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

  • M Yeste
    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
  • R Morató
    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
  • JE Rodríguez‐Gil
    Unit of Animal Reproduction Department of Animal Medicine and Surgery Faculty of Veterinary Medicine Autonomous University of Barcelona Bellaterra (Cerdanyola del Vallès) Barcelona Spain
  • S Bonet
    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
  • N Prieto‐Martínez
    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

書誌事項

公開日
2017-10
権利情報
  • http://onlinelibrary.wiley.com/termsAndConditions#vor
DOI
  • 10.1111/rda.13082
公開者
Wiley

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説明

<jats:title>Contents</jats:title><jats:p>Aquaporins (<jats:styled-content style="fixed-case">AQP</jats:styled-content>s) play a vital role for the transport of water and solutes across cell membranes. Classification of these ubiquitous proteins into three categories (orthodox <jats:styled-content style="fixed-case">AQP</jats:styled-content>s, aquaglyceroporins and superaquaporins) is based on their sequence similarity and substrate selectivity. In the male reproductive tract of mammals, most <jats:styled-content style="fixed-case">AQP</jats:styled-content>s (except <jats:styled-content style="fixed-case">AQP</jats:styled-content>6 and <jats:styled-content style="fixed-case">AQP</jats:styled-content>12) are found in different organs (including testis, efferent ducts and epididymis). <jats:styled-content style="fixed-case">AQP</jats:styled-content>1 and <jats:styled-content style="fixed-case">AQP</jats:styled-content>9 are the most abundant <jats:styled-content style="fixed-case">AQP</jats:styled-content>s in the efferent ducts and epididymis and play a crucial role for the secretion/reabsorption dynamics of luminal fluid during sperm transport and maturation. <jats:styled-content style="fixed-case">AQP</jats:styled-content>3, <jats:styled-content style="fixed-case">AQP</jats:styled-content>7, <jats:styled-content style="fixed-case">AQP</jats:styled-content>8 and <jats:styled-content style="fixed-case">AQP</jats:styled-content>11 are the most abundant <jats:styled-content style="fixed-case">AQP</jats:styled-content>s in sperm and are involved in the regulation of their volume, which is required for the differentiation of spermatids into spermatozoa during spermatogenesis, as well as in sperm transit along environments of different osmolality (male and female reproductive tracts). While different studies conducted in oocytes and embryos have demonstrated that <jats:styled-content style="fixed-case">AQP</jats:styled-content>s are important for cryotolerance, data in sperm are scarce. At present, mounting evidence indicates that <jats:styled-content style="fixed-case">AQP</jats:styled-content>3, <jats:styled-content style="fixed-case">AQP</jats:styled-content>7 and <jats:styled-content style="fixed-case">AQP</jats:styled-content>11 are involved in the sperm response to variations of osmolality and to freeze‐thawing procedures. All these studies contribute to understand the physiology of both male reproductive tract and sperm, and open up new research ventures on the improvement of sperm cryopreservation protocols.</jats:p>

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