Subclasses of cyclic AMP phosphodiesterase in cardiac muscle
Canine and guinea-pig left ventricular muscle contains multiple molecular forms of phosphodiesterase (PDE) which vary according to substrate specificity, stimulation by calmodulin and response to various selective and nonselective phosphodiesterase inhibitors. Both species possess a cyclic AMP-speci...
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Veröffentlicht in: | Journal of molecular and cellular cardiology 1987-10, Vol.19 (10), p.1025-1036 |
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description | Canine and guinea-pig left ventricular muscle contains multiple molecular forms of phosphodiesterase (PDE) which vary according to substrate specificity, stimulation by calmodulin and response to various selective and nonselective phosphodiesterase inhibitors. Both species possess a cyclic AMP-specific form of phosphodiesterase (PDE III). In the dog both soluble and particulate forms of PDE III are present. The particulate form of PDE III is potently inhibited by cyclic GMP and the selective PDE III inhibitors imazodan (CI-914) and cilostamide, but is only weakly inhibited by the selective PDE III inhibitors Ro 20-1724 and rolipram. In contrast, the soluble form of PDE III in canine left ventrcile is only weakly inhibited by cyclic GMP, imazodan and cilostamide, but is potently inhibited by Ro 20-1724 and rolipram. Guinea-pig left ventricle contains only one subclass of PDE III, which is potently inhibited by cyclic GMP, imazodan and cilostamide, but not by Ro 20-1724 or rolipram. However, whereas the imazodan-sensitive subclass of PDE III is a particulate enzyme in the canine left ventricle, in the guinea-pig this subclass of PDE III is a soluble enzyme. Both soluble and particulate PDE III's are (i) insensitive to calmodulin; (ii) possess comparable
K
m and
V
max values for hydrolysis of cyclic AMP; (iii) are equally inhibited by the nonselective PDE inhibitor theophylline, and (iv) are eluted from DEAE-cellulose anion-exchange resin by comparable concentrations of sodium acetate. The demonstration of distinct subclasses of the cyclic AMP-specific phosphodiesterase (PDE III) in canine left ventricular muscle associated with different domains of the cell suggests compartmentation of cyclic AMP. In addition, the observation that the imazodan-sensitive form of PDE III is a particulate enzyme in canine left ventricle and a soluble enzyme in guinea-pig left ventricle may explain the species differences which exist regarding the positive inotropic response to imazodan in these two species. |
doi_str_mv | 10.1016/S0022-2828(87)80574-6 |
format | Article |
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K
m and
V
max values for hydrolysis of cyclic AMP; (iii) are equally inhibited by the nonselective PDE inhibitor theophylline, and (iv) are eluted from DEAE-cellulose anion-exchange resin by comparable concentrations of sodium acetate. The demonstration of distinct subclasses of the cyclic AMP-specific phosphodiesterase (PDE III) in canine left ventricular muscle associated with different domains of the cell suggests compartmentation of cyclic AMP. In addition, the observation that the imazodan-sensitive form of PDE III is a particulate enzyme in canine left ventricle and a soluble enzyme in guinea-pig left ventricle may explain the species differences which exist regarding the positive inotropic response to imazodan in these two species.</description><identifier>ISSN: 0022-2828</identifier><identifier>EISSN: 1095-8584</identifier><identifier>DOI: 10.1016/S0022-2828(87)80574-6</identifier><identifier>PMID: 2830402</identifier><identifier>CODEN: JMCDAY</identifier><language>eng</language><publisher>Kent: Elsevier Ltd</publisher><subject>3',5'-Cyclic-AMP Phosphodiesterases - isolation & purification ; 3',5'-Cyclic-AMP Phosphodiesterases - metabolism ; Analytical, structural and metabolic biochemistry ; Animals ; Biological and medical sciences ; Cardiac muscle ; Cardiotonic ; Contractility ; Cyclic AMP ; Dogs ; Enzymes and enzyme inhibitors ; Fundamental and applied biological sciences. Psychology ; Guinea Pigs ; Heart Ventricles - enzymology ; Hydrolases ; Isoenzymes - isolation & purification ; Isoenzymes - metabolism ; Kinetics ; Myocardium - enzymology ; Phosphodiesterase ; Species Specificity</subject><ispartof>Journal of molecular and cellular cardiology, 1987-10, Vol.19 (10), p.1025-1036</ispartof><rights>1987 Academic Press Limited</rights><rights>1988 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c389t-8984e48d98ffb54a348b6e9416be21217c8f6aa0733c8a37db2bf2cf8e7491b73</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/S0022-2828(87)80574-6$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=7547288$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/2830402$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Weishaar, Ronald E.