Both beta(2)- and beta(1)-adrenergic receptors mediate hastened relaxation and phosphorylation of phospholamban and troponin I in ventricular myocardium of Fallot infants, consistent with selective coupling of beta(2)-adrenergic receptors to G(s)-protein
In adult human heart, both beta(1)- and beta(2)-adrenergic receptors mediate hastening of relaxation; however, it is unknown whether this also occurs in infant heart. We compared the effects of stimulation of beta(1)- and beta(2)-adrenergic receptors on relaxation and phosphorylation of phospholamba...
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| Veröffentlicht in: | Circulation (New York, N.Y.) N.Y.), 2000-10, Vol.102 (15), p.1814-1821 |
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| creator | Molenaar, P Bartel, S Cochrane, A Vetter, D Jalali, H Pohlner, P Burrell, K Karczewski, P Krause, E G Kaumann, A |
| description | In adult human heart, both beta(1)- and beta(2)-adrenergic receptors mediate hastening of relaxation; however, it is unknown whether this also occurs in infant heart. We compared the effects of stimulation of beta(1)- and beta(2)-adrenergic receptors on relaxation and phosphorylation of phospholamban and troponin I in ventricle obtained from infants with tetralogy of Fallot.
Myocardium dissected from the right ventricular outflow tract of 27 infants (age range 21/2 to 35 months) with tetralogy of Fallot was set up to contract 60 times per minute. Selective stimulation of beta(1)-adrenergic receptors with (-)-norepinephrine (NE) and beta(2)-adrenergic receptors with (-)-epinephrine (EPI) evoked phosphorylation of phospholamban (at serine-16 and threonine-17) and troponin I and caused concentration-dependent increases in contractile force (-log EC(50) [mol/L] NE 5.5+/-0.1, n=12; EPI 5.6+/-0.1, n=13 patients), hastening of the time to reach peak force (-log EC(50) [mol/L] NE 5.8+/-0.2; EPI 5.8+/-0.2) and 50% relaxation (-log EC(50) [mol/L] NE 5.7+/-0.2; EPI 5.8+/-0.1). Ventricular membranes from Fallot infants, labeled with (-)-[(125)I]-cyanopindolol, revealed a greater percentage of beta(1)- (71%) than beta(2)-adrenergic receptors (29%). Binding of (-)-epinephrine to beta(2)-receptors underwent greater GTP shifts than binding of (-)-norepinephrine to beta(1)-receptors.
Despite their low density, beta(2)-adrenergic receptors are nearly as effective as beta(1)-adrenergic receptors of infant Fallot ventricle in enhancing contraction, relaxation, and phosphorylation of phospholamban and troponin I, consistent with selective coupling to G(s)-protein. |
| doi_str_mv | 10.1161/01.cir.102.15.1814 |
| format | Article |
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Myocardium dissected from the right ventricular outflow tract of 27 infants (age range 21/2 to 35 months) with tetralogy of Fallot was set up to contract 60 times per minute. Selective stimulation of beta(1)-adrenergic receptors with (-)-norepinephrine (NE) and beta(2)-adrenergic receptors with (-)-epinephrine (EPI) evoked phosphorylation of phospholamban (at serine-16 and threonine-17) and troponin I and caused concentration-dependent increases in contractile force (-log EC(50) [mol/L] NE 5.5+/-0.1, n=12; EPI 5.6+/-0.1, n=13 patients), hastening of the time to reach peak force (-log EC(50) [mol/L] NE 5.8+/-0.2; EPI 5.8+/-0.2) and 50% relaxation (-log EC(50) [mol/L] NE 5.7+/-0.2; EPI 5.8+/-0.1). Ventricular membranes from Fallot infants, labeled with (-)-[(125)I]-cyanopindolol, revealed a greater percentage of beta(1)- (71%) than beta(2)-adrenergic receptors (29%). Binding of (-)-epinephrine to beta(2)-receptors underwent greater GTP shifts than binding of (-)-norepinephrine to beta(1)-receptors.
