Cellular distribution of gastric chief cell protein kinase C activity: Differential effects of diacylglycerol, phorbol esters, carbachol, and cholecystokinin

Stimulation of chief cells with carbachol or cholecystokinin (CCK) results in the production of inositol trisphosphate (IP3) and diacylglycerol (DAG). Although IP3 increases cell calcium concentration, thereby stimulating pepsinogen secretion, the role of DAG and its target, protein kinase C (PKC),...

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Veröffentlicht in:Journal of cellular biochemistry 1992-01, Vol.48 (1), p.107-113
Hauptverfasser: Raffaniello, Robert D., Raufman, Jean-Piean
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description Stimulation of chief cells with carbachol or cholecystokinin (CCK) results in the production of inositol trisphosphate (IP3) and diacylglycerol (DAG). Although IP3 increases cell calcium concentration, thereby stimulating pepsinogen secretion, the role of DAG and its target, protein kinase C (PKC), is less clear. To examine the relation between the cellular distribution of PKC activity and pepsinogen secretion, we determined PKC activity in cytosolic and membrane fractions from dispersed chief cells from guinea pig stomach. To validate our assay, we studied the actions of the phorbol ester PMA. PMA caused a rapid, dose‐dependent, 6‐fold increase in pepsinogen secretion and membrane‐associated PKC activity. Similarly, dose‐response curves for pepsinogen secretion and the increase in membrane‐associated PKC activity induced by a membrane‐permeant DAG (1‐oleoyl‐2‐acetylglycerol) were superimposable. In contrast, CCK (0.1 nM to 1.0 μM) and carbachol (0.1 μM to 1.0 mM) caused a 4‐fold increase in pepsinogen secretion, but did not alter the distribution of PKC activity. These results indicate that in gastric chief cells, PMA‐and DAG‐induced pepsinogen secretion is accompanied by increased membrane‐associated PKC activity. However, the cellular distribution of PKC activity is not altered by CCK or carbachol.
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Although IP3 increases cell calcium concentration, thereby stimulating pepsinogen secretion, the role of DAG and its target, protein kinase C (PKC), is less clear. To examine the relation between the cellular distribution of PKC activity and pepsinogen secretion, we determined PKC activity in cytosolic and membrane fractions from dispersed chief cells from guinea pig stomach. To validate our assay, we studied the actions of the phorbol ester PMA. PMA caused a rapid, dose‐dependent, 6‐fold increase in pepsinogen secretion and membrane‐associated PKC activity. Similarly, dose‐response curves for pepsinogen secretion and the increase in membrane‐associated PKC activity induced by a membrane‐permeant DAG (1‐oleoyl‐2‐acetylglycerol) were superimposable. In contrast, CCK (0.1 nM to 1.0 μM) and carbachol (0.1 μM to 1.0 mM) caused a 4‐fold increase in pepsinogen secretion, but did not alter the distribution of PKC activity. These results indicate that in gastric chief cells, PMA‐and DAG‐induced pepsinogen secretion is accompanied by increased membrane‐associated PKC activity. However, the cellular distribution of PKC activity is not altered by CCK or carbachol.</description><identifier>ISSN: 0730-2312</identifier><identifier>EISSN: 1097-4644</identifier><identifier>DOI: 10.1002/jcb.240480115</identifier><identifier>PMID: 1583072</identifier><identifier>CODEN: JCEBD5</identifier><language>eng</language><publisher>Hoboken: Wiley Subscription Services, Inc., A Wiley Company</publisher><subject>Animals ; Biological and medical sciences ; Carbachol - pharmacology ; Cell physiology ; Diglycerides - pharmacology ; Dose-Response Relationship, Drug ; Fundamental and applied biological sciences. Psychology ; Gastric Mucosa - cytology ; Gastric Mucosa - drug effects ; Gastric Mucosa - enzymology ; Guinea Pigs ; hormones ; Male ; Molecular and cellular biology ; pepsinogen secretion ; Pepsinogens - secretion ; Protein Kinase C - antagonists &amp; inhibitors ; Protein Kinase C - metabolism ; Responses to growth factors, tumor promotors, other factors ; signal transduction ; Sincalide - pharmacology ; stomach ; Tetradecanoylphorbol Acetate - pharmacology ; translocation</subject><ispartof>Journal of cellular biochemistry, 1992-01, Vol.48 (1), p.107-113</ispartof><rights>Copyright © 1992 Wiley‐Liss, Inc.