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Volumn 91, Issue 6, 2005, Pages 722-732

Optimization of tetracycline-responsive recombinant protein production and effect on cell growth and ER stress in mammalian cells

Author keywords

BiP; Cell culture; ER stress; Optimization; Tetracycline; Transferrin; Unfolded protein response

Indexed keywords

CELL CULTURE; CELLS; CONCENTRATION (PROCESS); GENES; OPTIMIZATION;

EID: 24644516989     PISSN: 00063592     EISSN: None     Source Type: Journal    
DOI: 10.1002/bit.20566     Document Type: Article
Times cited : (34)

References (36)
  • 1
    • 0033902975 scopus 로고    scopus 로고
    • N-glycan patterns of human transferrin produced in Trichoplusia ni insect cells: Effects of mammalian galactosyltransferase
    • Ailor E, Takahashi N, Tsukamoto Y, Masuda K, Rahman BA, Jarvis DL, Lee YC, Betenbaugh MJ. 2000. N-glycan patterns of human transferrin produced in Trichoplusia ni insect cells: Effects of mammalian galactosyltransferase. Glycobiology 10(8):837-847.
    • (2000) Glycobiology , vol.10 , Issue.8 , pp. 837-847
    • Ailor, E.1    Takahashi, N.2    Tsukamoto, Y.3    Masuda, K.4    Rahman, B.A.5    Jarvis, D.L.6    Lee, Y.C.7    Betenbaugh, M.J.8
  • 2
    • 0031892632 scopus 로고    scopus 로고
    • Transcriptional modulation of foreign gene expression in engineered somatic tissues
    • Bohl D, Heard JM. 1998. Transcriptional modulation of foreign gene expression in engineered somatic tissues. Cell Biol Toxicol 14(2):83-94.
    • (1998) Cell Biol Toxicol , vol.14 , Issue.2 , pp. 83-94
    • Bohl, D.1    Heard, J.M.2
  • 3
    • 0033739622 scopus 로고    scopus 로고
    • PERK mediates cell-cycle exit during the mammalian unfolded protein response
    • Brewer JW, Diehl JA. 2000. PERK mediates cell-cycle exit during the mammalian unfolded protein response. Proc Natl Acad Sci USA 97(23): 12625-12630.
    • (2000) Proc Natl Acad Sci USA , vol.97 , Issue.23 , pp. 12625-12630
    • Brewer, J.W.1    Diehl, J.A.2
  • 4
    • 0035716899 scopus 로고    scopus 로고
    • Update and perspectives on congenital disorders of glycosylation
    • Freeze HH. 2001. Update and perspectives on congenital disorders of glycosylation. Glycobiology 11(12):129R-143R.
    • (2001) Glycobiology , vol.11 , Issue.12
    • Freeze, H.H.1
  • 5
    • 0037137478 scopus 로고    scopus 로고
    • Human disorders in N-glycosylation and animal models
    • Freeze HH. 2002. Human disorders in N-glycosylation and animal models. Biochim Biophys Acta 1573(3):388-393.
    • (2002) Biochim Biophys Acta , vol.1573 , Issue.3 , pp. 388-393
    • Freeze, H.H.1
  • 6
    • 0035121677 scopus 로고    scopus 로고
    • The impact of mammalian gene regulation concepts on functional genomic research, metabolic engineering, and advanced gene therapies
    • Fussenegger M. 2001. The impact of mammalian gene regulation concepts on functional genomic research, metabolic engineering, and advanced gene therapies. Biotechnol Prog 17(1):1-51.
    • (2001) Biotechnol Prog , vol.17 , Issue.1 , pp. 1-51
    • Fussenegger, M.1
  • 7
    • 0026720075 scopus 로고
    • Tight control of gene expression in mammalian cells by tetracycline-responsive promoters
    • Gossen M, Bujard H. 1992. Tight control of gene expression in mammalian cells by tetracycline-responsive promoters. Proc Natl Acad Sci USA 89(12):5547-5551.
    • (1992) Proc Natl Acad Sci USA , vol.89 , Issue.12 , pp. 5547-5551
    • Gossen, M.1    Bujard, H.2
  • 8
    • 0029142564 scopus 로고
    • Overexpression of integral membrane proteins for structural studies
    • Grisshammer R, Tate CG. 1995. Overexpression of integral membrane proteins for structural studies. Q Rev Biophys 28(3):315-422.
    • (1995) Q Rev Biophys , vol.28 , Issue.3 , pp. 315-422
    • Grisshammer, R.1    Tate, C.G.2
  • 9
    • 0442309687 scopus 로고    scopus 로고