Despite their low density, beta(2)-adrenergic receptors are nearly as effective as beta(1)-adrenergic receptors of infant Fallot ventricle in enhancing contraction, relaxation, and phosphorylation of phospholamban and troponin I, consistent with selective coupling to G(s)-protein.</description><identifier>EISSN: 1524-4539</identifier><identifier>DOI: 10.1161/01.cir.102.15.1814</identifier><identifier>PMID: 11023937</identifier><language>eng</language><publisher>United States</publisher><subject>Calcium-Binding Proteins - metabolism ; Child, Preschool ; Cyclic AMP-Dependent Protein Kinases - metabolism ; Epinephrine - metabolism ; Female ; GTP-Binding Protein alpha Subunits, Gs - metabolism ; Guanosine Triphosphate - metabolism ; Heart Ventricles - cytology ; Heart Ventricles - physiopathology ; Humans ; Infant ; Male ; Myocardial Contraction ; Myocardium - metabolism ; Myocardium - pathology ; Phosphorylation ; Receptors, Adrenergic, beta-1 - metabolism ; Receptors, Adrenergic, beta-2 - metabolism ; Serine - metabolism ; Tetralogy of Fallot - metabolism ; Threonine - metabolism ; Troponin I - metabolism</subject><ispartof>Circulation (New York, N.Y.), 2000-10, Vol.102 (15), p.1814-1821</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>315,782,786,27933,27934</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11023937$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Molenaar, P</creatorcontrib><creatorcontrib>Bartel, S</creatorcontrib><creatorcontrib>Cochrane, A</creatorcontrib><creatorcontrib>Vetter, D</creatorcontrib><creatorcontrib>Jalali, H</creatorcontrib><creatorcontrib>Pohlner, P</creatorcontrib><creatorcontrib>Burrell, K</creatorcontrib><creatorcontrib>Karczewski, P</creatorcontrib><creatorcontrib>Krause, E G</creatorcontrib><creatorcontrib>Kaumann, A</creatorcontrib><title>Both beta(2)- and beta(1)-adrenergic receptors mediate hastened relaxation and phosphorylation of phospholamban and troponin I in ventricular myocardium of Fallot infants, consistent with selective coupling of beta(2)-adrenergic receptors to G(s)-protein</title><title>Circulation (New York, N.Y.)</title><addtitle>Circulation</addtitle><description>In adult human heart, both beta(1)- and beta(2)-adrenergic receptors mediate hastening of relaxation; however, it is unknown whether this also occurs in infant heart. We compared the effects of stimulation of beta(1)- and beta(2)-adrenergic receptors on relaxation and phosphorylation of phospholamban and troponin I in ventricle obtained from infants with tetralogy of Fallot.
Myocardium dissected from the right ventricular outflow tract of 27 infants (age range 21/2 to 35 months) with tetralogy of Fallot was set up to contract 60 times per minute. Selective stimulation of beta(1)-adrenergic receptors with (-)-norepinephrine (NE) and beta(2)-adrenergic receptors with (-)-epinephrine (EPI) evoked phosphorylation of phospholamban (at serine-16 and threonine-17) and troponin I and caused concentration-dependent increases in contractile force (-log EC(50) [mol/L] NE 5.5+/-0.1, n=12; EPI 5.6+/-0.1, n=13 patients), hastening of the time to reach peak force (-log EC(50) [mol/L] NE 5.8+/-0.2; EPI 5.8+/-0.2) and 50% relaxation (-log EC(50) [mol/L] NE 5.7+/-0.2; EPI 5.8+/-0.1). Ventricular membranes from Fallot infants, labeled with (-)-[(125)I]-cyanopindolol, revealed a greater percentage of beta(1)- (71%) than beta(2)-adrenergic receptors (29%). Binding of (-)-epinephrine to beta(2)-receptors underwent greater GTP shifts than binding of (-)-norepinephrine to beta(1)-receptors.
