Direct labelling of the human P2X7 receptor and identification of positive and negative cooperativity of binding
Background and Purpose: The P2X7 receptor exhibits complex pharmacological properties. In this study, binding of a [3H]‐labelled P2X7 receptor antagonist to human P2X7 receptors has been examined to further understand ligand interactions with this receptor. Experimental Approach: The P2X7 receptor a...
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| Veröffentlicht in: | British journal of pharmacology 2007-05, Vol.151 (1), p.84-95 |
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| creator | Michel, A D Chambers, L J Clay, W C Condreay, J P Walter, D S Chessell, I P |
| description | Background and Purpose:
The P2X7 receptor exhibits complex pharmacological properties. In this study, binding of a [3H]‐labelled P2X7 receptor antagonist to human P2X7 receptors has been examined to further understand ligand interactions with this receptor.
Experimental Approach:
The P2X7 receptor antagonist, N‐[2‐({2‐[(2‐hydroxyethyl)amino]ethyl}amino)‐5‐quinolinyl]‐2‐tricyclo[3.3.1.13,7]dec‐1‐ylacetamide (compound‐17), was radiolabelled with tritium and binding studies were performed using membranes prepared from U‐2 OS or HEK293 cells expressing human recombinant P2X7 receptors.
Key Results:
Binding of [3H]‐compound‐17 was higher in membranes prepared from cells expressing P2X7 receptors than from control cells and was inhibited by ATP suggesting labelled sites represented human P2X7 receptors. Binding was reversible, saturable and modulated by P2X7 receptor ligands (Brilliant Blue G, KN62, ATP, decavanadate). Furthermore, ATP potency was reduced in the presence of divalent cations or NaCl. Radioligand binding exhibited both positive and negative cooperativity. Positive cooperativity was evident from bell shaped Scatchard plots, reduction in radioligand dissociation rate by unlabelled compound‐17 and enhancement of radioligand binding by KN62 and unlabelled compound‐17. ATP and decavanadate inhibited binding in a negative cooperative manner as they enhanced radioligand dissociation.
Conclusions:
These data demonstrate that human P2X7 receptors can be directly labelled and provide novel insights into receptor function. The positive cooperativity observed suggests that binding of compound‐17 to one subunit in the P2X7 receptor complex enhances subsequent binding to other P2X7 subunits in the same complex. The negative cooperative effects of ATP suggest that ATP and compound‐17 bind at separate, interacting, sites on the P2X7 receptor.
British Journal of Pharmacology (2007) 151, 84–95. doi:10.1038/sj.bjp.0707196 |
| doi_str_mv | 10.1038/sj.bjp.0707196 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_pubme</sourceid><recordid>TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_2012979</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>1262520731</sourcerecordid><originalsourceid>FETCH-LOGICAL-p2829-532936087e76bd5ae2461a787206d8d7e5189a774757aa80ce034b28f24be0443</originalsourceid><addsrcrecordid>eNpdkktv1DAUhS0EotPCliWKkOhuBj-SXGeDVMqjSJXoAiR21k1yM-MoYwc7KZp_j9MOFFjZ1vl0fI59GXsh-EZwpd_EflP344YDB1GVj9hK5FCuC6XFY7binMNaCK1P2GmMPedJhOIpOxGgVKUVX7HxvQ3UTNmANQ2DddvMd9m0o2w379FlN_I7ZAmgcfIhQ9dmtiU32c42OFnvFnr00U72lu5kR1u8OzTejxSWvZ0OC1Zb1yb_Z-xJh0Ok58f1jH37-OHr5dX6-sunz5cX1-tRalmlBrJSJddAUNZtgSTzUiBokLxsdQtUCF0hQA4FIGreEFd5LXUn85p4nqsz9vbed5zrPbVNSh1wMGOwewwH49GafxVnd2brb43kQlZQJYPzo0HwP2aKk9nb2KRHQkd-jgbSLVCoMoGv_gN7PweXyhkpUt5KKpWgl3_H-ZPj908k4PURwNjg0AV0jY0PnIZcKVh6yXvupx3o8KBzs8yDib1J82CO82De3VwpXalf9g2o0Q</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>217209233</pqid></control><display><type>article</type><title>Direct labelling of the human P2X7 receptor and identification of positive and negative cooperativity of binding</title><source>MEDLINE</source><source>Wiley Online Library Free Content</source><source>Access via Wiley Online Library</source><source>EZB-FREE-00999 freely available EZB journals</source><source>PubMed Central</source><source>Alma/SFX Local Collection</source><creator>Michel, A D ; Chambers, L J ; Clay, W C ; Condreay, J P ; Walter, D S ; Chessell, I P</creator><creatorcontrib>Michel, A D ; Chambers, L J ; Clay, W C ; Condreay, J P ; Walter, D S ; Chessell, I P</creatorcontrib><description>Background and Purpose:
The P2X7 receptor exhibits complex pharmacological properties. In this study, binding of a [3H]‐labelled P2X7 receptor antagonist to human P2X7 receptors has been examined to further understand ligand interactions with this receptor.
