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- W1976790385 endingPage "4509" @default.
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- W1976790385 abstract "The ST6Gal sialyltransferase controls production of the Siaα2-6Galβ1-4GlcNAc (Sia6LacNAc) trisaccharide, which is the ligand for the lectin CD22. Binding of CD22 to Sia6LacNAc is implicated in regulating lymphocyte adhesion and activation. We have investigated mice that lack ST6Gal and report that they are viable, yet exhibit hallmarks of severe immunosuppression unlike CD22-deficient mice. Notably, Sia6LacNAc-deficient mice display reduced serum IgM levels, impaired B cell proliferation in response to IgM and CD40 crosslinking, and attenuated antibody production to T-independent and T-dependent antigens. Deficiency of ST6Gal was further found to alter phosphotyrosine accumulation during signal transduction from the B lymphocyte antigen receptor. These studies reveal that the ST6Gal sialyltransferase and corresponding production of the Sia6LacNAc oligosaccharide are essential in promoting B lymphocyte activation and immune function." @default.
- W1976790385 created "2016-06-24" @default.
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- W1976790385 date "1998-04-14" @default.
- W1976790385 modified "2023-10-16" @default.
- W1976790385 title "Immune regulation by the ST6Gal sialyltransferase" @default.
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- W1976790385 doi "https://doi.org/10.1073/pnas.95.8.4504" @default.
- W1976790385 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/22519" @default.
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