Activity of Human Placental Sulfatase and 11β-Hydroxysteroid Dehydrogenase with Respect to Steroids of the Pregn-4-ene C-21-yl Sulfate Series

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Abstract
Sulfatase and 11β-hydroxysteroid dehydrogenase activities of human placenta were studied with respect to four steroids of the pregn-4-ene C-21-yl-sulfate series. Homogenates, as well as the microsomal fraction of placenta obtained either at midterm or at term, possessed negligible sulfatase activity with respect to the sulfates of 11-dehydrocorticosterone and corticosterone, and low but consistent activity towards 11-deoxycorticosterone sulfate. Under the same conditions dehydroepiandrosterone sulfate was hydrolyzed almost quantitatively.Placental homogenates converted cortisol to cortisone and corticosterone to 11-dehydrocorticosterone. The reaction was greatly enhanced by the addition of NADP. In contrast, the corresponding 11β-hydroxy-C-21 steroid sulfates were poor substrates with respect to placental 11β-hydroxysteroid dehydrogenase, as indicated by the low yields of the sulfates of cortisone and 11-dehydrocorticosterone, even in the presence of NADP. These findings are consistent with the pattern of steroids of the pregn-4-ene series characterized in human cord plasma.

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