Abstract
Human thrombopoietin (hTPO) is a potential therapeutic glycoprotein for the amelioration of thrombocytopenia associated with chemotherapy, irradiation and bone marrow transplantation. Posttranslational modification of a product protein includes various rate-limiting interactions with numerous chaperones and enzymes in the secretory pathway. The efficient secretion of recombinant proteins from eukaryotic cells requires simple targeting the proteins to endoplasmic reticulum (ER) and directing their translocation into lumenal compartment of the ER. Although many groups overexpressed chaperone proteins in recombinant CHO cells (rCHO), effect of elevated ERp57 expression level on the secretion of foreign protein in CHO cells has not been reported yet.
Keywords
- Foreign Protein
- Recombinant Protein Productivity
- Endoplasmic Reticulum Chaperone
- Efficient Secretion
- Viable Cell Concentration
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.
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References
Raymond, D.; Kenneth, S.; Brian, R.; James, T.; Pranhitha, R. (2000) Effect of PDI overexpression on recombinant protein secretion in CHO c, Biotechnol. Prog, 16, 736–743.
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© 2003 Springer Science+Business Media Dordrecht
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Hwang, S.O., Chung, J.Y., Lee, G.M. (2003). Effect of Doxycycline-Regulated Chaperone Expression on Recombinant Protein Productivity in CHO Cells. In: Yagasaki, K., Miura, Y., Hatori, M., Nomura, Y. (eds) Animal Cell Technology: Basic & Applied Aspects. Animal Cell Technology: Basic & Applied Aspects, vol 13. Springer, Dordrecht. https://doi.org/10.1007/978-94-017-0726-8_26
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DOI: https://doi.org/10.1007/978-94-017-0726-8_26
Publisher Name: Springer, Dordrecht
Print ISBN: 978-90-481-6557-5
Online ISBN: 978-94-017-0726-8
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