{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,20]],"date-time":"2026-03-20T01:00:51Z","timestamp":1773968451280,"version":"3.50.1"},"reference-count":170,"publisher":"MDPI AG","issue":"3","license":[{"start":{"date-parts":[[2022,2,2]],"date-time":"2022-02-02T00:00:00Z","timestamp":1643760000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100001871","name":"Funda\u00e7\u00e3o para a Ci\u00eancia e Tecnologia","doi-asserted-by":"publisher","award":["UIDB\/50006\/2020"],"award-info":[{"award-number":["UIDB\/50006\/2020"]}],"id":[{"id":"10.13039\/501100001871","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001871","name":"Funda\u00e7\u00e3o para a Ci\u00eancia e Tecnologia","doi-asserted-by":"publisher","award":["UIDB\/00215\/2020"],"award-info":[{"award-number":["UIDB\/00215\/2020"]}],"id":[{"id":"10.13039\/501100001871","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001871","name":"Funda\u00e7\u00e3o para a Ci\u00eancia e Tecnologia","doi-asserted-by":"publisher","award":["UIDP\/00215\/2020"],"award-info":[{"award-number":["UIDP\/00215\/2020"]}],"id":[{"id":"10.13039\/501100001871","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001871","name":"Funda\u00e7\u00e3o para a Ci\u00eancia e Tecnologia","doi-asserted-by":"publisher","award":["LA\/P\/0064\/2020"],"award-info":[{"award-number":["LA\/P\/0064\/2020"]}],"id":[{"id":"10.13039\/501100001871","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001871","name":"Funda\u00e7\u00e3o para a Ci\u00eancia e Tecnologia","doi-asserted-by":"publisher","award":["UI\/BD\/150749\/2020"],"award-info":[{"award-number":["UI\/BD\/150749\/2020"]}],"id":[{"id":"10.13039\/501100001871","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001871","name":"Funda\u00e7\u00e3o para a Ci\u00eancia e Tecnologia","doi-asserted-by":"publisher","award":["SFRH\/BD\/136779\/2018"],"award-info":[{"award-number":["SFRH\/BD\/136779\/2018"]}],"id":[{"id":"10.13039\/501100001871","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Animals"],"abstract":"<jats:p>Cryopreservation is globally used as a method for long-term preservation, although freeze-thawing procedures may strongly impair the gamete function. The correct cryopreservation procedure is characterized by the balance between freezing rate and cryoprotective agents (CPAs), which minimizes cellular dehydration and intracellular ice formation. For this purpose, osmoregulation is a central process in cryopreservation. During cryopreservation, water and small solutes, including penetrating cryoprotective agents, cross the plasma membrane. Aquaporins (AQPs) constitute a family of channel proteins responsible for the transport of water, small solutes, and certain gases across biological membranes. Thirteen homologs of AQPs (AQP0-12) have been described. AQPs are widely distributed throughout the male and female reproductive systems, including the sperm and oocyte membrane. The composition of the male and female gamete membrane is of special interest for assisted reproductive techniques (ART), including cryopreservation. In this review, we detail the mechanisms involved in gamete cryopreservation, including the most used techniques and CPAs. In addition, the expression and function of AQPs in the male and female gametes are explored, highlighting the potential protective role of AQPs against damage induced during cryopreservation.<\/jats:p>","DOI":"10.3390\/ani12030359","type":"journal-article","created":{"date-parts":[[2022,2,3]],"date-time":"2022-02-03T05:42:33Z","timestamp":1643866953000},"page":"359","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":23,"title":["Aquaporins and Animal Gamete Cryopreservation: Advances and Future Challenges"],"prefix":"10.3390","volume":"12","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-1461-8875","authenticated-orcid":false,"given":"Jo\u00e3o C.","family":"Ribeiro","sequence":"first","affiliation":[{"name":"Clinical and Experimental Endocrinology, UMIB\u2014Unit for Multidisciplinary Research in Biomedicine, ICBAS\u2014School of Medicine and Biomedical Sciences, University of Porto, Rua Jorge Viterbo Ferreira 228, 4050-313 Porto, Portugal"},{"name":"QOPNA & LAQV, Department of Chemistry, University of Aveiro, Campus Universit\u00e1rio de Santiago, 3810-193 Aveiro, Portugal"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-0546-3480","authenticated-orcid":false,"given":"David F.","family":"Carrageta","sequence":"additional","affiliation":[{"name":"Clinical and Experimental Endocrinology, UMIB\u2014Unit for Multidisciplinary Research in Biomedicine, ICBAS\u2014School of Medicine and Biomedical Sciences, University of Porto, Rua Jorge Viterbo Ferreira 228, 4050-313 Porto, Portugal"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-1941-6634","authenticated-orcid":false,"given":"Raquel L.","family":"Bernardino","sequence":"additional","affiliation":[{"name":"Clinical and Experimental Endocrinology, UMIB\u2014Unit for Multidisciplinary Research in Biomedicine, ICBAS\u2014School of Medicine and Biomedical Sciences, University of Porto, Rua Jorge Viterbo Ferreira 228, 4050-313 Porto, Portugal"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-7635-783X","authenticated-orcid":false,"given":"Marco G.","family":"Alves","sequence":"additional","affiliation":[{"name":"Clinical and Experimental Endocrinology, UMIB\u2014Unit for Multidisciplinary Research in Biomedicine, ICBAS\u2014School of Medicine and Biomedical Sciences, University of Porto, Rua Jorge Viterbo Ferreira 228, 4050-313 Porto, Portugal"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-4989-5699","authenticated-orcid":false,"given":"Pedro F.","family":"Oliveira","sequence":"additional","affiliation":[{"name":"QOPNA & LAQV, Department of Chemistry, University of Aveiro, Campus Universit\u00e1rio de Santiago, 3810-193 Aveiro, Portugal"}]}],"member":"1968","published-online":{"date-parts":[[2022,2,2]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"268","DOI":"10.3389\/fvets.2019.00268","article-title":"Advances in Cryopreservation of Bull Sperm","volume":"6","author":"Ugur","year":"2019","journal-title":"Front. Vet. Sci."},{"key":"ref_2","first-page":"854837","article-title":"Human Sperm Cryopreservation: Update on Techniques, Effect on DNA Integrity, and Implications for ART","volume":"2012","author":"Tarozzi","year":"2012","journal-title":"Adv. Urol."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1002\/j.1939-4640.2000.tb03268.x","article-title":"Semen cryopreservation in domestic animals: A damaging and capacitating phenomenon","volume":"21","author":"Bailey","year":"2000","journal-title":"J. Androl."},{"key":"ref_4","unstructured":"Spallanzani, L., and Bonnet, C. (1776). Opuscoli di Fisica Animale e Vegetabile, Presso La Societa\u2019 Tipografica."