</rights><rights>1992 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4035-a4bdb85f8c0dcd93f4fcec30869ec08797886763339b8e0dae20ba85f9309fe83</citedby><cites>FETCH-LOGICAL-c4035-a4bdb85f8c0dcd93f4fcec30869ec08797886763339b8e0dae20ba85f9309fe83</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1002%2Fjcb.240480115$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1002%2Fjcb.240480115$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,780,784,1417,4024,27923,27924,27925,45574,45575</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&amp;idt=5537229$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/1583072$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Raffaniello, Robert D.</creatorcontrib><creatorcontrib>Raufman, Jean-Piean</creatorcontrib><title>Cellular distribution of gastric chief cell protein kinase C activity: Differential effects of diacylglycerol, phorbol esters, carbachol, and cholecystokinin</title><title>Journal of cellular biochemistry</title><addtitle>J. Cell. Biochem</addtitle><description>Stimulation of chief cells with carbachol or cholecystokinin (CCK) results in the production of inositol trisphosphate (IP3) and diacylglycerol (DAG). Although IP3 increases cell calcium concentration, thereby stimulating pepsinogen secretion, the role of DAG and its target, protein kinase C (PKC), is less clear. To examine the relation between the cellular distribution of PKC activity and pepsinogen secretion, we determined PKC activity in cytosolic and membrane fractions from dispersed chief cells from guinea pig stomach. To validate our assay, we studied the actions of the phorbol ester PMA. PMA caused a rapid, dose‐dependent, 6‐fold increase in pepsinogen secretion and membrane‐associated PKC activity. Similarly, dose‐response curves for pepsinogen secretion and the increase in membrane‐associated PKC activity induced by a membrane‐permeant DAG (1‐oleoyl‐2‐acetylglycerol) were superimposable. In contrast, CCK (0.1 nM to 1.0 μM) and carbachol (0.1 μM to 1.0 mM) caused a 4‐fold increase in pepsinogen secretion, but did not alter the distribution of PKC activity. These results indicate that in gastric chief cells, PMA‐and DAG‐induced pepsinogen secretion is accompanied by increased membrane‐associated PKC activity. However, the cellular distribution of PKC activity is not altered by CCK or carbachol.</description><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Carbachol - pharmacology</subject><subject>Cell physiology</subject><subject>Diglycerides - pharmacology</subject><subject>Dose-Response Relationship, Drug</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gastric Mucosa - cytology</subject><subject>Gastric Mucosa - drug effects</subject><subject>Gastric Mucosa - enzymology</subject><subject>Guinea Pigs</subject><subject>hormones</subject><subject>Male</subject><subject>Molecular and cellular biology</subject><subject>pepsinogen secretion</subject><subject>Pepsinogens - secretion</subject><subject>Protein Kinase C - antagonists &amp; inhibitors</subject><subject>Protein Kinase C - metabolism</subject><subject>Responses to growth factors, tumor promotors, other factors</subject><subject>signal transduction</subject><subject>Sincalide - pharmacology</subject><subject>stomach</subject><subject>Tetradecanoylphorbol Acetate - pharmacology</subject><subject>translocation</subject><issn>0730-2312</issn><issn>1097-4644</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1992</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kU1v1DAQhi0EKkvhyBHJB45NmdhJbHOjARZQVVSJj6PlTOyuWzdZ2VkgP4b_iqNdLZw4zYzeZz70DiHPSzgvAdirW-zOWQWVhLKsH5BVCUoUVVNVD8kKBIeC8ZI9Jk9SugUApTg7ISdlLTkItiK_WxvCLphIe5-m6Lvd5MeBjo7emKVGihtvHcWM0W0cJ-sHeucHkyxtqcHJ__DT_Jq-9c7ZaIfJm0BtznFKy5TeG5zDTZjRxjGc0e1mjN2YkTTZmM4omtgZ3CySGXq6ZBbnNI15hx-ekkfOhGSfHeIp-fr-3Zf2Q3H5ef2xfXNZYAW8LkzV9Z2snUTosVfcVQ4tcpCNsghSKCFlIxrOueqkhd5YBp3JDYqDclbyU1Ls52IcU4rW6W309ybOugS9uKyzy_rocuZf7Pntrru3_V96b2vWXx50k9AEF82APh2xuuaCMZUxscd--mDn_-_Un9qLfw84HJyfZn8dO028043gotbfr9aaXVdruP7W6iv-B0u_p-A</recordid><startdate>199201</startdate><enddate>199201</enddate><creator>Raffaniello, Robert D.