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Characterization of two Bunodosoma granulifera toxins active on cardiac sodium channels
Goudet, C.; Ferrero, T.; Galàn, L.; Artiles, A.; Batista, C.F.V.; Possani, L.D.; Alvarez, J.; Aneiros, A.; Tytgat, J. (2001). Characterization of two Bunodosoma granulifera toxins active on cardiac sodium channels. Br. J. Pharmacol. 134(6): 1195-1206. dx.doi.org/10.1038/sj.bjp.0704361
In: British Journal of Pharmacology. Nature Publishing Group: London. ISSN 0007-1188; e-ISSN 1476-5381
Peer reviewed article  
Beschikbaar in  Auteurs 
Trefwoorden
    Amino acid sequence
    Biology > Physiology > Electrophysiology
    Materials > Hazardous materials > Biological poisons > Neurotoxins
    Toxins
    Bunodosoma granulifera (Le Sueur, 1817) [WoRMS]; Xenopus laevis
    Marien/Kust
Author keywords
    sea anemone toxin; voltage-gated sodium channels; inactivation; ionicselectivity; cardiotoxin; neurotoxin
Auteurs  Top 
  • Goudet, C.
  • Ferrero, T.
  • Galàn, L.
  • Artiles, A.
  • Batista, C.F.V.
  • Possani, L.D.
  • Alvarez, J.
  • Aneiros, A.
  • Tytgat, J., meer
Abstract
    1. Two sodium channel toxins, BgII and BgIII, have been isolated and purified from the sea anemone Bunodosoma granulifera. Combining different techniques, we have investigated the electrophysiological properties of these toxins. 2. We examined the effect of BgII and BgIII on rat ventricular strips. These toxins prolong action potentials with EC50 values of 60 and 660 nM and modify the resting potentials. 3. The effect on Na+ currents in rat cardiomyocytes was studied using the patch-clamp technique. BgII and BgIII slow the rapid inactivation process and increase the current density with EC50 values of 58 and 78 nM, respectively. 4. On the cloned hH1 cardiac Na+ channel expressed in Xenopus laevis oocytes, BgII and BgIII slow the inactivation process of Na+ currents (respective EC50 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 BgII which is replaced by an aspartic acid in BgIII. In all experiments, BgII was more potent than BgIII suggesting that this conservative residue is important for the toxicity of sea anemone toxins. 6. We conclude that BgII and BgIII, generally known as neurotoxins, are also cardiotoxic and combine the classical effects of sea anemone Na+ channels toxins (slowing of inactivation kinetics, shift of steady-state activation and inactivation parameters) with a striking decrease on the ionic selectivity of Na+ channels.
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