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Kir2.1 encodes the inward rectifier potassium channel in rat arterial smooth muscle cells
The molecular nature of the strong inward rectifier K + channel in vascular smooth muscle was explored by using isolated cell RT-PCR, cDNA cloning and expression techniques. RT-PCR of RNA from single smooth muscle cells of rat cerebral (basilar), coronary and mesenteric arteries revealed transcripts...
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Published in: | The Journal of physiology 1999-03, Vol.515 (3), p.639-651 |
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creator | Bradley, Karri K. Jaggar, Jonathan H. Bonev, Adrian D. Heppner, Thomas J. Flynn, Elaine R.M. Nelson, Mark T. Horowitz, Burton |
description | The molecular nature of the strong inward rectifier K + channel in vascular smooth muscle was explored by using isolated cell RT-PCR, cDNA cloning and expression techniques.
RT-PCR of RNA from single smooth muscle cells of rat cerebral (basilar), coronary and mesenteric arteries revealed transcripts
for K ir 2.1. Transcripts for K ir 2.2 and K ir 2.3 were not found.
Quantitative PCR analysis revealed significant differences in transcript levels of K ir 2.1 between the different vascular preparations ( n = 3; P < 0.05). A two-fold difference was detected between K ir 2.1 mRNA and β-actin mRNA in coronary arteries when compared with relative levels measured in mesenteric and basilar preparations.
K ir 2.1 was cloned from rat mesenteric vascular smooth muscle cells and expressed in Xenopus oocytes. Currents were strongly inwardly rectifying and selective for K + .
The effect of extracellular Ba 2+ , Ca 2+ , Mg 2+ and Cs 2+ ions on cloned K ir 2.1 channels expressed in Xenopus oocytes was examined. Ba 2+ and Cs + block were steeply voltage dependent, whereas block by external Ca 2+ and Mg 2+ exhibited little voltage dependence. The apparent half-block constants and voltage dependences for Ba 2+ , Cs + , Ca 2+ and Mg 2+ were very similar for inward rectifier K + currents from native cells and cloned K ir 2.1 channels expressed in oocytes.
Molecular studies demonstrate that K ir 2.1 is the only member of the K ir 2 channel subfamily present in vascular arterial smooth muscle cells. Expression of cloned K ir 2.1 in Xenopus oocytes resulted in inward rectifier K + currents that strongly resemble those that are observed in native vascular arterial smooth muscle cells. We conclude that
K ir 2.1 encodes for inward rectifier K + channels in arterial smooth muscle. |
doi_str_mv | 10.1111/j.1469-7793.1999.639ab.x |
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RT-PCR of RNA from single smooth muscle cells of rat cerebral (basilar), coronary and mesenteric arteries revealed transcripts
for K ir 2.1. Transcripts for K ir 2.2 and K ir 2.3 were not found.
Quantitative PCR analysis revealed significant differences in transcript levels of K ir 2.1 between the different vascular preparations ( n = 3; P < 0.05). A two-fold difference was detected between K ir 2.1 mRNA and β-actin mRNA in coronary arteries when compared with relative levels measured in mesenteric and basilar preparations.
K ir 2.1 was cloned from rat mesenteric vascular smooth muscle cells and expressed in Xenopus oocytes. Currents were strongly inwardly rectifying and selective for K + .
The effect of extracellular Ba 2+ , Ca 2+ , Mg 2+ and Cs 2+ ions on cloned K ir 2.1 channels expressed in Xenopus oocytes was examined. Ba 2+ and Cs + block were steeply voltage dependent, whereas block by external Ca 2+ and Mg 2+ exhibited little voltage dependence. The apparent half-block constants and voltage dependences for Ba 2+ , Cs + , Ca 2+ and Mg 2+ were very similar for inward rectifier K + currents from native cells and cloned K ir 2.1 channels expressed in oocytes.
