Assembly of GABAA receptor subunits: role of the delta subunit
GABAA receptor channels (GABARs) composed of different combinations of rat alpha 1, beta 1, gamma 2L, and delta subunits were expressed transiently in mouse fibroblast cells (L929 cells). Whole-cell recordings were obtained from transfected cells to determine which combinations of GABAR subunits for...
Gespeichert in:
| Veröffentlicht in: | The Journal of neuroscience 1994-11, Vol.14 (11), p.7077-7086 |
|---|---|
| Hauptverfasser: | , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 7086 |
|---|---|
| container_issue | 11 |
| container_start_page | 7077 |
| container_title | The Journal of neuroscience |
| container_volume | 14 |
| creator | Saxena, NC Macdonald, RL |
| description | GABAA receptor channels (GABARs) composed of different combinations of rat alpha 1, beta 1, gamma 2L, and delta subunits were expressed transiently in mouse fibroblast cells (L929 cells). Whole-cell recordings were obtained from transfected cells to determine which combinations of GABAR subunits formed functional receptor channels, and to compare the electrophysiological and pharmacological characteristics of GABAR channels expressed in the presence and absence of the delta subunit. Only alpha 1 beta 1 gamma 2L, alpha 1 beta 1 gamma 2L delta, and alpha 1 beta 1 delta subunit combinations assembled to form functional GABAR channels and the presence of the delta-subunit slowed the rate of acute desensitization of GABA-evoked current during GABA application and the rate of recovery of GABA-evoked current following GABA application. These three different GABAR channel isoforms also showed distinct pharmacological profiles with differential sensitivity to block by zinc. Zinc was a potent blocker of alpha 1 beta 1 delta GABAR channels, a moderate-strength blocker of alpha 1 beta 1 gamma 2L delta GABAR channels, and did not block the alpha 1 beta 1 gamma 2L GABAR channels. These findings suggest that GABAR isoforms containing the delta subunit constitute a novel GABAR channel with distinct electrophysiological and pharmacological characteristics. |
| doi_str_mv | 10.1523/jneurosci.14-11-07077.1994 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_pubme</sourceid><recordid>TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_6577243</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>76825180</sourcerecordid><originalsourceid>FETCH-LOGICAL-c4914-a2299a5d75e7ca8f49ba0570a3ffa78b2ae716ade9099cdf5ea12e961f924aa33</originalsourceid><addsrcrecordid>eNpVkE1P3DAQhq2qFWxpfwJS1EM5Zetx7DjmgBRWfFWoSG05W5NkwgY5yWInXfHvSdgtak9zeJ95Z_Qw9gX4EpRIvj12NPo-lM0SZAwQc821XoIx8h1bTISJheTwni240DxOpZaH7GMIj5xPJOgDdqCVUJmRC3aWh0Bt4Z6jvo6u8vM8jzyVtBl6H4WxGLtmCKeR7x3NwLCmqCI34N_sE_tQowv0eT-P2P3lxe_VdXx7d3Wzym_jUprpRxTCGFSVVqRLzGppCuRKc0zqGnVWCCQNKVZkuDFlVStCEGRSqI2QiElyxM52vZuxaKkqqRs8OrvxTYv-2fbY2P-Trlnbh_6PTZXWQs4FX_cFvn8aKQy2bUJJzmFH_RisTjOhIOMTeLoDy8lw8FS_HQFuZ_v2-4-L-593v1Y3FqQFsK_27Wx_Wj7-98231b3uKT_Z5evmYb1tPNnQonMTDXa73e765rrkBWTJkWU</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>76825180</pqid></control><display><type>article</type><title>Assembly of GABAA receptor subunits: role of the delta subunit</title><source>PubMed Central Free</source><source>MEDLINE</source><source>EZB-FREE-00999 freely available EZB journals</source><creator>Saxena, NC ; Macdonald, RL</creator><creatorcontrib>Saxena, NC ; Macdonald, RL</creatorcontrib><description>GABAA receptor channels (GABARs) composed of different combinations of rat alpha 1, beta 1, gamma 2L, and delta subunits were expressed transiently in mouse fibroblast cells (L929 cells). Whole-cell recordings were obtained from transfected cells to determine which combinations of GABAR subunits formed functional receptor channels, and to compare the electrophysiological and pharmacological characteristics of GABAR channels expressed in the presence and absence of the delta subunit. Only alpha 1 beta 1 gamma 2L, alpha 1 beta 1 gamma 2L delta, and alpha 1 beta 1 delta subunit combinations assembled to form functional GABAR channels and the presence of the delta-subunit slowed the rate of acute desensitization of GABA-evoked current during GABA application and the rate of recovery of GABA-evoked current following GABA application. These three different GABAR channel isoforms also showed distinct pharmacological profiles with differential sensitivity to block by zinc. Zinc was a potent blocker of alpha 1 beta 1 delta GABAR channels, a moderate-strength blocker of alpha 1 beta 1 gamma 2L delta GABAR channels, and did not block the alpha 1 beta 1 gamma 2L GABAR channels. These findings suggest that GABAR isoforms containing the delta subunit constitute a novel GABAR channel with distinct electrophysiological and pharmacological characteristics.