</creator><creator>Raufman, Jean-Piean</creator><general>Wiley Subscription Services, Inc., A Wiley Company</general><general>Wiley-Liss</general><scope>BSCLL</scope><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope></search><sort><creationdate>199201</creationdate><title>Cellular distribution of gastric chief cell protein kinase C activity: Differential effects of diacylglycerol, phorbol esters, carbachol, and cholecystokinin</title><author>Raffaniello, Robert D. ; Raufman, Jean-Piean</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4035-a4bdb85f8c0dcd93f4fcec30869ec08797886763339b8e0dae20ba85f9309fe83</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1992</creationdate><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>Carbachol - pharmacology</topic><topic>Cell physiology</topic><topic>Diglycerides - pharmacology</topic><topic>Dose-Response Relationship, Drug</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Gastric Mucosa - cytology</topic><topic>Gastric Mucosa - drug effects</topic><topic>Gastric Mucosa - enzymology</topic><topic>Guinea Pigs</topic><topic>hormones</topic><topic>Male</topic><topic>Molecular and cellular biology</topic><topic>pepsinogen secretion</topic><topic>Pepsinogens - secretion</topic><topic>Protein Kinase C - antagonists &amp; inhibitors</topic><topic>Protein Kinase C - metabolism</topic><topic>Responses to growth factors, tumor promotors, other factors</topic><topic>signal transduction</topic><topic>Sincalide - pharmacology</topic><topic>stomach</topic><topic>Tetradecanoylphorbol Acetate - pharmacology</topic><topic>translocation</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Raffaniello, Robert D.</creatorcontrib><creatorcontrib>Raufman, Jean-Piean</creatorcontrib><collection>Istex</collection><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><jtitle>Journal of cellular biochemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Raffaniello, Robert D.</au><au>Raufman, Jean-Piean</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Cellular distribution of gastric chief cell protein kinase C activity: Differential effects of diacylglycerol, phorbol esters, carbachol, and cholecystokinin</atitle><jtitle>Journal of cellular biochemistry</jtitle><addtitle>J. Cell. Biochem</addtitle><date>1992-01</date><risdate>1992</risdate><volume>48</volume><issue>1</issue><spage>107</spage><epage>113</epage><pages>107-113</pages><issn>0730-2312</issn><eissn>1097-4644</eissn><coden>JCEBD5</coden><abstract>Stimulation of chief cells with carbachol or cholecystokinin (CCK) results in the production of inositol trisphosphate (IP3) and diacylglycerol (DAG). Although IP3 increases cell calcium concentration, thereby stimulating pepsinogen secretion, the role of DAG and its target, protein kinase C (PKC), is less clear. To examine the relation between the cellular distribution of PKC activity and pepsinogen secretion, we determined PKC activity in cytosolic and membrane fractions from dispersed chief cells from guinea pig stomach. To validate our assay, we studied the actions of the phorbol ester PMA. PMA caused a rapid, dose‐dependent, 6‐fold increase in pepsinogen secretion and membrane‐associated PKC activity. Similarly, dose‐response curves for pepsinogen secretion and the increase in membrane‐associated PKC activity induced by a membrane‐permeant DAG (1‐oleoyl‐2‐acetylglycerol) were superimposable. In contrast, CCK (0.1 nM to 1.0 μM) and carbachol (0.1 μM to 1.0 mM) caused a 4‐fold increase in pepsinogen secretion, but did not alter the distribution of PKC activity. These results indicate that in gastric chief cells, PMA‐and DAG‐induced pepsinogen secretion is accompanied by increased membrane‐associated PKC activity. However, the cellular distribution of PKC activity is not altered by CCK or carbachol.</abstract><cop>Hoboken</cop><pub>Wiley Subscription Services, Inc., A Wiley Company</pub><pmid>1583072</pmid><doi>10.1002/jcb.240480115</doi><tpages>7</tpages></addata></record>
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subjects Animals
Biological and medical sciences
Carbachol - pharmacology
Cell physiology
Diglycerides - pharmacology
Dose-Response Relationship, Drug
Fundamental and applied biological sciences. Psychology
Gastric Mucosa - cytology
Gastric Mucosa - drug effects
Gastric Mucosa - enzymology
Guinea Pigs
hormones
Male
Molecular and cellular biology
pepsinogen secretion
Pepsinogens - secretion
Protein Kinase C - antagonists & inhibitors
Protein Kinase C - metabolism
Responses to growth factors, tumor promotors, other factors
signal transduction
Sincalide - pharmacology
stomach
Tetradecanoylphorbol Acetate - pharmacology
translocation
title Cellular distribution of gastric chief cell protein kinase C activity: Differential effects of diacylglycerol, phorbol esters, carbachol, and cholecystokinin
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