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Volumn 1850, Issue 8, 2015, Pages 1566-1574

ROS, thiols and thiol-regulating systems in male gametogenesis

Author keywords

Glutathione peroxidase; Oxidative stress; Selenium; Selenoproteins; Spermatogenesis

Indexed keywords

GLUTAREDOXIN; GLUTATHIONE PEROXIDASE; GLUTATHIONE REDUCTASE; MANGANESE SUPEROXIDE DISMUTASE; MITOGEN ACTIVATED PROTEIN KINASE P38; PEROXIREDOXIN; POLYUNSATURATED FATTY ACID; REACTIVE OXYGEN METABOLITE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE 1; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE 3; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE 4; SELENIUM; SPERMATID SPECIFIC THIOREDOXIN; STRESS ACTIVATED PROTEIN KINASE; THIOL DERIVATIVE; THIOREDOXIN; UNCLASSIFIED DRUG; PHOSPHOLIPID-HYDROPEROXIDE GLUTATHIONE PEROXIDASE;

EID: 84929358937     PISSN: 03044165     EISSN: 18728006     Source Type: Journal    
DOI: 10.1016/j.bbagen.2014.10.020     Document Type: Review
Times cited : (33)

References (106)
  • 2
    • 0001655470 scopus 로고
    • Formation of hydrogen peroxide by spermatozoa and its inhibitory effect of respiration
    • J. Tosic, and A. Walton Formation of hydrogen peroxide by spermatozoa and its inhibitory effect of respiration Nature 158 1946 485
    • (1946) Nature , vol.158 , pp. 485
    • Tosic, J.1    Walton, A.2
  • 3
    • 84901316606 scopus 로고    scopus 로고
    • Cellular mechanisms and physiological consequences of redox-dependent signalling
    • K.M. Holmstrom, and T. Finkel Cellular mechanisms and physiological consequences of redox-dependent signalling Nat. Rev. Mol. Cell Biol. 15 2014 411 421
    • (2014) Nat. Rev. Mol. Cell Biol. , vol.15 , pp. 411-421
    • Holmstrom, K.M.1    Finkel, T.2
  • 6
    • 84907455071 scopus 로고    scopus 로고
    • Nox family NADPH oxidases: Molecular mechanisms of activation
    • R.P. Brandes, N. Weissmann, and K. Schroder Nox family NADPH oxidases: molecular mechanisms of activation Free Radic. Biol. Med. 2014 Aug 23;76C:208-226. http://dx.doi.org/10.1016/j.freeradbiomed.2014.07.046. [Epub ahead of print]
    • (2014) Free Radic. Biol. Med.
    • Brandes, R.P.1    Weissmann, N.2    Schroder, K.3
  • 9
    • 57849105193 scopus 로고    scopus 로고
    • Curcumin attenuates ischemia-reperfusion injury in rat testis
    • S.M. Wei, Z.Z. Yan, and J. Zhou Curcumin attenuates ischemia-reperfusion injury in rat testis Fertil. Steril. 91 2009 271 277
    • (2009) Fertil. Steril. , vol.91 , pp. 271-277
    • Wei, S.M.1    Yan, Z.Z.2    Zhou, J.3
  • 10
    • 0037115712 scopus 로고    scopus 로고
    • The housekeeping gene xanthine oxidoreductase is necessary for milk fat droplet enveloping and secretion: Gene sharing in the lactating mammary gland
    • C. Vorbach, A. Scriven, and M.R. Capecchi The housekeeping gene xanthine oxidoreductase is necessary for milk fat droplet enveloping and secretion: gene sharing in the lactating mammary gland Genes Dev. 16 2002 3223 3235
    • (2002) Genes Dev. , vol.16 , pp. 3223-3235
    • Vorbach, C.1    Scriven, A.2    Capecchi, M.R.3
  • 11
    • 54249166691 scopus 로고    scopus 로고
    • Mammalian sperm metabolism: Oxygen and sugar, friend and foe
    • B.T. Storey Mammalian sperm metabolism: oxygen and sugar, friend and foe Int. J. Dev. Biol. 52 2008 427 437
    • (2008) Int. J. Dev. Biol. , vol.52 , pp. 427-437
    • Storey, B.T.1
  • 12
    • 84914818482 scopus 로고    scopus 로고
    • Glycolysis plays an important role in energy transfer from the base to the distal end of the flagellum in mouse sperm
