Abstract
Inhibin, a specific and potent polypeptide inhibitor of the secretion of follicle-stimulating hormone (FSH)1, of gonadal origin and thus a potential contraceptive, may constitute a missing link in the mechanism controlling the differential secretion of the pituitary gonadotropins. Inhibin-like bioactivity has been reported in various fluids and extracts of testis2–5 and in ovarian follicular fluid6–10. Although there have been several attempts to purify inhibin from seminal plasma11–13, purification from follicular fluid has been more successful (refs 14–16; for review see ref. 17). We have previously isolated two forms (A and B) of inhibin from porcine follicular fluid14. Each form comprised two dissimilar subunits of relative molecular mass (Mr) 18,000 (18K, referred to here as the α-subunit) and 14K (the β-subunit), crosslinked by one or more disulphide bridges(s). Forms A and B differ in the N-terminal sequence of their 14K subunit. Preliminary structural characterization of porcine15 and bovine16 ovarian inhibins shows that they have similar properties. Here, we have used the N-terminal amino-acid sequence data on the subunits of each inhibin to identify cloned complementary DNAs encoding the biosynthetic precursors and report that inhibins are the product of a gene family that also includes transforming growth factor-β (TGF-β) and whose structural organization is similar to that of pituitary and placental glycoprotein hormones.
This is a preview of subscription content, access via your institution
Access options
Subscribe to this journal
Receive 51 print issues and online access
$199.00 per year
only $3.90 per issue
Buy this article
- Purchase on Springer Link
- Instant access to full article PDF
Prices may be subject to local taxes which are calculated during checkout
Similar content being viewed by others
References
McCullagh, D. R. Science 76, 19–20 (1932).
Keogh, E. et al. Endocrinology 98, 997–1004 (1976).
Setchell, B. & Jacks, F. J Endocr. 62, 675–676 (1974).
Franchimont, P., Chari, S., Hagelstein, M. & Duraiswami, S. Nature 257, 402–404 (1975).
Chari, S., Duraiswami, S. & Franchimont, P. Acta endocr. 87, 434–448 (1978).
de Jong, F. & Sharpe, R. Nature 263, 71–72 (1976).
Hopkinson, C. et al. J. Reprod. Fert. 50, 93–96 (1977).
Welschen, R., Hermans, W., Dullart, J. & de Jong, F. J. Reprod. Fert. 50, 129–131 (1977).
Schwartz, N. & Channing, C. Proc. natn. Acad. Aci. U.S.A. 74, 5721–5724 (1977).
Rivier, J. et al. in Endocrinology, int Congr. Ser. No. 655 (eds Labrie, F. & Proulx, L.) 1141–1144 (Excerpta Medica, Amsterdam, 1984).
Ramasharma, K. et al. Science 223, 1199–1201 (1984).
Li, C. H., Hammond, R. G., Ramasharma, K. & Chung, D. Proc. natn. Acad. Sci. U.S.A. 82, 4041–4044 (1985).
Seidah, N., Arbatti, N., Rochemont, J., Sheth, A. & Chretien, M. FEBS Lett. 175, 349–354 (1985).
Ling, N. et al. Proc. natn. Acad. Sci. U.S.A. 82, 7217–7221 (1985).
Miyamoto, K. et al. Biochem. biophys. Res. Commun. 129, 396–403 (1985).
Robertson, D. M. et al. Biochem. biophys. Res. Commun. 126, 220–226 (1985).
de Jong, F. & Robertson, D. M. Molec. cell. Endocr. 42, 95–103 (1985).
Anderson, S. & Kingston, I. B. Proc. natn. Acad. Sci. U.S.A. 80, 6836–6842 (1983).
Ullrich, A. et al. Nature 309, 418–425 (1984).
Derynck, R. et al. Nature 316, 701–705 (1985).
Seeburg, P. H. & Adelman, J. P. Nature 311, 666–668 (1984).
Dull, T. J., Gray, A., Hayflick, J. S. & Ullrich, A. Nature 310, 777–781 (1984).
Setzer, D. R., McGrogan, M., Nunberg, J. H. & Schimke, R. T. Cell 22, 361–370 (1980).
Tosi, M., Young, R. A., Hagenbuchle, O. & Schibler, U. Nucleic Acids Res. 9, 2313–2323 (1981).
Assoian, R. K., Komoriya, A., Meyers, C. A., Miller, D. M. & Sporn, M. B. J. biol Chem. 258, 7155–7160 (1983).
Pierce, J. & Parsons, T. A. Rev. Biochem. 50, 465–495 (1981).
Counis, R., Corbani, M., Poissonnier, M. & Jutisz, M. Biochem. biophys. Res. Commun. 107, 998–1005 (1982).
Tonegawa, S. Nature 302, 575–581 (1983).
Vale, W., Grant, G., Amoss, M., Blackwell, R. & Guillemin, R. Endocrinology 91, 562–572 (1972).
Kaplan, B. B., Bernstein, S. L. & Gioio, A. E. J. Biochem. 183, 181–184 (1979).
Huynh, T. V., Young, R. A. & Davis, R. W. in DNA Cloning Vol. 1, A Practical Approach (ed. Glover, D.) 49–78 (IRL, Oxford, 1985).
Wood, W. et al. Nature 312, 330–337 (1984).
Messing, J., Crea, R. & Seeburg, P. H. Nucleic Acids Res. 9, 309–321 (1981).
Sanger, F., Nicklen, S. & Coulson, A. R. Proc. natn. Acad. Sci. U.S.A. 74, 5463–5467 (1977).
Takahashi, Y. et al. Proc. natn. Acad. Sci. U.S.A. 82, 1931–1935 (1985).
Dobner, P. R., Kawasaki, E. S., Yu, L. Y. & Bancroft, F. C. Proc. natn. Acad. Sci. U. S. A. 78, 2230–2234 (1981).
Thomas, P. S. Proc. natn. Acad. Sci. U.S.A. 77, 5201–5205 (1980).
Taylor, J. M., Illmensee, R. & Summers, S. Biochim. biophys. Acta 442, 324–330 (1976).
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Mason, A., Hayflick, J., Ling, N. et al. Complementary DNA sequences of ovarian follicular fluid inhibin show precursor structure and homology with transforming growth factor-β. Nature 318, 659–663 (1985). https://doi.org/10.1038/318659a0
Received:
Accepted:
Issue Date:
DOI: https://doi.org/10.1038/318659a0
This article is cited by
-
Insights into in vivo follicle formation: a review of in vitro systems
Histochemistry and Cell Biology (2022)
-
Steroid hormone synthesis by the ovarian stroma surrounding epithelial ovarian tumors: a potential mechanism in ovarian tumorigenesis
Modern Pathology (2017)
-
Régulation des fonctions de l’épithélium épididymaire des mammifères: état des lieux
Andrologie (2006)
-
Genetic dissection of mammalian fertility pathways
Nature Medicine (2002)
Comments
By submitting a comment you agree to abide by our Terms and Community Guidelines. If you find something abusive or that does not comply with our terms or guidelines please flag it as inappropriate.