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Title 

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

Authors 

T W ChungK S KimS K KangJeong Woong LeeEun Young SongT H ChungYoung Il YeomC H Kim

Publisher 

Springer Verlag (Germany)

Issue Date 

2003

Citation 

Molecules and Cells, vol. 16, no. 3, pp. 343-353

Keywords 

GnT-IIIn-acetylglucosaminen-glycosylationtransgenic micexenotransplantationalbuminalpha 1,3 galactosyltransferasealpha 6 dextro mannoside beta 1,6 n acetylglucosaminyltransferase vbeta dextro mannoside beta 1,4 n acetylglucosaminyltransferase iiin acetylglucosamine

Abstract 

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.

ISSN 

1016-8478

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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