E. F. Adolph, Uptakes and uses of oxygen, from gametes to maturity: An overview, Respiration Physiology, vol.53, issue.2, 1983.
DOI : 10.1016/0034-5687(83)90063-4

Y. M. Ahn, Y. J. Kim, H. Park, B. Park, and H. Lee, Prenatal Vitamin C Status is Associated with Placental Apoptosis in Normal-term Human Pregnancies, Placenta, vol.28, issue.1, pp.31-39, 2007.
DOI : 10.1016/j.placenta.2006.01.018

M. Alfalah, R. Jacob, U. Preuss, K. P. Zimmer, H. Naim et al., O-linked glycans mediate apical sorting of human intestinal sucrase-isomaltase through association with lipid rafts, Current Biology, vol.9, issue.11, pp.593-599, 1999.
DOI : 10.1016/S0960-9822(99)80263-2

S. R. Allen, Epidemiology of Premature Rupture of the Fetal Membranes, Clinical Obstetrics and Gynecology, vol.34, issue.4, pp.685-93, 1991.
DOI : 10.1097/00003081-199112000-00004

Y. Atiya-nasagi, H. Cohen, O. Medalia, M. Fukudan, and R. Sagi-eisenberg, O-glycosylation is essential for intracellular targeting of synaptotagmins I and II in non-neuronal specialized secretory cells, Journal of Cell Science, vol.118, issue.7, pp.1363-72, 2005.
DOI : 10.1242/jcs.01710

M. Avgil and A. Ornoy, Herpes simplex virus and Epstein-Barr virus infections in pregnancy: consequences of neonatal or intrauterine infection, Reproductive Toxicology, vol.21, issue.4, pp.436-481, 2006.
DOI : 10.1016/j.reprotox.2004.11.014

J. M. Bedford and H. I. Calvin, The occurrence and possible functional significance of ?S-Scross-links in sperm heads, with particular reference to eutherian mammals, J Exp Zool, vol.187, pp.137-156, 1974.

J. M. Bedford and H. J. Calvin, Changes in ???S???S??? linked structures of the sperm tail during epididymal maturation, with comparative observations in sub-mammalian species, Journal of Experimental Zoology, vol.14, issue.2, pp.181-204, 1974.
DOI : 10.1002/jez.1401870202

S. Benoff, Carbohydrates and fertilization: an overview, Molecular Human Reproduction, vol.3, issue.7, pp.599-637, 1997.
DOI : 10.1093/molehr/3.7.599
URL : http://molehr.oxfordjournals.org/cgi/content/short/3/7/599

M. J. Berry, L. Banu, J. W. Harney, and P. R. Larsen, Functional characterization of the eukaryotic SECIS elements which direct selenocysteine insertion at UGA codons, EMBO J, vol.12, pp.3315-3337, 1993.

M. J. Berry, J. W. Harney, T. Ohama, and D. L. Hatfield, Selenocysteine insertion or termination: factors affecting UGA codon fate and complementary anticodon:codon mutations, Nucleic Acids Research, vol.22, issue.18, pp.3753-3762, 1994.
DOI : 10.1093/nar/22.18.3753
URL : http://doi.org/10.1093/nar/22.18.3753

A. Borchert, N. E. Savaskan, and H. Kuhn, Regulation of Expression of the Phospholipid Hydroperoxide/Sperm Nucleus Glutathione Peroxidase Gene. TISSUE-SPECIFIC EXPRESSION PATTERN AND IDENTIFICATION OF FUNCTIONAL CIS- AND TRANS-REGULATORY ELEMENTS, Journal of Biological Chemistry, vol.278, issue.4, pp.2571-80, 2003.
DOI : 10.1074/jbc.M209064200

M. M. Bradford, A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding, Analytical Biochemistry, vol.72, issue.1-2, pp.248-54, 1976.
DOI : 10.1016/0003-2697(76)90527-3

D. Brown, B. D. Yu, N. Joza, P. Bénit, J. Meneses et al., Loss of Aif function causes cell death in the mouse embryo, but the temporal progression of patterning is normal, Proceedings of the National Academy of Sciences, vol.103, issue.26, pp.9918-9941, 2006.
DOI : 10.1073/pnas.0603950103

H. G. Burkitt, B. Young, and J. W. Heath, Le tube digestif, Histologie Fonctionnelle Wheater, 1995.

E. Muller, J. L. Ravanat, and S. Sauvaigo, Recent aspects of oxidative DNA damage : guanine lesions, measurement and substrate specificity of DNA repair glycosylases, Biol Chem, vol.383, pp.933-976, 2002.

H. I. Calvin and J. M. Bedford, Formation of disulfide bonds in the nucleus and accessory structures of mammalian spermatozoa during maturation in the epididymis, J. Reprod. Fertil, vol.13, pp.65-75, 1971.

H. I. Calvin, C. C. Yu, and J. M. Bedford, Effects of epididymal maturation, zinc (II) and copper (II) on the reactive sulfhydryl content of structural elements in rat spermatozoa, Experimental Cell Research, vol.81, issue.2, 1973.
DOI : 10.1016/0014-4827(73)90523-5

B. Chance, B. Schoener, R. Oshino, F. Itshak, and Y. Nakase, Oxidation-reduction ratio studies of mitochondria in freeze-trapped samples. NADH and flavoprotein fluorescence signals, J Biol Chem, vol.254, pp.4764-71, 1979.