    • Effects of gene dosage, promoters, and substrates on unfolded protein stress of recombinant Pichia pastoris
    • Hohenblum H, Gasser B, Maurer M, Borth N, Mattanovich D. 2004. Effects of gene dosage, promoters, and substrates on unfolded protein stress of recombinant Pichia pastoris. Biotechnol Bioeng 85(4):367-375.
    • (2004) Biotechnol Bioeng , vol.85 , Issue.4 , pp. 367-375
    • Hohenblum, H.1    Gasser, B.2    Maurer, M.3    Borth, N.4    Mattanovich, D.5
  • 10
    • 0012152008 scopus 로고
    • Growth and maintenance of HeLa cells in serum-free medium supplemented with hormones
    • Hutchings SE, Sato GH. 1978. Growth and maintenance of HeLa cells in serum-free medium supplemented with hormones. Proc Natl Acad Sci USA 75(2):901-904.
    • (1978) Proc Natl Acad Sci USA , vol.75 , Issue.2 , pp. 901-904
    • Hutchings, S.E.1    Sato, G.H.2
  • 11
    • 0017891233 scopus 로고
    • Complete replacement of serum by albumin, transferrin, and soybean lipid in cultures of lipopolysaccharide-reactive B lymphocytes
    • Iscove NN, Melchers F. 1978. Complete replacement of serum by albumin, transferrin, and soybean lipid in cultures of lipopolysaccharide-reactive B lymphocytes. J Exp Med 147(3):923-933.
    • (1978) J Exp Med , vol.147 , Issue.3 , pp. 923-933
    • Iscove, N.N.1    Melchers, F.2
  • 12
    • 0033452061 scopus 로고    scopus 로고
    • Homogeneous tetracycline-regulatable gene expression in mammalian fibroblasts
    • Izumi M, Gilbert DM. 1999. Homogeneous tetracycline-regulatable gene expression in mammalian fibroblasts. J Cell Biochem 76(2):280-289.
    • (1999) J Cell Biochem , vol.76 , Issue.2 , pp. 280-289
    • Izumi, M.1    Gilbert, D.M.2
  • 13
    • 0036750868 scopus 로고    scopus 로고
    • Decreased protein expression and intermittent recoveries in BiP levels result from cellular stress during heterologous protein expression in Saccharomyces cerevisiae
    • Kauffman KJ, Pridgen EM, Doyle FJ III, Dhurjati PS, Robinson AS. 2002. Decreased protein expression and intermittent recoveries in BiP levels result from cellular stress during heterologous protein expression in Saccharomyces cerevisiae. Biotechnol Prog 18(5):942-950.
    • (2002) Biotechnol Prog , vol.18 , Issue.5 , pp. 942-950
    • Kauffman, K.J.1    Pridgen, E.M.2    Doyle III, F.J.3    Dhurjati, P.S.4    Robinson, A.S.5
  • 14
    • 0035916852 scopus 로고    scopus 로고
    • Comparative analysis of two controlled proliferation strategies regarding product quality, influence on tetracycline-regulated gene expression, and productivity
    • Kaufmann H, Mazur X, Marone R, Bailey JE, Fussenegger M. 2001. Comparative analysis of two controlled proliferation strategies regarding product quality, influence on tetracycline-regulated gene expression, and productivity. Biotechnol Bioeng 72(6):592-602.
    • (2001) Biotechnol Bioeng , vol.72 , Issue.6 , pp. 592-602
    • Kaufmann, H.1    Mazur, X.2    Marone, R.3    Bailey, J.E.4    Fussenegger, M.5
  • 15
    • 0023852783 scopus 로고
    • The presence of malfolded proteins in the endoplasmic reticulum signals the induction of glucose-regulated proteins
    • Kozutsumi Y, Segal M, Normington K, Gething MJ, Sambrook J. 1988. The presence of malfolded proteins in the endoplasmic reticulum signals the induction of glucose-regulated proteins. Nature 332(6163):462-464.
    • (1988) Nature , vol.332 , Issue.6163 , pp. 462-464
    • Kozutsumi, Y.1    Segal, M.2    Normington, K.3    Gething, M.J.4    Sambrook, J.5
  • 16
    • 0036192155 scopus 로고    scopus 로고
    • Overexpression of trehalose synthase and accumulation of intracellular trehalose in 293H and 293FTetR:Hyg cells
    • Lao G, Polayes D, Xia JL, Bloom FR, Levine F, Mansbridge J. 2001. Overexpression of trehalose synthase and accumulation of intracellular trehalose in 293H and 293FTetR:Hyg cells. Cryobiology 43(2):106-113.
