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논문 기본 정보
- 자료유형
- 학술저널
- 저자정보
- 발행연도
- 2019.6
- 수록면
- 73 - 79 (7page)
- DOI
- 10.7841/ksbbj.2019.34.2.73
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초록· 키워드
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Sialylation is very important for in vivo half-life of therapeutic proteins because sialic acids can reduce the rates of clearance in hepatocyte. Many studies were developed for supplementing various carbon sources which directly influcenced cellular metabolism and glycosylation. So it is necessary to investigate interconversion of carbons sources in combination because once they are absorbed into cells and synthesized into nucleotide sugars, they can be converted to different kinds of sugars and nucleotide sugars. Albumin-erythropoietin (Alb-EPO) has three glycan sites with tetra-antennary structure, so it can be added up to 14 sialic acids. Therefore, we demonstrated the effects of combination ratios of hexose (glucose:galactose:mannose) among the generally used carbon sources essential for cell growth on sialylation of a fusion protein, Alb-EPO. As a result, there was no negative effect on cell growth except the condition of the highest concentration. The titer of Alb-EPO was increased depending on increasing concentration of hexoses in order of mannose, glucose, and galactose and reached up to 1.7-fold in comparison to the control. On the other hand, there was more than 1.5-fold increase in sialylation followed by changed nucleotide sugar pool at the conditions supplemented with glucose and galactose at high concentration. In conclusion, our strategy of controlling the concentrations of available carbon sources offers an effective approach for the improved production of highly sialylated Alb-EPO without deleterious effect on growth.
목차
Abstract
1. INTRODUCTION
2. MATERIALS AND METHODS
3. RESULTS AND DISCUSSION
4. CONCLUSION
REFERENCES
참고문헌 (12)
참고문헌 신청
Kwak, C. Y. / 2017 / Enhancing the sialylation of recombinant EPO produced in CHO cells via the inhibition of glycosphingolipid biosynthesis / Sci. Rep 7:13059
Schriebl, K. / 2006 / Biochemical characterization of rhEpo-Fc fusion protein expressed in CHO cells / Protein expres. Purif 49:265~275
Sha, S. / 2016 / Nglycosylation design and control of therapeutic monoclonal antibodies / Trends Biotechnol 34:835~346
Blondeel, E. J. / 2018 / Supplementing glycosylation:A review of applying nucleotide-sugar precursors to growth medium to affect therapeutic recombinant protein glycoform distributions / Biotechnol. Adv 36:1505~1523
Wong, D. C. F. / 2005 / Impact of dynamic online fed-batch strategies on metabolism, productivity and N-glycosylation quality in CHO cell cultures / Biotechnol. Bioeng 89:164~177
Schriebl, K. / 2006 / Biochemical characterization of rhEpo-Fc fusion protein expressed in CHO cells / Protein expres. Purif 49:265~275
Sha, S. / 2016 / Nglycosylation design and control of therapeutic monoclonal antibodies / Trends Biotechnol 34:835~346
Blondeel, E. J. / 2018 / Supplementing glycosylation:A review of applying nucleotide-sugar precursors to growth medium to affect therapeutic recombinant protein glycoform distributions / Biotechnol. Adv 36:1505~1523
Wong, D. C. F. / 2005 / Impact of dynamic online fed-batch strategies on metabolism, productivity and N-glycosylation quality in CHO cell cultures / Biotechnol. Bioeng 89:164~177
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UCI(KEPA) : I410-ECN-0101-2019-470-000905203