Cytotechnology

, Volume 32, Issue 2, pp 109–123

Advances in animal cell recombinant protein production: GS-NS0 expression system

  • Louise M. Barnes
  • Catherine M. Bentley
  • Alan J. Dickson
Article

DOI: 10.1023/A:1008170710003

Cite this article as:
Barnes, L.M., Bentley, C.M. & Dickson, A.J. Cytotechnology (2000) 32: 109. doi:10.1023/A:1008170710003

Abstract

The production of recombinant proteins using mammalian cell expression systems is of growing importance within biotechnology, largely due to the ability of specific mammalian cells to carry out post-translational modifications of the correct fidelity. The Glutamine Synthetase-NS0 system is now one such industrially important expression system.Glutamine synthetase catalyses the formation ofglutamine from glutamate and ammonia. NS0 cellscontain extremely low levels of endogenous glutaminesynthetase activity, therefore exogenous glutaminesynthetase can be used efficiently as a selectablemarker to identify successful transfectants in theabsence of glutamine in the media. In addition, theinclusion of methionine sulphoximine, an inhibitor ofglutamine synthetase activity, enables furtherselection of those clones producing relatively highlevels of transfected glutamine synthetase and henceany heterologous gene which is coupled to it. Theglutamine synthetase system technology has been usedfor research and development purposes during thisdecade and its importance is clearly demonstrated nowthat two therapeutic products produced using thissystem have reached the market place.

gene amplification glutamine synthetase methioninesulphoximine NS0 productivity recombinant protein 

Copyright information

© Kluwer Academic Publishers 2000

Authors and Affiliations

  • Louise M. Barnes
    • 1
  • Catherine M. Bentley
    • 2
  • Alan J. Dickson
    • 3
  1. 1.2.205 School of Biological SciencesUniversity of ManchesterManchester
  2. 2.GlaxoWellcome Research and DevelopmentKentUK
  3. 3.2.205 School of Biological SciencesUniversity of ManchesterManchester

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