A. Chandra, K. R. Srinivasan, F. Jamal, P. K. Mehrotra, R. L. Singh et al., Posttranslational modifications in glycosylation status during epididymal passage and significance in fertility of a 33 kDa glycoprotein (MEF3) of rhesus monkey, 2008.

E. Y. Chen, M. Fujinaga, and A. J. Giaccia, Hypoxic microenvironment within an embryo induces apoptosis and is essential for proper morphological development, Teratology, vol.13, issue.4, pp.215-240, 1999.
DOI : 10.1002/(SICI)1096-9926(199910)60:4<215::AID-TERA6>3.0.CO;2-2

C. K. Chow, Vitamin E and oxidative stress, Free Radical Biology and Medicine, vol.11, issue.2, pp.215-247, 1991.
DOI : 10.1016/0891-5849(91)90174-2

T. H. Christlet and K. Veluraja, Database analysis of O-glycosylation sites in proteins, 2001.

F. F. Chu, J. H. Doroshow, and R. S. Esworthy, Expression, Characterization, and tissue distribution of a new cellular selenium-dependent glutathione peroxidase, GSHPx-GI, J Biol Chem, vol.268, pp.2571-2577, 1993.

M. Brielmeier, Essential role for mitochondrial thioredoxin reductase in hematopoiesis, heart development, and heart function, Mol Cell Biol, vol.24, pp.9414-9437, 2004.

M. Conrad, S. G. Moreno, F. Sinowatz, F. Ursini, S. Kölle et al., The Nuclear Form of Phospholipid Hydroperoxide Glutathione Peroxidase Is a Protein Thiol Peroxidase Contributing to Sperm Chromatin Stability, Molecular and Cellular Biology, vol.25, issue.17, 2005.
DOI : 10.1128/MCB.25.17.7637-7644.2005

G. A. Cornwall, D. Vindivich, S. Tillman, and T. S. Chang, The Effect of Sulfhdryl Oxidation on the Morphology of Immature Hamster Epididymal Spermatozoa Induced to Acquire Motility in Vitro1, Biology of Reproduction, vol.39, issue.1, pp.141-145, 1989.
DOI : 10.1095/biolreprod39.1.141

J. D. Crapo and D. F. Tierney, Superoxide dismutase and pulmonary oxygen toxicity, Am J Physiol, vol.226, pp.1401-1408, 1974.

T. Darribère, Le cycle de développement de la souris In : Le développement d'un mammifère : la souris, 2003.

T. N. Dear, K. Cambell, and T. H. Rabbitts, Molecular cloning of putative odorant-binding and odorant-metabolizing proteins, Biochemistry, vol.30, issue.43, pp.10376-82, 1991.
DOI : 10.1021/bi00107a003

D. Haan, J. B. Tymms, M. J. Cristiano, F. Kola, and I. , Expression of Copper/Zinc Superoxide Dismutase and Glutathione Peroxidase in Organs of Developing Mouse Embryos, Fetuses, and Neonates, Pediatric Research, vol.35, issue.2, pp.188-96, 1994.
DOI : 10.1203/00006450-199402000-00013

A. Delaunay, D. Pflieger, M. B. Barrault, J. Vinh, and M. B. Toledano, A Thiol Peroxidase Is an H2O2 Receptor and Redox-Transducer in Gene Activation, Cell, vol.111, issue.4, pp.471-481, 2002.
DOI : 10.1016/S0092-8674(02)01048-6

P. Derr, C. H. Yeung, T. G. Cooper, and C. Kirchhoff, Synthesis and glycosylation of CD52, the major 'maturation-associated' antigen of rat spermatozoa, in the cauda epididymidis, Reproduction, vol.121, issue.3, pp.435-481, 2001.
DOI : 10.1530/rep.0.1210435

J. P. Dufaure, J. J. Lareyre, V. Schwaab, M. G. Mattei, and J. R. Drevet, Structural Références Références Références Références -94 organization , chromosomal localization, expression and phylogenetic evaluation of mouse glutathione peroxidise encoding genes, C R Acad Sci III, vol.319, pp.559-68, 1996.

O. Epp, R. Ladenstein, and A. Wendel, The Refined Structure of the Selenoenzyme Glutathione Peroxidase at 0.2-nm Resolution, European Journal of Biochemistry, vol.6, issue.1, pp.51-69, 1983.
DOI : 10.1016/0005-2760(73)90145-8

H. Esterbauer, J. Gebicki, H. Puhl, and G. Jürgens, The role of lipid peroxidation and antioxidants in oxidative modification of LDL, Free Radical Biology and Medicine, vol.13, issue.4, pp.341-90, 1992.
DOI : 10.1016/0891-5849(92)90181-F

R. S. Esworthy, F. F. Chu, R. J. Paxton, S. Akman, and J. H. Doroshow, Characterization and partial amino acid sequence of human plasma glutathione peroxidase, Archives of Biochemistry and Biophysics, vol.286, issue.2, pp.330-336, 1991.
DOI : 10.1016/0003-9861(91)90048-N

