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Volumn 113, Issue 7, 2016, Pages 1468-1480

Mannose metabolism in recombinant CHO cells and its effect on IgG glycosylation

Author keywords

CHO; Flux analysis; Glycosylation; High mannose; IgG; Mannose; Metabolism

Indexed keywords

CELL GROWTH; CELLS; CYTOLOGY; GROWTH KINETICS; METABOLISM; METABOLITES; PHYSIOLOGY;

EID: 84958280421     PISSN: 00063592     EISSN: 10970290     Source Type: Journal    
DOI: 10.1002/bit.25924     Document Type: Article
Times cited : (33)

References (37)
  • 1
    • 84870668228 scopus 로고    scopus 로고
    • Parallel labeling experiments with [1,2-(13)C]glucose and [U-(13)C]glutamine provide new insights into CHO cell metabolism
    • Ahn WS, Antoniewicz MR. 2013. Parallel labeling experiments with [1, 2-(13)C]glucose and [U-(13)C]glutamine provide new insights into CHO cell metabolism. Metab Eng 15:34-47.
    • (2013) Metab Eng , vol.15 , pp. 34-47
    • Ahn, W.S.1    Antoniewicz, M.R.2
  • 2
    • 33745155105 scopus 로고    scopus 로고
    • Determination of confidence intervals of metabolic fluxes estimated from stable isotope measurements
    • Antoniewicz MR, Kelleher JK, Stephanopoulos G. 2006. Determination of confidence intervals of metabolic fluxes estimated from stable isotope measurements. Metab Eng 8:324-337.
    • (2006) Metab Eng , vol.8 , pp. 324-337
    • Antoniewicz, M.R.1    Kelleher, J.K.2    Stephanopoulos, G.3
  • 3
    • 33845679072 scopus 로고    scopus 로고
    • Elementary metabolite units (EMU): A novel framework for modeling isotopic distributions
    • Antoniewicz MR, Kelleher JK, Stephanopoulos G. 2007. Elementary metabolite units (EMU): A novel framework for modeling isotopic distributions. Metab Eng 9:68-86.
    • (2007) Metab Eng , vol.9 , pp. 68-86
    • Antoniewicz, M.R.1    Kelleher, J.K.2    Stephanopoulos, G.3
  • 4
    • 84859224265 scopus 로고    scopus 로고
    • In situ monitoring of intracellular glucose and glutamine in CHO cell culture
    • Behjousiar A, Kontoravdi C, Polizzi KM. 2012. In situ monitoring of intracellular glucose and glutamine in CHO cell culture. PLoS ONE 7:e34512.
    • (2012) PLoS ONE , vol.7 , pp. e34512
    • Behjousiar, A.1    Kontoravdi, C.2    Polizzi, K.M.3
  • 5
    • 80054092824 scopus 로고    scopus 로고
    • Synergizing metabolic flux analysis and nucleotide sugar metabolism to understand the control of glycosylation of recombinant protein in CHO cells
    • Burleigh SC, van de Laar T, Stroop CJ, van Grunsven WM, O'Donoghue N, Rudd PM, Davey GP. 2011. Synergizing metabolic flux analysis and nucleotide sugar metabolism to understand the control of glycosylation of recombinant protein in CHO cells. BMC Biotechnol 11:95.
    • (2011) BMC Biotechnol , vol.11 , pp. 95
    • Burleigh, S.C.1    van de Laar, T.2    Stroop, C.J.3    van Grunsven, W.M.4    O'Donoghue, N.5    Rudd, P.M.6    Davey, G.P.7
  • 6
    • 12544253860 scopus 로고    scopus 로고
    • Impact of dynamic online fed-batch strategies on metabolism, productivity, and N-glycosylation quality in CHO cell cultures
    • Chee Furng Wong D, Tin Kam Wong K, Tang Goh L, Kiat Heng C, Gek Sim Yap M. 2005. Impact of dynamic online fed-batch strategies on metabolism, productivity, and N-glycosylation quality in CHO cell cultures. Biotechnol Bioeng 89:164-177.
    • (2005) Biotechnol Bioeng , vol.89 , pp. 164-177
    • Chee Furng Wong, D.1    Tin Kam Wong, K.2    Tang Goh, L.3    Kiat Heng, C.4    Gek Sim Yap, M.5
  • 7
    • 33846927813 scopus 로고    scopus 로고
    • Amino acid and manganese supplementation modulates the glycosylation state of erythropoietin in a CHO culture system
    • Crowell CK, Grampp GE, Rogers GN, Miller J, Scheinman RI. 2007. Amino acid and manganese supplementation modulates the glycosylation state of erythropoietin in a CHO culture system. Biotechnol Bioeng 96:538-549.
    • (2007) Biotechnol Bioeng , vol.96 , pp. 538-549
