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Article: Characterization of muscarinic receptor subtypes in pig airways: Radioligand binding and Northern blotting studies

TitleCharacterization of muscarinic receptor subtypes in pig airways: Radioligand binding and Northern blotting studies
Authors
Issue Date1994
PublisherAmerican Physiological Society. The Journal's web site is located at http://intl-ajplung.physiology.org/
Citation
American Journal Of Physiology - Lung Cellular And Molecular Physiology, 1994, v. 266 n. 6 10-6, p. L642-L648 How to Cite?
AbstractThis study was undertaken to characterize the muscarinic receptor subtypes present in adult pig peripheral lung and airway smooth muscle. The binding of the nonselective muscarinic antagonist [N-methyl-3H]scopolamine ([3H]NMS) to pig airways showed a single class of binding sites with a maximum density of 172 and 450 fmol/mg protein in peripheral lung and airway smooth muscle, respectively. Unlike [3H]NMS, the M1-selective antagonist, [3H]telenzepine, recognized two populations of binding sites in peripheral lung. Approximately 14% of total [3H]telenzepine binding sites displayed high affinity [dissociation constant (K(d)) = 0.95 nM], whereas the remaining sites showed low affinity (K(d) = 14.2 nM). The high- and the low-affinity [3H]telenzepine binding sites displayed the pharmacological profile of M1 and M2 receptors, respectively. Heterogeneity of pig airways muscarinic receptor was also revealed by competitive binding experiments against [3H]NMS with the M2-selective antagonist methoctramine. This compound recognized 70 and 90% of total receptors with high affinity in airway smooth muscle (K(i) = 4.44 nM) and peripheral lung (K(i) = 9.82 nM), respectively. This result suggests that the dominant muscarinic receptor in pig airways is of the M2 subtype. Northern blot analysis demonstrated the presence of m1 and m2 mRNAs transcripts in peripheral lung and m2 and m3 mRNAs in airway smooth muscle with no evidence for m4 mRNA.
Persistent Identifierhttp://hdl.handle.net/10722/162051
ISSN
2015 Impact Factor: 4.721
2015 SCImago Journal Rankings: 1.838
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorHaddad, EBen_US
dc.contributor.authorMak, JCWen_US
dc.contributor.authorHislop, Aen_US
dc.contributor.authorHaworth, SGen_US
dc.contributor.authorBarnes, PJen_US
dc.date.accessioned2012-09-05T05:16:54Z-
dc.date.available2012-09-05T05:16:54Z-
dc.date.issued1994en_US
dc.identifier.citationAmerican Journal Of Physiology - Lung Cellular And Molecular Physiology, 1994, v. 266 n. 6 10-6, p. L642-L648en_US
dc.identifier.issn1040-0605en_US
dc.identifier.urihttp://hdl.handle.net/10722/162051-
dc.description.abstractThis study was undertaken to characterize the muscarinic receptor subtypes present in adult pig peripheral lung and airway smooth muscle. The binding of the nonselective muscarinic antagonist [N-methyl-3H]scopolamine ([3H]NMS) to pig airways showed a single class of binding sites with a maximum density of 172 and 450 fmol/mg protein in peripheral lung and airway smooth muscle, respectively. Unlike [3H]NMS, the M1-selective antagonist, [3H]telenzepine, recognized two populations of binding sites in peripheral lung. Approximately 14% of total [3H]telenzepine binding sites displayed high affinity [dissociation constant (K(d)) = 0.95 nM], whereas the remaining sites showed low affinity (K(d) = 14.2 nM). The high- and the low-affinity [3H]telenzepine binding sites displayed the pharmacological profile of M1 and M2 receptors, respectively. Heterogeneity of pig airways muscarinic receptor was also revealed by competitive binding experiments against [3H]NMS with the M2-selective antagonist methoctramine. This compound recognized 70 and 90% of total receptors with high affinity in airway smooth muscle (K(i) = 4.44 nM) and peripheral lung (K(i) = 9.82 nM), respectively. This result suggests that the dominant muscarinic receptor in pig airways is of the M2 subtype. Northern blot analysis demonstrated the presence of m1 and m2 mRNAs transcripts in peripheral lung and m2 and m3 mRNAs in airway smooth muscle with no evidence for m4 mRNA.en_US
dc.languageengen_US
dc.publisherAmerican Physiological Society. The Journal's web site is located at http://intl-ajplung.physiology.org/en_US
dc.relation.ispartofAmerican Journal of Physiology - Lung Cellular and Molecular Physiologyen_US
dc.subject.meshAnimalsen_US
dc.subject.meshBinding, Competitiveen_US
dc.subject.meshBlotting, Northernen_US
dc.subject.meshBronchi - Metabolismen_US
dc.subject.meshLung - Metabolismen_US
dc.subject.meshN-Methylscopolamineen_US
dc.subject.meshRna, Messenger - Metabolismen_US
dc.subject.meshRadioligand Assayen_US
dc.subject.meshReceptors, Muscarinic - Genetics - Metabolismen_US
dc.subject.meshScopolamine Derivatives - Metabolismen_US
dc.subject.meshSwineen_US
dc.subject.meshTrachea - Metabolismen_US
dc.titleCharacterization of muscarinic receptor subtypes in pig airways: Radioligand binding and Northern blotting studiesen_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.pmid8023952-
dc.identifier.scopuseid_2-s2.0-0028292075en_US
dc.identifier.volume266en_US
dc.identifier.issue6 10-6en_US
dc.identifier.spageL642en_US
dc.identifier.epageL648en_US
dc.identifier.isiWOS:A1994NV80900088-
dc.publisher.placeUnited Statesen_US
dc.identifier.scopusauthoridHaddad, EB=7102803008en_US
dc.identifier.scopusauthoridMak, JCW=7103323094en_US
dc.identifier.scopusauthoridHislop, A=7005801811en_US
dc.identifier.scopusauthoridHaworth, SG=35513064700en_US
dc.identifier.scopusauthoridBarnes, PJ=36064679400en_US

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