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A novel vanadium transporter of the Nramp family expressed at the vacuole of vanadium-accumulating cells of the ascidian Ascidia sydneiensis samea

https://hiroshima.repo.nii.ac.jp/records/2006389
https://hiroshima.repo.nii.ac.jp/records/2006389
3bfbd369-9ec1-41f0-9bdc-3f27fc42378d
名前 / ファイル ライセンス アクション
BBAGenSub_1810_457.pdf BBAGenSub_1810_457.pdf (1.3 MB)
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 A novel vanadium transporter of the Nramp family expressed at the vacuole of vanadium-accumulating cells of the ascidian Ascidia sydneiensis samea
言語 en
作成者 Ueki, Tatsuya

× Ueki, Tatsuya

en Ueki, Tatsuya

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Furuno, Nobuaki

× Furuno, Nobuaki

en Furuno, Nobuaki

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Michibata, Hitoshi

× Michibata, Hitoshi

en Michibata, Hitoshi

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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) 2011 Elsevier B.V. All rights reserved.
権利情報
権利情報 This manuscript version is made available under the CC-BY-NC-ND 4.0 license http://creativecommons.org/licenses/by-nc-nd/4.0/
主題
主題Scheme Other
主題 Membrane protein
主題
主題Scheme Other
主題 Transport metals
主題
主題Scheme Other
主題 Vanadium
主題
主題Scheme Other
主題 Ascidian
主題
主題Scheme NDC
主題 460
内容記述
内容記述 Background: Vanadium is an essential transition metal in biological systems. Several key proteins related to vanadium accumulation and its physiological function have been isolated, but no vanadium ion transporter has yet been identified. Methods: We identified and cloned a member of the Nramp/DCT family of membrane metal transporters (AsNramp) from the ascidian Ascidia sydneiensis samea, which can accumulate extremely high levels of vanadium in the vacuoles of a type of blood cell called signet ring cells (also called vanadocytes). We performed immunological and biochemical experiments to examine its expression and transport function. Results: Western blotting analysis showed that AsNramp was localized at the vacuolar membrane of vanadocytes. Using the Xenopus oocyte expression system, we showed that AsNramp transported VO2+ into the oocyte as pH-dependent manner above pH 6, while no significant activity was observed below pH 6. Kinetic parameters (Km and Vmax) of AsNramp-mediated VO2+ transport at pH 8.5 were 90 nM and 9.1 pmol/oocyte/h, respectively. A rat homolog, DCT1, did not transport VO2+ under the same conditions. Excess Fe2+, Cu2+, Mn2+ or Zn2+ inhibited the transport of VO2+. Conclusions: AsNramp was revealed to be a novel VO2+/H+ antiporter, and we propose that AsNramp mediates vanadium accumulation coupled with the electrochemical gradient generated by vacuolar H+-ATPase in vanadocytes. General Significance: This is the first report of identification and functional analysis on a membrane transporter for vanadium ions.
言語 en
内容記述
内容記述タイプ Other
内容記述 This work was supported in part by Grants-in-Aid from the Ministry of Education, Culture, Sports, Science and Technology, Japan (#17370026, #18570070, #20570070, and #21570077).
出版者
出版者 Elsevier B.V.
言語
言語 eng
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 journal article
出版タイプ
出版タイプ AO
出版タイプResource http://purl.org/coar/version/c_b1a7d7d4d402bcce
関連情報
識別子タイプ DOI
関連識別子 10.1016/j.bbagen.2010.12.006
関連情報
関連タイプ isVersionOf
識別子タイプ DOI
関連識別子 http://doi.org/10.1016/j.bbagen.2010.12.006
収録物識別子
収録物識別子タイプ ISSN
収録物識別子 0304-4165
収録物識別子
収録物識別子タイプ NCID
収録物識別子 AA11522932
開始ページ
開始ページ 457
書誌情報 Biochimica et Biophysica Acta (BBA) - General Subjects
Biochimica et Biophysica Acta (BBA) - General Subjects

巻 1810, 号 4, p. 457-464, 発行日 2011-04
旧ID 39961
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