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B Robaire

Publications and source records attributed to B Robaire.

At least 91 records · Page 5Linked to original sources

On the presence and regulation of 3 alpha-hydroxysteroid dehydrogenase in the adult rat ovary.

The presence of 3 alpha-hydroxysteroid dehydrogenase activity in adult rat ovaries was assessed by direct measurement of the conversion of dihydrotestosterone to 5 alpha-androstan-3 alpha, 17 beta-diol (3 alpha-diol). This enzyme was indeed found in this tissue with a high specific activity (414--560 nmol of 3 alpha-diol formed/h/mg protein) when compared to other hormone-dependent tissues. During the 4-day rat estrous cycle, the enzymatic activity was found to fluctuate by approximately 30% with the peak of activity at proestrus and the nadir at estrus. Further evidence for the hormonal regulation of this enzymatic activity was obtained with hypophysectomy and hormone replacement studies. Hypophysectomy resulted in a nearly 50% decrease when activity is expressed per ovary but this treatment had no significant effect on the specific activity (per mg ovary or per mg protein) of the enzyme. Hormone replacement, via polydimethylsiloxane capsules, with estradiol-17 beta resulted in a doubling of ovarian 3 alpha-HSD activity per mg protein but no significant change on a per ovary basis while replacement with testosterone caused a major decrease in activity to 15--30% (depending on the mode by which enzyme activity is expressed) of control hypophysectomized animals. These data thus indicate that this enzyme activity is present in the ovary and that it is regulated by gonadotrophins or gonadotrophin-induced steroids. The potential significance of these observations on follicular development and atresia is discussed.

3-Hydroxysteroid Dehydrogenases↗

Regulation of epididymal glutathione S-transferases: effects of orchidectomy and androgen replacement.

Glutathione S-transferases, a family of enzymes that catalyze the conjugation of glutathione to a variety of substrates, are present in rat epididymis. In order to study the hormonal regulation of these enzymes in this tissue, adult rats were orchidectomized and implanted with empty or androgen-filled polydimethylsiloxane capsules. Orchidectomy alone significantly decreased caput-corpus epididymal glutathione S-transferase activity toward 2 substrates, 1-chloro-2,4-dinitrobenzene and trans-4-phenylbut-3-en-2-one, but had no effect on transferase activity toward the third substrate, 1,2-dichloro-4-nitrobenzene. In contrast to these results, orchidectomy did not alter glutathione S-transferase activity towards these substrates in the cauda epididymidis. Androgen replacement with testosterone prevented the orchidectomy-induced decrease in caput-corpus glutathione S-transferase activity toward 1-chloro-2,4-dinitrobenzene and trans-4-phenylbut-3-en-2-one and had no effect on transferase activity toward 1,2-dichloro-4-nitrobenzene. The effects of 5 alpha-reduced metabolites of testosterone were also studied. Both dihydrotestosterone and 5 alpha-androstan-3 alpha, 17 beta-diol maintained caput-corpus glutathione S-transferase activity toward 1-chloro-2,4-dinitrobenzene, although a lower dose of dihydrotestosterone was sufficient; these 1 androgens were unable to maintain activity toward trans-4-phenylbut-3-en-2-one and caused a suprastimulation of activity toward 1,2-dichloro-4-nitrobenzene above control values. The third 5 alpha-reduced androgen studied, 5 alpha-androstan-3 beta, 17 beta-diol had no effect on the transferase activity toward any of the 3 substrates. These results demonstrate that the epididymal glutathione S-transferases are under separate control and are differentially regulated by testosterone and its 5 alpha-reduced metabolites.

Androgens↗

The presence and longitudinal distribution of the glutathione S-transferases in rat epididymis and vas deferens.

