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  • Title: Role, control and expression of estrone sulfatase and 17 beta-hydroxysteroid dehydrogenase activities in human breast cancer.
    Author: Pasqualini JR.
    Journal: Zentralbl Gynakol; 1997; 119 Suppl 2():48-53. PubMed ID: 9361395.
    Abstract:
    Breast cancer tissue contains the enzymes necessary for local synthesis of estradiol (E2) and it was demonstrated that, despite the presence of the sulfatase and its messenger in hormone-dependent and hormone-independent breast cancer cells, this enzyme operates particularly in hormone-dependent cells. Different progestins: Nomegestrol acetate, Promegestone, Tibolone (Org OD14) and its metabolites (Org-OM38, Org 4098 and Org 30126), as well as Danazol, can block the conversion of estrone sulfate to E2 very strongly in hormone-dependent breast cancer cells. The last step in the formation of E2 is the conversion of estrone (E1) to estrogen by the action of 17 beta-hydroxysteroid dehydrogenase. This activity is preferentially in the reductive direction (formation of E2) in hormone-dependent cells, but oxidative (E2-->E1) in hormone-independent cells. Using intact hormone-dependent cells, it was observed that Nomegestrol acetate. Promegestone as well as Danazol, can block the conversion of E1 to E2. Clinical trials of these "anti-enzyme" substances in breast cancer patients could be the next step to investigate new therapeutic possibilities for this disease.
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