</description><identifier>ISSN: 0270-6474</identifier><identifier>EISSN: 1529-2401</identifier><identifier>DOI: 10.1523/jneurosci.14-11-07077.1994</identifier><identifier>PMID: 7525894</identifier><language>eng</language><publisher>United States: Soc Neuroscience</publisher><subject>Animals ; Cell Line ; Diazepam - pharmacology ; Electrophysiology ; Evoked Potentials - physiology ; Fibroblasts ; Ion Channels - drug effects ; Ion Channels - physiology ; Lanthanum - pharmacology ; Mice ; Pentobarbital - pharmacology ; Plasmids ; Rats ; Receptors, GABA-A - chemistry ; Receptors, GABA-A - drug effects ; Receptors, GABA-A - physiology ; Recombinant Proteins ; Zinc - pharmacology</subject><ispartof>The Journal of neuroscience, 1994-11, Vol.14 (11), p.7077-7086</ispartof><rights>1994 by Society for Neuroscience 1994</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4914-a2299a5d75e7ca8f49ba0570a3ffa78b2ae716ade9099cdf5ea12e961f924aa33</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC6577243/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC6577243/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,727,780,784,885,27924,27925,53791,53793</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/7525894$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Saxena, NC</creatorcontrib><creatorcontrib>Macdonald, RL</creatorcontrib><title>Assembly of GABAA receptor subunits: role of the delta subunit</title><title>The Journal of neuroscience</title><addtitle>J Neurosci</addtitle><description>GABAA receptor channels (GABARs) composed of different combinations of rat alpha 1, beta 1, gamma 2L, and delta subunits were expressed transiently in mouse fibroblast cells (L929 cells). Whole-cell recordings were obtained from transfected cells to determine which combinations of GABAR subunits formed functional receptor channels, and to compare the electrophysiological and pharmacological characteristics of GABAR channels expressed in the presence and absence of the delta subunit. Only alpha 1 beta 1 gamma 2L, alpha 1 beta 1 gamma 2L delta, and alpha 1 beta 1 delta subunit combinations assembled to form functional GABAR channels and the presence of the delta-subunit slowed the rate of acute desensitization of GABA-evoked current during GABA application and the rate of recovery of GABA-evoked current following GABA application. These three different GABAR channel isoforms also showed distinct pharmacological profiles with differential sensitivity to block by zinc. Zinc was a potent blocker of alpha 1 beta 1 delta GABAR channels, a moderate-strength blocker of alpha 1 beta 1 gamma 2L delta GABAR channels, and did not block the alpha 1 beta 1 gamma 2L GABAR channels. These findings suggest that GABAR isoforms containing the delta subunit constitute a novel GABAR channel with distinct electrophysiological and pharmacological characteristics.</description><subject>Animals</subject><subject>Cell Line</subject><subject>Diazepam - pharmacology</subject><subject>Electrophysiology</subject><subject>Evoked Potentials - physiology</subject><subject>Fibroblasts</subject><subject>Ion Channels - drug effects</subject><subject>Ion Channels - physiology</subject><subject>Lanthanum - pharmacology</subject><subject>Mice</subject><subject>Pentobarbital - pharmacology</subject><subject>Plasmids</subject><subject>Rats</subject><subject>Receptors, GABA-A - chemistry</subject><subject>Receptors, GABA-A - drug effects</subject><subject>Receptors, GABA-A - physiology</subject><subject>Recombinant Proteins</subject><subject>Zinc - pharmacology</subject><issn>0270-6474</issn><issn>1529-2401</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1994</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpVkE1P3DAQhq2qFWxpfwJS1EM5Zetx7DjmgBRWfFWoSG05W5NkwgY5yWInXfHvSdgtak9zeJ95Z_Qw9gX4EpRIvj12NPo-lM0SZAwQc821XoIx8h1bTISJheTwni240DxOpZaH7GMIj5xPJOgDdqCVUJmRC3aWh0Bt4Z6jvo6u8vM8jzyVtBl6H4WxGLtmCKeR7x3NwLCmqCI34N_sE_tQowv0eT-P2P3lxe_VdXx7d3Wzym_jUprpRxTCGFSVVqRLzGppCuRKc0zqGnVWCCQNKVZkuDFlVStCEGRSqI2QiElyxM52vZuxaKkqqRs8OrvxTYv-2fbY2P-Trlnbh_6PTZXWQs4FX_cFvn8aKQy2bUJJzmFH_RisTjOhIOMTeLoDy8lw8FS_HQFuZ_v2-4-L-593v1Y3FqQFsK_27Wx_Wj7-98231b3uKT_Z5evmYb1tPNnQonMTDXa73e765rrkBWTJkWU</recordid><startdate>19941101</startdate><enddate>19941101</enddate><creator>Saxena, NC</creator><creator>Macdonald, RL</creator><general>Soc Neuroscience</general><general>Society for Neuroscience</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>19941101</creationdate><title>Assembly