ABSTRACT
The presence of thymidine phosphorylase in human healthy, adenomatous and cancerous prostate was demonstrated. The enzyme was responsible for the cleavage and synthesis of thymidine and for the transfer of deoxyribose from one deoxyribonucleoside to a pyrimidic base. The enzyme from normal and adenomatous prostate was retained on DEAE-Sephadex gel. In PC-3 cells, two enzymes with thymidine phosphorylase activity were present, one was retained on the gel, the second was excluded from it. Thymidine phosphorylase activity was higher in adenomatous and cancerous tissues that in healthy ones. In all tissues, the reactions of thymidine synthesis and of deoxyribose transfer were more important than that of thymidine cleavage.
Subject(s)
Prostate/enzymology , Prostatic Hyperplasia/enzymology , Prostatic Neoplasms/enzymology , Thymidine Phosphorylase/metabolism , Humans , Male , Thymidine/metabolismABSTRACT
The presence of thymidine phosphorylase was observed in healthy, adenomatous and tumoral prostatic cells. In healthy and adenomatous tissues the enzyme activity was recovered as a single peak after ion exchange chromatography on DEAE-Sephadex gel. On the contrary, two forms of thymidine phosphorylase were found in prostatic cancers, one of them, with high activity appeared consequently as a characteristic feature of prostatic tumoral cells.
Subject(s)
Pentosyltransferases/analysis , Prostatic Hyperplasia/enzymology , Prostatic Neoplasms/enzymology , Thymidine Phosphorylase/analysis , Chromatography, Ion Exchange , Humans , Male , Prostate/enzymology , Thymidine Phosphorylase/isolation & purification , Thymidine Phosphorylase/metabolismABSTRACT
Administration of phytooestrogens to immature female rats leads to a large increase in uterine thymidine kinase activity. That increase concerns to a large extent the fetal isoenzyme of thymidine kinase. These results confirm the estrogenic properties of phytoestrogens and allow to specify their physiological effects.