Remodeling of the major mouse xenoantigen, Galα1-3Galβ1-4GlcNAc-R, by N-acetylglucosaminyltransferase-III

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dc.contributor.authorT W Chung-
dc.contributor.authorK S Kim-
dc.contributor.authorS K Kang-
dc.contributor.authorJeong Woong Lee-
dc.contributor.authorEun Young Song-
dc.contributor.authorT H Chung-
dc.contributor.authorYoung Il Yeom-
dc.contributor.authorC H Kim-
dc.date.accessioned2017-04-19T09:00:43Z-
dc.date.available2017-04-19T09:00:43Z-
dc.date.issued2003-
dc.identifier.issn1016-8478-
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/6376-
dc.description.abstractβ-D-Mannoside β-1,4-N-acetylglucosaminyltransferase III (GnT-III) catalyses the attachment of an N-acetylglucosamine (GlcNAc) residue to mannose in the β(1-4) configuration in N-glycans, and forms a bisecting GlcNAc. We have generated transgenic mice that contain the human GnT-III gene under the control of the mouse albumin enhancer/promoter [Lee et al., (2003)]. Overexpression of this gene in mice reduced the antigenicity of N-glycans to human natural antibodies, especially in the case of the α-Gal epitope, Galα1-3Galβ1-4GlcNAc-R. Study of endothelial cells from the GnT-III transgenic mice revealed a significant reduction in antigenicity, and a dramatic decrease in both complement- and natural killer cell-mediated mouse cell lysis. Changes in the enzymatic activities of other glycosyltransferases, such as α1,3-galactosyltransferase, and α-6-D-mannoside β-1,6 N-acetylglucosaminyltransferase V, did not point to any interaction between GnT-III and these enzymes in the transgenic mice, suggesting that this approach may be useful in clinical xenotransplantation.-
dc.publisherKorea Soc-Assoc-Inst-
dc.titleRemodeling of the major mouse xenoantigen, Galα1-3Galβ1-4GlcNAc-R, by N-acetylglucosaminyltransferase-III-
dc.title.alternativeRemodeling of the major mouse xenoantigen, Galα1-3Galβ1-4GlcNAc-R, by N-acetylglucosaminyltransferase-III-
dc.typeArticle-
dc.citation.titleMolecules and Cells-
dc.citation.number3-
dc.citation.endPage353-
dc.citation.startPage343-
dc.citation.volume16-
dc.contributor.affiliatedAuthorJeong Woong Lee-
dc.contributor.affiliatedAuthorEun Young Song-
dc.contributor.affiliatedAuthorYoung Il Yeom-
dc.contributor.alternativeName정태욱-
dc.contributor.alternativeName김경숙-
dc.contributor.alternativeName강성구-
dc.contributor.alternativeName이정웅-
dc.contributor.alternativeName송은영-
dc.contributor.alternativeName정태화-
dc.contributor.alternativeName염영일-
dc.contributor.alternativeName김철호-
dc.identifier.bibliographicCitationMolecules and Cells, vol. 16, no. 3, pp. 343-353-
dc.subject.keywordGnT-III-
dc.subject.keywordn-acetylglucosamine-
dc.subject.keywordn-glycosylation-
dc.subject.keywordtransgenic mice-
dc.subject.keywordxenotransplantation-
dc.subject.localGnT-III-
dc.subject.localN-acetylglucosamine-
dc.subject.localN-Acetylglucosamine-
dc.subject.localN-Acetylglucosamine (GlcNAc)-
dc.subject.localN-acetylglucosamine (GlcNAc)-
dc.subject.localn-acetylglucosamine-
dc.subject.localn-glycosylation-
dc.subject.localN-Glycosylation-
dc.subject.localN-glycosylation-
dc.subject.localtransgenic mice-
dc.subject.localTransgenic mice-
dc.subject.localTransgenic mouse-
dc.subject.localtransgenic mouse-
dc.subject.localXenotransplantation-
dc.subject.localxenotransplantation-
dc.description.journalClassY-
Appears in Collections:
Division of Biomedical Research > Biotherapeutics Translational Research Center > 1. Journal Articles
Division of Biomedical Research > Personalized Genomic Medicine Research Center > 1. Journal Articles
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