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Purification and characterization of an FSH releasing protein from porcine ovarian follicular fluid

Abstract

A variety of hypophysiotropic peptides or proteins have been reported to be present in mammalian gonads. Inhibin, a hormone that under most circumstances selectively suppresses the secretion of follicle-stimulating hormone (FSH) but not luteinizing hormone (LH), has been isolated from the gonadal fluids of several species1–5 and characterized as a heterodimeric protein consisting of α- and β-polypeptides associated by disulphide bonds. The complete amino-acid sequences of the precursors of porcine6,7 and human7 inhibin α-subunits and two distinct porcine inhibin β-subunits (βA and βB)6 have been deduced from complementary DNA sequences. Gonadotropin releasing peptides have also been found in the gonad and have generally been shown to be active in radioreceptor assays for gonadotropin releasing hormone (GnRH) but to exhibit different chromatographic and immunological characteristics from those of GnRH8–14. During our purification of inhibin from porcine follicular fluid, we noted fractions that could stimulate the secretion of FSH by cultured anterior pituitary cells3. We report here the purification of an FSH releasing protein (FRP) and its characterization by SDS-polyacrylamide gel electrophoresis under non-reducing and reducing conditions and by partial sequence analysis. Our results indicate that porcine gonadal FRP is a homodimer consisting of two inhibin βA-chains linked by disulphide bonds. FRP is highly potent (50% effective concentration (EC50)25 pM) in stimulating the secretion and biosynthesis of FSH but not of LH or any other pituitary hormone. In contrast to the effects of GnRH and other reported gonadal gonadotropin releasing fractions, the action of FRP is not mediated by GnRH receptors.

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References

  1. Robertson, D. M. et al. Biochem. biophys. Res. Commun. 126, 220–226 (1985).

    Article  CAS  Google Scholar 

  2. Miyamoto, K. et al. Biochem. biophys. Res. Commun. 129, 396–403 (1985).

    Article  CAS  Google Scholar 

  3. Rivier, J., Spiess, J., McClintock, R., Vaughan, J. & Vale, W. Biochem. biophys. Res. Commun. 133, 120–127 (1985).

    Article  CAS  Google Scholar 

  4. Ling, N. et al. Proc. natn. Acad. Sci. U.S.A. 82, 7217–7221 (1985).

    Article  ADS  CAS  Google Scholar 

  5. Robertson, D. M. et al. Molec. cell. Endocr. 44, 271–277 (1986).

    Article  CAS  Google Scholar 

  6. Mason, A. J. et al. Nature 318, 659–663 (1985).

    Article  ADS  CAS  Google Scholar 

  7. Mayo, K. et al. Proc. natn. Acad. Sci. U.S.A. (in the press).

  8. Bhasin, S., Heber, D., Peterson, M. & Swerdloff, R. Endocrinology 112, 1144–1146 (1983).

    Article  CAS  Google Scholar 

  9. Dutlow, C. M. & Millar, R. P. Biochem. biophys. Res. Commun. 101, 486–494 (1981).

    Article  CAS  Google Scholar 

  10. Paull, W. K., Turkelson, C. M., Thomas, C. R. & Arimura, A. Science 213, 1263–1264 (1981).

    Article  ADS  CAS  Google Scholar 

  11. Sharpe, R. M. Biol. Reprod. 30, 29–49 (1984).

    Article  CAS  Google Scholar 

  12. Sharpe, R. M. & Fraser, H. M. Nature 287, 642–643 (1980).

    Article  ADS  CAS  Google Scholar 

  13. Aten, R. F., Wolin, D. L. & Behrman, H. R. Endocrinology 118, 961–967 (1983).

    Article  Google Scholar 

  14. Ying, S.-Y., Ling, N., Bohlen, P. & Guillemin, R. Endocrinology 108, 1206–1213 (1981).

    Article  CAS  Google Scholar 

  15. Vale, W., Grant, G., Amoss, M., Blackwell, R. & Guillemin, R. Endocrinology 91, 562–572 (1972).

    Article  CAS  Google Scholar 

  16. Derynek, R. et al. Nature 316, 701–705 (1985).

    Article  ADS  Google Scholar 

  17. Mizunauma, H. et al. Brain Res. Bull. 10, 623–629 (1984).

    Article  Google Scholar 

  18. Igarashi, M. & McCann, S. M. Endocrinology 74, 446–452 (1964).

    Article  CAS  Google Scholar 

  19. Igarashi, M., Taya, K. & Ishikawa, J. in Psychoneuro-endocrinology (ed. Hatotani, N.) 178–186 (Karger, Basel, 1973).

    Google Scholar 

  20. Dhariwal, A. P. S., Watanabe, S., Antunes-Rodrigues, J. & McCann, S. M. Neuro-endocrinology 2, 294–303 (1967).

    Article  CAS  Google Scholar 

  21. Schally, A. V. et al. Endocrinology 98, 380–391 (1976).

    Article  CAS  Google Scholar 

  22. Spiess, J. in New and Improved Methods in Protein Microsequence Analysis (eds Wittmann-Liebold, B., Salnikow, J. & Erdmann, V. A.) (Springer, New York, in the press).

  23. Spiess, J., Villareal, J. & Vale, W. Biochemistry 20, 1982–1988 (1981).

    Article  CAS  Google Scholar 

  24. Spiess, J., Rivier, J. & Vale, W. Biochemistry 22, 4341–4346 (1983).

    Article  CAS  Google Scholar 

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Vale, W., Rivier, J., Vaughan, J. et al. Purification and characterization of an FSH releasing protein from porcine ovarian follicular fluid. Nature 321, 776–779 (1986). https://doi.org/10.1038/321776a0

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