Molecular studies demonstrate that K ir 2.1 is the only member of the K ir 2 channel subfamily present in vascular arterial smooth muscle cells. Expression of cloned K ir 2.1 in Xenopus oocytes resulted in inward rectifier K + currents that strongly resemble those that are observed in native vascular arterial smooth muscle cells. We conclude that
K ir 2.1 encodes for inward rectifier K + channels in arterial smooth muscle.</description><identifier>ISSN: 0022-3751</identifier><identifier>EISSN: 1469-7793</identifier><identifier>DOI: 10.1111/j.1469-7793.1999.639ab.x</identifier><identifier>PMID: 10066894</identifier><language>eng</language><publisher>Oxford, UK: The Physiological Society</publisher><subject>Animals ; Barium - pharmacology ; Basilar Artery - metabolism ; Cesium - pharmacology ; Cloning, Molecular ; Coronary Vessels - metabolism ; Membrane Potentials - drug effects ; Mesenteric Arteries - metabolism ; Muscle, Smooth, Vascular - metabolism ; Oocytes - physiology ; Original ; Patch-Clamp Techniques ; Potassium - pharmacology ; Potassium Channels - drug effects ; Potassium Channels - genetics ; Potassium Channels - physiology ; Potassium Channels, Inwardly Rectifying ; Rats ; Rats, Sprague-Dawley ; Recombinant Proteins - metabolism ; Reverse Transcriptase Polymerase Chain Reaction ; Transcription, Genetic ; Xenopus laevis</subject><ispartof>The Journal of physiology, 1999-03, Vol.515 (3), p.639-651</ispartof><rights>1999 The Journal of Physiology © 1999 The Physiological Society</rights><rights>The Physiological Society 1999 1999</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/PMC2269194/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC2269194/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,723,776,780,881,27903,27904,53769,53771</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/10066894$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Bradley, Karri K.</creatorcontrib><creatorcontrib>Jaggar, Jonathan H.</creatorcontrib><creatorcontrib>Bonev, Adrian D.</creatorcontrib><creatorcontrib>Heppner, Thomas J.</creatorcontrib><creatorcontrib>Flynn, Elaine R.M.</creatorcontrib><creatorcontrib>Nelson, Mark T.</creatorcontrib><creatorcontrib>Horowitz, Burton</creatorcontrib><title>Kir2.1 encodes the inward rectifier potassium channel in rat arterial smooth muscle cells</title><title>The Journal of physiology</title><addtitle>J Physiol</addtitle><description>The molecular nature of the strong inward rectifier K + channel in vascular smooth muscle was explored by using isolated cell RT-PCR, cDNA cloning and expression techniques.
RT-PCR of RNA from single smooth muscle cells of rat cerebral (basilar), coronary and mesenteric arteries revealed transcripts
for K ir 2.1. Transcripts for K ir 2.2 and K ir 2.3 were not found.
Quantitative PCR analysis revealed significant differences in transcript levels of K ir 2.1 between the different vascular preparations ( n = 3; P < 0.05). A two-fold difference was detected between K ir 2.1 mRNA and β-actin mRNA in coronary arteries when compared with relative levels measured in mesenteric and basilar preparations.
K ir 2.1 was cloned from rat mesenteric vascular smooth muscle cells and expressed in Xenopus oocytes. Currents were strongly inwardly rectifying and selective for K + .
The effect of extracellular Ba 2+ , Ca 2+ , Mg 2+ and Cs 2+ ions on cloned K ir 2.1 channels expressed in Xenopus oocytes was examined. Ba 2+ and Cs + block were steeply voltage dependent, whereas block by external Ca 2+ and Mg 2+ exhibited little voltage dependence. The apparent half-block constants and voltage dependences for Ba 2+ , Cs + , Ca 2+ and Mg 2+ were very similar for inward rectifier K + currents from native cells and cloned K ir 2.1 channels expressed in oocytes.
