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Vol. 59, Issue 5, 981-986, May 2001
National Creative Research Initiative Center for Cell Death,
Graduate School of Biotechnology, Korea University, Seoul, Korea
(S.-J.E., J.E.L., J.S., E.-J.C.); and Department of Pharmacology
(E.Y.K., H.J.K., B.J.G.) and Brain Disease Research Center (S.U.K.),
School of Medicine, Ajou University, Suwon, Kyungki-do, Korea
Zn2+, one of the most abundant trace metal ions in
mammalian cells, modulates the functions of many regulatory proteins
associated with a variety of cellular activities. In the central
nervous system, Zn2+ is highly localized in the cerebral
cortex and hippocampus. It has been proposed to play a role in normal
brain function as well as in the pathophysiology of certain
neurodegenerative disorders. We here report that Zn2+
induced stimulation of the c-Jun N-terminal kinase (JNK) pathway in
mouse primary cortical cells and in various cell lines. Exposure of
cells to Zn2+ resulted in the stimulation of JNK and its
upstream kinases including stress-activated protein kinase kinase and
mitogen-activated protein kinase kinase kinase. Zn2+
also induced stimulation of phosphoinositide 3-kinase (PI3K) The
Zn2+-induced JNK stimulation was blocked by LY294002, a
PI3K inhibitor, or by a dominant-negative mutant of PI3K
.
Furthermore, overexpression of Rac1N17, a dominant negative mutant of
Rac1, suppressed the Zn2+- and PI3K-induced JNK
stimulation. The stimulatory effect of Zn2+ on both PI3K
and JNK was repressed by the free-radical scavenging agent
N-acetylcysteine. Taken together, our data suggest that Zn2+ induces stimulation of the JNK signaling pathway
through PI3K-Rac1 signals and that the free-radical generation may be
an important step in the Zn2+ induction of the JNK stimulation.
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