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Author: Bando M. Miyake Y. Shiina M. Wachi M. Nagai K. Kataoka T.
Publisher: Elsevier
ISSN: 0006-291X
Source: Biochemical and Biophysical Research Communications, Vol.290, Iss.1, 2002-01, pp. : 268-274
Disclaimer: Any content in publications that violate the sovereignty, the constitution or regulations of the PRC is not accepted or approved by CNPIEC.
Abstract
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-Fcγ RII/RIII receptor (FcγR) antibody, and defective in FcγR-negative A20 cells. Since the induction of Jo2-mediated apoptosis in FcγR-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 FcγR. Although cytochalasin D affected FcγR-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.
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