O-linked N-acetylglucosamine glycosylation of p65 aggravated the inflammation in both fibroblast-like synoviocytes stimulated by tumor necrosis factor-α and mice with collagen induced arthritis

Arthritis Res Ther. 2015 Sep 14;17(1):248. doi: 10.1186/s13075-015-0762-7.

Abstract

Introduction: We investigated the inflammatory potential of O-linked N-acetylglucosamine glycosylation (O-GlcNAcylation) of p65 in rheumatoid arthritis (RA).

Methods: Fibroblast-like synoviocytes (FLS) and MH7A cells were treated with synthetic ThiaMet-G (200 μM), an O-GlcNAcase (OGA) inhibitor, followed by tumor necrosis factor (TNF)-α (10 μg/mL). Proliferation of synovial cells was measured by MTT assay, and the levels of mRNAs encoding pro-inflammatory molecules were quantitated by RT-PCR. The nuclear localization of O-GlcNAcylated of p65 and its DNA binding affinity and transcriptional activity were assessed. The severity assessment of arthritis and a histopathological examination were done in mice with collagen induced arthritis (CIA). ThiaMet-G (20 mg/kg) intraperitoneal injection was done every other day for 26 days. Fluorescence-activated cell sorting (FACS) analysis of T cells was performed.

Results: Hyper-O-GlcNAcylation increased the proliferation and mRNA expression of pro-inflammatory genes in synoviocytes stimulated by TNF-α. Moreover, O-GlcNAcylation of p65 enhanced its proportion of nuclear localization, DNA binding affinity and transcriptional activity. In CIA mice, ThiaMet-G significantly aggravated the severity of arthritis clinically and histologically, and it also increased CD4 + IFN-γ + T cells and CD4 + IL-17+ T cells.

Conclusions: O-GlcNAcylation of p65 increased the effects of TNF-α-mediated inflammation both in vitro (in synovial cells) and in vivo (in mice with CIA).

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acetylglucosamine / metabolism*
  • Active Transport, Cell Nucleus / drug effects
  • Animals
  • Arthritis, Experimental / genetics
  • Arthritis, Experimental / metabolism*
  • Blotting, Western
  • Cell Line
  • Cell Nucleus / metabolism
  • Cell Proliferation / drug effects
  • Cell Proliferation / genetics
  • Chemokine CCL5 / genetics
  • Chemokine CCL5 / metabolism
  • Enzyme Inhibitors / pharmacology
  • Fibroblasts / drug effects*
  • Fibroblasts / metabolism
  • Gene Expression / drug effects
  • Glycosylation
  • Humans
  • Inflammation Mediators / metabolism*
  • Interleukin-8 / genetics
  • Interleukin-8 / metabolism
  • Male
  • Matrix Metalloproteinase 1 / genetics
  • Matrix Metalloproteinase 1 / metabolism
  • Mice, Inbred DBA
  • RNA Interference
  • Reverse Transcriptase Polymerase Chain Reaction
  • Synovial Membrane / drug effects
  • Synovial Membrane / metabolism
  • Transcription Factor RelA / metabolism*
  • Tumor Necrosis Factor-alpha / pharmacology*
  • beta-N-Acetylhexosaminidases / antagonists & inhibitors
  • beta-N-Acetylhexosaminidases / genetics
  • beta-N-Acetylhexosaminidases / metabolism

Substances

  • Chemokine CCL5
  • Enzyme Inhibitors
  • Inflammation Mediators
  • Interleukin-8
  • Transcription Factor RelA
  • Tumor Necrosis Factor-alpha
  • hexosaminidase C
  • beta-N-Acetylhexosaminidases
  • Matrix Metalloproteinase 1
  • Acetylglucosamine