O-linked β-N-acetylglucosamine transferase regulates macrophage polarization in diabetic periodontitis: In vivo and in vitro study

Figure 10  O-GlcNAc transferase promotes O-linked β-N-acetylglucosamine and phosphorylation of p38. A: The interaction between O-GlcNAc transferase (OGT) and p38 was analyzed using co-immunoprecipitation; B: The localization of OGT and p38 in RAW264.7 cells was observed using immunofluorescence staining. Scale bar: 20 μm; C: Potential O-linked β-N-acetylglucosamine (O-GlcNAcylation) sites in p38 were predicted using the DictyOGlyc 1.1 Server software; D: The O-GlcNAcylation sites were confirmed, and the effects on p38 phosphorylation were measured using Western blot; E: The relative protein expression levels were quantified. ^aP < 0.05. P value calculated vs wild-type. OGT: O-GlcNAc transferase; DAPI: 4’,6-Diamidino-2-phenylindole; WT: Wild-type; GAPDH: Glyceraldehyde-3-phosphate dehydrogenase; RL2: O-GlcNAc.