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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 |
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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. |
doi_str_mv | 10.1006/bbrc.1999.0504 |
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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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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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Moore, Yancy R.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c340t-c03f24314c8fb438c0d224647d8753860640a9f0a1f89affbff5e5f05aa6e89f3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1999</creationdate><topic>3-Pyridinecarboxylic acid, 1,4-dihydro-2,6-dimethyl-5-nitro-4-(2-(trifluoromethyl)phenyl)-, Methyl ester - pharmacology</topic><topic>Alkaline Phosphatase - genetics</topic><topic>Alkaline Phosphatase - metabolism</topic><topic>Alkaline Phosphatase - secretion</topic><topic>Amylases - metabolism</topic><topic>Amylases - secretion</topic><topic>Animals</topic><topic>Barium Compounds - pharmacology</topic><topic>Butyrates - pharmacology</topic><topic>Cell Line</topic><topic>Chlorides - pharmacology</topic><topic>Cholecystokinin - pharmacology</topic><topic>Cycloheximide - pharmacology</topic><topic>Cytoplasmic Granules - drug effects</topic><topic>Cytoplasmic Granules - metabolism</topic><topic>Cytoplasmic Granules - secretion</topic><topic>Dexamethasone - pharmacology</topic><topic>Pancreas - cytology</topic><topic>Pancreas - drug effects</topic><topic>Pancreas - metabolism</topic><topic>Pancreas - secretion</topic><topic>Potassium Chloride - pharmacology</topic><topic>Rats</topic><topic>Substance P - pharmacology</topic><topic>Tetradecanoylphorbol Acetate - pharmacology</topic><topic>Transfection</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Gorr, Sven-Ulrik</creatorcontrib><creatorcontrib>Moore, Yancy R.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><jtitle>Biochemical and biophysical research communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Gorr, Sven-Ulrik</au><au>Moore, Yancy R.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Sorting of a Constitutive Secretory Protein to the Regulated Secretory Pathway of Exocrine Cells</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>1999-04-13</date><risdate>1999</risdate><volume>257</volume><issue>2</issue><spage>545</spage><epage>548</epage><pages>545-548</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><abstract>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.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>10198248</pmid><doi>10.1006/bbrc.1999.0504</doi><tpages>4</tpages></addata></record> |
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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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