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Volumn 319, Issue 1-2, 2008, Pages 125-132

Deficiency of the cystine-transporter gene, xCT, does not exacerbate the deleterious phenotypic consequences of SOD1 knockout in mice

Author keywords

Anemia; Autoantibody; Double knockout; Erythrocyte; Glutathione; Oxidative stress; Reactive oxygen species; Redox; SOD1 knockout; xCT knockout

Indexed keywords

AMINO ACID TRANSPORTER; ANTIOXIDANT; AUTOANTIBODY; COPPER ZINC SUPEROXIDE DISMUTASE; CYSTINE TRANSPORTER; GLUTAMATE TRANSPORTER; GLUTATHIONE; LIPID; REACTIVE OXYGEN METABOLITE; THIOBARBITURIC ACID REACTIVE SUBSTANCE; UNCLASSIFIED DRUG;

EID: 55649102316     PISSN: 03008177     EISSN: 15734919     Source Type: Journal    
DOI: 10.1007/s11010-008-9885-3     Document Type: Article
Times cited : (13)

References (39)
  • 1
    • 0029053451 scopus 로고
    • Superoxide radical and superoxide dismutases
    • doi: 10.1146/annurev.bi.64.070195.000525
    • Fridovich I (1995) Superoxide radical and superoxide dismutases. Annu Rev Biochem 64:97-112. doi: 10.1146/annurev.bi.64.070195.000525
    • (1995) Annu Rev Biochem , vol.64 , pp. 97-112
    • Fridovich, I.1
  • 2
    • 0035914342 scopus 로고    scopus 로고
    • Subcellular distribution of superoxide dismutases (SOD) in rat liver: Cu, Zn-SOD in mitochondria
    • doi: 10.1074/jbc.M105395200
    • Okado-Matsumoto A, Fridovich I (2001) Subcellular distribution of superoxide dismutases (SOD) in rat liver: Cu, Zn-SOD in mitochondria. J Biol Chem 276:38388-38393. doi: 10.1074/jbc.M105395200
    • (2001) J Biol Chem , vol.276 , pp. 38388-38393
    • Okado-Matsumoto, A.1    Fridovich, I.2
  • 3
    • 22244479388 scopus 로고    scopus 로고
    • Copper-zinc superoxide dismutase and amyotrophic lateral sclerosis
    • doi: 10.1146/annurev.biochem.72.121801.161647
    • Valentine JS, Doucette PA, Potter SZ (2005) Copper-zinc superoxide dismutase and amyotrophic lateral sclerosis. Annu Rev Biochem 74:563-593. doi: 10.1146/annurev.biochem.72.121801.161647
    • (2005) Annu Rev Biochem , vol.74 , pp. 563-593
    • Valentine, J.S.1    Doucette, P.A.2    Potter, S.Z.3
  • 4
    • 0028827252 scopus 로고
    • Dilated cardiomyopathy and neonatal lethality in mutant mice lacking manganese superoxide dismutase
    • doi: 10.1038/ng1295-376
    • Li Y, Huang TT, Carlson EJ et al (1995) Dilated cardiomyopathy and neonatal lethality in mutant mice lacking manganese superoxide dismutase. Nat Genet 11:376-381. doi: 10.1038/ng1295-376
    • (1995) Nat Genet , vol.11 , pp. 376-381
    • Li, Y.1    Huang, T.T.2    Carlson, E.J.3
  • 5
    • 0032571387 scopus 로고    scopus 로고
    • Reduced fertility in female mice lacking copper-zinc superoxide dismutase
    • doi: 10.1074/jbc.273.13.7765
    • Ho YS, Gargano M, Cao J et al (1998) Reduced fertility in female mice lacking copper-zinc superoxide dismutase. J Biol Chem 273:7765-7769. doi: 10.1074/jbc.273.13.7765
    • (1998) J Biol Chem , vol.273 , pp. 7765-7769
    • Ho, Y.S.1    Gargano, M.2    Cao, J.3
  • 6
    • 0031760436 scopus 로고    scopus 로고
    • Ovarian function in superoxide dismutase 1 and 2 knockout mice
