PER.C6® Cells for the Manufacture of Biopharmaceutical Proteins

Modern Biopharmaceuticals: Design, Development and Optimization

Volumn 3, Issue , 2008, Pages 779-807

  Yallop, Chris ^a   Crowley, John ^b   Cote, Johanne ^b   Hegmans Brouwer, Kirsten ^a   Lagerwerf, Fija ^a   Gagne, Rodney ^b   Martin, Jose Coco ^b   Oosterhuis, Nico ^b   Opstelten, Dirk Jan ^a   Bout, Abraham ^a  

^a CRUCELL HOLLAND BV   (Netherlands)

^b DSM RESOLVE   (Netherlands)

Author keywords

Adenovirus; Glycan analyses; Glycosylation; Metabolic data; Pyroglutamate residue

Indexed keywords

EID: 84889953850     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1002/9783527620982.ch33     Document Type: Chapter

References (53)

1. Horwitz, M.S., Adenoviridae and their replication, in: B.N. Fields and D.M. Knipe (Eds) Virology, 1990, Raven Press, Ltd, New York, pp. 1679-1740.
2. Graham, F. L., J. Smiley, W.C. Russell, and R. Nairn, Characteristics of a human cell line transformed by DNA from adenovirus type 5. J. Gen. Virol., 1977, 36, 59-72.
3. Houweling, A., P. v. d. Elsen, and A. v. d. Eb, Partial transformation of primary rat cells by the left-most 4.5% of adenovirus 5 DNA. Virology, 1980, 105, 537-550.
4. Gallimore, P. H., R. J. A. Grand, and P. J. Byrd, Transformation of human embryo retinoblasts with simian virus 40, adenovirus and ras oncogenes. Anticancer Res., 1986, 6, 499-567.
5. Teodoro, J. and P. Branton, Regulation of apoptosis by viral gene products. J. Virol., 1997, 71, 1739-1746.
6. Sang, N., J. Caro, and A. Giordano, Adenoviral E1A: everlasting tool, versatile applications, continuous contributions and new hypotheses. Front. Biosci., 2002, 4, 407-413.
7. Zhang, Y. and Y. Xiong, Mutations in human ARF exon 2 disrupt its nucleolar localization and impair its ability to block nuclear export of MDM2 and p53. Mol. Cell, 1999, 3(5), 579-591.
8. Cuconati, A. and E. White, Viral homologues of BCL-2: role of apoptosis in the regulation of virus infection. Genes Dev., 2002, 16, 2465-2478.
9. Singer-Sam, J., D.H. Keith, K. Tani, R. L. Simmer, L. Shively, S. Lindsay, A. Yoshida, and A.D. Riggs, Sequence of the promoter region of the gene for X-linked 3-phosphoglycerate kinase. Gene, 1984, 32, 409-417.
10. Valerio, D., M.G. C. Duyvesteyn, B.M.M. Dekker, G. Weeda, T.M. Bervens, L. v. d. Voorn, H.v. Ormondt, and A. J. v. d. Eb, Adenosine deaminase: characterization and expression of a gene with a remarkable promoter. EMBO J., 1985, 4, 437-443.
11. Simonsen, C. and A. Levinson, Analysis of processing and polyadenylation signals of the hepatitis B Virus surface antigen gene by using simian virus 40-Hepatitis B Virus chimeric plasmids. Mol. Cell Biol., 1983, 3, 2250-2258.
12. Vaessen, R.T.M.J., A. Houweling, A. Israel, P. Kourilsky, and A. J. v. d. Eb, Adenovirus E1A-mediated regulation of class I MHC expression. EMBO J., 1986, 5, 335-341.
13. Fallaux, F. J., O. Kranenburg, S. J. Cramer, A. Houweling, H. v. Ormondt, R. C. Hoeben, and A. J. v. d. Eb, Characterization of 911: a new helper cell line for the titration and propagation of early-region-1-deleted adenoviral vectors. Hum. Gene Ther., 1996, 7, 215-222.
14. Byrd, P., K. Brown, and P. Gallimore, Malignant transformation of human embryo retinoblasts by cloned adenovirus 12 DNA. Nature, 1982, 298, 69-71.
15. Fallaux, F. J., A. Bout, I. v. d. Velde, D.J.M.v. d. Wollenberg, K. Hehir, J. Keegan, C. Auger, S. J. Cramer, H. v. Ormondt, A. J. v. d. Eb, D. Valerio, and R. C. Hoeben, New helper cells and matched early region 1-deleted adenovirus vectors prevent generation of replication-competent adenoviruses. Hum. Gene Ther., 1998, 9, 1909-1917.
