1. Academic Validation
  2. Cloning and expression of human uridine phosphorylase

Cloning and expression of human uridine phosphorylase

  • Biochem Biophys Res Commun. 1995 Nov 2;216(1):265-72. doi: 10.1006/bbrc.1995.2619.
S Watanabe 1 T Uchida
Affiliations

Affiliation

  • 1 Department of Oncology, Nippon Roche Research Center, Kamakura, Japan.
Abstract

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 alpha, interleukin 1 alpha and interferon gamma.

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