Skip to main content

Production of Recombinant Human EPO and EPO/Fc Fusion Proteins by Chinese Hamster Ovary Cells

  • Conference paper
  • First Online:
Animal Cell Technology: Basic & Applied Aspects

Part of the book series: Animal Cell Technology: Basic & Applied Aspects ((ANICELLTECH,volume 16))

  • 1121 Accesses

Abstract

Chinese hamster ovary (CHO) cell lines for the production of recombinant human erythropoietin (hEpo) and erythropoietin/Fc fusion protein (hEpo/Fc) were established. Productivities of the proteins by transient gene expression were up-regulated by the woodchuck hepatitis virus post-transcriptional regulatory element (WPRE) residing downstream hEpo and hEpo/Fc sequences. The cells have shown to correctly synthesize bioactive hEpo and hEpo/Fc proteins. Despite that hEpo presented a higher activity in vitro, hEpo/Fc bioactivity was partially conserved.

This is a preview of subscription content, log in via an institution to check access.

Access this chapter

Chapter
USD 29.95
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
eBook
USD 259.00
Price excludes VAT (USA)
  • Available as EPUB and PDF
  • Read on any device
  • Instant download
  • Own it forever
Softcover Book
USD 329.99
Price excludes VAT (USA)
  • Compact, lightweight edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info
Hardcover Book
USD 329.99
Price excludes VAT (USA)
  • Durable hardcover edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info

Tax calculation will be finalised at checkout

Purchases are for personal use only

Institutional subscriptions

References

  1. Aggarwal, S., (2007) What’s fueling the biotech engine? Nat. Biotechnol. 25(10): 1097–1104.

    Article  CAS  PubMed  Google Scholar 

  2. Bunn, H.F. (2007) New agents that stimulate erythropoiesis. Blood 109(3): 868–873.

    Article  CAS  PubMed  Google Scholar 

  3. Jelkmann, W. (1992) Erythropoietin: structure, control of production, and function. Physol Rev 72, 449–489.

    CAS  Google Scholar 

  4. D’Andrea, A.D., Lodish, H.F., and Wong, G.G. (1989) Expression cloning of the murine erythropoietin receptor. Cell 57: 277–285.

    Article  Google Scholar 

  5. Lacombe, C., and Mayeux, P. (1998) Biology of erythropoietin. Haematologica 83: 724–732.

    Google Scholar 

  6. Eschbach, J.W., Egrie, J.C., Downing, M.R., Browne, J.K., and Adamson, J.W. (1987) Correction of the anemia of end-stage renal disease with recombinant human erythropoietin. Results of a combined phase I and II clinical trial. N. Engl. J. Med. 316: 73–78.

    Article  CAS  PubMed  Google Scholar 

  7. Abels, R.I. (1992) Use of recombinant human erythropoietin in the treatment of anemia in patients who have cancer. Semin. Oncol. 19(3 suppl 8): 29–35.

    CAS  PubMed  Google Scholar 

  8. Elliott, S., Egrie, J., Browne, J., Lorenzini, T., Busse, L., Rogers, N., and Ponting, I. (2004) Control of rHuEPO biological activity. The role of carbohydrate. Exp. Hematol. 32: 1146–1155.

    Article  CAS  Google Scholar 

  9. Way, J.C., Lauder, S., Brunkhorst, B., Kong, S., Qi, A., Webster, G., Campbell, I., McKenzie, S., Lan, Y., Marelli, B., Nguyen, L.A., Degon, S., Lo, K.M., and Gillies, S.D. (2005) Improvement of Fc-erythropoietin structure and pharmacokinetics by modification at a disulfide bond. Protein Eng. Des. Sel. 18(3): 111–118.

    Article  CAS  PubMed  Google Scholar 

  10. Kodama, D., Nishimiya, D., Iwata, K., Yamaguchi, K., Yoshida, K., Kawabe, Y., Motono, M., Watanabe, H., Yamashita, T., Nishijima, K., Kamihira, M., and Iijima, S. (2008) Production of human erythropoietin by chimeric chickens. Biochem. Biophys. Res. Commun. 367(4): 834–839.

    Article  CAS  PubMed  Google Scholar 

  11. Kamihira, M., Ono, K., Esaka, K., Nishijima, K., Kigaku, R., Komatsu, H. Yamashita, T., Kyogoku, K., and Iijima, S. (2005) High-level expression of single-chain Fv-Fc fusion protein in serum and egg white of genetically manipulated chickens by using a retroviral vector. J. Virol. 79: 10864–10874.

    Article  CAS  PubMed  Google Scholar 

  12. Ueda, H., Kawahara, M., Aburatani, T., Tsumoto, K., Todokara, K., Suzuki, E., Nishimura, H., Schueler, P.A., Winter, G., Mahoney, W.C., Kumagai, I., and Nagamune, T. (2000) Cell-growth control by monomeric antigen: The cell surface expression of lysozyme-specific Ig V domains fused to truncated Epo receptor J. Immunol. Methods 241(1–2): 159–170.

    Article  CAS  PubMed  Google Scholar 

  13. Klein, R., Ruttkowski, B., Knapp, E., Salmons, B., Günzburg, W.H., and Hohenadl, C. (2006) WPRE mediated enhancement of gene expression is promoter and cell line specific. Gene 372: 153–161.

    Article  CAS  PubMed  Google Scholar 

  14. Bitonti, A.J., Dumont, J. A., Low, S.C., Peters, R.T., Kropp, K. E., Palombella, V.J., Stattel, J.M., Lu, Y., Tan, C.A., Song, J.J., Garcia, A.M., Simister, N.E., Spiekermann, G.M., Lencer, W.I., and Blumberg, R.S. (2004) Pulmonary delivery of an erythropoietin Fc fusion protein in non-human primates through an immunoglobulin transport pathway, Proc Natl Acad Sci U S A 101(26): 9763–9768.

    Article  CAS  PubMed  Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Corresponding author

Correspondence to Yoshinori Kawabe .

Editor information

Editors and Affiliations

Rights and permissions

Reprints and permissions

Copyright information

© 2010 Springer Science+Business Media B.V.

About this paper

Cite this paper

Penno, C.A., Kawabe, Y., Ito, A., Kamihira, M. (2010). Production of Recombinant Human EPO and EPO/Fc Fusion Proteins by Chinese Hamster Ovary Cells. In: Kamihira, M., Katakura, Y., Ito, A. (eds) Animal Cell Technology: Basic & Applied Aspects. Animal Cell Technology: Basic & Applied Aspects, vol 16. Springer, Dordrecht. https://doi.org/10.1007/978-90-481-3892-0_32

Download citation

Publish with us

Policies and ethics