Ubiquitin-Specific Peptidase 5, a Target Molecule of Vialinin A,Is a Key Molecule of TNF-α Production in RBL-2H3 Cells |
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| Authors: | 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 |
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| Institution: | 1. Department of Nutritional Science, Faculty of Applied Bio-science, Tokyo University of Agriculture, Tokyo, Japan.; 2. Department of Bioscience, Faculty of Applied Bio-science, Tokyo University of Agriculture, Tokyo, Japan.; 3. Department of Fermentation Science, Faculty of Applied Bio-science, Tokyo University of Agriculture, Tokyo, Japan.; 4. RIKEN (The Institute of Physical and Chemical Research), Wako, Saitama, Japan.; Stanford University, United States of America, |
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| Abstract: | 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. |
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