Abstract
In this study we report that protein kinase C ζ (PKC ζ), one of the atypical isoforms of the PKC family located predominantly in cytosol, is redistributed by C2-ceramide treatment in isolated hepatocytes. PKC ζ increased in membrane and nuclear fractions after 30 min of treatment with C2-ceramide in a dose- and time-dependent manner. The action of C2-ceramide was inhibited by wortmannin and LY 294002, indicating that C2-ceramide-induced PKC ζ increase in both nucleus and membrane fractions is mediated by phosphatidylinositol 3-kinase (PI3-kinase) activation. In addition, a significant translocation of PI3-kinase to the nucleus was observed after C2-ceramide treatment.
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