Emodin inhibits migration and invasion of DLD-1 (PRL-3) cells via inhibition of PRL-3 phosphatase activity

  • Bioorg Med Chem Lett. 2012 Jan 1;22(1):323-6. doi: 10.1016/j.bmcl.2011.11.008.
Young-Min Han  1 ,  Su-Kyung Lee ,  Dae Gwin Jeong ,  Seong Eon Ryu ,  Dong Cho Han ,  Dae Keun Kim ,  Byoung-Mog Kwon
Affiliations
  • 1. Laboratory of Chemical Genomics and Biology, Korea Research Institute of Bioscience and Biotechnology, 1125 Gwahakro, Yoosunggu, Daejeon 305-600, Republic of Korea.
PMID: 22137788 DOI: 10.1016/j.bmcl.2011.11.008
Abstract

Anthraquinones have been reported as Phosphatase inhibitors. Therefore, anthraquinone derivatives were screened to identify a potent Phosphatase Inhibitor against the Phosphatase of regenerating liver-3 (PRL-3). Emodin strongly inhibited Phosphatase activity of PRL-3 with IC(50) values of 3.5μM and blocked PRL-3-induced tumor cell migration and invasion in a dose-dependent manner. Emodin rescued the phosphorylation of ezrin, which is a known PRL-3 substrate. The results of this study reveal that emodin is a PRL-3 inhibitor and a good lead molecule for obtaining a selective PRL-3 inhibitor.