    • G.L. Takei, D. Miyashiro, C. Mukai, and M. Okuno Glycolysis plays an important role in energy transfer from the base to the distal end of the flagellum in mouse sperm J. Exp. Biol. 217 2014 1876 1886
    • (2014) J. Exp. Biol. , vol.217 , pp. 1876-1886
    • Takei, G.L.1    Miyashiro, D.2    Mukai, C.3    Okuno, M.4
  • 13
    • 84877039048 scopus 로고    scopus 로고
    • Glycolysis and mitochondrial respiration in mouse LDHC-null sperm
    • F. Odet, S. Gabel, R.E. London, E. Goldberg, and E.M. Eddy Glycolysis and mitochondrial respiration in mouse LDHC-null sperm Biol. Reprod. 88 2013 95
    • (2013) Biol. Reprod. , vol.88 , pp. 95
    • Odet, F.1    Gabel, S.2    London, R.E.3    Goldberg, E.4    Eddy, E.M.5
  • 14
    • 46449121493 scopus 로고    scopus 로고
    • Expression of the gene for mouse lactate dehydrogenase C (Ldhc) is required for male fertility
    • F. Odet, C. Duan, W.D. Willis, E.H. Goulding, A. Kung, E.M. Eddy, and E. Goldberg Expression of the gene for mouse lactate dehydrogenase C (Ldhc) is required for male fertility Biol. Reprod. 79 2008 26 34
    • (2008) Biol. Reprod. , vol.79 , pp. 26-34
    • Odet, F.1    Duan, C.2    Willis, W.D.3    Goulding, E.H.4    Kung, A.5    Eddy, E.M.6    Goldberg, E.7
  • 16
    • 49249112023 scopus 로고    scopus 로고
    • Significance of mitochondrial reactive oxygen species in the generation of oxidative stress in spermatozoa
    • A.J. Koppers, G.N. De Iuliis, J.M. Finnie, E.A. McLaughlin, and R.J. Aitken Significance of mitochondrial reactive oxygen species in the generation of oxidative stress in spermatozoa J. Clin. Endocrinol. Metab. 93 2008 3199 3207
    • (2008) J. Clin. Endocrinol. Metab. , vol.93 , pp. 3199-3207
    • Koppers, A.J.1    De Iuliis, G.N.2    Finnie, J.M.3    McLaughlin, E.A.4    Aitken, R.J.5
  • 17
    • 0023412036 scopus 로고
    • Spontaneous lipid peroxidation and production of hydrogen peroxide and superoxide in human spermatozoa. Superoxide dismutase as major enzyme protectant against oxygen toxicity
    • J.G. Alvarez, J.C. Touchstone, L. Blasco, and B.T. Storey Spontaneous lipid peroxidation and production of hydrogen peroxide and superoxide in human spermatozoa. Superoxide dismutase as major enzyme protectant against oxygen toxicity J. Androl. 8 1987 338 348
    • (1987) J. Androl. , vol.8 , pp. 338-348
    • Alvarez, J.G.1    Touchstone, J.C.2    Blasco, L.3    Storey, B.T.4
  • 18
    • 0018341406 scopus 로고
    • Peroxidative breakdown of phospholipids in human spermatozoa, spermicidal properties of fatty acid peroxides, and protective action of seminal plasma
    • R. Jones, T. Mann, and R. Sherins Peroxidative breakdown of phospholipids in human spermatozoa, spermicidal properties of fatty acid peroxides, and protective action of seminal plasma Fertil. Steril. 31 1979 531 537
    • (1979) Fertil. Steril. , vol.31 , pp. 531-537
    • Jones, R.1    Mann, T.2    Sherins, R.3
  • 19
    • 84869467151 scopus 로고    scopus 로고
    • Sperm motility is lost in vitro as a consequence of mitochondrial free radical production and the generation of electrophilic aldehydes but can be significantly rescued by the presence of nucleophilic thiols
    • R.J. Aitken, Z. Gibb, L.A. Mitchell, S.R. Lambourne, H.S. Connaughton, and G.N. De Iuliis Sperm motility is lost in vitro as a consequence of mitochondrial free radical production and the generation of electrophilic aldehydes but can be significantly rescued by the presence of nucleophilic thiols Biol. Reprod. 87 2012 110
    • (2012) Biol. Reprod. , vol.87 , pp. 110
