<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Bogard AS</submitter><funding>NHLBI NIH HHS</funding><pagination>586-95</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC3400804</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>342(2)</volume><pubmed_abstract>Adenylyl cyclases (ACs) are important regulators of airway smooth muscle function, because β-adrenergic receptor (βAR) agonists stimulate AC activity and cAMP production. We have previously shown in a number of cell types that AC6 selectively couples to βAR and these proteins are coexpressed in lipid rafts. We overexpressed AC2, AC3, and AC6 in mouse bronchial smooth muscle cells (mBSMCs) and human embryonic kidney (HEK)-293 cells by using recombinant adenoviruses and assessed their localization and regulation by various G protein-coupled receptors (GPCRs). AC3 and AC6 were expressed primarily in caveolin-rich fractions, whereas AC2 expression was excluded from these domains. AC6 expression enhanced cAMP production in response to isoproterenol but did not increase responses to butaprost, r</pubmed_abstract><journal>The Journal of pharmacology and experimental therapeutics</journal><pubmed_title>Adenylyl cyclase 2 selectively couples to E prostanoid type 2 receptors, whereas adenylyl cyclase 3 is not receptor-regulated in airway smooth muscle.</pubmed_title><pmcid>PMC3400804</pmcid><funding_grant_id>HL079166</funding_grant_id><funding_grant_id>R01 HL079166</funding_grant_id><pubmed_authors>Adris P</pubmed_authors><pubmed_authors>Bogard AS</pubmed_authors><pubmed_authors>Ostrom RS</pubmed_authors></additional><is_claimable>false</is_claimable><name>Adenylyl cyclase 2 selectively couples to E prostanoid type 2 receptors, whereas adenylyl cyclase 3 is not receptor-regulated in airway smooth muscle.</name><description>Adenylyl cyclases (ACs) are important regulators of airway smooth muscle function, because β-adrenergic receptor (βAR) agonists stimulate AC activity and cAMP production. We have previously shown in a number of cell types that AC6 selectively couples to βAR and these proteins are coexpressed in lipid rafts. We overexpressed AC2, AC3, and AC6 in mouse bronchial smooth muscle cells (mBSMCs) and human embryonic kidney (HEK)-293 cells by using recombinant adenoviruses and assessed their localization and regulation by various G protein-coupled receptors (GPCRs). AC3 and AC6 were expressed primarily in caveolin-rich fractions, whereas AC2 expression was excluded from these domains. AC6 expression enhanced cAMP production in response to isoproterenol but did not increase responses to butaprost, r</description><dates><release>2012-01-01T00:00:00Z</release><publication>2012 Aug</publication><modification>2025-04-04T18:55:31.542Z</modification><creation>2019-03-27T00:55:47Z</creation></dates><accession>S-EPMC3400804</accession><cross_references><pubmed>22619251</pubmed><doi>10.1124/jpet.112.193425</doi></cross_references></HashMap>