    • Crowell, C.K.1    Grampp, G.E.2    Rogers, G.N.3    Miller, J.4    Scheinman, R.I.5
  • 8
    • 0035921175 scopus 로고    scopus 로고
    • Expression of GnTIII in a recombinant anti-CD20 CHO production cell line: Expression of antibodies with altered glycoforms leads to an increase in ADCC through higher affinity for FC gamma RIII
    • Davies J, Jiang L, Pan LZ, LaBarre MJ, Anderson D, Reff M. 2001. Expression of GnTIII in a recombinant anti-CD20 CHO production cell line: Expression of antibodies with altered glycoforms leads to an increase in ADCC through higher affinity for FC gamma RIII. Biotechnol Bioeng 74:288-294.
    • (2001) Biotechnol Bioeng , vol.74 , pp. 288-294
    • Davies, J.1    Jiang, L.2    Pan, L.Z.3    LaBarre, M.J.4    Anderson, D.5    Reff, M.6
  • 9
    • 84876764895 scopus 로고    scopus 로고
    • Metabolic analysis of antibody producing CHO cells in fed-batch production
    • Dean J, Reddy P. 2013. Metabolic analysis of antibody producing CHO cells in fed-batch production. Biotechnol Bioeng 110:1735-1747.
    • (2013) Biotechnol Bioeng , vol.110 , pp. 1735-1747
    • Dean, J.1    Reddy, P.2
  • 11
    • 0015867376 scopus 로고
    • A new alpha-D-mannosidase occurring in Golgi membranes
    • Dewald B, Touster O. 1973. A new alpha-D-mannosidase occurring in Golgi membranes. J Biol Chem 248:7223-7233.
    • (1973) J Biol Chem , vol.248 , pp. 7223-7233
    • Dewald, B.1    Touster, O.2
  • 13
    • 0024278869 scopus 로고
    • Mathematical descriptions of hybridoma culture kinetics: I. Initial metabolic rates
    • Glacken MW, Adema E, Sinskey AJ. 1988. Mathematical descriptions of hybridoma culture kinetics: I. Initial metabolic rates. Biotechnol Bioeng 32:491-506.
    • (1988) Biotechnol Bioeng , vol.32 , pp. 491-506
    • Glacken, M.W.1    Adema, E.2    Sinskey, A.J.3
  • 14
    • 79958837668 scopus 로고    scopus 로고
    • High-mannose glycans on the Fc region of therapeutic IgG antibodies increase serum clearance in humans
    • Goetze AM, Liu YD, Zhang Z, Shah B, Lee E, Bondarenko PV, Flynn GC. 2011. High-mannose glycans on the Fc region of therapeutic IgG antibodies increase serum clearance in humans. Glycobiology 21:949-959.
    • (2011) Glycobiology , vol.21 , pp. 949-959
    • Goetze, A.M.1    Liu, Y.D.2    Zhang, Z.3    Shah, B.4    Lee, E.5    Bondarenko, P.V.6    Flynn, G.C.7
  • 15
    • 0035922885 scopus 로고    scopus 로고
    • Metabolic control of recombinant monoclonal antibody N-glycosylation in GS-NS0 cells
    • Hills AE, Patel A, Boyd P, James DC. 2001. Metabolic control of recombinant monoclonal antibody N-glycosylation in GS-NS0 cells. Biotechnol Bioeng 75:239-251.
    • (2001) Biotechnol Bioeng , vol.75 , pp. 239-251
    • Hills, A.E.1    Patel, A.2    Boyd, P.3    James, D.C.4
  • 16
    • 68749110765 scopus 로고    scopus 로고
    • Optimal and consistent protein glycosylation in mammalian cell culture
    • Hossler P, Khattak SF, Li ZJ. 2009. Optimal and consistent protein glycosylation in mammalian cell culture. Glycobiology 19:936-949.
    • (2009) Glycobiology , vol.19 , pp. 936-949
    • Hossler, P.1    Khattak, S.F.2    Li, Z.J.3
  • 17
    • 84928429962 scopus 로고    scopus 로고
    • A robust method for increasing fc glycan high mannose level of recombinant antibodies
    • Huang CJ, Lin H, Yang JX. 2015. A robust method for increasing fc glycan high mannose level of recombinant antibodies. Biotechnol Bioeng 112(6):1200-1209.
    • (2015) Biotechnol Bioeng , vol.112 , Issue.6 , pp. 1200-1209
    • Huang, C.J.1    Lin, H.2    Yang, J.X.3
  • 18
    • 0037008394 scopus 로고    scopus 로고
    • A new kinetic model proposed for enzymatic hydrolysis of lactose by beta-galactosidase from Kluyveromyces fragilis
    • Jurado EC, Luzon F, Vicaria G. 2002. A new kinetic model proposed for enzymatic hydrolysis of lactose by beta-galactosidase from Kluyveromyces fragilis. Enzyme Microb Technol 31:300-309.