Y. Z. Fang, S. Yang, and G. Wu, Free radicals, antioxidants, and nutrition, Nutrition, vol.18, issue.10, pp.872-881, 2002.
DOI : 10.1016/S0899-9007(02)00916-4

J. Faure, N. B. Ghyselinck, C. Jimenez, and J. P. Dufaure, Specific Distribution of Messenger Ribonucleic Acids for 24-Kilodalton Proteins in the Mouse Epididymis as Revealed by in Situ Hybridization: Developmental Expression and Regulation in the Adult1, Biology of Reproduction, vol.44, issue.1, pp.13-22, 1991.
DOI : 10.1095/biolreprod44.1.13

R. Kannan, T. Maddatu, C. Garcia-ruiz, J. Kuhlenkamp, and N. Kaplowitz, Regulation of hepatic glutathione In : Hepatic transport and bile secretion : Physiology and Pathophysiology, pp.363-395, 1993.

L. Flohé, W. A. Günzler, and H. H. Schock, Glutathione peroxidase: A selenoenzyme, FEBS Letters, vol.49, issue.1, pp.132-136, 1973.
DOI : 10.1016/0014-5793(73)80755-0

L. Flohé, The selenoprotein glutathione peroxidase In : Glutathione : chemical, biochemical, and medical aspects, 1989.

T. M. Florence, Free radicals, antioxidants and cancer prevention, Proc Nutr Soc Aust Annu Conf, vol.15, pp.88-93, 1990.

B. Frei, Ascorbic acid protects lipids in human plasma and low-density lipoprotein against oxidative damage, Am J Clin Nutr, vol.54, pp.1113-1118, 1991.

I. Fridovich, Superoxide dismutases. An adaptation to a paramagnetic gas, J Biol Chem, vol.264, pp.7761-7765, 1989.

T. G. Gabig, The NADPH-dependent O 2 -generating oxidase from human neutrophils, J, 1983.

R. Geiss-friedlander and . F. Melchior, Concepts in sumoylation: a decade on, Nature Reviews Molecular Cell Biology, vol.1773, issue.12, pp.947-956, 2007.
DOI : 10.1038/nrm2293

N. B. Ghyselinck, C. Jimenez, Y. Courty, and J. P. Dufaure, Androgen-dependent messenger RNA(s) related to secretory proteins in the mouse epididymis, Reproduction, vol.85, issue.2, pp.631-640, 1989.
DOI : 10.1530/jrf.0.0850631

E. Grignard, J. Morin, P. Vernet, and J. R. Drevet, GPX5 orthologs of mouse epididymisrestricted and sperm-bound selenium-independent glutathione peroxidase are not expressed with the same quantitative and spatial characteristics in large domestic animals, 2005.

P. Guérin, S. Mouatassim, and Y. Ménézo, Oxidative stress and protection against reactive oxygen species in the pre-implantation embryo and its surroundings, Human Reproduction Update, vol.7, issue.2, pp.175-89, 2001.
DOI : 10.1093/humupd/7.2.175

W. A. Günzler, H. Vergin, I. Müller, and L. Flohé, Glutathione peroxidase VI : the reaction of glutathione peroxidase with various hydroperoxides, Hoppe Seylers Z Physiol Chem, vol.353, pp.1001-1005, 1972.

B. Halliwell, The chemistry of free radicals, Toxicol Ind Health, vol.9, pp.1-21, 1993.

B. Halliwell and J. M. Gutteridge, Oxygen free radicals and iron in relation to biology and medicine: Some problems and concepts, Archives of Biochemistry and Biophysics, vol.246, issue.2, pp.501-515, 1986.
DOI : 10.1016/0003-9861(86)90305-X

B. Halliwell and J. M. Gutteridge, Biologically relevant metal ion-dependent hydroxyl radical generation An update, FEBS Letters, vol.8, issue.1, pp.108-120, 1992.
DOI : 10.1016/0014-5793(92)80911-Y

A. J. Harvery, The role of oxygen in ruminant preimplantation embryo development and metabolism, Animal Reproduction Science, vol.98, issue.1-2, pp.113-141, 2007.
DOI : 10.1016/j.anireprosci.2006.10.008

S. Herbette, P. Roeckel-drevet, and J. R. Drevet, Seleno-independent glutathione peroxidases, FEBS Journal, vol.85, issue.3, pp.2163-80, 2007.
DOI : 10.1111/j.1742-4658.2007.05774.x
URL : https://hal.archives-ouvertes.fr/hal-01189233

B. Hogan, R. Beddington, F. Costantini, and E. Lacy, Summary of mouse development In : Manipulating the Mouse Embryo : a laboratory manual, 1994.

H. Imai and Y. Nakagawa, Biological significance of phospholipid hydroperoxide glutathione peroxidase (PHGPx, GPx4) in mammalian cells, Free Radical Biology and Medicine, vol.34, issue.2, pp.145-69, 2003.
DOI : 10.1016/S0891-5849(02)01197-8

M. H. Angelis, W. Wurst, G. W. Bornkamm, M. Brielmeier, and M. Conrad, Cytoplasmic thioredoxin reductase is essential for embryogenesis but dispensable for cardiac development, Mol Cell Biol, vol.25, pp.1980-1988, 2005.

