메뉴 건너뛰기




Volumn 228, Issue 8, 2003, Pages 959-966

Copper,zinc-superoxide dismutase protein but not mRNA is lower in copper-deficient mice and mice lacking the copper chaperone for superoxide dismutase

Author keywords

CCS; Chaperone; Copper,zinc superoxide dismutase; Copper deficient; Enzyme activity, mRNA, Western blots; Mice; Rats

Indexed keywords

CHAPERONE; COPPER; COPPER ZINC SUPEROXIDE DISMUTASE; MESSENGER RNA; SUPEROXIDE DISMUTASE;

EID: 0141736847     PISSN: 15353702     EISSN: None     Source Type: Journal    
DOI: 10.1177/153537020322800812     Document Type: Article
Times cited : (51)

References (36)
  • 1
    • 0014691242 scopus 로고
    • Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein)
    • McCord JM, Fridovich I. Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein). J Biol Chem 244:6049-6055, 1969.
    • (1969) J Biol Chem , vol.244 , pp. 6049-6055
    • McCord, J.M.1    Fridovich, I.2
  • 2
    • 0025957551 scopus 로고
    • Evidence for coregulation of Cu,Zn superoxide dismutase and metallothionein gene expression in yeast through transcriptional control by copper via the ACE 1 factor
    • Carri MT, Galiazzo F, Ciriolo MR, Rotilio G. Evidence for coregulation of Cu,Zn superoxide dismutase and metallothionein gene expression in yeast through transcriptional control by copper via the ACE 1 factor. FEBS Lett 278:263-266, 1991.
    • (1991) FEBS Lett , vol.278 , pp. 263-266
    • Carri, M.T.1    Galiazzo, F.2    Ciriolo, M.R.3    Rotilio, G.4
  • 3
    • 0026046097 scopus 로고
    • ACE1, a copper-dependent transcription factor, activates expression of the yeast copper, zinc superoxide dismutase gene
    • Gralla EB, Thiele DJ, Silar P, Valentine JS. ACE1, a copper-dependent transcription factor, activates expression of the yeast copper, zinc superoxide dismutase gene. Proc Natl Acad Sci U S A 88:8558-8562, 1991.
    • (1991) Proc Natl Acad Sci U S A , vol.88 , pp. 8558-8562
    • Gralla, E.B.1    Thiele, D.J.2    Silar, P.3    Valentine, J.S.4
  • 4
    • 0025098310 scopus 로고
    • Cu,Zn superoxide dismutase and copper deprivation and toxicity in Saccharomyces cerevisiae
    • Greco MA, Hrab DI, Magner W, Kosman DJ. Cu,Zn superoxide dismutase and copper deprivation and toxicity in Saccharomyces cerevisiae. J Bacteriol 172:317-325, 1990.
    • (1990) J Bacteriol , vol.172 , pp. 317-325
    • Greco, M.A.1    Hrab, D.I.2    Magner, W.3    Kosman, D.J.4
  • 5
    • 0023890317 scopus 로고
    • Oxygen-independent induction of enzyme activities related to oxygen metabolism in yeast by copper
    • Galiazzo F, Schiesser A, Rotilio G. Oxygen-independent induction of enzyme activities related to oxygen metabolism in yeast by copper. Biochim Biophys Acta 965:46-51, 1988.
    • (1988) Biochim Biophys Acta , vol.965 , pp. 46-51
    • Galiazzo, F.1    Schiesser, A.2    Rotilio, G.3
  • 6
    • 0024044018 scopus 로고
    • ACE 1 regulates expression of the Saccharomyces cerevisiae metallothionein gene
    • Thiele DJ. ACE1 regulates expression of the Saccharomyces cerevisiae metallothionein gene. Mol Cell Biol 8:2745-2752, 1988.
    • (1988) Mol Cell Biol , vol.8 , pp. 2745-2752
    • Thiele, D.J.1
  • 7
    • 0038153078 scopus 로고
    • A physiological role for Saccharomyces cerevisiae copper/zinc superoxide dismutase in copper buffering
    • Culotta VC, Joh HD, Lin SJ, Slekar KH, Strain J. A physiological role for Saccharomyces cerevisiae copper/zinc superoxide dismutase in copper buffering. J Biol Chem 270:29991-29997, 1995.
    • (1995) J Biol Chem , vol.270 , pp. 29991-29997
