Specific Aquaporins Facilitate the Diffusion of Hydrogen Peroxide across Membranes
The metabolism of aerobic organisms continuously produces reactive oxygen species. Although potentially toxic, these compounds also function in signaling. One important feature of signaling compounds is their ability to move between different compartments, e.g. to cross membranes. Here we present ev...
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Published in | The Journal of biological chemistry Vol. 282; no. 2; pp. 1183 - 1192 |
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Main Authors | , , , , , , |
Format | Journal Article |
Language | English |
Published |
United States
Elsevier Inc
12.01.2007
American Society for Biochemistry and Molecular Biology |
Subjects | |
Online Access | Get full text |
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Abstract | The metabolism of aerobic organisms continuously produces reactive oxygen species. Although potentially toxic, these compounds also function in signaling. One important feature of signaling compounds is their ability to move between different compartments, e.g. to cross membranes. Here we present evidence that aquaporins can channel hydrogen peroxide (H2O2). Twenty-four aquaporins from plants and mammals were screened in five yeast strains differing in sensitivity toward oxidative stress. Expression of human AQP8 and plant Arabidopsis TIP1;1 and TIP1;2 in yeast decreased growth and survival in the presence of H2O2. Further evidence for aquaporin-mediated H2O2 diffusion was obtained by a fluorescence assay with intact yeast cells using an intracellular reactive oxygen species-sensitive fluorescent dye. Application of silver ions (Ag+), which block aquaporin-mediated water diffusion in a fast kinetics swelling assay, also reversed both the aquaporin-dependent growth repression and the H2O2-induced fluorescence. Our results present the first molecular genetic evidence for the diffusion of H2O2 through specific members of the aquaporin family. |
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AbstractList | The metabolism of aerobic organisms continuously produces reactive oxygen species. Although potentially toxic, these compounds also function in signaling. One important feature of signaling compounds is their ability to move between different compartments, e.g. to cross membranes. Here we present evidence that aquaporins can channel hydrogen peroxide (H2O2). Twenty-four aquaporins from plants and mammals were screened in five yeast strains differing in sensitivity toward oxidative stress. Expression of human AQP8 and plant Arabidopsis TIP1;1 and TIP1;2 in yeast decreased growth and survival in the presence of H2O2. Further evidence for aquaporin-mediated H2O2 diffusion was obtained by a fluorescence assay with intact yeast cells using an intracellular reactive oxygen species-sensitive fluorescent dye. Application of silver ions (Ag+), which block aquaporin-mediated water diffusion in a fast kinetics swelling assay, also reversed both the aquaporin-dependent growth repression and the H2O2-induced fluorescence. Our results present the first molecular genetic evidence for the diffusion of H2O2 through specific members of the aquaporin family.The metabolism of aerobic organisms continuously produces reactive oxygen species. Although potentially toxic, these compounds also function in signaling. One important feature of signaling compounds is their ability to move between different compartments, e.g. to cross membranes. Here we present evidence that aquaporins can channel hydrogen peroxide (H2O2). Twenty-four aquaporins from plants and mammals were screened in five yeast strains differing in sensitivity toward oxidative stress. Expression of human AQP8 and plant Arabidopsis TIP1;1 and TIP1;2 in yeast decreased growth and survival in the presence of H2O2. Further evidence for aquaporin-mediated H2O2 diffusion was obtained by a fluorescence assay with intact yeast cells using an intracellular reactive oxygen species-sensitive fluorescent dye. Application of silver ions (Ag+), which block aquaporin-mediated water diffusion in a fast kinetics swelling assay, also reversed both the aquaporin-dependent growth repression and the H2O2-induced fluorescence. Our results present the first molecular genetic evidence for the diffusion of H2O2 through specific members of the aquaporin family. The metabolism of aerobic organisms continuously produces reactive oxygen species. Although potentially toxic, these compounds also function in signaling. One important feature of signaling compounds is their ability to move between different compartments, e.g. to cross membranes. Here we present evidence that aquaporins can channel hydrogen peroxide (H2O2). Twenty-four aquaporins from plants and mammals were screened in five yeast strains differing in sensitivity toward oxidative stress. Expression of human AQP8 and plant Arabidopsis TIP1;1 and TIP1;2 in yeast decreased growth and survival in the presence of H2O2. Further evidence for aquaporin-mediated H2O2 diffusion was obtained by a fluorescence assay with intact yeast cells using an intracellular reactive oxygen species-sensitive fluorescent dye. Application of silver ions (Ag+), which block aquaporin-mediated water diffusion in a fast kinetics swelling assay, also reversed both the aquaporin-dependent growth repression and the H2O2-induced fluorescence. Our results present the first molecular genetic evidence for the diffusion of H2O2 through specific members of the aquaporin family. The metabolism of aerobic organisms continuously produces reactive oxygen species. Although potentially toxic, these compounds also function in signaling. One important feature of signaling compounds is their ability to move between different compartments, e.g. to cross membranes. Here we