| First Author | Jones MB | Year | 2016 |
| Journal | Proc Natl Acad Sci U S A | Volume | 113 |
| Issue | 26 | Pages | 7207-12 |
| PubMed ID | 27303031 | Mgi Jnum | J:234287 |
| Mgi Id | MGI:5789677 | Doi | 10.1073/pnas.1523968113 |
| Citation | Jones MB, et al. (2016) B-cell-independent sialylation of IgG. Proc Natl Acad Sci U S A 113(26):7207-12 |
| abstractText | IgG carrying terminal alpha2,6-linked sialic acids added to conserved N-glycans within the Fc domain by the sialyltransferase ST6Gal1 accounts for the anti-inflammatory effects of large-dose i.v. Ig (IVIg) in autoimmunity. Here, B-cell-specific ablation of ST6Gal1 in mice revealed that IgG sialylation can occur in the extracellular environment of the bloodstream independently of the B-cell secretory pathway. We also discovered that secreted ST6Gal1 is produced by cells lining central veins in the liver and that IgG sialylation is powered by serum-localized nucleotide sugar donor CMP-sialic acid that is at least partially derived from degranulating platelets. Thus, antibody-secreting cells do not exclusively control the sialylation-dependent anti-inflammatory function of IgG. Rather, IgG sialylation can be regulated by the liver and platelets through the corresponding release of enzyme and sugar donor into the cardiovascular circulation. |