Experimental Approach:
The P2X7 receptor antagonist, N‐[2‐({2‐[(2‐hydroxyethyl)amino]ethyl}amino)‐5‐quinolinyl]‐2‐tricyclo[3.3.1.13,7]dec‐1‐ylacetamide (compound‐17), was radiolabelled with tritium and binding studies were performed using membranes prepared from U‐2 OS or HEK293 cells expressing human recombinant P2X7 receptors.
Key Results:
Binding of [3H]‐compound‐17 was higher in membranes prepared from cells expressing P2X7 receptors than from control cells and was inhibited by ATP suggesting labelled sites represented human P2X7 receptors. Binding was reversible, saturable and modulated by P2X7 receptor ligands (Brilliant Blue G, KN62, ATP, decavanadate). Furthermore, ATP potency was reduced in the presence of divalent cations or NaCl. Radioligand binding exhibited both positive and negative cooperativity. Positive cooperativity was evident from bell shaped Scatchard plots, reduction in radioligand dissociation rate by unlabelled compound‐17 and enhancement of radioligand binding by KN62 and unlabelled compound‐17. ATP and decavanadate inhibited binding in a negative cooperative manner as they enhanced radioligand dissociation.
Conclusions:
These data demonstrate that human P2X7 receptors can be directly labelled and provide novel insights into receptor function. The positive cooperativity observed suggests that binding of compound‐17 to one subunit in the P2X7 receptor complex enhances subsequent binding to other P2X7 subunits in the same complex. The negative cooperative effects of ATP suggest that ATP and compound‐17 bind at separate, interacting, sites on the P2X7 receptor.
British Journal of Pharmacology (2007) 151, 84–95. doi:10.1038/sj.bjp.0707196</description><identifier>ISSN: 0007-1188</identifier><identifier>EISSN: 1476-5381</identifier><identifier>DOI: 10.1038/sj.bjp.0707196</identifier><identifier>PMID: 17339830</identifier><identifier>CODEN: BJPCBM</identifier><language>eng</language><publisher>Oxford, UK: Blackwell Publishing Ltd</publisher><subject>Adenosine Triphosphate - pharmacology ; Antibiotics. Antiinfectious agents. Antiparasitic agents ; Antiparasitic agents ; Antiviral agents ; ATP ; Binding Sites ; Biological and medical sciences ; BzATP ; Cells, Cultured ; Humans ; Iohexol - analogs & derivatives ; Iohexol - metabolism ; Kinetics ; KN62 ; Medical sciences ; P2X7 receptor ; Pharmacology. Drug treatments ; PPADS ; Radioligand Assay - methods ; radioligand binding ; Receptors, Purinergic P2 - analysis ; Receptors, Purinergic P2 - metabolism ; Receptors, Purinergic P2X7 ; Research Papers ; Suramin ; Tritium ; Vanadates - pharmacology</subject><ispartof>British journal of pharmacology, 2007-05, Vol.151 (1), p.84-95</ispartof><rights>2007 British Pharmacological Society</rights><rights>2007 INIST-CNRS</rights><rights>Copyright Nature Publishing Group May 2007</rights><rights>Copyright 2007, Nature Publishing Group 2007 Nature Publishing Group</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC2012979/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC2012979/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,727,780,784,885,1417,1433,27924,27925,45574,45575,46409,46833,53791,53793</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=18743374$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/17339830$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Michel, A D</creatorcontrib><creatorcontrib>Chambers, L J</creatorcontrib><creatorcontrib>Clay, W C</creatorcontrib><creatorcontrib>Condreay, J P</creatorcontrib><creatorcontrib>Walter, D S</creatorcontrib><creatorcontrib>Chessell, I P</creatorcontrib><title>Direct labelling of the human P2X7 receptor and identification of positive and negative cooperativity of binding</title><title>British journal of pharmacology</title><addtitle>Br J Pharmacol</addtitle><description>Background and Purpose:
The P2X7 receptor exhibits complex pharmacological properties. In this study, binding of a [3H]‐labelled P2X7 receptor antagonist to human P2X7 receptors has been examined to further understand ligand interactions with this receptor.
Experimental Approach:
The P2X7 receptor antagonist, N‐[2‐({2‐[(2‐hydroxyethyl)amino]ethyl}amino)‐5‐quinolinyl]‐2‐tricyclo[3.3.1.13,7]dec‐1‐ylacetamide (compound‐17), was radiolabelled with tritium and binding studies were performed using membranes prepared from U‐2 OS or HEK293 cells expressing human recombinant P2X7 receptors.