    • Aitken, R.J.1    Gibb, Z.2    Mitchell, L.A.3    Lambourne, S.R.4    Connaughton, H.S.5    De Iuliis, G.N.6
  • 20
    • 84866529392 scopus 로고    scopus 로고
    • Electrophilic aldehydes generated by sperm metabolism activate mitochondrial reactive oxygen species generation and apoptosis by targeting succinate dehydrogenase
    • R.J. Aitken, S. Whiting, G.N. De Iuliis, S. McClymont, L.A. Mitchell, and M.A. Baker Electrophilic aldehydes generated by sperm metabolism activate mitochondrial reactive oxygen species generation and apoptosis by targeting succinate dehydrogenase J. Biol. Chem. 287 2012 33048 33060
    • (2012) J. Biol. Chem. , vol.287 , pp. 33048-33060
    • Aitken, R.J.1    Whiting, S.2    De Iuliis, G.N.3    McClymont, S.4    Mitchell, L.A.5    Baker, M.A.6
  • 21
    • 84890922670 scopus 로고    scopus 로고
    • The role of iron and reactive oxygen species in cell death
    • S.J. Dixon, and B.R. Stockwell The role of iron and reactive oxygen species in cell death Nat. Chem. Biol. 10 2013 9 17
    • (2013) Nat. Chem. Biol. , vol.10 , pp. 9-17
    • Dixon, S.J.1    Stockwell, B.R.2
  • 23
    • 0025017074 scopus 로고
    • Role of lipoxygenase in the mechanism of acrosome reaction in mammalian spermatozoa
    • Y. Lax, S. Grossman, S. Rubinstein, N. Magid, and H. Breitbart Role of lipoxygenase in the mechanism of acrosome reaction in mammalian spermatozoa Biochim. Biophys. Acta 1043 1990 12 18
    • (1990) Biochim. Biophys. Acta , vol.1043 , pp. 12-18
    • Lax, Y.1    Grossman, S.2    Rubinstein, S.3    Magid, N.4    Breitbart, H.5
  • 26
    • 0001387519 scopus 로고
    • The role of oxygen in the metabolism and motility of human spermatozoa
    • J. MacLeod The role of oxygen in the metabolism and motility of human spermatozoa Am. J. Physiol. 138 1943 512 518
    • (1943) Am. J. Physiol. , vol.138 , pp. 512-518
    • Macleod, J.1
  • 29
    • 0033753955 scopus 로고    scopus 로고
    • Quantification of the nonenzymatic fast and slow TRAP in a postaddition assay in human seminal plasma and the antioxidant contributions of various seminal compounds
    • J.P. Rhemrev, F.W. van Overveld, G.R. Haenen, T. Teerlink, A. Bast, and J.P. Vermeiden Quantification of the nonenzymatic fast and slow TRAP in a postaddition assay in human seminal plasma and the antioxidant contributions of various seminal compounds J. Androl. 21 2000 913 920
    • (2000) J. Androl. , vol.21 , pp. 913-920
    • Rhemrev, J.P.1    Van Overveld, F.W.2    Haenen, G.R.3    Teerlink, T.4    Bast, A.5    Vermeiden, J.P.6
  • 30
    • 3543040601 scopus 로고    scopus 로고
    • Mice lacking catalase develop normally but show differential sensitivity to oxidant tissue injury
    • Y.S. Ho, Y. Xiong, W. Ma, A. Spector, and D.S. Ho Mice lacking catalase develop normally but show differential sensitivity to oxidant tissue injury J. Biol. Chem. 279 2004 32804 32812
    • (2004) J. Biol. Chem. , vol.279 , pp. 32804-32812
    • Ho, Y.S.1    Xiong, Y.2    Ma, W.3    Spector, A.4    Ho, D.S.5
  • 33
    • 33646871371 scopus 로고    scopus 로고
    • Peroxisomes are present in murine spermatogonia and disappear during the course of spermatogenesis
    • G.H. Luers, S. Thiele, A. Schad, A. Volkl, S. Yokota, and J. Seitz Peroxisomes are present in murine spermatogonia and disappear during the course of spermatogenesis Histochem. Cell Biol. 125 2006 693 703
    • (2006) Histochem. Cell Biol. , vol.125 , pp. 693-703
    • Luers, G.H.1    Thiele, S.2    Schad, A.3    Volkl, A.4    Yokota, S.5    Seitz, J.6
  • 35
    • 84876439035 scopus 로고    scopus 로고
