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*
Department of Immunology,
Allergy Research Center,
Department of Biochemistry, and
Division of Pathology, Central Laboratory of Medical Sciences, Juntendo University School of Medicine, Tokyo, Japan; and
¶ Precursory Research for Embryonic Science and Technology, Japan Science and Technology Corporation, Tokyo, Japan
TWEAK, a recently identified member of the TNF family, is expressed
on IFN-
-stimulated monocytes and induces cell death in certain tumor
cell lines. In this study, we characterized the TWEAK-induced cell
death in several tumor cell lines that exhibited distinct features.
Although the TWEAK-induced cell death in Kym-1 cells was indirectly
mediated by TNF-
and was inhibited by cycloheximide, the
TWEAK-induced cell death in HSC3 cells or IFN--treated HT-29
cells was not inhibited by anti-TNF- mAb or cycloheximide,
suggesting a direct triggering of cell death via TWEAK receptor in the
latter cell lines. The TWEAK-induced apoptosis in HSC3 cells and
IFN--treated HT-29 cells was associated with caspase-8 and caspase-3
activation. Although a pan-caspase inhibitor,
benzyloxycarbonyl-Val-Ala-Asp-fluoromethylketone, inhibited the
TWEAK-induced cell death in HSC3 cells, it rather sensitized HT-29
cells to TWEAK-induced cell death by necrosis. This necrosis was
abrogated by lysosomal proteinase inhibitors, particularly a cathepsin
B inhibitor,
[L-3-trans-(propylcarbamoyl)oxirane-2-carbonyl]-L-isoleucyl-L-proline
methyl ester. During the process of TWEAK-induced necrosis, cathepsin B
was released from lysosome to cytosol. Although DR3 has been reported
to be a receptor for TWEAK, all TWEAK-sensitive tumor cell lines used
in this study did not express DR3 at either protein or mRNA level, but
did bind CD8-TWEAK specifically. These results indicated that TWEAK
could induce multiple pathways of cell death, including both
caspase-dependent apoptosis and cathepsin B-dependent necrosis, in a
cell type-specific manner via TWEAK receptor(s) distinct from
DR3.
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