File Download

There are no files associated with this item.

  Links for fulltext
     (May Require Subscription)
Supplementary

Article: Modulation of 2-[125I]iodomelatonin binding in the guinea pig spleen by guanine nucleotides and cations

TitleModulation of 2-[125I]iodomelatonin binding in the guinea pig spleen by guanine nucleotides and cations
Authors
KeywordsCalcium ion
G protein
Guanine nucleotides
Magnesium ion
Melatonin receptor
Sodium ion
Issue Date1994
PublisherS Karger AG. The Journal's web site is located at http://www.karger.com/NEN
Citation
Neuroendocrinology, 1994, v. 59 n. 2, p. 156-162 How to Cite?
AbstractThe effect of guanine nucleotides on the binding of 2-[125I]iodomelatonin in membrane preparations of guinea pig spleen was studied. The GTP analogues guanosine 5'-O-(3-thiophosphate) and 5'-guanylimidodiphosphate dose-dependently inhibited the binding. Saturation studies revealed that the presence of GTP analogues either increased the equilibrium dissociation constant (K(d)) alone or both increased the K(d) and decreased the binding site density (B(max)). Our results suggest that melatonin receptors in the guinea pig spleen, similar to those in the neural and retinal tissues, are coupled to a G protein. This study showed that N+ and Li+ dose-dependently inhibited 2-[125I]iodomelatonin binding while Mg2+ potentiated the binding. K+ and choline were without significant effects. Low Ca2+ concentrations (1-5 mmol/l) potentiated the radioligand binding while higher concentrations were inhibitory. Saturation studies demonstrated that 125 mmol/l N+ decreased the B(max) while 2.4 mmol/l Ca2+ increased the B(max) and 40 mmol/l Ca2+ increased the K(d). Our results suggest that physiological concentrations of N+ and Ca2+ may play an important modulatory role on melatonin binding to its receptors in the spleen.
Persistent Identifierhttp://hdl.handle.net/10722/81194
ISSN
2015 Impact Factor: 2.583
2015 SCImago Journal Rankings: 1.479
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorPoon, AMSen_HK
dc.contributor.authorPang, SFen_HK
dc.date.accessioned2010-09-06T08:14:54Z-
dc.date.available2010-09-06T08:14:54Z-
dc.date.issued1994en_HK
dc.identifier.citationNeuroendocrinology, 1994, v. 59 n. 2, p. 156-162en_HK
dc.identifier.issn0028-3835en_HK
dc.identifier.urihttp://hdl.handle.net/10722/81194-
dc.description.abstractThe effect of guanine nucleotides on the binding of 2-[125I]iodomelatonin in membrane preparations of guinea pig spleen was studied. The GTP analogues guanosine 5'-O-(3-thiophosphate) and 5'-guanylimidodiphosphate dose-dependently inhibited the binding. Saturation studies revealed that the presence of GTP analogues either increased the equilibrium dissociation constant (K(d)) alone or both increased the K(d) and decreased the binding site density (B(max)). Our results suggest that melatonin receptors in the guinea pig spleen, similar to those in the neural and retinal tissues, are coupled to a G protein. This study showed that N+ and Li+ dose-dependently inhibited 2-[125I]iodomelatonin binding while Mg2+ potentiated the binding. K+ and choline were without significant effects. Low Ca2+ concentrations (1-5 mmol/l) potentiated the radioligand binding while higher concentrations were inhibitory. Saturation studies demonstrated that 125 mmol/l N+ decreased the B(max) while 2.4 mmol/l Ca2+ increased the B(max) and 40 mmol/l Ca2+ increased the K(d). Our results suggest that physiological concentrations of N+ and Ca2+ may play an important modulatory role on melatonin binding to its receptors in the spleen.en_HK
dc.languageengen_HK
dc.publisherS Karger AG. The Journal's web site is located at http://www.karger.com/NENen_HK
dc.relation.ispartofNeuroendocrinologyen_HK
dc.rightsNeuroendocrinology. Copyright © S Karger AG.en_HK
dc.subjectCalcium ionen_HK
dc.subjectG proteinen_HK
dc.subjectGuanine nucleotidesen_HK
dc.subjectMagnesium ionen_HK
dc.subjectMelatonin receptoren_HK
dc.subjectSodium ionen_HK
dc.titleModulation of 2-[125I]iodomelatonin binding in the guinea pig spleen by guanine nucleotides and cationsen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0028-3835&volume=59&spage=156&epage=162&date=1994&atitle=Modulation+of+2-+125I+Iodomelatonin+binding+in+the+guinea+pig+spleen+by+guanine+nucleotides+and+cationsen_HK
dc.identifier.emailPoon, AMS: amspoon@hkucc.hku.hken_HK
dc.identifier.authorityPoon, AMS=rp00354en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.pmid8127405en_HK
dc.identifier.scopuseid_2-s2.0-0028180049en_HK
dc.identifier.hkuros2916en_HK
dc.identifier.volume59en_HK
dc.identifier.issue2en_HK
dc.identifier.spage156en_HK
dc.identifier.epage162en_HK
dc.identifier.isiWOS:A1994MT76400009-
dc.publisher.placeSwitzerlanden_HK
dc.identifier.scopusauthoridPoon, AMS=7103068868en_HK
dc.identifier.scopusauthoridPang, SF=7402528719en_HK

Export via OAI-PMH Interface in XML Formats


OR


Export to Other Non-XML Formats