Platelet-derived endothelial cell growth factor has thymidine phosphorylase activity.
Article Details
- CitationCopy to clipboard
Usuki K, Saras J, Waltenberger J, Miyazono K, Pierce G, Thomason A, Heldin CH
Platelet-derived endothelial cell growth factor has thymidine phosphorylase activity.
Biochem Biophys Res Commun. 1992 May 15;184(3):1311-6.
- PubMed ID
- 1590793 [ View in PubMed]
- Abstract
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.