},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"666","DOI":"10.1038\/164666a0","article-title":"Revival of spermatozoa after vitrification and dehydration at low temperatures","volume":"164","author":"Polge","year":"1949","journal-title":"Nature"},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"626","DOI":"10.1038\/169626b0","article-title":"Fertilizing capacity of bull spermatozoa after freezing at \u221279 \u00b0C","volume":"169","author":"Polge","year":"1952","journal-title":"Nature"},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"767","DOI":"10.1038\/172767b0","article-title":"Fertilizing capacity of frozen human spermatozoa","volume":"172","author":"Bunge","year":"1953","journal-title":"Nature"},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"397","DOI":"10.1016\/S0015-0282(16)39678-9","article-title":"Synopsis of the Use of Frozen Human Semen Since 1964: State of the Art of Human Semen Banking","volume":"24","author":"Sherman","year":"1973","journal-title":"Fertil. Steril."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"439","DOI":"10.1016\/0002-9378(64)90499-5","article-title":"In Vivo Survival of Spermatozoa in Cervical Mucus","volume":"88","author":"Perloff","year":"1964","journal-title":"Am. J. Obstet. Gynecol."},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"552","DOI":"10.1111\/j.1439-0531.2008.01240.x","article-title":"Factors affecting the quality of cryopreserved buffalo (Bubalus bubalis) bull spermatozoa","volume":"44","author":"Andrabi","year":"2009","journal-title":"Reprod. Domest. Anim."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"278","DOI":"10.1002\/j.1939-4640.2001.tb02181.x","article-title":"Changes in motion characteristics, plasma membrane integrity, and acrosome morphology during cryopreservation of buffalo spermatozoa","volume":"22","author":"Rasul","year":"2001","journal-title":"J. Androl."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"578","DOI":"10.1016\/S1472-6483(10)61664-1","article-title":"A rational approach to oocyte cryopreservation","volume":"10","author":"Paynter","year":"2005","journal-title":"Reprod. Biomed. Online"},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"49","DOI":"10.1046\/j.1439-0531.2001.00248.x","article-title":"Cryopreservation of embryos of farm animals","volume":"36","author":"Massip","year":"2001","journal-title":"Reprod. Domest. Anim."},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"12","DOI":"10.1016\/j.imr.2016.12.001","article-title":"Cryopreservation and its clinical applications","volume":"6","author":"Jang","year":"2017","journal-title":"Integr. Med. Res."},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"4124","DOI":"10.1039\/b919724a","article-title":"Freezing, melting and structure of ice in a hydrophilic nanopore","volume":"12","author":"Moore","year":"2010","journal-title":"Phys. Chem. Chem. Phys."},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"506","DOI":"10.1038\/nature10586","article-title":"Structural transformation in supercooled water controls the crystallization rate of ice","volume":"479","author":"Moore","year":"2011","journal-title":"Nature"},{"key":"ref_17","doi-asserted-by":"crossref","unstructured":"Estudillo, E., Jimenez, A., Bustamante-Nieves, P.E., Palacios-Reyes, C., Velasco, I., and Lopez-Ornelas, A. (2021). Cryopreservation of Gametes and Embryos and Their Molecular Changes. Int. J. Mol. Sci., 22.","DOI":"10.3390\/ijms221910864"},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"178","DOI":"10.1016\/0011-2240(88)90024-7","article-title":"Manifestations of cell damage after freezing and thawing","volume":"25","author":"McGann","year":"1988","journal-title":"Cryobiology"},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"648684","DOI":"10.3389\/fchem.2021.648684","article-title":"The Feasibility of Antioxidants Avoiding Oxidative Damages from Reactive Oxygen Species in Cryopreservation","volume":"9","author":"Liu","year":"2021","journal-title":"Front. Chem."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"173","DOI":"10.1016\/0011-2240(71)90024-1","article-title":"Cryoprotective agents","volume":"8","author":"Meryman","year":"1971","journal-title":"Cryobiology"},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"287","DOI":"10.1016\/0011-2240(77)90177-8","article-title":"Freezing injury from \u201csolution effects\u201d and its prevention by natural or artificial cryoprotection","volume":"14","author":"Meryman","year":"1977","journal-title":"Cryobiology"},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"265","DOI":"10.1042\/bj0560265","article-title":"The protective action of neutral solutes against haemolysis by freezing and thawing","volume":"56","author":"Lovelock","year":"1954","journal-title":"Biochem. J."},{"key":"ref_23","doi-asserted-by":"crossref","unstructured":"Tharasanit, T., and Thuwanut, P. (2021). Oocyte Cryopreservation in Domestic Animals and Humans: Principles, Techniques and Updated Outcomes. Animals, 11.","DOI":"10.3390\/ani11102949"},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"BSR20191601","DOI":"10.1042\/BSR20191601","article-title":"The roles of reactive oxygen species and antioxidants in cryopreservation","volume":"39","author":"Len","year":"2019","journal-title":"Biosci. Rep."},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"125","DOI":"10.1016\/j.anireprosci.2008.10.002","article-title":"Lipid peroxidation, mitochondrial membrane potential and DNA integrity of spermatozoa in relation to intracellular reactive oxygen species in liquid and frozen-thawed buffalo semen","volume":"114","author":"Kadirvel","year":"2009","journal-title":"Anim. Reprod. Sci."},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"25","DOI":"10.1016\/j.cryobiol.2016.12.008","article-title":"Use of antioxidants reduce lipid peroxidation and improve quality of crossbred rAm. sperm during its cryopreservation","volume":"74","author":"Banday","year":"2017","journal-title":"Cryobiology"},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"95","DOI":"10.1016\/j.theriogenology.2017.01.011","article-title":"Cryopreservation of bull semen is associated with carbonylation of sperm proteins","volume":"92","author":"Mostek","year":"2017","journal-title":"Theriogenology"},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"11","DOI":"10.1016\/j.mrgentox.2019.02.002","article-title":"The comet assay for human biomonitoring: Effect of cryopreservation on DNA damage in different blood cell preparations","volume":"843","author":"Ladeira","year":"2019","journal-title":"Mutat. Res. Genet. Toxicol. Environ. Mutagen."},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"209","DOI":"10.1111\/j.2042-7158.1969.tb08235.x","article-title":"Cryoprotectants\u2014A new class of drugs","volume":"21","author":"Karow","year":"1969","journal-title":"J. Pharm. Pharmacol."