    • doi: 10.1210/en.139.9.4008
    • Matzuk MM, Dionne L, Guo Q et al (1998) Ovarian function in superoxide dismutase 1 and 2 knockout mice. Endocrinology 139:4008-4011. doi: 10.1210/en.139.9.4008
    • (1998) Endocrinology , vol.139 , pp. 4008-4011
    • Matzuk, M.M.1    Dionne, L.2    Guo, Q.3
  • 7
    • 0032813103 scopus 로고    scopus 로고
    • Age-related cochlear hair cell loss is enhanced in mice lacking copper/ zinc superoxide dismutase
    • doi: 10.1016/S0197-4580(99)00018-4
    • McFadden SL, Ding D, Reaume AG et al (1999) Age-related cochlear hair cell loss is enhanced in mice lacking copper/zinc superoxide dismutase. Neurobiol Aging 20:1-8. doi: 10.1016/S0197-4580(99)00018-4
    • (1999) Neurobiol Aging , vol.20 , pp. 1-8
    • McFadden, S.L.1    Ding, D.2    Reaume, A.G.3
  • 8
    • 0037112407 scopus 로고    scopus 로고
    • Increased superoxide and vascular dysfunction in CuZnSOD-deficient mice
    • doi: 10.1161/01.RES.0000043280.65241.04
    • Didion SP, Ryan MJ, Didion LA et al (2002) Increased superoxide and vascular dysfunction in CuZnSOD-deficient mice. Circ Res 91:938-944. doi: 10.1161/01.RES.0000043280.65241.04
    • (2002) Circ Res , vol.91 , pp. 938-944
    • Didion, S.P.1    Ryan, M.J.2    Didion, L.A.3
  • 9
    • 33746628449 scopus 로고    scopus 로고
    • Drusen, horoidal neovascularization, and retinal pigment epithelium dysfunction in SOD1-deficient mice: A model of age-related macular degeneration
    • doi: 10.1073/pnas.0602131103
    • Imamura Y, Noda S, Hashizume K et al (2006) Drusen, horoidal neovascularization, and retinal pigment epithelium dysfunction in SOD1-deficient mice: A model of age-related macular degeneration. Proc Natl Acad Sci USA 103:11282-11287. doi: 10.1073/pnas.0602131103
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 11282-11287
    • Imamura, Y.1    Noda, S.2    Hashizume, K.3
  • 10
    • 33845969893 scopus 로고    scopus 로고
    • CuZn-SOD deficiency causes ApoB degradation and induces hepatic lipid accumulation by impaired lipoprotein secretion in mice
    • doi: 10.1074/jbc.M603422200
    • Uchiyama S, Shimizu T, Shirasawa T (2006) CuZn-SOD deficiency causes ApoB degradation and induces hepatic lipid accumulation by impaired lipoprotein secretion in mice. J Biol Chem 281:31713-31719. doi: 10.1074/ jbc.M603422200
    • (2006) J Biol Chem , vol.281 , pp. 31713-31719
    • Uchiyama, S.1    Shimizu, T.2    Shirasawa, T.3
  • 11
    • 29244485582 scopus 로고    scopus 로고
    • Organ-specific increase in mutation accumulation and apoptosis rate in CuZn-superoxide dismutase-deficient mice
    • doi: 10.1158/0008-5472.CAN-05-2980
    • Busuttil RA, Garcia AM, Cabrera C et al (2005) Organ-specific increase in mutation accumulation and apoptosis rate in CuZn-superoxide dismutase-deficient mice. Cancer Res 65:11271-11275. doi: 10.1158/ 0008-5472.CAN-05-2980
    • (2005) Cancer Res , vol.65 , pp. 11271-11275
    • Busuttil, R.A.1    Garcia, A.M.2    Cabrera, C.3
  • 12
    • 13244277942 scopus 로고    scopus 로고
    • CuZnSOD deficiency leads to persistent and widespread oxidative damage and hepatocarcinogenesis later in life
    • doi: 10.1038/sj.onc.1208207
