Activin and inhibin have opposite effects on steroid 5-reductase activity in genital skin fibroblasts

Activin and inhibin have opposite effects on steroid 5-reductase activity in genital skin fibroblasts

sciencedirect.com/science?_o … 5ddb89faab


The transforming growth factor β (TGF-β) superfamily includes several closely related peptides including the activins and inhibins. Since we recently reported that TGF-β1 and β2 are potent inducers of steroid 5-reductase (5R), we have now studied the effects of these other peptides using primary cultures of human scrotal skin fibroblasts.

Recombinant human activin A or inhibin A were added to cultured cells (2 × 105 cells) for 2 days in a serum free media and 5R activity was measured by the %-conversion of tracer [3H]-testosterone to dihydrotestosterone (DHT) over a 4-h period.

Activin significantly stimulated 5R activity in a dose related manner (control 3.0 ± 0.4%, activin (1.2 × 10−9 M) 6 ± 0.7%, P < 0.01, (2.4 × 10−9 M) 8.5 ± 0.6%, P < 0.001).

In comparison, androgen (DHT 10−7 M) induction of 5R was 4.7 ± 0.2%, P < 0.05. Combined exposure of fibroblasts to activin (1.2 × 10−9 M) and androgen (10−7 M) did not result in additive or synergistic effect on 5R activity. In contrast, exposure of cells to an androgen (10−7 M) and TGF-β (2 × 10−10 M) led to synergistic effects on 5R activity (control 1.5 ± 0.1%, DHT 2.6 ± 0.2% TGF-β1 4.8 ± 0.5, TGF-β1+DHT 9.2 ± 1.2%).

Finasteride, a 4-aza steroid inhibitor of 5R (10−8 M) inhibited both activin and TGF-β-induced 5R activity suggesting that the type II isoenzyme is induced by these peptides.

Activin mediated 5R activity was abolished by the addition of cycloheximide, consistent with the proposition that enzyme induction requires new protein synthesis.

Recombinant human inhibin alone did not alter basal 5R activity but dose dependently inhibited DHT (10−7 M)-induced 5R activity (control 4.1 ± 0.4%, DHT 7.5 ± 0.7%, DHT + inhibin (0.6 × 10−9 M) 5.7 ± 0.5%, P < 0.05 DHT + inhibin (1.2 × 10−9 M] 4.3 ± 0.2%, P < 0.001).

The effects of activin or inhibin were not associated with changes in cell number or thymidine uptake.

These studies indicate that activin is 100 times more potent on a molar basis than androgen in induction of 5R activity. Although both activin and TGF-β1 induce 5R activity, the actions of the two peptides differ in the presence of an androgen. In contrast, inhibin significantly inhibits androgen induction of 5R. Activin and inhibin, two closely related molecules, potentially play opposite roles in DHT formation in sexual tissue.

I came across this study today.

They actually sell Recombinant human activin A. Does anyone know of anyone who took this to boost 5AR since it was bottlenecked by fin? Is that even possible?

Another puzzle piece fits together, thank you Mew and cdnuts. My FSH barely responds to clomiphene, yet my inhibin is very high (off clomiphene) and still ~50% greater than normal while on it.

I think we need a sticky section in Bloodwork, similar to the Adiol-G thread, to allow people to post their inhihibin B levels (along with T, FSH, LH if they have those).

cd, let me know what you find out about Activin

Kazman

Sertoli cells as a target for reproductive hazards.
Monsees TK, Franz M, Gebhardt S, Winterstein U, Schill WB, Hayatpour J.

Centre of Dermatology and Andrology, Justus Liebig University, Giessen, Germany. Thomas.Monsees@derma.med.uni-giessen.de

Abstract
Male fertility can be impaired by various toxicants. Some of them are known to target mainly Sertoli cells, which play an essential role in spermatogenesis. In this study, the in vitro response of immature rat Sertoli cells to various environmental pollutants, including pesticides, oestrogenic compounds and heavy metals, has been investigated. Mitochondrial dehydrogenase activity has been used to measure Sertoli cell viability, while production of lactate and secretion of inhibin B have been used as general and specific cell markers. Sertoli cell viability was not affected after 24-h exposure to lindane, DDT, ethinyloestradiol or bisphenol A in the concentration range analysed (up to 100, 25 or 50 microM, respectively). In contrast, mercury(II) (EC50 = 31 microM) and cisplatin (15% decrease in viability at 100 microM) induced some cytotoxic effect. With the exception of the pesticide DDT, all chemicals investigated induced a significant dose-dependent increase in lactate production after 24-h exposure to Sertoli cells. Owing to the cytotoxic effect of mercury(II), lactate levels dropped again at concentrations above 20 microM. The pesticide lindane (but not DDT) and both oestrogens significantly increased the production of the Sertoli cell specific hormone inhibin B without affecting cell viability. In contrast, the heavy metals mercury(II) and platinum(II) markedly decreased inhibin B levels. This sharp decrease was already significant at metal concentrations that reduced Sertoli cell viability only moderately (10-15%). In conclusion, the secretion of lactate and inhibin B by immature rat Sertoli cells seems to be a useful and sensitive marker with which to explore potential Sertoli cell toxicants.