The Temperature-Sensitive Ion Channel TRPV2 is Endogenously Expressed and Functional in the Primary Sensory Cell Line F-11

In sensory neurons heat is transduced by a subfamily of TRP channels sharing sequence homology with the capsaicin-sensitive vanilloid receptor subtype 1 (TRPV1), but differing in their thermal response thresholds. To identify a neuronal cell line endogenously expressing noxious heat-transducing ion...

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Veröffentlicht in:Cellular physiology and biochemistry 2005-01, Vol.15 (1-4), p.183-194
Hauptverfasser: Bender, Florian, Mederos y Schnitzler, Michael, Li, Yanzhang, Ji, Ailing, Weihe, Eberhard, Gudermann, Thomas, Schäfer, Martin
Format: Artikel
Sprache:eng
Schlagworte:
Online-Zugang:Volltext
Tags: Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
container_end_page 194
container_issue 1-4
container_start_page 183
container_title Cellular physiology and biochemistry
container_volume 15
creator Bender, Florian
Mederos y Schnitzler, Michael
Li, Yanzhang
Ji, Ailing
Weihe, Eberhard
Gudermann, Thomas
Schäfer, Martin
description In sensory neurons heat is transduced by a subfamily of TRP channels sharing sequence homology with the capsaicin-sensitive vanilloid receptor subtype 1 (TRPV1), but differing in their thermal response thresholds. To identify a neuronal cell line endogenously expressing noxious heat-transducing ion channels, we examined F-11 cells, a hybridoma derived from rat dorsal root ganglia and mouse neuroblastoma. Using RT-PCR, transcripts homologous to TRPV2 and TRPV4, but not to TRPV1 or TRPV3, were found. We isolated a full-length cDNA of 2.4 kb coding for a 757-amino acid protein corresponding to mouse TRPV2, which was further characterized by immunocytochemistry and electrophysiology. Using the whole-cell patch-clamp technique, we observed a heat-evoked increase in outward and inward currents with a threshold of 51.6 ± 0.2°C. The current-voltage relationship stimulated by a temperature of 52°C was characterized by an outward rectification with a reversal potential close to –10 mV. Heat-evoked currents could be inhibited by ruthenium red. There was no activation by stimulation with capsaicin or 2-aminoethoxydiphenyl borate. Our results indicate that F-11 cells express functional noxious heat-sensitive TRPV2 channels. Thus, we propose that F-11 cells represent a valuable in vitro model to characterize the properties of TRPV2 in a native neuronal environment.
doi_str_mv 10.1159/000083651
format Article
fullrecord <record><control><sourceid>proquest_karge</sourceid><recordid>TN_cdi_karger_primary_83651</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>67370386</sourcerecordid><originalsourceid>FETCH-LOGICAL-k186t-40e14f3146641e422a71700b842523897efa135bab1135ce9c55a7d6fa5610b73</originalsourceid><addsrcrecordid>eNptkM1Lw0AQxRdRbK0ePAuyePAW3UmyHzlqaLVQsGj1GjbNpI1NNzGbiPWvd23Vk3N5M_Dj8eYRcgrsCoBH18yNCgSHPdKH0AcvklLtu50B91SkZI8cWfvK3Ckj_5D0gAvBua_65HO2RDrDdY2NbrsGvSc0tmiLd6TjytB4qY3Bks4epy8-LSwdmqxaoKk6W27o8KNu0FrMqDYZHXVm3haV0SUtDG2d77Qp1rrZ0G_PymmMZUknhUE68gCOyUGuS4snPzogz6PhLL73Jg934_hm4q1AidYLGUKYBxAKEQKGvq8lSMZSFfrcD1QkMdcQ8FSn4GSO0ZxzLTORay6ApTIYkMudb91Ubx3aNlkXdu6iaIPuj0TIQLJACQee_4BdusYsqXfxk9-2HHCxA1a6WWDzB8TT2239SZ3lDjr7F9oSwRfDxX56</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>67370386</pqid></control><display><type>article</type><title>The Temperature-Sensitive Ion Channel TRPV2 is Endogenously Expressed and Functional in the Primary Sensory Cell Line F-11</title><source>MEDLINE</source><source>Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals</source><creator>Bender, Florian ; Mederos y Schnitzler, Michael ; Li, Yanzhang ; Ji, Ailing ; Weihe, Eberhard ; Gudermann, Thomas ; Schäfer, Martin</creator><creatorcontrib>Bender, Florian ; Mederos y Schnitzler, Michael ; Li, Yanzhang ; Ji, Ailing ; Weihe, Eberhard ; Gudermann, Thomas ; Schäfer, Martin</creatorcontrib><description>In sensory neurons heat is transduced by a subfamily of TRP channels sharing sequence homology with the capsaicin-sensitive vanilloid receptor subtype 1 (TRPV1), but differing in their thermal response thresholds. To identify a neuronal cell line endogenously expressing noxious heat-transducing ion channels, we examined F-11 cells, a hybridoma derived from rat dorsal root ganglia and mouse neuroblastoma. Using RT-PCR, transcripts homologous to TRPV2 and TRPV4, but not to TRPV1 or TRPV3, were found. We isolated a full-length cDNA of 2.4 kb coding for a 757-amino acid protein corresponding to mouse TRPV2, which was further characterized by immunocytochemistry and electrophysiology. Using the whole-cell patch-clamp technique, we observed a heat-evoked increase in outward and inward currents with a threshold of 51.6 ± 0.2°C. The current-voltage relationship stimulated by a temperature of 52°C was characterized by an outward rectification with a reversal potential close to –10 mV. Heat-evoked currents could be inhibited by ruthenium red. There was no activation by stimulation with capsaicin or 2-aminoethoxydiphenyl borate. Our results indicate that F-11 cells express functional noxious heat-sensitive TRPV2 channels. Thus, we propose that F-11 cells represent a valuable in vitro model to characterize the properties of TRPV2 in a native neuronal environment.</description><identifier>ISSN: 1015-8987</identifier><identifier>EISSN: 1421-9778</identifier><identifier>DOI: 10.1159/000083651</identifier><identifier>PMID: 15665528</identifier><language>eng</language><publisher>Basel, Switzerland</publisher><subject>Animals ; Cell Line ; Ganglia, Spinal - metabolism ; Humans ; Ion Channels - genetics ; Ion Channels - metabolism ; Male ; Mice ; Mice, Inbred BALB C ; Original Paper ; Protein Isoforms - genetics ; Protein Isoforms - metabolism ; Rats ; Rats, Wistar ; Receptors, Drug - genetics ; Receptors, Drug - metabolism ; RNA, Messenger - analysis ; RNA, Messenger - genetics ; Temperature ; TRPV Cation Channels</subject><ispartof>Cellular physiology and biochemistry, 2005-01, Vol.15 (1-4), p.183-194</ispartof><rights>2005 S. Karger AG, Basel</rights><rights>Copyright 2005 S. Karger AG, Basel.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27903,27904</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15665528$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Bender, Florian</creatorcontrib><creatorcontrib>Mederos y Schnitzler, Michael</creatorcontrib><creatorcontrib>Li, Yanzhang</creatorcontrib><creatorcontrib>Ji, Ailing</creatorcontrib><creatorcontrib>Weihe, Eberhard</creatorcontrib><creatorcontrib>Gudermann, Thomas</creatorcontrib><creatorcontrib>Schäfer, Martin</creatorcontrib><title>The Temperature-Sensitive Ion Channel TRPV2 is Endogenously Expressed and Functional in the Primary Sensory Cell Line F-11</title><title>Cellular physiology and biochemistry</title><addtitle>Cell Physiol Biochem</addtitle><description>In sensory neurons heat is transduced by a subfamily of TRP channels sharing sequence homology with the capsaicin-sensitive vanilloid receptor subtype 1 (TRPV1), but differing in their thermal response thresholds. To identify a neuronal cell line endogenously expressing noxious heat-transducing ion channels, we examined F-11 cells, a hybridoma derived from rat dorsal root ganglia and mouse neuroblastoma. Using RT-PCR, transcripts homologous to TRPV2 and TRPV4, but not to TRPV1 or TRPV3, were found. We isolated a full-length cDNA of 2.4 kb coding for a 757-amino acid protein corresponding to mouse TRPV2, which was further characterized by immunocytochemistry and electrophysiology. Using the whole-cell patch-clamp technique, we observed a heat-evoked