16. Nichols, W.W., R. Lardenoie, B. J. Ledwith, K. Brouwer, S. Manam, R. Vogels, D. Kaslow, D. Zuidgeest, A. J. Bett, J. Chen, M. Van der Kaaden, S.M. Galloway, R.B. Hill, S.V. Machotka, C. A. Anderson, J. B. Lewis, D. Martinez, J. Lebron, C. Russo, D. Valerio, and A. Bout, Propagation of adenoviral vectors: use of PER.C6 cells, in: D.T. Curiel and J.T. Douglas (Eds) Adenoviral vectors for gene therapy, 2002, Elsevier: San Diego, pp. 129-167.
17. Paterson, T., J. Innes, L. McMillan, I. Downing, and M.C. Carter, Variation in IgG1 heavy chain allotype does not contribute to differences in biological activity of two human anti-Rhesus (D) monoclonal antibodies. Immunotechnology, 1998, 4, 37-47.
18. Ljunggren, J. and L. Haggstrom, Glutamine limited fed-batch culture reduces the overflow metabolism of amino acids in myeloma cells. Cytotechnology, 1992, 8, 45-56.
19. Ljunggren, J. and L. Haggstrom, Catabolic control of hybridoma cells by glucose and glutamine limited fed-batch cultures. Biotechnol. Bioeng., 1994, 44, 808-818.
20. Xie, L. Z. and D.I. C. Wang, Fed-batch cultivation of animal cells using different medium design concepts and feeding strategies. Biotechnol. Bioeng., 1994, 43, 1175-1189.
21. Xie, L. Z. and D.I. C. Wang, Stoichiometric analysis of animal cell growth and its application in medium design. Biotechnol. Bioeng., 1994, 43, 1164-1174.
22. Sanfeliu, A., C. Paredes, J. J. Cairo, and F. Godia, Identification of key patterns in the metabolism of hybridoma cells in culture. Enzyme Microb. Technol., 1997, 21, 421-428.
23. Zhou, W. C., C. C. Chen, B. Buckland, and J. Aunins, Fed-batch culture of recombinant NS0 myeloma cells with high monoclonal antibody production. Biotechnol. Bioeng., 1997, 55, 783-792.
24. Zhou, W. C., J. Rehm, A. Europa, and W. S. Hu, Alteration of mammalian metabolism by dynamic nutrient feeding. Cytotechnology, 1997, 24, 99-108.
25. Europa, A. F., A. Gambhir, P.C. Fu, and W. S. Hu, Multiple steady states with distinct cellular metabolism in continuous culture of mammalian cells. Biotechnol. Bioeng., 2000, 67, 25-34.
26. Mercille, S., M. Johnson, S. Lanthier, A.A. Kamen, and B. Massie, Understanding factors that limit the productivity of suspension based perfusion cultures operated at high medium renewal rates. Biotechnol. Bioeng., 2000, 67(4), 435-447.
27. Banik, G.G. and C. A. Heath, An investigation of cell density effects on hybridoma metabolism in a homogeneous reactor. BioProcess Eng., 1994, 11, 229-237.
28. Brosie, D. d. l., M. Nosieux, R. Lemieux, and B. Massie, Long-term perfusion culture of hybridoma: a 'grow or die' cell cycle system. Biotechnol. Bioeng., 1991, 38, 781-787.
29. Richieri, R. A., L. S. Williams, and P. C. Chou, Cell cycle dependency of monoclonal antibody production in asynchronous serum-free hybridoma cultures. Cytotechnology, 1991, 5, 972-976.
30. Schenerman, M.A., B. R. Sunday, S. Kozlowski, K. Webber, H. Gazzano-Santoro, and A. Mire-Sluis, CMC Strategy Forum Report: Analysis and structure characterization of monoclonal antibodies. BioProcess Int., 2004, February, 42-52.
31. International Conference on Harmonisation Guidance on Specifications: Test procedures and acceptance criteria for biotechnological/biological products. Fed. Reg., 1996, 64, 2733.
32. Krips, D.M., R. O. Sitrin, and C.N. Oliver, A very rapid 2 min protein A HPLC assay for monoclonal antibodies. FASEB J., 1991, 5, A465.
33. Brown, M.A., L.M. Stenberg, U. Persson, and J. Stenflo, Identification and purification of vitamin K-dependent proteins and peptides with monoclonal antibodies specific for gamma-carboxyglutamyl (Gla) residues. J. Biol. Chem., 2000, 275, 19795-19802.
34. Jones, D., N. Kroos, R. Anema, B. van Montfort, A. Vooys, S. van der Kraats, E. van der Helm, S. Smits, J. Schouten, K. Bouwer, F. Lagerwerf, P. van Berkel, D.-J. Opstelten, T. Logtenberg, and B. Bout, High-level expression of recombinant IgG in the human cell line PER.C6. Biotechnol. Prog., 2003, 19, 163-168.
