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Department of Surgery, Toronto Hospital, and University of Toronto, Toronto, Ontario, Canada
IL-1ß-converting enzyme (ICE), also known as caspase-1, subserves
two dichotomous biologic roles. It processes newly synthesized
pro-IL-1ß to yield the active cytokine and, as the human homologue of
the Caenorhabditis elegans gene product, ced-3, it also
induces cellular apoptosis through the cleavage of key intracellular
structural and regulatory proteins and through the catalytic activation
of other caspase family members. We show here that two different
proinflammatory stimuli, LPS and granulocyte-macrophage-CSF,
up-regulate the expression of both ICE and IL-1ß in human
polymorphonuclear neutrophils, and that the ICE-dependent cleavage of
pro-IL-1ß results in delayed expression of the constitutive cell
death program. The apoptotic delay can be blocked by inhibiting
tyrosine kinases or NF-
B activation and by inhibiting protein
synthesis. Since an antisense oligonucleotide for IL-1ß, a blocking
Ab to IL-1ß, and preincubation with the IL-1R antagonist all prevent
the delay in apoptosis, we conclude that IL-1ß acts in an autocrine
manner to inhibit granulocyte programmed cell death. We conclude that
caspase-1 (ICE) subserves both pro- and antiapoptotic roles; the latter
role is evident during inflammation as an inhibition of spontaneous
neutrophil apoptosis through the processing of IL-1ß. The
ICE-dependent activation of IL-1ß may represent a common autocrine
pathway for the divergent stimuli that inhibit the constitutive
expression of neutrophil programmed cell death during inflammation.
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