Hormonal Control of Lysosomal Enzymes During Spermatogenesis in the Rat1

Abstract

Acid phosphatase and β-glucuronidase, 2 lysosomal enzymes, have been studied in terms of their specific activities and cytochemical localization during spermatogenesis in the rat. β-Glucuronidase activity is detectable only in Sertoli and spermatogonia cells. Its specific activity is high in the immature rat, but with development of the spermatocytes it is markedly reduced. Acid phosphatase is detectable in all germinal cells, and its specific activity increases with development of the spermatocytes and with the formation of the acid phosphatasecontaining Golgi and pro-acrosomal structures of the spermatids. Hypophysectomy at age 28 days prevents spermatid formation, and the relative levels of β-glucuronidase and acid phosphatase revert to the specific activities characteristic of the 10- to 15-day-old rat testis. Treatment of the hypophysectomized rats with FSH and LH or with testosterone permitted spermatid formation, and the specific activities of acid phosphatase and β-glucuronidase progressed to levels characteristic of the intact adult rat testis. During spermatogenesis the relative complement of lysosomal enzymes is altered. Acid phosphatase and β-glucuronidase thus serve as biochemical markers of biological development at specific, hormone-dependent steps in spermatogenesis. (Endocrinology88: 579, 1971)