Metabolic and proteomic study of NS0 myeloma cell line following the adaptation to protein-free medium

Journal of Proteomics

Volumn 71, Issue 2, 2008, Pages 133-147

  de la Luz Hernandez K R ^a,d   Rojas del Calvo, L ^a   Rabasa Legon Y ^a   Lage Castellanos, A ^b   Castillo Vitlloch, A ^a   Diaz J ^c   Gaskell, S ^d  

^a CENTER OF MOLECULAR IMMUNOLOGY   (Cuba)

^b CUBAN NEUROSCIENCE CENTER   (Cuba)

^c UNIVERSITY OF HAVANA   (Cuba)

^d UNIVERSITY OF MANCHESTER   (United Kingdom)

Author keywords

Metabolomics; Myeloma cell line; Protein free medium; Quantitative proteomics

Indexed keywords

ALBUMIN; CARBOHYDRATE; CHOLESTEROL; GLUCOSE; IMMUNOGLOBULIN G; INSULIN; LACTIC ACID; PEPTIDE; PHOSPHOLIPID; PHOSPHORUS; PROTEIN; TRIACYLGLYCEROL;

ADAPTATION; ANIMAL CELL; ARTICLE; CARBOHYDRATE METABOLISM; CELL CULTURE; CELL FRACTIONATION; CELL GROWTH; CELL VIABILITY; CULTURE MEDIUM; ELECTROSPRAY MASS SPECTROMETRY; LIQUID CHROMATOGRAPHY; MEMBRANE TRANSPORT; METABOLITE; METABOLOMICS; MOUSE; MYELOMA CELL; NONHUMAN; NUCLEOTIDE SEQUENCE; PEPTIDE ANALYSIS; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN SYNTHESIS; PROTEOMICS; SERUM; UNINDEXED SEQUENCE; WESTERN BLOTTING;

ADAPTATION, PHYSIOLOGICAL; ANIMALS; ANTIBODIES, MONOCLONAL; CELL CULTURE TECHNIQUES; CELL LINE, TUMOR; CULTURE MEDIA, SERUM-FREE; HUMANS; INSULIN; MICE; MULTIPLE MYELOMA; PROTEOME; PROTEOMICS; RECEPTOR, EPIDERMAL GROWTH FACTOR;

EID: 46249087893     PISSN: 18743919     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jprot.2008.02.003     Document Type: Article

References (31)

