Branch-specific sialylation of IgG-Fc glycans by ST6Gal-I.
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ABSTRACT:
SUBMITTER: Barb AW
PROVIDER: S-EPMC2761508 | biostudies-literature | 2009 Oct
REPOSITORIES: biostudies-literature
Publications
Branch-specific sialylation of IgG-Fc glycans by ST6Gal-I.
Barb Adam W AW Brady Evan K EK Prestegard James H JH
Biochemistry 20091001 41
Sialylated forms of the Fc fragment of immunoglobulin G, produced by the human alpha2-6 sialyltransferase ST6Gal-I, were identified as potent anti-inflammatory mediators in a mouse model of rheumatoid arthritis and are potentially the active components in intravenous IgG anti-inflammatory therapies. The activities and specificities of hST6Gal-I are, however, poorly characterized. Here MS and NMR methodology demonstrates glycan modification occurs in a branch-specific manner with the alpha1-3Man ...[more]
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