Abstract
In this study we test the postulate that estradiol conjugated to bovine serum albumin (E-BSA) acts via receptors for the steroid-binding protein sex hormone binding globulin (SHBG) by attempting to block E-BSA-stimulated release of oxytocin with two antagonists of SHBG receptor actions: the 5α-reduced androgens dihydrotestosterone (DHT) and 3α-diol. Simultaneous superfusion with either DHT or 3α-diol significantly blocked E-BSA-stimulated release of oxytocin. We also found that a wide range of free 17β-estradiol was unable to stimulate oxytocin release, suggesting that E-BSA stimulates receptors other than those for free estradiol to release oxytocin, perhaps SHBG receptors.
Published Version
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