C. Jimenez, N. B. Ghyselinck, A. Depeiges, and J. P. Dufaure, Immunochemical localization and association with spermatozoa of androgen-regulated proteins of MR 24000 secreted by the mouse epididymis, Biology of the Cell, vol.68, issue.2, pp.171-175, 1990.
DOI : 10.1016/0248-4900(90)90304-L

K. Jung and W. Henke, Developmental changes of antioxidant enzymes in kidney and liver from rats, Free Radical Biology and Medicine, vol.20, issue.4, pp.613-620, 1996.
DOI : 10.1016/0891-5849(95)02090-X

M. H. Kaufman, In : The Atlas of Mouse Development, 1992.

M. H. Kaufman and L. B. Bard, In : The anatomical basis of mouse development, 1999.

J. Y. Khan and S. M. Black, Developemental changes in murine brain antioxidant enzymes, 2003.

P. D. Kingsley, J. C. Whitin, H. J. Cohen, and J. Palis, Developmental expression of extracellular glutathione peroxidase suggests antioxidant roles in deciduum, visceral yolk sac, and skin, Molecular Reproduction and Development, vol.91, issue.4, pp.343-55, 1998.
DOI : 10.1002/(SICI)1098-2795(199804)49:4<343::AID-MRD1>3.0.CO;2-N

C. Kirchhoff, H. Obermann, M. Behnen, and B. Davies, Role of epididymal receptor HE6 in the regulation of sperm microenvironment, Molecular and Cellular Endocrinology, vol.250, issue.1-2, pp.43-48, 2006.
DOI : 10.1016/j.mce.2005.12.023

A. Labarga, F. Valentin, M. Anderson, and L. Rodrigo, Web Services at the European Bioinformatics Institute, Nucleic Acids Research, vol.35, issue.Web Server, pp.6-11, 2007.
DOI : 10.1093/nar/gkm291

R. Ladenstein and A. Wendel, Crystallographic data of the selenoenzyme glutathione peroxidase, Journal of Molecular Biology, vol.104, issue.4, pp.877-82, 1976.
DOI : 10.1016/0022-2836(76)90188-1

M. Lane, J. M. Maybach, and D. K. Gardner, Addition of ascorbate during cryopreservation stimulates subsequent embryo development, Human Reproduction, vol.17, issue.10, pp.2686-93, 2002.
DOI : 10.1093/humrep/17.10.2686

K. W. Lee and H. J. Lee, Biphasic effects of dietary antioxidants on oxidative stress-mediated carcinogenesis, Mechanisms of Ageing and Development, vol.127, issue.5, pp.424-455, 2006.
DOI : 10.1016/j.mad.2006.01.021

L. Lunghi, M. E. Ferretti, S. Medici, C. Biondi, and F. Vesce, Control of human trophoblast function, Reproductive Biology and Endocrinology, vol.5, issue.1, p.6, 2007.
DOI : 10.1186/1477-7827-5-6

A. Roveri, F. Ursini, and L. Flohé, Probing the presumed catalytic triad of seleniumcontaining peroxidase by mutational analysis of phospholipid hydroperoxide glutathione peroxidase (PHGPx), Biol Chem Hopp Seyler, vol.376, pp.651-60, 1995.

R. L. Maser, B. S. Magenheimer, and J. P. Calvet, Mouse plasma glutathione peroxidase. cDNA sequence analysis and renal proximal tubular expression and secretion, J Biol Chem, vol.269, pp.27066-73, 1994.

J. M. Matés and F. Sánchez-jiménez, Antioxidant enzymes and their implications in pathophysiologic processes, Frontiers in Bioscience, vol.4, issue.4, pp.339-384, 1999.
DOI : 10.2741/A432

M. C. Mcelroy, A. D. Postle, and F. J. Kelly, Catalase, superoxide dismutase and glutathione peroxidase activities of lung and liver during human development, Biochimica et Biophysica Acta (BBA) - General Subjects, vol.1117, issue.2, pp.153-161, 1992.
DOI : 10.1016/0304-4165(92)90073-4

G. C. Mills, Hemoglobin catabolism. I. Glutathione peroxidase, an erythrocyte enzyme which protects hemoglobin from oxidative breakdown, J Biol Chem, vol.229, pp.189-97, 1957.

