{"refrec":{"BRefID":121611,"RR":"<b>Goudet, C.; Ferrero, T.; Galàn, L.; Artiles, A.; Batista, C.F.V.; Possani, L.D.; Alvarez, J.; Aneiros, A.; Tytgat, J.</b> (2001). Characterization of two <i>Bunodosoma granulifera</i> toxins active on cardiac sodium channels. <i>Br. J. Pharmacol. 134(6)</i>: 1195-1206. <a href=\"http://dx.doi.org/10.1038/sj.bjp.0704361\" target=\"_blank\">dx.doi.org/10.1038/sj.bjp.0704361</a>","BEntID":115704,"PublicFlag":1,"CheckedFlag":1,"wosflag":1,"vabbflag":null,"RefStringPartII":". <i>Br. J. Pharmacol. 134(6)</i>: 1195-1206. <a href=\"https://dx.doi.org/10.1038/sj.bjp.0704361\" target=\"_blank\">https://dx.doi.org/10.1038/sj.bjp.0704361</a>","DocTypID":8,"DocType":"Journal article","MarineFlag":1,"FreshFlag":0,"BrackishFlag":0,"TerrestrialFlag":0,"Authorstring":"Goudet, C.; Ferrero, T.; Galàn, L.; Artiles, A.; Batista, C.F.V.; Possani, L.D.; Alvarez, J.; Aneiros, A.; Tytgat, J.","OrigTitleTranslFlag":0,"Authorstringtrunc":"Goudet, C. <i>et al.</i>","Englishabstract":"1. Two sodium channel toxins, <i>BgI</i>I and <i>Bg</i>III, have been isolated and purified from the sea anemone <i>Bunodosoma granulifera</i>. Combining different techniques, we have investigated the electrophysiological properties of these toxins. 2. We examined the effect of <i>Bg</i>II and <i>Bg</i>III on rat ventricular strips. These toxins prolong action potentials with EC<sub>50</sub> values of 60 and 660 nM and modify the resting potentials. 3. The effect on Na<sup>+</sup> currents in rat cardiomyocytes was studied using the patch-clamp technique. <i>Bg</i>II and <i>Bg</i>III slow the rapid inactivation process and increase the current density with EC<sub>50</sub> values of 58 and 78 nM, respectively. 4. On the cloned hH1 cardiac Na<sup>+</sup> channel expressed in <i>Xenopus laevis</i> oocytes, <i>Bg</i>II and <i>Bg</i>III slow the inactivation process of Na<sup>+</sup> currents (respective EC<sub>50</sub> values of 0.38 and 7.8 µM), shift the steady-state activation and inactivation parameters to more positive potentials and the reversal potential to more negative potentials. 5. The amino acid sequences of these toxins are almost identical except for an asparagine at position 16 in <i>Bg</i>II which is replaced by an aspartic acid in <i>Bg</i>III. In all experiments, <i>Bg</i>II was more potent than <i>Bg</i>III suggesting that this conservative residue is important for the toxicity of sea anemone toxins. 6. We conclude that <i>Bg</i>II and <i>Bg</i>III, generally known as neurotoxins, are also cardiotoxic and combine the classical effects of sea anemone Na<sup>+</sup> channels toxins (slowing of inactivation kinetics, shift of steady-state activation and inactivation parameters) with a striking decrease on the ionic selectivity of Na<sup>+</sup> channels.","AbstractOtherLang":null,"BibLvlCode":"AS","StandardTitle":"Characterization of two <i>Bunodosoma granulifera</i> toxins active on cardiac sodium channels","OrigTitleLangCode":"en","OrigTitleLangCodeExtended":"eng","OrigTitleLangID":15,"DateLastModified":{"date":"2024-12-10 01:33:17.368041","timezone_type":1,"timezone":"+01:00"},"UserAccessRight":null,"UserAccID":null,"AuthorKeywords":"sea anemone toxin; voltage-gated sodium channels; inactivation; ionicselectivity; cardiotoxin; neurotoxin","OtherDescriptors":null,"Notes":null,"AnaPub":2001,"MonPub":null,"DateUpdate":"2014-10-09","DateCreate":"2008-04-15","SecASFANote":null,"ConfID":null,"PeerRev":1,"VlizCoreFlag":1,"WoScode":"WOS:000172191400009","VABBcode":null,"OpenAcc":0,"DOI":"10.1038/sj.bjp.0704361"},"refs":null,"anarec":{"AnaID":121611,"PubliDate":2001,"Pagination":"1195-1206","XtraPublOfAnaID":null,"ISBN":null,"Volume":"134","Issue":"6","BRefMon":null,"BRefMonRR":null,"BRefXtra":null,"BRefXtraRR":null,"SerBRefID":121609,"SerRR":"British Journal of Pharmacology. 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