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Department of Cancer Chemotherapy, Institute for Cancer Research [K. M., T. S., N. H., S. A.], Department of Pathology [H. Y.], Faculty of Medicine, Kagoshima University, 8-35-1 Sakuragaoka Kagoshima 890, and Taiho Pharmaceutical Co. Ltd., Saitama 357 [W. K., Y. Y.], Japan
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.
1 To whom requests for reprints should be addressed.
Received 1/12/95. Accepted 2/14/95.
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