title: Cloning of a putative voltage-gated sodium channel from the turbellarian flatworm Bdelloura candida.
abstract: The neuromuscular sodium currents of early invertebrates such as platyhelminths display distinctive kinetic and pharmacological properties. We have cloned a cDNA from the horseshoe crab flatworm Bdelloura candida that encodes a protein homologous to the primary subunit of voltage-gated sodium channels. The B. candida protein, named BdNa1, exhibits amino acid identity of 40-47% to sodium channels of vertebrates and higher invertebrates. BdNa1 has the multidomain structure characteristic of sodium channels, and is most highly conserved in the hydrophobic transmembrane segments and the regions that form the pore of the channel. Northern blot analysis confirms the presence of a 5.4 kb BdNa1 transcript in B. candida tissue. The information provided by analysis of the BdNa1 sequence offers insight into the physiology of platyhelminth sodium currents.
authors.affiliation: Whitney Laboratory, University of Florida, St Augustine 32086, USA.
authors.forename: M C
authors.initials: MC
authors.lastname: Jeziorski
authors.forename: R M
authors.initials: RM
authors.lastname: Greenberg
authors.forename: P A
authors.initials: PA
authors.lastname: Anderson
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D019976:Cloning, Organism; D049832:Decapodiformes; D015801:Helminth Proteins / Q000096:biosynthesis / Q000737:chemistry; D006737:Horseshoe Crabs / Q000469:parasitology; D008565:Membrane Proteins; D008969:Molecular Sequence Data; D010802:Phylogeny; D016133:Polymerase Chain Reaction; D051381:Rats; D037401:Scyphozoa; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D015222:Sodium Channels / Q000096:biosynthesis* / Q000737:chemistry; D014419:Turbellaria / Q000502:physiology*
chemical_list: C109076:BdNa1 protein, Bdelloura candida; D015801:Helminth Proteins; D008565:Membrane Proteins; D015222:Sodium Channels