Abstract:
:Physiological concentrations of L-T4 were found previously to stimulate Ca2+-ATPase activity in vitro in reticulocyte membranes from female rabbits and to inhibit this enzyme in reticulocyte membranes from males. In these previous studies, preincubation of intact cells or ghosts with testosterone (5 X 10(-11) M) converted female-source reticulocyte membranes to male-type responsiveness to thyroid hormone (inhibition of Ca2+-ATPase activity). Preincubation of reticulocyte membranes with 17 beta-estradiol (5 X 10(-11) M) converted male-source membranes to female-type responsiveness (stimulation by L-T4 of membrane Ca2+-ATPase activity). Using this sex steroid-sensitive thyroid hormone-dependent membrane enzyme system, we investigated the structure-activity relationships of analogs of sex steroids and unrelated steroids. 5 beta-Androstanes were active compared to testosterone in assays using female-source membranes, while 5 alpha-androstanes were less active. Within the 5 beta-androstanes, activity was dependent on at least one hydroxyl group at the C3- or C17-position. Nongonadal steroids tested were less active, establishing specificity of the sex steroid effect in assays using female-source membranes. Assayed in male-source membranes, estrone and 3-hydroxy-1,3,5-(10)7-estratraen-17-one (equilin) were active compared for estrogen effect with 17 beta-estradiol, while estriol was less active. The activities of hydrocortisone and aldosterone were 76% and 71%, respectively, in this system. These structure-activity relationships are distinct from those described for gonadal steroid-cytoplasmic binding proteins or nuclear interactions, and represent a novel sex steroid-thyroid hormone effect on activity of a membrane enzyme.
journal_name
Endocrinologyjournal_title
Endocrinologyauthors
Lawrence WD,Osawa YM,Davis PJ,Blas SDdoi
10.1210/endo-119-6-2803subject
Has Abstractpub_date
1986-12-01 00:00:00pages
2803-8issue
6eissn
0013-7227issn
1945-7170journal_volume
119pub_type
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