1. Barnes D., and Sato G. Methods for growth of cultured cells in serum-free medium. Anal Biochem 102 (1980) 255-270
2. Seamans T.C., Gould S.L., DiStefano D.J., Silberklang M., and Robinson D.K. Use of lipid emulsions as nutritional supplements in mammalian cell culture. Ann N Y Acad Sci 745 (1994) 240-243
3. Jenkins N., Castro P., Menon S., Ison A., and Bull A. Effect of lipid supplements on the production and glycosylation of recombinant interferon-g expressed in CHO cells. Cytotechnology 15 (1994) 209-215
4. Birch J.R., Boraston R.C., Metcalfe H., Brown M.E., Bebbington C.R., and Field R.P. Selecting and designing cell lines for improved physiological characteristics. Cytotechnology 15 (1994) 11-16
5. Sinacore M.S., Dropeau D., and Adamson S.R. Adaptation of mammalian cells to growth in serum-free media. Mol Biotechnol 15 (2000) 249-257
6. Spens E., and Haggstrom L. Defined protein-free NS0 myeloma cell cultures: stimulation of proliferation by conditioned medium factor. Biotechnol Prog 21 (2005) 87-95
7. DeSouza L., Diehl G., Rodríguez M.J., Guo J., Romaschin A.D., Colgan T.J., et al. Search for cancer markers from endometrial tissues using differentially labelled tags iTRAQ and cICAT with multidimensional liquid chromatography and tandem mass spectrometry. J Proteome Res 4 (2005) 377-386
8. De la Luz-Hernández K., Rojas-del Calvo L., Victores-Sarasola S., Lage-Castellanos A., Eyers C., Hart S., Castellanos-Serra L., Castillo-Vitlloch A., and Gaskell S. Proteomic analysis of the adaptation of the host NS0 myeloma cell line to protein-free medium. Biotecnología Aplicada 24 (2008) 3-4
9. Mateo C., Moreno E., Amour K., Lombardero J., Harris W., and Perez R. Humanization of a mouse monoclonal antibody that blocks the epidermal growth factor receptor: recovery of antagonistic activity. Immunotechnology 3 (1997) 71-81
10. Roque L., Mateo C., Lombardero J., Mustelier A., Fernández A., Sosa K., et al. Humanization of predicted T-cell epitopes reduces the immunogenecity of chimeric antibodies: new evidences supporting a simple method. Hybridoma 22 (2003) 245-257
11. Castillo A.J., Victores S., Rojas L., Faife E., Rabasa Y., Pence B.L., et al. Adaptation and selection of NS0 myeloma cell lines producing recombinant monoclonal antibodies in protein-free medium. In: Lindner-Osson E., et al. (Ed). Animal cell technology: from target to market (2001), Kluwer Academic Publishers 160-163
12. Tijssen P. Quantitative enzyme immunoassays techniques. Practice and theory of enzyme immunoassays vol. 15 (1993), Elservier Science Publishers BV, Amsterdam, Netherland 329-344
13. Castillo A.J., Victores S., Faife E., Rabasa Y., and de la Luz K.R. Development o fan integrated strategy for recombinant cell line selection. In: Godia F., and Fussenegger M. (Eds). Animal cell technology meets genomics (2005), Springer 505-508
14. Shadforth I.P., Dunkley T.P., Lilley K.S., and Bessant C. i-Tracker: for quantitative proteomics using iTRAQ. BMC Genomics 20 (2005) 145
15. Yang Y., Hoh J., Broger C., Neeb M., Edington J., Lindpaintner K., et al. Statistical methods for analyzing microarray feature data with replications. J Comput Biol 10 (2003) 157-169
16. Bairoch A., Boeckmann B., Ferro S., and Gasteiger E. Swiss-Prot: juggling between evolution and stability. Brief Bioinform 5 (2004) 39-55
17. Bairoch A., Apweiler R., Wu C.H., Barker W.C., Boekmann B., Ferro S., et al. The universal protein resource (UniProt). Nucleic Acid Res 33 (2005) D154-D159
18. Kanehisa M., and Goto S. KEGG: Kyoto encyclopedia of genes and genomes. Nucleic Acid Res 28 (2000) 27-30
19. Kanehisa M. The KEGG database. Novartis Foundation Symposium vol. 247 (2002) 91-101
20. Kanehisa M., Goto S., Hattori M., Aoki-Kinoshita K.F., Itho M., Kawashima G., et al. From genomics to chemical genomics: new developments in KEGG. Nucleic Acid Res 34 (2006) D354-D357
21. Hoffmann R., and Valencia A. A gene network for navigating the literature. Nat Genet 36 (2004) 664-670
22. Whitford W. NS0 serum-free culture and applications (December 2003), BioProcess International 36-47
23. Bebbington C.R., Renner G., Thompson S., King D., Abrams D., and Yarranton G.T. High level expression of a recombinant antibody from myeloma cells using a glutamine synthetase gene as an amplificable selectable marker. Bio/Technology 10 (1992) 169-175
24. Barnes L.M., Bentley C.M., and Dickson A.J. Advances in animal cell recombinant protein production: GS-NS0 expression system. Cytotechnology 32 (2000) 109-123
25. Gygi S.P., Rist B., Gerber S.A., Turecek F., Gelb M.H., and Aebersold R. Quantitative analysis of complex protein mixtures using isotope-coded affinity tags. Nat Biotechnol 17 (1999) 994-999
26. Everley P.A., Krijgsveld J., Zetter B.R., and Gygi S.P. Quantitative cancer proteomics: stable isotope labeling with amino acids in cell culture (SILAC) as a tool for prostate cancer research. Mol Cell Proteomics 3 (2004) 729-735
27. Jung Y.Y., Oh M.S., Shin D.W., Kang S.H., and Oh H.S. Identifying differentially expressed genes in meta-analysis via Bayesian model-based clustering. Biom J 48 (2006) 435-450
28. Seth G., Philp R.J., Denoya C.D., McGrath K., Stuzman-Engwall K.J., Yap M., et al. Large-scale gene expression analysis of cholesterol dependence in NS0 cells. Biotechnol Bioeng 90 (2005) 552-567
29. Lewandowska K., Skierski J., and Doroszewski J. Influence of serum protein and medium composition on the dynamic adhesiveness of lymphocytes and erythrocytes. Arch Immunol Ther Exp 24 (1976) 749-754
30. Ozturk S.S., and Palsson B.O. Growth, metabolic, and antibody production kinetics of hybridoma cell culture: 2. Effects of serum concentration, dissolved oxygen concentration, and medium pH in a batch reactor. Biotechnol Prog 7 (1991) 481-494
31. Low K., and Harbour C. Growth kinetics of hybridoma cells: (2) The effects of varying energy source concentrations. Dev Biol Stand 60 (1985) 73-79