Glutathione Peroxidases at Work on Epididymal Spermatozoa: An Example of the Dual Effect of Reactive Oxygen Species on Mammalian Male Fertilizing Ability
The mammalian glutathione peroxidase (GPx) gene family encodes bifunctional enzymes that can work either as classical reactive oxygen species (ROS) scavengers or as thiol peroxidases, thereby introducing disulfide bridges in thiol‐containing proteins. These dual effects are nowhere better demonstrat...
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| Veröffentlicht in: | Journal of andrology 2011-11, Vol.32 (6), p.641-650 |
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| creator | Noblanc, Anaïs Kocer, Ayhan Chabory, Eléonore Vernet, Patrick Saez, Fabrice Cadet, Rémi Conrad, Marcus Drevet, Joël R. |
| description | The mammalian glutathione peroxidase (GPx) gene family encodes bifunctional enzymes that can work either as classical reactive oxygen species (ROS) scavengers or as thiol peroxidases, thereby introducing disulfide bridges in thiol‐containing proteins. These dual effects are nowhere better demonstrated than in epididymal maturing spermatozoa, where the concomitant actions of several GPx ensure the achievement of the structural maturation of sperm cells as well as their protection against ROS‐induced damage. We review here the roles played by the sperm‐associated forms of GPx4 (mitochondrial GPx4 and nuclear GPx4), the secreted GPx5 protein, and the epithelial proteins GPx1, GPx3, and cellular GPx4, all functioning in the mammalian epididymis at different stages of the sperm's epididymal journey, and in different epididymis compartments. |
| doi_str_mv | 10.2164/jandrol.110.012823 |
| format | Article |
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These dual effects are nowhere better demonstrated than in epididymal maturing spermatozoa, where the concomitant actions of several GPx ensure the achievement of the structural maturation of sperm cells as well as their protection against ROS‐induced damage. We review here the roles played by the sperm‐associated forms of GPx4 (mitochondrial GPx4 and nuclear GPx4), the secreted GPx5 protein, and the epithelial proteins GPx1, GPx3, and cellular GPx4, all functioning in the mammalian epididymis at different stages of the sperm's epididymal journey, and in different epididymis compartments.</description><identifier>ISSN: 0196-3635</identifier><identifier>EISSN: 1939-4640</identifier><identifier>DOI: 10.2164/jandrol.110.012823</identifier><identifier>PMID: 21441427</identifier><identifier>CODEN: JOAND3</identifier><language>eng</language><publisher>Oxford, UK: Blackwell Publishing Ltd</publisher><subject>Animals ; Biochemistry, Molecular Biology ; Biological and medical sciences ; disulfide bridges ; DNA condensation ; DNA oxidation ; Epididymis - enzymology ; Fertilization ; Fundamental and applied biological sciences. Psychology ; genomic stability ; Glutathione Peroxidase - metabolism ; Gynecology. Andrology. Obstetrics ; Humans ; Hydrogen peroxide ; Life Sciences ; lipid peroxidation ; Male ; Male genital diseases ; Mammalian male genital system ; Medical sciences ; Mice ; protamines ; Rats ; Reactive Oxygen Species - metabolism ; Reproductive Biology ; Sperm Maturation ; Spermatozoa - enzymology ; Vertebrates: reproduction</subject><ispartof>Journal of andrology, 2011-11, Vol.32 (6), p.641-650</ispartof><rights>2011 American Society of Andrology</rights><rights>2015 INIST-CNRS</rights><rights>Distributed under a Creative Commons Attribution 4.0 International License</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4157-a20d6368b4eb432de972865e0e269eb61d9a82ede99d929516b66b9cedcef48c3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.2164%2Fjandrol.110.012823$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.2164%2Fjandrol.110.012823$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>230,309,310,314,780,784,789,790,885,1433,23929,23930,25139,27923,27924,46408,46832</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=24723465$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/21441427$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://hal.science/hal-02084936$$DView record in HAL$$Hfree_for_read</backlink></links><search><creatorcontrib>Noblanc, Anaïs</creatorcontrib><creatorcontrib>Kocer, Ayhan</creatorcontrib><creatorcontrib>Chabory, Eléonore</creatorcontrib><creatorcontrib>Vernet, Patrick</creatorcontrib><creatorcontrib>Saez, Fabrice</creatorcontrib><creatorcontrib>Cadet, Rémi</creatorcontrib><creatorcontrib>Conrad, Marcus</creatorcontrib><creatorcontrib>Drevet, Joël R.