Proteomic profiling of CHO cells with enhanced rhBMP-2 productivity following co-expression of PACEsol

Proteomics

Volumn 8, Issue 13, 2008, Pages 2611-2624

  Meleady, Paula ^a   Henry, Michael ^a   Gammell, Patrick ^a,b   Doolan, Padraig ^a   Sinacore, Martin ^b   Melville, Mark ^b   Francullo, Linda ^b   Leonard, Mark ^b   Charlebois, Timothy ^b   Clynes, Martin ^a  

^a DUBLIN CITY UNIVERSITY   (Ireland)

^b PFIZER INC   (United States)

Author keywords

2 D DIGE; Bone morphogenetic protein; Chinese hamster ovary; High productivity; Paired basic amino acid cleaving enzyme

Indexed keywords

CHAPERONE; DIMER; ISOENZYME; PAIRED BASIC AMINO ACID CLEAVING ENZYME SOLUBLE PAIRED BASIC AMINO ACID CLEAVING ENZYME; RECOMBINANT BONE MORPHOGENETIC PROTEIN 2;

ANIMAL CELL; ARTICLE; CELL FUNCTION; CHO CELL; DOWN REGULATION; FEMALE; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN MODIFICATION; PROTEIN SECRETION; PROTEIN VARIANT; PROTEOMICS; UPREGULATION;

ANIMALS; BONE MORPHOGENETIC PROTEINS; CELL CULTURE TECHNIQUES; CELL LINE; CHO CELLS; CLONE CELLS; CRICETINAE; CRICETULUS; DIMERIZATION; ELECTROPHORESIS, GEL, TWO-DIMENSIONAL; FURIN; GENE EXPRESSION; GENE EXPRESSION PROFILING; HUMANS; PEPTIDE MAPPING; PROTEOME; PROTEOMICS; RECOMBINANT PROTEINS; SPECTROMETRY, MASS, MATRIX-ASSISTED LASER DESORPTION-IONIZATION; TRANSFECTION; TRANSFORMING GROWTH FACTOR BETA;

CRICETULUS GRISEUS;

EID: 47249159066     PISSN: 16159853     EISSN: 16159861     Source Type: Journal    
DOI: 10.1002/pmic.200700854     Document Type: Article

References (53)