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"4729","DOI":"10.1021\/jp111162w","article-title":"Molecular dynamics study of effects of temperature and concentration on hydrogen-bond abilities of ethylene glycol and glycerol: Implications for cryopreservation","volume":"115","author":"Weng","year":"2011","journal-title":"J. Phys. Chem. A"},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"74","DOI":"10.1016\/j.cryobiol.2017.04.004","article-title":"Cryoprotectants: A review of the actions and applications of cryoprotective solutes that modulate cell recovery from ultra-low temperatures","volume":"76","author":"Elliott","year":"2017","journal-title":"Cryobiology"},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"963689721999617","DOI":"10.1177\/0963689721999617","article-title":"Cryopreservation: An Overview of Principles and Cell-Specific Considerations","volume":"30","author":"Whaley","year":"2021","journal-title":"Cell Transpl."},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"367","DOI":"10.1016\/0304-4157(88)90015-9","article-title":"Interactions of sugars with membranes","volume":"947","author":"Crowe","year":"1988","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"76","DOI":"10.1016\/0011-2240(89)90035-7","article-title":"Lipid phase transitions measured in intact cells with Fourier transform infrared spectroscopy","volume":"26","author":"Crowe","year":"1989","journal-title":"Cryobiology"},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"074517","DOI":"10.1115\/1.3156802","article-title":"Effect of Me(2)SO on membrane phase behavior and protein denaturation of human pulmonary endothelial cells studied by in situ FTIR spectroscopy","volume":"131","author":"Spindler","year":"2009","journal-title":"J. Biomech. Eng."},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"95","DOI":"10.3109\/09687688.2012.674161","article-title":"Membrane phase behavior during cooling of stallion sperm and its correlation with freezability","volume":"29","author":"Oldenhof","year":"2012","journal-title":"Mol. Membr. Biol."},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"68","DOI":"10.1095\/biolreprod.112.104661","article-title":"Osmotic stress and membrane phase changes during freezing of stallion sperm: Mode of action of cryoprotective agents","volume":"88","author":"Oldenhof","year":"2013","journal-title":"Biol. Reprod."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"621","DOI":"10.3389\/fcell.2020.00621","article-title":"The Error-Prone Kinetochore-Microtubule Attachments During Meiosis I in Vitrified Oocytes","volume":"8","author":"Gao","year":"2020","journal-title":"Front. Cell Dev. Biol."},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"153","DOI":"10.1093\/biolre\/iox145","article-title":"Meiotic spindle formation in mammalian oocytes: Implications for human infertility","volume":"98","author":"Namgoong","year":"2018","journal-title":"Biol. Reprod."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"313","DOI":"10.1242\/dev.100.2.313","article-title":"The effect of dimethylsulphoxide on the microtubular system of the mouse oocyte","volume":"100","author":"Johnson","year":"1987","journal-title":"Development"},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"960","DOI":"10.1093\/oxfordjournals.humrep.a136826","article-title":"Effect of 1,2-propanediol and dimethylsulphoxide on the meiotic spindle of the mouse oocyte","volume":"3","author":"Jacobs","year":"1988","journal-title":"Hum. Reprod."},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"1101","DOI":"10.1093\/oxfordjournals.humrep.a138201","article-title":"Cryopreservation of mouse and human oocytes using 1,2-propanediol and the configuration of the meiotic spindle","volume":"8","author":"Gook","year":"1993","journal-title":"Hum. Reprod."},{"key":"ref_43","first-page":"375","article-title":"Cryoprotectants: The essential antifreezes to protect life in the frozen state","volume":"25","author":"Fuller","year":"2004","journal-title":"CryoLetters"},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"S54","DOI":"10.1016\/j.cryobiol.2009.07.001","article-title":"Cryopreservation of mammalian oocytes by using sugars: Intra- and extracellular raffinose with small amounts of dimethylsulfoxide yields high cryosurvival, fertilization, and development rates","volume":"60","author":"Eroglu","year":"2010","journal-title":"Cryobiology"},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"918","DOI":"10.1071\/RD12136","article-title":"Optimising vitrification of human oocytes using multiple cryoprotectants and morphological and functional assessment","volume":"25","author":"Seet","year":"2013","journal-title":"Reprod. Fertil. Dev."},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"675","DOI":"10.1262\/jrd.11-066H","article-title":"High developmental rates of mouse oocytes cryopreserved by an optimized vitrification protocol: The effects of cryoprotectants, calcium and cumulus cells","volume":"57","author":"Kohaya","year":"2011","journal-title":"J. Reprod. Dev."},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"1442","DOI":"10.1016\/j.theriogenology.2011.06.014","article-title":"Successful pregnancy following transfer of feline embryos derived from vitrified immature cat oocytes using \u2019stepwise\u2019 cryoprotectant exposure technique","volume":"76","author":"Tharasanit","year":"2011","journal-title":"Theriogenology"},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"11911","DOI":"10.1021\/jp3035538","article-title":"Molecular dynamics simulations of the interactions of DMSO with DPPC and DOPC phospholipid membranes","volume":"116","author":"Hughes","year":"2012","journal-title":"J. Phys. Chem. B"},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"134","DOI":"10.1016\/0003-9861(86)90197-9","article-title":"Effects of three stabilizing agents\u2014Proline, betaine, and trehalose\u2014on membrane phospholipids","volume":"245","author":"Rudolph","year":"1986","journal-title":"Arch. Biochem. Biophys."},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"161","DOI":"10.1095\/biolreprod55.1.161","article-title":"Changes in membrane integrity, cytoskeletal structure, and developmental potential of murine oocytes after vitrification in ethylene glycol","volume":"55","author":"Hotamisligil","year":"1996","journal-title":"Biol. Reprod."},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"145","DOI":"10.1111\/j.1537-2995.1972.tb00001.x","article-title":"A method for freezing and washing red blood cells using a high glycerol concentration","volume":"12","author":"Meryman","year":"1972","journal-title":"Transfusion"},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"1350","DOI":"10.1016\/S0140-6736(51)92800-0","article-title":"In-Vivo Survival of Rabbit\u2019s Red Cells Recovered after Freezing","volume":"257","author":"Sloviter","year":"1951","journal-title":"Lancet"},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"737","DOI":"10.1530\/jrf.0.0950737","article-title":"Osmotic shock of fertilized mouse ova","volume":"95","author":"Oda","year":"1992","journal-title":"J. Reprod. Fertil."},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"40","DOI":"10.1007\/BF01131379","article-title":"Experience with the cryopreservation of human embryos using the mouse as a model to establish successful techniques","volume":"3","author":"Quinn","year":"1986","journal-title":"J. Vitro Fert. Embryo Transf."