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Ruttenberg Cancer Center, Mount Sinai School of Medicine, New York, New York 10029 [Z. Y., V. N. I., H. H., Z. R.]; Department of Pharmacology, Fox Chase Cancer Center, Philadelphia, Pennsylvania 19111 [K. T.]
To elucidate mechanisms underlying glutathione
S-transferase p (GSTp)-mediated cellular protection
against oxidative stress-induced cell death, the effect of GSTp on
stress signaling pathways was investigated before and after
H2O2 treatment. Under nonstressed conditions,
increased expression of GSTp via a tet-off-inducible GSTp in NIH 3T3
cells increased the phosphorylation of mitogen-activated protein (MAP)
kinase kinase 4, p38, extracellular receptor kinase (ERK), and
inhibitor of 
-kinase (IKK), and reduced phosphorylation of MAP
kinase kinase 7 and Jun NH2-terminal kinase (JNK). Whereas
H2O2 treatment of cells induced JNK, p38, and
IKK activities, in the presence of H2O2 and
elevated GSTp expression there was an additional increase in ERK, p38,
and IKK activities and a decrease in JNK activity. GSTp-mediated
protection from H2O2-induced death was
attenuated upon inhibition of p38, nuclear factor B, or MAP kinase
by dominant negative or pharmacological inhibitors. Conversely,
expression of a dominant negative JNK protected cells from
H2O2-mediated death. These data suggest that
the coordinated regulation of stress kinases by GSTp, as reflected by
increased p38, ERK, and nuclear factor B activities together with
suppression of JNK signaling, contributes to protection of cells
against reactive oxygen species-mediated death.
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