ポスター発表
- 第4日 5月18日（金） ポスター会場
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4P-28 PDF
プロテオミクス法を用いた、ヒト滑膜線維芽細胞株におけるライリンの機能解析
[Aim] To understand physiological and pathological roles of layilin in synovial fibroblasts, we comprehensively investigated protein profile changes caused by layilin-silencing.
[Methods] Immortalized human synovial membrane fibroblasts (HSFs) were transfected with siRNA for layilin (siL) in TNF-α-treated and -non-tretaed conditions. Proteins affected by siL were comprehensively detected by 2-dimensional fluorescence difference gel electrophoresis (2D-DIGE). Proteins of interest were identified by mass spectrometry.
[Results] In the 2D-DIGE analysis, intensity of approximately one-fifth of the detected protein spots was significantly changed by siL both in the TNF-α-treated and -non-treated conditions (239/1092 spots and 201/1092 spots, respectively). Proteins were identified in 25 out of 87 protein spots with ±1.3-fold or greater intensity changes by siL. 16 (64%) of the 25 protein spots were assigned to epithelial-mesenchymal transition (EMT)-related proteins.
[Conclusion] Our data suggest that layilin is deeply involved in the regulation of EMT-related proteins. Functions of layilin in synovial fibroblasts should be investigated in the context of EMT, although synovial fibroblasts are not epithelial cells. Furthermore, the EMT-related proteins affected by layilin may be involved in the pathogenesis of rheumatoid arthritis, which was characterized by proliferation and invasion of synovial fibroblasts.