L. Montagnier, R. Olivier, and C. Pasquier, Oxidatvie stress in cancer, AIDS and neurodegenerative diseases, 1998.

S. G. Moreno, G. Laux, M. Brielmeier, G. W. Bornkamm, and M. Conrad, Testis-Specific Expression of the Nuclear Form of Phospholipid Hydroperoxide Glutathione Peroxidase (PHGPx), Biological Chemistry, vol.384, issue.4, 2003.
DOI : 10.1515/BC.2003.070

B. Morgenstern, DIALIGN 2: improvement of the segment-to-segment approach to multiple sequence alignment, Bioinformatics, vol.15, issue.3, pp.211-219, 1999.
DOI : 10.1093/bioinformatics/15.3.211

G. Morriss, Growing embryos in vitro, Nature, vol.278, issue.5703, p.402, 1979.
DOI : 10.1038/278402a0

G. T. Mullenbach, A. Tabrizi, B. D. Irvine, G. I. Bell, and R. A. Hallewell, Sequence of a cDNA coding for human glutathione peroxidase confirms TGA encodes active site selenocysteine, Nucleic Acids Research, vol.15, issue.13, p.5484, 1987.
DOI : 10.1093/nar/15.13.5484

D. A. New and P. T. Coppala, EFFECTS OF DIFFERENT OXYGEN CONCENTRATIONS ON THE DEVELOPMENT OF RAT EMBRYOS IN CULTURE, Reproduction, vol.21, issue.1, pp.109-127, 1970.
DOI : 10.1530/jrf.0.0210109

E. Niki, Y. Yamamoto, E. Komuro, and K. Sato, Membrane damage due to lipid oxidation, 1991.

L. Nonn, R. R. Williams, R. P. Erickson, and G. Powis, The Absence of Mitochondrial Thioredoxin 2 Causes Massive Apoptosis, Exencephaly, and Early Embryonic Lethality in Homozygous Mice, Molecular and Cellular Biology, vol.23, issue.3, pp.916-938, 2003.
DOI : 10.1128/MCB.23.3.916-922.2003

K. Ohyama, B. Yuan, T. Bessho, and T. Yamakawa, Progressive apoptosis in chorion laeve trophoblast cells of human fetal membrane tissues during in vitro incubation is suppressed by antioxidative reagents, European Journal of Biochemistry, vol.4, issue.23, pp.6182-6191, 2001.
DOI : 10.1046/j.0014-2956.2001.02573.x

W. C. Orr and R. S. Sohal, Effects of Cu-Zn Superoxide Dismutase Overexpression on Life Span and Resistance to Oxidative Stress in Transgenic Drosophila melanogaster, Archives of Biochemistry and Biophysics, vol.301, issue.1, pp.34-40, 1993.
DOI : 10.1006/abbi.1993.1111

W. C. Orr and R. S. Sohal, Extension of life-span by overexpression of superoxide dismutase and catalase in Drosophila melanogaster, Science, vol.263, issue.5150, pp.1128-1158, 1994.
DOI : 10.1126/science.8108730

J. E. Pabon, . Jr, W. E. Findley, and W. E. Gibbons, The toxic effect of short exposures to the atmospheric oxygen concentration on early mouse embryonic development, Fertility and Sterility, vol.51, issue.5, pp.896-900, 1989.
DOI : 10.1016/S0015-0282(16)60688-X

P. J. Park, W. K. Jung, K. S. Nam, F. Shahidi, and S. K. Kim, Purification and characterization of antioxidative peptides from protein hydrolysate of lecithin-free egg yolk, Journal of the American Oil Chemists' Society, vol.270, issue.6, pp.651-56, 2001.
DOI : 10.1007/s11746-001-0321-0

D. N. Perkins, D. J. Pappin, D. M. Creasy, and J. S. Cottrell, Probability-based protein identification by searching sequence databases using mass spectrometry data, Electrophoresis, vol.447, issue.18, 1999.
DOI : 10.1002/(SICI)1522-2683(19991201)20:18<3551::AID-ELPS3551>3.0.CO;2-2

A. C. Perry, R. Jones, and L. Hall, Isolation and characterization of a rat cDNA clone encoding a secreted superoxide dismutase reveals the epididymis to be a major site of its expression, Biochemical Journal, vol.293, issue.1, pp.21-26, 1993.
DOI : 10.1042/bj2930021

D. Behne, Identification of a specific sperm nuclei selenoenzyme necessary for protamine thiol cross-linking during sperm maturation, FASEB J, vol.15, pp.1236-1238, 2001.

J. Pontius, L. Wagner, and G. Schuler, UniGene: a unified view of the transcriptome, 2003.

T. J. Proszynski, K. Simons, and M. Bagnat, O-Glycosylation as a Sorting Determinant for Cell Surface Delivery in Yeast, Molecular Biology of the Cell, vol.15, issue.4, pp.1533-1576, 2004.
DOI : 10.1091/mbc.E03-07-0511

R. Puglisi, F. Tramer, E. Panfili, F. Micali, G. Sandri et al., Differential Splicing of the Phospholipid Hydroperoxide Glutathione Peroxidase Gene in Diploid and Haploid Male Germ Cells in the Rat1, Biology of Reproduction, vol.68, issue.2, pp.405-416, 2003.
DOI : 10.1095/biolreprod.102.006544

T. R. Pushpa-rekha, A. L. Burdsall, L. M. Oleksa, G. M. Chisolm, and D. M. Driscoll, Rat Phospholipid-hydroperoxide Glutathione Peroxidase: cDNA CLONING AND IDENTIFICATION OF MULTIPLE TRANSCRIPTION AND TRANSLATION START SITES, Journal of Biological Chemistry, vol.270, issue.45, pp.26993-27002, 1995.
DOI : 10.1074/jbc.270.45.26993