},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"33","DOI":"10.1007\/BF01131378","article-title":"Cryopreservation and transfer of baboon embryos","volume":"3","author":"Pope","year":"1986","journal-title":"J. In Vitro Fert. Embryo Transf."},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"411","DOI":"10.1093\/humrep\/16.3.411","article-title":"Human oocyte cryopreservation: New perspectives regarding oocyte survival","volume":"16","author":"Fabbri","year":"2001","journal-title":"Hum. Reprod."},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"64","DOI":"10.1016\/S1472-6483(10)60765-1","article-title":"Differential sucrose concentration during dehydration (0.2 mol\/l) and rehydration (0.3 mol\/l) increases the implantation rate of frozen human oocytes","volume":"14","author":"Bianchi","year":"2007","journal-title":"Reprod. Biomed. Online"},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"1771","DOI":"10.1093\/humrep\/del073","article-title":"Sucrose concentration influences the rate of human oocytes with normal spindle and chromosome configurations after slow-cooling cryopreservation","volume":"21","author":"Coticchio","year":"2006","journal-title":"Hum. Reprod."},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"2014.e7","DOI":"10.1016\/j.fertnstert.2008.01.106","article-title":"Blastocyst formation, pregnancy, and birth derived from human oocytes cryopreserved for 5 years","volume":"90","author":"Parmegiani","year":"2008","journal-title":"Fertil. Steril."},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"125","DOI":"10.1038\/233125a0","article-title":"Survival of mouse embryos after freezing and thawing","volume":"233","author":"Whittingham","year":"1971","journal-title":"Nature"},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"39","DOI":"10.1016\/j.theriogenology.2020.01.056","article-title":"Efficient one-step direct transfer to recipients of thawed bovine embryos cultured in vitro and frozen in chemically defined medium","volume":"146","author":"Gomez","year":"2020","journal-title":"Theriogenology"},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1530\/REP-10-0236","article-title":"Current progress in oocyte and embryo cryopreservation by slow freezing and vitrification","volume":"141","author":"Saragusty","year":"2011","journal-title":"Reproduction"},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"187","DOI":"10.1093\/ilar.41.4.187","article-title":"Mechanisms of cryoinjury in living cells","volume":"41","author":"Gao","year":"2000","journal-title":"ILAR J."},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"407","DOI":"10.1016\/0011-2240(84)90079-8","article-title":"Vitrification as an approach to cryopreservation","volume":"21","author":"Fahy","year":"1984","journal-title":"Cryobiology"},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"499","DOI":"10.1530\/jrf.0.0800499","article-title":"Development of mouse embryos cryopreserved by vitrification","volume":"80","author":"Rall","year":"1987","journal-title":"J. Reprod. Fertil."},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"11","DOI":"10.1016\/j.cryobiol.2009.05.007","article-title":"Thermodynamic aspects of vitrification","volume":"60","author":"Wowk","year":"2010","journal-title":"Cryobiology"},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"403","DOI":"10.1007\/s10815-008-9232-3","article-title":"Effects of cryopreservation on sperm parameters and ultrastructural morphology of human spermatozoa","volume":"25","author":"Ozkavukcu","year":"2008","journal-title":"J. Assist. Reprod. Genet."},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"2198","DOI":"10.1016\/j.mex.2019.09.022","article-title":"A simple method of human sperm vitrification","volume":"6","author":"Shah","year":"2019","journal-title":"MethodsX"},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"17","DOI":"10.1186\/s12958-020-00580-5","article-title":"Human sperm vitrification: The state of the art","volume":"18","author":"Tao","year":"2020","journal-title":"Reprod. Biol. Endocrinol."},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"1275","DOI":"10.1016\/0093-691X(94)90247-G","article-title":"Developmental potential of in vitro produced bovine embryos following cryopreservation and single-embryo transfer","volume":"42","author":"Wurth","year":"1994","journal-title":"Theriogenology"},{"key":"ref_71","doi-asserted-by":"crossref","first-page":"147","DOI":"10.1016\/S0093-691X(98)00121-6","article-title":"Transfer of fresh and cryopreserved IVP bovine embryos: Normal calving, birth weight and gestation lengths","volume":"50","author":"Agca","year":"1998","journal-title":"Theriogenology"},{"key":"ref_72","doi-asserted-by":"crossref","first-page":"1147","DOI":"10.1016\/j.theriogenology.2015.11.029","article-title":"A new direct transfer protocol for cryopreserved IVF embryos","volume":"85","author":"Sanches","year":"2016","journal-title":"Theriogenology"},{"key":"ref_73","doi-asserted-by":"crossref","first-page":"594","DOI":"10.1017\/S0967199414000215","article-title":"Comparison of vitrification and conventional freezing for cryopreservation of caprine embryos","volume":"23","author":"Moura","year":"2015","journal-title":"Zygote"},{"key":"ref_74","doi-asserted-by":"crossref","first-page":"1175","DOI":"10.1071\/RD14024","article-title":"Open pulled straw vitrification and slow freezing of sheep IVF embryos using different cryoprotectants","volume":"27","author":"Bhat","year":"2015","journal-title":"Reprod. Fertil. Dev."},{"key":"ref_75","doi-asserted-by":"crossref","first-page":"8","DOI":"10.1016\/j.cryobiol.2017.08.002","article-title":"Embryo survival and birth rate after minimum volume vitrification or slow freezing of in vivo and in vitro produced ovine embryos","volume":"78","author":"Cuadro","year":"2017","journal-title":"Cryobiology"},{"key":"ref_76","doi-asserted-by":"crossref","first-page":"701","DOI":"10.1111\/evj.12341","article-title":"Cellular damage suffered by equine embryos after exposure to cryoprotectants or cryopreservation by slow-freezing or vitrification","volume":"47","author":"Hendriks","year":"2015","journal-title":"Equine Vet. J."},{"key":"ref_77","doi-asserted-by":"crossref","first-page":"11","DOI":"10.1016\/j.theriogenology.2020.05.020","article-title":"Cryopreservation of donkey embryos: Comparison of embryo survival rate after in vitro culture between conventional freezing and vitrification","volume":"154","author":"Fanelli","year":"2020","journal-title":"Theriogenology"},{"key":"ref_78","doi-asserted-by":"crossref","first-page":"329","DOI":"10.1016\/j.anireprosci.2004.07.008","article-title":"Conventional slow freezing, vitrification and open pulled straw (OPS) vitrification of rabbit embryos","volume":"86","author":"Naik","year":"2005","journal-title":"Anim. Reprod. Sci."},{"key":"ref_79","doi-asserted-by":"crossref","first-page":"1328","DOI":"10.1111\/rda.13776","article-title":"Effects of slow freezing and vitrification on embryo development in domestic cat","volume":"55","author":"Mokrousova","year":"2020","journal-title":"Reprod. Domest. Anim."