Vialinin A is a ubiquitin-specific peptidase inhibitor

Bioorg Med Chem Lett. 2013 Aug 1;23(15):4328-31. doi: 10.1016/j.bmcl.2013.05.093. Epub 2013 Jun 6.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Anti-Inflammatory Agents / chemistry*
  • Anti-Inflammatory Agents / metabolism
  • Cell Line
  • Endopeptidases / chemistry*
  • Endopeptidases / genetics
  • Endopeptidases / metabolism
  • Protease Inhibitors / chemistry*
  • Protease Inhibitors / metabolism
  • Protein Binding
  • Rats
  • Recombinant Proteins / biosynthesis
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / genetics
  • Terphenyl Compounds / chemistry*
  • Terphenyl Compounds / metabolism

Substances

  • Anti-Inflammatory Agents
  • Protease Inhibitors
  • Recombinant Proteins
  • Terphenyl Compounds
  • vialinin A
  • Endopeptidases
  • ubiquitin isopeptidase