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Volumn 291, Issue 45, 2016, Pages 23578-23588

Male subfertility induced by heterozygous expression of catalytically inactive glutathione peroxidase 4 is rescued in vivo by systemic inactivation of the Alox15 gene

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; ANIMALS; BIOLOGICAL ORGANS; ENZYMES; GENES; MAMMALS; MITOCHONDRIA; PEPTIDES; PLANTS (BOTANY);

EID: 84994212708     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M116.738930     Document Type: Article
Times cited : (25)

References (53)
  • 1
    • 84885152034 scopus 로고    scopus 로고
    • The yin and yang of redox regulation
    • Olsen, L. F., and Issinger., O. G., and Guerra, B. (2013) The Yin and Yang of redox regulation. Redox Rep. 18, 245-252
    • (2013) Redox Rep , vol.18 , pp. 245-252
    • Olsen, L.F.1    Issinger, O.G.2    Guerra, B.3
  • 2
    • 84883271387 scopus 로고    scopus 로고
    • Free radicals and antioxidants: How to reestablish redox homeostasis in chronic diseases?
    • Bocci, V., and Valacchi, G. (2013) Free radicals and antioxidants: how to reestablish redox homeostasis in chronic diseases? Curr. Med. Chem. 20, 3397-3415
    • (2013) Curr. Med. Chem , vol.20 , pp. 3397-3415
    • Bocci, V.1    Valacchi, G.2
  • 3
    • 84877816996 scopus 로고    scopus 로고
    • A systematic review of oxidative stress and safety of antioxidants in diabetes: Focus on islets and their defense
    • Karunakaran, U., and Park, K. G. (2013) A systematic review of oxidative stress and safety of antioxidants in diabetes: focus on islets and their defense. Diabetes Metab. J. 37, 106-112
    • (2013) Diabetes Metab. J , vol.37 , pp. 106-112
    • Karunakaran, U.1    Park, K.G.2
  • 4
    • 84876515368 scopus 로고    scopus 로고
    • Oxidative stress in cardiovascular diseases and obesity: Role of p66Shc and protein kinase C
    • DeMarchi, E., Baldassari, F., Bononi, A., Wieckowski, M. R., and Pinton, P. (2013) Oxidative stress in cardiovascular diseases and obesity: role of p66Shc and protein kinase C. Oxid. Med. Cell Longev. 2013, 564961
    • (2013) Oxid. Med. Cell Longev , vol.2013
    • DeMarchi, E.1    Baldassari, F.2    Bononi, A.3    Wieckowski, M.R.4    Pinton, P.5
  • 8
    • 80054052917 scopus 로고    scopus 로고
    • Lipoxygenase and Leukotriene pathways: Biochemistry, biology, and roles in disease
    • Haeggström, J. Z., and Funk, C. D. (2011) Lipoxygenase and leukotriene pathways: biochemistry, biology, and roles in disease. Chem. Rev. 111, 5866-5898
    • (2011) Chem. Rev , vol.111 , pp. 5866-5898
    • Haeggström, J.Z.1    Funk, C.D.2
  • 9
    • 84941939717 scopus 로고    scopus 로고
    • Structural and functional biology of arachidonic acid 15-lipoxygenase-1 (ALOX15)
    • Ivanov, I., Kuhn, H., and Heydeck, D. (2015) Structural and functional biology of arachidonic acid 15-lipoxygenase-1 (ALOX15). Gene 573, 1-32
    • (2015) Gene , vol.573 , pp. 1-32
    • Ivanov, I.1    Kuhn, H.2    Heydeck, D.3
  • 11
    • 0037098867 scopus 로고    scopus 로고
    • Regulation of enzymatic lipid peroxidation: The interplay of peroxidizing and peroxide reducing enzymes
    • Kühn, H., and Borchert, A. (2002) Regulation of enzymatic lipid peroxidation: the interplay of peroxidizing and peroxide reducing enzymes. Free Radic. Biol. Med. 33, 154-172
    • (2002) Free Radic. Biol. Med , vol.33 , pp. 154-172
    • Kühn, H.1    Borchert, A.2
  • 12
    • 0018405264 scopus 로고
    • Rat testis lipoxygenase-like enzyme: Characterization of products from linoleic acid
    • Grossman, S., Shahin, I., and Sredni, B. (1979) Rat testis lipoxygenase-like enzyme: characterization of products from linoleic acid. Biochim. Biophys. Acta 572, 293-297
    • (1979) Biochim. Biophys. Acta , vol.572 , pp. 293-297
    • Grossman, S.1    Shahin, I.2    Sredni, B.3
  • 20
    • 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
  • 23
    • 33745822021 scopus 로고    scopus 로고
    • The role of phospholipid hydroperoxide glutathione peroxidase isoforms in murine embryogenesis
    • Borchert, A., and Wang., C. C., Ufer, C., Schiebel, H., Savaskan, N. E., and Kuhn, H. (2006) The role of phospholipid hydroperoxide glutathione peroxidase isoforms in murine embryogenesis. J. Biol. Chem. 281, 19655-19664
