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Department of Molecular Biology, Yokohama City University School of Medicine, Kanazawa-Ku, Yokohama 236, Japan
Protein kinase C (PKC) has been reported to
be associated with the activation of extracellular signal-regulated
kinase (ERK) by hyperosmolality. However, it is unclear whether
hyperosmolality induces PKC activation and which PKC isoforms are
involved in ERK activation. In this study, we demonstrate that NaCl
increases total PKC activity and induces PKC
, PKC
, and
PKC
translocation from the cytosol to the membrane in
NIH/3T3 cells, suggesting that hyperosmotic stress activates
conventional PKC (cPKC) and novel PKC (nPKC). Further studies show that
NaCl-inducible ERK1 and ERK2 (ERK1/2) activation is a consequence of
cPKC and nPKC activation, because either downregulation with
12-O-tetradecanoylphorbol 13-acetate
or selective inhibition of cPKC and nPKC by GF-109203X and rottlerin
largely inhibited the stimulation of ERK1/2 phosphorylation by NaCl. In
addition, we show that NaCl increases diacylglycerol (DAG) levels and
that a phospholipase C (PLC) inhibitor, U-73122, inhibits NaCl-induced
ERK1/2 phosphorylation. These results, together, suggest that a
hyperosmotic NaCl-induced signaling pathway that leads to activation of
ERK1/2 may sequentially involve PLC activation, DAG release, and cPKC
and nPKC activation.
sodium chloride; phospholipase C; diacylglycerol; phosphorylation; novel and conventional protein kinase C; extracellular signal-regulated kinase-1 and -2
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