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ID 17222
file
creator
Miyawaki, Yoshiyuki
Abe, Genbu
subject
FMRFamide
Amiloride
ENaC
Ion channel
Cloning
Aplysia
NDC
Biology
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.
journal title
Pflugers Archiv : European Journal of Physiology
volume
Volume 451
issue
Issue 5
start page
646
end page
656
date of issued
2006-02
publisher
Springer
issn
0031-6768
ncid
publisher doi
pubmed id
language
eng
nii type
Journal Article
HU type
Journal Articles
DCMI type
text
format
application/pdf
text version
author
rights
Copyright (c) 2006 Springer-Verlag. "The original publication is available at www.springerlink.com"
relation is version of URL
http://dx.doi.org/10.1007/s00424-005-1498-z
department
Graduate School of Integrated Arts and Sciences