S. Qanungo and M. Mukherjea, Ontogenic profile of some antioxidants and lipid peroxidation in human placental and fetal tissues, Molecular and Cellular Biochemistry, vol.215, issue.1/2, pp.11-20, 2000.
DOI : 10.1023/A:1026511420505

J. Remacle and P. Renard, Role of oxidative stress in aging, Pathol Biol, vol.44, pp.65-76, 1996.

H. Rejraji, P. Vernet, and J. R. Drevet, GPX5 is present in the mouse caput and cauda epididymidis lumen at three different locations, Molecular Reproduction and Development, vol.7, issue.1, pp.96-103, 2002.
DOI : 10.1002/mrd.10136

H. Rejraji, B. Sion, G. Prensier, M. Carreras, C. Motta et al., Lipid Remodeling of Murine Epididymosomes and Spermatozoa During Epididymal Maturation1, Biology of Reproduction, vol.74, issue.6, pp.1104-1117, 2006.
DOI : 10.1095/biolreprod.105.049304

I. Reveillaud, A. Niedzwiecki, K. G. Bensch, and J. E. Fleming, Expression of bovine superoxide dismutase in Drosophila melanogaster augments resistance of oxidative stress., Molecular and Cellular Biology, vol.11, issue.2, 1991.
DOI : 10.1128/MCB.11.2.632

S. G. Rhee, Redox signaling: hydrogen peroxide as intracellular messenger, Experimental & Molecular Medicine, vol.31, issue.2, pp.53-62, 1999.
DOI : 10.1038/emm.1999.9

G. M. Rickett and F. J. Kelly, Developmental expression of antioxidant enzymes in guinea pig lung and liver, Development, vol.108, pp.331-337, 1990.

N. Rigaudière, N. B. Ghyselinck, J. Faure, and J. P. Dufaure, Regulation of the epididymal glutathione peroxidase-like protein in the mouse: Dependence upon androgens and testicular factors, Molecular and Cellular Endocrinology, vol.89, issue.1-2, pp.67-77, 1992.
DOI : 10.1016/0303-7207(92)90212-O

A. Roveri, F. Ursini, L. Flohé, and M. Maiorino, PHGPx and spermatogenesis, BioFactors, vol.17, issue.2, pp.213-222, 2001.
DOI : 10.1002/biof.5520140127

P. Scheiffele and J. Füllekrug, Glycosylation and protein transport, Essays In Biochemistry, vol.36, pp.27-35, 2000.
DOI : 10.1042/bse0360027

J. Seligman, N. S. Kosower, R. Weissenberg, and R. Shalgi, Thiol-disulfide status of human sperm proteins, Reproduction, vol.101, issue.2, pp.435-454, 1994.
DOI : 10.1530/jrf.0.1010435

J. Seligman, G. L. Newton, R. C. Fahey, R. Shalgi, and N. S. Kosower, Nonprotein Thiols and Disulfides in Rat Epididymal Spermatozoa and Epididymal Fluid: Role of ??-Glutamyl-Transpeptidase in Sperm Maturation, Journal of Andrology, vol.26, issue.5, pp.629-640, 2005.
DOI : 10.2164/jandrol.05040

R. Shalgi, J. Seligman, and N. S. Kosover, Dynamics of the Thiol Status of Rat Spermatozoa during Maturation: Analysis with the Fluorescent Labeling Agent Monobromobimane1, Biology of Reproduction, vol.40, issue.5, pp.1037-1045, 1989.
DOI : 10.1095/biolreprod40.5.1037

Q. Shen, P. A. Mcquilkin, and P. E. Newburger, RNA-binding Proteins That Specifically Recognize the Selenocysteine Insertion Sequence of Human Cellular Glutathione Peroxidase mRNA, Journal of Biological Chemistry, vol.270, issue.51, pp.30448-52, 1995.
DOI : 10.1074/jbc.270.51.30448

Q. Shen, J. L. Leonard, and P. E. Newburger, Structure and function of the selenium translation element in the 3'-untranslated region of human cellular glutathione peroxidase mRNA, RNA, vol.1, pp.519-544, 1995.

Z. Z. Shi, J. Osei-frimpong, G. Kala, S. V. Kala, R. J. Barrios et al., Glutathione synthesis is essential for mouse development but not for cell growth in culture, Proceedings of the National Academy of Sciences, vol.97, issue.10, pp.5101-5107, 2000.
DOI : 10.1073/pnas.97.10.5101

M. C. Simon and B. Keith, The role of oxygen availability in embryonic development and stem cell function, Nature Reviews Molecular Cell Biology, vol.274, issue.4, pp.285-96, 2008.
DOI : 10.1038/nrm2354

M. C. Simurda, H. Van-keulen, D. M. Rekosh, and P. T. Loverde, Schistosoma mansoni: Identification and analysis of an mRNA and a gene encoding superoxide dismutase (), Experimental Parasitology, vol.67, issue.1, 1988.
DOI : 10.1016/0014-4894(88)90010-0

R. S. Sohal, R. J. Mockett, and W. C. Orr, Mechanisms of aging: an appraisal of the oxidative stress hypothesis1,2 1This article is part of a series of reviews on ???Oxidative Stress and Aging.??? The full list of papers may be found on the homepage of the journal. 2Guest Editor: Rajindar S. Sohal, Free Radical Biology and Medicine, vol.33, issue.5, pp.575-86, 2002.
DOI : 10.1016/S0891-5849(02)00886-9