of GABAA receptor subunits: role of the delta subunit</title><author>Saxena, NC ; Macdonald, RL</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4914-a2299a5d75e7ca8f49ba0570a3ffa78b2ae716ade9099cdf5ea12e961f924aa33</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1994</creationdate><topic>Animals</topic><topic>Cell Line</topic><topic>Diazepam - pharmacology</topic><topic>Electrophysiology</topic><topic>Evoked Potentials - physiology</topic><topic>Fibroblasts</topic><topic>Ion Channels - drug effects</topic><topic>Ion Channels - physiology</topic><topic>Lanthanum - pharmacology</topic><topic>Mice</topic><topic>Pentobarbital - pharmacology</topic><topic>Plasmids</topic><topic>Rats</topic><topic>Receptors, GABA-A - chemistry</topic><topic>Receptors, GABA-A - drug effects</topic><topic>Receptors, GABA-A - physiology</topic><topic>Recombinant Proteins</topic><topic>Zinc - pharmacology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Saxena, NC</creatorcontrib><creatorcontrib>Macdonald, RL</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>The Journal of neuroscience</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Saxena, NC</au><au>Macdonald, RL</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Assembly of GABAA receptor subunits: role of the delta subunit</atitle><jtitle>The Journal of neuroscience</jtitle><addtitle>J Neurosci</addtitle><date>1994-11-01</date><risdate>1994</risdate><volume>14</volume><issue>11</issue><spage>7077</spage><epage>7086</epage><pages>7077-7086</pages><issn>0270-6474</issn><eissn>1529-2401</eissn><abstract>GABAA receptor channels (GABARs) composed of different combinations of rat alpha 1, beta 1, gamma 2L, and delta subunits were expressed transiently in mouse fibroblast cells (L929 cells). Whole-cell recordings were obtained from transfected cells to determine which combinations of GABAR subunits formed functional receptor channels, and to compare the electrophysiological and pharmacological characteristics of GABAR channels expressed in the presence and absence of the delta subunit. Only alpha 1 beta 1 gamma 2L, alpha 1 beta 1 gamma 2L delta, and alpha 1 beta 1 delta subunit combinations assembled to form functional GABAR channels and the presence of the delta-subunit slowed the rate of acute desensitization of GABA-evoked current during GABA application and the rate of recovery of GABA-evoked current following GABA application. These three different GABAR channel isoforms also showed distinct pharmacological profiles with differential sensitivity to block by zinc. Zinc was a potent blocker of alpha 1 beta 1 delta GABAR channels, a moderate-strength blocker of alpha 1 beta 1 gamma 2L delta GABAR channels, and did not block the alpha 1 beta 1 gamma 2L GABAR channels. These findings suggest that GABAR isoforms containing the delta subunit constitute a novel GABAR channel with distinct electrophysiological and pharmacological characteristics.</abstract><cop>United States</cop><pub>Soc Neuroscience</pub><pmid>7525894</pmid><doi>10.1523/jneurosci.14-11-07077.1994</doi><tpages>10</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0270-6474 |
| ispartof | The Journal of neuroscience, 1994-11, Vol.14 (11), p.7077-7086 |
| issn | 0270-6474 1529-2401 |
| language | eng |
| recordid | cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_6577243 |
| source | PubMed Central Free; MEDLINE; EZB-FREE-00999 freely available EZB journals |
| subjects | Animals Cell Line Diazepam - pharmacology Electrophysiology Evoked Potentials - physiology Fibroblasts Ion Channels - drug effects Ion Channels - physiology Lanthanum - pharmacology Mice Pentobarbital - pharmacology Plasmids Rats Receptors, GABA-A - chemistry Receptors, GABA-A - drug effects Receptors, GABA-A - physiology Recombinant Proteins Zinc - pharmacology |
| title | Assembly of GABAA receptor subunits: role of the delta subunit |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-20T07%3A58%3A41IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_pubme&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Assembly%20of%20GABAA%20receptor%20subunits:%20role%20of%20the%20delta%20subunit&rft.jtitle=The%20Journal%20of%20neuroscience&rft.au=Saxena,%20NC&rft.date=1994-11-01&rft.volume=14&rft.issue=11&rft.spage=7077&rft.epage=7086&rft.pages=7077-7086&rft.issn=0270-6474&rft.eissn=1529-2401&rft_id=info:doi/10.1523/jneurosci.14-11-07077.1994&rft_dat=%3Cproquest_pubme%3E76825180%3C/proquest_pubme%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=76825180&rft_id=info:pmid/7525894&rfr_iscdi=true |