    • (2002) Enzyme Microb Technol , vol.31 , pp. 300-309
    • Jurado, E.C.1    Luzon, F.2    Vicaria, G.3
  • 19
    • 84865597532 scopus 로고    scopus 로고
    • Parellel labeling experiments with [U-13C]glucose validate E. coli metabolic network model for 13C metabolic flux analysis
    • Leighty RW, Antoniewicz MR. 2012. Parellel labeling experiments with [U-13C]glucose validate E. coli metabolic network model for 13C metabolic flux analysis. Metab Eng 14:533-541.
    • (2012) Metab Eng , vol.14 , pp. 533-541
    • Leighty, R.W.1    Antoniewicz, M.R.2
  • 20
    • 77958518175 scopus 로고    scopus 로고
    • Cell culture processes for monoclonal antibody production
    • Li F, Vijayasankaran N, Shen AY, Kiss R, Amanullah A. 2010. Cell culture processes for monoclonal antibody production. MAbs 2:466-479.
    • (2010) MAbs , vol.2 , pp. 466-479
    • Li, F.1    Vijayasankaran, N.2    Shen, A.Y.3    Kiss, R.4    Amanullah, A.5
  • 21
    • 0014199519 scopus 로고
    • Studies on the glycosidases in jack bean meal. I. Isolation and properties of alpha-mannosidase
    • Li YT. 1967. Studies on the glycosidases in jack bean meal. I. Isolation and properties of alpha-mannosidase. J Biol Chem 242:5474-5480.
    • (1967) J Biol Chem , vol.242 , pp. 5474-5480
    • Li, Y.T.1
  • 22
    • 84860498026 scopus 로고    scopus 로고
    • IsoCor: Correcting MS data in isotope labeling experiments
    • Millard P, Letisse F, Sokol S, Portais JC. 2012. IsoCor: Correcting MS data in isotope labeling experiments. Bioinformatics 28:1294-1296.
    • (2012) Bioinformatics , vol.28 , pp. 1294-1296
    • Millard, P.1    Letisse, F.2    Sokol, S.3    Portais, J.C.4
  • 23
    • 17944387597 scopus 로고    scopus 로고
    • Effects of buffering conditions and culture pH on production rates and glycosylation of clinical phase I anti-melanoma mouse IgG3 monoclonal antibody R24
    • Muthing J, Kemminer SE, Conradt HS, Sagi D, Nimtz M, Karst U, Peter-Katalinic J. 2003. Effects of buffering conditions and culture pH on production rates and glycosylation of clinical phase I anti-melanoma mouse IgG3 monoclonal antibody R24. Biotechnol Bioeng 83:321-334.
    • (2003) Biotechnol Bioeng , vol.83 , pp. 321-334
    • Muthing, J.1    Kemminer, S.E.2    Conradt, H.S.3    Sagi, D.4    Nimtz, M.5    Karst, U.6    Peter-Katalinic, J.7
  • 24
    • 80051798475 scopus 로고    scopus 로고
    • Effects of cell culture conditions on antibody N-linked glycosylation-what affects high mannose 5 glycoform
    • Pacis E, Yu M, Autsen J, Bayer R, Li F. 2011. Effects of cell culture conditions on antibody N-linked glycosylation-what affects high mannose 5 glycoform. Biotech Bioeng 108:2348-2358.
    • (2011) Biotech Bioeng , vol.108 , pp. 2348-2358
    • Pacis, E.1    Yu, M.2    Autsen, J.3    Bayer, R.4    Li, F.5
  • 25
    • 66949164842 scopus 로고    scopus 로고
    • OpenFLUX: Efficient modelling software for 13C-based metabolic flux analysis
    • Quek LE, Wittmann C, Nielsen LK, Kromer JO. 2009. OpenFLUX: Efficient modelling software for 13C-based metabolic flux analysis. Microb Cell Fact 8:25.
    • (2009) Microb Cell Fact , vol.8 , pp. 25
    • Quek, L.E.1    Wittmann, C.2    Nielsen, L.K.3    Kromer, J.O.4
  • 26
    • 48549090941 scopus 로고    scopus 로고
    • Terminal sugars of Fc glycans influence antibody effector functions of IgGs
    • Raju TS. 2008. Terminal sugars of Fc glycans influence antibody effector functions of IgGs. Curr Opin Immunol 20:471-478.
    • (2008) Curr Opin Immunol , vol.20 , pp. 471-478
    • Raju, T.S.1
  • 27
    • 84991918656 scopus 로고    scopus 로고
    • Enzyme Kinetics for Systems Biology. Ambrosius Publishing and Future Skill Software.
    • Sauro HM. 2011. Enzyme Kinetics for Systems Biology. Ambrosius Publishing and Future Skill Software.
    • (2011)
    • Sauro, H.M.1
  • 28
    • 13544265458 scopus 로고    scopus 로고
