Molecular cloning and functional characterization of the Aplysia FMRFamide-gated Na+ channel

Yasuo Furukawa, Yoshiyuki Miyawaki, Genbu Abe

Research output: Contribution to journalArticle

18 Citations (Scopus)

Abstract

FMRFamide-gated Na+ channel (FaNaC) is the only known peptide-gated ion channel, which belongs to the epithelial Na+ channel/degenerin (ENaC/ DEG) family. We have cloned a putative FaNaC from the Aplysia kurodai CNS library using PCR, and examined its characteristics in Xenopus oocytes. A. kurodai FaNaC (AkFaNaC) comprised with 653 amino acids, and the sequence predicts two putative membrane domains and a large extracellular domain as in other members of the ENaC/DEG family. In oocytes expressing AkFaNaC, FMRFamide evoked amiloride-sensitive Na+ current. Different from the known FaNaCs (Helix and Helisoma FaNaCs), AkFaNaC was blocked by external Ca2+ but not by Mg2+. Also, desensitization of the current was enhanced by Mg2+ but not by Ca2+. The FMRFamide-gated current was depressed in both low and high pH. These results indicate that AkFaNaC is an FaNaC of Aplysia, and that the channel has Aplysia specific functional domains.

Original languageEnglish
Pages (from-to)646-656
Number of pages11
JournalPflugers Archiv European Journal of Physiology
Volume451
Issue number5
DOIs
Publication statusPublished - 2006 Feb

Keywords

  • Amiloride
  • Aplysia
  • Cloning
  • ENaC
  • FMRFamide
  • Ion channel

ASJC Scopus subject areas

  • Physiology
  • Clinical Biochemistry
  • Physiology (medical)

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