</creatorcontrib><title>Glutathione Peroxidases at Work on Epididymal Spermatozoa: An Example of the Dual Effect of Reactive Oxygen Species on Mammalian Male Fertilizing Ability</title><title>Journal of andrology</title><addtitle>J Androl</addtitle><description>The mammalian glutathione peroxidase (GPx) gene family encodes bifunctional enzymes that can work either as classical reactive oxygen species (ROS) scavengers or as thiol peroxidases, thereby introducing disulfide bridges in thiol‐containing proteins. These dual effects are nowhere better demonstrated than in epididymal maturing spermatozoa, where the concomitant actions of several GPx ensure the achievement of the structural maturation of sperm cells as well as their protection against ROS‐induced damage. We review here the roles played by the sperm‐associated forms of GPx4 (mitochondrial GPx4 and nuclear GPx4), the secreted GPx5 protein, and the epithelial proteins GPx1, GPx3, and cellular GPx4, all functioning in the mammalian epididymis at different stages of the sperm's epididymal journey, and in different epididymis compartments.</description><subject>Animals</subject><subject>Biochemistry, Molecular Biology</subject><subject>Biological and medical sciences</subject><subject>disulfide bridges</subject><subject>DNA condensation</subject><subject>DNA oxidation</subject><subject>Epididymis - enzymology</subject><subject>Fertilization</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>genomic stability</subject><subject>Glutathione Peroxidase - metabolism</subject><subject>Gynecology. Andrology. Obstetrics</subject><subject>Humans</subject><subject>Hydrogen peroxide</subject><subject>Life Sciences</subject><subject>lipid peroxidation</subject><subject>Male</subject><subject>Male genital diseases</subject><subject>Mammalian male genital system</subject><subject>Medical sciences</subject><subject>Mice</subject><subject>protamines</subject><subject>Rats</subject><subject>Reactive Oxygen Species - metabolism</subject><subject>Reproductive Biology</subject><subject>Sperm Maturation</subject><subject>Spermatozoa - enzymology</subject><subject>Vertebrates: reproduction</subject><issn>0196-3635</issn><issn>1939-4640</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2011</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkc1uEzEUhUcIREPhBVggbxBikeK_8YzZRW3aggJF_Iildcdzp3HxjIM9KUnfhLfFUULZsrpX537nWPIpiueMnnCm5JsbGNoY_AnLAmW85uJBMWFa6KlUkj4sJpRpNRVKlEfFk5RuKOWUVeJxccSZlEzyalL8vvDrEcalCwOSTxjDxrWQMBEYyfcQf5AwkPnKta7d9uDJlxXGHsZwF-AtmeXTBvqVRxI6Mi6RnK0zM-86tONO-oxgR3eL5GqzvcZh57YuZ-fMD9DnPAe7LfvPMY7Ouzs3XJNZk7dx-7R41IFP-Owwj4tv5_Ovp5fTxdXFu9PZYmolK6spcNoqoepGYiMFb1FXvFYlUuRKY6NYq6HmmHXdaq5LphqlGm2xtdjJ2orj4vU-dwnerKLrIW5NAGcuZwuz0_Kv1VILdcsy-2rPrmL4ucY0mt4li97DgGGdTK1VySsqZSb5nrQxpBSxu49m1OzaM4f2TG7P7NvLpheH-HXTY3tv-VtXBl4eAEgWfBdhsC7942TFhVRl5uo998t53P7H0-b97OMZk3Ul_gACdLb1</recordid><startdate>201111</startdate><enddate>201111</enddate><creator>Noblanc, Anaïs</creator><creator>Kocer, Ayhan</creator><creator>Chabory, Eléonore</creator><creator>Vernet, Patrick</creator><creator>Saez, Fabrice</creator><creator>Cadet, Rémi</creator><creator>Conrad, Marcus</creator><creator>Drevet, Joël R.</creator><general>Blackwell Publishing Ltd</general><general>American Society of Andrology</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope><scope>1XC</scope></search><sort><creationdate>201111</creationdate><title>Glutathione Peroxidases at Work on Epididymal Spermatozoa: An Example of the Dual Effect of Reactive Oxygen Species on Mammalian Male Fertilizing Ability</title><author>Noblanc, Anaïs ; Kocer, Ayhan ; Chabory, Eléonore ; Vernet, Patrick ; Saez, Fabrice ; Cadet, Rémi ; Conrad, Marcus ; Drevet, Joël R.