Despite their low density, beta(2)-adrenergic receptors are nearly as effective as beta(1)-adrenergic receptors of infant Fallot ventricle in enhancing contraction, relaxation, and phosphorylation of phospholamban and troponin I, consistent with selective coupling to G(s)-protein.</description><subject>Calcium-Binding Proteins - metabolism</subject><subject>Child, Preschool</subject><subject>Cyclic AMP-Dependent Protein Kinases - metabolism</subject><subject>Epinephrine - metabolism</subject><subject>Female</subject><subject>GTP-Binding Protein alpha Subunits, Gs - metabolism</subject><subject>Guanosine Triphosphate - metabolism</subject><subject>Heart Ventricles - cytology</subject><subject>Heart Ventricles - physiopathology</subject><subject>Humans</subject><subject>Infant</subject><subject>Male</subject><subject>Myocardial Contraction</subject><subject>Myocardium - metabolism</subject><subject>Myocardium - pathology</subject><subject>Phosphorylation</subject><subject>Receptors, Adrenergic, beta-1 - metabolism</subject><subject>Receptors, Adrenergic, beta-2 - metabolism</subject><subject>Serine - metabolism</subject><subject>Tetralogy of Fallot - metabolism</subject><subject>Threonine - metabolism</subject><subject>Troponin I - metabolism</subject><issn>1524-4539</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2000</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNptkU1P4zAQhi0ktHzs_oE9IJ8QlUjwxPlojoD4kpD2spyriTOlRo4dbAe2fx6tS-mNg8fyvM_rGY8Z-w0iB6jhQkCutM9BFDlUOcyh3GOHUBVlVlayPWBHIbwIIWrZVD_YASROtrI5ZB9XLq54RxHPilnG0fbbA8wy7D1Z8s9acU-Kxuh84AP1GiPxFYaY1D5JBv9h1M5-mseVC2n5tdnm3HKXMjh0uIWid6Oz2vIHnsIb2ei1mgx6PqydQt_radg4b9EYFxOzRBvDOVfOBr2pG_m7Tm0HMqSifqOkTKPR9nnj2j3m2_6j43dnYZaN3kXS9ifbX6IJ9OtrP2ZPtzd_r--zxz93D9eXj9kIso1Zhyjn1EpooCwphU7Ivu4KoaCiCmtZpnHWApYFtD12JGRD9bzsykaoxNbymJ1u7011XycKcTHooMgYtOSmsGgKWRRV3STw5AucujTrxej1gH692P2Y_A--3JyQ</recordid><startdate>20001010</startdate><enddate>20001010</enddate><creator>Molenaar, P</creator><creator>Bartel, S</creator><creator>Cochrane, A</creator><creator>Vetter, D</creator><creator>Jalali, H</creator><creator>Pohlner, P</creator><creator>Burrell, K</creator><creator>Karczewski, P</creator><creator>Krause, E G</creator><creator>Kaumann, A</creator><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7X8</scope></search><sort><creationdate>20001010</creationdate><title>Both beta(2)- and beta(1)-adrenergic receptors mediate hastened relaxation and phosphorylation of phospholamban and troponin I in ventricular myocardium of Fallot infants, consistent with selective coupling of beta(2)-adrenergic receptors to G(s)-protein</title><author>Molenaar, P ; Bartel, S ; Cochrane, A ; Vetter, D ; Jalali, H ; Pohlner, P ; Burrell, K ; Karczewski, P ; Krause, E G ; Kaumann, A</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-p139t-baa38e9317144e714b03d6b20c15e5a634239601f219dabe037e684b470c4b063</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2000</creationdate><topic>Calcium-Binding Proteins - metabolism</topic><topic>Child, Preschool</topic><topic>Cyclic AMP-Dependent Protein Kinases - metabolism</topic><topic>Epinephrine - metabolism</topic><topic>Female</topic><topic>GTP-Binding Protein alpha Subunits, Gs - metabolism</topic><topic>Guanosine Triphosphate - metabolism</topic><topic>Heart Ventricles - cytology</topic><topic>Heart Ventricles - physiopathology</topic><topic>Humans</topic><topic>Infant</topic><topic>Male</topic><topic>Myocardial Contraction</topic><topic>Myocardium - metabolism</topic><topic>Myocardium - pathology</topic><topic>Phosphorylation</topic><topic>Receptors, Adrenergic, beta-1 - metabolism</topic><topic>Receptors, Adrenergic, beta-2 - metabolism</topic><topic>Serine - metabolism</topic><topic>Tetralogy of Fallot - metabolism</topic><topic>Threonine - metabolism</topic><topic>Troponin I - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Molenaar, P</creatorcontrib><creatorcontrib>Bartel, S</creatorcontrib><creatorcontrib>Cochrane, A</creatorcontrib><creatorcontrib>Vetter, D</creatorcontrib><creatorcontrib>Jalali, H</creatorcontrib><creatorcontrib>Pohlner, P</creatorcontrib><creatorcontrib>Burrell, K</creatorcontrib><creatorcontrib>Karczewski, P</creatorcontrib><creatorcontrib>Krause, E G</creatorcontrib><creatorcontrib>Kaumann, A</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>MEDLINE - Academic</collection><jtitle>Circulation (New York, N.Y.)