Abstract
Estradiol was found to stimulate the activity of adenylate cyclase in the cervicovaginal epithelium of neonatal mice, demonstrated with adenylyl-imidodiphosphate and also with adenosine triphosphate (ATP) as substrate. Measures were taken to exclude interference by other ATP-degrading enzymes. The deposits of the reaction product, indicating enzyme activity, were localized on the plasma membrane of all sides of the epithelial cells. A similar distribution of enzyme activity was recorded in both controls and estradiol-stimulated animals with either of the two substrates; however, the deposits appeared most prominent after estradiol-treatment. In view of a previous report on increased activity of the cyclic AMP-degrading enzyme phosphodiesterase after estradiol-treatment, it was concluded that the parallel elevation in activity of both adenylate cyclase and cyclic AMP-phosphodiesterase indicates a role of cyclic AMP in the action mechanism of estradiol.
Published Version
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