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Revisiting TRPC1 and TRPC6 mechanosensitivity
This article addresses whether TRPC1 or TRPC6 is an essential component of a mammalian stretch-activated mechano-sensitive Ca 2+ permeable cation channel (MscCa). We have transiently expressed TRPC1 and TRPC6 in African green monkey kidney (COS) or Chinese hamster ovary (CHO) cells and monitored the...
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| Published in: | Pflügers Archiv 2008-03, Vol.455 (6), p.1097-1103 |
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| container_end_page | 1103 |
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| container_title | Pflügers Archiv |
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| creator | Gottlieb, Philip Folgering, Joost Maroto, Rosario Raso, Albert Wood, Thomas G. Kurosky, Alex Bowman, Charles Bichet, Delphine Patel, Amanda Sachs, Frederick Martinac, Boris Hamill, Owen P. Honoré, Eric |
| description | This article addresses whether TRPC1 or TRPC6 is an essential component of a mammalian stretch-activated mechano-sensitive Ca
2+
permeable cation channel (MscCa). We have transiently expressed TRPC1 and TRPC6 in African green monkey kidney (COS) or Chinese hamster ovary (CHO) cells and monitored the activity of the stretch-activated channels using a fast pressure clamp system. Although both TRPC1 and TRPC6 are highly expressed at the protein level, the amplitude of the mechano-sensitive current is not significantly altered by overexpression of these subunits. In conclusion, although several TRPC channel members, including TRPC1 and TRPC6, have been recently proposed to form MscCa in vertebrate cells, the functional expression of these TRPC subunits in heterologous systems remains problematic. |
| doi_str_mv | 10.1007/s00424-007-0359-3 |
| format | article |
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2+
permeable cation channel (MscCa). We have transiently expressed TRPC1 and TRPC6 in African green monkey kidney (COS) or Chinese hamster ovary (CHO) cells and monitored the activity of the stretch-activated channels using a fast pressure clamp system. Although both TRPC1 and TRPC6 are highly expressed at the protein level, the amplitude of the mechano-sensitive current is not significantly altered by overexpression of these subunits. In conclusion, although several TRPC channel members, including TRPC1 and TRPC6, have been recently proposed to form MscCa in vertebrate cells, the functional expression of these TRPC subunits in heterologous systems remains problematic.</description><identifier>ISSN: 0031-6768</identifier><identifier>EISSN: 1432-2013</identifier><identifier>DOI: 10.1007/s00424-007-0359-3</identifier><identifier>PMID: 17957383</identifier><language>eng</language><publisher>Berlin/Heidelberg: Springer-Verlag</publisher><subject>Animals ; Biomedical and Life Sciences ; Biomedicine ; Cell Biology ; Cell Membrane ; Cell Membrane - metabolism ; Cells ; Cercopithecus aethiops ; CHO Cells ; COS Cells ; Cricetinae ; Cricetulus ; Human health and pathology ; Human Physiology ; Humans ; Ion Channels ; Life Sciences ; Mechanoreceptors ; Mechanoreceptors - physiology ; Microscopy, Confocal ; Molecular Medicine ; Neurons and Cognition ; Neurosciences ; Patch-Clamp Techniques ; Pharmaceutical sciences ; Plasmids ; Receptors ; Transfection ; TRPC Cation Channels ; TRPC Cation Channels - biosynthesis ; TRPC Cation Channels - genetics ; TRPC Cation Channels - physiology ; TRPC6 Cation Channel</subject><ispartof>Pflügers Archiv, 2008-03, Vol.455 (6), p.1097-1103</ispartof><rights>Springer-Verlag 2007</rights><rights>Springer-Verlag 2008</rights><rights>Distributed under a Creative Commons Attribution 4.0 International License</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c446t-80ca5a0a7be96f9eca49b948478c8a4a51c378d08669f8d75eb8d0c2f003a4833</citedby><cites>FETCH-LOGICAL-c446t-80ca5a0a7be96f9eca49b948478c8a4a51c378d08669f8d75eb8d0c2f003a4833</cites><orcidid>0000-0002-9601-089X ; 0000-0002-8007-0919</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>230,314,776,780,881,27903,27904</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/17957383$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://hal.science/hal-00315027$$DView record in HAL$$Hfree_for_read</backlink></links><search><creatorcontrib>Gottlieb, Philip</creatorcontrib><creatorcontrib>Folgering, Joost</creatorcontrib><creatorcontrib>Maroto, Rosario</creatorcontrib><creatorcontrib>Raso, Albert</creatorcontrib><creatorcontrib>Wood, Thomas G.