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MARCKS phosphorylation and amylase release in GLP-1-stimulated acini isolated from rat pancreas
Keitaro Satoh1, Motoshi Ouchi2, Asuka Morita2
1Department of Pharmacology, Asahi University School of Dentistry, 1851 Hozumi, Mizuho, Gifu, 501-0296, Japan. k-satoh@dent.asahi-u.ac.jp.
Abstract:
Little is known about the effects of glucagon-like peptide 1 (GLP-1) on the pancreatic exocrine gland. In the gland, secretagogues induce amylase release. That signal transduction is evoked mainly by an increase in intracellular Ca2+ levels and activation of protein kinase C (PKC). We previously demonstrated that myristoylated alanine-rich C kinase substrate (MARCKS), a PKC substrate, is involved in pancreatic amylase release. Here, we studied the effects of GLP-1 on MARCKS phosphorylation and amylase release in rat pancreatic acini. GLP-1 induced amylase release and MARCKS phosphorylation in isolated pancreatic acini. Inhibitors of cAMP-dependent protein kinase (PKA) suppressed those effects. Furthermore, a MARCKS-related peptide inhibited the GLP-1-induced amylase release. These findings suggest that GLP-1 induces amylase release through MARCKS phosphorylation via activation of PKA in isolated pancreatic acini.
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