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We are in no way affiliated or endorsed by the creators of the mentioned software, software links are posted for informational purposes only and we are not responsible for any content or activities on the linked sites.Inhibition of protein phosphatase 2A sensitizes p53-mediated cell death in human cancer cells.
It has been suggested that dephosphorylation of p53 may be important for its transactivation function. In the present study, we examined the effect of inhibition of protein phosphatase 2A (PP2A) on the p53-mediated cell death in human cancer cells. In both p53 wild-type and p53 mutant cells, PP2A inhibitor, okadaic acid, caused the increase in phosphorylation of p53 at serine 15 and the induction of p21 expression. Okadaic acid-induced p21 expression was enhanced by the transfection of small interfering RNA (siRNA) for p53, which caused the inhibition of PP2A. This indicates that p53-induced p21 expression was mediated through PP2A inhibition. In addition, we also examined the effect of okadaic acid on the p53-mediated apoptosis in cancer cells. Okadaic acid enhanced the activation of caspase-3
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