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J. Biol. Chem., Vol. 275, Issue 26, 19609-19619, June 30, 2000
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From the Laboratory of Signal Transduction, Molecular Endocrinology
Group, NIEHS, National Institutes of Health,
Research Triangle Park, North Carolina 27709
Cell shrinkage and loss of intracellular
K+ are early requisite features for the activation of
effector caspases and apoptotic nucleases in Fas receptor-mediated
apoptosis of Jurkat cells, although the mechanisms responsible for both
process remain unclear (Bortner, C. D., Hughes, F. M., Jr.,
and Cidlowski, J. A. (1997) J. Biol. Chem. 272, 32436-32442). We have now investigated the role of protein kinase C
(PKC)-dependent signaling in the regulation of Fas-induced
cell shrinkage and loss of K+ during apoptosis. Anti-Fas
induced cell shrinkage was blocked during PKC stimulation by the
phorbol ester 12-O-tetradecanoylphorbol-3-acetate (PMA) and
by bryostatin-1. Conversely, inhibition of PKC with Gö6976,
enhanced the anti-Fas-mediated loss of cell volume. Analyses of
mitochondrial membrane potential and DNA fragmentation revealed that
the PKC-mediated effect observed in cell volume is propagated to these
late features of apoptosis. Flow cytometric analyses and
86Rb efflux experiments revealed that a primary effect of
PKC appears to be on the modulation of Fas-induced K+
efflux, since both PMA and bryostatin-1 inhibited extrusion of K+ that occurs during Fas-mediated cell death, and
Gö6976 exacerbated the effect of anti-Fas. Interestingly, high
extracellular K+ significantly blocked the effect of
anti-Fas alone or anti-Fas combined with Gö6976, suggesting an
underlying effect of PKC on K+ loss. Western blot analyses
showed the caspase-dependent proteolysis of PKC isotypes
Protein Kinase C (PKC) Inhibits Fas Receptor-induced Apoptosis
through Modulation of the Loss of K+ and Cell Shrinkage
A ROLE FOR PKC UPSTREAM OF CASPASES*
,
, and 
in whole cell extracts from anti-Fas treated Jurkat T
cells. However, stimulation of PKC by PMA or bryostatin-1 prevented
this isotypic-specific PKC cleavage during apoptosis, providing further
evidence that PKC itself exerts an upstream signal in apoptosis and
controls the caspase-dependent proteolytic degradation of
PKC isotypes. Finally, we show that PMA or bryostatin-1 prevents the
activation of caspase-3 and caspase-8. Thus, this study shows that the
protective effect that PKC stimulation exerts in the Fas-mediated
apoptotic pathway occurs at a site upstream of caspases-3 and -8.
*
The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed: Laboratory of Signal
Transduction, Molecular Endocrinology Group, NIEHS, National Institutes
of Health, 111 Alexander Dr., Research Triangle Park, NC 27709. Tel.:
919-541-1564; Fax: 919-541-1367; E-mail:
cidlowski@niehs.nih.gov.
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