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*
Department of Microbiology and Immunology, Wonkwang University School of Medicine, Iksan, Chonbuk, Korea;
Medicinal Resources Research Center of Wonkwang University, Iksan, Chonbuk, Korea; and
Department of Biology, College of Natural Science, Kyung-Pook National University, Taegu, Korea
Nitric oxide (NO) induces apoptotic cell death in murine RAW 264.7
macrophages. To elucidate the inhibitory effects of protein kinase C
(PKC) on NO-induced apoptosis, we generated clones of RAW 264.7 cells
that overexpress one of the PKC isoforms and explored the possible
interactions between PKC and three structurally related
mitogen-activated protein (MAP) kinases in NO actions. Treatment of RAW
264.7 cells with sodium nitroprusside (SNP), a NO-generating agent,
activated both c-Jun N-terminal kinase/stress-activated protein kinase
(JNK/SAPK) and p38 kinase, but did not activate extracellular
signal-regulated kinase (ERK)-1 and ERK-2. In addition, SNP-induced
apoptosis was slightly blocked by the selective p38 kinase inhibitor
(SB203580) but not by the MAP/ERK1 kinase inhibitor (PD098059).
PKC transfectants (PKC-ßII, -
, and -
) showed substantial
protection from cell death induced by the exposure to NO donors such as
SNP and S-nitrosoglutathione (GSNO). In contrast, in RAW
264.7 parent or in empty vector-transformed cells, these NO donors
induced internucleosomal DNA cleavage. Moreover, overexpression of PKC
isoforms significantly suppressed SNP-induced JNK/SAPK and p38 kinase
activation, but did not affect ERK-1 and -2. We also explored the
involvement of CPP32-like protease in the NO-induced apoptosis.
Inhibition of CPP32-like protease prevented apoptosis in RAW 264.7
parent cells. In addition, SNP dramatically activated CPP32 in the
parent or in empty vector-transformed cells, while slightly activated
CPP32 in PKC transfectants. Therefore, we conclude that PKC protects
NO-induced apoptotic cell death, presumably nullifying the NO-mediated
activation of JNK/SAPK, p38 kinase, and CPP32-like protease in RAW
264.7 macrophages.
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