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* Respiratory Medicine Unit, Division of Genomic Medicine and
Cardiovascular Research Group, Division of Clinical Sciences (North), University of Sheffield, Sheffield, United Kingdom
Caspase-1, the prototypic caspase, is known to process the
cytokines IL-1
and IL-18 to mature forms but it is unclear whether,
like other caspases, it can induce apoptosis by activation of
downstream protease cascades. Neutrophils are known to express
caspase-1, to release IL-1 and to undergo rapid, caspase-dependent
apoptosis. We examined apoptosis and IL-1 production in peripheral
blood neutrophils of caspase-1-deficient and wild-type mice.
Constitutive apoptosis of caspase-1-deficient neutrophils was delayed
compared with wild-type neutrophils and LPS-mediated inhibition of
apoptosis was absent, but caspase-1-deficient neutrophils were
susceptible to Fas-mediated apoptosis. LPS-stimulated IL-1
production was absent from caspase-1-deficient neutrophils. To
ascertain whether these differences in apoptosis and IL-1 production
would alter the response to acute lung injury, we studied pulmonary
neutrophil accumulation following intratracheal administration of LPS.
Caspase-1-deficient mice showed increased, predominantly neutrophilic
pulmonary inflammation, but inflammation had resolved in both wild-type
and deficient animals by 72 h after LPS instillation. IL-1
production was increased in wild-type lungs but was also detected in
caspase-1-deficient mice. We conclude that caspase-1 modulates
apoptosis of both peripheral blood and inflammatory neutrophils, but is
not essential for IL-1 production in the
lung.
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