Role of protein kinase C-delta in isoproterenol-induced amylase release in rat parotid acinar cells.
In parotid acinar cells, beta-adrenergic receptor activation results in accumulation of intracellular cAMP. Subsequently, cAMP-dependent protein kinase (PKA) is activated and consequently amylase release is provoked. In this paper, we investigated involvement of protein kinase C-delta (PKC delta), a novel isoform of PKC, in amylase release induced by beta-adrenergic receptor stimulation. Amylase release stimulated with the beta-agonist isoproterenol (IPR) was inhibited by rottlerin, an inhibitor of PKC delta. IPR activated PKC delta and 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 detected 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 PKC delta activation is a downstream pathway of PKA activation and is involved in amylase release via MARCKS phosphorylation in rat parotid acinar cells stimulated with beta-adrenergic agonist.
Department of Physiology, Nihon University School of Dentistry at Matsudo, Matsudo, Chiba, Japan.
Hiroshi
H
Sugiya
Keitaro
K
Satoh
Miwako
M
Matsuki-Fukushima
Bing
B
Qi
Ming-Yu
MY
Guo
Junko
J
Fujita-Yoshigaki
D000098:Acetophenones / Q000494:pharmacology; D000318:Adrenergic beta-Agonists / Q000494:pharmacology*; D000681:Amylases / Q000378:metabolism*; D000818:Animals; D001578:Benzopyrans / Q000494:pharmacology; D017868:Cyclic AMP-Dependent Protein Kinases / Q000502:physiology; D004791:Enzyme Inhibitors / Q000494:pharmacology; D047908:Intracellular Signaling Peptides and Proteins / Q000378:metabolism; D007545:Isoproterenol / Q000494:pharmacology*; D008565:Membrane Proteins / Q000378:metabolism; D000076250:Myristoylated Alanine-Rich C Kinase Substrate; D010306:Parotid Gland / Q000166:cytology / Q000187:drug effects* / Q000378:metabolism*; D010766:Phosphorylation; D051745:Protein Kinase C-delta / Q000037:antagonists & inhibitors / Q000502:physiology*; D051381:Rats; D015398:Signal Transduction / Q000502:physiology
D000098:Acetophenones; D000318:Adrenergic beta-Agonists; D001578:Benzopyrans; D004791:Enzyme Inhibitors; D047908:Intracellular Signaling Peptides and Proteins; C000619712:Marcks protein, rat; D008565:Membrane Proteins; D000076250:Myristoylated Alanine-Rich C Kinase Substrate; C085746:rottlerin; D017868:Cyclic AMP-Dependent Protein Kinases; D051745:Protein Kinase C-delta; D000681:Amylases; D007545:Isoproterenol