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Volumn 290, Issue 23, 2015, Pages 14668-14678

Expression of a catalytically inactive mutant form of glutathione peroxidase 4 (Gpx4) confers a dominant-negative effect in male fertility

Author keywords

[No Author keywords available]

Indexed keywords

CELL DEATH; MITOCHONDRIA; PHOSPHOLIPIDS; PROTEINS;

EID: 84930623244     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M115.656363     Document Type: Article
Times cited : (76)

References (33)
  • 6
    • 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
    • Ursini, F., Maiorino, M., Valente, M., Ferri, L., and Gregolin, C. (1982) 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, 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
  • 7
    • 35348840292 scopus 로고    scopus 로고
    • Physiological role of phospholipid hydroperoxide glutathione peroxidase in mammals
    • Conrad, M., Schneider, M., Seiler, A., and Bornkamm, G. W. (2007) Physiological role of phospholipid hydroperoxide glutathione peroxidase in mammals. Biol. Chem. 388, 1019-1025
    • (2007) Biol. Chem. , vol.388 , pp. 1019-1025
    • Conrad, M.1    Schneider, M.2    Seiler, A.3    Bornkamm, G.W.4
  • 8
    • 0032855506 scopus 로고    scopus 로고
    • Mitochondrial phospholipid hydroperoxide glutathione peroxidase suppresses apoptosis mediated by a mitochondrial death pathway
    • Nomura, K., Imai, H., Koumura, T., Arai, M., and Nakagawa, Y. (1999) Mitochondrial phospholipid hydroperoxide glutathione peroxidase suppresses apoptosis mediated by a mitochondrial death pathway. J. Biol. Chem. 274, 29294-29302
    • (1999) J. Biol. Chem. , vol.274 , pp. 29294-29302
    • Nomura, K.1    Imai, H.2    Koumura, T.3    Arai, M.4    Nakagawa, Y.5
  • 14
    • 84896709062 scopus 로고    scopus 로고
    • Selenium and selenocysteine: Roles in cancer, health, and development
    • Hatfield, D. L., and Tsuji., P. A., Carlson, B. A., and Gladyshev, V. N. (2014) Selenium and selenocysteine: roles in cancer, health, and development. Trends Biochem. Sci. 39, 112-120
    • (2014) Trends Biochem. Sci. , vol.39 , pp. 112-120
    • Hatfield, D.L.1    Tsuji, P.A.2    Carlson, B.A.3    Gladyshev, V.N.4
  • 15
    • 0015880650 scopus 로고
    • Effect of selenium, vitamin E, and antioxidantsontesticular functioninrats
    • Wu, S. H., and Oldfield., J. E., Whanger, P. D., and Weswig, P. H. (1973) Effect of selenium, vitamin E, and antioxidantsontesticular functioninrats. Biol. Reprod. 8, 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
  • 18
    • 0020966028 scopus 로고
    • Progressive defects observed in mouse sperm during the course of three generations of selenium deficiency
    • Wallace, E., and Calvin., H. I., and Cooper, G. W. (1983) Progressive defects observed in mouse sperm during the course of three generations of selenium deficiency. Gamete Res. 7, 377-387
    • (1983) Gamete Res. , vol.7 , pp. 377-387
    • Wallace, E.1    Calvin, H.I.2    Cooper, G.W.3
  • 19
    • 0020964986 scopus 로고
    • Effects of selenium deficiency on the shape and arrangement of rodent sperm mitochondria
    • Wallace E., Cooper, G. W., and Calvin H. L. (1983) Effects of selenium deficiency on the shape and arrangement of rodent sperm mitochondria. Gamete Res. 7, 389-399
    • (1983) Gamete Res. , vol.7 , pp. 389-399
    • Wallace, E.1    Cooper, G.W.2    Calvin, H.L.3
  • 20
    • 0035348255 scopus 로고    scopus 로고
    • Identification of a specific sperm nuclei selenoenzyme necessary for protamine thiol cross-linking during sperm maturation
    • Pfeifer, H., Conrad, M., Roethlein, D., Kyriakopoulos, A., Brielmeier, M., Bornkamm, G. W., and Behne, D. (2001) Identification of a specific sperm nuclei selenoenzyme necessary for protamine thiol cross-linking during sperm maturation. FASEB J. 15, 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
  • 21
    • 23844508188 scopus 로고    scopus 로고
    • The nuclear form of phospholipid hydroperoxide glutathione peroxidase is a protein thiol peroxidase contributing to sperm chromatin stability
    • Conrad, M., and Moreno., S. G., Sinowatz, F., Ursini, F., Kölle, S., Roveri, A., Brielmeier, M., Wurst, W., Maiorino, M., and Bornkamm, G. W. (2005) The nuclear form of phospholipid hydroperoxide glutathione peroxidase is a protein thiol peroxidase contributing to sperm chromatin stability. Mol. Cell. Biol. 25, 7637-7644
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 7637-7644
