Efficient long-term and high-yielded production of a recombinant proteoglycan in eukaryotic HEK293 cells using a membrane-based bioreactor

• Published in: Biochemical and biophysical research communications Vol. 369; no. 2; pp. 297 - 302
• Main Authors: Adam, Estelle, Sarrazin, Stéphane, Landolfi, Cindy, Motte, Vincent, Lortat-Jacob, Hugues, Lassalle, Philippe, Delehedde, Maryse
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 02.05.2008; Elsevier
• Subjects: Biochemistry, Molecular Biology; Bioreactor CELLine; Bioreactors; Cell Culture Techniques - methods; Cell Line; Endocan; Glycosylation; High density cell culture; Humans; Kidney - physiology; Life Sciences; Membranes, Artificial; Neoplasm Proteins - biosynthesis; Neoplasm Proteins - genetics; Protein Engineering - methods; Proteoglycan; Proteoglycans - biosynthesis; Proteoglycans - genetics; Recombinant Proteins - biosynthesis; Proteoglycan; Bioreactor CELLine; Glycosylation; Endocan; High density cell culture
• ISSN: 0006-291X; 1090-2104
• DOI: 10.1016/j.bbrc.2008.01.141

Standard culture systems of eukaryotic cells generally failed to deliver sufficient amounts of recombinant proteins without increasing the costs of production. We here showed that membrane-based bioreactors, initially developed for the production of monoclonal antibodies, can be very useful for the production using engineered HEK293 cells, of a recombinant proteoglycan called endocan, with achievement of high level expression and efficient long-term production. When compared to standard procedures, the growth in suspension and at high density of these cells in one bioreactor promoted a 60-fold increase of the concentration of the soluble recombinant endocan. These culture conditions did not affect cell viability, stable expression, recognition by specific monoclonal antibodies or electrophoretic profile of the recombinant endocan. Such an easy to scale up system to produce recombinant protein should open soon new opportunities to study structure and functions of endocan or any other glycosylated cell products newly investigated.