Lysosomal glycosidase activities in rat testis during sexual maturation

Concentrations of testosterone and its metabolite dihydrotestosterone were determined in whole rat testis during the transition from the prepuberal to the mature status. The activities of five glycosidases (beta-N-acetylhexosaminidase, alpha-L-fucosidase, beta-D-galactosidase, alpha-D-glucosidase and alpha-D-mannosidase) were also investigated in the seminiferous tubules and interstitial tissues. The same androgens and enzyme activities were measured in testis of rats treated with 17-beta-N,N-diethylcarbamoyl-4-methyl-4-aza-5-alpha-androstan-3-on e, a potent inhibitor of the 5-alpha-reductase-mediated conversion of testosterone into dihydrotestosterone. Lysosomal glycosidic activities in seminiferous tubules were found to vary slightly with the age of the animals, and thus seemed not to depend on the hormonal status of the tested animals. In contrast, the enzyme activities were low in the immarure interstitium but increased sharply during the onset of sexual maturity. The activity of each glycosidase reached a maximum between the 45th and the 65th day, except for beta-N-acetylhexosaminidase which did not decrease significantly following the 55th day. The five lysosomal enzyme activities decreased in the interstitial compartment of rat testis treated with DMAA, suggesting a relationship between these glycosidic enzyme activities and dihydrotestosterone.