| First Author | Sugahara D | Year | 2012 |
| Journal | Sci Rep | Volume | 2 |
| Pages | 680 | PubMed ID | 23002422 |
| Mgi Jnum | J:207268 | Mgi Id | MGI:5555000 |
| Doi | 10.1038/srep00680 | Citation | Sugahara D, et al. (2012) Large-scale identification of target proteins of a glycosyltransferase isozyme by Lectin-IGOT-LC/MS, an LC/MS-based glycoproteomic approach. Sci Rep 2:680 |
| abstractText | Model organisms containing deletion or mutation in a glycosyltransferase-gene exhibit various physiological abnormalities, suggesting that specific glycan motifs on certain proteins play important roles in vivo. Identification of the target proteins of glycosyltransferase isozymes is the key to understand the roles of glycans. Here, we demonstrated the proteome-scale identification of the target proteins specific for a glycosyltransferase isozyme, beta1,4-galactosyltransferase-I (beta4GalT-I). Although beta4GalT-I is the most characterized glycosyltransferase, its distinctive contribution to beta1,4-galactosylation has been hardly described so far. We identified a large number of candidates for the target proteins specific to beta4GalT-I by comparative analysis of beta4GalT-I-deleted and wild-type mice using the LC/MS-based technique with the isotope-coded glycosylation site-specific tagging (IGOT) of lectin-captured N-glycopeptides. Our approach to identify the target proteins in a proteome-scale offers common features and trends in the target proteins, which facilitate understanding of the mechanism that controls assembly of a particular glycan motif on specific proteins. |
