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ペプチド作動性Na+チャネルの活性化とイオン透過性を制御する機能部位 <学位論文要旨>
https://hiroshima.repo.nii.ac.jp/records/2032758
https://hiroshima.repo.nii.ac.jp/records/2032758d31a5c20-2b03-42fa-99b3-42ef87102914
| 名前 / ファイル | ライセンス | アクション |
|---|---|---|
StudiesInHumanSciences_7_51.pdf (1.0 MB)
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| Item type | デフォルトアイテムタイプ_（フル）(1) | |||||||||
|---|---|---|---|---|---|---|---|---|---|---|
| 公開日 | 2023-03-18 | |||||||||
| タイトル | ||||||||||
| タイトル | ペプチド作動性Na+チャネルの活性化とイオン透過性を制御する機能部位 <学位論文要旨> | |||||||||
| 言語 | ja | |||||||||
| タイトル | ||||||||||
| タイトル | Functional sites controlling the activation and ion permeation of a peptide-gated Na+ channel <Summaries of the Doctoral Theses> | |||||||||
| 言語 | en | |||||||||
| 作成者 |
小谷, 侑
× 小谷, 侑
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| アクセス権 | ||||||||||
| アクセス権 | open access | |||||||||
| アクセス権URI | http://purl.org/coar/access_right/c_abf2 | |||||||||
| 権利情報 | ||||||||||
| 権利情報 | Copyright (c) 2012 by Graduate School of Integrated Arts and Sciences, Hiroshima University All rights reserved | |||||||||
| 主題 | ||||||||||
| 主題Scheme | NDC | |||||||||
| 主題 | 460 | |||||||||
| 内容記述 | ||||||||||
| 内容記述 | Peptides are ubiquitous signaling molecules in animals. Most of the peptide receptors identified so far are G protein-coupled receptors, but peptide-gated Na+ channels have also been cloned. This study investigated the structurefunction relationship of a peptide(FMRFamide)- gated Na+ channel (FaNaC). We focused on three polar residues (Y548, D552, D556) around the outer end of the second transmembrane domain of FaNaC. Site-directed mutagenesis and cysteine modification experiments uncovered that D552 is a critical determinant for various functional aspects of FaNaC, such as activation and desensitization kinetics, apparent FMRFamide sensitivity, channel block by FMRFamide, and current rectification. Double-mutant cycle analysis demonstrated that the interaction between D552 and Y548 regulates both activation and desensitization processes. Although point mutants in D556 were nonfunctional, a double mutant D552N/D556N was functional and showed markedly slow current kinetics. External Ca2+ inhibited the activation and desensitization of FaNaC. These Ca2+ actions were diminished by removal of the negative charge of D552, and notably, the Ca2+ action on desensitization was completely abolished in D552N/D556N, suggesting that D552 and D556 are involved in the Ca2+-binding site. In summary, Y548, D552, and D556 are important sites controlling the gating of FaNaC, and D552 also affects the ion permeation of the channel. | |||||||||
| 言語 | en | |||||||||
| 出版者 | ||||||||||
| 出版者 | 広島大学大学院総合科学研究科 | |||||||||
| 言語 | ||||||||||
| 言語 | jpn | |||||||||
| 資源タイプ | ||||||||||
| 資源タイプ識別子 | http://purl.org/coar/resource_type/c_6501 | |||||||||
| 資源タイプ | departmental bulletin paper | |||||||||
| 出版タイプ | ||||||||||
| 出版タイプ | VoR | |||||||||
| 出版タイプResource | http://purl.org/coar/version/c_970fb48d4fbd8a85 | |||||||||
| 収録物識別子 | ||||||||||
| 収録物識別子タイプ | ISSN | |||||||||
| 収録物識別子 | 1881-7688 | |||||||||
| 収録物識別子 | ||||||||||
| 収録物識別子タイプ | NCID | |||||||||
| 収録物識別子 | AA12198647 | |||||||||
| 開始ページ | ||||||||||
| 開始ページ | 51 | |||||||||
| 書誌情報 |
広島大学大学院総合科学研究科紀要. I, 人間科学研究 Bulletin of the Graduate School of Integrated Arts and Sciences, Hiroshima University. I, Studies in human sciences 巻 7, p. 51-53, 発行日 2012-12-31 |
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| 旧ID | 34622 | |||||||||
