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Volumn 29, Issue 2, 1999, Pages 93-102

Quantitative analysis of transcription and translation in gene amplified Chinese hamster ovary cells on the basis of a kinetic model

Author keywords

CHO cells; Gene expression; Kinetic model; Protein secretion; Transcription; Translation

Indexed keywords

ANTITHROMBIN III; COPY DNA; GENE AMPLIFICATION; HAMSTER; KINETIC MODEL; MAMMAL CELL; PROTEIN DEGRADATION; QUANTITATIVE GENETICS;

EID: 0344731401     PISSN: 09209069     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1008077603328     Document Type: Article
Times cited : (11)

References (44)
  • 1
    • 0020072091 scopus 로고
    • New approach to tryptophan production by Escherichia coli: Genetic manipulation of composite plasmids in vitro
    • Aiba S, Tsunekawa H and Imanaka T (1982) New approach to tryptophan production by Escherichia coli: Genetic manipulation of composite plasmids in vitro. Appl Environ Microbiol 43: 289-297.
    • (1982) Appl Environ Microbiol , vol.43 , pp. 289-297
    • Aiba, S.1    Tsunekawa, H.2    Imanaka, T.3
  • 3
    • 0020971025 scopus 로고
    • Kinetics of product formation and plasmid segregation in recombinant microbial populations
    • Bailey JE, Hjortso M, Lee SB and Srienc F (1983) Kinetics of product formation and plasmid segregation in recombinant microbial populations. Ann NY Acad Sci 413: 71-87.
    • (1983) Ann NY Acad Sci , vol.413 , pp. 71-87
    • Bailey, J.E.1    Hjortso, M.2    Lee, S.B.3    Srienc, F.4
  • 4
    • 0029762971 scopus 로고    scopus 로고
    • Inhibition of translational initiation by activators of the glucose-regulated stress protein and heat shock protein stress response systems. Role of the interferon-inducible double-stranded RNA-activated eukaryotic initiation factor 2α kinase
    • Brostrom CO, Prostko CR, Kaufman RJ and Brostrom MA (1996) Inhibition of translational initiation by activators of the glucose-regulated stress protein and heat shock protein stress response systems. Role of the interferon-inducible double-stranded RNA-activated eukaryotic initiation factor 2α kinase. J Biol Chem 271: 24995-25002.
    • (1996) J Biol Chem , vol.271 , pp. 24995-25002
    • Brostrom, C.O.1    Prostko, C.R.2    Kaufman, R.J.3    Brostrom, M.A.4
  • 5
    • 0023277545 scopus 로고
    • Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction
    • Chomczynski P and Sacchi N (1987) Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Anal Biochem 162: 156-159.
    • (1987) Anal Biochem , vol.162 , pp. 156-159
    • Chomczynski, P.1    Sacchi, N.2
  • 7
    • 0021230312 scopus 로고
    • Novel DNA rearrangements are associated with dihydrofolate reductase gene amplification
    • Federspiel NA, Beverley SM, Schilling JW and Schimke RT (1984) Novel DNA rearrangements are associated with dihydrofolate reductase gene amplification. J Biol Chem 259: 9127-9140.
    • (1984) J Biol Chem , vol.259 , pp. 9127-9140
    • Federspiel, N.A.1    Beverley, S.M.2    Schilling, J.W.3    Schimke, R.T.4
  • 8
    • 0019304936 scopus 로고
    • Structural studies on the carbohydrate portion of human antithrombin III
    • Franzén L-E and Svensson S (1980) Structural studies on the carbohydrate portion of human antithrombin III. J Biol Chem 255: 5090-5093.
    • (1980) J Biol Chem , vol.255 , pp. 5090-5093
    • Franzén, L.-E.1    Svensson, S.2
  • 9
    • 0022777520 scopus 로고
    • Structure of DNA formed in the first step of CAD gene amplification
    • Giulotto E, Saito I and Stark GR (1986) Structure of DNA formed in the first step of CAD gene amplification. EMBO J 5: 2110-2121.
    • (1986) EMBO J , vol.5 , pp. 2110-2121
    • Giulotto, E.1    Saito, I.2    Stark, G.R.3
  • 11
    • 0020959710 scopus 로고
    • Studies on transformation of Escherichia coli with plasmids
