Reduced glutamine concentration improves protein production in growth-arrested CHO-DG44 and HEK-293E cells |
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Authors: | Yashas Rajendra Divor Kiseljak Lucia Baldi David L Hacker Florian M Wurm |
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Institution: | (1) Laboratory for Cellular Biotechnology (LBTC), ?cole Polytechnique F?d?ral de Lausanne (EPFL), 1015 Lausanne, Switzerland;(2) EPFL SV-IBI-LBTC, CH J2-506 (Building CH), Station 6, 1015 Lausanne, Switzerland; |
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Abstract: | For most cultivated mammalian cells, glutamine is an essential medium component. However, glutamine consumption results in
the production of ammonia, a cytotoxic byproduct. Here we investigated the effect of glutamine reduction on recombinant protein
production and ammonia accumulation in transiently transfected CHO and HEK-293E cells maintained under conditions of growth
arrest. Maximum transient recombinant protein yields were observed in HEK-293E cultures without glutamine and in CHO cultures
with 2 mM glutamine. The initial concentration of glutamine correlated with the level of ammonia accumulation in each culture.
For both a stable CHO-derived cell line and a polyclonal population of recombinant CHO cells grown under conditions of mild
hypothermia, the highest volumetric protein productivity was observed in cultures without glutamine. Here, the level of ammonia
accumulation also corresponded to the initial glutamine concentration. Our data demonstrate that reduction of glutamine in
the medium is an effective approach to improve protein production in both transiently and stably transfected mammalian cells
when applying conditions that reduce or arrest the growth of these cells. |
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