    • Conrad, M.1    Moreno, S.G.2    Sinowatz, F.3    Ursini, F.4    Kölle, S.5    Roveri, A.6    Brielmeier, M.7    Wurst, W.8    Maiorino, M.9    Bornkamm, G.W.10
  • 22
    • 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
    • Puglisi, R., Maccari, I., Pipolo, S., Conrad, M., Mangia, F., and Boitani, C. (2012) 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, 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
  • 24
    • 0028291969 scopus 로고
    • Enzymatic and immunological measurements of soluble and membrane-bound phospholipid-hydroperoxide glutathione peroxidase
    • Roveri, A., Maiorino, M., and Ursini, F. (1994) Enzymatic and immunological measurements of soluble and membrane-bound phospholipid-hydroperoxide glutathione peroxidase. Methods Enzymol. 233, 202-212
    • (1994) Methods Enzymol. , vol.233 , pp. 202-212
    • Roveri, A.1    Maiorino, M.2    Ursini, F.3
  • 25
    • 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
    • Maiorino, M., Roveri, A., Benazzi, L., Bosello, V., Mauri, P., Toppo, S., Tosatto, S. C., and Ursini, F. (2005) 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, 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
  • 28
    • 0024353848 scopus 로고
    • Dynamics of the thiol status of rat spermatozoa during maturation: Analysis with the fluorescent labeling agent monobromobimane
    • Shalgi, R., Seligman, J., and Kosower, N. S. (1989) Dynamics of the thiol status of rat spermatozoa during maturation: analysis with the fluorescent labeling agent monobromobimane. Biol. Reprod. 40, 1037-1045
    • (1989) Biol. Reprod. , vol.40 , pp. 1037-1045
    • Shalgi, R.1    Seligman, J.2    Kosower, N.S.3
  • 29
    • 0030978102 scopus 로고    scopus 로고
    • Early embryonic lethality caused by targeted disruption of the mouse selenocysteine tRNA gene (Trsp)
    • Bösl, M. R., Takaku, K., Oshima, M., Nishimura, S., and Taketo, M. M. (1997) Early embryonic lethality caused by targeted disruption of the mouse selenocysteine tRNA gene (Trsp). Proc. Natl. Acad. Sci. U.S.A. 94, 5531-5534
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 5531-5534
    • Bösl, M.R.1    Takaku, K.2    Oshima, M.3    Nishimura, S.4    Taketo, M.M.5
  • 30
    • 84921357948 scopus 로고    scopus 로고
    • Expression of inactive glutathione peroxidase 4 leads to embryonic lethality, and inactivation of the alox15 gene does not rescue such knock-in mice
    • Brütsch, S. H., Wang, C. C., Li, L., Stender, H., Neziroglu, N., Richter, C., Kuhn, H., and Borchert, A. (2015) Expression of inactive glutathione peroxidase 4 leads to embryonic lethality, and inactivation of the alox15 gene does not rescue such knock-in mice. Antioxid. Redox Signal. 22, 281-293
    • (2015) Antioxid. Redox Signal. , vol.22 , pp. 281-293
    • Brütsch, S.H.1    Wang, C.C.2    Li, L.3    Stender, H.4    Neziroglu, N.5    Richter, C.6    Kuhn, H.7    Borchert, A.8
  • 31
    • 79960191503 scopus 로고    scopus 로고
    • Cysteine mutant of Mammalian GPx4 rescues cell death induced by disruption of the wild-type selenoenzyme
    • Mannes, A.M., Seiler, A., Bosello, V., Maiorino, M., and Conrad, M. (2011) Cysteine mutant of mammalian GPx4 rescues cell death induced by disruption of the wild-type selenoenzyme. FASEB J. 25, 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
  • 32
    • 0033560765 scopus 로고    scopus 로고
    • Dynamics and efficiency in vivo of UGA-directed selenocysteine insertion at the ribosome
    • Suppmann, S., Persson, B.C., and Böck, A. (1999) Dynamics and efficiency in vivo of UGA-directed selenocysteine insertion at the ribosome. EMBO J. 18, 2284-2293
    • (1999) EMBO J. , vol.18 , pp. 2284-2293
    • Suppmann, S.1    Persson, B.C.2    Böck, A.3
  • 33
    • 34548055862 scopus 로고    scopus 로고
    • Mice overexpressing the mitochondrial phospholipid hydroperoxide glutathione peroxidase in male germ cells show abnormal spermatogenesis and reduced fertility
    • Puglisi, R., Bevilacqua, A., Carlomagno, G., Lenzi, A., Gandini, L., Stefanini, M., Mangia, F., and Boitani, C. (2007) Mice overexpressing the mitochondrial phospholipid hydroperoxide glutathione peroxidase in male germ cells show abnormal spermatogenesis and reduced fertility. Endocrinology 148, 4302-4309
    • (2007) Endocrinology , vol.148 , pp. 4302-4309
    • Puglisi, R.1    Bevilacqua, A.2    Carlomagno, G.3    Lenzi, A.4    Gandini, L.5    Stefanini, M.6    Mangia, F.7    Boitani, C.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.