Antibodies specific for distinct Kv subunits unveil a heterooligomeric basis for subtypes of alpha-dendrotoxin-sensitive K+ channels in bovine brain
The authentic subunit compositions of neuronal K+ channels purified from bovine brain were analyzed using a monoclonal antibody (mAb 5), reactive exclusively with the Kv1.2 subunit of the latter and polyclonal antibodies specific for fusion proteins containing C-terminal regions of four mammalian Kv...
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Veröffentlicht in: | Biochemistry (Easton) 1994-02, Vol.33 (7), p.1617-1623 |
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creator | Scott, V E Muniz, Z M Sewing, S Lichtinghagen, R Parcej, D N Pongs, O Dolly, J O |
description | The authentic subunit compositions of neuronal K+ channels purified from bovine brain were analyzed using a monoclonal antibody (mAb 5), reactive exclusively with the Kv1.2 subunit of the latter and polyclonal antibodies specific for fusion proteins containing C-terminal regions of four mammalian Kv proteins. Western blotting of the K+ channels isolated from several brain regions, employing the selective blocker alpha-dendrotoxin (alpha-DTX), revealed the presence in each of four different Kvs. Variable amounts of Kv1.1 and 1.4 subunits were observed in the K+ channels purified from cerebellum, corpus striatum, hippocampus, cerebral cortex, and brain stem; on the other hand, contents of Kv1.6 and 1.2 subunits appeared uniform throughout. Each Kv-specific antibody precipitated a different proportion (anti-Kv1.2 > 1.1 >> 1.6 > 1.4) of the channels detectable with radioiodinated alpha-DTX in every brain region, consistent with a widespread distribution of these oligomeric subtypes. Such heterooligomeric combinations were further documented by the lack of additivity upon their precipitation with a mixture of antibodies to Kv1.1 and Kv1.2; moreover, cross-blotting of the multimers precipitated by mAb 5 showed that they contain all four Kv proteins. Collectively, these findings demonstrate that subtypes of alpha-DTX-susceptible K+ channels are prevalent throughout mammalian brain which are composed of different Kv proteins assembled in complexes, shown previously to also contain auxiliary beta-subunits [Parcej, D. N., Scott, V. E. S., & Dolly, J.O. (1992) Biochemistry 31, 11084-11088]. |
doi_str_mv | 10.1021/bi00173a001 |
format | Article |
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Western blotting of the K+ channels isolated from several brain regions, employing the selective blocker alpha-dendrotoxin (alpha-DTX), revealed the presence in each of four different Kvs. Variable amounts of Kv1.1 and 1.4 subunits were observed in the K+ channels purified from cerebellum, corpus striatum, hippocampus, cerebral cortex, and brain stem; on the other hand, contents of Kv1.6 and 1.2 subunits appeared uniform throughout. Each Kv-specific antibody precipitated a different proportion (anti-Kv1.2 > 1.1 >> 1.6 > 1.4) of the channels detectable with radioiodinated alpha-DTX in every brain region, consistent with a widespread distribution of these oligomeric subtypes. Such heterooligomeric combinations were further documented by the lack of additivity upon their precipitation with a mixture of antibodies to Kv1.1 and Kv1.2; moreover, cross-blotting of the multimers precipitated by mAb 5 showed that they contain all four Kv proteins. Collectively, these findings demonstrate that subtypes of alpha-DTX-susceptible K+ channels are prevalent throughout mammalian brain which are composed of different Kv proteins assembled in complexes, shown previously to also contain auxiliary beta-subunits [Parcej, D. N., Scott, V. E. S., & Dolly, J.O. (1992) Biochemistry 31, 11084-11088].</description><identifier>ISSN: 0006-2960</identifier><identifier>DOI: 10.1021/bi00173a001</identifier><identifier>PMID: 8110763</identifier><language>eng</language><publisher>United States</publisher><subject>Animals ; Antibodies, Monoclonal ; Base Sequence ; Blotting, Western ; Brain Chemistry ; Brain Stem - chemistry ; Cattle ; Cerebellum - chemistry ; Cerebral Cortex - chemistry ; Corpus Striatum - chemistry ; DNA, Complementary ; Elapid Venoms - pharmacology ; Hippocampus - chemistry ; Immunosorbent Techniques ; Macromolecular Substances ; Molecular Sequence Data ; Potassium Channels - chemistry ; Potassium Channels - immunology ; Recombinant Fusion Proteins - chemistry ; Recombinant Fusion Proteins - immunology ; Tissue