    • (2001) Cryobiology , vol.43 , Issue.2 , pp. 106-113
    • Lao, G.1    Polayes, D.2    Xia, J.L.3    Bloom, F.R.4    Levine, F.5    Mansbridge, J.6
  • 17
    • 0035065952 scopus 로고    scopus 로고
    • Pro-apoptotic and anti-apoptotic effects of transferrin and transferrin-derived glycans on hematopoietic cells and lymphocytes
    • Lesnikov V, Lesnikova M, Deeg HJ. 2001. Pro-apoptotic and anti-apoptotic effects of transferrin and transferrin-derived glycans on hematopoietic cells and lymphocytes. Exp Hematol 29(4):477-489.
    • (2001) Exp Hematol , vol.29 , Issue.4 , pp. 477-489
    • Lesnikov, V.1    Lesnikova, M.2    Deeg, H.J.3
  • 20
    • 0029278670 scopus 로고
    • Further development of the locus control region/murine erythroleukemia expression system: High level expression and characterization of recombinant human calcitonin receptor
    • Needham M, Egerton M, Millest A, Evans S, Popplewell M, Cerillo G, McPheat J, Monk A, Jack A, Johnstone D, Hollis M. 1995. Further development of the locus control region/murine erythroleukemia expression system: High level expression and characterization of recombinant human calcitonin receptor. Protein Expr Purif 6(2):124-131.
    • (1995) Protein Expr Purif , vol.6 , Issue.2 , pp. 124-131
    • Needham, M.1    Egerton, M.2    Millest, A.3    Evans, S.4    Popplewell, M.5    Cerillo, G.6    McPheat, J.7    Monk, A.8    Jack, A.9    Johnstone, D.10    Hollis, M.11
  • 21
    • 0029865151 scopus 로고    scopus 로고
    • Ecdysone-inducible gene expression in mammalian cells and transgenic mice
    • No D, Yao TP, Evans RM. 1996. Ecdysone-inducible gene expression in mammalian cells and transgenic mice. Proc Natl Acad Sci USA 93(8): 3346-3351.
    • (1996) Proc Natl Acad Sci USA , vol.93 , Issue.8 , pp. 3346-3351
    • No, D.1    Yao, T.P.2    Evans, R.M.3
  • 22
    • 0027295871 scopus 로고
    • Association of folding intermediates of glycoproteins with calnexin during protein maturation
    • Ou WJ, Cameron PH, Thomas DY, Bergeron JJ. 1993. Association of folding intermediates of glycoproteins with calnexin during protein maturation. Nature 364(6440):771-776.
    • (1993) Nature , vol.364 , Issue.6440 , pp. 771-776
    • Ou, W.J.1    Cameron, P.H.2    Thomas, D.Y.3    Bergeron, J.J.4
  • 23
    • 0026788147 scopus 로고
    • Phosphorylation of eukaryotic initiation factor (eIF) 2 alpha and inhibition of eIF-2B in GH3 pituitary cells by perturbants of early protein processing that induce GRP78
    • Prostko CR, Brostrom MA, Malara EM, Brostrom CO. 1992. Phosphorylation of eukaryotic initiation factor (eIF) 2 alpha and inhibition of eIF-2B in GH3 pituitary cells by perturbants of early protein processing that induce GRP78. J Biol Chem 267(24):16751-16754.
    • (1992) J Biol Chem , vol.267 , Issue.24 , pp. 16751-16754
    • Prostko, C.R.1    Brostrom, M.A.2    Malara, E.M.3    Brostrom, C.O.4
  • 26
    • 0031740332 scopus 로고    scopus 로고
    • Tetracycline-regulatable factors with distinct dimerization domains allow reversible growth inhibition by p16
    • Rossi FM, Guicherit OM, Spicher A, Kringstein AM, Fatyol K, Blakely BT, Blau HM. 1998. Tetracycline-regulatable factors with distinct dimerization domains allow reversible growth inhibition by p16. Nat Genet 20(4):389-393.
    • (1998) Nat Genet , vol.20 , Issue.4 , pp. 389-393
    • Rossi, F.M.1    Guicherit, O.M.2    Spicher, A.3    Kringstein, A.M.4    Fatyol, K.5    Blakely, B.T.6    Blau, H.M.7
  • 27
    • 0346096508 scopus 로고    scopus 로고
    • Quality control in the endoplasmic reticulum protein factory
    • Sitia R, Braakman I. 2003. Quality control in the endoplasmic reticulum protein factory. Nature 426(6968):891-894.
    • (2003) Nature , vol.426 , Issue.6968 , pp. 891-894
    • Sitia, R.1    Braakman, I.2
  • 28
    • 0034281735 scopus 로고    scopus 로고
    • Insulin-like growth factor-I and transferrin mediate growth and survival of Chinese hamster ovary cells