    • Culotta, V.C.1    Joh, H.D.2    Lin, S.J.3    Slekar, K.H.4    Strain, J.5
  • 9
    • 0035450413 scopus 로고    scopus 로고
    • Lower copper, zinc-superoxide dismutase protein but not mRNA in organs of copper-deficient rats
    • Prohaska JR, Brokate B. Lower copper, zinc-superoxide dismutase protein but not mRNA in organs of copper-deficient rats. Arch Biochem Biophys 393:170-176, 2001.
    • (2001) Arch Biochem Biophys , vol.393 , pp. 170-176
    • Prohaska, J.R.1    Brokate, B.2
  • 10
    • 0023657163 scopus 로고
    • Regulation of aortic CuZn-superoxide dismutase with copper. Effects in vivo
    • Dameron CT, Harris ED. Regulation of aortic CuZn-superoxide dismutase with copper. Effects in vivo. Biochem J 248:663-668, 1987.
    • (1987) Biochem J , vol.248 , pp. 663-668
    • Dameron, C.T.1    Harris, E.D.2
  • 11
    • 0023888613 scopus 로고
    • Role of copper in the regulation and accumulation of superoxide dismutase and metallothionein in rat liver
    • Chung K, Romero N, Tinker D, Keen CL, Amemiya K, Rucker R. Role of copper in the regulation and accumulation of superoxide dismutase and metallothionein in rat liver. J Nutr 118:859-864, 1988.
    • (1988) J Nutr , vol.118 , pp. 859-864
    • Chung, K.1    Romero, N.2    Tinker, D.3    Keen, C.L.4    Amemiya, K.5    Rucker, R.6
  • 12
    • 0024423078 scopus 로고
    • Dietary copper and the net accumulation of liver and lung superoxide dismutase
    • Tran DD, Romero N, Tinker D, Rucker R. Dietary copper and the net accumulation of liver and lung superoxide dismutase. Nutr Res 9:1161-1166, 1989.
    • (1989) Nutr Res , vol.9 , pp. 1161-1166
    • Tran, D.D.1    Romero, N.2    Tinker, D.3    Rucker, R.4
  • 13
    • 0024741368 scopus 로고
    • Copper activation of superoxide dismutase in rat erythrocytes
    • DiSilvestro RA. Copper activation of superoxide dismutase in rat erythrocytes. Arch Biochem Biophys 274:298-303, 1989.
    • (1989) Arch Biochem Biophys , vol.274 , pp. 298-303
    • DiSilvestro, R.A.1
  • 14
    • 0026321799 scopus 로고
    • Immunoquantitation of rat erythrocyte superoxide dismutase: Its use in copper deficiency
    • Levieux A, Levieux D, Lab C. Immunoquantitation of rat erythrocyte superoxide dismutase: its use in copper deficiency. Free Radical Biol Med 11:589-595, 1991.
    • (1991) Free Radical Biol Med , vol.11 , pp. 589-595
    • Levieux, A.1    Levieux, D.2    Lab, C.3
  • 15
    • 0028106354 scopus 로고
    • Differential decrease of copper content and of copper binding to superoxide dismutase in liver, heart and brain of copper-deficient rats
    • Rossi L, Ciriolo MR, Marchese E, De Martino A, Giorgi M, Rotilio G. Differential decrease of copper content and of copper binding to superoxide dismutase in liver, heart and brain of copper-deficient rats. Biochem Biophys Res Commun 203:1028-1034, 1994.
    • (1994) Biochem Biophys Res Commun , vol.203 , pp. 1028-1034
    • Rossi, L.1    Ciriolo, M.R.2    Marchese, E.3    De Martino, A.4    Giorgi, M.5    Rotilio, G.6
  • 16
    • 0030724620 scopus 로고    scopus 로고
    • Purification of a fully metal-depleted Cu, Zn superoxide dismutase from copper-deficient rat liver
    • Rossi L, Marchese E, De Martino A, Rotilio G, Ciriolo MR. Purification of a fully metal-depleted Cu, Zn superoxide dismutase from copper-deficient rat liver. Biometals 10:257-262, 1997.
    • (1997) Biometals , vol.10 , pp. 257-262
    • Rossi, L.1    Marchese, E.2    De Martino, A.3    Rotilio, G.4    Ciriolo, M.R.5
  • 19
    • 0028102256 scopus 로고
