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J Biol Chem, Vol. 273, Issue 8, 4523-4529, February 20, 1998
IDUN Pharmaceuticals, Inc., La Jolla, California 92037
Stimulation of the Fas or tumor necrosis factor
receptor 1 (TNFR1) cell surface receptors leads to the activation of
the death effector protease, caspase-8, and subsequent apoptosis. In
some cells, Bcl-xL overexpression can inhibit
anti-Fas- and tumor necrosis factor (TNF)-
-induced apoptosis. To
address the effect of Bcl-xL on caspase-8 processing, Fas-
and TNFR1-mediated apoptosis were studied in the MCF7 breast
carcinoma cell line stably transfected with human Fas cDNA (MCF7/F)
or double transfected with Fas and human Bcl-xL cDNAs
(MCF7/FB). Bcl-xL strongly inhibited apoptosis induced by
either anti-Fas or TNF-. In addition, Bcl-xL prevented the change in cytochrome c immunolocalization induced by
anti-Fas or TNF- treatment. Using antibodies that recognize the p20
and p10 subunits of active caspase-8, proteolytic processing of
caspase-8 was detected in MCF7/F cells following anti-Fas or TNF-,
but not during UV-induced apoptosis. In MCF7/FB cells, caspase-8 was processed normally while processing of the downstream caspase-7 was
markedly attenuated. Moreover, apoptosis induced by direct microinjection of recombinant, active caspase-8 was completely inhibited by Bcl-xL. These data demonstrate that
Bcl-xL can exert an anti-apoptotic function in cells in
which caspase-8 is activated. Thus, at least in some cells, caspase-8
signaling in response to Fas or TNFR1 stimulation is regulated by a
Bcl-xL-inhibitable step.
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