MARCKS phosphorylation and amylase release in GLP-1-stimulated acini isolated from rat pancreas

The journal of physiological sciences

article

Keitaro Satoh¹  Motoshi Ouchi²  Asuka Morita²  Masanori Kashimata¹ 

[1] Department of Pharmacology, Asahi University School of Dentistry;Department of Pharmacology and Toxicology, Dokkyo Medical University School of Medicine

关键词: GLP-1;    MARCKS;    Amylase;    PKA;    Exocytosis;   

DOI  :  10.1007/s12576-018-0621-9

来源: Springer

【 摘 要 】

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.

【 授权许可】

Unknown