Actin cytoskeleton is required for early apoptosis signaling induced by anti-Fas antibody but not Fas ligand in murine B lymphoma A20 cells

Biochem Biophys Res Commun. 2002 Jan 11;290(1):268-74. doi: 10.1006/bbrc.2001.6199.


Murine B lymphoma A20 cells are highly sensitive to Fas-mediated death signals induced by anti-Fas antibody Jo2 or cross-linked Fas ligand (FasL). We have found that the microfilament poison cytochalasin D blocks Fas-mediated apoptosis induced by Jo2 but not FasL in A20 cells. The induction of Fas-mediated apoptosis by Jo2 was antagonized by anti-Fcgamma RII/RIII receptor (FcgammaR) antibody, and defective in FcgammaR-negative A20 cells. Since the induction of Jo2-mediated apoptosis in FcgammaR-negative A20 cells was reversed by the addition of wild type A20 cells or the cross-linking agent protein A, Fas-expressing bystander A20 cells seem to be killed by other A20 cells that capture and cross-link monomeric Jo2 via FcgammaR. Although cytochalasin D affected FcgammaR-mediated cross-linking of Jo2 molecules, the drug markedly inhibited the intracellular signaling pathway induced by Jo2. The blockade of Jo2-induced apoptosis by cytochalasin D occurred upstream of caspase-8 activation. Thus, these observations suggest that actin cytoskeleton is required for early apoptosis signaling induced by Jo2, but not physiological FasL.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Actins / chemistry*
  • Actins / physiology*
  • Animals
  • Antibodies, Monoclonal / metabolism*
  • Antibodies, Monoclonal, Murine-Derived
  • Apoptosis*
  • Blotting, Western
  • Caspase 3
  • Caspase 8
  • Caspase 9
  • Caspases / biosynthesis
  • Cell Membrane / metabolism
  • Cell Separation
  • Cell Survival
  • Cells, Cultured
  • Chromatography, Gel
  • Cross-Linking Reagents / pharmacology
  • Cytochalasin D / pharmacology
  • Cytoskeleton / metabolism
  • Cytoskeleton / physiology*
  • DNA Fragmentation
  • Dose-Response Relationship, Drug
  • Fas Ligand Protein
  • Flow Cytometry
  • Humans
  • Membrane Glycoproteins / metabolism*
  • Mice
  • Models, Biological
  • Protein Binding
  • Recombinant Proteins / metabolism
  • Time Factors
  • Tumor Cells, Cultured


  • Actins
  • Antibodies, Monoclonal
  • Antibodies, Monoclonal, Murine-Derived
  • Cross-Linking Reagents
  • FASLG protein, human
  • Fas Ligand Protein
  • Fasl protein, mouse
  • Membrane Glycoproteins
  • Recombinant Proteins
  • anti-Fas monoclonal antibody
  • Cytochalasin D
  • CASP3 protein, human
  • CASP8 protein, human
  • CASP9 protein, human
  • Casp3 protein, mouse
  • Casp8 protein, mouse
  • Casp9 protein, mouse
  • Caspase 3
  • Caspase 8
  • Caspase 9
  • Caspases