Key Results:
Binding of [3H]‐compound‐17 was higher in membranes prepared from cells expressing P2X7 receptors than from control cells and was inhibited by ATP suggesting labelled sites represented human P2X7 receptors. Binding was reversible, saturable and modulated by P2X7 receptor ligands (Brilliant Blue G, KN62, ATP, decavanadate). Furthermore, ATP potency was reduced in the presence of divalent cations or NaCl. Radioligand binding exhibited both positive and negative cooperativity. Positive cooperativity was evident from bell shaped Scatchard plots, reduction in radioligand dissociation rate by unlabelled compound‐17 and enhancement of radioligand binding by KN62 and unlabelled compound‐17. ATP and decavanadate inhibited binding in a negative cooperative manner as they enhanced radioligand dissociation.
Conclusions:
These data demonstrate that human P2X7 receptors can be directly labelled and provide novel insights into receptor function. The positive cooperativity observed suggests that binding of compound‐17 to one subunit in the P2X7 receptor complex enhances subsequent binding to other P2X7 subunits in the same complex. The negative cooperative effects of ATP suggest that ATP and compound‐17 bind at separate, interacting, sites on the P2X7 receptor.
British Journal of Pharmacology (2007) 151, 84–95. doi:10.1038/sj.bjp.0707196</description><subject>Adenosine Triphosphate - pharmacology</subject><subject>Antibiotics. Antiinfectious agents. Antiparasitic agents</subject><subject>Antiparasitic agents</subject><subject>Antiviral agents</subject><subject>ATP</subject><subject>Binding Sites</subject><subject>Biological and medical sciences</subject><subject>BzATP</subject><subject>Cells, Cultured</subject><subject>Humans</subject><subject>Iohexol - analogs & derivatives</subject><subject>Iohexol - metabolism</subject><subject>Kinetics</subject><subject>KN62</subject><subject>Medical sciences</subject><subject>P2X7 receptor</subject><subject>Pharmacology. Drug treatments</subject><subject>PPADS</subject><subject>Radioligand Assay - methods</subject><subject>radioligand binding</subject><subject>Receptors, Purinergic P2 - analysis</subject><subject>Receptors, Purinergic P2 - metabolism</subject><subject>Receptors, Purinergic P2X7</subject><subject>Research Papers</subject><subject>Suramin</subject><subject>Tritium</subject><subject>Vanadates - pharmacology</subject><issn>0007-1188</issn><issn>1476-5381</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2007</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNpdkktv1DAUhS0EotPCliWKkOhuBj-SXGeDVMqjSJXoAiR21k1yM-MoYwc7KZp_j9MOFFjZ1vl0fI59GXsh-EZwpd_EflP344YDB1GVj9hK5FCuC6XFY7binMNaCK1P2GmMPedJhOIpOxGgVKUVX7HxvQ3UTNmANQ2DddvMd9m0o2w379FlN_I7ZAmgcfIhQ9dmtiU32c42OFnvFnr00U72lu5kR1u8OzTejxSWvZ0OC1Zb1yb_Z-xJh0Ok58f1jH37-OHr5dX6-sunz5cX1-tRalmlBrJSJddAUNZtgSTzUiBokLxsdQtUCF0hQA4FIGreEFd5LXUn85p4nqsz9vbed5zrPbVNSh1wMGOwewwH49GafxVnd2brb43kQlZQJYPzo0HwP2aKk9nb2KRHQkd-jgbSLVCoMoGv_gN7PweXyhkpUt5KKpWgl3_H-ZPj908k4PURwNjg0AV0jY0PnIZcKVh6yXvupx3o8KBzs8yDib1J82CO82De3VwpXalf9g2o0Q</recordid><startdate>200705</startdate><enddate>200705</enddate><creator>Michel, A D</creator><creator>Chambers, L J</creator><creator>Clay, W C</creator><creator>Condreay, J P</creator><creator>Walter, D S</creator><creator>Chessell, I P</creator><general>Blackwell Publishing Ltd</general><general>Nature Publishing</general><general>Nature Publishing Group</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>3V.</scope><scope>7QP</scope><scope>7RV</scope><scope>7TK</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8AO</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M7P</scope><scope>NAPCQ</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>200705</creationdate><title>Direct labelling of the human P2X7 receptor and identification of positive and negative cooperativity of binding</title><author>Michel, A D ; Chambers, L J ; Clay, W C ; Condreay, J P ; Walter, D S ; Chessell, I P</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-p2829-532936087e76bd5ae2461a787206d8d7e5189a774757aa80ce034b28f24be0443</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2007</creationdate><topic>Adenosine Triphosphate - pharmacology</topic><topic>Antibiotics. Antiinfectious agents. Antiparasitic agents</topic><topic>Antiparasitic agents</topic><topic>Antiviral agents</topic><topic>ATP</topic><topic>Binding Sites</topic><topic>Biological and medical sciences</topic><topic>BzATP</topic><topic>Cells, Cultured</topic><topic>Humans</topic><topic>Iohexol - analogs & derivatives</topic><topic>Iohexol - metabolism</topic><topic>Kinetics</topic><topic>KN62</topic><topic>Medical