Abstract
In today’s world, mammalian cell cultures are used to understand various physiological and pathophysiological cell signaling events related to normal as well as various diseased cells such as cancer cells and others. Besides, mammalian cells such as Chinese hamster ovary (CHO) cells, baby hamster kidney (BHK) cells, human embryonic kidney (HEK) cells, African green monkey kidney (COS) cells, NSO cells, HT1080 cell, and PER-C6 cells (many others too) as well as their culture products (various recombinant proteins) have widespread use in biotechnology, pharmacology, and medicine. The major usefulness of cultured mammalian cells and their products described in this chapter include (i) use as a model system for physiological and pathophysiological studies; (ii) use in experimental drug/toxin research; (iii) use in vaccine production, particularly against pathogenic viruses; (iv) use for various recombinant protein production; (v) in cell therapy; and finally (vi) in gene therapy. The various mammalian cell culture recombinant DNA products described in this chapter are tissue plasminogen activator, urokinase, follicle-stimulating hormone, blood clotting factor VIII, and erythropoietin. All these recombinant proteins exhibit widespread significance in the medical field. In comparison, cell and gene therapy are new fields and their success against various human diseases is substantially in the initial stages.
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References
Almo SC, Love JD. Better and faster: improvements and optimization for mammalian recombinant protein production. Curr Opin Struct Biol. 2014;26:39–43.
Andersen DC, Reilly DE. Production technologies for monoclonal antibodies and their fragments. Curr Opin Biotechnol. 2004;15:456–62.
Andersson LO, Forsman N, Huang K, et al. Isolation and characterization of human factor VIII: molecular forms in commercial factor VIII concentrate, cryopricitate, and plasma. PNAS USA. 1986;83:2979–83.
Aricescu AR, Lu W, Jones EY. A time and cost-efficient system for high-level protein production in mammalian cells. Acta Crystallogr D Biol Crystallogr. 2006;62:1243–50.
Barlow GH. Urinary and kidney cell plasminogen activator (urokinase). Methods in Enzymol. 1976;45:239–44.
Bernik MB, Kwaan HC. Plasminogen activator activity in cultures from human tissues. An immunological and histochemical study. J Clin Invest. 1969;48:1740–53.
Browne SM, Al-Rubeai M. Selection methods for high-producing mammalian cell lines. Trends Biotechnol. 2007;25:425–32.
Campos-da-Paz M, Costa CS, Quilici LS, Simoes IDC, Kyaw CM, Maranhao AQ, et al. Production of recombinant human factor VIII in different cell lines and the effect of human XBP1 co-expression. Mol Biotechnol. 2008;39:155–8.
Colosimo A, Goncz KK, Holmes AR, Kunzelmann K, Novelli G, Malone RW, et al. Transfer and expression of foreign genes in mammalian cells. Bio Techniques. 2000;20:314–31.
Dalton AC, Barton WA. Over-expression of secreted proteins from mammalian cell lines. Protein Sci. 2014;23:517–25.
Davis JM, Arakawa T. Characterization of recombinant human erythropoietin produced in Chinese hamster ovary cells. Biochemistry. 1987;26:2633–8.
Egrie J. The cloning and production of recombinant human erythropoietin. Pharmacotherapy. 1990;10:3S–8S.
Ekwall B. Screening of toxic compounds in tissue culture. Toxicology. 1980;17:127–42.
Ekwall B. Screening of toxic compounds in mammalian cell cultures. Ann N Y Acad Sci. 1983;407:64–77.
Fantacini DMC, Picanço-Castro V. Production of recombinant factor VIII in human cell lines. Methods Mol Biol. 2018;1674:63–74.
Fischbach MA, Bluestone JA, Lim WA. Cell-based therapeutics: the next pillar of medicine. Sci Transl Med. 2013;5:179ps7.
Geisse S, Henke M. Large-scale transient transfection of mammalian cells: a newly emerging attractive option for recombinant protein production. J Struct Funct Genom. 2005;6:165–70.
Gitschier J, Wood WI, Goralka TM, Wion KL, Chen EY, Eaton DH, et al. Characterization of the human factor VIII gene. Nature. 1984;312:326–30.
Gray D. Overview of protein expression by mammalian cells. Curr Protoc Protein Sci. 1997;10:5.9.1–5.9.18.
Griffiths JB, Electricwala A. Production of tissue plasminogen activators from animal cells. Vertebrate Cell Culture. 2005;I:147–66.
Hakola K, Van der Boogaart P, Mulders J, de Leeuw R, Schoonen W, Heyst JV, et al. Recombinant rat follicle-stimulating hormone; production by Chinese hamster ovary cells, purification and functional characterization. Mol Cell Endocrinol. 1997;127:59–69.
Howles CM. Genetic engineering of human FSH (gonal-F). Hum Reprod Update. 1996;2:172–91.
Huang TK, McDonald KA. Bioreactor engineering for recombinant protein production in plant cell suspension cultures. Biochem Eng J. 2009;45:168–84.
Hunter M, Yuan P, Vavilala D, Fox M. Optimization of protein expression in mammalian cells. Current Prot in Protein Sci. 2019;95:e77.
