| pubmed-article:16051698 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:16051698 | lifeskim:mentions | umls-concept:C0007634 | lld:lifeskim |
| pubmed-article:16051698 | lifeskim:mentions | umls-concept:C0005220 | lld:lifeskim |
| pubmed-article:16051698 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
| pubmed-article:16051698 | lifeskim:mentions | umls-concept:C0287638 | lld:lifeskim |
| pubmed-article:16051698 | lifeskim:mentions | umls-concept:C1880022 | lld:lifeskim |
| pubmed-article:16051698 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:16051698 | pubmed:dateCreated | 2005-10-20 | lld:pubmed |
| pubmed-article:16051698 | pubmed:abstractText | beta-Arrestin is an adaptor protein that has been shown to couple G protein-coupled receptors (GPCRs) to clathrin-coated pits and target them for subsequent internalization. More recently, beta-arrestin 2 has also been shown to be involved in the activation of mitogen-activated protein kinase cascades by G protein-coupled receptors independently of G protein activation. Direct interactions between proteins can be monitored using enzyme complementation between two inactive deletion mutants of beta-galactosidase (beta-gal; Deltaalpha and Deltaomega). In the present study, we have used fusion proteins of the human beta(2)-adrenoceptor (C-terminal beta-gal Deltaalpha) and beta-arrestin 2 (beta-gal Deltaomega) to study directly the pharmacology of this interaction in C2C12 cells expressing the beta(2)-adrenoceptor-beta-gal Deltaalpha fusion protein at low physiological levels (38.2 +/- 2.7 fmol . mg protein(-1)). Isoprenaline, noradrenaline, and adrenaline (-log EC(50) = 5.9, 5.5, and 5.7, respectively) stimulated an association between the beta(2)-adrenoceptor and beta-arrestin 2 at much higher concentrations than required for activation of cAMP accumulation (-log EC(50) = 7.6, 6.3, and 7.7, respectively). This was sensitive to inhibition by the beta(2)-adrenoceptor antagonists propranolol, timolol, and ICI 118551. Both salbutamol and terbutaline behaved as partial agonists of beta-gal complementation. Furthermore, the long-acting beta(2)-agonist salmeterol (-log K(D) for inhibition of [(3)H]CGP12177 binding = 8.7) behaved as an antagonist of isoprenaline-stimulated beta(2)-adrenoceptor-arrestin 2 interactions (-log K(D) = 8.0), whereas acting as a full agonist of cAMP accumulation in the same cells (-log EC(50) = 9.2). These data suggest that salmeterol can discriminate between receptor-G(S) protein and receptor-arrestin 2 complexes (in terms of efficacy and affinity) in a way that is favorable for its long duration of action. | lld:pubmed |
| pubmed-article:16051698 | pubmed:language | eng | lld:pubmed |
| pubmed-article:16051698 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16051698 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:16051698 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16051698 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:16051698 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16051698 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:16051698 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16051698 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16051698 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16051698 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16051698 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:16051698 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:16051698 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:16051698 | pubmed:issn | 0022-3565 | lld:pubmed |
| pubmed-article:16051698 | pubmed:author | pubmed-author:HillStephen... | lld:pubmed |
| pubmed-article:16051698 | pubmed:author | pubmed-author:CarterAlison... | lld:pubmed |
| pubmed-article:16051698 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:16051698 | pubmed:volume | 315 | lld:pubmed |
| pubmed-article:16051698 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:16051698 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:16051698 | pubmed:pagination | 839-48 | lld:pubmed |
| pubmed-article:16051698 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:16051698 | pubmed:year | 2005 | lld:pubmed |
| pubmed-article:16051698 | pubmed:articleTitle | Characterization of isoprenaline- and salmeterol-stimulated interactions between beta2-adrenoceptors and beta-arrestin 2 using beta-galactosidase complementation in C2C12 cells. | lld:pubmed |
| pubmed-article:16051698 | pubmed:affiliation | Institute of Cell Signaling, Medical School, Queen's Medical Centre, Nottingham, UK. | lld:pubmed |
| pubmed-article:16051698 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:16051698 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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