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- W4313404600 abstract "Abstract O-GlcNAcylation is a dynamic posttranslational modification, characterized by the addition of an O-linked-β-N-acetylglucosamine to a serine, threonine or tyrosine leading to the fine-tuning of various protein functions. Previously, we have shown that hyperglycemia induces O-GlcNAcylation of the nuclear factor kappa B (NF-κB) transcription factor c-Rel subunit at serine 350. We have found that c-Rel O-GlcNAcylation enhances the transcription of c-Rel dependent proinflammatory cytokines in T cells and inversely regulates FOXP3 expression in T regulatory cells. Other studies have shown that enhanced O-GlcNAcylation dysregulates IL-10 signal transduction and results in decreased IL-10 production. Regulatory B cells primarily secrete IL-10 to conduct its immunosuppressive function. Here, we show that c-Rel O-GlcNAcylation regulates c-Rel-dependent transcription in regulatory B cells. LPS, CD40L, and TLR stimulation under hyper O-GlcNAcylation condition differentially regulates the generation of regulatory B cells from primary B cells isolated from WT and c-Rel knockout C57BL/6 and NOD mice. Mutation of the O-GlcNAcylation site in c-Rel (serine 350 to alanine) also showed differential binding to the IL-10 promoter. This study reveals c-Rel O-GlcNAcylation as a novel mechanism regulating transcription in B regulatory cells with implications in autoimmunity. ARL was supported by the Visual Sciences Training Program grant from the National Institutes of Health (T32 EY007157). PR was supported by supported by the National Institute of Allergy and Infectious Diseases at National Institute of Health grants R01 AI116730 and R21 AI144264, and National Cancer Institute at National Institute of Health grant R21 CA246194." @default.
- W4313404600 created "2023-01-06" @default.
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- W4313404600 date "2022-05-01" @default.
- W4313404600 modified "2023-10-16" @default.
- W4313404600 title "Role of c-Rel O-GlcNAcylation in regulatory B cells" @default.
- W4313404600 doi "https://doi.org/10.4049/jimmunol.208.supp.53.03" @default.
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