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Vol. 59, Issue 5, 1147-1156, May 2001
College of Pharmacy and Research Institute of Pharmaceutical
Sciences, Seoul National University, Seoul, South Korea (K.W.K.,
M.K.C., S.G.K.); and College of Medicine, Hanyang University, Seoul,
South Korea (C.H.L.)
The protective adaptive response to electrophiles and reactive oxygen
species is mediated by enhanced expression of phase II detoxifying
genes, including glutathione S-transferases, through activation of antioxidant response element (ARE). The current study was
designed to investigate the role of phosphatidylinositol 3-kinase
(PI3-kinase)-Akt and mitogen-activated protein (MAP) kinase signaling
pathways in the induction of rGSTA2 by
tert-butylhydroquinone (t-BHQ). Nuclear
ARE complex was activated 1 to 6 h after treatment of H4IIE cells
with t-BHQ. The rGSTA2 mRNA level was elevated 6 to
24 h after t-BHQ treatment, which led to the enzyme
induction. Activities of PI3-kinase and Akt were increased 10 min
through 6 h after t-BHQ treatment, whereas
wortmannin or LY294002, PI3-kinase inhibitors, completely abolished ARE
binding activity and increases in rGSTA2 mRNA and protein.
Extracellular signal-regulated kinase (ERK), p38 MAP kinase, and c-Jun
N-terminal kinase (JNK) were all activated by t-BHQ.
Treatment with PD98059, an ERK inhibitor, however, increased rGSTA2
mRNA and further enhanced t-BHQ-induced expression of
rGSTA2. Neither SB203580 nor overexpression of JNK1 dominant negative
mutant altered t-BHQ-inducible rGSTA2 expression. These
results demonstrated that t-BHQ activated PI3-kinase and Akt, which was responsible for ARE-mediated rGSTA2 induction, and that
ERK might negatively regulate rGSTA2 expression, whereas activation of
p38 MAP kinase or of JNK by t-BHQ was not associated with the enzyme induction.
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