Sea Anemone Peptides with a Specific Blocking Activity against the Fast Inactivating Potassium Channel Kv3.4
Sea anemone venom is known to contain toxins that are active on voltage-sensitive Na + channels, as well as on delayed rectifier K + channels belonging to the Kv1 family. This report describes the properties of a new set of peptides from Anemonia sulcata that act as blockers of a specific member of...
Gespeichert in:
| Veröffentlicht in: | The Journal of biological chemistry 1998-03, Vol.273 (12), p.6744-6749 |
|---|---|
| Hauptverfasser: | , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 6749 |
|---|---|
| container_issue | 12 |
| container_start_page | 6744 |
| container_title | The Journal of biological chemistry |
| container_volume | 273 |
| creator | Diochot, Sylvie Schweitz, Hugues Béress, Lászlo Lazdunski, Michel |
| description | Sea anemone venom is known to contain toxins that are active on voltage-sensitive Na + channels, as well as on delayed rectifier K + channels belonging to the Kv1 family. This report describes the properties of a new set of peptides from Anemonia sulcata that act as blockers of a specific member of the Kv3 potassium channel family. These toxins, blood depressing substance (BDS)-I
and BDS-II, are 43 amino acids long and differ at only two positions. They share no sequence homologies with other K + channel toxins from sea anemones, such as AsKS, AsKC, ShK, or BgK. In COS-transfected cells, the Kv3.4 current was inhibited
in a reversible manner by BDS-I, with an IC 50 value of 47 n m . This inhibition is specific because BDS-I failed to block other K + channels in the Kv1, Kv2, Kv3, and Kv4 subfamilies. Inward rectifier K + channels are also insensitive to BDS-I. BDS-I and BDS-II share the same binding site on brain synaptic membranes, with K
0.5 values of 12 and 19 n m , respectively. We observed that BDS-I and BDS-II have some sequence homologies with other sea anemone Na + channels toxins, such as AsI, AsII, and AxI. However, they had a weak effect on tetrodotoxin-sensitive Na + channels in neuroblastoma cells and no effect on Na + channels in cardiac and skeletal muscle cells. BDS-I and BDS-II are the first specific blockers identified so far for the
rapidly inactivating Kv3.4 channel. |
| doi_str_mv | 10.1074/jbc.273.12.6744 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_16290046</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>16290046</sourcerecordid><originalsourceid>FETCH-LOGICAL-c392t-f8a8015c621ee91eab52935e960c6ddf5116a41d5ddaf53a440b5210621249143</originalsourceid><addsrcrecordid>eNpVkE1LJDEQhsOyorO6Z09CYGFv3abSSc_kOA66ygoKKngLNenq6Wh_jJ2M4r_fDDMIm0sF3qdeqIexUxA5iKk6f1m6XE6LHGReTpX6xiYgZkVWaHj-ziZCSMiM1LMj9iOEF5GeMnDIDo0WpZmqCWsfCPm8p27oid_TOvqKAv_wseHIH9bkfO0dv2gH9-r7FZ-76N99_OS4Qt-HyGND_ArT56bHbYZxi90PEUPwm44vGux7avnf9yJXJ-ygxjbQz_08Zk9Xl4-L6-z27s_NYn6bucLImNUznAnQrpRAZIBwqaUpNJlSuLKqag1QooJKVxXWukClRCJAJF6m81RxzH7vetfj8LahEG3ng6O2xZ6GTbBQSpNMlAk834FuHEIYqbbr0Xc4floQduvXJr82-bUg7dZv2jjbV2-WHVVf_F5oyn_t8savmg8_kl36wTXU_dfyD0UrgV0</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>16290046</pqid></control><display><type>article</type><title>Sea Anemone Peptides with a Specific Blocking Activity against the Fast Inactivating Potassium Channel Kv3.4</title><source>MEDLINE</source><source>EZB-FREE-00999 freely available EZB journals</source><source>Alma/SFX Local Collection</source><creator>Diochot, Sylvie ; Schweitz, Hugues ; Béress, Lászlo ; Lazdunski, Michel</creator><creatorcontrib>Diochot, Sylvie ; Schweitz, Hugues ; Béress, Lászlo ; Lazdunski, Michel</creatorcontrib><description>Sea anemone venom is known to contain toxins that are active on voltage-sensitive Na + channels, as well as on delayed rectifier K + channels belonging to the Kv1 family. This report describes the properties of a new set of peptides from Anemonia sulcata that act as blockers of a specific member of the Kv3 potassium channel family. These toxins, blood depressing substance (BDS)-I
