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Boric acid transport activity of marine teleost aquaporins expressed in Xenopus oocytes

Marine teleosts ingest large amounts of seawater containing various ions, including 0.4 mM boric acid, which can accumulate at toxic levels in the body. However, the molecular mechanisms by which marine teleosts absorb and excrete boric acid are not well understood. Aquaporins (Aqps) are homologous...

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Autores principales: Kumagai, Shiori, Watanabe, Erika, Hayashi, Naoko, Kimura, Yuuri, Kamiya, Takehiro, Nagashima, Ayumi, Ushio, Kazutaka, Imaizumi, Genki, Kim, Juhyun, Munakata, Keijiro, Umezawa, Takahiro, Hirose, Shigehisa, Kasai, Koji, Fujiwara, Toru, Romero, Michael F., Kato, Akira
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley and Sons Inc. 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10040401/
https://www.ncbi.nlm.nih.gov/pubmed/36967473
http://dx.doi.org/10.14814/phy2.15655
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author Kumagai, Shiori
Watanabe, Erika
Hayashi, Naoko
Kimura, Yuuri
Kamiya, Takehiro
Nagashima, Ayumi
Ushio, Kazutaka
Imaizumi, Genki
Kim, Juhyun
Munakata, Keijiro
Umezawa, Takahiro
Hirose, Shigehisa
Kasai, Koji
Fujiwara, Toru
Romero, Michael F.
Kato, Akira
author_facet Kumagai, Shiori
Watanabe, Erika
Hayashi, Naoko
Kimura, Yuuri
Kamiya, Takehiro
Nagashima, Ayumi
Ushio, Kazutaka
Imaizumi, Genki
Kim, Juhyun
Munakata, Keijiro
Umezawa, Takahiro
Hirose, Shigehisa
Kasai, Koji
Fujiwara, Toru
Romero, Michael F.
Kato, Akira
author_sort Kumagai, Shiori
collection PubMed
description Marine teleosts ingest large amounts of seawater containing various ions, including 0.4 mM boric acid, which can accumulate at toxic levels in the body. However, the molecular mechanisms by which marine teleosts absorb and excrete boric acid are not well understood. Aquaporins (Aqps) are homologous to the nodulin‐like intrinsic protein (NIP) family of plant boric acid channels. To investigate the potential roles of Aqps on boric acid transport across the plasma membrane in marine teleosts, we analyzed the function of Aqps of Japanese pufferfish (Takifugu rubripes) expressed in Xenopus laevis oocytes. Takifugu genome database contains 16 genes encoding the aquaporin family members (aqp0a, aqp0b, aqp1aa, aqp1ab, aqp3a, aqp4a, aqp7, aqp8bb, aqp9a, aqp9b, aqp10aa, aqp10bb, aqp11a, aqp11b, aqp12, and aqp14). When T. rubripes Aqps (TrAqps) were expressed in X. laevis oocytes, a swelling assay showed that boric acid permeability was significantly increased in oocytes expressing TrAqp3a, 7, 8bb, 9a, and 9b. The influx of boric acid into these oocytes was also confirmed by elemental quantification. Electrophysiological analysis using a pH microelectrode showed that these TrAqps increase B(OH)(3) permeability. These results indicate that TrAqp3a, 7, 8bb, 9a, and 9b act as boric acid transport systems, likely as channels, in marine teleosts.
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spelling pubmed-100404012023-03-28 Boric acid transport activity of marine teleost aquaporins expressed in Xenopus oocytes Kumagai, Shiori Watanabe, Erika Hayashi, Naoko Kimura, Yuuri Kamiya, Takehiro Nagashima, Ayumi Ushio, Kazutaka Imaizumi, Genki Kim, Juhyun Munakata, Keijiro Umezawa, Takahiro Hirose, Shigehisa Kasai, Koji Fujiwara, Toru Romero, Michael F. Kato, Akira Physiol Rep Original Articles Marine teleosts ingest large amounts of seawater containing various ions, including 0.4 mM boric acid, which can accumulate at toxic levels in the body. However, the molecular mechanisms by which marine teleosts absorb and excrete boric acid are not well understood. Aquaporins (Aqps) are homologous to the nodulin‐like intrinsic protein (NIP) family of plant boric acid channels. To investigate the potential roles of Aqps on boric acid transport across the plasma membrane in marine teleosts, we analyzed the function of Aqps of Japanese pufferfish (Takifugu rubripes) expressed in Xenopus laevis oocytes. Takifugu genome database contains 16 genes encoding the aquaporin family members (aqp0a, aqp0b, aqp1aa, aqp1ab, aqp3a, aqp4a, aqp7, aqp8bb, aqp9a, aqp9b, aqp10aa, aqp10bb, aqp11a, aqp11b, aqp12, and aqp14). When T. rubripes Aqps (TrAqps) were expressed in X. laevis oocytes, a swelling assay showed that boric acid permeability was significantly increased in oocytes expressing TrAqp3a, 7, 8bb, 9a, and 9b. The influx of boric acid into these oocytes was also confirmed by elemental quantification. Electrophysiological analysis using a pH microelectrode showed that these TrAqps increase B(OH)(3) permeability. These results indicate that TrAqp3a, 7, 8bb, 9a, and 9b act as boric acid transport systems, likely as channels, in marine teleosts. John Wiley and Sons Inc. 2023-03-26 /pmc/articles/PMC10040401/ /pubmed/36967473 http://dx.doi.org/10.14814/phy2.15655 Text en © 2023 The Authors. Physiological Reports published by Wiley Periodicals LLC on behalf of The Physiological Society and the American Physiological Society. https://creativecommons.org/licenses/by/4.0/This is an open access article under the terms of the http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
spellingShingle Original Articles
Kumagai, Shiori
Watanabe, Erika
Hayashi, Naoko
Kimura, Yuuri
Kamiya, Takehiro
Nagashima, Ayumi
Ushio, Kazutaka
Imaizumi, Genki
Kim, Juhyun
Munakata, Keijiro
Umezawa, Takahiro
Hirose, Shigehisa
Kasai, Koji
Fujiwara, Toru
Romero, Michael F.
Kato, Akira
Boric acid transport activity of marine teleost aquaporins expressed in Xenopus oocytes
title Boric acid transport activity of marine teleost aquaporins expressed in Xenopus oocytes
title_full Boric acid transport activity of marine teleost aquaporins expressed in Xenopus oocytes
title_fullStr Boric acid transport activity of marine teleost aquaporins expressed in Xenopus oocytes
title_full_unstemmed Boric acid transport activity of marine teleost aquaporins expressed in Xenopus oocytes
title_short Boric acid transport activity of marine teleost aquaporins expressed in Xenopus oocytes
title_sort boric acid transport activity of marine teleost aquaporins expressed in xenopus oocytes
topic Original Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10040401/
https://www.ncbi.nlm.nih.gov/pubmed/36967473
http://dx.doi.org/10.14814/phy2.15655
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