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Article: Characterization of guinea pig pulmonary neurokinin type 1 receptors using a novel antagonist ligand, [3H]FK888

TitleCharacterization of guinea pig pulmonary neurokinin type 1 receptors using a novel antagonist ligand, [3H]FK888
Authors
Issue Date1993
PublisherAmerican Society for Pharmacology and Experimental Therapeutics. The Journal's web site is located at http://www.molpharm.org
Citation
Molecular Pharmacology, 1993, v. 44 n. 3, p. 539-544 How to Cite?
AbstractWe have characterized the binding of a novel radioligand, [3H]FK888, to neurokinin (NK)1 receptors in guinea pig lung membranes and localized its binding in guinea pig lung sections by autoradiography. Lung membranes were incubated with [3H]FK888 at 25° and the assays were terminated by rapid filtration; nonspecific binding was defined as binding in the presence of 1 μM concentrations of the nonpeptide NK1-selective antagonist CP-96,345. Kinetic analysis showed that specific binding of [3H]FK888 (approximately 70% of total binding) was rapid, reaching a plateau by 20 min, and that binding was reversed by addition of 1 μM CP-96,345, giving a kinetic K(d) of 0.46 nM. Binding of [3H]FK888 was saturable at approximately 1 nM, and equilibrium binding analysis gave a K(d) of 0.32 ± 0.03 nM and a B(max) of 46.9 ± 7.1 fmol/mg of protein (four experiments). In competition studies, substance P, CP-96,345, and FK888 competed for [3H]FK888 binding, but NKA, NKB, and NK2-selective antagonists such as SR48968 and L-659,877 did not. Guanosine-5'-O-(3-thio)triphosphate significantly shifted the competition curve for substance P competition against [3H]FK888 binding to a lower affinity state, confirming that NK1 receptors are coupled to a G protein. Autoradiographic mapping in cryostat sections of lung showed that [3H]FK888 binding was dense over smooth muscle of all airways, with moderate binding over epithelium of bronchi and bronchioles as well as submucosal glands of trachea. No significant labeling of blood vessels was observed. [3H]FK888 binds to NK1 receptors in guinea pig lung and may be a useful tool for studying the expression and regulation of NK1 receptors.
Persistent Identifierhttp://hdl.handle.net/10722/161965
ISSN
2015 Impact Factor: 3.931
2015 SCImago Journal Rankings: 2.047

 

DC FieldValueLanguage
dc.contributor.authorMiyayasu, Ken_US
dc.contributor.authorMak, JCWen_US
dc.contributor.authorNishikawa, Men_US
dc.contributor.authorBarnes, PJen_US
dc.date.accessioned2012-09-05T05:16:21Z-
dc.date.available2012-09-05T05:16:21Z-
dc.date.issued1993en_US
dc.identifier.citationMolecular Pharmacology, 1993, v. 44 n. 3, p. 539-544en_US
dc.identifier.issn0026-895Xen_US
dc.identifier.urihttp://hdl.handle.net/10722/161965-
dc.description.abstractWe have characterized the binding of a novel radioligand, [3H]FK888, to neurokinin (NK)1 receptors in guinea pig lung membranes and localized its binding in guinea pig lung sections by autoradiography. Lung membranes were incubated with [3H]FK888 at 25° and the assays were terminated by rapid filtration; nonspecific binding was defined as binding in the presence of 1 μM concentrations of the nonpeptide NK1-selective antagonist CP-96,345. Kinetic analysis showed that specific binding of [3H]FK888 (approximately 70% of total binding) was rapid, reaching a plateau by 20 min, and that binding was reversed by addition of 1 μM CP-96,345, giving a kinetic K(d) of 0.46 nM. Binding of [3H]FK888 was saturable at approximately 1 nM, and equilibrium binding analysis gave a K(d) of 0.32 ± 0.03 nM and a B(max) of 46.9 ± 7.1 fmol/mg of protein (four experiments). In competition studies, substance P, CP-96,345, and FK888 competed for [3H]FK888 binding, but NKA, NKB, and NK2-selective antagonists such as SR48968 and L-659,877 did not. Guanosine-5'-O-(3-thio)triphosphate significantly shifted the competition curve for substance P competition against [3H]FK888 binding to a lower affinity state, confirming that NK1 receptors are coupled to a G protein. Autoradiographic mapping in cryostat sections of lung showed that [3H]FK888 binding was dense over smooth muscle of all airways, with moderate binding over epithelium of bronchi and bronchioles as well as submucosal glands of trachea. No significant labeling of blood vessels was observed. [3H]FK888 binds to NK1 receptors in guinea pig lung and may be a useful tool for studying the expression and regulation of NK1 receptors.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.meshAnimalsen_US
dc.subject.meshAutoradiographyen_US
dc.subject.meshBinding, Competitiveen_US
dc.subject.meshDipeptides - Diagnostic Use - Metabolismen_US
dc.subject.meshGuanosine 5'-O-(3-Thiotriphosphate) - Pharmacologyen_US
dc.subject.meshGuinea Pigsen_US
dc.subject.meshIndoles - Diagnostic Use - Metabolismen_US
dc.subject.meshLung - Metabolismen_US
dc.subject.meshMaleen_US
dc.subject.meshRadioligand Assayen_US
dc.subject.meshReceptors, Neurokinin-2en_US
dc.subject.meshReceptors, Neurotransmitter - Metabolismen_US
dc.subject.meshSubstance P - Pharmacologyen_US
dc.titleCharacterization of guinea pig pulmonary neurokinin type 1 receptors using a novel antagonist ligand, [3H]FK888en_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.pmid7690449-
dc.identifier.scopuseid_2-s2.0-0027184024en_US
dc.identifier.volume44en_US
dc.identifier.issue3en_US
dc.identifier.spage539en_US
dc.identifier.epage544en_US
dc.publisher.placeUnited Statesen_US
dc.identifier.scopusauthoridMiyayasu, K=6507160403en_US
dc.identifier.scopusauthoridMak, JCW=7103323094en_US
dc.identifier.scopusauthoridNishikawa, M=7402607361en_US
dc.identifier.scopusauthoridBarnes, PJ=36064679400en_US

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