A putative voltage-gated sodium channel alpha subunit (PpSCN1) from the hydrozoan jellyfish, Polyorchis penicillatus: Structural comparisons and evolutionary considerations. Spafford, J. D., Spencer, A. N., & Gallin, W. J. Biochemical and Biophysical Research Communications, 244(3):772–780, March, 1998. doi abstract bibtex 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 Naf 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 electrophysioloscally distinct Na+ currents that have been studied in P. penicillatus. (C) 1998 Academic Press.
@article{spafford_putative_1998,
title = {A putative voltage-gated sodium channel alpha subunit ({PpSCN1}) from the hydrozoan jellyfish, {Polyorchis} penicillatus: {Structural} comparisons and evolutionary considerations},
volume = {244},
shorttitle = {A putative voltage-gated sodium channel alpha subunit ({PpSCN1}) from the hydrozoan jellyfish, {Polyorchis} penicillatus: {Structural} comparisons and evolutionary considerations},
doi = {10.1006/bbrc.1998.8332},
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 Naf 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 electrophysioloscally distinct Na+ currents that have been studied in P. penicillatus. (C) 1998 Academic Press.},
number = {3},
journal = {Biochemical and Biophysical Research Communications},
author = {Spafford, J. D. and Spencer, A. N. and Gallin, W. J.},
month = mar,
year = {1998},
keywords = {Polyorchis penicillatus},
pages = {772--780},
}
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