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Conference Paper: The ligand binding properties of human membrane estrogen receptors

TitleThe ligand binding properties of human membrane estrogen receptors
Authors
KeywordsPharmacy and pharmacology environmental studies
Toxicology and environmental safety
Issue Date2010
PublisherBlackwell Publishing Ltd. The Journal's web site is located at http://www.blackwellpublishing.com/journals/PTO
Citation
The 16th World Congress on Basic and Clinical Pharmacology (WorldPharma2010), Copenhagen, Denmark, 17-23 July 2010. How to Cite?
AbstractEstrogen (17b-estradiol) exerts rapid non-genomic effects in various cell types. Surface binding sites for estrogen has been demonstrated using confocal microscopy. However, the identity of the putative membrane estrogen receptor (mER) and how well they bind with estrogen remained elusive. The present study aims to determine the binding affinities of estrogen to the mER candidates recently identified and to investigate the importance for mERs to be transported to the membrane for estrogen binding. Moreover, the relative binding affinities of the mERs with various estrogenic chemicals and phytoestrogens were evaluated. Human estrogen receptor-a66 (ER66), estrogen receptor-a46 (ER46), estrogen receptor-a36 (ER36) and G protein-coupled receptor 30 (GPR30) were cloned and expressed using cell-free expression systems in the presence of nanolipoprotein molecules as the membrane substitute. Expressed receptor proteins were used in radioactive binding assay. ER66 and ER46 have similar binding affinities towards estrogen (KdG79 pM), whereas ER36 and GPR30 displayed no specific binding. ER66 and ER46 expressed in prokaryotic system have lower binding affinities than the receptors expressed in eukaryotic system. Removal of nanolipoprotein molecules also reduced the binding affinities of ER66 and ER46. Our results suggested that post-translational modification and membrane trafficking of mERs are important for proper conformation for binding. Moreover, relative binding affinities to ER66 and ER46 are similar for the compounds tested, except for the estrogen antagonist, ICI 182 780.
DescriptionBasic & Clinical Pharmacology & Toxicology, 2010, v. 107, suppl. 1, p. 415
Paper No. 1205 - Focused Conference Group: P11 - G Protein-coupled 7tm Receptors: from Molecular to Physiological Function
Persistent Identifierhttp://hdl.handle.net/10722/126900
ISSN
2015 Impact Factor: 3.097
2015 SCImago Journal Rankings: 0.539

 

DC FieldValueLanguage
dc.contributor.authorLin, AHYen_HK
dc.contributor.authorLeung, GPHen_HK
dc.contributor.authorLeung, SWSen_HK
dc.contributor.authorMan, RYKen_HK
dc.date.accessioned2010-10-31T12:55:03Z-
dc.date.available2010-10-31T12:55:03Z-
dc.date.issued2010en_HK
dc.identifier.citationThe 16th World Congress on Basic and Clinical Pharmacology (WorldPharma2010), Copenhagen, Denmark, 17-23 July 2010.en_HK
dc.identifier.issn1742-7835-
dc.identifier.urihttp://hdl.handle.net/10722/126900-
dc.descriptionBasic & Clinical Pharmacology & Toxicology, 2010, v. 107, suppl. 1, p. 415-
dc.descriptionPaper No. 1205 - Focused Conference Group: P11 - G Protein-coupled 7tm Receptors: from Molecular to Physiological Function-
dc.description.abstractEstrogen (17b-estradiol) exerts rapid non-genomic effects in various cell types. Surface binding sites for estrogen has been demonstrated using confocal microscopy. However, the identity of the putative membrane estrogen receptor (mER) and how well they bind with estrogen remained elusive. The present study aims to determine the binding affinities of estrogen to the mER candidates recently identified and to investigate the importance for mERs to be transported to the membrane for estrogen binding. Moreover, the relative binding affinities of the mERs with various estrogenic chemicals and phytoestrogens were evaluated. Human estrogen receptor-a66 (ER66), estrogen receptor-a46 (ER46), estrogen receptor-a36 (ER36) and G protein-coupled receptor 30 (GPR30) were cloned and expressed using cell-free expression systems in the presence of nanolipoprotein molecules as the membrane substitute. Expressed receptor proteins were used in radioactive binding assay. ER66 and ER46 have similar binding affinities towards estrogen (KdG79 pM), whereas ER36 and GPR30 displayed no specific binding. ER66 and ER46 expressed in prokaryotic system have lower binding affinities than the receptors expressed in eukaryotic system. Removal of nanolipoprotein molecules also reduced the binding affinities of ER66 and ER46. Our results suggested that post-translational modification and membrane trafficking of mERs are important for proper conformation for binding. Moreover, relative binding affinities to ER66 and ER46 are similar for the compounds tested, except for the estrogen antagonist, ICI 182 780.-
dc.languageengen_HK
dc.publisherBlackwell Publishing Ltd. The Journal's web site is located at http://www.blackwellpublishing.com/journals/PTO-
dc.relation.ispartofWorldPharma2010en_HK
dc.rightsThe definitive version is available at www.blackwell-synergy.com-
dc.subjectPharmacy and pharmacology environmental studies-
dc.subjectToxicology and environmental safety-
dc.titleThe ligand binding properties of human membrane estrogen receptorsen_HK
dc.typeConference_Paperen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=1742-7835&volume=107, suppl. 1&spage=415&epage=&date=1/7/2010&atitle=The+ligand+binding+properties+of+human+membrane+estrogen+receptors-
dc.identifier.emailLin, AHY: amanlin@hkusua.hku.hken_HK
dc.identifier.emailLeung, GPH: leung_pak_heng@hotmail.comen_HK
dc.identifier.emailLeung, SWS: swsleung@HKUCC.hku.hken_HK
dc.identifier.emailMan, RYK: rykman@hkucc.hku.hken_HK
dc.identifier.hkuros175343en_HK
dc.identifier.volume107, suppl. 1en_HK
dc.identifier.spage415en_HK

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