    • Elchuri S, Oberley TD, Qi W et al (2005) CuZnSOD deficiency leads to persistent and widespread oxidative damage and hepatocarcinogenesis later in life. Oncogene 24:367-380. doi: 10.1038/sj.onc.1208207
    • (2005) Oncogene , vol.24 , pp. 367-380
    • Elchuri, S.1    Oberley, T.D.2    Qi, W.3
  • 13
    • 15844393658 scopus 로고    scopus 로고
    • Motor neurons in Cu/Zn superoxide dismutase-deficient mice develop normally but exhibit enhanced cell death after axonal injury
    • doi: 10.1038/ng0596-43
    • Reaume AG, Elliott JL, Hoffman EK et al (1996) Motor neurons in Cu/Zn superoxide dismutase-deficient mice develop normally but exhibit enhanced cell death after axonal injury. Nat Genet 3:43-47. doi: 10.1038/ ng0596-43
    • (1996) Nat Genet , vol.3 , pp. 43-47
    • Reaume, A.G.1    Elliott, J.L.2    Hoffman, E.K.3
  • 14
    • 0032860423 scopus 로고    scopus 로고
    • Mice lacking cytosolic copper/zinc superoxide dismutase display a distinctive motor axonopathy
    • Shefner JM, Reaume AG, Flood DG et al (1999) Mice lacking cytosolic copper/zinc superoxide dismutase display a distinctive motor axonopathy. Neurology 53:239-1246
    • (1999) Neurology , vol.53 , pp. 239-1246
    • Shefner, J.M.1    Reaume, A.G.2    Flood, D.G.3
  • 15
    • 0033967008 scopus 로고    scopus 로고
    • Targeted disruption of the mouse Sod I gene makes the hearts vulnerable to ischemic reperfusion injury
    • Yoshida T, Maulik N, Engelman RM et al (2000) Targeted disruption of the mouse Sod I gene makes the hearts vulnerable to ischemic reperfusion injury. Circ Res 86:264-269
    • (2000) Circ Res , vol.86 , pp. 264-269
    • Yoshida, T.1    Maulik, N.2    Engelman, R.M.3
  • 16
    • 21844442581 scopus 로고    scopus 로고
    • Accelerated impairment of spermatogenic cells in sod1-knockout mice under heat stress
    • doi: 10.1080/10715760500130517
    • Ishii T, Matsuki S, Iuchi Y et al (2005) Accelerated impairment of spermatogenic cells in sod1-knockout mice under heat stress. Free Radic Res 39:697-705. doi: 10.1080/10715760500130517
    • (2005) Free Radic Res , vol.39 , pp. 697-705
    • Ishii, T.1    Matsuki, S.2    Iuchi, Y.3
  • 17
    • 34250825268 scopus 로고    scopus 로고
    • Deterioration of ischemia/reperfusion-induced acute renal failure in SOD1-deficient mice
    • doi: 10.1080/10715760601038791
    • Yamanobe T, Okada F, Iuchi Y et al (2007) Deterioration of ischemia/ reperfusion-induced acute renal failure in SOD1-deficient mice. Free Radic Res 41:200-207. doi: 10.1080/10715760601038791
    • (2007) Free Radic Res , vol.41 , pp. 200-207
    • Yamanobe, T.1    Okada, F.2    Iuchi, Y.3
  • 18
    • 33847757480 scopus 로고    scopus 로고
    • Elevated oxidative stress in erythrocytes due to a SOD1 deficiency causes anaemia and triggers autoantibody production
    • doi: 10.1042/BJ20061386
    • Iuchi Y, Okada F, Onuma K et al (2007) Elevated oxidative stress in erythrocytes due to a SOD1 deficiency causes anaemia and triggers autoantibody production. Biochem J 402:219-227. doi: 10.1042/BJ20061386
    • (2007) Biochem J , vol.402 , pp. 219-227
    • Iuchi, Y.1    Okada, F.2    Onuma, K.3
  • 19
