Open AccessInhibition of steroid sulfatase activity by danazol
Author(s) -
Carlström Kjell,
Döberl Anton,
Pousette Åke,
Rannevik Gunnar,
Wilking Nils
Publication year - 1984
Publication title -
acta obstetricia et gynecologica scandinavica
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.401
H-Index - 102
eISSN - 1600-0412
pISSN - 0001-6349
DOI - 10.3109/00016348409156994
Subject(s) - danazol , steroid sulfatase , estrone sulfate , estrone , medicine , endocrinology , steroid , dehydroepiandrosterone sulfate , dehydroepiandrosterone , aminoglutethimide , medroxyprogesterone acetate , in vivo , in vitro , hydrolysis , pharmacology , hormone , androgen , chemistry , biochemistry , biology , aromatase , endometriosis , microbiology and biotechnology , cancer , breast cancer
. The hydrolysis of dehydroepiandrosterone sulfate (DHAS) by human liver cells in culture and the hydrolysis of and formation of estradiol‐17β (E 2 ) from estrone sulfate PIS) by human breast tumor preparations in vitro were studies in the presence and absence of danazol. In the latter tissue the effects of medroxyprogesterone acetate (MPA), trilostane, aminoglutethimide (AG) and tamoxifen were tested for comparison. Danazol at concentrations of 1.4 × M strongly inhibited the hydrolysis of DHAS as well as the hydrolysis of and formation of E 2 from E 1 S. With the exception of a slight inhibitory effect of trilostane upon E 1 S hydrolysis, the other four drugs did not inhibit the metabolism of E 1 S. Danazol, at concentrations corresponding to those occurring in vivo during therapy, is a potent inhibitor of steroid sulfatase activity. This may be one of the ways in which the drug affects peripheral and target tissue levels of steroid hormones.