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4157-a20d6368b4eb432de972865e0e269eb61d9a82ede99d929516b66b9cedcef48c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2011</creationdate><topic>Animals</topic><topic>Biochemistry, Molecular Biology</topic><topic>Biological and medical sciences</topic><topic>disulfide bridges</topic><topic>DNA condensation</topic><topic>DNA oxidation</topic><topic>Epididymis - enzymology</topic><topic>Fertilization</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>genomic stability</topic><topic>Glutathione Peroxidase - metabolism</topic><topic>Gynecology. Andrology. Obstetrics</topic><topic>Humans</topic><topic>Hydrogen peroxide</topic><topic>Life Sciences</topic><topic>lipid peroxidation</topic><topic>Male</topic><topic>Male genital diseases</topic><topic>Mammalian male genital system</topic><topic>Medical sciences</topic><topic>Mice</topic><topic>protamines</topic><topic>Rats</topic><topic>Reactive Oxygen Species - metabolism</topic><topic>Reproductive Biology</topic><topic>Sperm Maturation</topic><topic>Spermatozoa - enzymology</topic><topic>Vertebrates: reproduction</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Noblanc, Anaïs</creatorcontrib><creatorcontrib>Kocer, Ayhan</creatorcontrib><creatorcontrib>Chabory, Eléonore</creatorcontrib><creatorcontrib>Vernet, Patrick</creatorcontrib><creatorcontrib>Saez, Fabrice</creatorcontrib><creatorcontrib>Cadet, Rémi</creatorcontrib><creatorcontrib>Conrad, Marcus</creatorcontrib><creatorcontrib>Drevet, Joël R.</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>Hyper Article en Ligne (HAL)</collection><jtitle>Journal of andrology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Noblanc, Anaïs</au><au>Kocer, Ayhan</au><au>Chabory, Eléonore</au><au>Vernet, Patrick</au><au>Saez, Fabrice</au><au>Cadet, Rémi</au><au>Conrad, Marcus</au><au>Drevet, Joël R.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Glutathione Peroxidases at Work on Epididymal Spermatozoa: An Example of the Dual Effect of Reactive Oxygen Species on Mammalian Male Fertilizing Ability</atitle><jtitle>Journal of andrology</jtitle><addtitle>J Androl</addtitle><date>2011-11</date><risdate>2011</risdate><volume>32</volume><issue>6</issue><spage>641</spage><epage>650</epage><pages>641-650</pages><issn>0196-3635</issn><eissn>1939-4640</eissn><coden>JOAND3</coden><abstract>The mammalian glutathione peroxidase (GPx) gene family encodes bifunctional enzymes that can work either as classical reactive oxygen species (ROS) scavengers or as thiol peroxidases, thereby introducing disulfide bridges in thiol‐containing proteins. These dual effects are nowhere better demonstrated than in epididymal maturing spermatozoa, where the concomitant actions of several GPx ensure the achievement of the structural maturation of sperm cells as well as their protection against ROS‐induced damage. We review here the roles played by the sperm‐associated forms of GPx4 (mitochondrial GPx4 and nuclear GPx4), the secreted GPx5 protein, and the epithelial proteins GPx1, GPx3, and cellular GPx4, all functioning in the mammalian epididymis at different stages of the sperm's epididymal journey, and in different epididymis compartments.</abstract><cop>Oxford, UK</cop><pub>Blackwell Publishing Ltd</pub><pmid>21441427</pmid><doi>10.2164/jandrol.110.012823</doi><tpages>10</tpages></addata></record> |
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| ispartof | Journal of andrology, 2011-11, Vol.32 (6), p.641-650 |
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| source | MEDLINE; Wiley Free Content; EZB-FREE-00999 freely available EZB journals |
| subjects | Animals Biochemistry, Molecular Biology Biological and medical sciences disulfide bridges DNA condensation DNA oxidation Epididymis - enzymology Fertilization Fundamental and applied biological sciences. Psychology genomic stability Glutathione Peroxidase - metabolism Gynecology. Andrology. Obstetrics Humans Hydrogen peroxide Life Sciences lipid peroxidation Male Male genital diseases Mammalian male genital system Medical sciences Mice protamines Rats Reactive Oxygen Species - metabolism Reproductive Biology Sperm Maturation Spermatozoa - enzymology Vertebrates: reproduction |
| title | Glutathione Peroxidases at Work on Epididymal Spermatozoa: An Example of the Dual Effect of Reactive Oxygen Species on Mammalian Male Fertilizing Ability |
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