    • Impaired fertilizing ability of superoxide dismutase 1-deficient mouse sperm during in vitro fertilization
    • S. Tsunoda, N. Kawano, K. Miyado, N. Kimura, and J. Fujii Impaired fertilizing ability of superoxide dismutase 1-deficient mouse sperm during in vitro fertilization Biol. Reprod. 87 2012 121
    • (2012) Biol. Reprod. , vol.87 , pp. 121
    • Tsunoda, S.1    Kawano, N.2    Miyado, K.3    Kimura, N.4    Fujii, J.5
  • 36
    • 0035957325 scopus 로고    scopus 로고
    • Selenoprotein oxidoreductase with specificity for thioredoxin and glutathione systems
    • Q.A. Sun, L. Kirnarsky, S. Sherman, and V.N. Gladyshev Selenoprotein oxidoreductase with specificity for thioredoxin and glutathione systems Proc. Natl. Acad. Sci. U. S. A. 98 2001 3673 3678
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 3673-3678
    • Sun, Q.A.1    Kirnarsky, L.2    Sherman, S.3    Gladyshev, V.N.4
  • 37
    • 78649629122 scopus 로고    scopus 로고
    • Redox atlas of the mouse. Immunohistochemical detection of glutaredoxin-, peroxiredoxin-, and thioredoxin-family proteins in various tissues of the laboratory mouse
    • J.R. Godoy, M. Funke, W. Ackermann, P. Haunhorst, S. Oesteritz, F. Capani, H.P. Elsasser, and C.H. Lillig Redox atlas of the mouse. Immunohistochemical detection of glutaredoxin-, peroxiredoxin-, and thioredoxin-family proteins in various tissues of the laboratory mouse Biochim. Biophys. Acta 1810 2011 2 92
    • (2011) Biochim. Biophys. Acta , vol.1810 , pp. 2-92
    • Godoy, J.R.1    Funke, M.2    Ackermann, W.3    Haunhorst, P.4    Oesteritz, S.5    Capani, F.6    Elsasser, H.P.7    Lillig, C.H.8
  • 38
    • 0036838553 scopus 로고    scopus 로고
    • Developmental expression of spermatid-specific thioredoxin-1 protein: Transient association to the longitudinal columns of the fibrous sheath during sperm tail formation
    • Y. Yu, R. Oko, and A. Miranda-Vizuete Developmental expression of spermatid-specific thioredoxin-1 protein: transient association to the longitudinal columns of the fibrous sheath during sperm tail formation Biol. Reprod. 67 2002 1546 1554
    • (2002) Biol. Reprod. , vol.67 , pp. 1546-1554
    • Yu, Y.1    Oko, R.2    Miranda-Vizuete, A.3
  • 39
    • 0242691001 scopus 로고    scopus 로고
    • Cloning and developmental analysis of murid spermatid-specific thioredoxin-2 (SPTRX-2), a novel sperm fibrous sheath protein and autoantigen
    • A. Miranda-Vizuete, K. Tsang, Y. Yu, A. Jimenez, M. Pelto-Huikko, C.J. Flickinger, P. Sutovsky, and R. Oko Cloning and developmental analysis of murid spermatid-specific thioredoxin-2 (SPTRX-2), a novel sperm fibrous sheath protein and autoantigen J. Biol. Chem. 278 2003 44874 44885
    • (2003) J. Biol. Chem. , vol.278 , pp. 44874-44885
    • Miranda-Vizuete, A.1    Tsang, K.2    Yu, Y.3    Jimenez, A.4    Pelto-Huikko, M.5    Flickinger, C.J.6    Sutovsky, P.7    Oko, R.8
  • 40
  • 41
    • 84883682066 scopus 로고    scopus 로고
    • Functional deletion of Txndc2 and Txndc3 increases the susceptibility of spermatozoa to age-related oxidative stress
    • T.B. Smith, M.A. Baker, H.S. Connaughton, U. Habenicht, and R.J. Aitken Functional deletion of Txndc2 and Txndc3 increases the susceptibility of spermatozoa to age-related oxidative stress Free Radic. Biol. Med. 65 2013 872 881
    • (2013) Free Radic. Biol. Med. , vol.65 , pp. 872-881
    • Smith, T.B.1    Baker, M.A.2    Connaughton, H.S.3    Habenicht, U.4    Aitken, R.J.5
  • 46
    • 0037305881 scopus 로고    scopus 로고
    • The absence of mitochondrial thioredoxin 2 causes massive apoptosis, exencephaly, and early embryonic lethality in homozygous mice
