Inhibition of hormone-stimulated adenylate cyclase activity after altering turkey erythrocyte phospholipid composition with a nonspecific lipid transfer protein. Phosphatidylinositol uncouples catecholamine binding from adenylate cyclase activation
The nonspecific lipid transfer protein from beef liver was used to modify the phospholipid composition of intact turkey erythrocytes in order to study the dependence of isoproterenol-stimulated adenylate cyclase activity on membrane phospholipid composition. Incorporation of phosphatidylinositol int...
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| Veröffentlicht in: | The Journal of biological chemistry 1983-11, Vol.258 (21), p.13017-13026 |
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| container_issue | 21 |
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| container_title | The Journal of biological chemistry |
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| creator | McOsker, C C Weiland, G A Zilversmit, D B |
| description | The nonspecific lipid transfer protein from beef liver was used to modify the phospholipid composition of intact turkey erythrocytes in order to study the dependence of isoproterenol-stimulated adenylate cyclase activity on membrane phospholipid composition. Incorporation of phosphatidylinositol into turkey erythrocytes inhibited isoproterenol-stimulated cyclic AMP accumulation in a linear, concentration-dependent manner. Inhibition was relatively specific for phosphatidylinositol; phosphatidylcholine, phosphatidylethanolamine, phosphatidylserine, phosphatidylglycerol and phosphatidic acid were from 3 to 7 times less effective as inhibitors of hormone-stimulated cyclase activity. Inhibition by phosphatidylinositol was not reversible when up to 90% of the incorporated phosphatidylinositol was removed, either by incubation with phosphatidylinositol-specific phospholipase C or a second incubation with transfer protein; possibly adenylate cyclase activity depends on a small pool of phosphatidylinositol that is inaccessible to either phospholipase C hydrolysis or removal by lipid transfer protein. Phosphatidylinositol incorporation inhibits adenylate cyclase activity by uncoupling beta-adrenergic receptors from the remainder of the cyclase complex. Phosphatidylinositol incorporation had no effect on stimulation of cAMP accumulation by either cholera toxin or forskolin, indicating that inhibition occurs only at the level of receptor. Phosphodiesterase activity was not altered in phosphatidylinositol-modified cells. Inhibition of cAMP accumulation was not the result of changes in either membrane fluidity or in cAMP transport out of modified turkey erythrocytes. Phosphatidylinositol inhibition of isoproterenol-stimulated cyclase activity may serve as a useful model system for hormone-induced desensitization. |
| doi_str_mv | 10.1016/S0021-9258(17)44074-9 |
| format | Article |
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Phosphatidylinositol uncouples catecholamine binding from adenylate cyclase activation</title><source>MEDLINE</source><source>EZB-FREE-00999 freely available EZB journals</source><source>Alma/SFX Local Collection</source><creator>McOsker, C C ; Weiland, G A ; Zilversmit, D B</creator><creatorcontrib>McOsker, C C ; Weiland, G A ; Zilversmit, D B</creatorcontrib><description>The nonspecific lipid transfer protein from beef liver was used to modify the phospholipid composition of intact turkey erythrocytes in order to study the dependence of isoproterenol-stimulated adenylate cyclase activity on membrane phospholipid composition. Incorporation of phosphatidylinositol into turkey erythrocytes inhibited isoproterenol-stimulated cyclic AMP accumulation in a linear, concentration-dependent manner. Inhibition was relatively specific for phosphatidylinositol; phosphatidylcholine, phosphatidylethanolamine, phosphatidylserine, phosphatidylglycerol and phosphatidic acid were from 3 to 7 times less effective as inhibitors of hormone-stimulated cyclase activity. Inhibition by phosphatidylinositol was not reversible when up to 90% of the incorporated phosphatidylinositol was removed, either by incubation with phosphatidylinositol-specific phospholipase C or a second incubation with transfer protein; possibly adenylate cyclase activity depends on a small pool of phosphatidylinositol that is inaccessible to either phospholipase C hydrolysis or removal by lipid transfer protein. Phosphatidylinositol incorporation inhibits adenylate cyclase activity by uncoupling beta-adrenergic receptors from the remainder of the cyclase complex. Phosphatidylinositol incorporation had no effect on stimulation of cAMP accumulation by either cholera toxin or forskolin, indicating that inhibition occurs only at the level of receptor. Phosphodiesterase activity was not altered in phosphatidylinositol-modified cells. Inhibition of cAMP accumulation was not the result of changes in either membrane fluidity or in cAMP transport out of modified turkey erythrocytes. Phosphatidylinositol inhibition of isoproterenol-stimulated cyclase activity may serve as a useful model system for hormone-induced desensitization.