    • (2006) J. Biol. Chem , vol.281 , pp. 19655-19664
    • Borchert, A.1    Wang, C.C.2    Ufer, C.3    Schiebel, H.4    Savaskan, N.E.5    Kuhn, H.6
  • 28
    • 0030789727 scopus 로고    scopus 로고
    • Expression of selenoproteins in various rat and human tissues And cell lines
    • Dreher, I., Schmutzler, C., Jakob, F., and Köhrle, J. (1997) Expression of selenoproteins in various rat and human tissues and cell lines. J. Trace Elem. Med. Biol. 11, 83-91
    • (1997) J. Trace Elem. Med. Biol , vol.11 , pp. 83-91
    • Dreher, I.1    Schmutzler, C.2    Jakob, F.3    Köhrle, J.4
  • 29
    • 0026760653 scopus 로고
    • Phospholipid hydroperoxide glutathione peroxidase of rat testis: Gonadotropin dependence and immunocytochemical identification
    • Roveri, A., Casasco, A., Maiorino, M., Dalan, P., Calligaro, A., and Ursini, F. (1992) Phospholipid hydroperoxide glutathione peroxidase of rat testis: gonadotropin dependence and immunocytochemical identification. J. Biol. Chem. 267, 6142-6146
    • (1992) J. Biol. Chem , vol.267 , pp. 6142-6146
    • Roveri, A.1    Casasco, A.2    Maiorino, M.3    Dalan, P.4    Calligaro, A.5    Ursini, F.6
  • 30
  • 33
    • 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
  • 34
    • 77957005605 scopus 로고    scopus 로고
    • Defining the immunoreactive epitope for the monoclonal anti-human glutathione peroxidase-4 antibody anti-hGPx4 mab63-1
    • Borchert, A., Küttner, G., Giessmann, E., and Wang., C. C., Wessner, H., Volkmer, R., Höhne, W., and Kuhn, H. (2010) Defining the immunoreactive epitope for the monoclonal anti-human glutathione peroxidase-4 antibody anti-hGPx4 Mab63-1. Immunol. Lett. 133, 85-93
    • (2010) Immunol. Lett , vol.133 , pp. 85-93
    • Borchert, A.1    Küttner, G.2    Giessmann, E.3    Wang, C.C.4    Wessner, H.5    Volkmer, R.6    Höhne, W.7    Kuhn, H.8
  • 36
    • 0029915115 scopus 로고    scopus 로고
    • The selenoenzyme phospholipid hydroperoxide glutathione peroxidase controls the activity of the 15-lipoxygenase with complex substrates and preserves the specificity of the oxygenation products
    • Schnurr, K., Belkner, J., Ursini, F., Schewe, T., and Kühn, H. (1996) The selenoenzyme phospholipid hydroperoxide glutathione peroxidase controls the activity of the 15-lipoxygenase with complex substrates and preserves the specificity of the oxygenation products. J. Biol. Chem. 271, 4653-4658
    • (1996) J. Biol. Chem , vol.271 , pp. 4653-4658
    • Schnurr, K.1    Belkner, J.2    Ursini, F.3    Schewe, T.4    Kühn, H.5
  • 37
    • 0032905308 scopus 로고    scopus 로고
    • Inverse regulation of lipidperoxidizing and hydroperoxyl lipid-reducing enzymes by Interleukins 4 and
    • Schnurr, K., Borchert, A., and Kuhn, H. (1999) Inverse regulation of lipidperoxidizing and hydroperoxyl lipid-reducing enzymes by interleukins 4 and FASEB J. 13, 143-154
    • (1999) FASEB J , vol.13 , pp. 143-154
    • Schnurr, K.1    Borchert, A.2    Kuhn, H.3
  • 38
    • 0025084538 scopus 로고
    • Oxygenation of biological membranesbythe pure reticulocyte lipoxygenase
    • Kuhn, H., Belkner, J., Wiesner, R., and Brash, A. R. (1990) Oxygenation of biological membranesbythe pure reticulocyte lipoxygenase. J. Biol. Chem. 265, 18351-18361
    • (1990) J. Biol. Chem , vol.265 , pp. 18351-18361
    • Kuhn, H.1    Belkner, J.2    Wiesner, R.3    Brash, A.R.4
  • 39
    • 0025358908 scopus 로고
    • Subcellular distribution of lipoxygenase products in rabbit reticulocyte membranes
    • Kühn, H., Belkner, J., and Wiesner, R. (1990) Subcellular distribution of lipoxygenase products in rabbit reticulocyte membranes. Eur. J. Biochem. 191, 221-227
    • (1990) Eur. J. Biochem , vol.191 , pp. 221-227
    • Kühn, H.1    Belkner, J.2    Wiesner, R.3
  • 40
    • 46449094871 scopus 로고    scopus 로고
    • Peroxidase: A term of many meanings
    • Flohé, L., and Ursini, F. (2008) Peroxidase: a term of many meanings. Antioxid. Redox Signal. 10, 1485-1490
    • (2008) Antioxid. Redox Signal , vol.10 , pp. 1485-1490
    • Flohé, L.1    Ursini, F.2
  • 42
    • 84923067392 scopus 로고    scopus 로고
