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Peroxisome proliferator-activated receptor beta (delta)-dependent regulation of ubiquitin C expression contributes to attenuation of skin carcinogenesis

  1. Author:
    Kim, D. J.
    Akiyama, T. E.
    Harman, F. S.
    Burns, A. M.
    Shan, W. W.
    Ward, J. M.
    Kennett, M. J.
    Gonzalez, F. J.
    Peters, J. M.

  2. Author Address

    Peters, JM, Penn State Univ, Dept Vet Sci, Fenske Lab 226, University Pk, PA 16802 USA Penn State Univ, Dept Vet Sci, Fenske Lab 226, University Pk, PA 16802 USA. Penn State Univ, Ctr Mol Toxicol & Carcinogenesis, University Pk, PA 16802 USA. Penn State Univ, Grad Program Biochem Microbiol Mol Biol, University Pk, PA 16802 USA. Penn State Univ, Grad Program Genet, University Pk, PA 16802 USA. Penn State Univ, Grad Program Mol Toxicol, Huck Inst Life Sci, University Pk, PA 16802 USA. NCI, Lab Metab, NIH, Bethesda, MD 20892 USA. NCI, Vet & Tumor Pathol Sect, Ctr Canc Res, Frederick, MD 21702 USA.
    1. Year: 2004
  2. Journal: Journal of Biological Chemistry
    1. 279
    2. 22
    3. Pages: 23719-23727
  4. Type of Article: Article
  1. Abstract:

    The role of peroxisome proliferator-activated receptor-beta( PPARbeta) in the molecular regulation of skin carcinogenesis was examined. Increased caspase-3 activity associated with apoptosis was found in the skin of wildtype mice after tumor promotion with 12-O-tetradecanoylphorbol-13- acetate, and this effect was diminished in PPARbeta-null mice. The onset of tumor formation, tumor size, and tumor multiplicity induced from a two-stage carcinogen bioassay ( 7,12-dimethylbenz[a] anthracene/ 12-O-tetradecanoylphorbol-13- acetate) were significantly enhanced in PPARbeta-null mice compared with wild-type mice. To begin to characterize the molecular changes underlying this PPARbeta-dependent phenotype, microarray analysis was performed and a number of differentially regulated gene products were identified including ubiquitin C. Subsequent promoter analysis, reporter gene assays, site-directed mutagenesis, and electrophoretic mobility shift assays provide evidence that PPARbeta regulates ubiquitin C expression, and that ubiquitination of proteins is influenced by PPARbeta. These results strongly suggest that activation of PPARbeta-dependent target genes provides a novel strategy to inhibit tumor promotion and carcinogenesis

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