    • 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 Mol. Cell. Biol. 23 2003 916 922
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 916-922
    • Nonn, L.1    Williams, R.R.2    Erickson, R.P.3    Powis, G.4
  • 47
    • 2042470971 scopus 로고    scopus 로고
    • Early embryonic lethality caused by targeted disruption of the mouse thioredoxin gene
    • M. Matsui, M. Oshima, H. Oshima, K. Takaku, T. Maruyama, J. Yodoi, and M.M. Taketo Early embryonic lethality caused by targeted disruption of the mouse thioredoxin gene Dev. Biol. 178 1996 179 185
    • (1996) Dev. Biol. , vol.178 , pp. 179-185
    • Matsui, M.1    Oshima, M.2    Oshima, H.3    Takaku, K.4    Maruyama, T.5    Yodoi, J.6    Taketo, M.M.7
  • 52
    • 22544451578 scopus 로고    scopus 로고
    • Mammalian selenoprotein thioredoxin-glutathione reductase. Roles in disulfide bond formation and sperm maturation
    • D. Su, S.V. Novoselov, Q.A. Sun, M.E. Moustafa, Y. Zhou, R. Oko, D.L. Hatfield, and V.N. Gladyshev Mammalian selenoprotein thioredoxin-glutathione reductase. Roles in disulfide bond formation and sperm maturation J. Biol. Chem. 280 2005 26491 26498
    • (2005) J. Biol. Chem. , vol.280 , pp. 26491-26498
    • Su, D.1    Novoselov, S.V.2    Sun, Q.A.3    Moustafa, M.E.4    Zhou, Y.5    Oko, R.6    Hatfield, D.L.7    Gladyshev, V.N.8
  • 53
    • 34548844721 scopus 로고    scopus 로고
    • Targeted disruption of the glutaredoxin 1 gene does not sensitize adult mice to tissue injury induced by ischemia/reperfusion and hyperoxia
    • Y.S. Ho, Y. Xiong, D.S. Ho, J. Gao, B.H. Chua, H. Pai, and J.J. Mieyal Targeted disruption of the glutaredoxin 1 gene does not sensitize adult mice to tissue injury induced by ischemia/reperfusion and hyperoxia Free Radic. Biol. Med. 43 2007 1299 1312
    • (2007) Free Radic. Biol. Med. , vol.43 , pp. 1299-1312
    • Ho, Y.S.1    Xiong, Y.2    Ho, D.S.3    Gao, J.4    Chua, B.H.5    Pai, H.6    Mieyal, J.J.7
  • 54
    • 53449095486 scopus 로고    scopus 로고
    • Effect of thioltransferase (glutaredoxin) deletion on cellular sensitivity to oxidative stress and cell proliferation in lens epithelial cells of thioltransferase knockout mouse
    • S. Lofgren, M.R. Fernando, K.Y. Xing, Y. Wang, C.A. Kuszynski, Y.S. Ho, and M.F. Lou Effect of thioltransferase (glutaredoxin) deletion on cellular sensitivity to oxidative stress and cell proliferation in lens epithelial cells of thioltransferase knockout mouse Invest. Ophthalmol. Vis. Sci. 49 2008 4497 4505
    • (2008) Invest. Ophthalmol. Vis. Sci. , vol.49 , pp. 4497-4505
    • Lofgren, S.1    Fernando, M.R.2    Xing, K.Y.3    Wang, Y.4    Kuszynski, C.A.5    Ho, Y.S.6    Lou, M.F.7
  • 55
    • 80255140367 scopus 로고    scopus 로고
    • Glutaredoxin 2 knockout increases sensitivity to oxidative stress in mouse lens epithelial cells
    • H. Wu, L. Lin, F. Giblin, Y.S. Ho, and M.F. Lou Glutaredoxin 2 knockout increases sensitivity to oxidative stress in mouse lens epithelial cells Free Radic. Biol. Med. 51 2011 2108 2117
    • (2011) Free Radic. Biol. Med. , vol.51 , pp. 2108-2117
    • Wu, H.1    Lin, L.2    Giblin, F.3    Ho, Y.S.4    Lou, M.F.5
  • 57
    • 79955668953 scopus 로고    scopus 로고
    • Redox regulation of fertilisation and the spermatogenic process
    • J. Fujii, and S. Tsunoda Redox regulation of fertilisation and the spermatogenic process Asian J. Androl. 13 2011 420 423
    • (2011) Asian J. Androl. , vol.13 , pp. 420-423
    • Fujii, J.1    Tsunoda, S.2
  • 58
    • 0036920229 scopus 로고    scopus 로고
