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Research Article |
1 Institute of Cell Biology and Immunology, University of Stuttgart, Allmandring
31, 70569 Stuttgart, Germany
2 National Institute for Medical Research, Division of Membrane Biology, The
Ridgeway, Mill Hill, London NW7 1AA, UK
3 Institut für Gefäßbiologie und Thromboseforschung, University
of Vienna, 1235 Vienna, Austria
* These authors contributed equally to this work
Author for correspondence (e-mail:
harald.wajant{at}po.uni-stuttgart.de
)
Accepted 27 March 2002
We have recently shown that stimulation of TNF-R2 selectively enhances
apoptosis induction by the death receptor TNF-R1. Here, we demonstrate that
stimulation of CD30 or CD40 also leads to selective enhancement of
TNF-R1-induced cell death. Enhancement of apoptosis was correlated with the
depletion of endogenous TRAF2 within 1 to 6 hours. Selective prestimulation of
TNF-R2 for several hours inhibited TNF-R2-induced activation of the
anti-apoptotic NF-
B pathway up to 90% and dramatically enhanced
apoptosis induction by this receptor. When both TNF-receptors were stimulated
simultaneously, TNF-R1-induced NF-B activation remained unaffected but
TNF-R1-induced apoptosis was still significantly enhanced. Compared with
FasL-induced cell death TNF-R1-induced activation of caspase-8 was
significantly weaker and delayed. Costimulation or prestimulation of TNF-R2
enhanced caspase-8 processing. Life cell imaging and confocal microscopy
revealed that both TNF-R1 and TNF-R2 recruited the anti-apoptotic factor cIAP1
in a TRAF2-dependent manner. Thus, TNF-R2 may compete with TNF-R1 for the
recruitment of newly synthesized TRAF2-bound anti-apoptotic factors, thereby
promoting the formation of a caspase-8-activating TNF-R1 complex. Hence,
TNF-R2 triggering can interfere with TNF-R1-induced apoptosis by inhibition of
NF-B-dependent production of anti-apoptotic factors and by blocking the
action of anti-apoptotic factors at the post-transcriptional level.
Key words: Caspase-8, Cell death, TNF, TNF-R2, TRAF2
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