},{"key":"ref_80","doi-asserted-by":"crossref","first-page":"2827","DOI":"10.1093\/humrep\/14.11.2827","article-title":"Comparison of the effects of controlled-rate cryopreservation and vitrification on 2-cell mouse embryos and their subsequent development","volume":"14","author":"Uechi","year":"1999","journal-title":"Hum. Reprod."},{"key":"ref_81","doi-asserted-by":"crossref","first-page":"1091","DOI":"10.1007\/s10815-013-0056-4","article-title":"Slow freezing and vitrification of mouse morula and early blastocysts","volume":"30","author":"Lane","year":"2013","journal-title":"J. Assist. Reprod. Genet."},{"key":"ref_82","doi-asserted-by":"crossref","first-page":"77","DOI":"10.1016\/j.cryobiol.2018.07.005","article-title":"Minimum volume Spatula MVD vitrification method improves embryo survival compared to traditional slow freezing, both for in vivo and in vitro produced mice embryos","volume":"84","author":"Meikle","year":"2018","journal-title":"Cryobiology"},{"key":"ref_83","doi-asserted-by":"crossref","first-page":"15","DOI":"10.1095\/biolreprod.110.083733","article-title":"Production of donor-derived offspring from cryopreserved ovarian tissue in Japanese quail (Coturnix japonica)","volume":"83","author":"Liu","year":"2010","journal-title":"Biol. Reprod."},{"key":"ref_84","doi-asserted-by":"crossref","first-page":"13861","DOI":"10.1038\/s41598-019-50169-1","article-title":"Preservation of zebrafish genetic resources through testis cryopreservation and spermatogonia transplantation","volume":"9","author":"Marinovic","year":"2019","journal-title":"Sci. Rep."},{"key":"ref_85","doi-asserted-by":"crossref","first-page":"37","DOI":"10.1095\/biolreprod.113.110783","article-title":"Subcellular localization of selectively permeable aquaporins in the male germ line of a marine teleost reveals spatial redistribution in activated spermatozoa","volume":"89","author":"Chauvigne","year":"2013","journal-title":"Biol. Reprod."},{"key":"ref_86","doi-asserted-by":"crossref","first-page":"291","DOI":"10.1242\/jeb.52.2.291","article-title":"Water Balance in the Salmon Egg","volume":"52","author":"Loeffler","year":"1970","journal-title":"J. Exp. Biol."},{"key":"ref_87","doi-asserted-by":"crossref","first-page":"15353","DOI":"10.1038\/s41598-019-51696-7","article-title":"Slow freezing versus vitrification for the cryopreservation of zebrafish (Danio rerio) ovarian tissue","volume":"9","author":"Marques","year":"2019","journal-title":"Sci. Rep."},{"key":"ref_88","doi-asserted-by":"crossref","first-page":"291","DOI":"10.1111\/ahe.12197","article-title":"Ultra-Structural Alterations in In Vitro Produced Four-Cell Bovine Embryos Following Controlled Slow Freezing or Vitrification","volume":"45","author":"Cavusoglu","year":"2016","journal-title":"Anat. Histol. Embryol."},{"key":"ref_89","doi-asserted-by":"crossref","first-page":"317","DOI":"10.3109\/19396368.2014.923542","article-title":"Ovarian tissue vitrification is more efficient than slow freezing in protecting oocyte and granulosa cell DNA integrity","volume":"60","author":"Mathias","year":"2014","journal-title":"Syst Biol Reprod Med"},{"key":"ref_90","doi-asserted-by":"crossref","first-page":"229","DOI":"10.1002\/mrd.22018","article-title":"Comparison of DNA apoptosis in mouse and human blastocysts after vitrification and slow freezing","volume":"79","author":"Li","year":"2012","journal-title":"Mol. Reprod. Dev."},{"key":"ref_91","doi-asserted-by":"crossref","first-page":"110","DOI":"10.1016\/j.cryobiol.2020.05.009","article-title":"Gene expression patterns of in vivo-derived sheep blastocysts is more affected by vitrification than slow freezing technique","volume":"95","author":"Brair","year":"2020","journal-title":"Cryobiology"},{"key":"ref_92","doi-asserted-by":"crossref","unstructured":"Pradiee, J., Esteso, M.C., Casta\u00f1o, C., Toledano-D\u00edaz, A., Lopez-Sebasti\u00e1n, A., Guerra, R., and Santiago-Moreno, J. (2017). Conventional slow freezing cryopreserves mouflon spermatozoa better than vitrification. Andrologia, 49.","DOI":"10.1111\/and.12629"},{"key":"ref_93","first-page":"123","article-title":"Comparative effects of slow freezing and vitrification on cryosurvival of spermatozoa obtained from west African dwarf goat bucks","volume":"37","author":"Daramola","year":"2016","journal-title":"CryoLetters"},{"key":"ref_94","doi-asserted-by":"crossref","first-page":"409","DOI":"10.1016\/j.theriogenology.2011.02.016","article-title":"Effect of cryopreservation protocol on postthaw characteristics of stallion sperm","volume":"76","author":"Salazar","year":"2011","journal-title":"Theriogenology"},{"key":"ref_95","doi-asserted-by":"crossref","first-page":"201","DOI":"10.1016\/j.anireprosci.2018.04.069","article-title":"Effect of cooling rate on sperm quality of cryopreserved Andalusian donkey spermatozoa","volume":"193","author":"Bottrel","year":"2018","journal-title":"Anim. Reprod. Sci."},{"key":"ref_96","doi-asserted-by":"crossref","first-page":"396","DOI":"10.30802\/AALAS-JAALAS-20-000028","article-title":"Cryopreservation and Preparation of Thawed Spermatozoa from Rhesus Macaques (Macaca mulatta) for In Vitro Fertilization","volume":"60","author":"Ramsey","year":"2021","journal-title":"J. Am. Assoc. Lab. Anim. Sci."},{"key":"ref_97","doi-asserted-by":"crossref","first-page":"204","DOI":"10.4236\/ojas.2012.23028","article-title":"Comparison of slow freezing and vitrification methods for Venda cockerel\u2019s spermatozoa","volume":"02","author":"Mphaphathi","year":"2012","journal-title":"Open J. Anim. Sci."},{"key":"ref_98","doi-asserted-by":"crossref","first-page":"166039","DOI":"10.1016\/j.bbadis.2020.166039","article-title":"Aquaporins and (in)fertility: More than just water transport","volume":"1867","author":"Ribeiro","year":"2021","journal-title":"Biochim. Biophys. Acta (BBA) Mol. Basis Dis."},{"key":"ref_99","doi-asserted-by":"crossref","first-page":"4278","DOI":"10.1002\/anie.200460804","article-title":"Aquaporin water channels (Nobel Lecture)","volume":"43","author":"Agre","year":"2004","journal-title":"Angew. Chem. Int. Ed. Engl."},{"key":"ref_100","doi-asserted-by":"crossref","first-page":"6718","DOI":"10.4238\/2013.December.13.5","article-title":"Structure, function, and localization of aquaporins: Their possible implications on gamete cryopreservation","volume":"12","author":"Sales","year":"2013","journal-title":"Genet. Mol. Res."},{"key":"ref_101","doi-asserted-by":"crossref","first-page":"1507","DOI":"10.1016\/j.bbagen.2013.10.039","article-title":"The role of mammalian superaquaporins inside the cell","volume":"1840","author":"Ishibashi","year":"2014","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_102","doi-asserted-by":"crossref","first-page":"217","DOI":"10.1016\/j.bbrc.2010.01.104","article-title":"Aquaporin-8-facilitated mitochondrial ammonia transport","volume":"393","author":"Soria","year":"2010","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_103","doi-asserted-by":"crossref","first-page":"108222","DOI":"10.1016\/j.abb.2019.108222","article-title":"Aquaporins and male (in)fertility: Expression and role throughout the male reproductive tract","volume":"679","author":"Carrageta","year":"2020","journal-title":"Arch. Biochem. Biophys."