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Article: High affinity [3H]formoterol binding sites in lung: Characterization and autoradiographic mapping

TitleHigh affinity [3H]formoterol binding sites in lung: Characterization and autoradiographic mapping
Authors
Issue Date1994
Citation
European Journal Of Pharmacology - Molecular Pharmacology Section, 1994, v. 269 n. 1, p. 35-41 How to Cite?
AbstractAgonist binding to the β2-adrenoceptors and its mapping were studied using the newly developed radioligand [3H]formoterol. The results of [3H]formoterol saturation binding and formoterol inhibition of [3H]formoterol binding were consistent with binding to a single class of receptors (K(d) = 1.34 ± 0.15 nM, B(max) = 154.9 ± 8.0 fmol/mg protein in guinea pig lung membranes, n = 8; K(d) = 1.05 ± 0.17 nM, B(max) = 67.8 ± 8.1 fmol/mg protein in human lung membranes, n = 5) and competition assays with other agonists and antagonists disclosed only a single class of site. The nonhydrolyzable GTP analogue GTPγS caused a reduction in both K(d) and B(max), indicating that the receptors labelled by [3H]formoterol are coupled to a guanine nucleotide binding regulatory protein. Receptor mapping of [3H]formoterol binding sites shows that β2-adrenoceptors were widely distributed in both guinea pig and human lung, with dense labelling over airway epithelium and uniformly over alveolar walls, and sparse labelling of airway and vascular smooth muscle. In addition, submucosal glands were also sparsely labelled in human bronchus. The distribution of β2-adrenoceptors was similar to the pattern previously described with non-selective radiolabelled antagonists in the presence of selective β1-adrenoceptor antagonists.
Persistent Identifierhttp://hdl.handle.net/10722/162062
ISSN
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorMak, JCWen_US
dc.contributor.authorGrandordy, Ben_US
dc.contributor.authorBarnes, PJen_US
dc.date.accessioned2012-09-05T05:16:59Z-
dc.date.available2012-09-05T05:16:59Z-
dc.date.issued1994en_US
dc.identifier.citationEuropean Journal Of Pharmacology - Molecular Pharmacology Section, 1994, v. 269 n. 1, p. 35-41en_US
dc.identifier.issn0922-4106en_US
dc.identifier.urihttp://hdl.handle.net/10722/162062-
dc.description.abstractAgonist binding to the β2-adrenoceptors and its mapping were studied using the newly developed radioligand [3H]formoterol. The results of [3H]formoterol saturation binding and formoterol inhibition of [3H]formoterol binding were consistent with binding to a single class of receptors (K(d) = 1.34 ± 0.15 nM, B(max) = 154.9 ± 8.0 fmol/mg protein in guinea pig lung membranes, n = 8; K(d) = 1.05 ± 0.17 nM, B(max) = 67.8 ± 8.1 fmol/mg protein in human lung membranes, n = 5) and competition assays with other agonists and antagonists disclosed only a single class of site. The nonhydrolyzable GTP analogue GTPγS caused a reduction in both K(d) and B(max), indicating that the receptors labelled by [3H]formoterol are coupled to a guanine nucleotide binding regulatory protein. Receptor mapping of [3H]formoterol binding sites shows that β2-adrenoceptors were widely distributed in both guinea pig and human lung, with dense labelling over airway epithelium and uniformly over alveolar walls, and sparse labelling of airway and vascular smooth muscle. In addition, submucosal glands were also sparsely labelled in human bronchus. The distribution of β2-adrenoceptors was similar to the pattern previously described with non-selective radiolabelled antagonists in the presence of selective β1-adrenoceptor antagonists.en_US
dc.languageengen_US
dc.relation.ispartofEuropean Journal of Pharmacology - Molecular Pharmacology Sectionen_US
dc.subject.meshAdrenergic Beta-Agonists - Metabolismen_US
dc.subject.meshAnimalsen_US
dc.subject.meshAutoradiographyen_US
dc.subject.meshBinding Sitesen_US
dc.subject.meshBinding, Competitive - Drug Effectsen_US
dc.subject.meshComputer Simulationen_US
dc.subject.meshEthanolamines - Metabolismen_US
dc.subject.meshGuanosine 5'-O-(3-Thiotriphosphate) - Pharmacologyen_US
dc.subject.meshGuinea Pigsen_US
dc.subject.meshHumansen_US
dc.subject.meshLung - Metabolismen_US
dc.subject.meshMaleen_US
dc.subject.meshPulmonary Alveoli - Metabolismen_US
dc.subject.meshRadioligand Assayen_US
dc.subject.meshTissue Distributionen_US
dc.titleHigh affinity [3H]formoterol binding sites in lung: Characterization and autoradiographic mappingen_US
dc.typeArticleen_US
dc.identifier.emailMak, JCW:judymak@hku.hken_US
dc.identifier.authorityMak, JCW=rp00352en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1016/0922-4106(94)90023-X-
dc.identifier.pmid7828656-
dc.identifier.scopuseid_2-s2.0-0028774314en_US
dc.identifier.volume269en_US
dc.identifier.issue1en_US
dc.identifier.spage35en_US
dc.identifier.epage41en_US
dc.identifier.isiWOS:A1994PH56000005-
dc.identifier.scopusauthoridMak, JCW=7103323094en_US
dc.identifier.scopusauthoridGrandordy, B=6701645822en_US
dc.identifier.scopusauthoridBarnes, PJ=36064679400en_US

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