Cloning and expression of human uridine phosphorylase.

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.

• Authors: S Watanabe, T Uchida
• Journal: Biochemical and biophysical research communications (Biochem Biophys Res Commun) Vol. 216 Issue 1 Pg. 265-72 (Nov 02 1995) ISSN: 0006-291X [Print] United States
• PMID: 7488099 (Publication Type: Comparative Study, Journal Article)

Chemical References

• Cytokines
• DNA Probes
• DNA, Complementary
• Interleukin-1
• RNA, Messenger
• Recombinant Proteins
• Tumor Necrosis Factor-alpha
• Interferon-gamma
• Uridine Phosphorylase
• Calcitriol

Topics

• Amino Acid Sequence
• Animals
• Base Sequence
• Calcitriol (pharmacology)
• Cell Line
• Chlorocebus aethiops
• Cloning, Molecular
• Colorectal Neoplasms
• Cytokines (pharmacology)
• DNA Probes
• DNA, Complementary
• Gene Expression (drug effects)
• Humans
• Interferon-gamma (pharmacology)
• Interleukin-1 (pharmacology)
• Kinetics
• Mice
• Molecular Sequence Data
• RNA, Messenger (biosynthesis)
• Recombinant Proteins (biosynthesis, chemistry, metabolism)
• Reference Values
• Sequence Homology, Amino Acid
• Tumor Cells, Cultured
• Tumor Necrosis Factor-alpha (pharmacology)
• Uridine Phosphorylase (biosynthesis, chemistry, metabolism)