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Publication : Polylactosamine synthesis and branch formation of N-glycans in beta1,4-galactosyltransferase-1-deficient mice.

First Author  Kotani N Year  2004
Journal  Arch Biochem Biophys Volume  426
Issue  2 Pages  258-65
PubMed ID  15158676 Mgi Jnum  J:90896
Mgi Id  MGI:3045482 Doi  10.1016/j.abb.2004.03.001
Citation  Kotani N, et al. (2004) Polylactosamine synthesis and branch formation of N-glycans in beta1,4-galactosyltransferase-1-deficient mice. Arch Biochem Biophys 426(2):258-65
abstractText  Analysis of glycans from erythrocyte membrane glycoproteins from beta1,4-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-acetylglucosaminyltransferases 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-glycan.
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