and BDS-II, are 43 amino acids long and differ at only two positions. They share no sequence homologies with other K + channel toxins from sea anemones, such as AsKS, AsKC, ShK, or BgK. In COS-transfected cells, the Kv3.4 current was inhibited
in a reversible manner by BDS-I, with an IC 50 value of 47 n m . This inhibition is specific because BDS-I failed to block other K + channels in the Kv1, Kv2, Kv3, and Kv4 subfamilies. Inward rectifier K + channels are also insensitive to BDS-I. BDS-I and BDS-II share the same binding site on brain synaptic membranes, with K
0.5 values of 12 and 19 n m , respectively. We observed that BDS-I and BDS-II have some sequence homologies with other sea anemone Na + channels toxins, such as AsI, AsII, and AxI. However, they had a weak effect on tetrodotoxin-sensitive Na + channels in neuroblastoma cells and no effect on Na + channels in cardiac and skeletal muscle cells. BDS-I and BDS-II are the first specific blockers identified so far for the
rapidly inactivating Kv3.4 channel.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1074/jbc.273.12.6744</identifier><identifier>PMID: 9506974</identifier><language>eng</language><publisher>United States: American Society for Biochemistry and Molecular Biology</publisher><subject>Amino Acid Sequence ; Anemonia sulcata ; Animals ; Cnidarian Venoms - chemistry ; Cnidarian Venoms - isolation & purification ; Cnidarian Venoms - pharmacology ; COS Cells ; Iodine Radioisotopes ; Ion Channel Gating - drug effects ; Marine ; Molecular Sequence Data ; Potassium Channel Blockers ; Rats ; Sea Anemones ; Sequence Homology, Amino Acid ; Xenopus laevis</subject><ispartof>The Journal of biological chemistry, 1998-03, Vol.273 (12), p.6744-6749</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c392t-f8a8015c621ee91eab52935e960c6ddf5116a41d5ddaf53a440b5210621249143</citedby><cites>FETCH-LOGICAL-c392t-f8a8015c621ee91eab52935e960c6ddf5116a41d5ddaf53a440b5210621249143</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>315,781,785,27928,27929</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9506974$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Diochot, Sylvie</creatorcontrib><creatorcontrib>Schweitz, Hugues</creatorcontrib><creatorcontrib>Béress, Lászlo</creatorcontrib><creatorcontrib>Lazdunski, Michel</creatorcontrib><title>Sea Anemone Peptides with a Specific Blocking Activity against the Fast Inactivating Potassium Channel Kv3.4</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>Sea anemone venom is known to contain toxins that are active on voltage-sensitive Na + channels, as well as on delayed rectifier K + channels belonging to the Kv1 family. This report describes the properties of a new set of peptides from Anemonia sulcata that act as blockers of a specific member of the Kv3 potassium channel family. These toxins, blood depressing substance (BDS)-I
and BDS-II, are 43 amino acids long and differ at only two positions. They share no sequence homologies with other K + channel toxins from sea anemones, such as AsKS, AsKC, ShK, or BgK. In COS-transfected cells, the Kv3.4 current was inhibited
in a reversible manner by BDS-I, with an IC 50 value of 47 n m . This inhibition is specific because BDS-I failed to block other K + channels in the Kv1, Kv2, Kv3, and Kv4 subfamilies. Inward rectifier K + channels are also insensitive to BDS-I. BDS-I and BDS-II share the same binding site on brain synaptic membranes, with K
