Mechanism of charybdotoxin block of a voltage-gated K+ channel
Charybdotoxin block of a Shaker K+ channel was studied in Xenopus oocyte macropatches. Toxin on rate increases linearly with toxin concentration in an ionic strength-dependent fashion and is competitively diminished by tetraethylammonium. On rate is insensitive to transmembrane voltage and to K+ on...
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| Veröffentlicht in: | Biophysical journal 1993-10, Vol.65 (4), p.1613-1619 |
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| creator | Goldstein, S.A. Miller, C. |
| description | Charybdotoxin block of a Shaker K+ channel was studied in Xenopus oocyte macropatches. Toxin on rate increases linearly with toxin concentration in an ionic strength-dependent fashion and is competitively diminished by tetraethylammonium. On rate is insensitive to transmembrane voltage and to K+ on the opposite side of the membrane. Conversely, toxin off rate is insensitive to toxin concentration, ionic strength, and added tetraethylammonium but is enhanced by membrane depolarization or K+ (or Na+) in the trans solution. Charge neutralization of charybdotoxin Lys27, however, renders off rate voltage insensitive. Our results argue that block of voltage-gated K+ channels results from the binding of one toxin molecule, so that Lys27 enters the pore and interacts with K+ (or Na+) in the ion conduction pathway. |
| doi_str_mv | 10.1016/S0006-3495(93)81200-1 |
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Toxin on rate increases linearly with toxin concentration in an ionic strength-dependent fashion and is competitively diminished by tetraethylammonium. On rate is insensitive to transmembrane voltage and to K+ on the opposite side of the membrane. Conversely, toxin off rate is insensitive to toxin concentration, ionic strength, and added tetraethylammonium but is enhanced by membrane depolarization or K+ (or Na+) in the trans solution. Charge neutralization of charybdotoxin Lys27, however, renders off rate voltage insensitive. Our results argue that block of voltage-gated K+ channels results from the binding of one toxin molecule, so that Lys27 enters the pore and interacts with K+ (or Na+) in the ion conduction pathway.</description><identifier>ISSN: 0006-3495</identifier><identifier>EISSN: 1542-0086</identifier><identifier>DOI: 10.1016/S0006-3495(93)81200-1</identifier><identifier>PMID: 7506068</identifier><identifier>CODEN: BIOJAU</identifier><language>eng</language><publisher>Bethesda, MD: Elsevier Inc</publisher><subject>Animal poisons toxicology. Antivenoms ; Animals ; Binding, Competitive ; Biological and medical sciences ; Biophysical Phenomena ; Biophysics ; Charybdotoxin ; Drosophila ; Female ; Ion Channel Gating ; Kinetics ; Medical sciences ; Membrane Potentials ; Mutation ; Oocytes - drug effects ; Oocytes - metabolism ; Peptides - antagonists & inhibitors ; Peptides - genetics ; Peptides - metabolism ; Potassium Channel Blockers ; Potassium Channels - drug effects ; Potassium Channels - metabolism ; Recombinant Proteins - genetics ; Recombinant Proteins - pharmacology ; Scorpion Venoms - genetics ; Scorpion Venoms - pharmacology ; Shaker Superfamily of Potassium Channels ; Toxicology ; Xenopus</subject><ispartof>Biophysical journal, 1993-10, Vol.65 (4), p.1613-1619</ispartof><rights>1993 The Biophysical Society</rights><rights>1994 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c557t-e6d9e020c24a24923c7bffe477d0cd310e8259b4b6aae7220559128f52a5a0743</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/PMC1225887/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://dx.doi.org/10.1016/S0006-3495(93)81200-1$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>230,314,727,780,784,885,3550,27924,27925,45995,53791,53793</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=4105815$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/7506068$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Goldstein, S.A.</creatorcontrib><creatorcontrib>Miller, C.</creatorcontrib><title>Mechanism of charybdotoxin block of a voltage-gated K+ channel</title><title>Biophysical journal</title><addtitle>Biophys J</addtitle><description>Charybdotoxin block of a Shaker K+ channel was studied in Xenopus oocyte macropatches. Toxin on rate increases linearly with toxin concentration in an ionic strength-dependent fashion and is competitively diminished by tetraethylammonium. On rate is insensitive to transmembrane voltage and to K+ on the opposite side of the membrane. Conversely, toxin off rate is insensitive to toxin concentration, ionic strength, and added tetraethylammonium but is enhanced by membrane depolarization or K+ (or Na+) in the trans solution. Charge neutralization of charybdotoxin Lys27, however, renders off rate voltage insensitive. Our results argue that block of voltage-gated K+ channels results from the binding of one toxin molecule, so that Lys27 enters the pore and interacts with K+ (or Na+) in the ion conduction pathway.