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Article: Characteristics of 2-[125I]iodomelatonin binding sites in the pigeon spleen and modulation of binding by guanine nucleotides

TitleCharacteristics of 2-[125I]iodomelatonin binding sites in the pigeon spleen and modulation of binding by guanine nucleotides
Authors
Issue Date1993
PublisherBlackwell Munksgaard. The Journal's web site is located at http://www.blackwellpublishing.com/journals/JPI
Citation
Journal Of Pineal Research, 1993, v. 14 n. 4, p. 169-177 How to Cite?
Abstract2-[125I]Iodomelatonin binding sites in membrane preparations of pigeon spleen have been characterized. The binding was stable, saturable, reversible, and of high affinity. Rosenthal and Hill analyses showed that the radioligand-receptor interaction involved a single class of binding sites. Analysis of the binding results of spleens collected during mid-light revealed an equilibrium dissociation constant (Kd) of 36.6 ± 4.8 pmol/l (mean ± sem, n = 10) and a maximum density (Bmax) of 2.3 ± 0.2 fmol/mg protein. There was no significant difference in the Kd (46.9 ± 5.0 pmol/l) or the Bmax values (2.4 ± 0.3 fmol/mg protein) for spleens collected during mid-dark (n = 9), although the mid-dark serum and pineal melatonin levels were significantly higher (P < 0.05) than the corresponding mid-light values. Kinetic analysis showed a Kd of 8.6 ± 2.0 pmol/l (n ± 4), in agreement with that derived from the saturation studies. Except for inhibition by 2- iodomelatonin, melatonin, 6-chloromelatonin, 6-hydroxymelatonin and N- acetylserotonin, the other indoles or neurotransmitters tested have little inhibition on the binding. In addition, guanosine 5'-O-(3-thiophosphate) (GTPγS), a nonhydrolysable analog of GTP, was found to inhibit the binding in a dose-dependent manner. Saturation studies revealed that this is due to a decrease in both the affinity and density of the binding sites. These data suggest that a single type of melatonin receptor is found in the pigeon spleen and that the site is coupled to a guinine nucleotide binding protein (G-protein). Our findings support a direct pineal melatonin action on the immune system.
Persistent Identifierhttp://hdl.handle.net/10722/171584
ISSN
2015 Impact Factor: 9.314
2015 SCImago Journal Rankings: 2.655
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorPoon, AMSen_US
dc.contributor.authorWang, XLen_US
dc.contributor.authorPang, SFen_US
dc.date.accessioned2012-10-30T06:15:49Z-
dc.date.available2012-10-30T06:15:49Z-
dc.date.issued1993en_US
dc.identifier.citationJournal Of Pineal Research, 1993, v. 14 n. 4, p. 169-177en_US
dc.identifier.issn0742-3098en_US
dc.identifier.urihttp://hdl.handle.net/10722/171584-
dc.description.abstract2-[125I]Iodomelatonin binding sites in membrane preparations of pigeon spleen have been characterized. The binding was stable, saturable, reversible, and of high affinity. Rosenthal and Hill analyses showed that the radioligand-receptor interaction involved a single class of binding sites. Analysis of the binding results of spleens collected during mid-light revealed an equilibrium dissociation constant (Kd) of 36.6 ± 4.8 pmol/l (mean ± sem, n = 10) and a maximum density (Bmax) of 2.3 ± 0.2 fmol/mg protein. There was no significant difference in the Kd (46.9 ± 5.0 pmol/l) or the Bmax values (2.4 ± 0.3 fmol/mg protein) for spleens collected during mid-dark (n = 9), although the mid-dark serum and pineal melatonin levels were significantly higher (P < 0.05) than the corresponding mid-light values. Kinetic analysis showed a Kd of 8.6 ± 2.0 pmol/l (n ± 4), in agreement with that derived from the saturation studies. Except for inhibition by 2- iodomelatonin, melatonin, 6-chloromelatonin, 6-hydroxymelatonin and N- acetylserotonin, the other indoles or neurotransmitters tested have little inhibition on the binding. In addition, guanosine 5'-O-(3-thiophosphate) (GTPγS), a nonhydrolysable analog of GTP, was found to inhibit the binding in a dose-dependent manner. Saturation studies revealed that this is due to a decrease in both the affinity and density of the binding sites. These data suggest that a single type of melatonin receptor is found in the pigeon spleen and that the site is coupled to a guinine nucleotide binding protein (G-protein). Our findings support a direct pineal melatonin action on the immune system.en_US
dc.languageengen_US
dc.publisherBlackwell Munksgaard. The Journal's web site is located at http://www.blackwellpublishing.com/journals/JPIen_US
dc.relation.ispartofJournal of Pineal Researchen_US
dc.subject.meshAnimalsen_US
dc.subject.meshBinding Sites - Drug Effectsen_US
dc.subject.meshCell Membrane - Metabolismen_US
dc.subject.meshCircadian Rhythmen_US
dc.subject.meshColumbidaeen_US
dc.subject.meshGtp-Binding Proteins - Metabolismen_US
dc.subject.meshGuanine Nucleotides - Pharmacologyen_US
dc.subject.meshKineticsen_US
dc.subject.meshLigandsen_US
dc.subject.meshMelatonin - Analogs & Derivatives - Analysis - Metabolismen_US
dc.subject.meshPineal Gland - Chemistryen_US
dc.subject.meshRadioimmunoassayen_US
dc.subject.meshReceptors, Melatoninen_US
dc.subject.meshReceptors, Neurotransmitter - Drug Effects - Metabolismen_US
dc.subject.meshSpleen - Drug Effects - Metabolismen_US
dc.titleCharacteristics of 2-[125I]iodomelatonin binding sites in the pigeon spleen and modulation of binding by guanine nucleotidesen_US
dc.typeArticleen_US
dc.identifier.emailPoon, AMS:amspoon@hkucc.hku.hken_US
dc.identifier.authorityPoon, AMS=rp00354en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1111/j.1600-079X.1993.tb00499.x-
dc.identifier.pmid8393924-
dc.identifier.scopuseid_2-s2.0-0027338346en_US
dc.identifier.volume14en_US
dc.identifier.issue4en_US
dc.identifier.spage169en_US
dc.identifier.epage177en_US
dc.identifier.isiWOS:A1993LJ30100002-
dc.publisher.placeDenmarken_US
dc.identifier.scopusauthoridPoon, AMS=7103068868en_US
dc.identifier.scopusauthoridWang, XL=7501861824en_US
dc.identifier.scopusauthoridPang, SF=7402528719en_US

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