present evidence that aquaporins can channel hydrogen peroxide (H₂O₂). Twenty-four aquaporins from plants and mammals were screened in five yeast strains differing in sensitivity toward oxidative stress. Expression of human AQP8 and plant Arabidopsis TIP1;1 and TIP1;2 in yeast decreased growth and survival in the presence of H₂O₂. Further evidence for aquaporin-mediated H₂O₂ diffusion was obtained by a fluorescence assay with intact yeast cells using an intracellular reactive oxygen species-sensitive fluorescent dye. Application of silver ions (Ag⁺), which block aquaporin-mediated water diffusion in a fast kinetics swelling assay, also reversed both the aquaporin-dependent growth repression and the H₂O₂-induced fluorescence. Our results present the first molecular genetic evidence for the diffusion of H₂O₂ through specific members of the aquaporin family. The metabolism of aerobic organisms continuously produces reactive oxygen species. Although potentially toxic, these compounds also function in signaling. One important feature of signaling compounds is their ability to move between different compartments, e.g. to cross membranes. Here we present evidence that aquaporins can channel hydrogen peroxide (H 2 O 2 ). Twenty-four aquaporins from plants and mammals were screened in five yeast strains differing in sensitivity toward oxidative stress. Expression of human AQP8 and plant Arabidopsis TIP1;1 and TIP1;2 in yeast decreased growth and survival in the presence of H 2 O 2 . Further evidence for aquaporin-mediated H 2 O 2 diffusion was obtained by a fluorescence assay with intact yeast cells using an intracellular reactive oxygen species-sensitive fluorescent dye. Application of silver ions (Ag + ), which block aquaporin-mediated water diffusion in a fast kinetics swelling assay, also reversed both the aquaporin-dependent growth repression and the H 2 O 2 -induced fluorescence. Our results present the first molecular genetic evidence for the diffusion of H 2 O 2 through specific members of the aquaporin family. The metabolism of aerobic organisms continuously produces reactive oxygen species. Although potentially toxic, these compounds also function in signaling. One important feature of signaling compounds is their ability to move between different compartments, e.g. to cross membranes. Here we present evidence that aquaporins can channel hydrogen peroxide (H(2)O(2)). Twenty-four aquaporins from plants and mammals were screened in five yeast strains differing in sensitivity toward oxidative stress. Expression of human AQP8 and plant Arabidopsis TIP1;1 and TIP1;2 in yeast decreased growth and survival in the presence of H(2)O(2). Further evidence for aquaporin-mediated H(2)O(2) diffusion was obtained by a fluorescence assay with intact yeast cells using an intracellular reactive oxygen species-sensitive fluorescent dye. Application of silver ions (Ag⁺), which block aquaporin-mediated water diffusion in a fast kinetics swelling assay, also reversed both the aquaporin-dependent growth repression and the H(2)O(2)-induced fluorescence. Our results present the first molecular genetic evidence for the diffusion of H(2)O(2) through specific members of the aquaporin family. |
Author | Schjoerring, Jan K. Møller, Anders L.B. Jahn, Thomas P. Kristiansen, Kim A. Schulz, Alexander Møller, Ian M. Bienert, Gerd P. |
Author_xml | – sequence: 1 givenname: Gerd P. surname: Bienert fullname: Bienert, Gerd P. organization: Department of Agricultural Sciences, Faculty of Life Science, Copenhagen University, DK-1871 Frederiksberg C, Denmark – sequence: 2 givenname: Anders L.B. surname: Møller fullname: Møller, Anders L.B. organization: Department of Agricultural Sciences, Faculty of Life Science, Copenhagen University, DK-1871 Frederiksberg C, Denmark – sequence: 3 givenname: Kim A. surname: Kristiansen fullname: Kristiansen, Kim A. organization: Department of Plant Biology, Faculty of Life Science, Copenhagen University, DK-1871 Frederiksberg C, Denmark – sequence: 4 givenname: Alexander surname: Schulz fullname: Schulz, Alexander organization: Department of Plant Biology, Faculty of Life Science, Copenhagen University, DK-1871 Frederiksberg C, Denmark – sequence: 5 givenname: Ian M. surname: Møller fullname: Møller, Ian M. organization: Department of Agricultural Sciences, Faculty of Life Science, Copenhagen University, DK-1871 Frederiksberg C, Denmark – sequence: 6 givenname: Jan K. surname: Schjoerring fullname: Schjoerring, Jan K. organization: Department of Agricultural Sciences, Faculty of Life Science, Copenhagen University, DK-1871 Frederiksberg C, Denmark – sequence: 7 givenname: Thomas P. surname: Jahn fullname: Jahn, Thomas P. email: tpj@kvl.dk organization: Department of Agricultural Sciences, Faculty of Life Science, Copenhagen University, DK-1871 Frederiksberg C, Denmark |
BackLink | https://www.ncbi.nlm.nih.gov/pubmed/17105724$$D View this record in MEDLINE/PubMed |
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SubjectTerms | Animals Aquaporin 1 - genetics Aquaporin 1 - metabolism Aquaporin 2 - genetics Aquaporin 2 - metabolism Aquaporin 3 - genetics Aquaporin 3 - metabolism Aquaporin 4 - genetics Aquaporin 4 - metabolism Aquaporin 5 - genetics Aquaporin 5 - metabolism Aquaporins - genetics Aquaporins - metabolism Arabidopsis Arabidopsis Proteins - genetics Arabidopsis Proteins - metabolism Catalase - metabolism Cell Membrane - metabolism Diffusion Gene Expression Humans Hydrogen Peroxide - pharmacokinetics Microscopy, Confocal Osmosis - physiology Rats Saccharomyces cerevisiae - genetics Saccharomyces cerevisiae - metabolism Silver - pharmacology Spheroplasts - metabolism Transformation, Genetic Water - metabolism |
Title | Specific Aquaporins Facilitate the Diffusion of Hydrogen Peroxide across Membranes |
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