| First Author | Takeuchi T | Year | 2013 |
| Journal | Biochem Biophys Res Commun | Volume | 436 |
| Issue | 3 | Pages | 509-13 |
| PubMed ID | 23751344 | Mgi Jnum | J:204419 |
| Mgi Id | MGI:5532470 | Doi | 10.1016/j.bbrc.2013.05.135 |
| Citation | Takeuchi T, et al. (2013) Mammalian galectins bind galactosebeta1-4fucose disaccharide, a unique structural component of protostomial N-type glycoproteins. Biochem Biophys Res Commun 436(3):509-13 |
| abstractText | Galactosebeta1-4Fucose (Galbeta1-4Fuc) is a unique disaccharide exclusively found in N-glycans of protostomia, and is recognized by some galectins of Caenorhabditis elegans and Coprinopsis cinerea. In the present study, we investigated whether mammalian galectins also bind such a disaccharide. We examined sugar-binding ability of human galectin-1 (hGal-1) and found that hGal-1 preferentially binds Galbeta1-4Fuc compared to Galbeta1-4GlcNAc, which is its endogenous recognition unit. We also tested other human and mouse galectins, i.e., hGal-3, and -9 and mGal-1, 2, 3, 4, 8, and 9. All of them also showed substantial affinity to Galbeta1-4Fuc disaccharide. Further, we assessed the inhibitory effect of Galbeta1-4Fuc, Galbeta1-4Glc, and Gal on the interaction between hGal-1 and its model ligand glycan, and found that Galbeta1-4Fuc is the most effective. Although the biological significance of galectin-Galbeta1-4Fuc interaction is obscure, it might be possible that Galbeta1-4Fuc disaccharide is recognized as a non-self-glycan antigen. Furthermore, Galbeta1-4Fuc could be a promising seed compound for the synthesis of novel galectin inhibitors. |
