High-throughput clonal selection of recombinant CHO cells using a dominant selectable and amplifiable metallothionein-GFP fusion protein

2002 ◽  
Vol 80 (6) ◽  
pp. 670-676 ◽  
Author(s):  
Charles G. Bailey ◽  
A. Sasha Tait ◽  
Noelle-Ann Sunstrom
Keyword(s):  
Fusion Protein ◽  
High Throughput ◽  
Cho Cells ◽  
Clonal Selection ◽  
Recombinant Cho Cells ◽  
Gfp Fusion Protein ◽  
Selection Of

Clonal selection of high producing, stably transfected HEK293 cell lines utilizing modified, high-throughput FACS screening

2011 ◽  
Vol 86 (7) ◽  
pp. 935-941 ◽  
Author(s):  
Michael Song ◽  
Kristin Raphaelli ◽  
Martina L. Jones ◽  
Khosrow Aliabadi-Zadeh ◽  
Kar Man Leung ◽  
...  
Keyword(s):  
Cell Lines ◽  
High Throughput ◽  
Hek293 Cell ◽  
Clonal Selection ◽  
Transfected Hek293 Cell ◽  
Selection Of

Accelerated Clone Selection for Recombinant CHO Cells Using a FACS-Based High-Throughput Screen

2007 ◽  
Vol 23 (2) ◽  
pp. 465-472 ◽  
Author(s):  
C.T. DeMaria ◽  
V. Cairns ◽  
C. Schwarz ◽  
J. Zhang ◽  
M. Guerin ◽  
...  
Keyword(s):  
High Throughput ◽  
Cho Cells ◽  
High Throughput Screen ◽  
Clone Selection ◽  
Recombinant Cho Cells ◽  
Selection For

scholarly journals A GFP-based method facilitates clonal selection of transfected CHO cells

2010 ◽  
Vol 5 (1) ◽  
pp. 24-31 ◽  
Author(s):  
Denise Freimark ◽  
Valèrie Jèrôme ◽  
Ruth Freitag
Keyword(s):  
Cho Cells ◽  
Clonal Selection ◽  
Selection Of

A novel control scheme for inducing angiostatin-human IgG fusion protein production using recombinant CHO cells in a oscillating bioreactor

2006 ◽  
Vol 121 (3) ◽  
pp. 418-428 ◽  
Author(s):  
Ing-Kae Wang ◽  
Sing-Ying Hsieh ◽  
King-Ming Chang ◽  
Yu-Chi Wang ◽  
Andy Chu ◽  
...  
Keyword(s):  
Fusion Protein ◽  
Cho Cells ◽  
Protein Production ◽  
Human Igg ◽  
Recombinant Cho Cells ◽  
Control Scheme

Inhibition of clathrin-coated pit assembly by an Eps15 mutant

1999 ◽  
Vol 112 (9) ◽  
pp. 1303-1311 ◽  
Author(s):  
A. Benmerah ◽  
M. Bayrou ◽  
N. Cerf-Bensussan ◽  
A. Dautry-Varsat
Keyword(s):  
Plasma Membrane ◽  
Fusion Protein ◽  
Binding Site ◽  
Specific Marker ◽  
Coated Pits ◽  
Receptor Mediated Endocytosis ◽  
Gfp Fusion Protein ◽  
Protein Encoding ◽  
Homology Domains

Recent data have shown that Eps15, a newly identified component of clathrin-coated pits constitutively associated with the AP-2 complex, is required for receptor-mediated endocytosis. However, its precise function remains unknown. Interestingly, Eps15 contains three EH (Eps15-Homology) domains also found in proteins required for the internalization step of endocytosis in yeast. Results presented here show that EH domains are required for correct coated pit targeting of Eps15. Furthermore, when cells expressed an Eps15 mutant lacking EH domains, the plasma membrane punctate distribution of both AP-2 and clathrin was lost, implying the absence of coated pits. This was further confirmed by the fact that dynamin, a GTPase found in coated pits, was homogeneously redistributed on the plasma membrane and that endocytosis of transferrin, a specific marker of clathrin-dependent endocytosis, was strongly inhibited. Altogether, these results strongly suggest a role for Eps15 in coated pit assembly and more precisely a role for Eps15 in the docking of AP-2 onto the plasma membrane. This hypothesis is supported by the fact that a GFP fusion protein encoding the ear domain of (alpha)-adaptin, the AP-2 binding site for Eps15, was efficiently targeted to plasma membrane coated pits.

Expression of human Mn SOD in Chinese hamster ovary cells confers protection from oxidant injury

1993 ◽  
Vol 264 (6) ◽  
pp. L598-L605
Author(s):  
B. Warner ◽  
R. Papes ◽  
M. Heile ◽  
D. Spitz ◽  
J. Wispe
Keyword(s):  
Chinese Hamster Ovary ◽  
Cho Cells ◽  
Chinese Hamster Ovary Cells ◽  
Lethal Dose ◽  
Chinese Hamster ◽  
Eukaryotic Expression ◽  
Wild Type ◽  
Oxidant Injury ◽  
Sod Activity ◽  
Recombinant Cho Cells

Manganese superoxide dismutase (Mn SOD) is an important component of antioxidant defense in aerobic cells because of its location in the mitochondria, a significant source of oxygen radicals and an important target of oxidant injury. To test the hypothesis that increased mitochondrial Mn SOD protects from oxidant injury, Chinese hamster ovary (CHO) cells were transfected with a eukaryotic expression vector containing the human Mn SOD cDNA. In recombinant CHO cells, Mn SOD activity was increased threefold over wild-type controls. Acute survival during paraquat exposure (0–500 microM) was significantly improved in CHO cells expressing human Mn SOD, with 71% of recombinant CHO cells surviving at the 50% lethal dose (LD50) for wild-type CHO controls. Cell growth following exposure to paraquat (100 microM) was also significantly improved in recombinant CHO cells. CHO cells expressing human Mn SOD continued to grow and divide after paraquat exposure, whereas growth of wild-type CHO cells was negligible. Protection against oxidant-induced injury was directly related to increased Mn SOD, occurring in the absence of changes in other antioxidant enzymes including catalase, Cu,Zn SOD, and glutathione associated cellular antioxidant mechanisms. We conclude that increased expression of human Mn SOD in vitro directly confers protection against oxidant injury.

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