Molecular studies demonstrate that K ir 2.1 is the only member of the K ir 2 channel subfamily present in vascular arterial smooth muscle cells. Expression of cloned K ir 2.1 in Xenopus oocytes resulted in inward rectifier K + currents that strongly resemble those that are observed in native vascular arterial smooth muscle cells. We conclude that
K ir 2.1 encodes for inward rectifier K + channels in arterial smooth muscle.</description><subject>Animals</subject><subject>Barium - pharmacology</subject><subject>Basilar Artery - metabolism</subject><subject>Cesium - pharmacology</subject><subject>Cloning, Molecular</subject><subject>Coronary Vessels - metabolism</subject><subject>Membrane Potentials - drug effects</subject><subject>Mesenteric Arteries - metabolism</subject><subject>Muscle, Smooth, Vascular - metabolism</subject><subject>Oocytes - physiology</subject><subject>Original</subject><subject>Patch-Clamp Techniques</subject><subject>Potassium - pharmacology</subject><subject>Potassium Channels - drug effects</subject><subject>Potassium Channels - genetics</subject><subject>Potassium Channels - physiology</subject><subject>Potassium Channels, Inwardly Rectifying</subject><subject>Rats</subject><subject>Rats, Sprague-Dawley</subject><subject>Recombinant Proteins - metabolism</subject><subject>Reverse Transcriptase Polymerase Chain Reaction</subject><subject>Transcription, Genetic</subject><subject>Xenopus laevis</subject><issn>0022-3751</issn><issn>1469-7793</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1999</creationdate><recordtype>article</recordtype><recordid>eNpVkctu1DAUhi0EokPhFZBXsErwJbFzJISEKu6VYFEWrCyPc9J4lMSD7XQ6b0_ClKp4Y0v_5ej4I4RyVvLlvNmVvFJQaA2y5ABQKgl2W94-Ipt74THZMCZEIXXNz8izlHaMcckAnpIzzphSDVQb8uubj6LkFCcXWkw090j9dLCxpRFd9p3HSPch25T8PFLX22nCYbHQaDO1MWP0dqBpDCH3dJyTG5A6HIb0nDzp7JDwxd19Tn5-_HB18bm4_P7py8X7y6KXnEHhKl6LrqmtA6WBVw6ddjWrhBAW2ka3W1Cda2qsseVWCu6w40x1Sktta9fIc_Lu1LuftyO2Dqcc7WD20Y82Hk2w3vyvTL431-HGCKGAQ7UUvLoriOH3jCmb0ad1BTthmJNRoJgWwBbjy4eT7kf8-83F8PZkOPgBjw90s1IzO7PCMSscs1Izf6mZW3P19cfyXOKvT_HeX_cHH9Hs-2PyIQXnMR9NzWsj15D8A_Scmz0</recordid><startdate>19990315</startdate><enddate>19990315</enddate><creator>Bradley, Karri K.</creator><creator>Jaggar, Jonathan H.</creator><creator>Bonev, Adrian D.</creator><creator>Heppner, Thomas J.</creator><creator>Flynn, Elaine R.M.</creator><creator>Nelson, Mark T.</creator><creator>Horowitz, Burton</creator><general>The Physiological Society</general><general>Blackwell Science Ltd</general><general>Blackwell Science Inc</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>19990315</creationdate><title>Kir2.1 encodes the inward rectifier potassium channel in rat arterial smooth muscle cells</title><author>Bradley, Karri K. ; Jaggar, Jonathan H. ; Bonev, Adrian D. ; Heppner, Thomas J. ; Flynn, Elaine R.M. ; Nelson, Mark T. ; Horowitz, Burton</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-h3109-c4152f85ac967914cec7c504222a9d87db96fc85e5ed1a321cef106f6737a5c83</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1999</creationdate><topic>Animals</topic><topic>Barium - pharmacology</topic><topic>Basilar Artery - metabolism</topic><topic>Cesium - pharmacology</topic><topic>Cloning, Molecular</topic><topic>Coronary Vessels - metabolism</topic><topic>Membrane Potentials - drug effects</topic><topic>Mesenteric Arteries - metabolism</topic><topic>Muscle, Smooth, Vascular - metabolism</topic><topic>Oocytes - physiology</topic><topic>Original</topic><topic>Patch-Clamp Techniques</topic><topic>Potassium - pharmacology</topic><topic>Potassium Channels - drug effects</topic><topic>Potassium Channels - genetics</topic><topic>Potassium Channels - physiology</topic><topic>Potassium Channels, Inwardly Rectifying</topic><topic>Rats</topic><topic>Rats, Sprague-Dawley</topic><topic>Recombinant Proteins - metabolism</topic><topic>Reverse Transcriptase Polymerase Chain Reaction</topic><topic>Transcription, Genetic</topic><topic>Xenopus laevis</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Bradley, Karri K.