Distribution</subject><ispartof>Biochemistry (Easton), 1994-02, Vol.33 (7), p.1617-1623</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27915,27916</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8110763$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Scott, V E</creatorcontrib><creatorcontrib>Muniz, Z M</creatorcontrib><creatorcontrib>Sewing, S</creatorcontrib><creatorcontrib>Lichtinghagen, R</creatorcontrib><creatorcontrib>Parcej, D N</creatorcontrib><creatorcontrib>Pongs, O</creatorcontrib><creatorcontrib>Dolly, J O</creatorcontrib><title>Antibodies specific for distinct Kv subunits unveil a heterooligomeric basis for subtypes of alpha-dendrotoxin-sensitive K+ channels in bovine brain</title><title>Biochemistry (Easton)</title><addtitle>Biochemistry</addtitle><description>The authentic subunit compositions of neuronal K+ channels purified from bovine brain were analyzed using a monoclonal antibody (mAb 5), reactive exclusively with the Kv1.2 subunit of the latter and polyclonal antibodies specific for fusion proteins containing C-terminal regions of four mammalian Kv proteins. Western blotting of the K+ channels isolated from several brain regions, employing the selective blocker alpha-dendrotoxin (alpha-DTX), revealed the presence in each of four different Kvs. Variable amounts of Kv1.1 and 1.4 subunits were observed in the K+ channels purified from cerebellum, corpus striatum, hippocampus, cerebral cortex, and brain stem; on the other hand, contents of Kv1.6 and 1.2 subunits appeared uniform throughout. Each Kv-specific antibody precipitated a different proportion (anti-Kv1.2 > 1.1 >> 1.6 > 1.4) of the channels detectable with radioiodinated alpha-DTX in every brain region, consistent with a widespread distribution of these oligomeric subtypes. Such heterooligomeric combinations were further documented by the lack of additivity upon their precipitation with a mixture of antibodies to Kv1.1 and Kv1.2; moreover, cross-blotting of the multimers precipitated by mAb 5 showed that they contain all four Kv proteins. Collectively, these findings demonstrate that subtypes of alpha-DTX-susceptible K+ channels are prevalent throughout mammalian brain which are composed of different Kv proteins assembled in complexes, shown previously to also contain auxiliary beta-subunits [Parcej, D. N., Scott, V. E. S., & Dolly, J.O. (1992) Biochemistry 31, 11084-11088].</description><subject>Animals</subject><subject>Antibodies, Monoclonal</subject><subject>Base Sequence</subject><subject>Blotting, Western</subject><subject>Brain Chemistry</subject><subject>Brain Stem - chemistry</subject><subject>Cattle</subject><subject>Cerebellum - chemistry</subject><subject>Cerebral Cortex - chemistry</subject><subject>Corpus Striatum - chemistry</subject><subject>DNA, Complementary</subject><subject>Elapid Venoms - pharmacology</subject><subject>Hippocampus - chemistry</subject><subject>Immunosorbent Techniques</subject><subject>Macromolecular Substances</subject><subject>Molecular Sequence Data</subject><subject>Potassium Channels - chemistry</subject><subject>Potassium Channels - immunology</subject><subject>Recombinant Fusion Proteins - chemistry</subject><subject>Recombinant Fusion Proteins - immunology</subject><subject>Tissue Distribution</subject><issn>0006-2960</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1994</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNotkD1PwzAYhD2ASilMzEieWFDAdlo7GSvEl1qJBebIjt_QFyV2sJ2I_g9-MAG63Omk5244Qi44u-FM8FuDjHGV60mPyJwxJjNRSnZCTmP8mOKSqeWMzArOmZL5nHyvXULjLUKksYcaG6xp4wO1GBO6OtHNSONgBocp0sGNgC3VdAcJgvctvvsOwlQxOmL8K05w2vfTnG-obvudziw4G3zyX-iyCC5iwhHo5prWO-0ctJGio8aP6ICaoNGdkeNGtxHOD74gbw_3r3dP2fbl8fluvc16wWTKlBFWWGYVl7lasYLXVpe5MdAopkEWpTV1IYEJY_Ja2NIKJorCagt21ZS6yBfk6n-3D_5zgJiqDmMNbasd-CFW00NyWapf8PIADqYDW_UBOx321eHG_AdQPnZr</recordid><startdate>19940222</startdate><enddate>19940222</enddate><creator>Scott, V E</creator><creator>Muniz, Z M</creator><creator>Sewing, S</creator><creator>Lichtinghagen, R</creator><creator>Parcej, D N</creator><creator>Pongs, O</creator><creator>Dolly, J O</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>19940222</creationdate><title>Antibodies specific for distinct Kv subunits unveil a heterooligomeric basis for subtypes of alpha-dendrotoxin-sensitive K+ channels in bovine brain</title><author>Scott, V E ; Muniz, Z M ; Sewing, S ; Lichtinghagen, R ; Parcej, D N ; Pongs, O ; Dolly, J