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Characterization of the Aquaporin-9 Inhibitor RG100204 In Vitro and in db/db Mice.
Florio, Marilina; Engfors, Angelica; Gena, Patrizia; Larsson, Jessica; Massaro, Alessandro; Timpka, Stella; Reimer, Martina Kvist; Kjellbom, Per; Beitz, Eric; Johanson, Urban; Rützler, Michael; Calamita, Giuseppe.
Afiliación
  • Florio M; Department of Biosciences, Biotechnologies and Environment, University of Bari Aldo Moro, 70125 Bari, Italy.
  • Engfors A; Division of Biochemistry and Structural Biology, Department of Chemistry, Lund University, 22100 Lund, Sweden.
  • Gena P; Department of Biosciences, Biotechnologies and Environment, University of Bari Aldo Moro, 70125 Bari, Italy.
  • Larsson J; Red Glead Discovery AB, Medicon Village, 22381 Lund, Sweden.
  • Massaro A; Department of Management, Finance and Technology, Libera Università Mediterranea (LUM) "Giuseppe Degennaro" LUM University, 70010 Casamassima, Italy.
  • Timpka S; LUM Enterprise Srl, S.S. 100-Km18, Parco il Baricentro, 70010 Bari, Italy.
  • Reimer MK; Red Glead Discovery AB, Medicon Village, 22381 Lund, Sweden.
  • Kjellbom P; Red Glead Discovery AB, Medicon Village, 22381 Lund, Sweden.
  • Beitz E; Division of Biochemistry and Structural Biology, Department of Chemistry, Lund University, 22100 Lund, Sweden.
  • Johanson U; Department of Pharmaceutical and Medicinal Chemistry, Pharmaceutical Institute, Christian-Albrechts-University of Kiel, Gutenbergstr. 76, 24118 Kiel, Germany.
  • Rützler M; Division of Biochemistry and Structural Biology, Department of Chemistry, Lund University, 22100 Lund, Sweden.
  • Calamita G; Division of Biochemistry and Structural Biology, Department of Chemistry, Lund University, 22100 Lund, Sweden.
Cells ; 11(19)2022 10 04.
Article en En | MEDLINE | ID: mdl-36231080
Aquaporin-9 (AQP9) is a facilitator of glycerol and other small neutral solute transmembrane diffusion. Identification of specific inhibitors for aquaporin family proteins has been difficult, due to high sequence similarity between the 13 human isoforms, and due to the limited channel surface areas that permit inhibitor binding. The few AQP9 inhibitor molecules described to date were not suitable for in vivo experiments. We now describe the characterization of a new small molecule AQP9 inhibitor, RG100204 in cell-based calcein-quenching assays, and by stopped-flow light-scattering recordings of AQP9 permeability in proteoliposomes. Moreover, we investigated the effects of RG100204 on glycerol metabolism in mice. In cell-based assays, RG100204 blocked AQP9 water permeability and glycerol permeability with similar, high potency (~5 × 10-8 M). AQP9 channel blocking by RG100204 was confirmed in proteoliposomes. After oral gavage of db/db mice with RG100204, a dose-dependent elevation of plasma glycerol was observed. A blood glucose-lowering effect was not statistically significant. These experiments establish RG100204 as a direct blocker of the AQP9 channel, and suggest its use as an experimental tool for in vivo experiments on AQP9 function.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Acuaporinas / Glicerol Límite: Animals / Humans Idioma: En Revista: Cells Año: 2022 Tipo del documento: Article País de afiliación: Italia Pais de publicación: Suiza

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Acuaporinas / Glicerol Límite: Animals / Humans Idioma: En Revista: Cells Año: 2022 Tipo del documento: Article País de afiliación: Italia Pais de publicación: Suiza