</creatorcontrib><creatorcontrib>Kurosky, Alex</creatorcontrib><creatorcontrib>Bowman, Charles</creatorcontrib><creatorcontrib>Bichet, Delphine</creatorcontrib><creatorcontrib>Patel, Amanda</creatorcontrib><creatorcontrib>Sachs, Frederick</creatorcontrib><creatorcontrib>Martinac, Boris</creatorcontrib><creatorcontrib>Hamill, Owen P.</creatorcontrib><creatorcontrib>Honoré, Eric</creatorcontrib><title>Revisiting TRPC1 and TRPC6 mechanosensitivity</title><title>Pflügers Archiv</title><addtitle>Pflugers Arch - Eur J Physiol</addtitle><addtitle>Pflugers Arch</addtitle><description>This article addresses whether TRPC1 or TRPC6 is an essential component of a mammalian stretch-activated mechano-sensitive Ca
2+
permeable cation channel (MscCa). We have transiently expressed TRPC1 and TRPC6 in African green monkey kidney (COS) or Chinese hamster ovary (CHO) cells and monitored the activity of the stretch-activated channels using a fast pressure clamp system. Although both TRPC1 and TRPC6 are highly expressed at the protein level, the amplitude of the mechano-sensitive current is not significantly altered by overexpression of these subunits. In conclusion, although several TRPC channel members, including TRPC1 and TRPC6, have been recently proposed to form MscCa in vertebrate cells, the functional expression of these TRPC subunits in heterologous systems remains problematic.</description><subject>Animals</subject><subject>Biomedical and Life Sciences</subject><subject>Biomedicine</subject><subject>Cell Biology</subject><subject>Cell Membrane</subject><subject>Cell Membrane - metabolism</subject><subject>Cells</subject><subject>Cercopithecus aethiops</subject><subject>CHO Cells</subject><subject>COS Cells</subject><subject>Cricetinae</subject><subject>Cricetulus</subject><subject>Human health and pathology</subject><subject>Human Physiology</subject><subject>Humans</subject><subject>Ion Channels</subject><subject>Life Sciences</subject><subject>Mechanoreceptors</subject><subject>Mechanoreceptors - physiology</subject><subject>Microscopy, Confocal</subject><subject>Molecular Medicine</subject><subject>Neurons and Cognition</subject><subject>Neurosciences</subject><subject>Patch-Clamp Techniques</subject><subject>Pharmaceutical sciences</subject><subject>Plasmids</subject><subject>Receptors</subject><subject>Transfection</subject><subject>TRPC Cation Channels</subject><subject>TRPC Cation Channels - biosynthesis</subject><subject>TRPC Cation Channels - genetics</subject><subject>TRPC Cation Channels - physiology</subject><subject>TRPC6 Cation Channel</subject><issn>0031-6768</issn><issn>1432-2013</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2008</creationdate><recordtype>article</recordtype><recordid>eNp1kEtLAzEUhYMotlZ_gBspLgQX0ZvXJLOUolYoKKWuQyaTaafMo046hf57M06xILjKyc2Xc-89CF0TeCAA8tEDcMpxkBiYiDE7QUPCGcUUCDtFQwBGcCQjNUAX3q8BgHJFz9GAyFhIptgQ4bnb5T7f5tVyvJh_TMjYVOmPisalsytT1d5VHbDLt_tLdJaZwrurwzlCny_Pi8kUz95f3yZPM2w5j7ZYgTXCgJGJi6MsdtbwOIm54lJZZbgRxDKpUlBRFGcqlcIl4WZpFgY2XDE2Qve978oUetPkpWn2uja5nj7NdFfrNhNA5Y4E9q5nN0391Tq_1WXurSsKU7m69VoCZVQQEcDbP-C6bpsq7KFp8IOYShUg0kO2qb1vXPbbnoDuQtd96LqTXei6m_bmYNwmpUuPPw4pB4D2gA9P1dI1x87_u34DOl2IrQ</recordid><startdate>20080301</startdate><enddate>20080301</enddate><creator>Gottlieb, Philip</creator><creator>Folgering, Joost</creator><creator>Maroto, Rosario</creator><creator>Raso, Albert</creator><creator>Wood, Thomas G.</creator><creator>Kurosky, Alex</creator><creator>Bowman, Charles</creator><creator>Bichet, Delphine</creator><creator>Patel, Amanda</creator><creator>Sachs, Frederick</creator><creator>Martinac, Boris</creator><creator>Hamill, Owen P.</creator><creator>Honoré, Eric</creator><general>Springer-Verlag</general><general>Springer Nature B.V</general><general>Springer Verlag</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>3V.