{"refrec":{"BRefID":227398,"RR":"<b>Billen, B.; Debaveye, S.; Béress, L.; Garateixand, A.; Tytgat, J.</b> (2010). Phyla- and subtype-selectivity of CgNa, a Na<sup>+</sup> channel toxin from the venom of the Giant Caribbean Sea Anemone <i>Condylactis gigantea</i>. <i>Front. Pharmacol. 1</i>: 133. <a href=\"http://dx.doi.org/10.3389/fphar.2010.00133\" target=\"_blank\">http://dx.doi.org/10.3389/fphar.2010.00133</a>","BEntID":219119,"PublicFlag":1,"CheckedFlag":1,"wosflag":1,"vabbflag":1,"RefStringPartII":". <i>Front. Pharmacol. 1</i>: 133. <a href=\"http://dx.doi.org/10.3389/fphar.2010.00133\" target=\"_blank\">http://dx.doi.org/10.3389/fphar.2010.00133</a>","DocTypID":8,"DocType":"Journal article","MarineFlag":1,"FreshFlag":0,"BrackishFlag":0,"TerrestrialFlag":0,"Authorstring":"Billen, B.; Debaveye, S.; Béress, L.; Garateixand, A.; Tytgat, J.","OrigTitleTranslFlag":0,"Authorstringtrunc":"Billen, B. <i>et al.</i>","Englishabstract":"Because of their prominent role in electro-excitability, voltage-gated sodium (Na<sub>V</sub>) channels have become the foremost important target of animal toxins. These toxins have developed the ability to discriminate between closely related Na<sub>V</sub> subtypes, making them powerful tools to study Na<sub>V</sub> channel function and structure. CgNa is a 47-amino acid residue type I toxin isolated from the venom of the Giant Caribbean Sea Anemone <i>Condylactis gigantean</i>. Previous studies showed that this toxin slows the fast inactivation of tetrodotoxin-sensitive Na<sub>V</sub> currents in rat dorsal root ganglion neurons. To illuminate the underlying NaV subtype-selectivity pattern, we have assayed the effects of CgNa on a broad range of mammalian isoforms (Na<sub>V</sub>1.2– Na<sub>V</sub>1.8) expressed in <i>Xenopus</i> oocytes. This study demonstrates that CgNa selectively slows the fast inactivation of r Na<sub>V</sub>1.3/ß1, m Na<sub>V</sub>1.6/ß1 and, to a lesser extent, h Na<sub>V</sub>1.5/ß1, while the other mammalian isoforms remain unaffected. Importantly, CgNa was also examined on the insect sodium channel Dm Na<sub>V</sub>1/tipE, revealing a clear phyla-selectivity in the efficacious actions of the toxin. CgNa strongly inhibits the inactivation of the insect Na<sub>V</sub> channel, resulting in a dramatic increase in peak current amplitude and complete removal of fast and steady-state inactivation. Together with the previously determined solution structure, the subtype-selective effects revealed in this study make of CgNa an interesting pharmacological probe to investigate the functional role of specific Na<sub>V</sub> channel subtypes. Moreover, further structural studies could provide important information on the molecular mechanism of Na<sub>V</sub> channel inactivation.","AbstractOtherLang":null,"BibLvlCode":"AS","StandardTitle":"Phyla- and subtype-selectivity of CgNa, a Na<sup>+</sup> channel toxin from the venom of the Giant Caribbean Sea Anemone <i>Condylactis gigantea</i>","OrigTitleLangCode":"en","OrigTitleLangCodeExtended":"eng","OrigTitleLangID":15,"DateLastModified":{"date":"2026-06-06 01:32:51.076051","timezone_type":1,"timezone":"+02:00"},"UserAccessRight":null,"UserAccID":null,"AuthorKeywords":"Condylactis gigantea","OtherDescriptors":null,"Notes":null,"AnaPub":2010,"MonPub":null,"DateUpdate":"2018-02-13","DateCreate":"2013-07-15","SecASFANote":null,"ConfID":null,"PeerRev":1,"VlizCoreFlag":1,"WoScode":"WOS:000209177100031","VABBcode":null,"OpenAcc":1,"DOI":"10.3389/fphar.2010.00133"},"refs":null,"anarec":{"AnaID":227398,"PubliDate":2010,"Pagination":"133","XtraPublOfAnaID":null,"ISBN":null,"Volume":"1","Issue":null,"BRefMon":null,"BRefMonRR":null,"BRefXtra":null,"BRefXtraRR":null,"SerBRefID":227255,"SerRR":"Frontiers in Pharmacology. 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