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Molenaar, P</au><au>Bartel, S</au><au>Cochrane, A</au><au>Vetter, D</au><au>Jalali, H</au><au>Pohlner, P</au><au>Burrell, K</au><au>Karczewski, P</au><au>Krause, E G</au><au>Kaumann, A</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Both beta(2)- and beta(1)-adrenergic receptors mediate hastened relaxation and phosphorylation of phospholamban and troponin I in ventricular myocardium of Fallot infants, consistent with selective coupling of beta(2)-adrenergic receptors to G(s)-protein</atitle><jtitle>Circulation (New York, N.Y.)</jtitle><addtitle>Circulation</addtitle><date>2000-10-10</date><risdate>2000</risdate><volume>102</volume><issue>15</issue><spage>1814</spage><epage>1821</epage><pages>1814-1821</pages><eissn>1524-4539</eissn><abstract>In adult human heart, both beta(1)- and beta(2)-adrenergic receptors mediate hastening of relaxation; however, it is unknown whether this also occurs in infant heart. We compared the effects of stimulation of beta(1)- and beta(2)-adrenergic receptors on relaxation and phosphorylation of phospholamban and troponin I in ventricle obtained from infants with tetralogy of Fallot.
Myocardium dissected from the right ventricular outflow tract of 27 infants (age range 21/2 to 35 months) with tetralogy of Fallot was set up to contract 60 times per minute. Selective stimulation of beta(1)-adrenergic receptors with (-)-norepinephrine (NE) and beta(2)-adrenergic receptors with (-)-epinephrine (EPI) evoked phosphorylation of phospholamban (at serine-16 and threonine-17) and troponin I and caused concentration-dependent increases in contractile force (-log EC(50) [mol/L] NE 5.5+/-0.1, n=12; EPI 5.6+/-0.1, n=13 patients), hastening of the time to reach peak force (-log EC(50) [mol/L] NE 5.8+/-0.2; EPI 5.8+/-0.2) and 50% relaxation (-log EC(50) [mol/L] NE 5.7+/-0.2; EPI 5.8+/-0.1). Ventricular membranes from Fallot infants, labeled with (-)-[(125)I]-cyanopindolol, revealed a greater percentage of beta(1)- (71%) than beta(2)-adrenergic receptors (29%). Binding of (-)-epinephrine to beta(2)-receptors underwent greater GTP shifts than binding of (-)-norepinephrine to beta(1)-receptors.
Despite their low density, beta(2)-adrenergic receptors are nearly as effective as beta(1)-adrenergic receptors of infant Fallot ventricle in enhancing contraction, relaxation, and phosphorylation of phospholamban and troponin I, consistent with selective coupling to G(s)-protein.</abstract><cop>United States</cop><pmid>11023937</pmid><doi>10.1161/01.cir.102.15.1814</doi><tpages>8</tpages></addata></record> |
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| source | MEDLINE; American Heart Association Journals; EZB-FREE-00999 freely available EZB journals; Journals@Ovid Complete |
| subjects | Calcium-Binding Proteins - metabolism Child, Preschool Cyclic AMP-Dependent Protein Kinases - metabolism Epinephrine - metabolism Female GTP-Binding Protein alpha Subunits, Gs - metabolism Guanosine Triphosphate - metabolism Heart Ventricles - cytology Heart Ventricles - physiopathology Humans Infant Male Myocardial Contraction Myocardium - metabolism Myocardium - pathology Phosphorylation Receptors, Adrenergic, beta-1 - metabolism Receptors, Adrenergic, beta-2 - metabolism Serine - metabolism Tetralogy of Fallot - metabolism Threonine - metabolism Troponin I - metabolism |
| title | Both beta(2)- and beta(1)-adrenergic receptors mediate hastened relaxation and phosphorylation of phospholamban and troponin I in ventricular myocardium of Fallot infants, consistent with selective coupling of beta(2)-adrenergic receptors to G(s)-protein |
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