    • 0018889650 scopus 로고
    • Changes in the levels of glutathione in phagocytosing human neutrophils
    • Voetman AA, Loos JA, Roos D (1980) Changes in the levels of glutathione in phagocytosing human neutrophils. Blood 55:741-747
    • (1980) Blood , vol.55 , pp. 741-747
    • Voetman, A.A.1    Loos, J.A.2    Roos, D.3
  • 20
    • 0025734987 scopus 로고
    • Glutathione metabolism in activated human neutrophils: Stimulation of glutathione synthesis and consumption of glutathione by reactive oxygen species
    • doi: 10.1111/j.1365-2362.1991.tb01376.x
    • Bilzer M, Lauterburg BH (1991) Glutathione metabolism in activated human neutrophils: Stimulation of glutathione synthesis and consumption of glutathione by reactive oxygen species. Eur J Clin Invest 21:316-322. doi: 10.1111/j.1365-2362.1991.tb01376.x
    • (1991) Eur J Clin Invest , vol.21 , pp. 316-322
    • Bilzer, M.1    Lauterburg, B.H.2
  • 21
    • 0030708939 scopus 로고    scopus 로고
    • Oxidation of neutrophil glutathione and protein thiols by myeloperoxidase-derived hypochlorous acid
    • Carr AC, Winterbourn CC (1997) Oxidation of neutrophil glutathione and protein thiols by myeloperoxidase-derived hypochlorous acid. Biochem J 327:275-281
    • (1997) Biochem J , vol.327 , pp. 275-281
    • Carr, A.C.1    Winterbourn, C.C.2
  • 22
    • 0030995351 scopus 로고    scopus 로고
    • Neutrophil antioxidant capacity during the respiratory burst: Loss of glutathione induced by chloramines
    • doi: 10.1016/S0891-5849(97)00115-9
    • Ogino T, Packer L, Maguire JJ (1997) Neutrophil antioxidant capacity during the respiratory burst: Loss of glutathione induced by chloramines. Free Radic Biol Med 23:445-452. doi: 10.1016/ S0891-5849(97)00115-9
    • (1997) Free Radic Biol Med , vol.23 , pp. 445-452
    • Ogino, T.1    Packer, L.2    Maguire, J.J.3
  • 23
    • 0022638764 scopus 로고
    • Role of membrane transport in metabolism and function of glutathione in mammals
    • doi: 10.1007/BF01870891
    • Bannai S, Tateishi N (1986) Role of membrane transport in metabolism and function of glutathione in mammals. J Membr Biol 89:1-8. doi: 10.1007/ BF01870891
    • (1986) J Membr Biol , vol.89 , pp. 1-8
    • Bannai, S.1    Tateishi, N.2
  • 24
    • 0018963749 scopus 로고
    • Transport interaction of l -cystine and l -glutamate in human diploid fibroblasts in culture
    • Bannai S, Kitamura E (1980) Transport interaction of l -cystine and l -glutamate in human diploid fibroblasts in culture. J Biol Chem 255:2372-2376
    • (1980) J Biol Chem , vol.255 , pp. 2372-2376
    • Bannai, S.1    Kitamura, E.2
  • 25
    • 0023178836 scopus 로고
    • Induction of cystine transport activity in mouse peritoneal macrophages
    • doi: 10.1084/jem.165.3.628
    • Watanabe H, Bannai S (1987) Induction of cystine transport activity in mouse peritoneal macrophages. J Exp Med 165:628-640. doi: 10.1084/ jem.165.3.628
    • (1987) J Exp Med , vol.165 , pp. 628-640
    • Watanabe, H.1    Bannai, S.2
  • 26
    • 33947693792 scopus 로고    scopus 로고
    • Expression and function of cystine/glutamate transporter in neutrophils
    • doi: 10.1189/jlb.0606385
