Journal
BIOORGANIC & MEDICINAL CHEMISTRY LETTERS
Volume 23, Issue 15, Pages 4328-4331Publisher
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.bmcl.2013.05.093
Keywords
Anti-inflammatory activity; Deubiquitinating enzyme; Thelephora vialis; Thiol protease; Tumor necrosis factor-alpha
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Funding
- Advanced Research Project of the Tokyo University of Agriculture
- Chemical Genomics Project of RIKEN
- Ministry of Education, Science, Sports, and Culture of Japan
- Grants-in-Aid for Scientific Research [24580168] Funding Source: KAKEN
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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. (C) 2013 Elsevier Ltd. All rights reserved.
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