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Vol. 58, Issue 5, 1017-1025, November 2000
College of Pharmacy and Research Institute of Pharmaceutical
Sciences, Seoul National University, Seoul, South Korea
The protective adaptive response to electrophiles and reactive
oxygen species is mediated by the enhanced expression of the phase II
detoxifying genes through antioxidant response elements (AREs). The
current study was designed to identify the signaling pathways
responsible for the expression of rGSTA2 in response to cellular
oxidative stress and to establish the molecular mechanistic basis.
Deprivation of cystine and methionine caused oxidative stress in H4IIE
hepatoma cells as evidenced by a marked decrease in the reduced
glutathione (first order rate constant = 0.056 h
1;
t1/2 = 12.6 h) and an increase in
pro-oxidant production. Electrophoretic mobility shift assay revealed
that the ARE complex, consisting of Nrf-1/2 and Maf proteins, was
activated 12 to 48 h after sulfur amino acid deprivation (SAAD).
The rGSTA2 mRNA level was elevated by SAAD beginning at 24 h,
whereas the rGSTA2 subunit was maximally induced at 48 h. Nuclear
ARE activation and rGSTA2 mRNA increase were both completely inhibited
by wortmannin or LY294002, the phosphatidylinositol 3-kinase
(PI3-kinase) inhibitors. The p38 mitogen-activated protein (MAP) kinase
was activated at 0.5 to 3 h after SAAD, followed by sustained
diminished activation up to 12 h. Inhibition of p38 MAP kinase by
SB203580 prevented the ARE-mediated rGSTA2 induction. The activation of
p38 MAP kinase, however, failed to be inhibited by wortmannin or
LY294002, showing that PI3-kinase is not involved in the activation of
p38 MAP kinase. Data showed that PI3-kinase plays an essential role in
the ARE-mediated rGSTA2 induction by oxidative stress after SAAD, which
activates the p38 MAP kinase and leads to rGSTA2 induction.
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