Ubiquitin-specific peptidase 5, a target molecule of vialinin A, is a key molecule of TNF-α production in RBL-2H3 cells.
oleh: Yasukiyo Yoshioka, Yue Qi Ye, Kiyoshi Okada, Kayoko Taniguchi, Ayaka Yoshida, Kouichi Sugaya, Jun-ichi Onose, Hiroyuki Koshino, Shunya Takahashi, Arata Yajima, Shunsuke Yajima, Naoki Abe
| Format: | Article |
|---|---|
| Diterbitkan: | Public Library of Science (PLoS) 2013-01-01 |
Deskripsi
Tumor necrosis factor alpha (TNF-α), a central mediator of the inflammatory response, is released from basophilic cells and other cells in response to a variety of proinflammatory stimuli. Vialinin A is a potent inhibitor of TNF-α production and is released from RBL-2H3 cells. Ubiquitin-specific peptidase 5 (USP5), a deubiquitinating enzyme, was identified as a target molecule of vialinin A and its enzymatic activity was inhibited by vialinin A. Here we report production of TNF-α is decreased in USP5 siRNA-knockdown RBL-2H3 cells, compared with control cells. The finding of the present study strongly suggests that USP5 is one of the essential molecules for the production of TNF-α in RBL-2H3.