Phosphorylation of 3 particulate proteins in rat pancreatic acini in response to vasoactive intestinal peptide (VIP), secretin and cholecystokinin (CCK-8)
Author:
Publisher
Elsevier BV
Subject
Cellular and Molecular Neuroscience,Endocrinology,Physiology,Biochemistry
Reference38 articles.
1. β-Adrenergic regulation of protein phosphorylation and its relationship to exocrine secretion in dispersed rat parotid gland acinar cells;Baum;J Biol Chem,1981
2. Effects of carbachol, cholecystokinin, and insulin on protein phosphorylation in isolated pancreatic acini;Burnham;J Biol Chem,1982
3. Gastrointestinal hormone-receptor interactions in the pancreas;Christophe,1980
4. Stimulation of pancreatic growth by secretin, caerulein and pentagastrin;Dembinski;Endocrinology,1980
5. In vitro interactions of gastrointestinal hormones on cyclic adenosine 3′:5′-monophosphate levels and amylase output in the rat pancreas;Deschodt-Lanckman;Gastroenterology,1975
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1. CRHSP-24 phosphorylation is regulated by multiple signaling pathways in pancreatic acinar cells;American Journal of Physiology-Gastrointestinal and Liver Physiology;2003-10
2. Calcium Induces Rapid Changes in Protein Phosphorylation in Permeabilized Pancreatic Acini;Pancreas;1995-10
3. Evidence of a functional VIP receptor in cultured human retinal pigment epithelium;Current Eye Research;1995-01
4. Effects of synthetic cyclic AMP analogs on amylase exocytosis from rat pancreatic acini;Canadian Journal of Physiology and Pharmacology;1994-10-01
5. Secretagogue regulation of pancreatic acinar cell protein phosphorylation shown by large-scale 2D-PAGE;American Journal of Physiology-Gastrointestinal and Liver Physiology;1994-10-01
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