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Boric acid transport activity of human aquaporins expressed in Xenopus oocytes.
Ushio, Kazutaka; Watanabe, Erika; Kamiya, Takehiro; Nagashima, Ayumi; Furuta, Tadaomi; Imaizumi, Genki; Fujiwara, Toru; Romero, Michael F; Kato, Akira.
Afiliación
  • Ushio K; School of Life Science and Technology, Tokyo Institute of Technology, Yokohama, Japan.
  • Watanabe E; School of Life Science and Technology, Tokyo Institute of Technology, Yokohama, Japan.
  • Kamiya T; Department of Applied Biological Chemistry, Graduate School of Agricultural and Life Sciences, The University of Tokyo, Tokyo, Japan.
  • Nagashima A; School of Life Science and Technology, Tokyo Institute of Technology, Yokohama, Japan.
  • Furuta T; School of Life Science and Technology, Tokyo Institute of Technology, Yokohama, Japan.
  • Imaizumi G; School of Life Science and Technology, Tokyo Institute of Technology, Yokohama, Japan.
  • Fujiwara T; Department of Applied Biological Chemistry, Graduate School of Agricultural and Life Sciences, The University of Tokyo, Tokyo, Japan.
  • Romero MF; Department of Physiology and Biomedical Engineering, Mayo Clinic College of Medicine & Science, Rochester, Minnesota, USA.
  • Kato A; Nephrology and Hypertension, Mayo Clinic College of Medicine & Science, Rochester, Minnesota, USA.
Physiol Rep ; 10(1): e15164, 2022 01.
Article en En | MEDLINE | ID: mdl-35014212
Boric acid is a vital micronutrient that is toxic at high concentrations in animals. However, the mechanisms underlying boric acid transport in animal cells remain unclear. To identify the plasma membrane boric acid channels in animals, we analyzed the function of human aquaporins (AQPs), which are homologous to the nodulin-like intrinsic protein family of plant boric acid channels. When human AQPs were expressed in Xenopus laevis oocytes, the results of the swelling assay showed that boric acid permeability significantly increased in oocytes expressing AQP3, 7, 8, 9, and 10, but not in those expressing AQP1, 2, 4, and 5. The boric acid influxes of these oocytes were also confirmed by elemental quantification. Electrophysiological analysis using a pH microelectrode showed that these AQPs transported boric acid (B(OH)3 ) but not borate ions (B(OH)4- ). These results indicate that AQP3, 7, 8, 9, and 10 act as boric acid transport systems, likely as channels in humans.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Ácidos Bóricos / Acuaporinas Límite: Animals / Humans Idioma: En Revista: Physiol Rep Año: 2022 Tipo del documento: Article País de afiliación: Japón Pais de publicación: Estados Unidos

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Ácidos Bóricos / Acuaporinas Límite: Animals / Humans Idioma: En Revista: Physiol Rep Año: 2022 Tipo del documento: Article País de afiliación: Japón Pais de publicación: Estados Unidos