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      Aquaporins in the male reproductive tract and sperm: Functional implications and cryobiology

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          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 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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            Aquaporin water channels--from atomic structure to clinical medicine.

            The water permeability of biological membranes has been a longstanding problem in physiology, but the proteins responsible for this remained unknown until discovery of the aquaporin 1 (AQP1) water channel protein. AQP1 is selectively permeated by water driven by osmotic gradients. The atomic structure of human AQP1 has recently been defined. Each subunit of the tetramer contains an individual aqueous pore that permits single-file passage of water molecules but interrupts the hydrogen bonding needed for passage of protons. At least 10 mammalian aquaporins have been identified, and these are selectively permeated by water (aquaporins) or water plus glycerol (aquaglyceroporins). The sites of expression coincide closely with the clinical phenotypes--ranging from congenital cataracts to nephrogenic diabetes insipidus. More than 200 members of the aquaporin family have been found in plants, microbials, invertebrates and vertebrates, and their importance to the physiology of these organisms is being uncovered.
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              The aquaporin water channels.

              Peter Agre (2005)
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                Author and article information

                Journal
                Reproduction in Domestic Animals
                Reprod Dom Anim
                Wiley
                09366768
                October 2017
                October 2017
                October 20 2017
                : 52
                : 12-27
                Affiliations
                [1 ]Biotechnology of Animal and Human Reproduction (TechnoSperm); Unit of Cell Biology; Department of Biology; Institute of Food and Agricultural Technology; Faculty of Sciences; University of Girona; Girona Spain
                [2 ]Unit of Animal Reproduction; Department of Animal Medicine and Surgery; Faculty of Veterinary Medicine; Autonomous University of Barcelona; Bellaterra (Cerdanyola del Vallès) Barcelona Spain
                Article
                10.1111/rda.13082
                29052330
                593bb56b-fe47-40ee-9286-12ada9566b9e
                © 2017

                http://doi.wiley.com/10.1002/tdm_license_1.1

                http://onlinelibrary.wiley.com/termsAndConditions#vor

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