Glucagon-like peptide-1 does not mediate amylase release from AR42J cells

Autor: Chahrzad Montrose-Rafizadeh, Andrzej M. Janczewski, Steven J. Sollott, Marco A. Pineyro, Yihong Wang, Jie Zhou, Josephine M. Egan
Rok vydání: 1999
Předmět:
Zdroj: Journal of Cellular Physiology. 181:470-478
ISSN: 1097-4652
0021-9541
DOI: 10.1002/(sici)1097-4652(199912)181:3<470::aid-jcp11>3.0.co;2-p
Popis: In this study, AR42J pancreatic acinar cells were used to investigate if glucagon-like peptide-1 (GLP-1) or glucagon might influence amylase release and acinar cell function. We first confirmed the presence of GLP-1 receptors on AR42J cells by reverse trasncriptase-polymerase chain reaction (RT-PCR), Western blotting, and partial sequencing analysis. While cholecystokinin (CCK) increased amylase release from AR42J cells, GLP-1, alone or in the presence of CCK, had no effect on amylase release but both CCK and GLP-1 increased intracellular calcium. Similar to GLP-1, glucagon increased both cyclic adenosine monophosphate (cAMP) and intracellular calcium in AR42J cells but it actually decreased CCK-mediated amylase release (n = 20, P < 0.01). CCK stimulation resulted in an increase in tyrosine phosphorylation of several cellular proteins, unlike GLP-1 treatment, where no such increased phosphorylation was seen. Instead, GLP-1 decreased such protein phosphorylations. Genestein blocked CCK-induced phosphorylation events and amylase secretion while vanadate increased amylase secretion. These results provide evidence that tyrosine phosphorylation is necessary for amylase release and that signaling through GLP-1 receptors does not mediate amylase release in AR42J cells. J. Cell. Physiol. 181:470–478, 1999. Published 1999 Wiley-Liss, Inc.
Databáze: OpenAIRE
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