Carbachol activates protein kinase C in dispersed gastric chief cells
We used an 'in situ' kinase assay to examine agonist-induced protein kinase C. (PKC) activation in dispersed chief cells from guinea-pig stomach. Phorbol 12-myristate 13-acetate (PMA), a phorbol ester, and carbamoylcholine, a cholinergic agent, caused a 4- and 3-fold increase in pepsinogen...
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| Veröffentlicht in: | Biochemical journal 1994-05, Vol.300 (1), p.21-24 |
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| creator | RAFFANIELLO, R. D RAUFMAN, J.-P |
| description | We used an 'in situ' kinase assay to examine agonist-induced protein kinase C. (PKC) activation in dispersed chief cells from guinea-pig stomach. Phorbol 12-myristate 13-acetate (PMA), a phorbol ester, and carbamoylcholine, a cholinergic agent, caused a 4- and 3-fold increase in pepsinogen secretion from dispersed chief cells respectively. Whereas PMA caused a rapid 3-fold increase in peptide kinase activity, carbachol caused a 15% increase in activity that was inhibited by the PKC inhibitor, CGP 41,251. Concentrations of carbamoylcholine and a Ca2+ ionophore that were sub-maximal for stimulation of pepsinogen secretion did not cause PKC activation. These results indicate that, in the absence of PKC activation, other mechanisms, most likely involving changes in cellular Ca2+, are sufficient to stimulate pepsinogen secretion. Nevertheless, carbamoylcholine stimulated maximal secretion of pepsinogen only at concentrations that also resulted in activation of PKC. Moreover, these data indicate that relatively small increases in PKC activity (5-10%) can stimulate pepsinogen secretion from dispersed chief cells. |
| doi_str_mv | 10.1042/bj3000021 |
| format | Article |
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D ; RAUFMAN, J.-P</creator><creatorcontrib>RAFFANIELLO, R. D ; RAUFMAN, J.-P</creatorcontrib><description>We used an 'in situ' kinase assay to examine agonist-induced protein kinase C. (PKC) activation in dispersed chief cells from guinea-pig stomach. Phorbol 12-myristate 13-acetate (PMA), a phorbol ester, and carbamoylcholine, a cholinergic agent, caused a 4- and 3-fold increase in pepsinogen secretion from dispersed chief cells respectively. Whereas PMA caused a rapid 3-fold increase in peptide kinase activity, carbachol caused a 15% increase in activity that was inhibited by the PKC inhibitor, CGP 41,251. Concentrations of carbamoylcholine and a Ca2+ ionophore that were sub-maximal for stimulation of pepsinogen secretion did not cause PKC activation. These results indicate that, in the absence of PKC activation, other mechanisms, most likely involving changes in cellular Ca2+, are sufficient to stimulate pepsinogen secretion. Nevertheless, carbamoylcholine stimulated maximal secretion of pepsinogen only at concentrations that also resulted in activation of PKC. Moreover, these data indicate that relatively small increases in PKC activity (5-10%) can stimulate pepsinogen secretion from dispersed chief cells.</description><identifier>ISSN: 0264-6021</identifier><identifier>EISSN: 1470-8728</identifier><identifier>DOI: 10.1042/bj3000021</identifier><identifier>PMID: 8198535</identifier><language>eng</language><publisher>Colchester: Portland Press</publisher><subject>Animals ; Biological and medical sciences ; Carbachol - pharmacology ; Cell physiology ; Enzyme Activation - drug effects ; Fundamental and applied biological sciences. Psychology ; Guinea Pigs ; Male ; Molecular and cellular biology ; Pepsinogens - metabolism ; Phosphorylation ; Protein Kinase C - antagonists & inhibitors ; Protein Kinase C - metabolism ; Signal transduction ; Stomach - cytology ; Stomach - enzymology ; Tetradecanoylphorbol Acetate - pharmacology</subject><ispartof>Biochemical journal, 1994-05, Vol.300 (1), p.21-24</ispartof><rights>1994 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c399t-bb3af48799d5492a4a575ea0d5d45157a858de8a17c77dbd2a294727e1ec463c3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC1138116/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC1138116/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,727,780,784,885,27923,27924,53790,53792</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=4066835$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8198535$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>RAFFANIELLO, R. D</creatorcontrib><creatorcontrib>RAUFMAN, J.-P</creatorcontrib><title>Carbachol activates protein kinase C in dispersed gastric chief cells</title><title>Biochemical journal</title><addtitle>Biochem J</addtitle><description>We used an 'in situ' kinase assay to examine agonist-induced protein kinase C. (PKC) activation in dispersed chief cells from guinea-pig stomach. Phorbol 12-myristate 13-acetate (PMA), a phorbol ester, and carbamoylcholine, a cholinergic agent, caused a 4- and 3-fold increase in pepsinogen secretion from dispersed chief cells respectively. Whereas PMA caused a rapid 3-fold increase in peptide kinase activity, carbachol caused a 15% increase in activity that was inhibited by the PKC inhibitor, CGP 41,251. Concentrations of carbamoylcholine and a Ca2+ ionophore that were sub-maximal for stimulation of pepsinogen secretion did not cause PKC activation. These results indicate that, in the absence of PKC activation, other mechanisms, most likely involving changes in cellular Ca2+, are sufficient to stimulate pepsinogen secretion. Nevertheless, carbamoylcholine stimulated maximal secretion of pepsinogen only at concentrations that also resulted in activation of PKC. Moreover, these data indicate that relatively small increases in PKC activity (5-10%) can stimulate pepsinogen secretion from dispersed chief cells.