</creatorcontrib><creatorcontrib>Kobylarz-Singer, Dianne C.</creatorcontrib><creatorcontrib>Kaplan, Harvey R.</creatorcontrib><title>Subclasses of cyclic AMP phosphodiesterase in cardiac muscle</title><title>Journal of molecular and cellular cardiology</title><addtitle>J Mol Cell Cardiol</addtitle><description>Canine and guinea-pig left ventricular muscle contains multiple molecular forms of phosphodiesterase (PDE) which vary according to substrate specificity, stimulation by calmodulin and response to various selective and nonselective phosphodiesterase inhibitors. Both species possess a cyclic AMP-specific form of phosphodiesterase (PDE III). In the dog both soluble and particulate forms of PDE III are present. The particulate form of PDE III is potently inhibited by cyclic GMP and the selective PDE III inhibitors imazodan (CI-914) and cilostamide, but is only weakly inhibited by the selective PDE III inhibitors Ro 20-1724 and rolipram. In contrast, the soluble form of PDE III in canine left ventrcile is only weakly inhibited by cyclic GMP, imazodan and cilostamide, but is potently inhibited by Ro 20-1724 and rolipram. Guinea-pig left ventricle contains only one subclass of PDE III, which is potently inhibited by cyclic GMP, imazodan and cilostamide, but not by Ro 20-1724 or rolipram. However, whereas the imazodan-sensitive subclass of PDE III is a particulate enzyme in the canine left ventricle, in the guinea-pig this subclass of PDE III is a soluble enzyme. Both soluble and particulate PDE III's are (i) insensitive to calmodulin; (ii) possess comparable
K
m and
V
max values for hydrolysis of cyclic AMP; (iii) are equally inhibited by the nonselective PDE inhibitor theophylline, and (iv) are eluted from DEAE-cellulose anion-exchange resin by comparable concentrations of sodium acetate. The demonstration of distinct subclasses of the cyclic AMP-specific phosphodiesterase (PDE III) in canine left ventricular muscle associated with different domains of the cell suggests compartmentation of cyclic AMP. In addition, the observation that the imazodan-sensitive form of PDE III is a particulate enzyme in canine left ventricle and a soluble enzyme in guinea-pig left ventricle may explain the species differences which exist regarding the positive inotropic response to imazodan in these two species.</description><subject>3',5'-Cyclic-AMP Phosphodiesterases - isolation & purification</subject><subject>3',5'-Cyclic-AMP Phosphodiesterases - metabolism</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Cardiac muscle</subject><subject>Cardiotonic</subject><subject>Contractility</subject><subject>Cyclic AMP</subject><subject>Dogs</subject><subject>Enzymes and enzyme inhibitors</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Guinea Pigs</subject><subject>Heart Ventricles - enzymology</subject><subject>Hydrolases</subject><subject>Isoenzymes - isolation & purification</subject><subject>Isoenzymes - metabolism</subject><subject>Kinetics</subject><subject>Myocardium - enzymology</subject><subject>Phosphodiesterase</subject><subject>Species Specificity</subject><issn>0022-2828</issn><issn>1095-8584</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1987</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkE1r20AQhpeSkDhpf0JAhxKag5L9knYEgWBC2wQcWkh7XlajWbpBttwdq5B_Xzk2vuYwzGGemXl5hLhQ8lpJVd88S6l1qUHDF3BXICtny_qDmCnZVCVUYI_E7ICcijPmFyllY405EScajLRSz8Tt89hiH5iJiyEW-Ip9wmL-9LNY_xl4qi4RbygHpiKtCgy5SwGL5cjY00dxHEPP9Gnfz8Xvb19_3T-Uix_fH-_nixINNJsSGrBkoWsgxraywVhoa2qsqlvSSiuHEOsQpDMGIRjXtbqNGiOQs41qnTkXl7u76zz8Hac8fpkYqe_DioaRvXONgcrpCax2IOaBOVP065yWIb96Jf3Wmn-z5rdKPDj_Zs3X097F_sHYLqk7bO01TfPP-3lgDH3MYYWJD5irrNMAE3a3w2iS8S9R9oyJVkhdyoQb3w3pnSD_Ab9BiCc</recordid><startdate>19871001</startdate><enddate>19871001</enddate><creator>Weishaar, Ronald E.</creator><creator>Kobylarz-Singer, Dianne C.</creator><creator>Kaplan, Harvey R.</creator><general>Elsevier Ltd</general><general>Elsevier</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>7X8</scope></search><sort><creationdate>19871001</creationdate><title>Subclasses of cyclic AMP phosphodiesterase in cardiac muscle</title><author>Weishaar, Ronald E. ; Kobylarz-Singer, Dianne C. ; Kaplan, Harvey R.