Vialinin A is a ubiquitin-specific peptidase inhibitor |
| |
| Authors: | Kiyoshi Okada Yue Qi Ye Kayoko Taniguchi Ayaka Yoshida Tomonori Akiyama Yasukiyo Yoshioka Jun-ichi Onose Hiroyuki Koshino Shunya Takahashi Arata Yajima Naoki Abe Shunsuke Yajima |
| |
| Affiliation: | 1. Department of Bioscience, Tokyo University of Agriculture, Tokyo 156-8502, Japan;2. Department of Nutritional Science, Tokyo University of Agriculture, Tokyo 156-8502, Japan;3. Department of Fermentation Science, Tokyo University of Agriculture, Tokyo 156-8502, Japan;4. Chemical Biology Department, RIKEN Advance Science Institute, Saitama 351-0198, Japan |
| |
| Abstract: | Vialinin A, a small compound isolated from the Chinese mushroom Thelephora vialis, exhibits more effective anti-inflammatory activity than the widely used immunosuppressive drug tacrolimus (FK506). Here, we show that ubiquitin-specific peptidase 5/isopeptidase T (USP5/IsoT) is a target molecule of vialinin A, identified by using a beads-probe method. Vialinin A inhibited the peptidase activity of USP5/IsoT and also inhibited the enzymatic activities of USP4 among deubiquitinating enzymes tested. Although USPs are a member of thiol protease family, vialinin A exhibited no inhibitions for other thiol proteases, such as calpain and cathepsin. |
| |
| Keywords: | Anti-inflammatory activity Deubiquitinating enzyme Thiol protease Tumor necrosis factor-α |
| 本文献已被 ScienceDirect 等数据库收录！ |
|
