Chromostatin Inhibits Catecholamine Secretion in Adrenal Chromaffin Cells by Activating a Protein Phosphatase
Chromostatin is a 20-residue peptide derived from chromogranin A (CGA), the major soluble component of secretory granules in adrenal medullary chromaffin cells. One known biological function of chromostatin is to inhibit the secretagogue-evoked catecholamine secretion from chromaffin cells. Putative...
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| Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 1992-08, Vol.89 (16), p.7398-7402 |
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| creator | Galindo, Estelle Zwiller, Jean Bader, Marie-France Aunis, Dominique |
| description | Chromostatin is a 20-residue peptide derived from chromogranin A (CGA), the major soluble component of secretory granules in adrenal medullary chromaffin cells. One known biological function of chromostatin is to inhibit the secretagogue-evoked catecholamine secretion from chromaffin cells. Putative receptors are present on the chromaffin-cell plasma membrane, and the activation of such receptors leads to the inhibition of L-type voltage-sensitive calcium channels. We report here that exposure of chromaffin cells to chromostatin modifies neither cAMP and cGMP levels nor protein kinase C activity but does provoke the activation of soluble protein phosphatase (PPase) type 2A in a dose-dependent manner compatible with the peptide concentration inhibiting catecholamine secretion. The activation of the PPase as well as the inhibition of both secretagogue-induced Ca2+entry and catecholamine secretion by chromostatin were all blocked by okadaic acid, a specific PPase inhibitor. We suggest that chromostatin directly or indirectly stimulates PPase-2A, dephosphorylating a target protein and lowering its activity in the secretory process. |
| doi_str_mv | 10.1073/pnas.89.16.7398 |
| format | Article |
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One known biological function of chromostatin is to inhibit the secretagogue-evoked catecholamine secretion from chromaffin cells. Putative receptors are present on the chromaffin-cell plasma membrane, and the activation of such receptors leads to the inhibition of L-type voltage-sensitive calcium channels. We report here that exposure of chromaffin cells to chromostatin modifies neither cAMP and cGMP levels nor protein kinase C activity but does provoke the activation of soluble protein phosphatase (PPase) type 2A in a dose-dependent manner compatible with the peptide concentration inhibiting catecholamine secretion. The activation of the PPase as well as the inhibition of both secretagogue-induced Ca2+entry and catecholamine secretion by chromostatin were all blocked by okadaic acid, a specific PPase inhibitor. We suggest that chromostatin directly or indirectly stimulates PPase-2A, dephosphorylating a target protein and lowering its activity in the secretory process.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.89.16.7398</identifier><identifier>PMID: 1323834</identifier><identifier>CODEN: PNASA6</identifier><language>eng</language><publisher>Washington, DC: National Academy of Sciences of the United States of America</publisher><subject>Adrenal Medulla - drug effects ; Adrenal Medulla - enzymology ; Adrenal Medulla - physiology ; Adrenals. Interrenals ; Adrenomedullary hormones. Regulation ; Animals ; Biological and medical sciences ; Calcium - metabolism ; Catecholamines ; Cattle ; Cells, Cultured ; Cellular biology ; Chromaffin cells ; Chromogranin A ; Chromogranins - pharmacology ; Cultured cells ; Cyclic nucleotides ; Enzyme Activation ; Enzymes ; Ethers, Cyclic - pharmacology ; Fundamental and applied biological sciences. Psychology ; Kinetics ; Lasalocid - pharmacology ; Norepinephrine - metabolism ; Okadaic Acid ; P type calcium channels ; Peptide Fragments - pharmacology ; Phosphatases ; Phosphoprotein Phosphatases - metabolism ; Protein Kinase C - antagonists & inhibitors ; Protein Kinase C - metabolism ; Proteins ; Rats ; Receptors ; Secretion ; Ungulates ; Vertebrates: endocrinology</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 1992-08, Vol.89 (16), p.7398-7402</ispartof><rights>Copyright 1992 The National Academy of Sciences of the United States of America</rights><rights>1992 INIST-CNRS</rights><rights>Copyright National Academy of Sciences Aug 15, 