title: Denitrosylation of S-nitrosylated OGT is triggered in LPS-stimulated innate immune response.
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.
authors: Department of Life Science, Laboratory of Functional Glycomics, Ajou University, San 5, Wonchon-dong, Suwon 443-749, Republic of Korea.
authors: In-Hyun
authors: IH
authors: Ryu
authors: Su-Il
authors: SI
authors: Do
mesh_terms: D000818:Animals; D002460:Cell Line; D007113:Immunity, Innate; D008070:Lipopolysaccharides / Q000276:immunology; D008264:Macrophages / Q000276:immunology; D051379:Mice; D008807:Mice, Inbred BALB C; D017351:N-Acetylglucosaminyltransferases / Q000378:metabolism*; D009569:Nitric Oxide / Q000378:metabolism*; D011499:Protein Processing, Post-Translational; D015854:Up-Regulation
chemical_list: D008070:Lipopolysaccharides; D009569:Nitric Oxide; D017351:N-Acetylglucosaminyltransferases