    • Hanahan D (1983) Studies on transformation of Escherichia coli with plasmids. J Mol Biol 166: 557-580.
    • (1983) J Mol Biol , vol.166 , pp. 557-580
    • Hanahan, D.1
  • 12
    • 14744285266 scopus 로고
    • Single-step recovery of a secreted recombinant protein by expanded bed adsorption
    • Hansson M, Stahl S, Hjorth R, Uhlen M and Moks T (1994) Single-step recovery of a secreted recombinant protein by expanded bed adsorption. Bio/Technology 12: 285-288.
    • (1994) Bio/Technology , vol.12 , pp. 285-288
    • Hansson, M.1    Stahl, S.2    Hjorth, R.3    Uhlen, M.4    Moks, T.5
  • 13
    • 0025997323 scopus 로고
    • High-level expression of foreign genes in mammalian cells
    • Setlow JK (Ed) Plenum Press, New York
    • Kane SE (1991) High-level expression of foreign genes in mammalian cells. In: Setlow JK (Ed) Genetic Engineering. Vol. 13, Plenum Press, New York, pp. 167-182.
    • (1991) Genetic Engineering. , vol.13 , pp. 167-182
    • Kane, S.E.1
  • 14
    • 0000960851 scopus 로고
    • Amplification and expression of transfected genes in mammalian cells
    • Kellems RE (Ed) Marcel Dekker, New York
    • Kaufman RJ (1993) Amplification and expression of transfected genes in mammalian cells. In: Kellems RE (Ed) Gene Amplification in Mammalian Cells. Marcel Dekker, New York, pp. 315-343.
    • (1993) Gene Amplification in Mammalian Cells , pp. 315-343
    • Kaufman, R.J.1
  • 15
    • 0344615302 scopus 로고
    • Factors limiting biosynthesis and secretion of factor VIII in mammalian cells
    • Alitalo KK, Huhtala M-L, Knowles J and Vaheri A (Eds) Elsevier Science Publishers, Amsterdam
    • Kaufman RJ, Pittman DD, Marquette KA, Wasley LC and Dorner AJ (1990) Factors limiting biosynthesis and secretion of factor VIII in mammalian cells. In: Alitalo KK, Huhtala M-L, Knowles J and Vaheri A (Eds) Recombinant Systems in Protein Expression. Elsevier Science Publishers, Amsterdam, pp. 63-74.
    • (1990) Recombinant Systems in Protein Expression , pp. 63-74
    • Kaufman, R.J.1    Pittman, D.D.2    Marquette, K.A.3    Wasley, L.C.4    Dorner, A.J.5
  • 16
    • 0026235642 scopus 로고
    • Gene amplification in mammalian cells: Strategies for protein production
    • Kellems RE (1991) Gene amplification in mammalian cells: strategies for protein production. Curr Opin Biotechnol 2: 723-729.
    • (1991) Curr Opin Biotechnol , vol.2 , pp. 723-729
    • Kellems, R.E.1
  • 17
    • 14744271625 scopus 로고
    • Protein aggregation in vitro and in vivo: A quantitative model of the kinetic competition between folding and aggregation
    • Kiefhaber T, Rudolph R, Kohler H-H and Buchner J (1991) Protein aggregation in vitro and in vivo: A quantitative model of the kinetic competition between folding and aggregation. Bio/Technology 9: 825-829.
    • (1991) Bio/Technology , vol.9 , pp. 825-829
    • Kiefhaber, T.1    Rudolph, R.2    Kohler, H.-H.3    Buchner, J.4
  • 18
  • 19
    • 0019270813 scopus 로고
    • Structural studies of the carbohydrate moiety of human antithrombin III
    • Mizuochi T, Fujii J, Kurachi K and Kobata A (1980) Structural studies of the carbohydrate moiety of human antithrombin III. Arch Biochem Biophys 203: 458-465.
    • (1980) Arch Biochem Biophys , vol.203 , pp. 458-465
    • Mizuochi, T.1    Fujii, J.2    Kurachi, K.3    Kobata, A.4
  • 20
    • 0027319027 scopus 로고
    • Expression of a phosphorylation-resistant eukaryotic initiation factor 2 α-subunit mitigates heat shock inhibition of protein synthesis
    • Murtha-Riel P, Davies MV, Scherer BJ, Choi SY, Hershey JWB and Kaufman RJ (1993) Expression of a phosphorylation-resistant eukaryotic initiation factor 2 α-subunit mitigates heat shock inhibition of protein synthesis. J Biol Chem 268: 12946-12951.
    • (1993) J Biol Chem , vol.268 , pp. 12946-12951