    • Impaired expression of peroxiredoxin 4 in damaged testes by artificial cryptorchidism
    • S. Matsuki, I. Sasagawa, Y. Iuchi, and J. Fujii Impaired expression of peroxiredoxin 4 in damaged testes by artificial cryptorchidism Redox Rep. 7 2002 276 278
    • (2002) Redox Rep. , vol.7 , pp. 276-278
    • Matsuki, S.1    Sasagawa, I.2    Iuchi, Y.3    Fujii, J.4
  • 60
    • 80655125022 scopus 로고    scopus 로고
    • Identification and characterization of alternatively transcribed form of peroxiredoxin IV gene that is specifically expressed in spermatids of postpubertal mouse testis
    • S.H. Yim, Y.J. Kim, S.Y. Oh, J. Fujii, Y. Zhang, V.N. Gladyshev, and S.G. Rhee Identification and characterization of alternatively transcribed form of peroxiredoxin IV gene that is specifically expressed in spermatids of postpubertal mouse testis J. Biol. Chem. 286 2011 39002 39012
    • (2011) J. Biol. Chem. , vol.286 , pp. 39002-39012
    • Yim, S.H.1    Kim, Y.J.2    Oh, S.Y.3    Fujii, J.4    Zhang, Y.5    Gladyshev, V.N.6    Rhee, S.G.7
  • 62
    • 84893849639 scopus 로고    scopus 로고
    • Identification of peroxiredoxin-5 in bovine cauda epididymal sperm
    • S.K. Nagdas, T. Buchanan, and S. Raychoudhury Identification of peroxiredoxin-5 in bovine cauda epididymal sperm Mol. Cell. Biochem. 387 2014 113 121
    • (2014) Mol. Cell. Biochem. , vol.387 , pp. 113-121
    • Nagdas, S.K.1    Buchanan, T.2    Raychoudhury, S.3
  • 67
    • 80455178791 scopus 로고    scopus 로고
    • Glutathione peroxidases at work on epididymal spermatozoa: An example of the dual effect of reactive oxygen species on mammalian male fertilizing ability
    • A. Noblanc, A. Kocer, E. Chabory, P. Vernet, F. Saez, R. Cadet, M. Conrad, and J.R. Drevet Glutathione peroxidases at work on epididymal spermatozoa: an example of the dual effect of reactive oxygen species on mammalian male fertilizing ability J. Androl. 32 2011 641 650
    • (2011) J. Androl. , vol.32 , pp. 641-650
    • Noblanc, A.1    Kocer, A.2    Chabory, E.3    Vernet, P.4    Saez, F.5    Cadet, R.6    Conrad, M.7    Drevet, J.R.8
  • 68
    • 0026353263 scopus 로고
    • Protein thiols in spermatozoa and epididymal fluid of rats
    • J. Seligman, and R. Shalgi Protein thiols in spermatozoa and epididymal fluid of rats J. Reprod. Fertil. 93 1991 399 408
    • (1991) J. Reprod. Fertil. , vol.93 , pp. 399-408
    • Seligman, J.1    Shalgi, R.2
  • 73
    • 0015880650 scopus 로고
    • Effect of selenium, vitamin E, and antioxidants on testicular function in rats
    • S.H. Wu, J.E. Oldfield, P.D. Whanger, and P.H. Weswig Effect of selenium, vitamin E, and antioxidants on testicular function in rats Biol. Reprod. 8 1973 625 629
    • (1973) Biol. Reprod. , vol.8 , pp. 625-629
    • Wu, S.H.1    Oldfield, J.E.2    Whanger, P.D.3    Weswig, P.H.4
  • 74
    • 0020966028 scopus 로고
    • Progressive defects observed in mouse sperm during the course of three generations of selenium deficiency
    • E. Wallace, H.I. Calvin, and G.W. Cooper Progressive defects observed in mouse sperm during the course of three generations of selenium deficiency Gamete Res. 4 1983 377 387
    • (1983) Gamete Res. , vol.4 , pp. 377-387
    • Wallace, E.1    Calvin, H.I.2    Cooper, G.W.3
  • 75
    • 0020964986 scopus 로고
    • Effects of selenium deficiency on the shape and arrangement of rodent sperm mitochondria
    • C.G.W. Wallace E, and H.L. Calvin Effects of selenium deficiency on the shape and arrangement of rodent sperm mitochondria Gamete Res. 4 1983 389 399
