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
Thymidine kinase activity of the ventral prostate from adult rats could be stimulated by administration to the animal of casomorphin or casomorphin (morphiceptin). On the other hand addition of both drugs to the culture medium of prostatic cells from immature rats enhanced the cells growth. In both cases, morphiceptin was more efficient than casomorphin. These results suggest than casomorphins have other properties than their morphinomimetic effects previously described.
Subject(s)
Cell Division/drug effects , Endorphins/pharmacology , Milk Proteins/pharmacology , Prostate/cytology , Animals , Male , Prostate/enzymology , Rats , Thymidine Kinase/metabolismABSTRACT
Inhibitory effects of Celiptium on the thymidine kinase synthesis induced by oestradiol-17 beta in the rat uterus. In the rat uterus, the synthesis of thymidine kinase specifically induced by oestradiol-17 beta was inhibited by Celiptium. The synthesis was totally inhibited when the drug was administered before the oestrogen and partially when it was administered after. These facts suggested that Celiptium was competitive to the acceptor sites for oestradiol-receptors and inhibited the expression of the thymidine kinase gene.