Enhanced sialylation of recombinant erythropoietin in genetically engineered Chinese-hamster ovary cells

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dc.contributor.authorJeong, Yeon Taeko
dc.contributor.authorChoi, Oneko
dc.contributor.authorSon, Young Dokko
dc.contributor.authorPark, Seung Yeolko
dc.contributor.authorKim, Jung Hoeko
dc.date.accessioned2010-05-14T02:19:19Z-
dc.date.available2010-05-14T02:19:19Z-
dc.date.created2012-02-06-
dc.date.created2012-02-06-
dc.date.issued2009-04-
dc.identifier.citationBIOTECHNOLOGY AND APPLIED BIOCHEMISTRY, v.52, no.4, pp.283 - 291-
dc.identifier.issn0885-4513-
dc.identifier.urihttp://hdl.handle.net/10203/18320-
dc.description.abstractSialic acid, the terminal sugar in N-linked complex glycans, is usually found in glycoproteins and plays a major role in determining the circulatory lifespan of glycoproteins. In the present study we attempted to enhance the sialylation of recombinant EPO (erythropoietin) in CHO (Chinese-hamster ovary) cells. To enhance EPO sialylation, we introduced human alpha 2,3-ST (alpha 2,3-sialyltransferase) and CMP-SAS (CMP-sialic acid synthase) into recombinant human EPO-producing CHO cells. The sialylation of EPO was increased by the expression of alpha 2,3-ST alone. Although the co-expression of alpha 2,3-ST and CMP-SAS did not further increase sialylation, an increase in the intracellular pool of CMP-sialic acid was noted. On the basis of these observations, it was postulated that the transport capacity of CMP-sialic acid into the Golgi lumen was limited, thereby causing the reduced availability of CMP-sialic acid substrate for sialylation. Therefore, we co-expressed human alpha 2,3-ST and CMP-SAS, as well as overexpress Chinese hamster CMP-sialic acid transporter (CMP-SAT) in CHO cells, which produced recombinant human EPO. When alpha 2,3-ST, CMP-SAS, and CMP-SAT were overexpressed in CHO cells, there was a corresponding increase in siallylation compared with the co-expression of alpha 2,3-ST and CMP-SAS. The present study provides a useful strategy for enhancing the sialylation of therapeutic glycoproteins produced in CHO cells.-
dc.description.sponsorshipThis work was supported by the Korea Science and Engineering Foundation [grant no. M10619000005-07N1900-00511].en
dc.languageEnglish-
dc.language.isoen_USen
dc.publisherPORTLAND PRESS LTD-
dc.subjectCMP-SIALIC ACID-
dc.subjectACETYLGLUCOSAMINE 2-EPIMERASE/N-ACETYLMANNOSAMINE KINASE-
dc.subjectPERFORMANCE LIQUID-CHROMATOGRAPHY-
dc.subjectN-ACETYLNEURAMINIC ACID-
dc.subjectINTERFERON-GAMMA-
dc.subjectINSECT CELLS-
dc.subjectCHO-CELLS-
dc.subjectMETABOLIC CONTROL-
dc.subjectSUGAR CHAINS-
dc.subjectGLYCOSYLATION-
dc.titleEnhanced sialylation of recombinant erythropoietin in genetically engineered Chinese-hamster ovary cells-
dc.typeArticle-
dc.identifier.wosid000264903400004-
dc.identifier.scopusid2-s2.0-66149104098-
dc.type.rimsART-
dc.citation.volume52-
dc.citation.issue4-
dc.citation.beginningpage283-
dc.citation.endingpage291-
dc.citation.publicationnameBIOTECHNOLOGY AND APPLIED BIOCHEMISTRY-
dc.identifier.doi10.1042/BA20080044-
dc.embargo.liftdate9999-12-31-
dc.embargo.terms9999-12-31-
dc.contributor.localauthorKim, Jung Hoe-
dc.contributor.nonIdAuthorJeong, Yeon Tae-
dc.contributor.nonIdAuthorChoi, One-
dc.contributor.nonIdAuthorSon, Young Dok-
dc.contributor.nonIdAuthorPark, Seung Yeol-
dc.type.journalArticleArticle-
dc.subject.keywordAuthorChinese-hamster ovary cells (CHO cells)-
dc.subject.keywordAuthorCIMP-sialic acid synthase-
dc.subject.keywordAuthorCMP-sialic acid transporter-
dc.subject.keywordAuthorerythropoietin-
dc.subject.keywordAuthorsialylation-
dc.subject.keywordAuthorsialyltransferase-
dc.subject.keywordPlusCMP-SIALIC ACID-
dc.subject.keywordPlusACETYLGLUCOSAMINE 2-EPIMERASE/N-ACETYLMANNOSAMINE KINASE-
dc.subject.keywordPlusPERFORMANCE LIQUID-CHROMATOGRAPHY-
dc.subject.keywordPlusN-ACETYLNEURAMINIC ACID-
dc.subject.keywordPlusINTERFERON-GAMMA-
dc.subject.keywordPlusINSECT CELLS-
dc.subject.keywordPlusCHO-CELLS-
dc.subject.keywordPlusMETABOLIC CONTROL-
dc.subject.keywordPlusSUGAR CHAINS-
dc.subject.keywordPlusGLYCOSYLATION-
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