Binding properties of 3H-PbTx-3 and 3H-Saxitoxin to brain membranes and to skeletal muscle membranes of puffer fish Fugu pardalis and the primary structure of a voltage-gated Na+ channel α-subunit (fMNa1) from skeletal muscle of F. pardalis

Mari Yotsu-Yamashita, Katsuhiko Nishimori, Yoko Nitanai, Masako Isemura, Atsuko Sugimoto, Takeshi Yasumoto

Research output: Contribution to journalArticlepeer-review

50 Citations (Scopus)

Abstract

The dissociation constants for 3H-saxitoxin to brain membranes and to skeletal muscle membranes of puffer fish Fugu pardalis have been estimated to be 190- and 460-fold, respectively, larger than those to corresponding membranes of rat, by a rapid filtration assay, while these values for 3H-PbTx-3 have been estimated to be one-third and one-half of those to rat, respectively. We have obtained a cDNA, encoding an entire voltage-gated Na+ channel α-subunit (fMNa1, 1880 residues) from skeletal muscle of F. pardalis by composition of the fragments obtained from cDNA library and RT-PCR products. In fMNa1 protein, the residues for ion-selective filter and voltage sensor and the charged residues in SS2 regions of domains I-IV were conserved, but the aromatic amino acid (Phe/Tyr), commonly located in the SS2 region of domain I of tetrodotoxin-sensitive Na+ channels, was replaced by Asn. With this particular criterion, we propose that the fMNa1 protein is a tetrodotoxin-resistant Na+ channel. (C) 2000 Academic Press.

Original languageEnglish
Pages (from-to)403-412
Number of pages10
JournalBiochemical and biophysical research communications
Volume267
Issue number1
DOIs
Publication statusPublished - 2000 Jan 7

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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