    • Modeling hybridoma cell metabolism using a generic genome-scale metabolic model of Mus musculus
    • Sheikh K, Forster J, Nielsen LK. 2005. Modeling hybridoma cell metabolism using a generic genome-scale metabolic model of Mus musculus. Biotechnol Prog 21:112-121.
    • (2005) Biotechnol Prog , vol.21 , pp. 112-121
    • Sheikh, K.1    Forster, J.2    Nielsen, L.K.3
  • 29
    • 84906780136 scopus 로고    scopus 로고
    • Recent advances in the understanding of biological implications and modulation methodologies of monoclonal antibody N-linked high mannose glycans
    • Shi HH, Goudar CT. 2014. Recent advances in the understanding of biological implications and modulation methodologies of monoclonal antibody N-linked high mannose glycans. Biotechnol Bioeng 111(10):1907-1919.
    • (2014) Biotechnol Bioeng , vol.111 , Issue.10 , pp. 1907-1919
    • Shi, H.H.1    Goudar, C.T.2
  • 30
    • 67449119292 scopus 로고    scopus 로고
    • Effects of glycosylation on the stability of protein pharmaceuticals
    • Sola RJ, Griebenow K. 2009. Effects of glycosylation on the stability of protein pharmaceuticals. J Pharm Sci 98:1223-1245.
    • (2009) J Pharm Sci , vol.98 , pp. 1223-1245
    • Sola, R.J.1    Griebenow, K.2
  • 31
    • 75149183678 scopus 로고    scopus 로고
    • Glycosylation of therapeutic proteins: An effective strategy to optimize efficacy
    • Sola RJ, Griebenow K. 2010. Glycosylation of therapeutic proteins: An effective strategy to optimize efficacy. BioDrugs 24:9-21.
    • (2010) BioDrugs , vol.24 , pp. 9-21
    • Sola, R.J.1    Griebenow, K.2
  • 32
    • 35248882544 scopus 로고    scopus 로고
    • Modulation of protein biophysical properties by chemical glycosylation: Biochemical insights and biomedical implications
    • Sola RJ, Rodriguez-Martinez JA, Griebenow K. 2007. Modulation of protein biophysical properties by chemical glycosylation: Biochemical insights and biomedical implications. Cell Mol Life Sci 64:2133-2152.
    • (2007) Cell Mol Life Sci , vol.64 , pp. 2133-2152
    • Sola, R.J.1    Rodriguez-Martinez, J.A.2    Griebenow, K.3
  • 33
    • 84878388792 scopus 로고    scopus 로고
    • Peak antibody production is associated with increased oxidative metabolism in an industrially relevant fed-batch CHO cell culture
    • Templeton N, Dean J, Reddy P, Young JD. 2013. Peak antibody production is associated with increased oxidative metabolism in an industrially relevant fed-batch CHO cell culture. Biotechnol Bioeng 110:2013-2024.
    • (2013) Biotechnol Bioeng , vol.110 , pp. 2013-2024
    • Templeton, N.1    Dean, J.2    Reddy, P.3    Young, J.D.4
  • 35
    • 33749860977 scopus 로고    scopus 로고
    • Post-translational modifications in the context of therapeutic proteins
    • Walsh G, Jefferis R. 2006. Post-translational modifications in the context of therapeutic proteins. Nat Biotech 24:1241-1252.
    • (2006) Nat Biotech , vol.24 , pp. 1241-1252
    • Walsh, G.1    Jefferis, R.2
  • 36
    • 84863440630 scopus 로고    scopus 로고
    • Production, characterization, and pharmacokinetic properties of antibodies with N-linked mannose-5 glycans
    • Yu M, Brown D, Reed C, Chung S, Lutman J, Stefanich E, Wong A, Stephan JP, Bayer R. 2012. Production, characterization, and pharmacokinetic properties of antibodies with N-linked mannose-5 glycans. MAbs 4:475-487.
    • (2012) MAbs , vol.4 , pp. 475-487
    • Yu, M.1    Brown, D.2    Reed, C.3    Chung, S.4    Lutman, J.5    Stefanich, E.6    Wong, A.7    Stephan, J.P.8    Bayer, R.9
  • 37
    • 81255197729 scopus 로고    scopus 로고
    • The impact of glycosylation on monoclonal antibody conformation and stability
    • Zheng K, Bantog C, Bayer R. 2011. The impact of glycosylation on monoclonal antibody conformation and stability. MAbs 3:568-576.
    • (2011) MAbs , vol.3 , pp. 568-576
    • Zheng, K.1    Bantog, C.2    Bayer, R.3


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