4.5 Article

Vialinin A is a ubiquitin-specific peptidase inhibitor

期刊

BIOORGANIC & MEDICINAL CHEMISTRY LETTERS
卷 23, 期 15, 页码 4328-4331

出版社

PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.bmcl.2013.05.093

关键词

Anti-inflammatory activity; Deubiquitinating enzyme; Thelephora vialis; Thiol protease; Tumor necrosis factor-alpha

资金

  1. Advanced Research Project of the Tokyo University of Agriculture
  2. Chemical Genomics Project of RIKEN
  3. Ministry of Education, Science, Sports, and Culture of Japan
  4. Grants-in-Aid for Scientific Research [24580168] Funding Source: KAKEN

向作者/读者索取更多资源

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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