35. Biedermann, K., Sabater, M., Sorensen, J., Fiedler, H., and Emborg, C, Quantitative binding studies of a monoclonal antibody to immobilized protein-A. Bioseparation, 1991, 2, 309-314.
36. Shapiro, A., E. Vinuela, and J. Maizel, Molecular weight estimation of polypeptide chains by electrophoresis in SDS polyacrylamide gels. Biochem. Biophys. Res. Commun., 1967, 28, 815.
37. Righetti, P. G., Isoelectric Focussing: theory, methodology and applications. 1983, Elsevier Biomedical Press, Amsterdam.
38. Harris, R. J., B. Kabakoff, F. D. Macchi, F. J. Shen, M. Kwong, J. D. Andya, S. J. Shire, N. Bjork, K. Totpal, and A.B. Chen, Identification of multiple sources of charge heterogeneity in a recombinant antibody. J. Chromatogr. B, 2001, 752, 233-245.
39. Perkins, M., R. Theiler, S. Lunte, and M. Jeschke, Determination of the origin of charge heterogeneity in a murine monoclonal antibody. Pharm. Res., 2000, 17, 1110-1117.
40. Wehr, T., R. Rodriguez-Diaz, and M. Zhu, Recent advances in capillary isoelectric focussing. Chromatographia Suppl., 2001, 53, S47-S58.
41. Jenkins, N., R. B. Parekh, and D.C. James, Getting the glycosylation right: Implications for the biotechnology industry. Nature Biotechnol., 1996, 14, 975-981.
42. Cumming, D.A., Glycosylation of recombinant protein therapeutics: Control and functional implications. Glycobiology, 1991, 1, 115-130.
43. Wright, A. and S. Morrison, Effect of glycosylation on antibody function: implications for genetic engineering. Trends Biotechnol., 1997, 15, 26-32.
44. Jefferis, R., Glycosylation of Human IgG antibodies: Relevance to therapeutic applications. BioPharmacology, 2001, September, 19-27.
45. Raju, T. S., Glycosylation variations with expression systems and their impact on biological activity of therapeutic immunoglobulins. Bio Process Int., 2003, April, 44-53.
46. Raju, T. S., J. B. Briggs, S.M. Borge, and A. J. S. Jones, Species-specific variation in glycosylation of IgG: Evidence for the speciesspecific sialylation and branch-specific galactosylation and importance for engineering recombinant glycoprotein therapeutics. Glycobiology, 2000, 10, 477-486.
47. Hills, A. E., A. K. Patel, P. N. Boyd, and D.C. James, Control of therapeutic antibody glycosylation, in: A. Bernard, et al. (Ed) Animal Cell Technology: Products from cells, cells as products, 1999, Kluwer Academic Press, Dordrecht, The Netherlands, pp. 255-257.
48. Borys, M.C., D.H. Linzer, and E.T. Papoutsakis, Ammonia affects the glycosylation patterns of recombinant mouse placental lactogen-I by Chinese hamster ovary cells in pH dependent manner. Biotechnol. Bioeng., 1994, 43, 505-514.
49. Andersen, D.C. and C. Goochee, The effect of ammonia on the O-linked glycosylation of granulocyte colony stimulating factor by Chinese hamster ovary cells. Biotechnol. Bioeng., 1995, 47, 96-105.
50. Gawlitzek, M., U. Valley, and R. Wagner, Ammonium ion and glucosamine dependent increases of oligosaccharide complexity in recombinant glycoproteins secreted from cultivated BHK-21 cells. Biotechnol. Bioeng., 1998, 57, 518-528.
51. Hills, A. E., A. Patel, P. Boyd, and D.C. James, Metabolic control of recombinant monoclonal antibody N-glycosylation in GS-NS0 cells. Biotechnol. Bioeng., 2001, 75, 239-251.
52. Bongers, J., J. J. Cummings, M.B. Ebert, M.M. Federici, L. Gledhill, D. Gulati, G.M. Hilliard, B.H. Jones, K. R. Lee, J. Modzanowski, M. Naimoli, and S. Burman, Validation of a peptide mapping method for a therapeutic antibody: what could we possibly learn about a method we have run 100 times? J. Pharm. Biomed. Anal., 2000, 21, 1099-1128.
53. Harris, R. J., Processing of C-terminal lysine and arginine residues of proteins isolated from mammalian cell culture. J. Chromatogr. A., 1995, 705, 129-134.