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- and 
Protein Kinase C in NG108-15 Cells
Ernest Gallo Clinic and Research Center and Department
of Neurology (A.S.G., L.Y., Z.-L.W., I.R.C., I.D.),
Department of
Cellular and Molecular Pharmacology and Neuroscience Program (A.S.G.,
I.D.), University of California, San Francisco, California 94110
Protein kinase C (PKC) has been shown to regulate the ethanol
sensitivity of membrane-bound receptors and transporters, but little is
known about the molecular mechanisms underlying this regulation. PKC is
a family of isozymes that translocate to new intracellular sites on
activation. Here we present immunochemical data showing that ethanol
causes translocation of 
- and 
-PKC to new intracellular sites.
Ethanol causes translocation of -PKC from the Golgi to the
perinucleus; this translocation is similar to that induced by
activation of PKC with phorbol esters. In contrast, -PKC
translocation caused by ethanol is different from that induced by
phorbol esters; ethanol causes translocation of -PKC from the
perinucleus to the cytoplasm, whereas phorbol ester activation causes
translocation of -PKC to the nucleus. Because the substrate specificity of these kinases is determined by their site of
localization, ethanol-induced translocation of - and -PKC to new
intracellular sites may explain some of the pleiotropic effects of
ethanol on cellular functions.
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