0.5 values of 12 and 19 n m , respectively. We observed that BDS-I and BDS-II have some sequence homologies with other sea anemone Na + channels toxins, such as AsI, AsII, and AxI. However, they had a weak effect on tetrodotoxin-sensitive Na + channels in neuroblastoma cells and no effect on Na + channels in cardiac and skeletal muscle cells. BDS-I and BDS-II are the first specific blockers identified so far for the
rapidly inactivating Kv3.4 channel.</description><subject>Amino Acid Sequence</subject><subject>Anemonia sulcata</subject><subject>Animals</subject><subject>Cnidarian Venoms - chemistry</subject><subject>Cnidarian Venoms - isolation & purification</subject><subject>Cnidarian Venoms - pharmacology</subject><subject>COS Cells</subject><subject>Iodine Radioisotopes</subject><subject>Ion Channel Gating - drug effects</subject><subject>Marine</subject><subject>Molecular Sequence Data</subject><subject>Potassium Channel Blockers</subject><subject>Rats</subject><subject>Sea Anemones</subject><subject>Sequence Homology, Amino Acid</subject><subject>Xenopus laevis</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1998</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpVkE1LJDEQhsOyorO6Z09CYGFv3abSSc_kOA66ygoKKngLNenq6Wh_jJ2M4r_fDDMIm0sF3qdeqIexUxA5iKk6f1m6XE6LHGReTpX6xiYgZkVWaHj-ziZCSMiM1LMj9iOEF5GeMnDIDo0WpZmqCWsfCPm8p27oid_TOvqKAv_wseHIH9bkfO0dv2gH9-r7FZ-76N99_OS4Qt-HyGND_ArT56bHbYZxi90PEUPwm44vGux7avnf9yJXJ-ygxjbQz_08Zk9Xl4-L6-z27s_NYn6bucLImNUznAnQrpRAZIBwqaUpNJlSuLKqag1QooJKVxXWukClRCJAJF6m81RxzH7vetfj8LahEG3ng6O2xZ6GTbBQSpNMlAk834FuHEIYqbbr0Xc4floQduvXJr82-bUg7dZv2jjbV2-WHVVf_F5oyn_t8savmg8_kl36wTXU_dfyD0UrgV0</recordid><startdate>19980320</startdate><enddate>19980320</enddate><creator>Diochot, Sylvie</creator><creator>Schweitz, Hugues</creator><creator>Béress, Lászlo</creator><creator>Lazdunski, Michel</creator><general>American Society for Biochemistry and Molecular Biology</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>7U7</scope><scope>8FD</scope><scope>C1K</scope><scope>F1W</scope><scope>FR3</scope><scope>H97</scope><scope>H99</scope><scope>L.F</scope><scope>L.G</scope><scope>P64</scope></search><sort><creationdate>19980320</creationdate><title>Sea Anemone Peptides with a Specific Blocking Activity against the Fast Inactivating Potassium Channel Kv3.4</title><author>Diochot, Sylvie ; Schweitz, Hugues ; Béress, Lászlo ; Lazdunski, Michel</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c392t-f8a8015c621ee91eab52935e960c6ddf5116a41d5ddaf53a440b5210621249143</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1998</creationdate><topic>Amino Acid Sequence</topic><topic>Anemonia sulcata</topic><topic>Animals</topic><topic>Cnidarian Venoms - chemistry</topic><topic>Cnidarian Venoms - isolation & purification</topic><topic>Cnidarian Venoms - pharmacology</topic><topic>COS Cells</topic><topic>Iodine Radioisotopes</topic><topic>Ion Channel Gating - drug effects</topic><topic>Marine</topic><topic>Molecular Sequence Data</topic><topic>Potassium Channel Blockers</topic><topic>Rats</topic><topic>Sea Anemones</topic><topic>Sequence Homology, Amino Acid</topic><topic>Xenopus laevis</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Diochot, Sylvie</creatorcontrib><creatorcontrib>Schweitz, Hugues</creatorcontrib><creatorcontrib>Béress, Lászlo</creatorcontrib><creatorcontrib>Lazdunski, Michel</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Toxicology Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ASFA: Aquatic Sciences and Fisheries Abstracts</collection><collection>Engineering Research Database</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) 3: Aquatic Pollution & Environmental Quality</collection><collection>ASFA: Marine Biotechnology