Abstract
Great interest has developed in recent years on the intratesticular site of enzymes necessary for steroid hormone synthesis in mammalian testes. We have been interested in the intratesticular localization of steroid sulfatase. Steroid sulfates have been observed to be present in high concentrations in human testicular tissue. Ruokonen et al . (1) determined the amount of various free steroids and steroid sulfates in testes obtained at the time of orchiectomy for prostatic carcinoma. In their study the major steroids isolated from human testes were testosterone, pregnenolone sulfate and dehydroepiandrosterone sulfate; the concentration of each expressed as µg free steroid/ 100 g of tissue was 55, 51 and 41 respectively. In earlier studies from our laboratory (2), we demonstrated that pregnenolone sulfate, dehydroepiandrosterone sulfate and androstenediol-3-sulfate are cleaved by the same testicular steroid sulfatase with pregnenolone sulfate exhibiting the lowest Km. Further studies on the steroid sulfatase activity of homogenates or minces of testicular tissues from patients indicated that sulfatase activity was greater in isolated seminiferous tubules than in intact testicular tissue (3). As part of the same study, when pregnenolone was used as the substrate intact testicular tissue metabolized more than twice as much pregnenolone as did tubules.
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