Platelet-derived endothelial cell growth factor has thymidine phosphorylase activity

Biochem Biophys Res Commun. 1992 May 15;184(3):1311-6. doi: 10.1016/s0006-291x(05)80025-7.


Platelet-derived endothelial cell growth factor (PD-ECGF), a protein which stimulates angiogenesis in vivo, is shown to have a 39.2% amino acid sequence similarity over a 439 amino acid region with the thymidine phosphorylase of Escherichia coli (E. coli). Using recombinant human PD-ECGF, we show that PD-ECGF has thymidine phosphorylase activity. Analysis by gel chromatography revealed that recombinant human PD-ECGF occurs as a 90 kDa homodimer, similar to other thymidine phosphorylases. In addition to a possible effect on DNA synthesis, PD-ECGF was shown to affect [3H]thymidine assays in a manner which is not related to cell proliferation. The in vitro and in vivo effects of PD-ECGF may thus occur by an indirect mechanism through its enzymatic activity.

Publication types

  • Comparative Study

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Cells, Cultured
  • Chromatography, Gel
  • Endothelium, Vascular / metabolism
  • Escherichia coli / enzymology
  • Genes, Bacterial
  • Humans
  • Kinetics
  • Molecular Sequence Data
  • Recombinant Proteins / isolation & purification
  • Recombinant Proteins / metabolism
  • Sequence Homology, Nucleic Acid
  • Swine
  • Thymidine / metabolism
  • Thymidine Phosphorylase / genetics*
  • Thymidine Phosphorylase / isolation & purification
  • Thymidine Phosphorylase / metabolism*


  • Recombinant Proteins
  • Thymidine Phosphorylase
  • Thymidine