Polylactosamine synthesis and branch formation of N-glycans in β1,4-galactosyltransferase-1-deficient mice

被引:6
|
作者
Kotani, N
Asano, M
Inoue, N
Iwakura, Y
Takasaki, S
机构
[1] Univ Tokyo, Inst Med Sci, Div Biochem, Minato Ku, Tokyo 1088639, Japan
[2] Univ Tokyo, Inst Med Sci, Ctr Med Expt, Minato Ku, Tokyo 1088639, Japan
[3] Kirin Brewery Co Ltd, R&D Ctr, Div Pharmaceut, Gunma 3700013, Japan
关键词
beta; 4GalT-1; knockout; galactosylation; polylactosainines; branch formation;
D O I
10.1016/j.abb.2004.03.001
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Analysis of glycans from erythrocyte membrane glycoproteins from beta(1),4-galactosyltransferase-1 (beta4GAlT-1)-deficient mice revealed moderately decreased galactosylation but comparable polylactosamine content compared to control beta4GalT-1(+/-) mice. The increased expression of more branched N-glycans was observed in beta4GalT-1(-/-) mice, and its extent was more remarkable in elder beta4GalT-1(-/-) mice (28 weeks old) than in younger beta4GalT-1(-/-) mice (6-9 weeks old). In relation to this issue, the less galactosylation of biantennary glycans was observed in the elder group, suggesting that beta4GalTs actually compete with N-acetyl-ghucosatminyltransferases IV and V in erythroid cells. In contrast, approximately 80% of core 2 O-glycans were not beta1,4-galactosylated regardless of age of the knockout mice. These results suggest that beta4GalT-1 expressed in erythroid cells may regulate a constant branch formation of N-glycans and plays a predominant role in beta1,4-galactosylation of core 2 O-glyean. (C) 2004 Elsevier Inc. All rights reserved.
引用
收藏
页码:258 / 265
页数:8
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