Cloning and Expression of Human Uridine Phosphorylase

Shin Ichi Watanabe, Takafumi Uchida

    Research output: Contribution to journalArticlepeer-review

    40 Citations (Scopus)


    Using a mouse cDNA probe we have identified a human uridine phosphorylase cDNA clone from the cDNA library of a human colorectal tumor cell line, HCT116. The recombinant human uridine phosphorylase expressed in COS-7 cells demonstrated specific enzyme activity with uridine as the substrate; this activity was inhibited by the competitive inhibitor 2,2′-anhydro-5-ethyluridine. Northern blot analysis with the cDNA as a probe demonstrated high levels of mRNA expression in several tumor cell lines but very low level in normal cell, WI-38. The expression of uridine phosphorylase mRNA in HCT-116 cells was further enhanced by treating the cells with vitamin D3 and the inflammatory cytokines: tumor necrosis factor α, interleukin 1α and interferon γ.

    Original languageEnglish
    Pages (from-to)265-272
    Number of pages8
    JournalBiochemical and biophysical research communications
    Issue number1
    Publication statusPublished - 1995

    ASJC Scopus subject areas

    • Biophysics
    • Biochemistry
    • Molecular Biology
    • Cell Biology


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