Jones AJ, Garnick RL. Quality control of rDNA-derived human tissue-type plasminogen activator. Bioprocess Technol. 1990;10:543–66.
Khan KH. Gene expression in mammalian cells and its applications. Adv Pharm Bull. 2013;3:257–63.
Kost TA, Condreay JP. Recombinant baculoviruses as mammalian cell gene-delivery vectors. Trends Biotechnol. 2002;20:173–80.
Lai T, Yang Y, Ng SK. Advances in mammalian cell line development technologies for recombinant protein production. Pharmaceuticals (Basel). 2013;6:579–603.
Li F, Vijayasankaran N, Shen A, Kiss R, Amanullah A. Cell culture processes for monoclonal antibody production. MAbs. 2010;2:466–77.
Liu C, Dalby B, Chen W, Kilzer JM, Chiou HC. Transient transfection factors for high-level recombinant protein production in suspension cultured mammalian cells. Mol Biotechnol. 2008;39:141–53.
Masters JRW. Human cancer cell lines: fact and fantasy. Nat Rev Mol Cell Biol. 2000;1:233–6.
Mills M, Estes MK. Physiologically relevant human tissue models for infectious diseases. Drug Discov Today. 2016;21:1540–52.
Mirabelli P, Coppola L, Salvatore M. Cancer cell lines are useful model systems for medical research. Cancers (Basel). 2019;11:1098.
Montagnon BJ, Fanget B, Nicolas AJ. The large-scale cultivation of Vero cells in microcarrier-culture for virus-vaccine production: preliminary results for killed poliovirus-vaccine. Dev Biol Stand. 1981;47:55–64.
Omasa T. Gene amplification and its application in cell and tissue engineering. J Biosci Bioeng. 2002;94:600–5.
Paganuzzi-Stammati A, Silano V, Zucco F. Toxicology investigations with cell culture systems. Toxicology. 1981;20:91–153.
Plotkin SA, Eagle H, Hayflick L, Ikic D, Koprowski H, Perkins F. Serially cultured animal cells for preparation of viral vaccines. Science. 1969;165:1278–82.
Rijken DC, Collen D. Purification and characterization of the plasminogen activator secreted by human melanoma cells in culture. J Biol Chem. 1981;256:7035–41.
Sambrook, Fritsch, Maniatis. Molecular cloning: a laboratory manual. 2nd ed. New York: Cold Spring Harbor Laboratory Press, Cold Spring Harbor; 1989;3:Apendix B.12
Schimke RT. Gene amplification in cultured animal cells. Cell. 1984;37:705–13.
Sissolak B, Kandra K, Stosch MV, Mayer M, Striedner G. Quality by control: towards model predictive control of mammalian cell culture bioprocesses. Biotechnol. 2017;12. Special Issue: Biochemical Engineering Science
Takeuchi M, Inoue N, Strickland TW, Kubota M, Wada M, Shimizu R, et al. Relationship between sugar chain structure and biological activity of recombinant human erythropoietin produced in Chinese hamster ovary cells. Proc Nati Acad Sci USA. 1989;86:7819–22.
Trill JJ, Shatzman AR, Ganguly S. Production of monoclonal antibodies in COS and CHO cells. Curr Opin Biotechnol. 1995;6:553–60.
Walter JK, Werz W, Berthold W. Virus removal and inactivation. Concept and data for process validation of downstream processing. Biotech Forum Europe. 1992;9:560–4.
Werz W, Hoffmann H, Haberer K, Walter JK. Strategies to avoid virus transmissions by biopharmaceutic products. Arch Virol Suppl. 1997;13:245–56.
White WF, Barlow GH, Mozen MM. The isolation and characterization of plasminogen activators (urokinase) from human urine. Biochemist. 1966;5:2160–9.
Wu SC, Huang GYL, Liu JH. Production of retrovirus and adenovirus vectors for gene therapy: a comparative study using microcarrier and stationary cell culture. Biotechnol Prog. 2002;18:617–22.
Wurm FM. Production of recombinant protein therapeutics in cultivated mammalian cells. Nat Biotechnol. 2004;22:1393–8.
Yarranton GT. Mammalian recombinant proteins: vectors and expression systems. Curr Opin Biotechnol. 1990;1:133–40.
Zeyda M, Borth N, Kunert R, Katinger H. Optimization of sorting conditions for the selection of stable, high-producing mammalian cell lines. Biotechnol Prog. 1999;15:953–7.
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Mukherjee, S., Malik, P., Mukherjee, T.K. (2023). Mammalian Cells, Tissues and Organ Culture: Applications. In: Mukherjee, T.K., Malik, P., Mukhopadhyay, S. (eds) Practical Approach to Mammalian Cell and Organ Culture. Springer, Singapore. https://doi.org/10.1007/978-981-19-1731-8_17-1
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DOI: https://doi.org/10.1007/978-981-19-1731-8_17-1
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Mammalian Cells, Tissues and Organ Culture: Applications- Published:
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Mammalian Cells, Tissues and Organ Culture: Applications- Published:
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DOI: https://doi.org/10.1007/978-981-19-1731-8_17-1