Role of platelet derived endothelial cell growth factor/thymidine phosphorylase in fluoropyrimidine sensitivity and potential role of deoxyribose-1-phosphate

M. De Bruin, T. Van Capel, K. Smid, K. Van Der Born, M. Fukushima, K. Hoekman, H. M. Pinedo, G. J. Peters

Research output: Contribution to journalArticlepeer-review

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 languageEnglish (US)
Pages (from-to)1485-1490
Number of pages6
JournalNucleosides, Nucleotides and Nucleic Acids
Volume23
Issue number8-9
DOIs
StatePublished - 2004
Externally publishedYes

Keywords

  • Deoxyribose-1-phosphate
  • Fluoropyrimidines
  • Platelet derived endothelial cell growth factor
  • Thymidine phosphorylase

ASJC Scopus subject areas

  • Genetics
  • Biochemistry

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