Glycosylation of Erythropoietin Receptor

  • S. Masuda
  • Y. Hisada
  • M. Ueda
  • R. Sasaki


The size of the murine erythropoietin (EPO) receptor (EPO-R), 105 kDa, estimated from EPO.EPO-R cross-linked products,is much higher than that, 53 kDa, predicted from EPO-R cDNA. The lectinbinding properties of the solubilized EPO-R suggested that EPO-R was N-glycosylated. To find whether glycosylation of EPO-R accounted for the difference in size, the decrease in size of [125I]EPO•EPO-R cross-linked products by enzymatic deglycosylation was examined. N-glycosylation of EPO-R was at most 10 kDa, not accounting for the difference in size predicted from cDNA and from cross-linked experiments. The possibilities that may cause the difference in receptor size are discussed.


Sialic Acid Erythroid Cell Erythropoietin Receptor Fucose Residue Friend Virus 
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  1. 1.
    Krantz, S. B. and Goldwasser, E. (1984) ‘Specific binding of erythropoietin to spleen cells infected with the anemia strain of Friend virus’, Proc. Natl. Acad. Sci. USA 81, 7574–7578PubMedCrossRefGoogle Scholar
  2. 2.
    Sasaki, R., Yanagawa, S., Hitomi, K. and Chiba, H. (1987) ‘Characterization of erythropoietin receptor of murine erythroid cells’, Eur. J. Biochem. 168, 43–48PubMedCrossRefGoogle Scholar
  3. 3.
    Todokoro, K., Kanazawa, S., Amanuma, H. and Ikawa, Y. (1987) ‘Specific binding of erythropoietin to its receptor on responsive erythroleukemia cells’, Proc. Natl. Acad. Sci. USA 84, 4126–4134PubMedCrossRefGoogle Scholar
  4. 4.
    Sawyer, S. T., Krantz, S. B. and Luma, J. (1987) ‘Identification of the receptor for erythropoietin by cross-linking to Friend virus-infected erythroid cells’,Proc. Natl. Acad. Sci. USA 84, 3690–3694PubMedCrossRefGoogle Scholar
  5. 5.
    Tojo, A., Fukamachi, H., Kasuga, M., Urabe, A. and Takaku, F. (1987)’Identification of erythropoietin receptors on fetal erythroid cells’, Biochem. Biophys. Res. Commun. 148,443–448PubMedCrossRefGoogle Scholar
  6. 6.
    Mayeux, P., Billat, C. and Jacquot, R. (1987) ‘The erythropoietin receptor of rat erythroid progenitor cells’, J. Biol. Chem. 262, 13985–13990PubMedGoogle Scholar
  7. 7.
    Hitomi, K., Fujita, K., Sasaki, R., Chiba, H., Okuno, Y., Ichiba, S., Takahashi, T. and Imura, H. (1988) ‘Erythropoietin receptor of a human leukemic cell line with erythroid characteristics’, Biochem. Biophys. Res. Commun. 154, 902–909PubMedCrossRefGoogle Scholar
  8. 8.
    Broudy, V., Lin, N., Egrie, J., de Haen, C., Weiss, T., Papayannopoupolou, T. and Adamson, J. W. (1988) ‘Identification of the receptor for erythropoietin on human and murine erythroleukemia cells and modulation by phorbol ester and dimethyl sufoxide’, Proc. Natl. Acad. Sci. USA 85, 6513–6517PubMedCrossRefGoogle Scholar
  9. 9.
    Goto, M., Akai, K., Murakami, A., Hashimoto, C., Tsuda, E., Ueda, M., Kawanishi, G., Takahashi, N., Ishimoto, A., Chiba, H. and Sasaki, R. (1988) ‘Production of recombinant human erythropoietin in mammalian cells: host-cell dependency of the biological activity of the cloned glycoprotein’, Bio/Technology 6, 67–71CrossRefGoogle Scholar
  10. 10.
    Sawyer, S. T. (1989) ‘The two proteins of the erythropoietin receptor are structurally similar’, J. Biol. Chem. 264, 13343–13347PubMedGoogle Scholar
  11. 11.
    D’Andrea, A. D., Lodish, H. F. and Wong, G. G. (1989) ‘Expression cloning of the murine erythropoietin receptor’, Cell 57, 277–285PubMedCrossRefGoogle Scholar
  12. 12.
    Hitomi, K., Masuda, S., Ito, K., Ueda, M. and Sasaki, R. (1989) ‘Solubilization and characterization of erythropoietin receptor from transplantable mouse erythroblastic leukemic cells’, Biochem. Biophys. Res. Commun. 160, 1140–1148PubMedCrossRefGoogle Scholar
  13. 13.
    Tsuda, E., Kawanishi, G., Ueda, M., Masuda, S. and Sasaki, R. (1990) ‘The role of carbohydrate in recombinant human erythropoietin’, Eur. J. Biochem. 188, 405–411PubMedCrossRefGoogle Scholar
  14. 14.
    Yoshimura, A., D’Andrea, A. D., and Lodish, H. (1990) ‘Friend spleen focus-forming virus glycoprotein gp55 interacts with the erythropoietin receptor in the endoplasmic reticulum and affects receptor metabolism’, Proc. Natl. Acad. Sci. USA 87, 4139–4143PubMedCrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media Dordrecht 1991

Authors and Affiliations

  • S. Masuda
    • 1
  • Y. Hisada
    • 1
  • M. Ueda
    • 2
  • R. Sasaki
    • 1
  1. 1.Department of Food Science and Technology, Faculty of AgricultureKyoto UniversityKyotoJapan
  2. 2.Research Institute of Life ScienceSnow Brand MilkTochigiJapan

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