whereas exposure to the tumor promoter phorbol ester, 12-O-retradecanoyl-phorbol-13-acetate (TPA), decreased it in vivo following 3 hours incubation with mouse epidermal JB6 cells. Exposure to the c-AMP dependent protein kinase (PKA) activator, forskolin, did not decrease the phosphorylation of p53 protein. In the transient transfection/luciferase reporter transactivation assay,H7 modestly increased the mouse double minute (MDM) 2 reporter transactivation activity of p53 protein after 24 hours treatment, and TPA completely blocked it. These results suggest that the accelerated phosphorylation of wild type p53 protein is inversely related to PKC activation, and that p53 phosphorylation may have some relation to transcription factor function. [References: 30]

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