Abstract
Inhibin is a hypophysiotropic hormone which selectively suppresses the secretion of pituitary follicle-stimulating hormone. It has been isolated from gonadal fluids and characterized as a protein heterodimer consisting of an α subunit and one of two β subunits (βA or βB)1–4. FSH-releasing protein (FRP), also named activin, is a dimer consisting of two inhibin β-chains5–6. A factor from conditioned medium of a leukaemia cell line has been isolated which can induce mouse Friend cells to become benzidine-positive, and which shares a similar N-terminal sequence with porcine FRP7. In this report, we find that FRP and inhibin modulate both the induction of haemoglobin accumulation in a human erythroleukaemic cell line, K562, and the proliferation of erythroid progenitor cells in human bone marrow culture. These two proteins could constitute a novel humoral regulatory control of erythropoiesis which would involve two types of related protein dimers with functionally opposite effects.
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References
1. Robertson, D. M. et al. Biochem. biophys. Res. Commun. 126, 220-226 (1985). 2. Miyamoto, K. el al. Biochem. biophys. Res. Commun. 129, 396-403 (1985). 3. Rivier, J., Spiess, J., McClintock, R., Vaughan, J. & Vale, W. Biochem. Biophys. Res. Commun. 133, 120-127 (1985). 4. Ling, N. et al. Proc. natn. Acad. Sci. U.S.A. 82, 7217-7221 (1985). 5. Vale, W. et al. Nature 321, 776-779 (1986). 6. Ling, N. et al. Nature 321, 779-782 (1986). 7. Eto, Y. et al. Biochem. biophys. Res. Commun. 142, 1095-1103 (1987). 8. Lozzio, C. B. & Lozzio, B. B. Blood 45, 321-334 (1975). 9. Rutherford, T. R., Clegg, J. B. & Weatherall, D. J. Nature 280, 164-165, (1979). 10. Jokinen, M., Gahmberg, C. G. & Andersson, L. C. Nature 279, 604-607 (1979). 11. Fukuda, M. Nature 285, 405-407 (1980). 12. Rowley, P. T., Betsy, M. O. & Barbara, A. F. Blood 65, 862-868 (1985). 13. Tsiftsoglou, A. S., Gusella, J. F., Vollock, V. & Housman, D. E. Cancer Res. 39, 3849-3855 (1979). 14. Sokal, R. R. & Rohlf F. J. in Biometry 321-371 (Freeman, San Francisco, 1981. 15. Metcalf, D. Science 229, 16-22 (1985). 16. Mason, A. J. et al. Nature 318, 659-663 (1985). 17. Mayo, K. E. et al. Proc. natn. Acad. Sci. U.S.A. 83, 5849-5853 (1986). 18. Orkin, S. H., Harao, P. I. & Leder, P. Proc. natn. Acad. Sci. U.S.A. 72, 98-102 (1975). 19. Ogawa, M. Parmley, R. T. Bank, H. L. & Spicer, S. S. Blood 48, 407-417 (1976). 20. Singh, M. K. & Yu, J. Nature 309, 631-633 (1984). 21. Hsu, S. M., Raine, L. & Fanger, H. Am. J. din. Pathol. 75, 734-738 (1981).
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Yu, J., Shao, Le., Lemas, V. et al. Importance of FSH-releasing protein and inhibin in erythrodifferentiation. Nature 330, 765–767 (1987). https://doi.org/10.1038/330765a0
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DOI: https://doi.org/10.1038/330765a0