},{"key":"ref_104","doi-asserted-by":"crossref","first-page":"1099","DOI":"10.1071\/RD17340","article-title":"Aquaporin 11 is related to cryotolerance and fertilising ability of frozen-thawed bull spermatozoa","volume":"30","author":"Hidalgo","year":"2018","journal-title":"Reprod. Fertil. Dev."},{"key":"ref_105","doi-asserted-by":"crossref","first-page":"1153","DOI":"10.1111\/andr.12410","article-title":"Relationship of aquaporins 3 (AQP3), 7 (AQP7), and 11 (AQP11) with boar sperm resilience to withstand freeze-thawing procedures","volume":"5","author":"Vilagran","year":"2017","journal-title":"Andrology"},{"key":"ref_106","doi-asserted-by":"crossref","first-page":"312","DOI":"10.1016\/j.cryobiol.2008.09.012","article-title":"Expression and immunodetection of aquaporin 1 (AQP1) in canine spermatozoa","volume":"57","author":"Ito","year":"2008","journal-title":"Cryobiology"},{"key":"ref_107","doi-asserted-by":"crossref","first-page":"323","DOI":"10.1002\/1098-2795(200012)57:4<323::AID-MRD3>3.0.CO;2-5","article-title":"mRNAs encoding aquaporins are present during murine preimplantation development","volume":"57","author":"Offenberg","year":"2000","journal-title":"Mol. Reprod. Dev."},{"key":"ref_108","doi-asserted-by":"crossref","first-page":"93","DOI":"10.1086\/BBLv229n1p93","article-title":"Aquaporin biology of spermatogenesis and sperm physiology in mammals and teleosts","volume":"229","author":"Boj","year":"2015","journal-title":"Biol. Bull."},{"key":"ref_109","doi-asserted-by":"crossref","first-page":"19","DOI":"10.1007\/s10695-012-9608-2","article-title":"Water homeostasis in the fish oocyte: New insights into the role and molecular regulation of a teleost-specific aquaporin","volume":"39","author":"Cerda","year":"2013","journal-title":"Fish Physiol. Biochem."},{"key":"ref_110","doi-asserted-by":"crossref","first-page":"922","DOI":"10.1038\/cr.2010.169","article-title":"Aquaporin3 is a sperm water channel essential for postcopulatory sperm osmoadaptation and migration","volume":"21","author":"Chen","year":"2011","journal-title":"Cell Res."},{"key":"ref_111","doi-asserted-by":"crossref","first-page":"1249","DOI":"10.1071\/RD16077","article-title":"Aquaglyceroporins 3 and 7 in bull spermatozoa: Identification, localisation and their relationship with sperm cryotolerance","volume":"29","author":"Hidalgo","year":"2017","journal-title":"Reprod. Fertil. Dev."},{"key":"ref_112","doi-asserted-by":"crossref","first-page":"171","DOI":"10.1006\/cryo.1999.2228","article-title":"Expression of mRNAs of the aquaporin family in mouse oocytes and embryos","volume":"40","author":"Edashige","year":"2000","journal-title":"Cryobiology"},{"key":"ref_113","doi-asserted-by":"crossref","first-page":"2338","DOI":"10.1093\/humrep\/14.9.2338","article-title":"Permeability characteristics of human oocytes in the presence of the cryoprotectant dimethylsulphoxide","volume":"14","author":"Paynter","year":"1999","journal-title":"Hum. Reprod."},{"key":"ref_114","doi-asserted-by":"crossref","first-page":"9","DOI":"10.1017\/S0967199410000171","article-title":"Effect of maturation on the expression of aquaporin 3 in mouse oocyte","volume":"19","author":"Jo","year":"2011","journal-title":"Zygote"},{"key":"ref_115","doi-asserted-by":"crossref","first-page":"17741","DOI":"10.1038\/srep17741","article-title":"Aquaporin7 plays a crucial role in tolerance to hyperosmotic stress and in the survival of oocytes during cryopreservation","volume":"5","author":"Tan","year":"2015","journal-title":"Sci. Rep."},{"key":"ref_116","doi-asserted-by":"crossref","first-page":"649","DOI":"10.1159\/000350084","article-title":"Expression of aquaporins in human embryos and potential role of AQP3 and AQP7 in preimplantation mouse embryo development","volume":"31","author":"Xiong","year":"2013","journal-title":"Cell Physiol. Biochem."},{"key":"ref_117","doi-asserted-by":"crossref","first-page":"342","DOI":"10.1016\/S0012-1606(02)00127-6","article-title":"Aquaporin proteins in murine trophectoderm mediate transepithelial water movements during cavitation","volume":"256","author":"Barcroft","year":"2003","journal-title":"Dev. Biol."},{"key":"ref_118","doi-asserted-by":"crossref","first-page":"1121","DOI":"10.1369\/jhc.2008.951947","article-title":"Membrane domain specificity in the spatial distribution of aquaporins 5, 7, 9, and 11 in efferent ducts and epididymis of rats","volume":"56","author":"Hermo","year":"2008","journal-title":"J. Histochem. Cytochem."},{"key":"ref_119","doi-asserted-by":"crossref","first-page":"162","DOI":"10.1016\/j.theriogenology.2016.11.011","article-title":"Associations of hypoosmotic swelling test, relative sperm volume shift, aquaporin7 mRNA abundance and bull fertility estimates","volume":"89","author":"Kasimanickam","year":"2017","journal-title":"Theriogenology"},{"key":"ref_120","doi-asserted-by":"crossref","first-page":"F956","DOI":"10.1152\/ajprenal.00314.2006","article-title":"AQP7 is localized in capillaries of adipose tissue, cardiac and striated muscle: Implications in glycerol metabolism","volume":"292","author":"Skowronski","year":"2007","journal-title":"Am. J. Physiol. Renal Physiol."},{"key":"ref_121","doi-asserted-by":"crossref","first-page":"665","DOI":"10.1111\/rda.12728","article-title":"Membrane Stress During Thawing Elicits Redistribution of Aquaporin 7 But Not of Aquaporin 9 in Boar Spermatozoa","volume":"51","author":"Ekwall","year":"2016","journal-title":"Reprod. Domest. Anim."},{"key":"ref_122","doi-asserted-by":"crossref","first-page":"61","DOI":"10.1111\/rda.13059","article-title":"First evidence for the presence of aquaporins in stallion sperm","volume":"52","author":"Noto","year":"2017","journal-title":"Reprod. Domest. Anim."},{"key":"ref_123","doi-asserted-by":"crossref","first-page":"915","DOI":"10.1369\/jhc.2009.954057","article-title":"Immunolocalization of aquaporin-1, -5, and -7 in the avian testis and vas deferens","volume":"57","author":"Skowronski","year":"2009","journal-title":"J. Histochem. Cytochem."},{"key":"ref_124","doi-asserted-by":"crossref","first-page":"350","DOI":"10.1095\/biolreprod.108.071928","article-title":"Aquaporin isoforms involved in physiological volume regulation of murine spermatozoa","volume":"80","author":"Yeung","year":"2009","journal-title":"Biol. Reprod."},{"key":"ref_125","first-page":"63","article-title":"Canine sperm cells express aquaporin-8, but not aquaporin-2","volume":"54","author":"Santiago","year":"2019","journal-title":"Reprod. Domest. Anim."},{"key":"ref_126","doi-asserted-by":"crossref","first-page":"117","DOI":"10.1016\/S1534-5807(03)00373-3","article-title":"Dynamics of global gene expression changes during mouse preimplantation development","volume":"6","author":"Hamatani","year":"2004","journal-title":"Dev. Cell"},{"key":"ref_127","doi-asserted-by":"crossref","first-page":"7789","DOI":"10.1038\/srep07789","article-title":"Mitochondrial aquaporin-8-mediated hydrogen peroxide transport is essential for teleost spermatozoon motility","volume":"5","author":"Chauvigne","year":"2015","journal-title":"Sci. Rep."