Role of protein kinase C-δ in isoproterenol-induced amylase release in rat parotid acinar cells

In parotid acinar cells, -adrenergic receptor activation results in accumula- tion of intracellular cAMP. Subsequently, cAMP-dependent protein kinase (PKA) is acti- vated and consequently amylase release is provoked. In this paper, we investigated in- volvement of protein kinase C-(PKC), a novel isoform of PKC, in amylase release in- duced by -adrenergic receptor stimulation. Amylase release stimulated with the - agonsit isoproterenol (IPR) was inhibited by rottlerin, an inhibitor of PKC .I PR acti- vated PKCand the effect of IPR were inhibited by a PKA inhibitor, H89. Myristoylated alanine-rich C kinase substrate (MARCKS), a major cellular substrate for PKC, was de- tected in rat parotid acinar cells, and a MARCKS inhibitor, MARCKS-related peptide, inhibited the IPR-induced amylase release. IPR stimulated MARCKS phosphorylation, which was found to be inhibited by H89 and rottlerin. These observations suggest that PKCactivation is a downstream pathway of PKA activation and is involved in amylase release via MARCKS phosphorylation in rat parotid acinar cells stimulated with - adrenergic agonist. J. Med. Invest. 56 Suppl. : 368-370, December, 2009

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