    • Murtha-Riel, P.1    Davies, M.V.2    Scherer, B.J.3    Choi, S.Y.4    Hershey, J.5    Kaufman, R.J.6
  • 21
    • 0024623218 scopus 로고
    • Quantitative analysis of membrane and secretory protein processing and intracellular transport
    • Noe DA and Delenick JC (1989) Quantitative analysis of membrane and secretory protein processing and intracellular transport. J Cell Sci 92: 449-459.
    • (1989) J Cell Sci , vol.92 , pp. 449-459
    • Noe, D.A.1    Delenick, J.C.2
  • 22
    • 0009651043 scopus 로고
    • The size and shape of human and bovine antithrombin III
    • Nordenman B, Nyström C and Björk I (1977) The size and shape of human and bovine antithrombin III. J Biol Chem 258: 8389-8394.
    • (1977) J Biol Chem , vol.258 , pp. 8389-8394
    • Nordenman, B.1    Nyström, C.2    Björk, I.3
  • 24
    • 0027112480 scopus 로고
    • Effect of cloned gene dosage on cell growth and hepatitis B surface antigen synthesis and secretion in recombinant CHO cells
    • Pendse GJ, Karkare S and Bailey JE (1992) Effect of cloned gene dosage on cell growth and hepatitis B surface antigen synthesis and secretion in recombinant CHO cells. Biotechnol Bioeng 40: 119-129.
    • (1992) Biotechnol Bioeng , vol.40 , pp. 119-129
    • Pendse, G.J.1    Karkare, S.2    Bailey, J.E.3
  • 26
    • 0028938425 scopus 로고
    • Activation of the double-stranded RNA-regulated protein kinase by depletion of endoplasmic reticular calcium stores
    • Prostko CR, Dholakia JN, Brostrom MA and Brostrom CO (1995) Activation of the double-stranded RNA-regulated protein kinase by depletion of endoplasmic reticular calcium stores. J Biol Chem 270: 6211-6215.
    • (1995) J Biol Chem , vol.270 , pp. 6211-6215
    • Prostko, C.R.1    Dholakia, J.N.2    Brostrom, M.A.3    Brostrom, C.O.4
  • 27
    • 0028263821 scopus 로고
    • Expression of mutant eukaryotic initiation factor 2 α subunit (eIF2α) reduces inhibition of guanine nucleotide exchange activity of eIF-2B mediated by eIF-2α phosphorylation
    • Ramaiah KVA, Davies M, Chen JJ and Kaufman RJ (1994) Expression of mutant eukaryotic initiation factor 2 α subunit (eIF2α) reduces inhibition of guanine nucleotide exchange activity of eIF-2B mediated by eIF-2α phosphorylation. Mol Cell Biol 14: 4546-4553.
    • (1994) Mol Cell Biol , vol.14 , pp. 4546-4553
    • Kva, R.1    Davies, M.2    Chen, J.J.3    Kaufman, R.J.4
  • 28
    • 0029165020 scopus 로고
    • mRNA stability in mammalian cells
    • Ross J (1995) mRNA stability in mammalian cells. Microbiol Rev 59: 423-450.
    • (1995) Microbiol Rev , vol.59 , pp. 423-450
    • Ross, J.1
  • 29
    • 0027712790 scopus 로고
    • Folding, assembly, and post-translational modification of proteins within the lumen of the endoplasmic reticulum
    • Rowling PJE and Freedman RB (1993) Folding, assembly, and post-translational modification of proteins within the lumen of the endoplasmic reticulum. Subcell Biochem 21: 41-81.
    • (1993) Subcell Biochem , vol.21 , pp. 41-81
    • Pje, R.1    Freedman, R.B.2
  • 30
    • 84952934128 scopus 로고
    • Bioprocess kinetics and modelling of recombinant fermentation
    • Rehm H-J, Reed G, Pühler A, Stadler P and Schügerl K (Eds) VCH, Weinheim
    • Ryu DDY, Kim J-Y and Lee SB (1991) Bioprocess kinetics and modelling of recombinant fermentation. In: Rehm H-J, Reed G, Pühler A, Stadler P and Schügerl K (Eds) Biotechnology, Vol. 4: Measuring, Modelling, and Control. VCH, Weinheim, pp. 485-505.
    • (1991) Biotechnology, Vol. 4: Measuring, Modelling, and Control , vol.4 , pp. 485-505
    • Ryu, D.D.Y.1    Kim, J.-Y.2    Lee, S.B.3
  • 32
    • 0345960852 scopus 로고    scopus 로고
    • Overexpression of recombinant human antithrombin III in Chinese hamster ovary cells results in malformation and decreased secretion of the recombinant protein
