Apoptosis induction by epigallocatechin gallate involves its binding to Fas

Biochem Biophys Res Commun. 2001 Aug 3;285(5):1102-6. doi: 10.1006/bbrc.2001.5293.


Epigallocatechin gallate (EGCG) is known to induce apoptosis in various types of tumor cells, but the precise mechanism by which EGCG induces apoptosis remains to be elucidated. The Fas-Fas ligand system is one of the major pathways operating in the apoptotic cascade. The aim of this study was to examine the possibility that EGCG-binding to Fas triggers the Fas-mediated apoptosis. The EGCG treatment of human monocytic leukemia U937 cells resulted in elevation of caspase 8 activity and fragmentation of caspase 8. The DNA ladder formation caused by the EGCG treatment was inhibited by the caspase 8 inhibitor. These findings suggested the involvement of the Fas-mediated cascade in the EGCG-induced apoptosis in U937 cells. Affinity chromatography revealed the binding between EGCG and Fas. Thus, the results suggest that EGCG-binding to Fas, presumably on the cell surface, triggers the Fas-mediated apoptosis in U937 cells.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Apoptosis* / drug effects
  • Blotting, Western
  • Caspase 8
  • Caspase 9
  • Caspase Inhibitors
  • Caspases / metabolism
  • Catechin / analogs & derivatives
  • Catechin / metabolism*
  • Catechin / pharmacology
  • Chromatography, Affinity
  • Cysteine Proteinase Inhibitors / pharmacology
  • Dose-Response Relationship, Drug
  • Enzyme Activation / drug effects
  • Flow Cytometry
  • Humans
  • Protein Binding / drug effects
  • Protein Binding / physiology
  • U937 Cells
  • fas Receptor / metabolism*


  • Caspase Inhibitors
  • Cysteine Proteinase Inhibitors
  • fas Receptor
  • Catechin
  • epigallocatechin gallate
  • CASP8 protein, human
  • CASP9 protein, human
  • Caspase 8
  • Caspase 9
  • Caspases