D. R. Spitz, J. W. Phillips, D. T. Adams, C. M. Sherman, D. F. Deen et al., Cellular resistance to oxidative stress is accompanied by resistance to cisplatin: The significance of increased catalase activity and total glutathione in hydrogen peroxide-resistant fibroblasts, Journal of Cellular Physiology, vol.292, issue.1, pp.72-81, 1993.
DOI : 10.1002/jcp.1041560111

N. Spodsberg, M. Alfalah, and H. Y. Naim, Characteristics and Structural Requirements of Apical Sorting of the Rat Growth Hormone through the O-Glycosylated Stalk Region of Intestinal Sucrase-isomaltase, Journal of Biological Chemistry, vol.276, issue.49, pp.46597-604, 2001.
DOI : 10.1074/jbc.M108187200

R. Sullivan, G. Frenette, and J. Girouard, Epididymosomes are involved in the acquisition of new sperm proteins during epididymal transit, Asian Journal of Andrology, vol.9, issue.4, pp.483-91, 2007.
DOI : 10.1111/j.1745-7262.2007.00281.x

K. Takahashi, N. Avissar, J. Whitin, and H. Cohen, Purification and characterization of human plasma glutathione peroxidase: A selenoglycoprotein distinct from the known cellular enzyme, Archives of Biochemistry and Biophysics, vol.256, issue.2, pp.677-86, 1987.
DOI : 10.1016/0003-9861(87)90624-2

R. Beiglböck, A. Pera, I. Ellerbrock, K. Kirchhoff, and C. , Dog epididymis-specific mRNA encoding secretory glutathione peroxidase-like protein, Reproduction, vol.112, issue.2, pp.357-367, 1998.
DOI : 10.1530/jrf.0.1120357

A. Borchert, N. E. Savaskan, H. A. Kuhn, A. D. Isnard, and M. B. Toledano, Regulation of expression of the phospholipid hydroperoxide/sperm nucleus glutathione peroxidase gene H 2 O 2 sensing through oxidation of the Yap1 transcription factor, J. Biol. Chem. EMBO J.EMBOJ, vol.27819, issue.19, pp.2571-2580, 2000.

J. R. Drevet, Glutathione peroxidase expression in the mammalian epididymis and vas deferens, pp.4270-4462, 2000.

J. R. Drevet, The antioxidant glutathione peroxidase family and spermatozoa: A complex story, Molecular and Cellular Endocrinology, vol.250, issue.1-2, pp.70-79, 2006.
DOI : 10.1016/j.mce.2005.12.027

J. P. Dufaure, J. J. Lareyre, V. Schwaab, M. G. Mattei, and J. R. Drevet, Structural organization, chromosomal localization, expression and philogenetic evaluation of mouse glutathione peroxidase encoding genes, C. R. Acad. Sci. III, vol.319, pp.559-568, 1996.

O. Epp, R. Ladenstein, W. , and A. , The Refined Structure of the Selenoenzyme Glutathione Peroxidase at 0.2-nm Resolution, European Journal of Biochemistry, vol.6, issue.1, 1983.
DOI : 10.1016/0005-2760(73)90145-8

J. Faure, N. B. Ghyselicnk, C. Jimenez, and J. P. Dufaure, Specific Distribution of Messenger Ribonucleic Acids for 24-Kilodalton Proteins in the Mouse Epididymis as Revealed by in Situ Hybridization: Developmental Expression and Regulation in the Adult1, Biology of Reproduction, vol.44, issue.1, pp.13-22, 1991.
DOI : 10.1095/biolreprod44.1.13

N. B. Ghyselinck, I. Dufaure, J. J. Lareyre, N. Rigaudiere, M. G. Mattei et al., Structural organization and regulation of the gene encoding the androgen-dependent glutathione peroxidase-like protein specific to the mouse epididymis, Mol. Endocrinol, vol.7, pp.258-272, 1993.

E. Grignard, J. Morin, P. Vernet, and J. R. Drevet, GPX5 orthologs of the mouse epididymis-restricted and sperm-bound selenium-independent glutathione peroxidase are not expressed with the same quantitative and spatial characteristics in large domestic animals, Theriogenology, vol.64, issue.4, pp.1016-1033, 2005.
DOI : 10.1016/j.theriogenology.2005.01.008

E. Grignard, R. Cadet, F. Saez, J. R. Drevet, and P. Vernet, Identification of sperm antigens as a first step towards the generation of a contraceptive vaccine to decrease fossorial water vole Arvicola terrestris Scherman proliferations, Theriogenology, vol.68, issue.5, pp.779-795, 2007.
DOI : 10.1016/j.theriogenology.2007.06.010

L. Hall, K. Williams, A. C. Perry, J. Frayne, and J. A. Jury, The majority of human glutathione peroxidase type 5 (GPX5) transcripts are incorrectly spliced: implications for the role of GPX5 in the male reproductive tract, Biochemical Journal, vol.333, issue.1, pp.5-9, 1998.
DOI : 10.1042/bj3330005

