RT Journal Article
SR Electronic
T1 Role of Thymidine Phosphorylase Activity in the Angiogenic Effect of Platelet-derived Endothelial Cell Growth Factor/Thymidine Phosphorylase
JF Cancer Research
JO Cancer Res
FD American Association for Cancer Research
SP 1687
OP 1690
VO 55
IS 8
A1 Miyadera, Kazutaka
A1 Sumizawa, Tomoyuki
A1 Haraguchi, Misako
A1 Yoshida, Hiroki
A1 Konstanty, Wierzba
A1 Yamada, Yuji
A1 Akiyama, Shin-ichi
YR 1995
UL http://cancerres.aacrjournals.org/content/55/8/1687.abstract
AB Human thymidine phosphorylase (dThdPase) has been reported to be identical with the platelet-derived endothelial cell growth factor (PD-ECGF). To investigate whether the dThdPase activity of PD-ECGF/dThdPase is indispensable to its angiogenic activity, three PD-ECGF/dThdPase mutants, K115E (Lys-115 → Glu), L148R (Leu-148 → Arg) and R202S (Arg-202 → Ser) were made by site-directed mutagenesis. Although the expression level of the three mutant PD-ECGF/dThdPases in the COS-7 cells was similar to that of wild-type PD-ECGF/dThdPase, dThdPase activity was not detected in the COS-7 cells transfected with the mutant PD-ECGF/dThdPase cDNA. The lysates of COS-7 cells transfected with the wild-type PD-ECGF/dThdPase cDNA had angiogenic activity, but those transfected with the mutant PD-ECGF/dThdPase cDNAs did not. An inhibitor of dThdPase, 6-amino-5-chlorouracil, inhibited the angiogenic activity of purified dThdPase. These findings indicate that dThdPase activity is indispensable to the angiogenic activity of PD-ECGF/dThdPase. ©1995 American Association for Cancer Research.