Microbioreactors and Scale-Down Models: Growth of CHO Cells Using the Pall Micro24 MicroReactor System

2013 ◽  
pp. 149-165 ◽  
Author(s):  
Steve R. C. Warr
Keyword(s):  
Cho Cells ◽  
Scale Down

Reconstruction of Industrial Processes for Cultivating CHO Cells in a Scale-Down Bioreactor Model

2021 ◽  
Vol 37 (4) ◽  
pp. 112-122
Author(s):  
A.N. Morozov ◽  
Z.V. Zakharov ◽  
S.V. Kalenov ◽  
R.A. Khamitov
Keyword(s):  
Monoclonal Antibodies ◽  
Production Process ◽  
Cho Cells ◽  
International Standards ◽  
Specific Power ◽  
Laboratory Model ◽  
Production Volume ◽  
Working Volume ◽  
Scale Down

According to generally accepted international standards, the characterization and confirmation of the quality of biological pharmaceutical substances requires the use of not only a combination of physicochemical and biological tests, but also an in-depth knowledge of the production process and its control. The study of such an industrial process involves considerable expenditure of time and material resources. Gaining a deep knowledge of the production process is greatly facilitated by using laboratory models of industrial installations that effectively reproduce large-scale processes in a research laboratory. On the basis of a laboratory bioreactor for the cultivation of eukaryotic cells with a working volume of 2 L, a scale-down model of a pilot bioreactor has been developed, linearly scalable to a production volume of 1000 L. The laboratory model reproduces the key parameters of cultivation on a pilot scale: the ratio of the geometric dimensions of the reactor, the peripheral speed of the mixer, the specific power input, the coefficient of oxygen mass transfer, the type and intensity of aeration, strategies for defoaming, feeding and maintaining the pH level. Experiments using the developed model showed high similarity in the kinetics of cell growth, productivity and quality of the expressed monoclonal antibodies in laboratory and pilot bioreactors. Key words: cultivation, CHO cells, monoclonal antibodies, scale-down model

A predictive high-throughput scale-down model of monoclonal antibody production in CHO cells

2009 ◽  
Vol 104 (6) ◽  
pp. 1107-1120 ◽  
Author(s):  
Rachel Legmann ◽  
H. Brett Schreyer ◽  
Rodney G. Combs ◽  
Ellen L. McCormick ◽  
A. Peter Russo ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
High Throughput ◽  
Antibody Production ◽  
Cho Cells ◽  
Monoclonal Antibody Production ◽  
Scale Down

Metabolic engineering of CHO cells to prepare glycoproteins

2018 ◽  
Vol 2 (3) ◽  
pp. 433-442 ◽  
Author(s):  
Qiong Wang ◽  
Michael J. Betenbaugh
Keyword(s):  
Metabolic Engineering ◽  
Cho Cells ◽  
Genetic Manipulation ◽  
Chinese Hamster ◽  
Post Translational Modification ◽  
Effector Functions ◽  
Recombinant Glycoproteins ◽  
Production Platform ◽  
Chemical Inhibitors ◽  
Amino Acid Mutations

As a complex and common post-translational modification, N-linked glycosylation affects a recombinant glycoprotein's biological activity and efficacy. For example, the α1,6-fucosylation significantly affects antibody-dependent cellular cytotoxicity and α2,6-sialylation is critical for antibody anti-inflammatory activity. Terminal sialylation is important for a glycoprotein's circulatory half-life. Chinese hamster ovary (CHO) cells are currently the predominant recombinant protein production platform, and, in this review, the characteristics of CHO glycosylation are summarized. Moreover, recent and current metabolic engineering strategies for tailoring glycoprotein fucosylation and sialylation in CHO cells, intensely investigated in the past decades, are described. One approach for reducing α1,6-fucosylation is through inhibiting fucosyltransferase (FUT8) expression by knockdown and knockout methods. Another approach to modulate fucosylation is through inhibition of multiple genes in the fucosylation biosynthesis pathway or through chemical inhibitors. To modulate antibody sialylation of the fragment crystallizable region, expressions of sialyltransferase and galactotransferase individually or together with amino acid mutations can affect antibody glycoforms and further influence antibody effector functions. The inhibition of sialidase expression and chemical supplementations are also effective and complementary approaches to improve the sialylation levels on recombinant glycoproteins. The engineering of CHO cells or protein sequence to control glycoforms to produce more homogenous glycans is an emerging topic. For modulating the glycosylation metabolic pathways, the interplay of multiple glyco-gene knockouts and knockins and the combination of multiple approaches, including genetic manipulation, protein engineering and chemical supplementation, are detailed in order to achieve specific glycan profiles on recombinant glycoproteins for superior biological function and effectiveness.

Cell-specific regulation of IRS-1 gene expression: role of E box and C/EBP binding site in HepG2 cells and CHO cells

Diabetes ◽  
1997 ◽  
Vol 46 (3) ◽  
pp. 354-362 ◽  
Author(s):  
K. Matsuda ◽  
E. Araki ◽  
R. Yoshimura ◽  
K. Tsuruzoe ◽  
N. Furukawa ◽  
...  
Keyword(s):  
Gene Expression ◽  
Binding Site ◽  
Cho Cells ◽  
Hepg2 Cells ◽  
E Box ◽  
Specific Regulation

Optimization of Perfusion Rate Acceleration is a Key Stage in Development of Highly Productive Perfusion Cultivation of CHO Cells

2016 ◽  
Vol 32 (4) ◽  
pp. 60-67
Author(s):  
A. N. MOROZOV ◽  
Z. V. ZAKHAROV ◽  
R. A. KOCHELABOV ◽  
D. V. TYUPA ◽  
A. V. ISERKAPOV ◽  
...  
Keyword(s):  
Cho Cells ◽  
Perfusion Rate ◽  
Rate Acceleration ◽  
Perfusion Cultivation
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