    • Sakakura Y, Sato H, Shiiya A et al (2007) Expression and function of cystine/glutamate transporter in neutrophils. J Leukoc Biol 81:974-982. doi: 10.1189/jlb.0606385
    • (2007) J Leukoc Biol , vol.81 , pp. 974-982
    • Sakakura, Y.1    Sato, H.2    Shiiya, A.3
  • 27
    • 0033597349 scopus 로고    scopus 로고
    • Cloning and expression of a plasma membrane cystine/glutamate exchange transporter composed of two distinct proteins
    • doi: 10.1074/jbc.274.17.11455
    • Sato H, Tamba M, Ishii T et al (1999) Cloning and expression of a plasma membrane cystine/glutamate exchange transporter composed of two distinct proteins. J Biol Chem 274:11455-11458. doi: 10.1074/jbc.274.17.11455
    • (1999) J Biol Chem , vol.274 , pp. 11455-11458
    • Sato, H.1    Tamba, M.2    Ishii, T.3
  • 28
    • 0037160092 scopus 로고    scopus 로고
    • Electrophile response element-mediated induction of the cystine/ glutamate exchange transporter gene expression
    • doi: 10.1074/jbc.M208704200
    • Sasaki H, Sato H, Kuriyama-Matsumura K et al (2004) Electrophile response element-mediated induction of the cystine/glutamate exchange transporter gene expression. J Biol Chem 277:44765-44771. doi: 10.1074/ jbc.M208704200
    • (2004) J Biol Chem , vol.277 , pp. 44765-44771
    • Sasaki, H.1    Sato, H.2    Kuriyama-Matsumura, K.3
  • 29
    • 0024455312 scopus 로고
    • Induction of cystine transport activity in human fibroblasts by oxygen
    • Bannai S, Sato H, Ishii T et al (1989) Induction of cystine transport activity in human fibroblasts by oxygen. J Biol Chem 264:18480-18484
    • (1989) J Biol Chem , vol.264 , pp. 18480-18484
    • Bannai, S.1    Sato, H.2    Ishii, T.3
  • 30
    • 0029057036 scopus 로고
    • Induction of cystine transport activity in mouse peritoneal macrophages by bacterial lipopolysaccharide
    • Sato H, Fujiwara K, Sagara J et al (1995) Induction of cystine transport activity in mouse peritoneal macrophages by bacterial lipopolysaccharide. Biochem J 310:547-551
    • (1995) Biochem J , vol.310 , pp. 547-551
    • Sato, H.1    Fujiwara, K.2    Sagara, J.3
  • 31
    • 27844530663 scopus 로고    scopus 로고
    • Redox imbalance in cystine/glutamate transporter-deficient mice
    • doi: 10.1074/jbc.M506439200
    • Sato H, Shiiya A, Kimata M et al (2005) Redox imbalance in cystine/ glutamate transporter-deficient mice. J Biol Chem 280:37423-37429. doi: 10.1074/jbc.M506439200
    • (2005) J Biol Chem , vol.280 , pp. 37423-37429
    • Sato, H.1    Shiiya, A.2    Kimata, M.3
  • 32
    • 1642494585 scopus 로고    scopus 로고
    • Accumulation of manganese superoxide dismutase under metal-depleted conditions: Proposed role for zinc ions in cellular redox balance
    • doi: 10.1042/BJ20030935
    • Otsu K, Ikeda Y, Fujii J (2004) Accumulation of manganese superoxide dismutase under metal-depleted conditions: Proposed role for zinc ions in cellular redox balance. Biochem J 377:241-248. doi: 10.1042/BJ20030935
    • (2004) Biochem J , vol.377 , pp. 241-248
    • Otsu, K.1    Ikeda, Y.2    Fujii, J.3
  • 33
    • 0036787228 scopus 로고    scopus 로고
