PURPOSE. Because lens connexins are phosphoproteins and intercellular communication between lens cells may be modulated by connexin phosphorylation, experiments were designed to characterize the expression of protein kinase C (PKC) isoenzymes in the chicken lens and in lentoidcontaining cultures and to study the effects of 12-O-tetradecanoylphorbol-13-acetate (TPA) treatment on the distribution of PKC isoenzymes and intercellular communication. METHODS. The presence and distribution of PKC isoenzymes were studied by immunoblot analysis and immunofluorescence in chicken lens sections and in cell cultures under control conditions and after treatment with TPA. Intercellular communication was assessed by transfer of microinjected Lucifer yellow. RESULTS. PKC �, �, �, �, and � were detected in lens homogenates by immunoblot analysis. The levels of PKC �, �, �, and � decreased between the 7th and the 18th embryonic days. Levels of PKC � remained relatively constant during the period of study. Similarly, lens cells in culture expressed isoenzymes �, �, �, �, and �. PKC � was not detected in lens or culture homogenates. In lens sections, all PKC isoenzymes analyzed were present in epithelial cells, in the annular pad region, and in the posterior aspect of fiber cells. The anti-PKC � antibody also stained fiber cell membranes
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