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

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Remodeling of the major mouse xenoantigen, Galα1-3Galβ1-4GlcNAc-R, by N-acetylglucosaminyltransferase-III
T W Chung; K S Kim; S K Kang; Jeong Woong Lee; Eun Young Song; T H Chung; Young Il Yeom; C H Kim
Bibliographic Citation
Molecules and Cells, vol. 16, no. 3, pp. 343-353
Publication Year
β-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.
GnT-IIIn-acetylglucosaminen-glycosylationtransgenic micexenotransplantation
Korea Soc-Assoc-Inst
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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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