ArticlePhysiological reports2022
Boric acid transport activity of human aquaporins expressed in Xenopus oocytes.
Article in Physiological reports, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 10 citations in OpenAlex.
- Elongationless start-stop elements are stress-resilient translation gates that are more repressive than uTranslons.Nucleic acids research · 2026Article
- Genome-wide identification and solute selectivity of aquaporins in the sharpnose sevengill shark, Heptranchias perlo.Physiological reports · 2026Article
- The flavonoid isoliquiritigenin promotes lifespan extension of Caenorhabditis elegans through the transcription factor DAF-16 and aquaporin-2.Brazilian journal of medical and biological research = Revista brasileira de pesquisas medicas e biologicas · 2026Article
- Loss and Gain of Aqp10 Paralogs With Broad Solute Selectivity in Anguillid Eels.Genome biology and evolution · 2025Article
- Yeast Complementation Assays Demonstrating the Importance of the Affinity Tag Position in Membrane Protein Purification, as Exemplified bySmall science · 2025Article
- Functional Divergence in Solute Permeability between Ray-Finned Fish-Specific Paralogs of aqp10.Genome biology and evolution · 2024Article
- Aquaporin water channels: roles beyond renal water handling.Nature reviews. Nephrology · 2023Review
- Redox Mechanisms Underlying the Cytostatic Effects of Boric Acid on Cancer Cells-An Issue Still Open.Antioxidants (Basel, Switzerland) · 2023Review
- Boric acid transport activity of marine teleost aquaporins expressed in Xenopus oocytes.Physiological reports · 2023Article
- Boric acid transport activity of human aquaporins expressed in Xenopus oocytes.Physiological reports · 2022Article
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Authors and funding
9 authors at 3 institutions in 2 countries.
Funding
Abstract
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)
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