Send to

Choose Destination
Biochem Biophys Res Commun. 1995 Nov 2;216(1):265-72.

Cloning and expression of human uridine phosphorylase.

Author information

Department of Oncology, Nippon Roche Research Center, Kamakura, Japan.


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.

[Indexed for MEDLINE]

Supplemental Content

Full text links

Icon for Elsevier Science
Loading ...
Support Center