},{"key":"ref_128","doi-asserted-by":"crossref","first-page":"151","DOI":"10.1007\/s002320001084","article-title":"Water permeability in rat oocytes at different maturity stages: Aquaporin-9 expression","volume":"176","author":"Ford","year":"2000","journal-title":"J. Membr. Biol."},{"key":"ref_129","doi-asserted-by":"crossref","first-page":"880","DOI":"10.1095\/biolreprod.109.077933","article-title":"Evidence for the involvement of aquaporins in sperm motility activation of the teleost gilthead sea bream (Sparus aurata)","volume":"81","author":"Zilli","year":"2009","journal-title":"Biol. Reprod."},{"key":"ref_130","doi-asserted-by":"crossref","first-page":"663","DOI":"10.1071\/RD14237","article-title":"Aquaporins 7 and 11 in boar spermatozoa: Detection, localisation and relationship with sperm quality","volume":"28","author":"Vilagran","year":"2016","journal-title":"Reprod. Fertil. Dev."},{"key":"ref_131","doi-asserted-by":"crossref","first-page":"209","DOI":"10.1530\/REP-09-0298","article-title":"Aquaporin AQP11 in the testis: Molecular identity and association with the processing of residual cytoplasm of elongated spermatids","volume":"139","author":"Yeung","year":"2010","journal-title":"Reproduction"},{"key":"ref_132","doi-asserted-by":"crossref","first-page":"422","DOI":"10.1002\/mrd.20306","article-title":"Functional challenge affects aquaporin mRNA abundance in mouse blastocysts","volume":"71","author":"Offenberg","year":"2005","journal-title":"Mol. Reprod. Dev."},{"key":"ref_133","doi-asserted-by":"crossref","first-page":"109","DOI":"10.1016\/j.cryobiol.2003.08.003","article-title":"Cryopreservation of canine spermatozoa: Theoretical prediction of optimal cooling rates in the presence and absence of cryoprotective agents","volume":"47","author":"Thirumala","year":"2003","journal-title":"Cryobiology"},{"key":"ref_134","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.cellbi.2005.06.004","article-title":"Sperm motility in fishes. (II) Effects of ions and osmolality: A review","volume":"30","author":"Alavi","year":"2006","journal-title":"Cell Biol. Int."},{"key":"ref_135","doi-asserted-by":"crossref","first-page":"671","DOI":"10.1016\/j.fertnstert.2006.07.1522","article-title":"Morphologic and functional analysis of sperm and testes in Aquaporin 7 knockout mice","volume":"87","author":"Sohara","year":"2007","journal-title":"Fertil. Steril."},{"key":"ref_136","doi-asserted-by":"crossref","first-page":"142","DOI":"10.1038\/178142b0","article-title":"Metabolism of glycerol, sorbitol and related compounds by spermatozoa","volume":"178","author":"Mann","year":"1956","journal-title":"Nature"},{"key":"ref_137","doi-asserted-by":"crossref","first-page":"279","DOI":"10.1007\/s004410051234","article-title":"Immunohistochemical localization of a water channel, aquaporin 7 (AQP7), in the rat testis","volume":"295","author":"Ishibashi","year":"1999","journal-title":"Cell Tissue Res."},{"key":"ref_138","doi-asserted-by":"crossref","first-page":"1660","DOI":"10.1095\/biolreprod64.6.1660","article-title":"Expression and localization of the aquaporin-8 water channel in rat testis","volume":"64","author":"Calamita","year":"2001","journal-title":"Biol. Reprod."},{"key":"ref_139","doi-asserted-by":"crossref","first-page":"490","DOI":"10.1038\/aja.2010.40","article-title":"Aquaporins in spermatozoa and testicular germ cells: Identification and potential role","volume":"12","author":"Yeung","year":"2010","journal-title":"Asian J. Androl."},{"key":"ref_140","doi-asserted-by":"crossref","first-page":"e2019346118","DOI":"10.1073\/pnas.2019346118","article-title":"A multiplier peroxiporin signal transduction pathway powers piscine spermatozoa","volume":"118","author":"Chauvigne","year":"2021","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_141","doi-asserted-by":"crossref","unstructured":"Laforenza, U., Pellavio, G., Marchetti, A.L., Omes, C., Todaro, F., and Gastaldi, G. (2016). Aquaporin-Mediated Water and Hydrogen Peroxide Transport Is Involved in Normal Human Spermatozoa Functioning. Int. J. Mol. Sci., 18.","DOI":"10.3390\/ijms18010066"},{"key":"ref_142","doi-asserted-by":"crossref","first-page":"12","DOI":"10.1111\/rda.13082","article-title":"Aquaporins in the male reproductive tract and sperm: Functional implications and cryobiology","volume":"52","author":"Yeste","year":"2017","journal-title":"Reprod. Domest. Anim."},{"key":"ref_143","doi-asserted-by":"crossref","first-page":"327","DOI":"10.1262\/jrd.2017-166","article-title":"Expression and localization of aquaporins 3 and 7 in bull spermatozoa and their relevance to sperm motility after cryopreservation","volume":"64","author":"Fujii","year":"2018","journal-title":"J. Reprod. Dev."},{"key":"ref_144","doi-asserted-by":"crossref","first-page":"77","DOI":"10.1186\/s40104-019-0388-8","article-title":"Aquaglyceroporins but not orthodox aquaporins are involved in the cryotolerance of pig spermatozoa","volume":"10","author":"Llavanera","year":"2019","journal-title":"J. Anim. Sci. Biotechnol."},{"key":"ref_145","doi-asserted-by":"crossref","unstructured":"Delgado-Bermudez, A., Noto, F., Bonilla-Correal, S., Garcia-Bonavila, E., Catalan, J., Papas, M., Bonet, S., Miro, J., and Yeste, M. (2019). Cryotolerance of Stallion Spermatozoa Relies on Aquaglyceroporins rather than Orthodox Aquaporins. Biology, 8.","DOI":"10.3390\/biology8040085"},{"key":"ref_146","doi-asserted-by":"crossref","unstructured":"Delgado-Bermudez, A., Llavanera, M., Recuero, S., Mateo-Otero, Y., Bonet, S., Barranco, I., Fernandez-Fuertes, B., and Yeste, M. (2019). Effect of AQP Inhibition on Boar Sperm Cryotolerance Depends on the Intrinsic Freezability of the Ejaculate. Int. J. Mol. Sci., 20.","DOI":"10.3390\/ijms20246255"},{"key":"ref_147","doi-asserted-by":"crossref","first-page":"17149","DOI":"10.1074\/jbc.C400595200","article-title":"The inner mitochondrial membrane has aquaporin-8 water channels and is highly permeable to water","volume":"280","author":"Calamita","year":"2005","journal-title":"J. Biol. Chem."},{"key":"ref_148","doi-asserted-by":"crossref","first-page":"70","DOI":"10.1086\/BBLv229n1p70","article-title":"Water transport and functional dynamics of aquaporins in osmoregulatory organs of fishes","volume":"229","author":"Madsen","year":"2015","journal-title":"Biol. Bull"},{"key":"ref_149","doi-asserted-by":"crossref","first-page":"149","DOI":"10.1007\/978-94-024-1057-0_10","article-title":"The Physiological Role and Regulation of Aquaporins in Teleost Germ Cells","volume":"969","author":"Cerda","year":"2017","journal-title":"Adv. Exp. Med. Biol."},{"key":"ref_150","doi-asserted-by":"crossref","first-page":"71","DOI":"10.1186\/1477-7827-9-71","article-title":"Expression and localization of aquaporin 1b during oocyte development in the Japanese eel (Anguilla japonica)","volume":"9","author":"Kagawa","year":"2011","journal-title":"Reprod. Biol. Endocrinol."