The sea anemone Bunodosoma caissarum toxin BcIII modulates the sodium current kinetics of rat dorsal root ganglia neurons and is displaced in a voltage-dependent manner

Sea anemone toxins bind to site 3 of the sodium channels, which is partially formed by the extracellular linker connecting S3 and S4 segments of domain IV, slowing down the inactivation process. In this work we have characterized the actions of BcIII, a sea anemone polypeptide toxin isolated from Bu...

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Veröffentlicht in:	Peptides (New York, N.Y. : 1980) N.Y. : 1980), 2010-03, Vol.31 (3), p.412-418
Hauptverfasser:	Salceda, Emilio, López, Omar, Zaharenko, André J., Garateix, Anoland, Soto, Enrique
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Anemonia viridis Animals ATX-II Bunodosoma caissarum Cells, Cultured CgNa Cnidarian Venoms - chemistry Cnidarian Venoms - pharmacology Condylactis gigantea Electrophysiology Fast inactivation Ganglia, Spinal - cytology Molecular Sequence Data Neurons - drug effects Neurons - metabolism Neurotoxins Rats Rats, Wistar Sequence Homology, Amino Acid Site-3 toxins Sodium - metabolism Sodium Channels - drug effects Voltage-gated sodium channels
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