Danazol binding to steroid receptors in human uterine endometrium.

Abstract:

:To understand the mechanism of action of danazol, the binding of danazol to multiple classes of intracellular steroid binding proteins was studied in the human uterine endometrium. Danazol bound to endometrial receptors for estrogen, progesterone, and androgen and seemed to bind to endometrial intracellular corticosteroid-binding globulin and sex-hormone-binding globulin. Danazol occupies almost all binding sites of steroids in the steroid target cells in spite of the presence of endogenous steroids. It is speculated that the binding behavior of danazol may be related to its therapeutic effect on endometriosis. :Binding of danazol to multiple classes of intracellular steroid binding proteins was studied in the human uterine endometrium in an effort to understand danazol's mechanism of action. Danazol, which binds to human endometrial cytosol receptors for androgen (AR), progestin (PR), and estrogen (ER), also appears to interact with sex hormone binding globulin and corticosteroid binding globulin present in the cytosol preparations. 17 beta-hydroxy-17 alpha-methyl-estra-4, 9, 11-trine-3-one-[17 alpha-methyl-3h], 87 Ci/mmol (3H-R1881) binds to AR and PR in the human uterine endometirum. Thus, 3H-R1881/PR binding was abolished by the presence of progesterone. Previously reported studies have demonstrated that danazol binds with relatively high affinity to AR. Also, the danazol/AR complex can translocate to the nucleus. These findings are consistent with the observed androgenic effects of danazol in rats and women. Danazol binds with moderate affinity to PR. The danazol/PR complex is poorly translocated to the nucleus, suggesting that danazol is antiprogestational. Yet, a major metabolite of danazol, ethisterone, is progestational. The progestational vs. the antiprogestational effects of danazol remain controversial. Danazol displacement of 6, 7-3H-)stradial-17 beta (3H-E2) from ER is not parallel to E2 displacement of 3H-E2 when compared with that of PR or AR. This discrepancy may derive from an affinity difference. Danazol binds poorly to ER, yet circulating concentrations of danazol in vivo may lead to complete occupancy of the ER by danazol, which may interfere with normal endometrial ER dynamics, resulting in an antiestrogenic effect. Danazol occupies almost all binding sites of steroids in the steroid target cells despite the presence of endogenous steroids. The binding behavior of danazol may be related to its therapeutic effect on endometriosis.

journal_name

Fertil Steril

journal_title

Fertility and sterility

authors

Tamaya T,Wada K,Fujimoto J,Yamada T,Okada H

doi

10.1016/s0015-0282(16)47840-4

subject

Has Abstract

pub_date

1984-05-01 00:00:00

pages

732-5

issue

5

eissn

0015-0282

issn

1556-5653

pii

S0015-0282(16)47840-4

journal_volume

41

pub_type

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