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J Biol Chem, Vol. 273, Issue 6, 3388-3393, February 6, 1998
From the Tumor Immunology Program, German Cancer Research Center,
Im Neuenheimer Feld 280, 69120 Heidelberg, Germany
The Bcl-2 family member Bcl-xL
has often been correlated with apoptosis resistance. We have shown
recently that in peripheral human T cells resistance to CD95-mediated
apoptosis is characterized by a lack of caspase-8 recruitment to the
CD95 death-inducing signaling complex (DISC) and by increased
expression of Bcl-xL (Peter, M. E., Kischkel, F. C., Scheuerpflug, C. G., Medema, J. P., Debatin, K.-M., and
Krammer, P. H. (1997) Eur. J. Immunol. 27, 1207-1212). This raises the possibility that Bcl-xL
directly prevents caspase-8 activation by the DISC. To test this
hypothesis a cell line in which CD95 signaling was inhibited by
overexpression of Bcl-xL was used. In these
MCF7-Fas-bcl-xL cells Bcl-xL had no effect on
the recruitment of caspase-8 to the DISC. It did not affect the
activity of the DISC nor the generation of the caspase-8 active
subunits p18 and p10. In contrast, cleavage of a typical substrate for
caspase-3-like proteases, poly(ADP-ribose) polymerase, was inhibited in
comparison with the control-transfected CD95-sensitive MCF7-Fas
cells. To test whether Bcl-xL would inhibit active
caspase-8 subunits in the cytoplasm, a number of immunoprecipitation experiments were performed. Using monoclonal antibodies directed against different domains of caspase-8, anti-Bcl-xL
antibodies, or fusion proteins of glutathione S-transferase
with different domains of caspase-8, no evidence for a direct or
indirect physical interaction between caspase-8 and Bcl-xL
was found. Moreover, overexpression of Bcl-xL did not
inhibit the activity of the caspase-8 active subunits p18/p10.
Therefore, in this cell line that has become resistant to CD95-induced
apoptosis due to overexpression of Bcl-xL,
Bcl-xL acts independently and downstream of caspase-8.
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