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) for 2h. Western blot analysis revealed that S6K is the most potent inactivation of JNK.Fig. 2Cell death induced by hypoxia in HCT 116 cells. Western blot analysis demonstrated that all three molecules of JNK (p46, p54, and p52) were activated by hypoxia and survived for 12h. The MAPK inhibitor (tobacco etch virus protease inhibitor; 4-FDI) attenuated the cell death induced by a combination of hypoxia and etoposide (5μM). At 24h after 5μM etoposide administration, the S6K inhibitor (PP242) preserved the residual JNK phosphorylation (p54) and abrogated the cell death. However, S6K was not phosphorylated and cell death was not observed in the presence of the same amount of LY249002 (10μM) as the negative control.
A part of JNK phosphorylation is known to be mediated by the upstream kinase MKK7, but which was inhibited by protease inhibitor treatment in these experiments.
At the same time, S6K inhibition was found to be the most potent inactivator of JNK. S6K knockdown also induced a greater degree of cell death than S6K overexpression ([Fig. 3](#fig3){ref-type="fig"}A, B).Fig. 3Cell death induced by knockdown or overexpression of S6K. Control cells (Cont), cells transfected with negative control (siCont), or cells transfected with siS6K-targeting sequence (siS6K) were grown in normoxia and exposed to hypoxia for 24h. Cells transfected with siCont produced a very small degree
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