O</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-p206t-7b2d2d0d716375081cda93bbef70ae689dbc86e02bb3c2d9d20288daded5f9a83</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1994</creationdate><topic>Animals</topic><topic>Antibodies, Monoclonal</topic><topic>Base Sequence</topic><topic>Blotting, Western</topic><topic>Brain Chemistry</topic><topic>Brain Stem - chemistry</topic><topic>Cattle</topic><topic>Cerebellum - chemistry</topic><topic>Cerebral Cortex - chemistry</topic><topic>Corpus Striatum - chemistry</topic><topic>DNA, Complementary</topic><topic>Elapid Venoms - pharmacology</topic><topic>Hippocampus - chemistry</topic><topic>Immunosorbent Techniques</topic><topic>Macromolecular Substances</topic><topic>Molecular Sequence Data</topic><topic>Potassium Channels - chemistry</topic><topic>Potassium Channels - immunology</topic><topic>Recombinant Fusion Proteins - chemistry</topic><topic>Recombinant Fusion Proteins - immunology</topic><topic>Tissue Distribution</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Scott, V E</creatorcontrib><creatorcontrib>Muniz, Z M</creatorcontrib><creatorcontrib>Sewing, S</creatorcontrib><creatorcontrib>Lichtinghagen, R</creatorcontrib><creatorcontrib>Parcej, D N</creatorcontrib><creatorcontrib>Pongs, O</creatorcontrib><creatorcontrib>Dolly, J O</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>Biochemistry (Easton)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Scott, V E</au><au>Muniz, Z M</au><au>Sewing, S</au><au>Lichtinghagen, R</au><au>Parcej, D N</au><au>Pongs, O</au><au>Dolly, J O</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Antibodies specific for distinct Kv subunits unveil a heterooligomeric basis for subtypes of alpha-dendrotoxin-sensitive K+ channels in bovine brain</atitle><jtitle>Biochemistry (Easton)</jtitle><addtitle>Biochemistry</addtitle><date>1994-02-22</date><risdate>1994</risdate><volume>33</volume><issue>7</issue><spage>1617</spage><epage>1623</epage><pages>1617-1623</pages><issn>0006-2960</issn><abstract>The authentic subunit compositions of neuronal K+ channels purified from bovine brain were analyzed using a monoclonal antibody (mAb 5), reactive exclusively with the Kv1.2 subunit of the latter and polyclonal antibodies specific for fusion proteins containing C-terminal regions of four mammalian Kv proteins. Western blotting of the K+ channels isolated from several brain regions, employing the selective blocker alpha-dendrotoxin (alpha-DTX), revealed the presence in each of four different Kvs. Variable amounts of Kv1.1 and 1.4 subunits were observed in the K+ channels purified from cerebellum, corpus striatum, hippocampus, cerebral cortex, and brain stem; on the other hand, contents of Kv1.6 and 1.2 subunits appeared uniform throughout. Each Kv-specific antibody precipitated a different proportion (anti-Kv1.2 > 1.1 >> 1.6 > 1.4) of the channels detectable with radioiodinated alpha-DTX in every brain region, consistent with a widespread distribution of these oligomeric subtypes. Such heterooligomeric combinations were further documented by the lack of additivity upon their precipitation with a mixture of antibodies to Kv1.1 and Kv1.2; moreover, cross-blotting of the multimers precipitated by mAb 5 showed that they contain all four Kv proteins. Collectively, these findings demonstrate that subtypes of alpha-DTX-susceptible K+ channels are prevalent throughout mammalian brain which are composed of different Kv proteins assembled in complexes, shown previously to also contain auxiliary beta-subunits [Parcej, D. N., Scott, V. E. S., & Dolly, J.O. (1992) Biochemistry 31, 11084-11088].</abstract><cop>United States</cop><pmid>8110763</pmid><doi>10.1021/bi00173a001</doi><tpages>7</tpages></addata></record> |
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subjects | Animals Antibodies, Monoclonal Base Sequence Blotting, Western Brain Chemistry Brain Stem - chemistry Cattle Cerebellum - chemistry Cerebral Cortex - chemistry Corpus Striatum - chemistry DNA, Complementary Elapid Venoms - pharmacology Hippocampus - chemistry Immunosorbent Techniques Macromolecular Substances Molecular Sequence Data Potassium Channels - chemistry Potassium Channels - immunology Recombinant Fusion Proteins - chemistry Recombinant Fusion Proteins - immunology Tissue Distribution |
title | Antibodies specific for distinct Kv subunits unveil a heterooligomeric basis for subtypes of alpha-dendrotoxin-sensitive K+ channels in bovine brain |
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