Production of analytical quantities of recombinant proteins in Chinese hamster ovary cells using sodium butyrate to elevate gene expression

Palermo, Daniel P.; DeGraaf, M.E.; Marotti, Keith R.; Rehberg, E; Post, Leonard

doi:10.1016/0168-1656(91)90073-5

Cited by 141 publications

(103 citation statements)

References 16 publications

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“…Approximately 67% of HeLa cells and 54% of CHO accumulated in the G1-phase following NaBu treatment (Xue and Rao 1981;Hendrick et al 2001). The specific and volumetric productivity were also increased (Palermo et al 1992;Hendrick et al 2001;Lee 2001, 2002;Lee and Lee 2003). However increased apoptosis was also observed in these cultures therefore undermining the beneficiary effects of improved productivity (Xue and Rao 1981;Chang et al 1999;Lee 2001, 2002).…”

Section: (Ii) Cell Engineering Based Approachesmentioning

confidence: 99%

Proliferation control strategies to improve productivity and survival during CHO based production culture

2007

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Chinese Hamster Ovary cells are the primary system for the production of recombinant proteins for therapeutic use. Protein productivity is directly proportional to viable biomass, viability and culture longevity of the producer cells and a number of approaches have been taken to optimise these parameters. Cell cycle arrest, particularly in G1 phase, typically using reduced temperature cultivation and nutritional control have been used to enhance productivity in production cultures by prolonging the production phase, but the mechanism by which these approaches work is still not fully understood. In this article, we analyse the public literature on proliferation control approaches as they apply to production cell lines with particular reference to what is known about the mechanisms behind each approach.

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Section: (Ii) Cell Engineering Based Approachesmentioning

confidence: 99%

Proliferation control strategies to improve productivity and survival during CHO based production culture

2007

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“…DMSO treatment can have a stimulatory effect on protein expression in animal cells (14,15) while sodium butyrate has been known to increase recombinant protein expression in animal cells (16,17). Although the mechanism of DMSO and sodium butyrate-mediated induction of protein expression is not clearly defined, DMSO is suggested to improve recombinant protein production by increasing the stability of the recombinant protein or by increasing transcription efficiency a The content of recombinant VP1 obtained from medium fraction of non-treated cultures was represented as 100.…”

Section: Resultsmentioning

confidence: 99%

Enhancement of Protein Productivity of Recombinant Hepatitis A Virus VP1 in Stably TransfectedDrosophila melanogasterS2 Cells

et al. 2012

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The effect of DMSO and sodium butyrate on the production of recombinant hepatitis A virus (HAV) capsid protein VP1 was evaluated and optimized in the culture of stably transfected Drosophila melanogaster S2 cells using culture plates and spinner flasks. The effect of DMSO and sodium butyrate was also evaluated to improve the recombinant VP1 production in stably transfected Drosophila S2 cells. A production level of 0.88 mg of recombinant VP1/liter was obtained in the culture-plate culture of stably transfected S2 cells at 6 days after induction with 0.5 mM CuSO 4 . The supplements of 2% DMSO and 10 mM sodium butyrate at 4 days post-inoculation increased recombinant VP1 accumulation by 141 and 104%, respectively, resulting in 2.17 and 1.7 mg/liter of recombinant VP1 production. In spinner flasks, recombinant VP1 production reached maximum level at 9 days after induction with 0.5 mM CuSO 4 , with approximately 4.96 mg/liter of recombinant VP1 production level. When 2% DMSO or 10 mM sodium butyrate was added at 5 days post-inoculation, the recombinant VP1 production was increased to 8.35 and 5.85 mg/liter, respectively. However, the synergistic effects of DMSO and sodium butyrate were not observed. These results indicate that DMSO and/or sodium butyrate can be successfully used to improve the recombinant HAV VP1 production in culture plates and spinner flasks.

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“…Sodium butyrate는 가장 널리 사용되는 SME 중 하나 로, 동물세포배양을 이용하여 tPA [9], α 1 -antitrypsin [10], hEPO [11], scu-PA [12], immunoglobulin [13] Fig. 3(a) .…”

Section: 서론unclassified

Enhanced Production of hCTLA4Ig by Adding Sodium Butyrate and Sodium Pyruvate

유미희¹,

김수진²,

권준영³

et al. 2011

KSBB Journal

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1) Human cytotoxic T-lymphocyte antigen 4-immunoglobulin (hCTLA4Ig), an immunosuppressive agent, was expressed in transgenic rice cells using RAmy3D promoter and RAmy1A signal peptide for the inducible production and secretion into culture media by sugar depletion. In this study, sodium butyrate was used as a small molecular enhancer (SME) to enhance the production of hCTLA4Ig in transgenic rice cell suspension cultures. When 1 mM sodium butyrate was added in sugar-free media, relative viability was not reduced, while the productivity was improved 1.3-fold. In addition, by supplementing 87 mM sodium pyruvate as an alternative energy source during the production phase, death rate of the cells was decreased. When sodium pyruvate was not added, most cells became dead at day 6. However, by adding sodium pyruvate, 18% of viability can be maintained until day 10 and the production of hCTLA4Ig was enhanced 1.4-fold. When the combination of sodium pyruvate and sodium butyrate at optimum concentrations was added, the highest viability and hCTLA4Ig production could be obtained.

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Production of analytical quantities of recombinant proteins in Chinese hamster ovary cells using sodium butyrate to elevate gene expression

Cited by 141 publications

References 16 publications

Proliferation control strategies to improve productivity and survival during CHO based production culture

Proliferation control strategies to improve productivity and survival during CHO based production culture

Enhancement of Protein Productivity of Recombinant Hepatitis A Virus VP1 in Stably TransfectedDrosophila melanogasterS2 Cells

Enhanced Production of hCTLA4Ig by Adding Sodium Butyrate and Sodium Pyruvate

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