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Article: Simultaneous activation of adenylyl cyclase and protein kinase C induces production of nitric oxide by vascular smooth muscle cells

TitleSimultaneous activation of adenylyl cyclase and protein kinase C induces production of nitric oxide by vascular smooth muscle cells
Authors
Issue Date1994
PublisherAmerican Society for Pharmacology and Experimental Therapeutics. The Journal's web site is located at http://www.molpharm.org
Citation
Molecular Pharmacology, 1994, v. 46 n. 2, p. 274-282 How to Cite?
AbstractRat aortic smooth muscle cells produced large quantities of nitric oxide (NO) after exposure to interleukin-1β, and this was depressed in the presence of the protein kinase C inhibitor bisindolylmaleimide. Intracellular cAMP levels were elevated mildly in cytokine-treated smooth muscle cells, and the presence of forskolin enhanced both the cAMP levels and NO production. Inhibition of GTP:cyclohydrolase I by 2,4-diamino-6-hydroxypyrimidine attenuated NO production by interleukin-1β-treated cells. GTP:cyclohydrolase is the regulatory enzyme for de novo tetrahydrobiopterin synthesis, and the latter is a required cofactor for NO synthase activity. Treatment of smooth muscle cells with forskolin induced GTP:cyclohydrolase mRNA expression, and simultaneous treatment of cells with forskolin and phorbol esters elicited NO production. Angiotensin II and arginine-vasopressin, acknowledged agonists for protein kinase C, elicited production of NO by forskolin-treated smooth muscle cells. These observations confirm the importance of GTP:cyclohydrolase activity for NO production by cultured smooth muscle cells and implicate both adenylyl cyclase and protein kinase C in this process.
Persistent Identifierhttp://hdl.handle.net/10722/171128
ISSN
2015 Impact Factor: 3.931
2015 SCImago Journal Rankings: 2.047
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorScottBurden, Ten_US
dc.contributor.authorElizondo, Een_US
dc.contributor.authorGe, Ten_US
dc.contributor.authorBoulanger, CMen_US
dc.contributor.authorVanhoutte, PMen_US
dc.date.accessioned2012-10-30T06:12:18Z-
dc.date.available2012-10-30T06:12:18Z-
dc.date.issued1994en_US
dc.identifier.citationMolecular Pharmacology, 1994, v. 46 n. 2, p. 274-282en_US
dc.identifier.issn0026-895Xen_US
dc.identifier.urihttp://hdl.handle.net/10722/171128-
dc.description.abstractRat aortic smooth muscle cells produced large quantities of nitric oxide (NO) after exposure to interleukin-1β, and this was depressed in the presence of the protein kinase C inhibitor bisindolylmaleimide. Intracellular cAMP levels were elevated mildly in cytokine-treated smooth muscle cells, and the presence of forskolin enhanced both the cAMP levels and NO production. Inhibition of GTP:cyclohydrolase I by 2,4-diamino-6-hydroxypyrimidine attenuated NO production by interleukin-1β-treated cells. GTP:cyclohydrolase is the regulatory enzyme for de novo tetrahydrobiopterin synthesis, and the latter is a required cofactor for NO synthase activity. Treatment of smooth muscle cells with forskolin induced GTP:cyclohydrolase mRNA expression, and simultaneous treatment of cells with forskolin and phorbol esters elicited NO production. Angiotensin II and arginine-vasopressin, acknowledged agonists for protein kinase C, elicited production of NO by forskolin-treated smooth muscle cells. These observations confirm the importance of GTP:cyclohydrolase activity for NO production by cultured smooth muscle cells and implicate both adenylyl cyclase and protein kinase C in this process.en_US
dc.languageengen_US
dc.publisherAmerican Society for Pharmacology and Experimental Therapeutics. The Journal's web site is located at http://www.molpharm.orgen_US
dc.relation.ispartofMolecular Pharmacologyen_US
dc.subject.meshAdenylate Cyclase - Metabolismen_US
dc.subject.meshAmino Acid Oxidoreductases - Biosynthesis - Metabolismen_US
dc.subject.meshAnimalsen_US
dc.subject.meshCells, Cultureden_US
dc.subject.meshCyclic Amp - Pharmacologyen_US
dc.subject.meshEnzyme Activationen_US
dc.subject.meshForskolin - Pharmacologyen_US
dc.subject.meshGtp Cyclohydrolase - Antagonists & Inhibitors - Genetics - Metabolismen_US
dc.subject.meshGene Expression Regulation, Enzymologicen_US
dc.subject.meshIndoles - Pharmacologyen_US
dc.subject.meshInterleukin-1 - Pharmacologyen_US
dc.subject.meshMaleimides - Pharmacologyen_US
dc.subject.meshMuscle, Smooth, Vascular - Cytology - Enzymology - Metabolismen_US
dc.subject.meshNitric Oxide - Biosynthesisen_US
dc.subject.meshNitric Oxide Synthaseen_US
dc.subject.meshProtein Kinase C - Metabolismen_US
dc.subject.meshRna, Messenger - Metabolismen_US
dc.subject.meshRatsen_US
dc.subject.meshSignal Transductionen_US
dc.titleSimultaneous activation of adenylyl cyclase and protein kinase C induces production of nitric oxide by vascular smooth muscle cellsen_US
dc.typeArticleen_US
dc.identifier.emailVanhoutte, PM:vanhoutt@hku.hken_US
dc.identifier.authorityVanhoutte, PM=rp00238en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.pmid7521513-
dc.identifier.scopuseid_2-s2.0-0028141485en_US
dc.identifier.volume46en_US
dc.identifier.issue2en_US
dc.identifier.spage274en_US
dc.identifier.epage282en_US
dc.identifier.isiWOS:A1994PE36400008-
dc.publisher.placeUnited Statesen_US
dc.identifier.scopusauthoridScottBurden, T=7004306459en_US
dc.identifier.scopusauthoridElizondo, E=6603922947en_US
dc.identifier.scopusauthoridGe, T=7003328740en_US
dc.identifier.scopusauthoridBoulanger, CM=7006599024en_US
dc.identifier.scopusauthoridVanhoutte, PM=7202304247en_US

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