    • Glutathione peroxidases as redox sensor proteins in plant cells
    • Passaia, G., and Margis-Pinheiro, M. (2015) Glutathione peroxidases as redox sensor proteins in plant cells. Plant Sci. 234, 22-26
    • (2015) Plant Sci , vol.234 , pp. 22-26
    • Passaia, G.1    Margis-Pinheiro, M.2
  • 44
    • 78651306433 scopus 로고    scopus 로고
    • Bid-mediated mitochondrial damage is a key mechanism in glutamate-induced oxidative stress and AIF-dependent cell death in immortalized HT-22 hippocampal neurons
    • Tobaben, S., Grohm, J., Seiler, A., Conrad, M., Plesnila, N., and Culmsee, C. (2011) Bid-mediated mitochondrial damage is a key mechanism in glutamate-induced oxidative stress and AIF-dependent cell death in immortalized HT-22 hippocampal neurons. Cell Death Differ. 18, 282-292
    • (2011) Cell Death Differ , vol.18 , pp. 282-292
    • Tobaben, S.1    Grohm, J.2    Seiler, A.3    Conrad, M.4    Plesnila, N.5    Culmsee, C.6
  • 48
    • 0029844659 scopus 로고    scopus 로고
    • Disruption of 12/15-lipoxygenase expression in peritoneal macrophages. Enhanced utilization of the 5-lipoxygenase pathway and diminished oxidation of low density lipoprotein
    • Sun, D., and Funk, C. D. (1996) Disruption of 12/15-lipoxygenase expression in peritoneal macrophages. Enhanced utilization of the 5-lipoxygenase pathway and diminished oxidation of low density lipoprotein. J. Biol. Chem. 271, 24055-24062
    • (1996) J. Biol. Chem , vol.271 , pp. 24055-24062
    • Sun, D.1    Funk, C.D.2
  • 49
    • 0027274940 scopus 로고
    • Rat 12-lipoxygenase: Mutations of amino acids implicated in the positional specificity of 15- and 12-lipoxygenases
    • Watanabe, T., and Haeggström, J. Z. (1993) Rat 12-lipoxygenase: mutations of amino acids implicated in the positional specificity of 15- and 12-lipoxygenases. Biochem. Biophys. Res. Commun. 192, 1023-1029
    • (1993) Biochem. Biophys. Res. Commun , vol.192 , pp. 1023-1029
    • Watanabe, T.1    Haeggström, J.Z.2
  • 50
    • 84924956536 scopus 로고    scopus 로고
    • Mutagenesis of triad determinants of rat alox15 alters the specificity of fatty acid and phospholipid oxygenation
    • Pekárová, M., Kuhn, H., Bezáková, L., Ufer, C., and Heydeck, D. (2015) Mutagenesis of triad determinants of rat Alox15 alters the specificity of fatty acid and phospholipid oxygenation. Arch. Biochem. Biophys. 571, 50-57
    • (2015) Arch. Biochem. Biophys , vol.571 , pp. 50-57
    • Pekárová, M.1    Kuhn, H.2    Bezáková, L.3    Ufer, C.4    Heydeck, D.5
  • 51
    • 8244253670 scopus 로고    scopus 로고
    • Attenuation of diet-induced atherosclerosis in rabbits with a highly selective 15-lipoxygenase inhibitor lacking significant antioxidant properties
    • Sendobry, S. M., and Cornicelli., J. A., Welch, K., Bocan, T., Tait, B., and Trivedi., B. K., Colbry, N., Dyer, R. D., and Feinmark., S. J., and Daugherty, A. (1997) Attenuation of diet-induced atherosclerosis in rabbits with a highly selective 15-lipoxygenase inhibitor lacking significant antioxidant properties. Br. J. Pharmacol. 120, 1199-1206
    • (1997) Br. J. Pharmacol , vol.120 , pp. 1199-1206
    • Sendobry, S.M.1    Cornicelli, J.A.2    Welch, K.3    Bocan, T.4    Tait, B.5    Trivedi, B.K.6    Colbry, N.7    Dyer, R.D.8    Feinmark, S.J.9    Daugherty, A.10
  • 52
    • 84939609363 scopus 로고    scopus 로고
    • Differences in ATP generation via glycolysis and oxidative phosphorylation and relationships with sperm motility in mouse species
    • Tourmente, M., Villar-Moya, P., Rial, E., and Roldan, E. R. (2015) Differences in ATP generation via glycolysis and oxidative phosphorylation and relationships with sperm motility in mouse species. J. Biol. Chem. 290, 20613-20626
    • (2015) J. Biol. Chem , vol.290 , pp. 20613-20626
    • Tourmente, M.1    Villar-Moya, P.2    Rial, E.3    Roldan, E.R.4
  • 53
    • 33845261493 scopus 로고
    • A rapid method of total lipid extraction and purification
    • Bligh, E. G., and Dyer, W. J. (1959) A rapid method of total lipid extraction and purification. Can J. Biochem. Physiol. 37, 911-917
    • (1959) Can J. Biochem. Physiol , vol.37 , pp. 911-917
    • Bligh, E.G.1    Dyer, W.J.2


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