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J Biol Chem, Vol. 273, Issue 12, 6736-6743, March 20, 1998
From the Center for Pediatric Research, Children's Hospital of The
King's Daughters, Eastern Virginia Medical School,
Norfolk, Virginia 23510
Current data suggest that apoptosis controls
neutrophil numbers in tissues. We analyzed roles for and the sites of
action for the cAMP-dependent protein kinases (cAPKs) in
apoptosis induced in human neutrophils by in vitro storage,
cycloheximide (CHX) exposure, and anti-Fas exposure. Treatment with
8-chlorophenylthio-cAMP (8-CPT-cAMP) prolonged the time required for
50% of the cells to exhibit apoptotic morphology
(t50) from 16.3 to 41.8 h (in vitro culture), from 2.4 to 7.8 h (CHX), and from 4.8 to
6.5 h (anti-Fas). CHX ± 8-CPT-cAMP did not significantly
alter resting intracellular calcium levels and H-89, a selective
inhibitor of cAPK, had no effect on apoptosis in the absence of the
analogue. In contrast, site-selective cAMP analogues that specifically
activated the type I cAPK, but not type II cAPK, synergistically
attenuated apoptosis. Exposure to 8-CPT-cAMP delayed, in parallel, the
activity of caspase-3 (CPP-32
), whereas mitogen-activated protein
kinase kinase (MAPKK) inhibitor, PD98059, had no effect on CHX-induced apoptosis ± 8-CPT-cAMP. Together these results indicate that type I cAPK activation is necessary and sufficient to mediate cAMP-induced delay in human neutrophil apoptosis induced by several mechanisms and
suggest that one of the major sites of cAPK action is upstream of
caspase-3 (CPP-32) activation.
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