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• W2064581098 abstract "O-linked N-acetylglucosaminyltransferase (OGT)-mediated protein O-GlcNAcylation has been revealing various aspects of functional significance in biological processes, such as cellular signaling and activation of immune system. We found that OGT is maintained as S-nitrosylated form in resting cells, and its denitrosylation is triggered in innate immune response of lipopolysaccharide (LPS)-treated macrophage cells. S-nitrosylation of OGT strongly inhibits its catalytic activity up to more than 80% of native OGT, and denitrosylation of OGT leads to protein hyper-O-GlcNAcylation. Furthermore, blockage of increased protein O-GlcNAcylation results in significant loss of nitric oxide and cytokine production. We propose that denitrosylation of S-nitrosylated OGT is a direct mechanism for upregulation of OGT activity by which immune defense is critically controlled in LPS-stimulated innate immune response." @default.
• W2064581098 created "2016-06-24" @default.
• W2064581098 creator A5030469266 @default.
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• W2064581098 date "2011-04-01" @default.
• W2064581098 modified "2023-09-24" @default.
• W2064581098 title "Denitrosylation of S-nitrosylated OGT is triggered in LPS-stimulated innate immune response" @default.
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• W2064581098 doi "https://doi.org/10.1016/j.bbrc.2011.03.115" @default.
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