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J Biol Chem, Vol. 274, Issue 9, 5310-5317, February 26, 1999
From the Molecular Biology Research Laboratory, Department of
Neurosurgery, Hyogo College of Medicine, 1-1 Mukogawa-cho,
Nishinomiya, Hyogo 663-8501, Japan
Apoptosis was induced in human glioma cell lines
by exposure to 100 nM calphostin C, a specific
inhibitor of protein kinase C. Calphostin C-induced apoptosis was
associated with synchronous down-regulation of Bcl-2 and
Bcl-xL as well as activation of caspase-3 but not
caspase-1. The exposure to calphostin C led to activation of
stress-activated protein kinase/c-Jun NH2-terminal kinase
(SAPK/JNK) and p38 kinase and concurrent inhibition of extracellular
signal-regulated kinase (ERK). Upstream of ERK, Shc was shown to be
activated, but its downstream Raf1 and ERK were inhibited. The
pretreatment with acetyl-Tyr-Val-Ala-Asp-aldehyde, a relatively
selective inhibitor of caspase-3, or
benzyloxycarbonyl-Val-Ala-Asp-fluoromethylketone (z-VAD.fmk), a broad
spectrum caspase inhibitor, similarly inhibited calphostin C-induced
activation of SAPK/JNK and p38 kinase as well as apoptotic nuclear
damages (chromatin condensation and DNA fragmentation) and cell
shrinkage, suggesting that caspase-3 functions upstream of SAPK/JNK and
p38 kinase, but did not block calphostin C-induced surface blebbing and
cell death. On the other hand, the inhibition of SAPK/JNK by
transfection of dominant negative SAPK/JNK and that of p38 kinase by
SB203580 induced similar effects on the calphostin C-induced apoptotic
phenotypes and cell death as did z-VAD.fmk and
acetyl-Tyr-Val-Ala-Asp-aldehyde, but the calphostin C-induced PARP
cleavage was not changed, suggesting that SAPK/JNK and p38 kinase are
involved in the DNA fragmentation pathway downstream of caspase-3. The
present findings suggest, therefore, that the activation of SAPK/JNK
and p38 kinase is dispensable for calphostin C-mediated and
z-VAD.fmk-resistant cell death.
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