1992</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c549t-81f94fc8f2e743e42e78e1e597b38b430db02e825aa9a7cf54fea334a6202cd13</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/89/16.cover.gif</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/2360097$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/2360097$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,727,780,784,803,885,27924,27925,53791,53793,58017,58250</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=5516742$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/1323834$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Galindo, Estelle</creatorcontrib><creatorcontrib>Zwiller, Jean</creatorcontrib><creatorcontrib>Bader, Marie-France</creatorcontrib><creatorcontrib>Aunis, Dominique</creatorcontrib><title>Chromostatin Inhibits Catecholamine Secretion in Adrenal Chromaffin Cells by Activating a Protein Phosphatase</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>Chromostatin is a 20-residue peptide derived from chromogranin A (CGA), the major soluble component of secretory granules in adrenal medullary chromaffin cells. One known biological function of chromostatin is to inhibit the secretagogue-evoked catecholamine secretion from chromaffin cells. Putative receptors are present on the chromaffin-cell plasma membrane, and the activation of such receptors leads to the inhibition of L-type voltage-sensitive calcium channels. We report here that exposure of chromaffin cells to chromostatin modifies neither cAMP and cGMP levels nor protein kinase C activity but does provoke the activation of soluble protein phosphatase (PPase) type 2A in a dose-dependent manner compatible with the peptide concentration inhibiting catecholamine secretion. The activation of the PPase as well as the inhibition of both secretagogue-induced Ca2+entry and catecholamine secretion by chromostatin were all blocked by okadaic acid, a specific PPase inhibitor. We suggest that chromostatin directly or indirectly stimulates PPase-2A, dephosphorylating a target protein and lowering its activity in the secretory process.</description><subject>Adrenal Medulla - drug effects</subject><subject>Adrenal Medulla - enzymology</subject><subject>Adrenal Medulla - physiology</subject><subject>Adrenals. Interrenals</subject><subject>Adrenomedullary hormones. Regulation</subject><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Calcium - metabolism</subject><subject>Catecholamines</subject><subject>Cattle</subject><subject>Cells, Cultured</subject><subject>Cellular biology</subject><subject>Chromaffin cells</subject><subject>Chromogranin A</subject><subject>Chromogranins - pharmacology</subject><subject>Cultured cells</subject><subject>Cyclic nucleotides</subject><subject>Enzyme Activation</subject><subject>Enzymes</subject><subject>Ethers, Cyclic - pharmacology</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Kinetics</subject><subject>Lasalocid - pharmacology</subject><subject>Norepinephrine - metabolism</subject><subject>Okadaic Acid</subject><subject>P type calcium channels</subject><subject>Peptide Fragments - pharmacology</subject><subject>Phosphatases</subject><subject>Phosphoprotein Phosphatases - metabolism</subject><subject>Protein Kinase C - antagonists & inhibitors</subject><subject>Protein Kinase C - metabolism</subject><subject>Proteins</subject><subject>Rats</subject><subject>Receptors</subject><subject>Secretion</subject><subject>Ungulates</subject><subject>Vertebrates: endocrinology</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1992</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9ks1v1DAQxSMEKtvCmQugqEJwytZfiW2Jyyrio1IlKgFna-K1G6-SeGt7K_rf47DLFjhwGsnvN2_Gfi6KFxgtMeL0YjtBXAq5xM2SUykeFQuMJK4aJtHjYoEQ4ZVghD0tTmPcIIRkLdBJcYIpoYKyRTG2ffCjjwmSm8rLqXedS7FsIRnd-wFGN5nyq9HBJOenMjOrdTATDOWvRrA2H7VmGGLZ3Zcrndzd7HRTQnkdfDJZve593PaQIJpnxRMLQzTPD_Ws-P7xw7f2c3X15dNlu7qqdM1kqgS2klktLDGcUcNyEQabWvKOio5RtO4QMYLUABK4tjWzBihl0BBE9BrTs-L93ne760az1mZKAQa1DW6EcK88OPW3Mrle3fg7xSTHPLe_PbQHf7szManRRZ0vCZPxu6hww2qKuMjg-T_gxu9Cfp2oCMJENJSTDF3sIR18jMHY4x4YqTlENYeohMy-ag4xd7z6c_0Hfp9a1t8cdIgaBhtg0i4esbrGDWfz4HcHbPb_rT7MUXY3DMn8SJl8_V8yAy_3wCYmH44EoU3-Upz-BL8-yNE</recordid><startdate>19920815</startdate><enddate>19920815</enddate><creator>Galindo, Estelle</creator><creator>Zwiller, Jean</creator><creator>Bader, Marie-France</creator><creator>Aunis, Dominique</creator><general>National Academy of Sciences of the United States of America</general><general>National Acad Sciences</general><general>National Academy of Sciences</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>7QG</scope><scope>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7SN</scope><scope>7SS</scope><scope>7T5</scope><scope>7TK</scope><scope>7TM</scope><scope>7TO</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>5PM</scope></search><sort><creationdate>19920815</creationdate><title>Chromostatin Inhibits Catecholamine Secretion in Adrenal Chromaffin Cells by Activating a Protein Phosphatase</title><author>Galindo, Estelle ; Zwiller, Jean ; Bader, Marie-France ; Aunis, Dominique</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c549t-81f94fc8f2e743e42e78e1e597b38b430db02e825aa9a7cf54fea334a6202cd13</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1992</creationdate><topic>Adrenal Medulla - drug effects</topic><topic>Adrenal Medulla - enzymology</topic><topic>Adrenal Medulla - physiology</topic><topic>Adrenals. Interrenals</topic><topic>Adrenomedullary hormones. Regulation</topic><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>Calcium - metabolism</topic><topic>Catecholamines</topic><topic>Cattle</topic><topic>Cells, Cultured</topic><topic>Cellular biology</topic><topic>Chromaffin cells</topic><topic>Chromogranin A</topic><topic>Chromogranins - pharmacology</topic><topic>Cultured cells</topic><topic>Cyclic nucleotides</topic><topic>Enzyme Activation</topic><topic>Enzymes</topic><topic>Ethers, Cyclic - pharmacology</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Kinetics</topic><topic>Lasalocid - pharmacology</topic><topic>Norepinephrine - metabolism</topic><topic>Okadaic Acid</topic><topic>P type calcium channels</topic><topic>Peptide Fragments - pharmacology</topic><topic>Phosphatases</topic><topic>Phosphoprotein Phosphatases - metabolism</topic><topic>Protein Kinase C - antagonists & inhibitors</topic><topic>Protein Kinase C - metabolism</topic><topic>Proteins</topic><topic>Rats</topic><topic>Receptors</topic><topic>Secretion</topic><topic>Ungulates</topic><topic>Vertebrates: endocrinology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Galindo, Estelle</creatorcontrib><creatorcontrib>Zwiller, Jean</creatorcontrib><creatorcontrib>Bader, Marie-France</creatorcontrib><creatorcontrib>Aunis, Dominique</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>Animal Behavior Abstracts</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Ecology Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Immunology Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Oncogenes and Growth Factors Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Galindo, Estelle</au><au>Zwiller, Jean</au><au>Bader, Marie-France</au><au>Aunis, Dominique</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Chromostatin Inhibits Catecholamine Secretion in Adrenal Chromaffin Cells by Activating a Protein Phosphatase</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>1992-08-15</date><risdate>1992</risdate><volume>89</volume><issue>16</issue><spage>7398</spage><epage>7402</epage><pages>7398-7402</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><coden>PNASA6</coden><abstract>Chromostatin is a 20-residue peptide derived from chromogranin A (CGA), the major soluble component of secretory granules in adrenal medullary chromaffin cells. One known biological function of chromostatin is to inhibit the secretagogue-evoked catecholamine secretion from chromaffin cells. Putative receptors are present on the chromaffin-cell plasma membrane, and the activation of such receptors leads to the inhibition of L-type voltage-sensitive calcium channels. We report here that exposure of chromaffin cells to chromostatin modifies neither cAMP and cGMP levels nor protein kinase C activity but does provoke the activation of soluble protein phosphatase (PPase) type 2A in a dose-dependent manner compatible with the peptide concentration inhibiting catecholamine secretion. The activation of the PPase as well as the inhibition of both secretagogue-induced Ca2+entry and catecholamine secretion by chromostatin were all blocked by okadaic acid, a specific PPase inhibitor. We suggest that chromostatin directly or indirectly stimulates PPase-2A, dephosphorylating a target protein and lowering its activity in the secretory process.</abstract><cop>Washington, DC</cop><pub>National Academy of Sciences of the United States of America</pub><pmid>1323834</pmid><doi>10.1073/pnas.89.16.7398</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Adrenal Medulla - drug effects Adrenal Medulla - enzymology Adrenal Medulla - physiology Adrenals. Interrenals Adrenomedullary hormones. Regulation Animals Biological and medical sciences Calcium - metabolism Catecholamines Cattle Cells, Cultured Cellular biology Chromaffin cells Chromogranin A Chromogranins - pharmacology Cultured cells Cyclic nucleotides Enzyme Activation Enzymes Ethers, Cyclic - pharmacology Fundamental and applied biological sciences. Psychology Kinetics Lasalocid - pharmacology Norepinephrine - metabolism Okadaic Acid P type calcium channels Peptide Fragments - pharmacology Phosphatases Phosphoprotein Phosphatases - metabolism Protein Kinase C - antagonists & inhibitors Protein Kinase C - metabolism Proteins Rats Receptors Secretion Ungulates Vertebrates: endocrinology |
| title | Chromostatin Inhibits Catecholamine Secretion in Adrenal Chromaffin Cells by Activating a Protein Phosphatase |
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