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Sorting of a Constitutive Secretory Protein to the Regulated Secretory Pathway of Exocrine Cells

Exocrine cells secrete granule proteins by regulated or constitutive-like secretory pathways. It is thought that all secretory proteins can enter immature secretory granules in exocrine cells. To test this hypothesis, we expressed the constitutive secretory protein secreted alkaline phosphatase (SEA...

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Published in:Biochemical and biophysical research communications 1999-04, Vol.257 (2), p.545-548
Main Authors: Gorr, Sven-Ulrik, Moore, Yancy R.
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Language:English
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description Exocrine cells secrete granule proteins by regulated or constitutive-like secretory pathways. It is thought that all secretory proteins can enter immature secretory granules in exocrine cells. To test this hypothesis, we expressed the constitutive secretory protein secreted alkaline phosphatase (SEAP) in the exocrine cell line AR42J and compared its secretion to that of amylase, an endogenous regulated secretory protein. Secretion of SEAP and amylase were stimulated about 1.5-fold by substance P and 2-fold by barium chloride. In dexamethasone-treated cells, SEAP and amylase secretion were stimulated about 1.8-fold by substance P, 5-fold by barium chloride, and 4-fold by cholecystokinin-8. Cycloheximide reduced basal secretion of SEAP and amylase by 50%, increasing cholecystokinin-stimulated secretion to about 10-fold. Sodium butyrate induced expression of SEAP 2-fold but had no effect on stimulated secretion. These results suggest that SEAP is stored in secretory granules in AR42J cells.
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It is thought that all secretory proteins can enter immature secretory granules in exocrine cells. To test this hypothesis, we expressed the constitutive secretory protein secreted alkaline phosphatase (SEAP) in the exocrine cell line AR42J and compared its secretion to that of amylase, an endogenous regulated secretory protein. Secretion of SEAP and amylase were stimulated about 1.5-fold by substance P and 2-fold by barium chloride. In dexamethasone-treated cells, SEAP and amylase secretion were stimulated about 1.8-fold by substance P, 5-fold by barium chloride, and 4-fold by cholecystokinin-8. Cycloheximide reduced basal secretion of SEAP and amylase by 50%, increasing cholecystokinin-stimulated secretion to about 10-fold. Sodium butyrate induced expression of SEAP 2-fold but had no effect on stimulated secretion. 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subjects 3-Pyridinecarboxylic acid, 1,4-dihydro-2,6-dimethyl-5-nitro-4-(2-(trifluoromethyl)phenyl)-, Methyl ester - pharmacology
Alkaline Phosphatase - genetics
Alkaline Phosphatase - metabolism
Alkaline Phosphatase - secretion
Amylases - metabolism
Amylases - secretion
Animals
Barium Compounds - pharmacology
Butyrates - pharmacology
Cell Line
Chlorides - pharmacology
Cholecystokinin - pharmacology
Cycloheximide - pharmacology
Cytoplasmic Granules - drug effects
Cytoplasmic Granules - metabolism
Cytoplasmic Granules - secretion
Dexamethasone - pharmacology
Pancreas - cytology
Pancreas - drug effects
Pancreas - metabolism
Pancreas - secretion
Potassium Chloride - pharmacology
Rats
Substance P - pharmacology
Tetradecanoylphorbol Acetate - pharmacology
Transfection
title Sorting of a Constitutive Secretory Protein to the Regulated Secretory Pathway of Exocrine Cells
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