},{"key":"ref_151","doi-asserted-by":"crossref","first-page":"250","DOI":"10.1016\/j.ydbio.2006.03.034","article-title":"Yolk proteolysis and aquaporin-1o play essential roles to regulate fish oocyte hydration during meiosis resumption","volume":"295","author":"Fabra","year":"2006","journal-title":"Dev. Biol."},{"key":"ref_152","doi-asserted-by":"crossref","first-page":"3151","DOI":"10.1093\/molbev\/msr146","article-title":"Dual neofunctionalization of a rapidly evolving aquaporin-1 paralog resulted in constrained and relaxed traits controlling channel function during meiosis resumption in teleosts","volume":"28","author":"Zapater","year":"2011","journal-title":"Mol. Biol. Evol."},{"key":"ref_153","doi-asserted-by":"crossref","first-page":"545","DOI":"10.1126\/science.1106305","article-title":"Marine fish egg hydration is aquaporin-mediated","volume":"307","author":"Fabra","year":"2005","journal-title":"Science"},{"key":"ref_154","doi-asserted-by":"crossref","first-page":"752","DOI":"10.1002\/jez.560","article-title":"Oocyte hydration in the Japanese eel (Anguilla japonica) during meiosis resumption and ovulation","volume":"311","author":"Kagawa","year":"2009","journal-title":"J. Exp. Zool. A Ecol. Genet. Physiol."},{"key":"ref_155","doi-asserted-by":"crossref","unstructured":"Tingaud-Sequeira, A., Chauvigne, F., Fabra, M., Lozano, J., Raldua, D., and Cerda, J. (2008). Structural and functional divergence of two fish aquaporin-1 water channels following teleost-specific gene duplication. BMC Evol. Biol., 8.","DOI":"10.1186\/1471-2148-8-259"},{"key":"ref_156","doi-asserted-by":"crossref","first-page":"162","DOI":"10.1016\/j.ygcen.2010.10.002","article-title":"Molecular and functional characterization of catfish (Heteropneustes fossilis) aquaporin-1b: Changes in expression during ovarian development and hormone-induced follicular maturation","volume":"170","author":"Chaube","year":"2011","journal-title":"Gen. Comp. Endocrinol."},{"key":"ref_157","doi-asserted-by":"crossref","first-page":"504","DOI":"10.1016\/j.ygcen.2010.02.020","article-title":"An involvement of vasotocin in oocyte hydration in the catfish Heteropneustes fossilis: A comparison with effects of isotocin and hCG","volume":"166","author":"Singh","year":"2010","journal-title":"Gen. Comp. Endocrinol."},{"key":"ref_158","doi-asserted-by":"crossref","first-page":"272","DOI":"10.1093\/humupd\/dmq036","article-title":"Dynamic changes in gene expression during human early embryo development: From fundamental aspects to clinical applications","volume":"17","author":"Assou","year":"2011","journal-title":"Hum. Reprod. Update"},{"key":"ref_159","doi-asserted-by":"crossref","first-page":"36","DOI":"10.1002\/rmb2.12007","article-title":"Permeability of the plasma membrane to water and cryoprotectants in mammalian oocytes and embryos: Its relevance to vitrification","volume":"16","author":"Edashige","year":"2017","journal-title":"Reprod. Med. Biol."},{"key":"ref_160","doi-asserted-by":"crossref","first-page":"625","DOI":"10.1095\/biolreprod.105.045823","article-title":"Channel-dependent permeation of water and glycerol in mouse morulae","volume":"74","author":"Edashige","year":"2006","journal-title":"Biol. Reprod."},{"key":"ref_161","doi-asserted-by":"crossref","first-page":"365","DOI":"10.1095\/biolreprod.106.059261","article-title":"The role of aquaporin 3 in the movement of water and cryoprotectants in mouse morulae","volume":"77","author":"Edashige","year":"2007","journal-title":"Biol. Reprod."},{"key":"ref_162","doi-asserted-by":"crossref","first-page":"87","DOI":"10.1095\/biolreprod.112.107250","article-title":"Rapid movement of water and cryoprotectants in pig expanded blastocysts via channel processes: Its relevance to their higher tolerance to cryopreservation","volume":"89","author":"Jin","year":"2013","journal-title":"Biol. Reprod."},{"key":"ref_163","doi-asserted-by":"crossref","first-page":"834","DOI":"10.1095\/biolreprod.110.088641","article-title":"Pathway for the movement of water and cryoprotectants in bovine oocytes and embryos","volume":"85","author":"Jin","year":"2011","journal-title":"Biol. Reprod."},{"key":"ref_164","doi-asserted-by":"crossref","first-page":"87","DOI":"10.1095\/biolreprod.101.002394","article-title":"Artificial expression of aquaporin-3 improves the survival of mouse oocytes after cryopreservation","volume":"68","author":"Edashige","year":"2003","journal-title":"Biol. Reprod."},{"key":"ref_165","doi-asserted-by":"crossref","first-page":"450","DOI":"10.1002\/mrd.22310","article-title":"Enhanced water and cryoprotectant permeability of porcine oocytes after artificial expression of human and zebrafish aquaporin-3 channels","volume":"81","author":"Morato","year":"2014","journal-title":"Mol. Reprod. Dev."},{"key":"ref_166","doi-asserted-by":"crossref","first-page":"839","DOI":"10.1017\/S0967199416000174","article-title":"Expression of the T85A mutant of zebrafish aquaporin 3b improves post-thaw survival of cryopreserved early mammalian embryos","volume":"24","author":"Chauvigne","year":"2016","journal-title":"Zygote"},{"key":"ref_167","doi-asserted-by":"crossref","first-page":"160","DOI":"10.1016\/j.cryobiol.2006.05.003","article-title":"Expression of aquaporin-3 improves the permeability to water and cryoprotectants of immature oocytes in the medaka (Oryzias latipes)","volume":"53","author":"Valdez","year":"2006","journal-title":"Cryobiology"},{"key":"ref_168","doi-asserted-by":"crossref","unstructured":"Chauvigne, F., Lubzens, E., and Cerda, J. (2011). Design and characterization of genetically engineered zebrafish aquaporin-3 mutants highly permeable to the cryoprotectant ethylene glycol. BMC Biotechnol., 11.","DOI":"10.1186\/1472-6750-11-34"},{"key":"ref_169","doi-asserted-by":"crossref","first-page":"67","DOI":"10.1085\/jgp.106.1.67","article-title":"The relationship between membrane fluidity and permeabilities to water, solutes, ammonia, and protons","volume":"106","author":"Lande","year":"1995","journal-title":"J. Gen. Physiol."},{"key":"ref_170","doi-asserted-by":"crossref","first-page":"2160","DOI":"10.1093\/humrep\/15.10.2160","article-title":"Membrane fluidity predicts the outcome of cryopreservation of human spermatozoa","volume":"15","author":"Giraud","year":"2000","journal-title":"Hum. Reprod."}],"container-title":["Animals"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/2076-2615\/12\/3\/359\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,10]],"date-time":"2025-10-10T22:12:51Z","timestamp":1760134371000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/2076-2615\/12\/3\/359"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2022,2,2]]},"references-count":170,"journal-issue":{"issue":"3","published-online":{"date-parts":[[2022,2]]}},"alternative-id":["ani12030359"],"URL":"https:\/\/doi.org\/10.3390\/ani12030359","relation":{},"ISSN":["2076-2615"],"issn-type":[{"value":"2076-2615","type":"electronic"}],"subject":[],"published":{"date-parts":[[2022,2,2]]}}}