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  • Title: Time dependent conversion from alpha 1- to beta-adrenoceptor-mediated glycogenolysis in isolated rat hepatocytes: role of membrane phospholipase A2 and protein kinase C.
    Author: Ishac EJ, Kunos G.
    Journal: Clin Exp Pharmacol Physiol; 1987 May; 14(5):429-35. PubMed ID: 2824106.
    Abstract:
    1. Incubation of isolated rat liver cells in a serum-free buffer leads to the reduction of the glycogenolytic effect of phenylephrine and the simultaneous emergence of the response to isoprenaline within 4 h. 2. Inhibitors of phospholipase A2 reverse the adrenergic activation of phosphorylase alpha from a beta- to an alpha 1-receptor-mediated event. Conversely activators of phospholipase A2 enhance the conversion. 3. In vitro incubation of hepatocytes leads to a translocation of protein kinase C from the cytosol to the membrane which can be mimicked by phorbol 12-myristate 13-acetate (PMA), an activator of protein kinase C. PMA is also associated with transformation from alpha 1- to beta-adrenoceptor-mediated glycogenolysis. 4. It is proposed that coupling of hepatic alpha 1- and beta-adrenoceptors to postreceptor pathways are regulated by changes in membrane phospholipase A2 and protein kinase C activity.
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