sciences</topic><topic>P2X7 receptor</topic><topic>Pharmacology. Drug treatments</topic><topic>PPADS</topic><topic>Radioligand Assay - methods</topic><topic>radioligand binding</topic><topic>Receptors, Purinergic P2 - analysis</topic><topic>Receptors, Purinergic P2 - metabolism</topic><topic>Receptors, Purinergic P2X7</topic><topic>Research Papers</topic><topic>Suramin</topic><topic>Tritium</topic><topic>Vanadates - pharmacology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Michel, A D</creatorcontrib><creatorcontrib>Chambers, L J</creatorcontrib><creatorcontrib>Clay, W C</creatorcontrib><creatorcontrib>Condreay, J P</creatorcontrib><creatorcontrib>Walter, D S</creatorcontrib><creatorcontrib>Chessell, I P</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>ProQuest Central (Corporate)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Nursing & Allied Health Database</collection><collection>Neurosciences Abstracts</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Biological Science Database</collection><collection>Nursing & Allied Health Premium</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>British journal of pharmacology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Michel, A D</au><au>Chambers, L J</au><au>Clay, W C</au><au>Condreay, J P</au><au>Walter, D S</au><au>Chessell, I P</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Direct labelling of the human P2X7 receptor and identification of positive and negative cooperativity of binding</atitle><jtitle>British journal of pharmacology</jtitle><addtitle>Br J Pharmacol</addtitle><date>2007-05</date><risdate>2007</risdate><volume>151</volume><issue>1</issue><spage>84</spage><epage>95</epage><pages>84-95</pages><issn>0007-1188</issn><eissn>1476-5381</eissn><coden>BJPCBM</coden><abstract>Background and Purpose:
The P2X7 receptor exhibits complex pharmacological properties. In this study, binding of a [3H]‐labelled P2X7 receptor antagonist to human P2X7 receptors has been examined to further understand ligand interactions with this receptor.
Experimental Approach:
The P2X7 receptor antagonist, N‐[2‐({2‐[(2‐hydroxyethyl)amino]ethyl}amino)‐5‐quinolinyl]‐2‐tricyclo[3.3.1.13,7]dec‐1‐ylacetamide (compound‐17), was radiolabelled with tritium and binding studies were performed using membranes prepared from U‐2 OS or HEK293 cells expressing human recombinant P2X7 receptors.
Key Results:
Binding of [3H]‐compound‐17 was higher in membranes prepared from cells expressing P2X7 receptors than from control cells and was inhibited by ATP suggesting labelled sites represented human P2X7 receptors. Binding was reversible, saturable and modulated by P2X7 receptor ligands (Brilliant Blue G, KN62, ATP, decavanadate). Furthermore, ATP potency was reduced in the presence of divalent cations or NaCl. Radioligand binding exhibited both positive and negative cooperativity. Positive cooperativity was evident from bell shaped Scatchard plots, reduction in radioligand dissociation rate by unlabelled compound‐17 and enhancement of radioligand binding by KN62 and unlabelled compound‐17. ATP and decavanadate inhibited binding in a negative cooperative manner as they enhanced radioligand dissociation.
Conclusions:
These data demonstrate that human P2X7 receptors can be directly labelled and provide novel insights into receptor function. The positive cooperativity observed suggests that binding of compound‐17 to one subunit in the P2X7 receptor complex enhances subsequent binding to other P2X7 subunits in the same complex. The negative cooperative effects of ATP suggest that ATP and compound‐17 bind at separate, interacting, sites on the P2X7 receptor.
British Journal of Pharmacology (2007) 151, 84–95. doi:10.1038/sj.bjp.0707196</abstract><cop>Oxford, UK</cop><pub>Blackwell Publishing Ltd</pub><pmid>17339830</pmid><doi>10.1038/sj.bjp.0707196</doi><tpages>12</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Adenosine Triphosphate - pharmacology Antibiotics. Antiinfectious agents. Antiparasitic agents Antiparasitic agents Antiviral agents ATP Binding Sites Biological and medical sciences BzATP Cells, Cultured Humans Iohexol - analogs & derivatives Iohexol - metabolism Kinetics KN62 Medical sciences P2X7 receptor Pharmacology. Drug treatments PPADS Radioligand Assay - methods radioligand binding Receptors, Purinergic P2 - analysis Receptors, Purinergic P2 - metabolism Receptors, Purinergic P2X7 Research Papers Suramin Tritium Vanadates - pharmacology |
| title | Direct labelling of the human P2X7 receptor and identification of positive and negative cooperativity of binding |
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