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用于重组蛋白生产的哺乳动物细胞表达新技术 被引量:1

Arising Technologies Applied in Mammalian Cell Expression for Recombinant Protein
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摘要 近年来,用于重组蛋白生产的哺乳动物细胞表达领域涌现出一系列革命性的新技术。优化的工程细胞为表达重组蛋白提供了优良的宿主;基于荧光的筛选方法可以快捷地得到高表达细胞株;高通量的培养工艺能够预测适合外源蛋白表达的细胞培养条件;可抛弃式生物反应器为大规模细胞培养提供了更多的选择;大规模瞬时表达技术节省了重组蛋白的生产时间。这些新技术提高了重组蛋白的研发和生产效率,加快了蛋白药物的工业化进程。 In recent years, some revolutionary new technologies in mammalian cell expression field have been developed for industrial recombinant protein production. Optimized engineered cells were applied to express recom- binant protein as more suitable hosts. High-expressing cell lines can be easily obtained through fluores- cence-based screening methods. The best conditions for expression of heterologous proteins were predicted by high-throughput culture platform. Disposable bioreactors can be developed as alternative facilities for large-scale cell culture. The manufacture period of recombinant proteins was saved due to large-scale transient expression technology. By means of these technologies, the efficiency of research and production was greatly improved to ac- celerate industrialization of protein drug.
出处 《生物技术通讯》 CAS 2012年第6期900-903,共4页 Letters in Biotechnology
基金 国家科技重大专项(2012ZX09103301-037)
关键词 重组蛋白 哺乳动物细胞表达 生物反应器 高通量筛选 recombinant protein mammalian cell expression bioreactor high-throughput screening
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  • 1Leader B, Baca Q J, Golan D E. Protein therapeutics: a summary and pharmacological classification[J]. Nat Rev Drug Discoy, 2008,7(1):21-39.
  • 2Mullard A. 2011 FDA drug approvals[J]. Nat Rev Drug Discov, 2012,11(2):91-94.
  • 3Zhu J. Mammalian cell protein expression for biopharmaceutical production[J]. Biotechnol Adv,2012,30(5):1158-1170.
  • 4Omasa T, Onitsuka M, Kim W D. Cell engineering and cultivation of chinese hamster ovary(CHO) cells[J]. Curr Pharm Biotechnol, 2010,11(3):233-240.
  • 5Tabuchi H, Sugiyama T, Tanaka S, et al. Overexpression of taurine transporter in Chinese hamster ovary cells can enhance cell viability and product yield, while promoting glutamine consumption[J]. Biotechnol Bioeng, 2010,107(6):998-1003.
  • 6Parampalli A, Eskridge K, Smith L, et al. Developement of serum-free media in CHO-DG44 cells using a central composite statistical design[J]. Cytotechnology, 2007,54(1):57-68.
  • 7Mohan C, Kim Y G, Koo J, et al. Assessment of cell engineering strategies for improved therapeutic protein production in CHO cells[J]. Biotechnol J, 2008,3(5):624-630.
  • 8Hermes P A, Castro C D. A fully defined, fed-batch, recombinant NS0 cuhure process for monoclonal antibody production [J]. Biotechnol Prog, 2010,26(5):1411-1416.
  • 9Browne S M, Al-Rubeai M. Analysis of an artificially selected GS-NS0 variant with increased resistance to apoptosis[J]. Biotechnol Bioeng, 2011,108(4):880-892.
  • 10Cacciatore J J, Chasin L A, Leonard E F. Gene amplification and vector engineering to achieve rapid and high-level therapeutic protein production using the Dhfr-based CHO cell selection system[J]. Biotechnol Adv, 2010,28(6):673-681.

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