The structure-activity relationship of various YO compounds, novel plasmin inhibitors, in the apoptosis induction

Biochim Biophys Acta. 2004 Nov 1;1674(3):291-8. doi: 10.1016/j.bbagen.2004.07.004.

Abstract

We have previously reported that YO-2, a selective plasmin inhibitor, induces thymocyte apoptosis. To elucidate the mechanism of YO-2-induced apoptosis, other YO compounds with different plasmin inhibitory action were tested for the pro-apoptotic activity in this study. The treatment of rat thymocytes with the YO compounds which had the hydrophobic but not the hydrophilic moiety at the C-terminal increased DNA fragmentation, the number of condensed nuclei and caspase-3-like activity. All pro-apoptotic YO compounds not only were potent plasmin inhibitors but also had the hydrophobic C-terminal as the common structure. Therefore, the target molecule of the YO compounds may be located not on the cell surface but rather inside the cells.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Apoptosis / drug effects*
  • DNA Fragmentation / drug effects
  • Dipeptides / chemistry
  • Dipeptides / pharmacology*
  • Fibrinolysin / antagonists & inhibitors*
  • Male
  • Molecular Conformation
  • Rats
  • Rats, Sprague-Dawley
  • Structure-Activity Relationship

Substances

  • Dipeptides
  • YO 1 compound
  • YO 2 compound
  • Fibrinolysin