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Blood, Vol. 94 No. 1 (July 1), 1999:
pp. 291-301
Caspase-Mediated Proteolysis and Activation of Protein Kinase C
Plays a Central Role in Neutrophil Apoptosis
Asim Khwaja and
Louise Tatton
From the Department of Haematology, University College London Medical
School, London, UK.
Neutrophils undergo constitutive apoptosis when aged ex vivo. Recent
studies have indicated roles for Fas/CD95 and the nicotinamide adenine
dinucleotide phosphate (NADPH)-oxidase system in this process. We have investigated the role of protein kinase C (PKC) in
neutrophil death. We show that there is proteolysis and activation of
the novel isoform PKC in aged neutrophils and that this process is
accelerated by the addition of an agonistic Fas antibody. PKC proteolysis occurs before the onset of any detectable features of
apoptosis and pharmacologic inhibition of this enzyme inhibits neutrophil apoptosis. PKC cleavage and activation is dependent on
caspase-8/FADD-like interleukin-1 converting enzyme
(FLICE)-mediated processing of caspase-3/CPP32.
Neutrophil survival is prolonged by the addition of broad spectrum
(BD.fmk) or caspase-8 targeted (zIETD.fmk) peptide caspase inhibitors.
Inhibition of PKC does not prevent apoptosis triggered by factor
withdrawal in immature hematopoietic cells, including normal human
CD34+ progenitors indicating that within a given lineage,
the mechanisms of apoptosis may be differentiation-stage-specific. Ex
vivo aging of neutrophils leads to the increasing production of
reactive oxygen species and this is attenuated in cells treated with
either caspase or PKC inhibitors. Proteolytically activated PKC
acts as a molecular link between the Fas/CD95 receptor and the
NADPH-oxidase system and plays a central role in regulating the process
of neutrophil apoptosis.
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