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The protein kinase C (PKC) family of isoenzymes plays a key role in the regulation of hepatocellular secretion. The hydrophobic and cholestatic bile acid, taurolithocholic acid (TLCA), acts as a potent Ca ؉؉ agonist in isolated hepatocytes. However, its effect on PKC isoforms has not been elucidated. Here we investigate the effects of TLCA at low micromolar concentrations on the distribution of PKC isoforms and on membrane-associated PKC activity. The distribution of PKC isoforms was determined in isolated rat hepatocytes in short-term culture using Western blotting and immunofluorescence techniques. PKC activity was measured radiochemically. TLCA (10 mol/L) induced selective translocation of ⑀-PKC by 47.9% ؎ 20.5% (P F .02 vs. controls; n ‫؍‬ 7), but not of ␣-, ␦-, and -PKC to the hepatocellular membranes, whereas the phorbol ester, phorbol 12-myristate 13-acetate (

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NaHCO3, 5.0; cysteine.HCl.H20, 0.3; vitamin B12, 0.0001 (33); and hemin, 0.002 (when required). Glucose, NaHCO3, cysteine, hemin (dissolved in 0.02% NaOH), and vitamin B12 were sterilized separately; B12 and hemin solutions were filter sterilized and the remainder was autoclaved. Medium preparation was carried out anaerobically under an atmosphere of 100% C02, except for glucose, cysteine, and hemin which were prepared under 100% N2. All traces of oxy-436 on July 31, 2020 by guest