Abstracts</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) Marine Biotechnology Abstracts</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) Professional</collection><collection>Biotechnology and BioEngineering Abstracts</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Diochot, Sylvie</au><au>Schweitz, Hugues</au><au>Béress, Lászlo</au><au>Lazdunski, Michel</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Sea Anemone Peptides with a Specific Blocking Activity against the Fast Inactivating Potassium Channel Kv3.4</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1998-03-20</date><risdate>1998</risdate><volume>273</volume><issue>12</issue><spage>6744</spage><epage>6749</epage><pages>6744-6749</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>Sea anemone venom is known to contain toxins that are active on voltage-sensitive Na + channels, as well as on delayed rectifier K + channels belonging to the Kv1 family. This report describes the properties of a new set of peptides from Anemonia sulcata that act as blockers of a specific member of the Kv3 potassium channel family. These toxins, blood depressing substance (BDS)-I
and BDS-II, are 43 amino acids long and differ at only two positions. They share no sequence homologies with other K + channel toxins from sea anemones, such as AsKS, AsKC, ShK, or BgK. In COS-transfected cells, the Kv3.4 current was inhibited
in a reversible manner by BDS-I, with an IC 50 value of 47 n m . This inhibition is specific because BDS-I failed to block other K + channels in the Kv1, Kv2, Kv3, and Kv4 subfamilies. Inward rectifier K + channels are also insensitive to BDS-I. BDS-I and BDS-II share the same binding site on brain synaptic membranes, with K
0.5 values of 12 and 19 n m , respectively. We observed that BDS-I and BDS-II have some sequence homologies with other sea anemone Na + channels toxins, such as AsI, AsII, and AxI. However, they had a weak effect on tetrodotoxin-sensitive Na + channels in neuroblastoma cells and no effect on Na + channels in cardiac and skeletal muscle cells. BDS-I and BDS-II are the first specific blockers identified so far for the
rapidly inactivating Kv3.4 channel.</abstract><cop>United States</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>9506974</pmid><doi>10.1074/jbc.273.12.6744</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0021-9258 |
| ispartof | The Journal of biological chemistry, 1998-03, Vol.273 (12), p.6744-6749 |
| issn | 0021-9258 1083-351X |
| language | eng |
| recordid | cdi_proquest_miscellaneous_16290046 |
| source | MEDLINE; EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection |
| subjects | Amino Acid Sequence Anemonia sulcata Animals Cnidarian Venoms - chemistry Cnidarian Venoms - isolation & purification Cnidarian Venoms - pharmacology COS Cells Iodine Radioisotopes Ion Channel Gating - drug effects Marine Molecular Sequence Data Potassium Channel Blockers Rats Sea Anemones Sequence Homology, Amino Acid Xenopus laevis |
| title | Sea Anemone Peptides with a Specific Blocking Activity against the Fast Inactivating Potassium Channel Kv3.4 |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-17T04%3A46%3A41IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Sea%20Anemone%20Peptides%20with%20a%20Specific%20Blocking%20Activity%20against%20the%20Fast%20Inactivating%20Potassium%20Channel%20Kv3.4&rft.jtitle=The%20Journal%20of%20biological%20chemistry&rft.au=Diochot,%20Sylvie&rft.date=1998-03-20&rft.volume=273&rft.issue=12&rft.spage=6744&rft.epage=6749&rft.pages=6744-6749&rft.issn=0021-9258&rft.eissn=1083-351X&rft_id=info:doi/10.1074/jbc.273.12.6744&rft_dat=%3Cproquest_cross%3E16290046%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=16290046&rft_id=info:pmid/9506974&rfr_iscdi=true |