    • (1983) Gamete Res. , vol.4 , pp. 389-399
    • Wallace, E.C.G.W.1    Calvin, H.L.2
  • 78
    • 34249654101 scopus 로고    scopus 로고
    • Apolipoprotein e receptor-2 (ApoER2) mediates selenium uptake from selenoprotein P by the mouse testis
    • G.E. Olson, V.P. Winfrey, S.K. Nagdas, K.E. Hill, and R.F. Burk Apolipoprotein E receptor-2 (ApoER2) mediates selenium uptake from selenoprotein P by the mouse testis J. Biol. Chem. 282 2007 12290 12297
    • (2007) J. Biol. Chem. , vol.282 , pp. 12290-12297
    • Olson, G.E.1    Winfrey, V.P.2    Nagdas, S.K.3    Hill, K.E.4    Burk, R.F.5
  • 80
    • 0032227107 scopus 로고    scopus 로고
    • Characterization, regulation of the expression and putative roles of two glutathione peroxidase proteins found in the mouse epididymis
    • V. Schwaab, J.J. Lareyre, P. Vernet, E. Pons, J. Faure, J.P. Dufaure, and J.R. Drevet Characterization, regulation of the expression and putative roles of two glutathione peroxidase proteins found in the mouse epididymis J. Reprod. Fertil. Suppl. 53 1998 157 162
    • (1998) J. Reprod. Fertil. Suppl. , vol.53 , pp. 157-162
    • Schwaab, V.1    Lareyre, J.J.2    Vernet, P.3    Pons, E.4    Faure, J.5    Dufaure, J.P.6    Drevet, J.R.7
  • 84
    • 0020065662 scopus 로고
    • Purification from pig liver of a protein which protects liposomes and biomembranes from peroxidative degradation and exhibits glutathione peroxidase activity on phosphatidylcholine hydroperoxides
    • F. Ursini, M. Maiorino, M. Valente, L. Ferri, and C. Gregolin Purification from pig liver of a protein which protects liposomes and biomembranes from peroxidative degradation and exhibits glutathione peroxidase activity on phosphatidylcholine hydroperoxides Biochim. Biophys. Acta 710 1982 197 211
    • (1982) Biochim. Biophys. Acta , vol.710 , pp. 197-211
    • Ursini, F.1    Maiorino, M.2    Valente, M.3    Ferri, L.4    Gregolin, C.5
  • 85
    • 0024353848 scopus 로고
    • Dynamics of the thiol status of rat spermatozoa during maturation: Analysis with the fluorescent labeling agent monobromobimane
    • R. Shalgi, J. Seligman, and N.S. Kosower Dynamics of the thiol status of rat spermatozoa during maturation: analysis with the fluorescent labeling agent monobromobimane Biol. Reprod. 40 1989 1037 1045
    • (1989) Biol. Reprod. , vol.40 , pp. 1037-1045
    • Shalgi, R.1    Seligman, J.2    Kosower, N.S.3
  • 86
    • 33644670813 scopus 로고    scopus 로고
    • Functional interaction of phospholipid hydroperoxide glutathione peroxidase with sperm mitochondrion-associated cysteine-rich protein discloses the adjacent cysteine motif as a new substrate of the selenoperoxidase
    • M. Maiorino, A. Roveri, L. Benazzi, V. Bosello, P. Mauri, S. Toppo, S.C. Tosatto, and F. Ursini Functional interaction of phospholipid hydroperoxide glutathione peroxidase with sperm mitochondrion-associated cysteine-rich protein discloses the adjacent cysteine motif as a new substrate of the selenoperoxidase J. Biol. Chem. 280 2005 38395 38402
    • (2005) J. Biol. Chem. , vol.280 , pp. 38395-38402
    • Maiorino, M.1    Roveri, A.2    Benazzi, L.3    Bosello, V.4    Mauri, P.5    Toppo, S.6    Tosatto, S.C.7    Ursini, F.8
  • 87
    • 84888434329 scopus 로고    scopus 로고
    • Mouse models for glutathione peroxidase 4 (GPx4)
    • Springer
    • M. Conrad Mouse models for glutathione peroxidase 4 (GPx4) Selenium 2012 Springer 547 559
    • (2012) Selenium , pp. 547-559
    • Conrad, M.1
  • 88
  • 89
    • 0035348255 scopus 로고    scopus 로고
