This article is a US Government work and, as such, is in the public domain in the United States of America.
Original Article
Glucagon-like peptide-1 does not mediate amylase release from AR42J cells†
Article first published online: 19 OCT 1999
DOI: 10.1002/(SICI)1097-4652(199912)181:3<470::AID-JCP11>3.0.CO;2-P
Copyright © 1999 Wiley-Liss, Inc.
Additional Information
How to Cite
Zhou, J., Montrose-Rafizadeh, C., Janczewski, A. M., Pineyro, M. A., Sollott, S. J., Wang, Y. and Egan, J. M. (1999), Glucagon-like peptide-1 does not mediate amylase release from AR42J cells. Journal of Cellular Physiology, 181: 470–478. doi: 10.1002/(SICI)1097-4652(199912)181:3<470::AID-JCP11>3.0.CO;2-P
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Publication History
- Issue published online: 19 OCT 1999
- Article first published online: 19 OCT 1999
- Manuscript Accepted: 29 JUN 1999
- Manuscript Received: 5 APR 1999
- Abstract
- References
- Cited By
Abstract
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.

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