ID | 111477 |
Author |
Sugiya, Hiroshi
Nihon University
Satoh, Keitaro
Nihon University
Matsuki-Fukushima, Miwako
Nihon University
Qi, Bing
Nihon University
Guo, Ming-Yu
Nihon University
Fujita-Yoshigaki, Junko
Nihon University
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Keywords | PKCδ
amylase release
MARCKS
parotid acinar cells
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Content Type |
Journal Article
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Description | In parotid acinar cells, β-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-δ(PKCδ), a novel isoform of PKC, in amylase release induced by β-adrenergic receptor stimulation. Amylase release stimulated with the β-agonsit isoproterenol (IPR) was inhibited by rottlerin, an inhibitor of PKCδ. IPR activated PKCδ 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 PKCδ activation is a downstream pathway of PKA activation and is involved in amylase release via MARCKS phosphorylation in rat parotid acinar cells stimulated with β-adrenergic agonist.
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Journal Title |
The Journal of Medical Investigation
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ISSN | 13496867
13431420
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NCID | AA11166929
AA12022913
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Publisher | Faculty of Medicine Tokushima University
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Volume | 56
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Issue | Supplement
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Start Page | 368
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End Page | 370
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Sort Key | 368
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Published Date | 2009-12
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DOI (Published Version) | |
URL ( Publisher's Version ) | |
FullText File | |
language |
eng
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TextVersion |
Publisher
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