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During spermatogenesis and the epididymal maturation, the spermatozoon acquires antioxidant enzymes needed to face possible increases of reactive oxygen species (\n                      <jats:styled-content style=\"fixed-case\">ROS<\/jats:styled-content>\n                      ) produced by its own aerobic metabolism but also due to\n                      <jats:styled-content style=\"fixed-case\">ROS<\/jats:styled-content>\n                      produced in high quantities by abnormal spermatozoa.\n                    <\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Objectives<\/jats:title>\n                    <jats:p>Provide an up\u2010to\u2010date review of the enzymatic antioxidant system in the epididymis.<\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Material and methods<\/jats:title>\n                    <jats:p>A thorough literature review was performed for papers concerning the players of the antioxidant defenses in the epididymis.<\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Results<\/jats:title>\n                    <jats:p>\n                      The antioxidant system in the epididymis is composed by superoxide dismutases, catalase, glutathione peroxidases, peroxiredoxins, glutathione\u2010S\u2010transferases, thioredoxins and thioredoxin reductase. They work together to maintain low levels of\n                      <jats:styled-content style=\"fixed-case\">ROS<\/jats:styled-content>\n                      during the epididymal maturation. Knockout models revealed that the absence of one of the enzyme impact sperm quality affecting a variety of proteins involved in motility, the ability to fertilize oocyte, and promotes oxidative damage to the sperm\n                      <jats:styled-content style=\"fixed-case\">DNA<\/jats:styled-content>\n                      .\n                    <\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Discussion and conclusions<\/jats:title>\n                    <jats:p>These findings suggest that each enzyme is playing a specific role, and in most of the cases, no compensatory mechanisms are put in place when one enzyme is absent. This review highlights the different antioxidant enzymes in the epididymis and their role during maturation of the spermatozoon.<\/jats:p>\n                  <\/jats:sec>","DOI":"10.1111\/andr.12630","type":"journal-article","created":{"date-parts":[[2019,5,2]],"date-time":"2019-05-02T01:11:52Z","timestamp":1556759512000},"page":"662-668","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":88,"title":["Orchestrating the antioxidant defenses in the epididymis"],"prefix":"10.1111","volume":"7","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-8884-1274","authenticated-orcid":false,"given":"C.","family":"O'Flaherty","sequence":"first","affiliation":[{"name":"Departments of Surgery (Urology Division) and Pharmacology and Therapeutics McGill University Montr\u00e9al QC Canada"},{"name":"The Research Institute of the McGill University Health Centre Montr\u00e9al QC Canada"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2019,5]]},"reference":[{"key":"e_1_2_4_2_1","doi-asserted-by":"publisher","DOI":"10.1016\/0891-5849(96)00119-0"},{"key":"e_1_2_4_3_1","doi-asserted-by":"publisher","DOI":"10.4103\/1008-682X.122203"},{"key":"e_1_2_4_4_1","doi-asserted-by":"publisher","DOI":"10.1007\/978-1-61779-776-7_6"},{"key":"e_1_2_4_5_1","doi-asserted-by":"publisher","DOI":"10.1093\/humrep\/15.6.1338"},{"key":"e_1_2_4_6_1","doi-asserted-by":"publisher","DOI":"10.2527\/jas.2009-2583"},{"key":"e_1_2_4_7_1","first-page":"2074","article-title":"Epididymis seleno\u2010independent glutathione peroxidase 5 maintains sperm DNA integrity in mice","volume":"119","author":"Chabory E","year":"2009","journal-title":"J Clin Invest"},{"key":"e_1_2_4_8_1","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M005073200"},{"key":"e_1_2_4_9_1","doi-asserted-by":"publisher","DOI":"10.1128\/MCB.25.17.7637-7644.2005"},{"key":"e_1_2_4_10_1","doi-asserted-by":"publisher","DOI":"10.4103\/1008-682X.175097"},{"key":"e_1_2_4_11_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.reprotox.2018.08.013"},{"key":"e_1_2_4_12_1","doi-asserted-by":"publisher","DOI":"10.1007\/s10815-013-0015-0"},{"key":"e_1_2_4_13_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.febslet.2004.06.080"},{"key":"e_1_2_4_14_1","first-page":"559","article-title":"Structural organization, chromosomal localization, expression and phylogenetic evaluation of mouse glutathione peroxidase encoding genes","volume":"319","author":"Dufaure JP","year":"1996","journal-title":"C R Acad Sci III"},{"key":"e_1_2_4_15_1","doi-asserted-by":"publisher","DOI":"10.1093\/humrep\/dey221"},{"key":"e_1_2_4_16_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.abb.2016.12.003"},{"key":"e_1_2_4_17_1","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.274.30.21326"},{"key":"e_1_2_4_18_1","first-page":"292","article-title":"A novel lysophosphatidylcholine acyl transferase activity is expressed by peroxiredoxin 6","volume":"31","author":"Fisher AB","year":"2016","journal-title":"J Lipid Res"},{"key":"e_1_2_4_19_1","doi-asserted-by":"publisher","DOI":"10.1095\/biolreprod.102.003822"},{"key":"e_1_2_4_20_1","doi-asserted-by":"publisher","DOI":"10.1095\/biolreprod.109.082438"},{"key":"e_1_2_4_21_1","doi-asserted-by":"publisher","DOI":"10.1210\/me.7.2.258"},{"key":"e_1_2_4_22_1","doi-asserted-by":"publisher","DOI":"10.1111\/j.1365-2605.2011.01203.x"},{"key":"e_1_2_4_23_1","doi-asserted-by":"publisher","DOI":"10.2164\/jandrol.111.016162"},{"key":"e_1_2_4_24_1","doi-asserted-by":"publisher","DOI":"10.1071\/RD9950731"},{"key":"e_1_2_4_25_1","first-page":"61","volume-title":"Current topics in Developmental Biology","author":"Hinton BT","year":"1996"},{"key":"e_1_2_4_26_1","doi-asserted-by":"publisher","DOI":"10.1007\/978-3-319-18881-2_4"},{"key":"e_1_2_4_27_1","doi-asserted-by":"publisher","DOI":"10.1093\/nass\/44.1.139"},{"key":"e_1_2_4_28_1","doi-asserted-by":"publisher","DOI":"10.1038\/aja.2013.92"},{"key":"e_1_2_4_29_1","doi-asserted-by":"publisher","DOI":"10.2164\/jandrol.106.000265"},{"key":"e_1_2_4_30_1","doi-asserted-by":"crossref","first-page":"368","DOI":"10.1002\/j.1939-4640.1992.tb03327.x","article-title":"Reactive oxygen species and human spermatozoa. 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