    • Differential expression of glutathione reductase and cytosolic glutathione peroxidase, GPX1, in developing rat lungs and kidneys
    • doi: 10.1080/1071576021000006725
    • Fujii T, Endo T, Fujii J et al (2002) Differential expression of glutathione reductase and cytosolic glutathione peroxidase, GPX1, in developing rat lungs and kidneys. Free Radic Res 36:1041-1049. doi: 10.1080/1071576021000006725
    • (2002) Free Radic Res , vol.36 , pp. 1041-1049
    • Fujii, T.1    Endo, T.2    Fujii, J.3
  • 34
    • 0022272493 scopus 로고
    • Determination of glutathione and glutathione disulfide in biological samples
    • doi: 10.1016/S0076-6879(85)13073-9
    • Anderson ME (1985) Determination of glutathione and glutathione disulfide in biological samples. Methods Enzymol 113:548-555. doi: 10.1016/S0076-6879(85)13073-9
    • (1985) Methods Enzymol , vol.113 , pp. 548-555
    • Anderson, M.E.1
  • 35
    • 0024468830 scopus 로고
    • Erythrocytes fail to induce glutathione in response to diethyl maleate or hyperoxia
    • Phelps DT, Deneke SM, Baxter DF et al (1989) Erythrocytes fail to induce glutathione in response to diethyl maleate or hyperoxia. Am J Physiol 257:L272-L276
    • (1989) Am J Physiol , vol.257
    • Phelps, D.T.1    Deneke, S.M.2    Baxter, D.F.3
  • 36
    • 34447636583 scopus 로고    scopus 로고
    • Kinetics of uptake and deacetylation of N-acetylcysteine by human erythrocytes
    • doi: 10.1016/j.biocel.2007.04.014
    • Raftos JE, Whillier S, Chapman BE et al (2007) Kinetics of uptake and deacetylation of N-acetylcysteine by human erythrocytes. Int J Biochem Cell Biol 39:1698-1706. doi: 10.1016/j.biocel.2007.04.014
    • (2007) Int J Biochem Cell Biol , vol.39 , pp. 1698-1706
    • Raftos, J.E.1    Whillier, S.2    Chapman, B.E.3
  • 37
    • 0022259872 scopus 로고
    • Inactivation of glutathione peroxidase by superoxide radical
    • doi: 10.1016/0003-9861(85)90056-6
    • Blum J, Fridovich I (1985) Inactivation of glutathione peroxidase by superoxide radical. Arch Biochem Biophys 240:500-508. doi: 10.1016/ 0003-9861(85)90056-6
    • (1985) Arch Biochem Biophys , vol.240 , pp. 500-508
    • Blum, J.1    Fridovich, I.2
  • 38
    • 0034284002 scopus 로고    scopus 로고
    • Red cells from glutathione peroxidase-1-deficient mice have nearly normal defenses against exogenous peroxides
    • Johnson RM, Goyetter G Jr, Ravindranath Y et al (2000) Red cells from glutathione peroxidase-1-deficient mice have nearly normal defenses against exogenous peroxides. Blood 96:1985-1988
    • (2000) Blood , vol.96 , pp. 1985-1988
    • Johnson, R.M.1    Goyetter Jr., G.2    Ravindranath, Y.3
  • 39
    • 33947204162 scopus 로고    scopus 로고
    • Peroxiredoxin 2 functions as a noncatalytic scavenger of low-level hydrogen peroxide in the erythrocyte
    • doi: 10.1182/blood-2006-09-048728
    • Low FM, Hampton MB, Peskin AV et al (2007) Peroxiredoxin 2 functions as a noncatalytic scavenger of low-level hydrogen peroxide in the erythrocyte. Blood 109:2611-2617. doi: 10.1182/blood-2006-09-048728
    • (2007) Blood , vol.109 , pp. 2611-2617
    • Low, F.M.1    Hampton, M.B.2    Peskin, A.V.3


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