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
Keywords
PKCδ
amylase release
MARCKS
parotid acinar cells
Content Type
Journal Article
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.
Journal Title
The Journal of Medical Investigation
ISSN
13496867
13431420
NCID
AA11166929
AA12022913
Publisher
Faculty of Medicine Tokushima University
Volume
56
Issue
Supplement
Start Page
368
End Page
370
Sort Key
368
Published Date
2009-12
DOI (Published Version)
URL ( Publisher's Version )
FullText File
language
eng
TextVersion
Publisher