    • Schröder M and Friedl P (1997) Overexpression of recombinant human antithrombin III in Chinese hamster ovary cells results in malformation and decreased secretion of the recombinant protein. Biotechnol Bioeng 53: 547-559.
    • (1997) Biotechnol Bioeng , vol.53 , pp. 547-559
    • Schröder, M.1    Friedl, P.2
  • 33
    • 0022407889 scopus 로고
    • Effects of recombinant plasmid content on growth properties and cloned gene product formation in Escherichia coli
    • Seo J-H and Bailey JE (1985) Effects of recombinant plasmid content on growth properties and cloned gene product formation in Escherichia coli. Biotechnol Bioeng 27: 1668-1674.
    • (1985) Biotechnol Bioeng , vol.27 , pp. 1668-1674
    • Seo, J.-H.1    Bailey, J.E.2
  • 34
    • 0022792136 scopus 로고
    • Continuous cultivation of recombinant Escherichia coli: Existence of an optimum dilution rate for maximum plasmid and gene product concentration
    • Seo J-H and Bailey JE (1986) Continuous cultivation of recombinant Escherichia coli: Existence of an optimum dilution rate for maximum plasmid and gene product concentration. Biotechnol Bioeng 28: 1590-1594.
    • (1986) Biotechnol Bioeng , vol.28 , pp. 1590-1594
    • Seo, J.-H.1    Bailey, J.E.2
  • 35
    • 0027548779 scopus 로고
    • A rapid procedure for isolation of RNA-free genomic DNA from mammalian cells
    • Sharma RC, Murphy AJM, DeWald MG and Schimke RT (1993) A rapid procedure for isolation of RNA-free genomic DNA from mammalian cells. BioTechniques 14: 176-178.
    • (1993) BioTechniques , vol.14 , pp. 176-178
    • Sharma, R.C.1    Murphy, A.J.M.2    Dewald, M.G.3    Schimke, R.T.4
  • 36
    • 0029067408 scopus 로고
    • Calcium depletion from the endoplasmic reticulum activates the double-stranded RNA-dependent protein kinase (PKR) to inhibit protein synthesis
    • Srivastava SP, Davies MV and Kaufman RJ (1995) Calcium depletion from the endoplasmic reticulum activates the double-stranded RNA-dependent protein kinase (PKR) to inhibit protein synthesis. J Biol Chem 270: 16619-16624.
    • (1995) J Biol Chem , vol.270 , pp. 16619-16624
    • Srivastava, S.P.1    Davies, M.V.2    Kaufman, R.J.3
  • 37
    • 0027465163 scopus 로고
    • Loss of resolution in gel electrophoresis of RNA: A problem associated with the presence of formaldehyde gradients
    • Tsang SS, Yin X, Guzzo-Arkuran C, Jones VS and Davison AJ (1993) Loss of resolution in gel electrophoresis of RNA: A problem associated with the presence of formaldehyde gradients. BioTechniques 14: 380-381.
    • (1993) BioTechniques , vol.14 , pp. 380-381
    • Tsang, S.S.1    Yin, X.2    Guzzo-Arkuran, C.3    Jones, V.S.4    Davison, A.J.5
  • 38
    • 0001127374 scopus 로고
    • Isolation of Chinese hamster cell mutants deficient in dihydrofolate reductase activity
    • Urlaub G and Chasin LA (1980) Isolation of Chinese hamster cell mutants deficient in dihydrofolate reductase activity. Proc Natl Acad Sci USA 77: 4216-4220.
    • (1980) Proc Natl Acad Sci USA , vol.77 , pp. 4216-4220
    • Urlaub, G.1    Chasin, L.A.2
  • 43
    • 0018788361 scopus 로고
    • Reconstitution of lactic dehydrogenase. Noncovalent aggregation vs. reactivation
    • Zettlmeissl G, Rudolph R and Jaenicke R (1979) Reconstitution of lactic dehydrogenase. Noncovalent aggregation vs. reactivation. Biochemistry 18: 5567-5571.
    • (1979) Biochemistry , vol.18 , pp. 5567-5571
    • Zettlmeissl, G.1    Rudolph, R.2    Jaenicke, R.3
  • 44
    • 0023224194 scopus 로고
    • Expression of biologically active human antithrombin III in Chinese hamster ovary cells
    • Zettlmeissl G, Ragg H and Karges HE (1987) Expression of biologically active human antithrombin III in Chinese hamster ovary cells. Bio/Technology 5: 720-725.
    • (1987) Bio/Technology , vol.5 , pp. 720-725
    • Zettlmeissl, G.1    Ragg, H.2    Karges, H.E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.