First Author | Yu J | Year | 2007 |
Journal | Biochem Biophys Res Commun | Volume | 360 |
Issue | 4 | Pages | 759-64 |
PubMed ID | 17631277 | Mgi Jnum | J:123490 |
Mgi Id | MGI:3718734 | Doi | 10.1016/j.bbrc.2007.06.110 |
Citation | Yu J, et al. (2007) Synthetic glycan ligand excludes CD22 from antigen receptor-containing lipid rafts. Biochem Biophys Res Commun 360(4):759-764 |
abstractText | CD22/Siglec-2 is a B cell membrane-bound lectin that recognizes glycan ligands containing alpha2,6-linked sialic acid, and negatively regulates signaling through the B cell antigen receptor (BCR). Previous studies demonstrated that synthetic sialosides that bind to CD22 augment BCR signaling by inhibiting CD22-mediated BCR regulation. Here we demonstrate that, after antigen stimulation, CD22 forms a cap together with BCR, and translocates to lipid rafts. Both co-capping of CD22 with BCR and translocation of CD22 to lipid rafts were markedly blocked by a synthetic alpha2,6-linked sialic acid, Neu5Gcalpha2-6GalbetaSE. These results strongly suggest that synthetic glycan ligand excludes CD22 from BCR-containing lipid rafts. Because CD22-mediated signal regulation requires phosphorylation of CD22 by Lyn that localizes in lipid rafts and is activated by BCR, synthetic glycan ligand regulates localization of CD22 crucial for signal regulation. |