</scope><scope>7QP</scope><scope>7TK</scope><scope>7TS</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</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>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>7X8</scope><scope>1XC</scope><orcidid>https://orcid.org/0000-0002-9601-089X</orcidid><orcidid>https://orcid.org/0000-0002-8007-0919</orcidid></search><sort><creationdate>20080301</creationdate><title>Revisiting TRPC1 and TRPC6 mechanosensitivity</title><author>Gottlieb, Philip ; Folgering, Joost ; Maroto, Rosario ; Raso, Albert ; Wood, Thomas G. ; Kurosky, Alex ; Bowman, Charles ; Bichet, Delphine ; Patel, Amanda ; Sachs, Frederick ; Martinac, Boris ; Hamill, Owen P. ; Honoré, Eric</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c446t-80ca5a0a7be96f9eca49b948478c8a4a51c378d08669f8d75eb8d0c2f003a4833</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2008</creationdate><topic>Animals</topic><topic>Biomedical and Life Sciences</topic><topic>Biomedicine</topic><topic>Cell Biology</topic><topic>Cell Membrane</topic><topic>Cell Membrane - 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Academic</collection><collection>Hyper Article en Ligne (HAL)</collection><jtitle>Pflügers Archiv</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Gottlieb, Philip</au><au>Folgering, Joost</au><au>Maroto, Rosario</au><au>Raso, Albert</au><au>Wood, Thomas G.</au><au>Kurosky, Alex</au><au>Bowman, Charles</au><au>Bichet, Delphine</au><au>Patel, Amanda</au><au>Sachs, Frederick</au><au>Martinac, Boris</au><au>Hamill, Owen P.</au><au>Honoré, Eric</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Revisiting TRPC1 and TRPC6 mechanosensitivity</atitle><jtitle>Pflügers Archiv</jtitle><stitle>Pflugers Arch - Eur J Physiol</stitle><addtitle>Pflugers Arch</addtitle><date>2008-03-01</date><risdate>2008</risdate><volume>455</volume><issue>6</issue><spage>1097</spage><epage>1103</epage><pages>1097-1103</pages><issn>0031-6768</issn><eissn>1432-2013</eissn><abstract>This article addresses whether TRPC1 or TRPC6 is an essential component of a mammalian stretch-activated mechano-sensitive Ca
2+
permeable cation channel (MscCa). We have transiently expressed TRPC1 and TRPC6 in African green monkey kidney (COS) or Chinese hamster ovary (CHO) cells and monitored the activity of the stretch-activated channels using a fast pressure clamp system. Although both TRPC1 and TRPC6 are highly expressed at the protein level, the amplitude of the mechano-sensitive current is not significantly altered by overexpression of these subunits. In conclusion, although several TRPC channel members, including TRPC1 and TRPC6, have been recently proposed to form MscCa in vertebrate cells, the functional expression of these TRPC subunits in heterologous systems remains problematic.</abstract><cop>Berlin/Heidelberg</cop><pub>Springer-Verlag</pub><pmid>17957383</pmid><doi>10.1007/s00424-007-0359-3</doi><tpages>7</tpages><orcidid>https://orcid.org/0000-0002-9601-089X</orcidid><orcidid>https://orcid.org/0000-0002-8007-0919</orcidid><oa>free_for_read</oa></addata></record> |
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| identifier | ISSN: 0031-6768 |
| ispartof | Pflügers Archiv, 2008-03, Vol.455 (6), p.1097-1103 |
| issn | 0031-6768 1432-2013 |
| language | eng |
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| source | Springer Nature |
| subjects | Animals Biomedical and Life Sciences Biomedicine Cell Biology Cell Membrane Cell Membrane - metabolism Cells Cercopithecus aethiops CHO Cells COS Cells Cricetinae Cricetulus Human health and pathology Human Physiology Humans Ion Channels Life Sciences Mechanoreceptors Mechanoreceptors - physiology Microscopy, Confocal Molecular Medicine Neurons and Cognition Neurosciences Patch-Clamp Techniques Pharmaceutical sciences Plasmids Receptors Transfection TRPC Cation Channels TRPC Cation Channels - biosynthesis TRPC Cation Channels - genetics TRPC Cation Channels - physiology TRPC6 Cation Channel |
| title | Revisiting TRPC1 and TRPC6 mechanosensitivity |
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