1. Chu, L., Robinson, D. K., Industrial choices for protein production by large scale cell culture. Curr. Opin. Biotechnol. 2001, 12, 180-187.
2. Smales, C. M., Dinnis, D. M., Stansfield, S. H., Alete, D. et al., Comparative proteomic analysis of GS-NSO murine myeloma cells lines with varying recombinant monoclonal antibody production rate. Biotechnol. Bioeng. 2004, 88, 474-488.
3. Baik, J. Y., Lee, M. S., An, S. R., Yoon, S. K. et al., Initial transcriptome and proteome analyses of low culture temperature-induced expression in CHO cells producing erythropoietin. Biotechnol. Bioeng. 2006, 93, 361-371.
4. Seth, G., Philp, R. J., Lau, A., Jiun, K. Y. et al., Molecular portrait of high productivity in recombinant NSO cells. Biotechnol. Bioeng. 2007, 97, 933-951.
5. Nissom, P. M., Sanny, A., Kok, Y. J., Hiang, Y. T. et al., Transcriptome and proteome profiling to understanding the biology of high productivity CHO cells. Mol. Biotechnol. 2006, 34, 125-140.
6. Wong, D. C. F., Wong, K. T. K., Lee, Y. Y., Morin, P. N. et al., Transcriptional profiling of apoptotic pathways in batch and fed-batch CHO cell cultures. Biotechnol. Bioeng. 2006, 94, 373-382.
7. Wang, E. A., Rosen, V., D'Alessandro, J. S., Bauduy, M. et al., Recombinant human bone morphogenetic protein induces bone formation. Proc. Natl. Acad. Sci.USA 1990, 87, 2220-2224.
8. Wozney, J. M., Rosen, V., Bone morphogenetic protein and bone morphogenetic protein gene family in bone formation and repair. Clin. Orthop. 1998, 346, 26-37.
9. Israel, D. I., Nove, J., Kerns, K. M., Moutsatsos, I. K., Kaufman, R. J., Expression and characterisation of bone morphogenetic protein-2 in Chinese Hamster Ovary cells. Growth Factors 1992, 7, 139-150.
10. Ayoubi, T. A. Y., Meulemans, S. M., Roebroek, A. J., Van de Ven, W. J., Production of recombinant proteins in Chinese hamster ovary cells overexpressing subtilisin-like proprotein converting enzyme furin. Mol. Biol. Rep. 1996, 23, 87-95.
11. Roe, S., Francullo, L. E., Paradis, T. M., Porter, T. J. et al., Effects of posttranslational processing on rhBMP-2 cellular productivity and product quality. Bioprocess Int. 2004, 2, 32-43.
12. Wasley, L. C., Rehemtulla, A., Bristol, J. A., Kaufman, R. J., PACE/Furin can process the vitamin K-dependent profactor IX precursor within the secretory pathway. J. Biol. Chem. 1993, 268, 8458-8465.
13. Wong, M. J., Goldberger, G., Isenman, D. E., Minta, J. O., Processing of human factor I in cos-1 cells co-transfected with factor I and paired basic amino acid cleaving enzyme (PACE) cDNA. Mol. Immunol. 1995, 32, 379-387.
14. Robertson, B. J., Moehring, J. M., Moehring, T. J., Defective processing of the insulin receptor in an endoprotease-deficient Chinese hamster cell strain is corrected by expression of mouse furin. J. Biol. Chem. 1993, 268, 24274-24277.
15. Wise, R. J., Barr, P. J., Wong, P. A., Kiefer, M. C. et al., Expression of a human proprotein processing enzyme: Correct cleavage of the von Willebrand factor precursor at a paired basic amino acid. Proc. Natl. Acad. Sci. USA 1990, 87, 9378-9382.
16. Preininger, A., Schlokat, U., Mohr, G., Himmelspach, M. et al., Strategies for recombinant furin employment in a biotechnological process: Complete target protein precursor cleavage. Cytotechnology 1999, 30, 1-15.
17. Alban, A., David, S. O., Bjorkesten, L., Andersson, C. et al., A novel experimental design for comparative two-dimensional analysis: Two-dimensional difference gel electrophoresis incorporating a pooled internal standard. Proteomics 2003, 3, 36-44.
18. Duckert, P., Brunak, S., Blom, N., Prediction of proprotein convertase cleavage sites. Protein Eng., Des. Select. 2004, 1, 107-112.
19. Doolan, P., Melville, M., Gammell, P., Sinacore, M. et al., Transcriptional profiling of gene expression changes in a PACE-transfected CHO D UKX cell line secreting high levels of rhBMP-2. Mol. Biotechnol. 2008, DOI 10.1007/s12033-008-9039-6, Epub ahead of print.
20. Freiden, P. J., Gaut, J. R., Hendershot, L. M., Interconversion of three differentially modified and assembled forms of BiP. Embo J. 1992, 11, 63-70.
21. Peneff, C., Ferrari, P., Charrier, V., Taburet, Y. et al., Crystal structures of two human pyrophosphorylase isoforms in complexes with UDPGlc(Gal)NAc: Role of the alternatively spliced insert in the enzyme oligomeric assembly and active site architecture. EMBO J. 2001, 20, 6191-6202.
22. Lu, Y., Hu, Q., Yang, C., Gao, F., Histidine 89 is an essential residue for Hsp70 in the phosphate transfer reaction. Cell Stress Chaperones 2006, 11, 148-153.
23. Bassi, D. E., Fu, J., Lopez de Cicco, R., Klein-Szanto, A. J., Proprotein convertases: "Master switches" in the regulation of tumour growth and progression. Mol. Carcinog. 2005, 44, 151-161.
24. Wick, W., Naumann, U., Weller, M., Transforming growth factor-b: A molecular target for the future therapy of glioblastoma. Curr. Pharm. Des. 2006, 12, 341-349.
25. McMahon, S., Grondin, F., McDonald, P. P., Richard, D. E., Dubois, C. M., Hypoxia-enhanced expression of the proprotein convertase furin is mediated by hypoxia-inducible factor-1. J. Biol. Chem. 2005, 280, 6561-6569.
26. Kleizen, B., Braakman, I., Protein folding and quality control in the endoplasmic reticulum. Curr. Opin. Cell. Biol. 2004, 16, 343-349.
27. Schroder, M., Kaufman, R. J., The mammalian unfolded protein response. Annu. Rev. Biochem. 2005, 74, 739-789.
