作者: Eileen M. Westphale , Viviana M. Berthoud , Anna Grigoryeva , Eric C. Beyer
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摘要: Purpose Because lens connexins are phosphoproteins and intercellular communication between cells may be modulated by connexin phosphorylation, experiments were designed to characterize the expression of protein kinase C (PKC) isoenzymes in chicken lentoid-containing cultures study effects 12-O-tetradecanoylphorbol-13-acetate (TPA) treatment on distribution PKC communication. Methods The presence studied immunoblot analysis immunofluorescence sections cell under control conditions after with TPA. Intercellular was assessed transfer microinjected Lucifer yellow. Results alpha, gamma, iota, epsilon, mu detected homogenates analysis. levels decreased 7th 18th embryonic days. Levels epsilon remained relatively constant during period study. Similarly, culture expressed mu. beta not or homogenates. In sections, all analyzed present epithelial cells, annular pad region, posterior aspect fiber cells. anti-PKC gamma antibody also stained membranes. Analysis lentoid revealed that iota minimal amounts alpha Treatment 200 nM TPA for 15 30 minutes induced translocation plasma membrane significantly reduced Conclusions Several situ culture. isoenzyme, fibers, activated TPA, a known activator PKC. We have previously demonstrated TPA-induced phosphorylation gap junction connexin56 (Cx56). new data presented current demonstrate Taken together, results suggest differential Cx56 PKCgamma induce conformational change which, turn, might lead channel closure.