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Departments of
* Immunology,
Biochemistry, and
Respiratory Medicine,
Division of Pathology, Central Laboratory of Medical Sciences, and
¶ Allergy Research Center, Juntendo University School of Medicine, Tokyo, Japan
TWEAK, a TNF family member, is produced by
IFN-
-stimulated monocytes and induces multiple pathways of cell
death, including caspase-dependent apoptosis, cathepsin B-dependent
necrosis, and endogenous TNF-
-mediated cell death, in a cell
type-specific manner. However, the TWEAK receptor(s) that mediates
these multiple death pathways remains to be identified. Recently,
fibroblast growth factor-inducible 14 (Fn14) has been identified to be
a TWEAK receptor, which was responsible for TWEAK-induced proliferation
of endothelial cells and angiogenesis. Because Fn14 lacks the
cytoplasmic death domain, it remains unclear whether Fn14 can also
mediate the TWEAK-induced cell death. In this study, we demonstrated
that TWEAK could induce apoptotic cell death in Fn14 transfectants. A
pan-caspase inhibitor,
benzyloxycarbonyl-Val-Ala-Asp-fluoromethylketone, rather sensitized the
Fn14 transfectants to TWEAK-induced cell death by necrosis via reactive
oxygen intermediates and cathepsin B-dependent pathway. By using newly
generated agonistic anti-Fn14 mAbs, we also observed that Fn14 is
constitutively expressed on the cell surface of all TWEAK-sensitive
tumor cell lines, and can transmit the multiple death signals.
Moreover, an anti-Fn14 mAb that blocks TWEAK-Fn14 interaction could
totally abrogate TWEAK binding and TWEAK-induced cell death in all
TWEAK-sensitive tumor cell lines. These results revealed that the
multiple pathways of TWEAK-induced cell death are solely mediated by
Fn14.
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