Secretion of glycosidases in human epididymal cell cultures.

The dynamics of glycosidase secretion was evaluated in human epididymal cell culture. Epithelial cells from caput, corpus, and cauda epididymis were isolated from tissue obtained from patients undergoing therapeutic orchidectomy due to prostatic carcinoma. The activities of alpha-glucosidase, N-acetylglucosaminidase, beta-glucuronidase, and alpha-mannosidase were analyzed in conditioned culture media. Glycosidase activity was significantly higher in corpus and/or cauda than in caput epididymis. There was a time-dependent increase in enzyme activities that was maximal between 10 and 14 days of culture in all epididymal regions. Epididymal glycosidases are secreted by cultured epithelial cell from human epididymis with an increase toward the distal regions of this organ, which may be related to the dynamics of sperm maturation. Cultures from different epididymal regions may represent a valuable tool to study of human epididymal function.

Flutamide as a tool to study the hormonal regulation of the reproductive tract in the golden hamster.

The effect of flutamide (FLU) administered during 6 weeks at doses of 50 or 100 mg kg-1 body weight, on various reproductive characteristics of sexually active male golden hamsters was studied. The weight of seminal vesicles and epididymides showed a dose dependent inhibition with FLU, while testicular weight exhibited a biphasic response, its value being increased by 20% at lower FLU doses and reduced by 15% at higher FLU doses. An elevation of testicular and epididymal androgen-binding protein (ABP) content and also of testicular testosterone content was observed with both doses of FLU. Serum levels of LH and testosterone exhibited a four-fold increase, at both doses of FLU, while FSH serum level was elevated depending on the dose of FLU used. Results suggest that in the golden hamster the maintenance of the weight of testes and accessory organs depends mainly on androgenic stimulation, while production and transport of ABP is probably regulated by gonadotropins.

Effects of cyproterone acetate on the reproductive tract and pituitary-gonadal axis of the golden hamster.

The effects of cyproterone acetate (CA) on the reproductive tract and serum levels of gonadotropins and testosterone in male golden hamsters exposed to long days, were studied. The daily injection of CA at 100 mg kg-1 body weight during 8 weeks reduced sperm count, both in caput and cauda epididymidis. The weight of epididymis and seminal vesicles were also reduced, while testicular weight and histology were not affected. Serum levels of testosterone and LH were increased 3.6 and 1.8 fold, respectively, above controls, while FSH was not affected by the treatment with CA. The absence of an inhibitory action of CA on the testis could be explained through an increase in LH stimulation, thus suggesting that in the golden hamster CA is devoid of progestagenic partial effects.

Identification of androgen binding-protein (ABP) from testis and epididymis of the seasonal rodent, Octodon degus (Molina, 1872).

ABP, a Sertoli cell secretory product, was identified in the seasonal rodent Octodon degus (Molina, 1872). It was shown to be present in cytosols from the testis and epididymis. It migrated with an Rf of 0.37 on nondenaturing polyacrylamide gels. Ligation of the vas efferens caused the disappearance of ABP from the epididymis and its accumulation in the testis, indicating its testicular origin. Binding to [3H]5 alpha-DHT was specific and completely reversible, with an apparent Kd of 3.5 +/- 0.4 X 10(-9) M. Half-times of association and dissociation were at 15 and 120 minutes, respectively. Binding equilibrium was achieved at 120 minutes. Steroid affinity relative to the best competitor, 5 alpha-DHT, was 0.27 for testosterone, 0.06 for 17 beta-estradiol, and 0.01 for cyproterone acetate. The presence and similar characteristics of ABP in a wide variety of mammals, including those with special reproductive strategies such as seasonal breeding, suggests that this protein may play a general role in the mechanisms regulating spermatogenesis, probably affecting the transport and concentration of androgens in the testis and epididymis.

Characterization of a testis specific antigen in the mouse.

The partial characterization of a mouse hydrosoluble testis specific protein by crossed immunoelectrophoresis, ion-exchange chromatography and SDS-Page was made. This protein presented a low electrophoretic motility at pH 8.6. It was not adsorbed to DEAE-Sephacel at pH 8.6, but was slightly adsorbed at pH 9.0, while in CM-Sephadex it was readily adsorbed at pH 6.0, indicating the basic nature of this protein. The apparent molecular weight was determined to be of 28 Kd by SDS-Page. The previously reported testis specificity of this protein was corroborated by its absence in a liver extract.