The effect of adrenocorticotrophic hormone on sulfate metabolism in the rat adrenal gland.

Abstract

An existing method for the measurement of m-aminophenyl sulfate by the formation of an azo dye has been modified so that in the presence of free m-aminophenol low, constant blanks were obtained. This permitted large groups of sample to be handled with ease. The enzymes for the synthesis of phosphoadenosine-phosphosulfate were shown to be present in the soluble fraction of the adrenal gland. The synthesis was stimulated by Cl- and to a lesser extent by Br-. Administration of adrenocorticotropic hormone, in vivo, and 3′,5′-cyclic AMP, in vitro, had no effect on the synthesis. Using methods which were shown to be adequate for the assay of steroid sulfokinase with preparations from rat liver, no activity could be measured in rat adrenal preparations. Experimental manipulation of rats to produce adrenals which mimic some human pathological states, i.e., hyperplasia and a block in 3β-hydroxysteroid dehydrogenase, also resulted in no measurable steroid sulfokinase activity. Rat adrenals were, however, able to sulfate m-aminophenol but to a considerably lesser extent than rat liver. Steroid sulfatase was localized in the microsomal fraction. p-Nitrophenyl sulfate was also hydrolyzed by this fraction. When steroid sulfatase was measured at different times after the administration of adrenocorticotropic hormone a small, marginally significant increase was found five min after injection. (Endocrinology91: 852, 1972)