</description><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Carbachol - pharmacology</subject><subject>Cell physiology</subject><subject>Enzyme Activation - drug effects</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Guinea Pigs</subject><subject>Male</subject><subject>Molecular and cellular biology</subject><subject>Pepsinogens - metabolism</subject><subject>Phosphorylation</subject><subject>Protein Kinase C - antagonists & inhibitors</subject><subject>Protein Kinase C - metabolism</subject><subject>Signal transduction</subject><subject>Stomach - cytology</subject><subject>Stomach - enzymology</subject><subject>Tetradecanoylphorbol Acetate - pharmacology</subject><issn>0264-6021</issn><issn>1470-8728</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1994</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpVkE9LxDAQxYMo67p68AMIOXjxUE3SpEkvgpT1Dyx40XOZJtPdrN22JHXBb2_FpehcZpj3mzfwCLnk7JYzKe6qbcrGEvyIzLnULDFamGMyZyKTSTbuT8lZjFvGuGSSzcjM8NyoVM3JsoBQgd10DQU7-D0MGGkfugF9Sz98CxFpQcfZ-dhjiOjoGuIQvKV247GmFpsmnpOTGpqIF4e-IO-Py7fiOVm9Pr0UD6vEpnk-JFWVQi2NznOnZC5AgtIKgTnlpOJKg1HGoQGurdaucgJELrXQyNHKLLXpgtz_-vaf1Q6dxXYI0JR98DsIX2UHvvyvtH5Trrt9yXlqOM9Gg5tfAxu6GAPW0y1n5U-U5RTlyF79fTaRh-xG_fqgQ7TQ1AFa6-OESZZlZsS-Aa6SfBo</recordid><startdate>19940515</startdate><enddate>19940515</enddate><creator>RAFFANIELLO, R. D</creator><creator>RAUFMAN, J.-P</creator><general>Portland Press</general><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><scope>5PM</scope></search><sort><creationdate>19940515</creationdate><title>Carbachol activates protein kinase C in dispersed gastric chief cells</title><author>RAFFANIELLO, R. D ; RAUFMAN, J.-P</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c399t-bb3af48799d5492a4a575ea0d5d45157a858de8a17c77dbd2a294727e1ec463c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1994</creationdate><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>Carbachol - pharmacology</topic><topic>Cell physiology</topic><topic>Enzyme Activation - drug effects</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Guinea Pigs</topic><topic>Male</topic><topic>Molecular and cellular biology</topic><topic>Pepsinogens - metabolism</topic><topic>Phosphorylation</topic><topic>Protein Kinase C - antagonists & inhibitors</topic><topic>Protein Kinase C - metabolism</topic><topic>Signal transduction</topic><topic>Stomach - cytology</topic><topic>Stomach - enzymology</topic><topic>Tetradecanoylphorbol Acetate - pharmacology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>RAFFANIELLO, R. D</creatorcontrib><creatorcontrib>RAUFMAN, J.-P</creatorcontrib><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><collection>PubMed Central (Full Participant titles)</collection><jtitle>Biochemical journal</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>RAFFANIELLO, R. D</au><au>RAUFMAN, J.-P</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Carbachol activates protein kinase C in dispersed gastric chief cells</atitle><jtitle>Biochemical journal</jtitle><addtitle>Biochem J</addtitle><date>1994-05-15</date><risdate>1994</risdate><volume>300</volume><issue>1</issue><spage>21</spage><epage>24</epage><pages>21-24</pages><issn>0264-6021</issn><eissn>1470-8728</eissn><abstract>We used an 'in situ' kinase assay to examine agonist-induced protein kinase C. (PKC) activation in dispersed chief cells from guinea-pig stomach. Phorbol 12-myristate 13-acetate (PMA), a phorbol ester, and carbamoylcholine, a cholinergic agent, caused a 4- and 3-fold increase in pepsinogen secretion from dispersed chief cells respectively. Whereas PMA caused a rapid 3-fold increase in peptide kinase activity, carbachol caused a 15% increase in activity that was inhibited by the PKC inhibitor, CGP 41,251. Concentrations of carbamoylcholine and a Ca2+ ionophore that were sub-maximal for stimulation of pepsinogen secretion did not cause PKC activation. These results indicate that, in the absence of PKC activation, other mechanisms, most likely involving changes in cellular Ca2+, are sufficient to stimulate pepsinogen secretion. Nevertheless, carbamoylcholine stimulated maximal secretion of pepsinogen only at concentrations that also resulted in activation of PKC. Moreover, these data indicate that relatively small increases in PKC activity (5-10%) can stimulate pepsinogen secretion from dispersed chief cells.</abstract><cop>Colchester</cop><pub>Portland Press</pub><pmid>8198535</pmid><doi>10.1042/bj3000021</doi><tpages>4</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Biochemical journal, 1994-05, Vol.300 (1), p.21-24 |
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| language | eng |
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| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; PubMed Central; Alma/SFX Local Collection |
| subjects | Animals Biological and medical sciences Carbachol - pharmacology Cell physiology Enzyme Activation - drug effects Fundamental and applied biological sciences. Psychology Guinea Pigs Male Molecular and cellular biology Pepsinogens - metabolism Phosphorylation Protein Kinase C - antagonists & inhibitors Protein Kinase C - metabolism Signal transduction Stomach - cytology Stomach - enzymology Tetradecanoylphorbol Acetate - pharmacology |
| title | Carbachol activates protein kinase C in dispersed gastric chief cells |
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