Title |
MARCKS phosphorylation and amylase release in GLP-1-stimulated acini isolated from rat pancreas
|
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Published in |
The Journal of Physiological Sciences, May 2018
|
DOI | 10.1007/s12576-018-0621-9 |
Pubmed ID | |
Authors |
Keitaro Satoh, Motoshi Ouchi, Asuka Morita, Masanori Kashimata |
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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Country | Count | As % |
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Spain | 4 | 31% |
United States | 3 | 23% |
Canada | 2 | 15% |
Mexico | 1 | 8% |
Malaysia | 1 | 8% |
Serbia | 1 | 8% |
Unknown | 1 | 8% |
Demographic breakdown
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Members of the public | 7 | 54% |
Scientists | 4 | 31% |
Practitioners (doctors, other healthcare professionals) | 2 | 15% |
Mendeley readers
Geographical breakdown
Country | Count | As % |
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Unknown | 5 | 100% |
Demographic breakdown
Readers by professional status | Count | As % |
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Student > Ph. D. Student | 2 | 40% |
Student > Postgraduate | 1 | 20% |
Other | 1 | 20% |
Unknown | 1 | 20% |
Readers by discipline | Count | As % |
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Veterinary Science and Veterinary Medicine | 1 | 20% |
Biochemistry, Genetics and Molecular Biology | 1 | 20% |
Unknown | 3 | 60% |