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Role of protein kinase-C in the α1-adrenoceptor-mediated responses of perfused rat liver

AuthorsUrcelay, Elena; Butta, Nora CSIC ORCID CVN; González-Manchón, Consuelo CSIC ORCID ; Ciprés, Guadalupe; Martín Requero, A.; Sánchez Ayuso, Matilde CSIC ORCID ; Parrilla, Roberto L.
Issue Date1-Nov-1993
PublisherOxford University Press
CitationEndocrinology 133(5): 2105-2115 (1993)
AbstractThe present work aimed to determine the role played by protein kinase-C (PKC) in the α1-adrenoceptor-induced activation of hepatic metabolism. The following observations indicate that activation of PKC is a condition necessary for α1-adrenoceptor activation of hepatic functions, but not sufficient to mimic the receptor-mediated effects in the absence of external physiological stimuli. 1) α1-Adrenoceptor activation promoted the translocation of PKC from the cytosol to its active form in the plasma membrane. 2) Activation of PKC by the phorbol ester 12-myristate 13-acetate or exogenous diacylglycerols or by elevation of endogenous levels of diacylglycerols by inhibiting diacylglycerol kinase mimicked the α1- adrenoceptor-mediated actions. However, the time course and magnitude of the nonreceptor responses differ from those mediated by α1-adrenoceptor activation. In addition, nonreceptor-mediated activation of PKC decreased the α1-adrenoceptor responsiveness. 3) Inhibition of PKC by either H-7 [1-(5- isoquinolinilsulfonyl)2-methylpiperazine] or staurosporine inhibited all of the α1-adrenoceptor-induced responses, except gluconeogenesis. The vasopressin effects were not inhibited by H-7, indicating that PKC activation is a distinct feature of the hepatic α1-adrenoceptor activation that is not shared by all the Ca2+-mobilizing agonists. The diacylglycerol-PKC branch of the α1-adrenoceptor signaling pathway seems to control the sustained phase of stimulation of hepatic functions. In these studies we have also observed that phorbol 12-myristate 13-acetate produces a concentration- dependent inhibition of hepatic respiration. However, decreased energy availability does not seem to be the cause of its action to decrease α1- adrenoceptor responsiveness.
Publisher version (URL)https://doi.org/10.1210/endo.133.5.8404660
Identifiersdoi: 10.1210/endo.133.5.8404660
issn: 0013-7227
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