</description><subject>Animal poisons toxicology. Antivenoms</subject><subject>Animals</subject><subject>Binding, Competitive</subject><subject>Biological and medical sciences</subject><subject>Biophysical Phenomena</subject><subject>Biophysics</subject><subject>Charybdotoxin</subject><subject>Drosophila</subject><subject>Female</subject><subject>Ion Channel Gating</subject><subject>Kinetics</subject><subject>Medical sciences</subject><subject>Membrane Potentials</subject><subject>Mutation</subject><subject>Oocytes - drug effects</subject><subject>Oocytes - metabolism</subject><subject>Peptides - antagonists & inhibitors</subject><subject>Peptides - genetics</subject><subject>Peptides - metabolism</subject><subject>Potassium Channel Blockers</subject><subject>Potassium Channels - drug effects</subject><subject>Potassium Channels - metabolism</subject><subject>Recombinant Proteins - genetics</subject><subject>Recombinant Proteins - pharmacology</subject><subject>Scorpion Venoms - genetics</subject><subject>Scorpion Venoms - pharmacology</subject><subject>Shaker Superfamily of Potassium Channels</subject><subject>Toxicology</subject><subject>Xenopus</subject><issn>0006-3495</issn><issn>1542-0086</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1993</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkMlOwzAQhi0EKqXwCJVy4ABCgbFjZ7mAUMUmijgAZ8txJq0htas4VPD2JG0VwYnTWPMvHn2EjCmcU6DxxQsAxGHEM3GSRacpZQAh3SFDKjgLAdJ4lwx7yz458P4dgDIBdEAGiYAY4nRILp9Qz5U1fhG4Mmif9XdeuMZ9GRvkldMf3VoFK1c1aobhTDVYBI9nndNarA7JXqkqj0fbOSJvtzevk_tw-nz3MLmehlqIpAkxLjIEBppxxXjGIp3kZYk8SQrQRUQBUyaynOexUpgwBkJklKWlYEooSHg0Ipeb3uVnvsBCo21qVcllbRbtxdIpI_8q1szlzK0kZUykadIWiE2Brp33NZZ9loLseMo1T9nBklkk1zwlbXPj3x_3qS3AVj_e6sprVZW1str43sYpiJSK1na1sWELaWWwll4btBoLU6NuZOHMP4f8AO0zkXM</recordid><startdate>19931001</startdate><enddate>19931001</enddate><creator>Goldstein, S.A.</creator><creator>Miller, C.</creator><general>Elsevier Inc</general><general>Biophysical Society</general><scope>6I.</scope><scope>AAFTH</scope><scope>IQODW</scope><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>5PM</scope></search><sort><creationdate>19931001</creationdate><title>Mechanism of charybdotoxin block of a voltage-gated K+ channel</title><author>Goldstein, S.A. ; Miller, C.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c557t-e6d9e020c24a24923c7bffe477d0cd310e8259b4b6aae7220559128f52a5a0743</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1993</creationdate><topic>Animal poisons toxicology. Antivenoms</topic><topic>Animals</topic><topic>Binding, Competitive</topic><topic>Biological and medical sciences</topic><topic>Biophysical Phenomena</topic><topic>Biophysics</topic><topic>Charybdotoxin</topic><topic>Drosophila</topic><topic>Female</topic><topic>Ion Channel Gating</topic><topic>Kinetics</topic><topic>Medical sciences</topic><topic>Membrane Potentials</topic><topic>Mutation</topic><topic>Oocytes - drug effects</topic><topic>Oocytes - metabolism</topic><topic>Peptides - antagonists & inhibitors</topic><topic>Peptides - genetics</topic><topic>Peptides - metabolism</topic><topic>Potassium Channel Blockers</topic><topic>Potassium Channels - drug effects</topic><topic>Potassium Channels - metabolism</topic><topic>Recombinant Proteins - genetics</topic><topic>Recombinant Proteins - pharmacology</topic><topic>Scorpion Venoms - genetics</topic><topic>Scorpion Venoms - pharmacology</topic><topic>Shaker Superfamily of Potassium Channels</topic><topic>Toxicology</topic><topic>Xenopus</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Goldstein, S.A.</creatorcontrib><creatorcontrib>Miller, C.</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Biophysical journal</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Goldstein, S.A.</au><au>Miller, C.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Mechanism of charybdotoxin block of a voltage-gated K+ channel</atitle><jtitle>Biophysical journal</jtitle><addtitle>Biophys J</addtitle><date>1993-10-01</date><risdate>1993</risdate><volume>65</volume><issue>4</issue><spage>1613</spage><epage>1619</epage><pages>1613-1619</pages><issn>0006-3495</issn><eissn>1542-0086</eissn><coden>BIOJAU</coden><abstract>Charybdotoxin block of a Shaker K+ channel was studied in Xenopus oocyte macropatches. Toxin on rate increases linearly with toxin concentration in an ionic strength-dependent fashion and is competitively diminished by tetraethylammonium. On rate is insensitive to transmembrane voltage and to K+ on the opposite side of the membrane. Conversely, toxin off rate is insensitive to toxin concentration, ionic strength, and added tetraethylammonium but is enhanced by membrane depolarization or K+ (or Na+) in the trans solution. Charge neutralization of charybdotoxin Lys27, however, renders off rate voltage insensitive. Our results argue that block of voltage-gated K+ channels results from the binding of one toxin molecule, so that Lys27 enters the pore and interacts with K+ (or Na+) in the ion conduction pathway.</abstract><cop>Bethesda, MD</cop><pub>Elsevier Inc</pub><pmid>7506068</pmid><doi>10.1016/S0006-3495(93)81200-1</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
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| source | MEDLINE; Cell Press Free Archives; Access via ScienceDirect (Elsevier); EZB-FREE-00999 freely available EZB journals; PubMed Central |
| subjects | Animal poisons toxicology. Antivenoms Animals Binding, Competitive Biological and medical sciences Biophysical Phenomena Biophysics Charybdotoxin Drosophila Female Ion Channel Gating Kinetics Medical sciences Membrane Potentials Mutation Oocytes - drug effects Oocytes - metabolism Peptides - antagonists & inhibitors Peptides - genetics Peptides - metabolism Potassium Channel Blockers Potassium Channels - drug effects Potassium Channels - metabolism Recombinant Proteins - genetics Recombinant Proteins - pharmacology Scorpion Venoms - genetics Scorpion Venoms - pharmacology Shaker Superfamily of Potassium Channels Toxicology Xenopus |
| title | Mechanism of charybdotoxin block of a voltage-gated K+ channel |
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