    • Identification of a specific sperm nuclei selenoenzyme necessary for protamine thiol cross-linking during sperm maturation
    • H. Pfeifer, M. Conrad, D. Roethlein, A. Kyriakopoulos, M. Brielmeier, G.W. Bornkamm, and D. Behne Identification of a specific sperm nuclei selenoenzyme necessary for protamine thiol cross-linking during sperm maturation FASEB J. 15 2001 1236 1238
    • (2001) FASEB J. , vol.15 , pp. 1236-1238
    • Pfeifer, H.1    Conrad, M.2    Roethlein, D.3    Kyriakopoulos, A.4    Brielmeier, M.5    Bornkamm, G.W.6    Behne, D.7
  • 90
    • 0037508927 scopus 로고    scopus 로고
    • Testis-specific expression of the nuclear form of phospholipid hydroperoxide glutathione peroxidase (PHGPx)
    • 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) Biol. Chem. 384 2003 635 643
    • (2003) Biol. Chem. , vol.384 , pp. 635-643
    • Moreno, S.G.1    Laux, G.2    Brielmeier, M.3    Bornkamm, G.W.4    Conrad, M.5
  • 92
    • 0028825467 scopus 로고
    • Rat phospholipid-hydroperoxide glutathione peroxidase. CDNA cloning and identification of multiple transcription and translation start sites
    • 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 J. Biol. Chem. 270 1995 26993 26999
    • (1995) J. Biol. Chem. , vol.270 , pp. 26993-26999
    • Pushpa-Rekha, T.R.1    Burdsall, A.L.2    Oleksa, L.M.3    Chisolm, G.M.4    Driscoll, D.M.5
  • 96
    • 71449113005 scopus 로고    scopus 로고
    • Short form glutathione peroxidase 4 is the essential isoform required for survival and somatic mitochondrial functions
    • H. Liang, S.E. Yoo, R. Na, C.A. Walter, A. Richardson, and Q. Ran Short form glutathione peroxidase 4 is the essential isoform required for survival and somatic mitochondrial functions J. Biol. Chem. 284 2009 30836 30844
    • (2009) J. Biol. Chem. , vol.284 , pp. 30836-30844
    • Liang, H.1    Yoo, S.E.2    Na, R.3    Walter, C.A.4    Richardson, A.5    Ran, Q.6
  • 99
    • 79960191503 scopus 로고    scopus 로고
    • Cysteine mutant of mammalian GPx4 rescues cell death induced by disruption of the wild-type selenoenzyme
    • A.M. Mannes, A. Seiler, V. Bosello, M. Maiorino, and M. Conrad Cysteine mutant of mammalian GPx4 rescues cell death induced by disruption of the wild-type selenoenzyme FASEB J. 25 2011 2135 2144
    • (2011) FASEB J. , vol.25 , pp. 2135-2144
    • Mannes, A.M.1    Seiler, A.2    Bosello, V.3    Maiorino, M.4    Conrad, M.5
  • 100
    • 0030348185 scopus 로고    scopus 로고
    • In vitro expression of a mouse tissue specific glutathione-peroxidase-like protein lacking the selenocysteine can protect stably transfected mammalian cells against oxidative damage
    • P. Vernet, N. Rigaudiere, N. 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 Biochem. Cell Biol. 74 1996 125 131
    • (1996) Biochem. Cell Biol. , vol.74 , pp. 125-131
    • Vernet, P.1    Rigaudiere, N.2    Ghyselinck, N.3    Dufaure, J.P.4    Drevet, J.R.5
  • 102
    • 84855719823 scopus 로고    scopus 로고
    • The nuclear form of glutathione peroxidase 4 is associated with sperm nuclear matrix and is required for proper paternal chromatin decondensation at fertilization
    • R. Puglisi, I. Maccari, S. Pipolo, M. Conrad, F. Mangia, and C. Boitani The nuclear form of glutathione peroxidase 4 is associated with sperm nuclear matrix and is required for proper paternal chromatin decondensation at fertilization J. Cell. Physiol. 227 2012 1420 1427
    • (2012) J. Cell. Physiol. , vol.227 , pp. 1420-1427
    • Puglisi, R.1    Maccari, I.2    Pipolo, S.3    Conrad, M.4    Mangia, F.5    Boitani, C.6


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