increase in outward and inward currents with a threshold of 51.6 ± 0.2°C. The current-voltage relationship stimulated by a temperature of 52°C was characterized by an outward rectification with a reversal potential close to –10 mV. Heat-evoked currents could be inhibited by ruthenium red. There was no activation by stimulation with capsaicin or 2-aminoethoxydiphenyl borate. Our results indicate that F-11 cells express functional noxious heat-sensitive TRPV2 channels. Thus, we propose that F-11 cells represent a valuable in vitro model to characterize the properties of TRPV2 in a native neuronal environment.</description><subject>Animals</subject><subject>Cell Line</subject><subject>Ganglia, Spinal - metabolism</subject><subject>Humans</subject><subject>Ion Channels - genetics</subject><subject>Ion Channels - metabolism</subject><subject>Male</subject><subject>Mice</subject><subject>Mice, Inbred BALB C</subject><subject>Original Paper</subject><subject>Protein Isoforms - genetics</subject><subject>Protein Isoforms - metabolism</subject><subject>Rats</subject><subject>Rats, Wistar</subject><subject>Receptors, Drug - genetics</subject><subject>Receptors, Drug - metabolism</subject><subject>RNA, Messenger - analysis</subject><subject>RNA, Messenger - genetics</subject><subject>Temperature</subject><subject>TRPV Cation Channels</subject><issn>1015-8987</issn><issn>1421-9778</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2005</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNptkM1Lw0AQxRdRbK0ePAuyePAW3UmyHzlqaLVQsGj1GjbNpI1NNzGbiPWvd23Vk3N5M_Dj8eYRcgrsCoBH18yNCgSHPdKH0AcvklLtu50B91SkZI8cWfvK3Ckj_5D0gAvBua_65HO2RDrDdY2NbrsGvSc0tmiLd6TjytB4qY3Bks4epy8-LSwdmqxaoKk6W27o8KNu0FrMqDYZHXVm3haV0SUtDG2d77Qp1rrZ0G_PymmMZUknhUE68gCOyUGuS4snPzogz6PhLL73Jg934_hm4q1AidYLGUKYBxAKEQKGvq8lSMZSFfrcD1QkMdcQ8FSn4GSO0ZxzLTORay6ApTIYkMudb91Ubx3aNlkXdu6iaIPuj0TIQLJACQee_4BdusYsqXfxk9-2HHCxA1a6WWDzB8TT2239SZ3lDjr7F9oSwRfDxX56</recordid><startdate>20050101</startdate><enddate>20050101</enddate><creator>Bender, Florian</creator><creator>Mederos y Schnitzler, Michael</creator><creator>Li, Yanzhang</creator><creator>Ji, Ailing</creator><creator>Weihe, Eberhard</creator><creator>Gudermann, Thomas</creator><creator>Schäfer, Martin</creator><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7X8</scope></search><sort><creationdate>20050101</creationdate><title>The Temperature-Sensitive Ion Channel TRPV2 is Endogenously Expressed and Functional in the Primary Sensory Cell Line F-11</title><author>Bender, Florian ; Mederos y Schnitzler, Michael ; Li, Yanzhang ; Ji, Ailing ; Weihe, Eberhard ; Gudermann, Thomas ; Schäfer, Martin</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-k186t-40e14f3146641e422a71700b842523897efa135bab1135ce9c55a7d6fa5610b73</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2005</creationdate><topic>Animals</topic><topic>Cell Line</topic><topic>Ganglia, Spinal - metabolism</topic><topic>Humans</topic><topic>Ion Channels - genetics</topic><topic>Ion Channels - metabolism</topic><topic>Male</topic><topic>Mice</topic><topic>Mice, Inbred BALB C</topic><topic>Original Paper</topic><topic>Protein Isoforms - genetics</topic><topic>Protein Isoforms - metabolism</topic><topic>Rats</topic><topic>Rats, Wistar</topic><topic>Receptors, Drug - genetics</topic><topic>Receptors, Drug - metabolism</topic><topic>RNA, Messenger - analysis</topic><topic>RNA, Messenger - genetics</topic><topic>Temperature</topic><topic>TRPV Cation Channels</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Bender, Florian</creatorcontrib><creatorcontrib>Mederos y Schnitzler, Michael</creatorcontrib><creatorcontrib>Li, Yanzhang</creatorcontrib><creatorcontrib>Ji, Ailing</creatorcontrib><creatorcontrib>Weihe, Eberhard</creatorcontrib><creatorcontrib>Gudermann, Thomas</creatorcontrib><creatorcontrib>Schäfer, Martin</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>MEDLINE - Academic</collection><jtitle>Cellular physiology and biochemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Bender, Florian</au><au>Mederos y Schnitzler, Michael</au><au>Li, Yanzhang</au><au>Ji, Ailing</au><au>Weihe, Eberhard</au><au>Gudermann, Thomas</au><au>Schäfer, Martin</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The Temperature-Sensitive Ion Channel TRPV2 is Endogenously Expressed and Functional in the Primary Sensory Cell Line F-11</atitle><jtitle>Cellular physiology and biochemistry</jtitle><addtitle>Cell Physiol Biochem</addtitle><date>2005-01-01</date><risdate>2005</risdate><volume>15</volume><issue>1-4</issue><spage>183</spage><epage>194</epage><pages>183-194</pages><issn>1015-8987</issn><eissn>1421-9778</eissn><abstract>In sensory neurons heat is transduced by a subfamily of TRP channels sharing sequence homology with the capsaicin-sensitive vanilloid receptor subtype 1 (TRPV1), but differing in their thermal response thresholds. To identify a neuronal cell line endogenously expressing noxious heat-transducing ion channels, we examined F-11 cells, a hybridoma derived from rat dorsal root ganglia and mouse neuroblastoma. Using RT-PCR, transcripts homologous to TRPV2 and TRPV4, but not to TRPV1 or TRPV3, were found. We isolated a full-length cDNA of 2.4 kb coding for a 757-amino acid protein corresponding to mouse TRPV2, which was further characterized by immunocytochemistry and electrophysiology. Using the whole-cell patch-clamp technique, we observed a heat-evoked increase in outward and inward currents with a threshold of 51.6 ± 0.2°C. The current-voltage relationship stimulated by a temperature of 52°C was characterized by an outward rectification with a reversal potential close to –10 mV. Heat-evoked currents could be inhibited by ruthenium red. There was no activation by stimulation with capsaicin or 2-aminoethoxydiphenyl borate. Our results indicate that F-11 cells express functional noxious heat-sensitive TRPV2 channels. Thus, we propose that F-11 cells represent a valuable in vitro model to characterize the properties of TRPV2 in a native neuronal environment.</abstract><cop>Basel, Switzerland</cop><pmid>15665528</pmid><doi>10.1159/000083651</doi><tpages>12</tpages></addata></record>
fulltext fulltext
identifier ISSN: 1015-8987
ispartof Cellular physiology and biochemistry, 2005-01, Vol.15 (1-4), p.183-194
issn 1015-8987
1421-9778
language eng
recordid cdi_karger_primary_83651
source MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals
subjects Animals
Cell Line
Ganglia, Spinal - metabolism
Humans
Ion Channels - genetics
Ion Channels - metabolism
Male
Mice
Mice, Inbred BALB C
Original Paper
Protein Isoforms - genetics
Protein Isoforms - metabolism
Rats
Rats, Wistar
Receptors, Drug - genetics
Receptors, Drug - metabolism
RNA, Messenger - analysis
RNA, Messenger - genetics
Temperature
TRPV Cation Channels
title The Temperature-Sensitive Ion Channel TRPV2 is Endogenously Expressed and Functional in the Primary Sensory Cell Line F-11
url https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-23T21%3A44%3A33IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_karge&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=The%20Temperature-Sensitive%20Ion%20Channel%20TRPV2%20is%20Endogenously%20Expressed%20and%20Functional%20in%20the%20Primary%20Sensory%20Cell%20Line%20F-11&rft.jtitle=Cellular%20physiology%20and%20biochemistry&rft.au=Bender,%20Florian&rft.date=2005-01-01&rft.volume=15&rft.issue=1-4&rft.spage=183&rft.epage=194&rft.pages=183-194&rft.issn=1015-8987&rft.eissn=1421-9778&rft_id=info:doi/10.1159/000083651&rft_dat=%3Cproquest_karge%3E67370386%3C/proquest_karge%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=67370386&rft_id=info:pmid/15665528&rfr_iscdi=true