Molecular cloning and functional characterization of the Aplysia FMRFamide-gated Na+ channel
Pflugers Archiv : European Journal of Physiology 451 巻 5 号
646-656 頁
2006-02 発行
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| ファイル情報(添付) | |
| タイトル ( eng ) |
Molecular cloning and functional characterization of the Aplysia FMRFamide-gated Na+ channel
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| 作成者 |
Miyawaki Yoshiyuki
Abe Genbu
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| 収録物名 |
Pflugers Archiv : European Journal of Physiology
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| 巻 | 451 |
| 号 | 5 |
| 開始ページ | 646 |
| 終了ページ | 656 |
| 抄録 |
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.
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| 著者キーワード |
FMRFamide
Amiloride
ENaC
Ion channel
Cloning
Aplysia
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| NDC分類 |
生物科学・一般生物学 [ 460 ]
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| 言語 |
英語
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| 資源タイプ | 学術雑誌論文 |
| 出版者 |
Springer
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| 発行日 | 2006-02 |
| 権利情報 |
Copyright (c) 2006 Springer-Verlag. "The original publication is available at www.springerlink.com"
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| 出版タイプ | Author’s Original（十分な品質であるとして、著者から正式な査読に提出される版） |
| アクセス権 | オープンアクセス |
| 収録物識別子 |
[ISSN] 0031-6768
[DOI] 10.1007/s00424-005-1498-z
[PMID] 16133260
[NCID] AA00771833
[DOI] http://dx.doi.org/10.1007/s00424-005-1498-z
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