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2017 ; 277
(1
): 76-89
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Caspase-8: regulating life and death
#MMPMID28462525
Tummers B
; Green DR
Immunol Rev
2017[May]; 277
(1
): 76-89
PMID28462525
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Roles for cell death in development, homeostasis, and the control of infections
and cancer have long been recognized. Although excessive cell damage results in
passive necrosis, cells can be triggered to engage molecular programs that result
in cell death. Such triggers include cellular stress, oncogenic signals that
engage tumor suppressor mechanisms, pathogen insults, and immune mechanisms. The
best-known forms of programmed cell death are apoptosis and a recently recognized
regulated necrosis termed necroptosis. Of the two best understood pathways of
apoptosis, the extrinsic and intrinsic (mitochondrial) pathways, the former is
induced by the ligation of death receptors, a subset of the TNF receptor (TNFR)
superfamily. Ligation of these death receptors can also induce necroptosis. The
extrinsic apoptosis and necroptosis pathways regulate each other and their
balance determines whether cells live. Integral in the regulation and initiation
of death receptor-mediated activation of programmed cell death is the
aspartate-specific cysteine protease (caspase)-8. This review describes the role
of caspase-8 in the initiation of extrinsic apoptosis execution and the mechanism
by which caspase-8 inhibits necroptosis. The importance of caspase-8 in the
development and homeostasis and the way that dysfunctional caspase-8 may
contribute to the development of malignancies in mice and humans are also
explored.
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