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Conference Paper: The ligand binding properties of human membrane estrogen receptors
Title | The ligand binding properties of human membrane estrogen receptors |
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Authors | |
Keywords | Pharmacy and pharmacology environmental studies Toxicology and environmental safety |
Issue Date | 2010 |
Publisher | Blackwell 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 (WorldPharma 2010), Copenhagen, Denmark, 17-23 July 2010. In Basic & Clinical Pharmacology & Toxicology, 2010, v. 107 suppl. 1, p. 415 How to Cite? |
Abstract | Estrogen (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. |
Description | Paper no. 1205 - Focused Conference Group: P11 - G Protein-coupled 7tm Receptors: from Molecular to Physiological Function |
Persistent Identifier | http://hdl.handle.net/10722/126900 |
ISSN | 2023 Impact Factor: 2.7 2023 SCImago Journal Rankings: 0.744 |
DC Field | Value | Language |
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dc.contributor.author | Lin, AHY | en_HK |
dc.contributor.author | Leung, GPH | en_HK |
dc.contributor.author | Leung, SWS | en_HK |
dc.contributor.author | Man, RYK | en_HK |
dc.date.accessioned | 2010-10-31T12:55:03Z | - |
dc.date.available | 2010-10-31T12:55:03Z | - |
dc.date.issued | 2010 | en_HK |
dc.identifier.citation | The 16th World Congress on Basic and Clinical Pharmacology (WorldPharma 2010), Copenhagen, Denmark, 17-23 July 2010. In Basic & Clinical Pharmacology & Toxicology, 2010, v. 107 suppl. 1, p. 415 | en_HK |
dc.identifier.issn | 1742-7835 | - |
dc.identifier.uri | http://hdl.handle.net/10722/126900 | - |
dc.description | Paper no. 1205 - Focused Conference Group: P11 - G Protein-coupled 7tm Receptors: from Molecular to Physiological Function | - |
dc.description.abstract | Estrogen (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.language | eng | en_HK |
dc.publisher | Blackwell Publishing Ltd. The Journal's web site is located at http://www.blackwellpublishing.com/journals/PTO | - |
dc.relation.ispartof | Basic & Clinical Pharmacology & Toxicology | en_HK |
dc.rights | The definitive version is available at www.blackwell-synergy.com | - |
dc.subject | Pharmacy and pharmacology environmental studies | - |
dc.subject | Toxicology and environmental safety | - |
dc.title | The ligand binding properties of human membrane estrogen receptors | en_HK |
dc.type | Conference_Paper | en_HK |
dc.identifier.openurl | http://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.email | Lin, AHY: amanlin@hkusua.hku.hk | en_HK |
dc.identifier.email | Leung, GPH: leung_pak_heng@hotmail.com | en_HK |
dc.identifier.email | Leung, SWS: swsleung@HKUCC.hku.hk | en_HK |
dc.identifier.email | Man, RYK: rykman@hkucc.hku.hk | en_HK |
dc.identifier.hkuros | 175343 | en_HK |
dc.identifier.volume | 107 | en_HK |
dc.identifier.issue | suppl. 1 | - |
dc.identifier.spage | 415 | en_HK |
dc.identifier.epage | 415 | - |
dc.identifier.issnl | 1742-7835 | - |