Rapid disappearance of deoxyribose-1-phosphate in platelet derived endothelial cell growth factor/thymidine phosphorylase overexpressing cells

M. De Bruin, K. Smid, A. C. Laan, P. Noordhuis, M. Fukushima, K. Hoekman, H. M. Pinedo, G. J. Peters

Research output: Contribution to journalArticle

Abstract

Platelet derived endothelial cell growth factor/thymidine phosphorylase (PD-ECGF/TP) catalyzes the phosphorolysis of thymidine (TdR) to thymine and deoxyribose-1-phosphate (dR-1-P) and has a pro-angiogenic effect for which dR-1-P may be responsible. Using a purine nucleoside phosphorylase based assay it was found that TdR incubation did not increase dR-1-P accumulation in colon cancer cell line Colo320 and its PD-ECGF/TP transfected variant Colo320TP1. The assay was linear up to 25,000pmol dR-1-P with complete recovery of dR-1-P from cellular extracts. There was a huge discrepancy between thymine production and the measured dR-1-P level, 0.05% of the expected value for dR-1-P was found, indicating that there was a rapid disappearance of dR-1-P. However, in cellular extracts, TdR incubation increased dR-1-P, measurable by trapping, which was inhibited by a thymidine phosphorylase inhibitor. dR-1-P directly added to cellular extracts disappeared within 5-10min. In conclusion, large amounts of dR-1-P are produced by Colo320TP1 cells, which rapidly disappear thus not resulting in a net accumulation of dR-1-P in these cells.

Original languageEnglish (US)
Pages (from-to)675-679
Number of pages5
JournalBiochemical and Biophysical Research Communications
Volume301
Issue number3
DOIs
StatePublished - Feb 14 2003
Externally publishedYes

Keywords

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

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

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