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1016/S0021-9258(17)44074-9</identifier><identifier>PMID: 6630218</identifier><identifier>CODEN: JBCHA3</identifier><language>eng</language><publisher>Bethesda, MD: Elsevier Inc</publisher><subject>Adenylyl Cyclase Inhibitors ; Adenylyl Cyclases - blood ; Analytical, structural and metabolic biochemistry ; Animals ; Biological and medical sciences ; Carrier Proteins - metabolism ; Catecholamines - blood ; Enzymes and enzyme inhibitors ; Erythrocyte Membrane - metabolism ; Fundamental and applied biological sciences. Psychology ; Isoproterenol - pharmacology ; Kinetics ; Lyases ; Membrane Lipids - blood ; Phosphatidylinositols - pharmacology ; Phospholipids - blood ; Phospholipids - pharmacology ; Protein Binding ; Turkeys</subject><ispartof>The Journal of biological chemistry, 1983-11, Vol.258 (21), p.13017-13026</ispartof><rights>1983 © 1983 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology.</rights><rights>1984 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c397t-dccc2683f78a191bffa5ab5789f037dbcc0251baabea811a1dfe4d4066bd034c3</citedby><cites>FETCH-LOGICAL-c397t-dccc2683f78a191bffa5ab5789f037dbcc0251baabea811a1dfe4d4066bd034c3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=9427283$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/6630218$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>McOsker, C C</creatorcontrib><creatorcontrib>Weiland, G A</creatorcontrib><creatorcontrib>Zilversmit, D B</creatorcontrib><title>Inhibition of hormone-stimulated adenylate cyclase activity after altering turkey erythrocyte phospholipid composition with a nonspecific lipid transfer protein. Phosphatidylinositol uncouples catecholamine binding from adenylate cyclase activation</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>The nonspecific lipid transfer protein from beef liver was used to modify the phospholipid composition of intact turkey erythrocytes in order to study the dependence of isoproterenol-stimulated adenylate cyclase activity on membrane phospholipid composition. Incorporation of phosphatidylinositol into turkey erythrocytes inhibited isoproterenol-stimulated cyclic AMP accumulation in a linear, concentration-dependent manner. Inhibition was relatively specific for phosphatidylinositol; phosphatidylcholine, phosphatidylethanolamine, phosphatidylserine, phosphatidylglycerol and phosphatidic acid were from 3 to 7 times less effective as inhibitors of hormone-stimulated cyclase activity. Inhibition by phosphatidylinositol was not reversible when up to 90% of the incorporated phosphatidylinositol was removed, either by incubation with phosphatidylinositol-specific phospholipase C or a second incubation with transfer protein; possibly adenylate cyclase activity depends on a small pool of phosphatidylinositol that is inaccessible to either phospholipase C hydrolysis or removal by lipid transfer protein. Phosphatidylinositol incorporation inhibits adenylate cyclase activity by uncoupling beta-adrenergic receptors from the remainder of the cyclase complex. Phosphatidylinositol incorporation had no effect on stimulation of cAMP accumulation by either cholera toxin or forskolin, indicating that inhibition occurs only at the level of receptor. Phosphodiesterase activity was not altered in phosphatidylinositol-modified cells. Inhibition of cAMP accumulation was not the result of changes in either membrane fluidity or in cAMP transport out of modified turkey erythrocytes. Phosphatidylinositol inhibition of isoproterenol-stimulated cyclase activity may serve as a useful model system for hormone-induced desensitization.</description><subject>Adenylyl Cyclase Inhibitors</subject><subject>Adenylyl Cyclases - blood</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Carrier Proteins - metabolism</subject><subject>Catecholamines - blood</subject><subject>Enzymes and enzyme inhibitors</subject><subject>Erythrocyte Membrane - metabolism</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Isoproterenol - pharmacology</subject><subject>Kinetics</subject><subject>Lyases</subject><subject>Membrane Lipids - blood</subject><subject>Phosphatidylinositols - pharmacology</subject><subject>Phospholipids - blood</subject><subject>Phospholipids - pharmacology</subject><subject>Protein Binding</subject><subject>Turkeys</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1983</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFUU1rFTEUHUSptfoTClmI6GJq8uZ7JVL8KBQUVHAXMjc3naszyZhkWuafuzTz3qOuxEA-4J5zz8k9WXYu-IXgon79hfOdyLtd1b4Uzauy5E2Zdw-yU8HbIi8q8f1hdnoPeZw9CeEHT6vsxEl2UtdFKrWn2e8rO1BPkZxlzrDB-clZzEOkaRlVRM2URrtuTwYrjCogUxDpluLKlInomRrTSfaGxcX_xJWhX-PgHayJMg8upD3STJqBm2YXDlp3FAemmHU2zAhkCNgBFL2ywaS2s3cRyV6wz_seKpJeR7JbAzeyxYJb5hEDg2QNkoSayCLryerNi_Fu-pd1tTl4mj0yagz47HifZd_ev_t6-TG__vTh6vLtdQ5F18RcA8CubgvTtEp0ojdGVaqvmrYzvGh0D8B3leiV6lG1QiihDZa65HXda16UUJxlLw59039-LRiinCgAjqOy6JYgW96Iqi6LBKwOQPAuBI9Gzp4m5VcpuNwSl_vE5RanFI3cJy67xDs_Ciz9hPqedYw41Z8f6yqAGk2aL1C4h3Xlrtm1xV_YQDfDHXmUPTkYcJKbXtIVBRdNgr05wDDN7JbQywCEFlAnCkSpHf3H7x_UIN9n</recordid><startdate>19831110</startdate><enddate>19831110</enddate><creator>McOsker, C C</creator><creator>Weiland, G A</creator><creator>Zilversmit, D B</creator><general>Elsevier Inc</general><general>American Society for Biochemistry and Molecular Biology</general><scope>6I.