</creatorcontrib><creatorcontrib>Jaggar, Jonathan H.</creatorcontrib><creatorcontrib>Bonev, Adrian D.</creatorcontrib><creatorcontrib>Heppner, Thomas J.</creatorcontrib><creatorcontrib>Flynn, Elaine R.M.</creatorcontrib><creatorcontrib>Nelson, Mark T.</creatorcontrib><creatorcontrib>Horowitz, Burton</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>The Journal of physiology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Bradley, Karri K.</au><au>Jaggar, Jonathan H.</au><au>Bonev, Adrian D.</au><au>Heppner, Thomas J.</au><au>Flynn, Elaine R.M.</au><au>Nelson, Mark T.</au><au>Horowitz, Burton</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Kir2.1 encodes the inward rectifier potassium channel in rat arterial smooth muscle cells</atitle><jtitle>The Journal of physiology</jtitle><addtitle>J Physiol</addtitle><date>1999-03-15</date><risdate>1999</risdate><volume>515</volume><issue>3</issue><spage>639</spage><epage>651</epage><pages>639-651</pages><issn>0022-3751</issn><eissn>1469-7793</eissn><abstract>The molecular nature of the strong inward rectifier K + channel in vascular smooth muscle was explored by using isolated cell RT-PCR, cDNA cloning and expression techniques.
RT-PCR of RNA from single smooth muscle cells of rat cerebral (basilar), coronary and mesenteric arteries revealed transcripts
for K ir 2.1. Transcripts for K ir 2.2 and K ir 2.3 were not found.
Quantitative PCR analysis revealed significant differences in transcript levels of K ir 2.1 between the different vascular preparations ( n = 3; P < 0.05). A two-fold difference was detected between K ir 2.1 mRNA and β-actin mRNA in coronary arteries when compared with relative levels measured in mesenteric and basilar preparations.
K ir 2.1 was cloned from rat mesenteric vascular smooth muscle cells and expressed in Xenopus oocytes. Currents were strongly inwardly rectifying and selective for K + .
The effect of extracellular Ba 2+ , Ca 2+ , Mg 2+ and Cs 2+ ions on cloned K ir 2.1 channels expressed in Xenopus oocytes was examined. Ba 2+ and Cs + block were steeply voltage dependent, whereas block by external Ca 2+ and Mg 2+ exhibited little voltage dependence. The apparent half-block constants and voltage dependences for Ba 2+ , Cs + , Ca 2+ and Mg 2+ were very similar for inward rectifier K + currents from native cells and cloned K ir 2.1 channels expressed in oocytes.
Molecular studies demonstrate that K ir 2.1 is the only member of the K ir 2 channel subfamily present in vascular arterial smooth muscle cells. Expression of cloned K ir 2.1 in Xenopus oocytes resulted in inward rectifier K + currents that strongly resemble those that are observed in native vascular arterial smooth muscle cells. We conclude that
K ir 2.1 encodes for inward rectifier K + channels in arterial smooth muscle.</abstract><cop>Oxford, UK</cop><pub>The Physiological Society</pub><pmid>10066894</pmid><doi>10.1111/j.1469-7793.1999.639ab.x</doi><tpages>13</tpages><oa>free_for_read</oa></addata></record> |
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source | Wiley-Blackwell Read & Publish Collection; PubMed Central |
subjects | Animals Barium - pharmacology Basilar Artery - metabolism Cesium - pharmacology Cloning, Molecular Coronary Vessels - metabolism Membrane Potentials - drug effects Mesenteric Arteries - metabolism Muscle, Smooth, Vascular - metabolism Oocytes - physiology Original Patch-Clamp Techniques Potassium - pharmacology Potassium Channels - drug effects Potassium Channels - genetics Potassium Channels - physiology Potassium Channels, Inwardly Rectifying Rats Rats, Sprague-Dawley Recombinant Proteins - metabolism Reverse Transcriptase Polymerase Chain Reaction Transcription, Genetic Xenopus laevis |
title | Kir2.1 encodes the inward rectifier potassium channel in rat arterial smooth muscle cells |
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