| First Author | Kotani N | Year | 1999 |
| Journal | Biochem Biophys Res Commun | Volume | 260 |
| Issue | 1 | Pages | 94-8 |
| PubMed ID | 10381349 | Mgi Jnum | J:55876 |
| Mgi Id | MGI:1339510 | Doi | 10.1006/bbrc.1999.0872 |
| Citation | Kotani N, et al. (1999) Impaired galactosylation of core 2 O-glycans in erythrocytes of beta1,4-galactosyltransferase knockout mice. Biochem Biophys Res Commun 260(1):94-8 |
| abstractText | O- and N-glycans included in erythrocyte membrane glycoproteins from beta1,4-galactosyltransferase I (GalT-I) knockout mice were analyzed to examine how this enzyme deficiency affects glycosylation of proteins in erythroid cells. The results indicated that greater than 80% of core 2 O-glycans from GalT-I-/- mice are not galactosylated by beta1,4 linkage, resulting in the expression of Neu5Acalpha2 --> 3Galbeta1 --> 3(GlcNAcbeta1 --> 6)GalNAc, while core 2 O-glycans from GalT-I+/+ mice are fully galactosylated and occur as Neu5Acalpha2 --> 3Galbeta1 --> 3(Neu5Acalpha2 --> 3 Galbeta1 --> 4GlcNAcbeta1 --> 6)GalNAc. On the other hand, beta1, 4-galactosylation of N-glycans of the mutant was approximately 60% that of the wild type. Thus, it is suggested that GalT-I is predominantly responsible for beta1,4-galactosylation of the core 2 O-glycan branch in erythroid cells. Copyright 1999 Academic Press. |