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c389t-8984e48d98ffb54a348b6e9416be21217c8f6aa0733c8a37db2bf2cf8e7491b73</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1987</creationdate><topic>3',5'-Cyclic-AMP Phosphodiesterases - isolation & purification</topic><topic>3',5'-Cyclic-AMP Phosphodiesterases - metabolism</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>Cardiac muscle</topic><topic>Cardiotonic</topic><topic>Contractility</topic><topic>Cyclic AMP</topic><topic>Dogs</topic><topic>Enzymes and enzyme inhibitors</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Guinea Pigs</topic><topic>Heart Ventricles - enzymology</topic><topic>Hydrolases</topic><topic>Isoenzymes - isolation & purification</topic><topic>Isoenzymes - metabolism</topic><topic>Kinetics</topic><topic>Myocardium - enzymology</topic><topic>Phosphodiesterase</topic><topic>Species Specificity</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Weishaar, Ronald E.</creatorcontrib><creatorcontrib>Kobylarz-Singer, Dianne C.</creatorcontrib><creatorcontrib>Kaplan, Harvey R.</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>MEDLINE - Academic</collection><jtitle>Journal of molecular and cellular cardiology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Weishaar, Ronald E.</au><au>Kobylarz-Singer, Dianne C.</au><au>Kaplan, Harvey R.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Subclasses of cyclic AMP phosphodiesterase in cardiac muscle</atitle><jtitle>Journal of molecular and cellular cardiology</jtitle><addtitle>J Mol Cell Cardiol</addtitle><date>1987-10-01</date><risdate>1987</risdate><volume>19</volume><issue>10</issue><spage>1025</spage><epage>1036</epage><pages>1025-1036</pages><issn>0022-2828</issn><eissn>1095-8584</eissn><coden>JMCDAY</coden><abstract>Canine and guinea-pig left ventricular muscle contains multiple molecular forms of phosphodiesterase (PDE) which vary according to substrate specificity, stimulation by calmodulin and response to various selective and nonselective phosphodiesterase inhibitors. Both species possess a cyclic AMP-specific form of phosphodiesterase (PDE III). In the dog both soluble and particulate forms of PDE III are present. The particulate form of PDE III is potently inhibited by cyclic GMP and the selective PDE III inhibitors imazodan (CI-914) and cilostamide, but is only weakly inhibited by the selective PDE III inhibitors Ro 20-1724 and rolipram. In contrast, the soluble form of PDE III in canine left ventrcile is only weakly inhibited by cyclic GMP, imazodan and cilostamide, but is potently inhibited by Ro 20-1724 and rolipram. Guinea-pig left ventricle contains only one subclass of PDE III, which is potently inhibited by cyclic GMP, imazodan and cilostamide, but not by Ro 20-1724 or rolipram. However, whereas the imazodan-sensitive subclass of PDE III is a particulate enzyme in the canine left ventricle, in the guinea-pig this subclass of PDE III is a soluble enzyme. Both soluble and particulate PDE III's are (i) insensitive to calmodulin; (ii) possess comparable
K
m and
V
max values for hydrolysis of cyclic AMP; (iii) are equally inhibited by the nonselective PDE inhibitor theophylline, and (iv) are eluted from DEAE-cellulose anion-exchange resin by comparable concentrations of sodium acetate. The demonstration of distinct subclasses of the cyclic AMP-specific phosphodiesterase (PDE III) in canine left ventricular muscle associated with different domains of the cell suggests compartmentation of cyclic AMP. In addition, the observation that the imazodan-sensitive form of PDE III is a particulate enzyme in canine left ventricle and a soluble enzyme in guinea-pig left ventricle may explain the species differences which exist regarding the positive inotropic response to imazodan in these two species.</abstract><cop>Kent</cop><pub>Elsevier Ltd</pub><pmid>2830402</pmid><doi>10.1016/S0022-2828(87)80574-6</doi><tpages>12</tpages></addata></record> |
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subjects | 3',5'-Cyclic-AMP Phosphodiesterases - isolation & purification 3',5'-Cyclic-AMP Phosphodiesterases - metabolism Analytical, structural and metabolic biochemistry Animals Biological and medical sciences Cardiac muscle Cardiotonic Contractility Cyclic AMP Dogs Enzymes and enzyme inhibitors Fundamental and applied biological sciences. Psychology Guinea Pigs Heart Ventricles - enzymology Hydrolases Isoenzymes - isolation & purification Isoenzymes - metabolism Kinetics Myocardium - enzymology Phosphodiesterase Species Specificity |
title | Subclasses of cyclic AMP phosphodiesterase in cardiac muscle |
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