</scope><scope>AAFTH</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><scope>7X8</scope></search><sort><creationdate>19831110</creationdate><title>Inhibition of hormone-stimulated adenylate cyclase activity after altering turkey erythrocyte phospholipid composition with a nonspecific lipid transfer protein. Phosphatidylinositol uncouples catecholamine binding from adenylate cyclase activation</title><author>McOsker, C C ; Weiland, G A ; Zilversmit, D B</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c397t-dccc2683f78a191bffa5ab5789f037dbcc0251baabea811a1dfe4d4066bd034c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1983</creationdate><topic>Adenylyl Cyclase Inhibitors</topic><topic>Adenylyl Cyclases - blood</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>Carrier Proteins - metabolism</topic><topic>Catecholamines - blood</topic><topic>Enzymes and enzyme inhibitors</topic><topic>Erythrocyte Membrane - metabolism</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Isoproterenol - pharmacology</topic><topic>Kinetics</topic><topic>Lyases</topic><topic>Membrane Lipids - blood</topic><topic>Phosphatidylinositols - pharmacology</topic><topic>Phospholipids - blood</topic><topic>Phospholipids - pharmacology</topic><topic>Protein Binding</topic><topic>Turkeys</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>McOsker, C C</creatorcontrib><creatorcontrib>Weiland, G A</creatorcontrib><creatorcontrib>Zilversmit, D B</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</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><collection>MEDLINE - Academic</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>McOsker, C C</au><au>Weiland, G A</au><au>Zilversmit, D B</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Inhibition of hormone-stimulated adenylate cyclase activity after altering turkey erythrocyte phospholipid composition with a nonspecific lipid transfer protein. Phosphatidylinositol uncouples catecholamine binding from adenylate cyclase activation</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1983-11-10</date><risdate>1983</risdate><volume>258</volume><issue>21</issue><spage>13017</spage><epage>13026</epage><pages>13017-13026</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><coden>JBCHA3</coden><abstract>The nonspecific lipid transfer protein from beef liver was used to modify the phospholipid composition of intact turkey erythrocytes in order to study the dependence of isoproterenol-stimulated adenylate cyclase activity on membrane phospholipid composition. Incorporation of phosphatidylinositol into turkey erythrocytes inhibited isoproterenol-stimulated cyclic AMP accumulation in a linear, concentration-dependent manner. Inhibition was relatively specific for phosphatidylinositol; phosphatidylcholine, phosphatidylethanolamine, phosphatidylserine, phosphatidylglycerol and phosphatidic acid were from 3 to 7 times less effective as inhibitors of hormone-stimulated cyclase activity. Inhibition by phosphatidylinositol was not reversible when up to 90% of the incorporated phosphatidylinositol was removed, either by incubation with phosphatidylinositol-specific phospholipase C or a second incubation with transfer protein; possibly adenylate cyclase activity depends on a small pool of phosphatidylinositol that is inaccessible to either phospholipase C hydrolysis or removal by lipid transfer protein. Phosphatidylinositol incorporation inhibits adenylate cyclase activity by uncoupling beta-adrenergic receptors from the remainder of the cyclase complex. Phosphatidylinositol incorporation had no effect on stimulation of cAMP accumulation by either cholera toxin or forskolin, indicating that inhibition occurs only at the level of receptor. Phosphodiesterase activity was not altered in phosphatidylinositol-modified cells. Inhibition of cAMP accumulation was not the result of changes in either membrane fluidity or in cAMP transport out of modified turkey erythrocytes. Phosphatidylinositol inhibition of isoproterenol-stimulated cyclase activity may serve as a useful model system for hormone-induced desensitization.</abstract><cop>Bethesda, MD</cop><pub>Elsevier Inc</pub><pmid>6630218</pmid><doi>10.1016/S0021-9258(17)44074-9</doi><tpages>10</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | The Journal of biological chemistry, 1983-11, Vol.258 (21), p.13017-13026 |
| issn | 0021-9258 1083-351X |
| language | eng |
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| source | MEDLINE; EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection |
| subjects | Adenylyl Cyclase Inhibitors Adenylyl Cyclases - blood Analytical, structural and metabolic biochemistry Animals Biological and medical sciences Carrier Proteins - metabolism Catecholamines - blood Enzymes and enzyme inhibitors Erythrocyte Membrane - metabolism Fundamental and applied biological sciences. Psychology Isoproterenol - pharmacology Kinetics Lyases Membrane Lipids - blood Phosphatidylinositols - pharmacology Phospholipids - blood Phospholipids - pharmacology Protein Binding Turkeys |
| title | Inhibition of hormone-stimulated adenylate cyclase activity after altering turkey erythrocyte phospholipid composition with a nonspecific lipid transfer protein. Phosphatidylinositol uncouples catecholamine binding from adenylate cyclase activation |
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