[
Abstract]
[
Full Text PDF] （in Japanese / 3438KB）
[Members Only And Two Factor Auth.] J.Jpn. Surg. Soc.. 94(9): 993-999, 1993
Original article
THYMIDINE KINASE AND THYMIDYLATE SYNTHELASE ACTIVITIES IN HUMAN GASTRIC CANCER
Thyrnidine kinase (TK) and thyrnidylate synthetase (TS) are known to catalyse the phosphorylation of thyrnidine for the salvage synthesis of dTMP and the rnethylation of dUMP for the de novo synthesis of dTMP, respectively. High TK and TS activities and the existence of TK isozyrnes have been observed in rapidly proliferting tissues. In this work I measured TK, TK-isozyrne and TS activities, and DNA and RNA in human gastric cancer tissue. Tissue containing gastric cancer, (well differentiated adenocarcinorna (well: n=29), poorly differentiated adenocarcinoma (por: n=28)), and noninvolved paired normal gastric mucosa were obtained from fresh surgical specimens. Total TK and peak A TK activity of gastric cancer increased to 184% and 299% of activity of normal gastric mucosa.TK activity of “well” was higher than that of “por”. On the other hand TS activity of gastric cancer increased to 122% of activity of normal gastric mucosa. TS activity of “por” was higher than that of “well”. DNA and RNA content of gastric cancer increased to 294% and 228% than that of normal gastric mucosa.But difference wasn't observed between “well” and “por”. These characteristics of gastric cancer suggest its susceptibility to control by inhibition of TK and TS.
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