28. Mosser, D. D., Caron, A. W., Bourget, L., Meriin, A. B. et al., The chaperone function of hsp70 is required for protection against stress-induced apoptosis. Mol. Cell. Biol. 2000, 20, 7146-7159.
29. Garrido, C., Brunet, M., Didelot, C., Zermati, Y. et al., Heat shock proteins 27 and 70: Anti-apoptotic proteins with tumorigenic properties. Cell Cycle 2006, 5, 2592-2601.
30. Kozutsumi, Y., Segal, M., Normington, K., Gething, M. J., Sambrook, J., The presence of malfolded proteins in the endoplasmic reticulum signals the induction of glucose-regulated proteins. Nature 1988, 332, 462-464.
31. Hsu, T. A., Betenbaugh, M. J., Coexpression of molecular chaperone BiP improves immunoglobulin solubility and IgG secretion from Trichoplusia ni insect cells. Biotechnol. Prog. 1997, 13, 96-104.
32. Dorner, A. J., Wasley, L. C., Kaufman, R. J., Overexpression of GRP78 mitigates stress induction of glucose regulated proteins and blocks secretion of selective proteins in Chinese hamster ovary cells. EMBO J. 1992, 11, 1563-1571.
33. Dorner, A. J., Krane, M. G., Kaufman, R. J., Reduction of endogenous GRP78 levels improves secretion of heterologous protein in CHO cells. Mol. Cell. Biol. 1988, 8, 4063-4070.
34. Van Dyk, D. D., Misztal, D. R., Wilkins, M. R., Mackintosh, J. A. et al., Identification of cellular changes associated with increased production of human growth hormone in a recombinant Chinese hamster ovary cell line. Proteomics 2003, 3, 147-156.
35. Alete, D. E., Racher, A. J., Birch, J. R., Stansfield, S. H. et al., Proteomic analysis of enriched microsomal fractions from GS-NS0 murine myeloma cells with varying secreted recombinant monoclonal antibody productivities. Proteomics 2005, 5, 4689-4704.
36. Ostermeier, M., De Sutter, K., Georgiou, G., Eukaryotic protein disulphide isomerase complements Escherichia coli dsbA mutants and increases the yield of heterologous secreted protein with disulphide bonds. J. Biol. Chem. 1996, 271, 10616-10622.
37. Robinson, A. S., Hines, V., Wittrup, K. D., Protein disulphide isomerase overexpression increases secretion of foreign proteins in Saccharomyces cerevisiae. Biotechnology 1994, 12, 381-384.
38. Arrigo, A. P., The cellular "networking" of mammalian Hsp27 and its functions in the control of protein folding, redox state and apoptosis. Adv. Exp. Med. Biol. 2007, 594, 14-26.
39. Dunn, A. Y., Melville, M. W., Frydman, J., Review: Cellular substrates of the eukaryotic chaperonin TRiC/CCT. J. Struct. Biol. 2001, 135, 176-184.
40. Valpuesta, J. M., Martin-Benito, J., Gomez-Puertas, P., Carrascosa, J. L., Willison, K. R., Structure and function of a protein folding machine: The eukaryotic cytosolic chaperonin CCT. FEBS Lett. 2002, 529, 11-16.
41. McCallum, C. D., Do, H., Johnson, A. E., Frydman, J., The interaction of the chaperonin tailless complex polypeptide 1 (TCP1) ring complex (TRiC) with ribosome-bound nascent chains examined during photo-crosslinking. J. Cell. Biol. 2000, 149, 591-602.
42. Hinnebusch, A. G., elF3: A versatile scaffold for translation initiation complexes. Trends Biochem. Sci. 2006, 31, 553-562.
43. Le Sourd, F., Boulben, S., Le Bouffant, R., Cormier, P. et al., elF1B: At the dawn of the 21st century. Biochim. Biophys. Acta 2006, 1759, 13-31.
44. Sanders, J., Raggiaschi, R., Morales, J., Moller, W., The human leucine zipper-containing guanine-nucleotide exchange protein elongation factor-1 delta. Biochim. Biophys. Acta 1993, 1174, 87-90.
45. Petrushenko, Z. M., Budkevich, T. V., Shalak, V. F., Negrutskii, B. S., El'skaya, A. V., Novel complexes of mammalian cell translation elongation factor eEF1A.GDP with uncharged tRNA and aminoacyl-tRNA synthetase. Implications for tRNA channelling. Eur. J. Biochem. 2002, 269, 4811-4818.
46. Dinnis, D. M., Stansfield, S. H., Schlatter, S., Smales, C. M. et al., Functional proteomic analysis of GS-NS0 murine myeloma cell lines with varying recombinant monoclonal antibody production rate. Biotech. Bioeng. 2006, 94, 830-841.
47. Seow, T. K., Korke, R., Liang, R. C. M. Y., Ong, S. E. et al., Proteomic investigation of metabolic shift in mammalian cell culture. Biotechnol. Prog. 2001, 17, 1137-1144.
48. Tang, D. D., Bai, Y., Gunst, S. J., Silencing of p21-activated kinase attenuates vimentin phosphorylation on Ser-56 and reorientation of the vimentin network during stimulation of smooth muscle cells by 5-hydroxytryptamine. Biochem. J. 2005, 388, 773-783.
49. Eriksson, J. E., He, T., Trejo-Skalli, A. V., Harmala-Brasken, A. S. et al., Specific in vivo phosphorylation sites determines the assembly dynamics of vimentin intermediate filaments. J. Cell. Sci. 2004, 117, 919-932.
50. Stapulionis, R., Kolli, S., Deutscher, M. P., Efficient mammalian protein synthesis requires an intact F-actin system. J. Biol. Chem. 1997, 272, 24980-24986.
51. Ohuchida, K., Mizumoto, K., Ohhashi, S., Yamaguchi, H. et al., S100A11, a putative tumour suppressor gene, is overexpressed in pancreatic carcinogenesis. Clin. Cancer Res. 2006, 12, 5417-5422.
52. Padmanabhan, V., Callas, P., Philips, G., Trainer, T. D., Beatty, B. G., DNA replication regulation protein Mcm7 as a marker of proliferation in prostate cancer. J. Clin. Pathol. 2004, 57, 1057-1062.
53. Pancholi, V., Multifunctional alpha-enolase: Its role in disease. Cell Mol. Life Sci. 2001, 58, 902-920.