    • Sunstrom NA, Gay RD, Wong DC, Kitchen NA, DeBoer L, Gray PP. 2000. Insulin-like growth factor-I and transferrin mediate growth and survival of Chinese hamster ovary cells. Biotechnol Prog 16(5):698-702.
    • (2000) Biotechnol Prog , vol.16 , Issue.5 , pp. 698-702
    • Sunstrom, N.A.1    Gay, R.D.2    Wong, D.C.3    Kitchen, N.A.4    Deboer, L.5    Gray, P.P.6
  • 29
    • 0348003908 scopus 로고    scopus 로고
    • Comparison of seven different heterologous protein expression systems for the production of the serotonin transporter
    • Tate CG, Haase J, Baker C, Boorsma M, Magnani F, Vallis Y, Williams DC. 2003. Comparison of seven different heterologous protein expression systems for the production of the serotonin transporter. Biochim Biophys Acta 1610(1):141-153.
    • (2003) Biochim Biophys Acta , vol.1610 , Issue.1 , pp. 141-153
    • Tate, C.G.1    Haase, J.2    Baker, C.3    Boorsma, M.4    Magnani, F.5    Vallis, Y.6    Williams, D.C.7
  • 30
    • 0015400277 scopus 로고
    • Biological effects of transferrin on human lymphocytes in vitro
    • Tormey DC, Mueller GC. 1972. Biological effects of transferrin on human lymphocytes in vitro. Exp Cell Res 74(1):220-226.
    • (1972) Exp Cell Res , vol.74 , Issue.1 , pp. 220-226
    • Tormey, D.C.1    Mueller, G.C.2
  • 31
    • 0033527910 scopus 로고    scopus 로고
    • Tetracycline-regulated overexpression of glycosyltransferases in Chinese hamster ovary cells
    • Umana P, Jean-Mairet J, Bailey JE. 1999. Tetracycline-regulated overexpression of glycosyltransferases in Chinese hamster ovary cells. Biotechnol Bioeng 65(5):542-549.
    • (1999) Biotechnol Bioeng , vol.65 , Issue.5 , pp. 542-549
    • Umana, P.1    Jean-Mairet, J.2    Bailey, J.E.3
  • 32
    • 0034984663 scopus 로고    scopus 로고
    • Mif1: A missing link between the unfolded protein response pathway and ER-associated protein degradation?
    • van Laar T, van der Eb AJ, Terleth C. 2001. Mif1: A missing link between the unfolded protein response pathway and ER-associated protein degradation? Curr Protein Pept Sci 2(2): 169-190.
    • (2001) Curr Protein Pept Sci , vol.2 , Issue.2 , pp. 169-190
    • Van Laar, T.1    Van Der Eb, A.J.2    Terleth, C.3
  • 33
    • 0030815129 scopus 로고    scopus 로고
    • Promotion of transferrin folding by cyclic interactions with calnexin and calreticulin
    • Wada I, Kai M, Imai S, Sakane F, Kanoh H. 1997. Promotion of transferrin folding by cyclic interactions with calnexin and calreticulin. Embo J 16(17):5420-5432.
    • (1997) Embo J , vol.16 , Issue.17 , pp. 5420-5432
    • Wada, I.1    Kai, M.2    Imai, S.3    Sakane, F.4    Kanoh, H.5
  • 35
    • 0032170171 scopus 로고    scopus 로고
    • Tetracycline repressor, tetR, rather than the tetR-mammalian cell transcription factor fusion derivatives, regulates inducible gene expression in mammalian cells
    • Yao F, Svensjo T, Winkler T, Lu M, Eriksson C, Eriksson E. 1998. Tetracycline repressor, tetR, rather than the tetR-mammalian cell transcription factor fusion derivatives, regulates inducible gene expression in mammalian cells. Hum Gene Ther 9(13):1939-1950.
    • (1998) Hum Gene Ther , vol.9 , Issue.13 , pp. 1939-1950
    • Yao, F.1    Svensjo, T.2    Winkler, T.3    Lu, M.4    Eriksson, C.5    Eriksson, E.6
  • 36
    • 0021965799 scopus 로고
    • Variability in transport rates of secretory glycoproteins through the endoplasmic reticulum and Golgi in human hepatoma cells
    • Yeo KT, Parent JB, Yeo TK, Olden K. 1985. Variability in transport rates of secretory glycoproteins through the endoplasmic reticulum and Golgi in human hepatoma cells. J Biol Chem 260(13):7896-7902.
    • (1985) J Biol Chem , vol.260 , Issue.13 , pp. 7896-7902
    • Yeo, K.T.1    Parent, J.B.2    Yeo, T.K.3    Olden, K.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.