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      A putative voltage-gated sodium channel alpha subunit (PpSCN1) from the hydrozoan jellyfish, Polyorchis penicillatus: structural comparisons and evolutionary considerations.

      Biochemical and Biophysical Research Communications
      Amino Acid Sequence, Animals, Base Sequence, Cloning, Molecular, Cnidaria, genetics, DNA, Complementary, Electrophysiology, Evolution, Molecular, Ion Channel Gating, Membrane Potentials, Molecular Sequence Data, Protein Conformation, RNA, Messenger, Sequence Analysis, DNA, Sequence Homology, Amino Acid, Sodium, metabolism, Sodium Channels

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          Abstract

          Extant cnidarians are probably the simplest metazoans with discrete nervous systems and rapid, transient voltage-gated currents carried exclusively by Na+ ions. Thus cnidarians are pivotal organisms for studying the evolution of voltage-gated Na+ channels. We have isolated a full-length Na+ channel alpha subunit cDNA (PpSCN1) from the hydrozoan jellyfish, Polyorchis penicillatus, that has one of the smallest known coding regions of a four domain Na+ channel (1695 amino acids). Homologous residues that have a critical bearing on the selectivity filter, voltage-sensor and binding sites for tetrodotoxin and lidocaine in vertebrates and most invertebrates differ in cnidarians. PpSCN1 is not alternatively-spliced and may be the only pore-forming alpha subunit available to account for at least three electrophysiologically distinct Na+ currents that have been studied in P. penicillatus.

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