The presence of the glutathione S-transferases, enzymes that catalyse the conjugation of glutathione with a variety of compounds, is reported here, for the first time, in the mammalian epididymis-vas deferens. These glutathione S-transferases, approx. 50% of those from rat liver on a per-mg-of-protein basis, are resolved by isoelectric focusing into six peaks, each with a characteristic isoelectric point and substrate specificity. By these same criteria, the first three peaks (pI 8.9, 8.2 and 7.8) can be identified as transferases B, A and C respectively. The fifth peak (pI7.2) may correspond to transferase M; the fourth (pI7.5) and sixth (pI7.0) peaks do not correspond to previously described transferases. The distribution of transferase activity towards any one substrate studied differs in sequential sections of the epididymis and vas deferens; in addition, the longitudinal-distribution pattern differs for each of the three substrates studied. Isoelectric focusing of the cytosol fractions of the different sections further substantiates these observations. The potential significance of these enzymes and of their distribution in terms of epididymal function, maturation of spermatozoa, is discussed.

Animals↗

Steroid delta 4-5 alpha-reductase and 3 alpha-hydroxysteroid dehydrogenase in the rat epididymis during development.

delta 4-5 alpha-Reductase activity is apparently regulated by a testicular factor(s) secreted directly into the epididymis, whereas 3 alpha-hydroxysteroid dehydrogenase activity, in this tissue, appears to reflect circulating androgen levels. To test whether the factor(s) regulating delta 4-5 alpha-reductase activity is directly associated with spermatozoa, a developmental study was undertaken to temporally correlate various parameters of the male reproductive tract with enzymatic activities. delta 4-5 alpha-Reductase activity is first detectable at 21 days of age. Activity increases until day 77, after which time enzymatic activity decreases by more than 60%, reaching steady adult values at 105 days. 3 alpha-Hydroxysteroid dehydrogenase activity is detectable as early as 7 days. Levels of this enzyme increase until day 63, after which time constant adult values are maintained until at least 1 yr. Spermatids and/or spermatozoa are first seen in the testes at 42 days, and plateau levels are reached by day 77. Spermatozoa are first seen in the epididymis at 49 days and reach maximal values by 91 days; no significant change occurs thereafter (until 365 days). Increases in seminal vesicle and ventral prostate weights are of a sigmoidal type, paralleling increases in plasma androgens, with the greatest rate of rise between days 35--63. This sigmoidal type of increase in tissue weights and plasma androgens is similar to that seen for epididymal 3 alpha-hydroxysteroid dehydrogenase but markedly different from that found for delta 4-5 alpha-reductase. The importance of delta 4-5 alpha-reductase and 3 alpha-hydroxysteroid dehydrogenase activities in the epididymis before the entry of spermatozoa and the decline in delta 4-5 alpha-reductase activity with age is discussed.

3-Hydroxysteroid Dehydrogenases↗

Effects of unilateral orchidectomy on rat epididymal delta 4-5 alpha-reductase and 3 alpha-hydroxysteroid dehydrogenase.

The effects of unilateral orchidectomy on the adult rat epidiymal testosterone metabolizing enzymes, delta 4-5 alpha-reductase and 3 alpha-hydroxysteroid dehydrogenase, are investigated. Five weeks following unilateral orchidectomy, it is found that the activity of 3 alpha-hydroxysteroid dehydrogenase per organ is not altered, whereas delta 4-5 alpha-reductase activity decreased by more than 80% on the side of the orchidectomy. Neither accessory sex tissue weights, ventral prostate and seminal vesicles, nor the concentration of circulating testosterone, luteinizing hormone, follicle-stimulating hormone, or prolactin is altered by unilateral orchidectomy. These data indicate that (1) epididymal 3 alpha-hydroxysteroid dehydrogenase activity can be maintained by circulating androgens and that (2) the major factor regulating delta 4-5 alpha-reductase activity is not a substance secreted by the testes into the peripheral circulation. It is suggested that a substance directly secreted into the epididymis by the testis regulates epididymal delta 4-5 alpha-reductase activity.

3-Hydroxysteroid Dehydrogenases↗