Sorting of a constitutive secretory protein to the regulated secretory pathway of exocrine cells

Sven Ulrik Gorr, Yancy R. Moore

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17 Scopus citations


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.

Original languageEnglish (US)
Pages (from-to)545-548
Number of pages4
JournalBiochemical and Biophysical Research Communications
Issue number2
StatePublished - Apr 13 1999

Bibliographical note

Funding Information:
This work was supported by PHS grants 1 R03 DE 11469-01, 1 R01 DK 53667-01 and a ULSD research grant.

Copyright 2017 Elsevier B.V., All rights reserved.

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