S. Herbette, C. Lenne, N. Leblanc, J. L. Julien, J. R. Drevet et al., are antioxidant enzymes with phospholipid hydroperoxide glutathione peroxidase and thioredoxin peroxidase activities, European Journal of Biochemistry, vol.13, issue.9, pp.2414-2420, 2002.
DOI : 10.1046/j.1432-1033.2002.02905.x
URL : https://hal.archives-ouvertes.fr/hal-01189670

S. Herbette, P. Roeckel-drevet, and J. R. Drevet, Selenoindependent glutathione peroxidases: more than simple antioxidant scavengers, FEBS J, vol.274, 2007.
DOI : 10.1111/j.1742-4658.2007.05774.x
URL : https://hal.archives-ouvertes.fr/hal-01189233

J. J. Lareyre, F. Claessens, W. Rombauts, J. P. Dufaure, and J. R. Drevet, Characterization of an androgen response element within the promoter of the epididymis-specific murine glutathione peroxidase 5 gene, Molecular and Cellular Endocrinology, vol.129, issue.1, pp.33-46, 1997.
DOI : 10.1016/S0303-7207(97)04038-0

M. Maiorino, K. D. Aumann, R. Brigelius-flohe, D. Doria, J. Van-den-heuvel et al., Probing the Presumed Catalytic Triad of Selenium-Containing Peroxidases by Mutational Analysis of Phospholipid Hydroperoxide Glutathione Peroxidase (PHGPx), Biological Chemistry Hoppe-Seyler, vol.376, issue.11, pp.651-660, 1995.
DOI : 10.1515/bchm3.1995.376.11.651

M. Maiorino, M. Scapin, F. Ursini, M. Biasolo, V. Bosello et al., Distinct promoters determine alternative transcription of gpx4 into phospholipids-hydroperoxide glutathione peroxidase variants Molecular cloning and characterization of the epididymis-specific glutathione peroxidaselike protein secreted in the porcine epididymal fluid, J. Biol. Chem. Biochim. Biophys. Acta, vol.278, issue.1336, pp.286-320, 1997.

A. C. Perry, R. Jones, L. S. Niang, R. M. Jackson, and L. Hall, Genetic evidence for an androgen-regulated epididymal secretory glutathione peroxidase whose transcript does not contain a selenocysteine codon, Biochemical Journal, vol.285, issue.3, pp.863-870, 1992.
DOI : 10.1042/bj2850863

T. R. Pushpa-rekha, A. L. Burdsall, L. M. Oleksa, G. M. Chisolm, and D. M. Driscoll, Rat phospholipid-hydroperoxide glutathione http://www.publish.csiro.au/journals/rfd peroxidase. cDNA cloning and identification of multiple transcription and translation start sites, J. Biol. Chem, vol.270, issue.26, pp.993-1019, 1995.

H. Rejraji, P. Vernet, and J. R. Drevet, GPX5 is present in the mouse caput and cauda epididymis lumen at three different locations, 2002.

N. Rigaudière, N. B. Ghyselinck, J. Faure, J. P. Dufaure, E. F. Fritsch et al., Regulation of the epididymal glutathione peroxidase-like protein in the mouse: Dependence upon androgens and testicular factors, Molecular Cloning. A laboratory Manual.' (Cold Spring Harbor University Press: Cold Spring Harbo, pp.67-77, 1989.
DOI : 10.1016/0303-7207(92)90212-O

V. Schwaab, E. Baud, N. B. Ghyselinck, M. G. Mattei, J. P. Dufaure et al., Cloning of the mouse gene encoding plasma glutathione peroxidase: organization, sequence and chromosomal localization GPX3: the plasma-type glutathione peroxidase is expressed under androgenic control in the mouse epididymis and vas deferens Concepts and principles of O-linked glycosylation, 4<362::AID- MRD2>3.0.CO;2-L van den, pp.25-31, 1995.

P. Vernet, N. Rigaudiere, N. B. Ghyselinck, J. P. Dufaure, and J. R. Drevet, In vitro expression of a mouse tissue specific glutathione-peroxidase-like protein lacking the selenocysteine can protect stably transfected mammalian cells against oxidative damage, Biochemistry and Cell Biology, vol.74, issue.1, pp.125-131, 1996.
DOI : 10.1139/o96-014

P. Vernet, J. Faure, J. P. Dufaure, and J. R. Drevet, Tissue and developmental distribution, dependence upon testicular factors and attchment to spermatozoa of GPX5, a murine epididymis-specific glutathione peroxidase, 1<87::AID-MRD12>3.0.CO, pp.87-981098, 1997.

P. Vernet, E. Rock, A. Mazur, Y. Rayssiguier, J. P. Dufaure et al., Selenium-independent epididymis-restricted glutathione peroxidase 5 protein (GPX5) can back up failing Se-dependent GPXs in mice subjected to selenium deficiency, 4<362::AID- MRD6>3.0.CO Expression of extracellular glutathione peroxidase type 5 (GPX5) in the rat male reproductive tract, 1998.
DOI : 10.1002/(SICI)1098-2795(199912)54:4<362::AID-MRD6>3.0.CO;2-#