| First Author | Kotani N | Year | 2001 |
| Journal | Biochem J | Volume | 357 |
| Issue | Pt 3 | Pages | 827-34 |
| PubMed ID | 11463354 | Mgi Jnum | J:70854 |
| Mgi Id | MGI:2148393 | Doi | 10.1042/0264-6021:3570827 |
| Citation | Kotani N, et al. (2001) Knockout of mouse beta 1,4-galactosyltransferase-1 gene results in a dramatic shift of outer chain moieties of N-glycans from type 2 to type 1 chains in hepatic membrane and plasma glycoproteins. Biochem J 357(Pt 3):827-34 |
| abstractText | To understand the contribution of beta 1,4-galactosyltransferase (beta 4Gal-T)-1 to galactosylation in vivo, N-glycans of hepatic membrane glycoproteins and plasma glycoproteins from beta 4Gal-T1 wild-type (beta 4Gal-T1(+/+)) and beta 4Gal-T1 knockout mice were compared. Unexpectedly, glycoproteins from the knockout mice were found to express considerable amounts of sialylated, galactosylated N-glycans. A striking contrast was that galactose residues were largely beta 1,4-linked to GlcNAc residues in the beta 4Gal-T1(+/+) mouse glycans but beta 1,3-linked in the knockout mouse glycans, thus resulting in the shift of the backbone structure from type 2 chain (Gal beta 1-->4GlcNAc) to type 1 chain (Gal beta 1-->3GlcNAc). Detailed analysis of plasma glycoproteins revealed that the expression of sialyl linkage in N-glycans was shifted from the Sia alpha 2-->6Gal to the Sia alpha 2-->3Gal, and oversialylated type 1 chains were, remarkably, found in the knockout mouse glycans. Thus beta 4Gal-T1 deficiency was primarily compensated for by beta1,3-galactosyltransferases, which resulted in different sialyl linkages being formed on the outer chains and altered backbone structures, depending on the acceptor specificities of sialyltransferases. These results suggest that beta 4Gal-T1 in mouse liver plays a central role in the synthesis of type 2 chain and is also involved in the regulation of sialylation of N-glycans. The knockout mice may prove useful in investigation of the mechanism which regulates the tissue-dependent terminal glycosylation. |
