Abstract
Thymidine phosphorylase (TP) catalyzes the phosphorolytic cleavage of thymidine (TdR) to thymine and deoxyribose-1-phosphate (dR-1-P). TP, which is overexpressed in a wide variety of solid tumors, is involved in the activation and inactivation of fluoropyrimidines. We investigated the role of TP in 5′-deoxy-5-fluorouridine (5′DFUR), 5-fluorouracil (5FU) and trifluorothymidine (TFT) sensitivity. TP had no effect on TFT while it activated 5′DFUR and to a lesser extent 5FU. In order to provide an explanation for this difference in activation of 5′DFUR and 5FU, we studied the role of the 5FU co-substrate, dR-1-P, needed for its activation.
Original language | English (US) |
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Pages (from-to) | 1485-1490 |
Number of pages | 6 |
Journal | Nucleosides, Nucleotides and Nucleic Acids |
Volume | 23 |
Issue number | 8-9 |
DOIs | |
State | Published - 2004 |
Externally published | Yes |
Keywords
- Deoxyribose-1-phosphate
- Fluoropyrimidines
- Platelet derived endothelial cell growth factor
- Thymidine phosphorylase
ASJC Scopus subject areas
- Genetics
- Biochemistry