    • Regional specificity in alterations of rat brain copper and catecholamines following perinatal copper deficiency
    • Prohaska JR, Bailey WR. Regional specificity in alterations of rat brain copper and catecholamines following perinatal copper deficiency. J Neurochem 63:1551-1557, 1994.
    • (1994) J Neurochem , vol.63 , pp. 1551-1557
    • Prohaska, J.R.1    Bailey, W.R.2
  • 20
    • 0027321276 scopus 로고
    • Persistent regional changes in brain copper, cuproenzymes and catecholamines following perinatal copper deficiency in mice
    • Prohaska JR, Bailey WR. Persistent regional changes in brain copper, cuproenzymes and catecholamines following perinatal copper deficiency in mice. J Nutr 123:1226-1234, 1993.
    • (1993) J Nutr , vol.123 , pp. 1226-1234
    • Prohaska, J.R.1    Bailey, W.R.2
  • 21
    • 0018178434 scopus 로고
    • A modification of the Lowry procedure to simplify protein determination in membrane and lipoprotein samples
    • Markwell MA, Haas SM, Bieber LL, Tolbert NE. A modification of the Lowry procedure to simplify protein determination in membrane and lipoprotein samples. Anal Biochem 87:206-210, 1978.
    • (1978) Anal Biochem , vol.87 , pp. 206-210
    • Markwell, M.A.1    Haas, S.M.2    Bieber, L.L.3    Tolbert, N.E.4
  • 22
    • 0021087046 scopus 로고
    • Changes in tissue growth, concentrations of copper, iron, cytochrome oxidase and superoxide dismutase subsequent to dietary or genetic copper deficiency in mice
    • Prohaska JR. Changes in tissue growth, concentrations of copper, iron, cytochrome oxidase and superoxide dismutase subsequent to dietary or genetic copper deficiency in mice. J Nutr 113:2048-2058, 1983.
    • (1983) J Nutr , vol.113 , pp. 2048-2058
    • Prohaska, J.R.1
  • 23
    • 0016266425 scopus 로고
    • Total reconstitution of copper-zinc superoxide dismutase
    • Beem KM, Rich WE, Rajagopalan KV. Total reconstitution of copper-zinc superoxide dismutase. J Biol Chem 249:7298-7305, 1974.
    • (1974) J Biol Chem , vol.249 , pp. 7298-7305
    • Beem, K.M.1    Rich, W.E.2    Rajagopalan, K.V.3
  • 24
    • 0032698850 scopus 로고    scopus 로고
    • Copper deficiency alters rat dopamine β-monooxygenase mRNA and activity
    • Prohaska JR, Brokate B. Copper deficiency alters rat dopamine β-monooxygenase mRNA and activity. J Nutr 129:2147-2153, 1999.
    • (1999) J Nutr , vol.129 , pp. 2147-2153
    • Prohaska, J.R.1    Brokate, B.2
  • 25
    • 0034993967 scopus 로고    scopus 로고
    • Dietary copper deficiency alters protein levels of rat dopamine-β-monooxygenase and tyrosine monooxygenase
    • Prohaska JR, Brokate B. Dietary copper deficiency alters protein levels of rat dopamine-β-monooxygenase and tyrosine monooxygenase. Exp Biol Med 226:199-207, 2001.
    • (2001) Exp Biol Med , vol.226 , pp. 199-207
    • Prohaska, J.R.1    Brokate, B.2
  • 26
    • 0036792121 scopus 로고    scopus 로고
    • The timing of perinatal copper deficiency in mice influences offspring survival
    • Prohaska JR, Brokate B. The timing of perinatal copper deficiency in mice influences offspring survival. J Nutr 132:3142-3145, 2002.
    • (2002) J Nutr , vol.132 , pp. 3142-3145
    • Prohaska, J.R.1    Brokate, B.2
  • 27
    • 0016146549 scopus 로고
    • Copper deficiency in the developing rat brain: A possible model for Menkes' steely-hair disease
    • Prohaska JR, Wells WW. Copper deficiency in the developing rat brain: a possible model for Menkes' steely-hair disease. J Neurochem 23:91-98, 1974.
    • (1974) J Neurochem , vol.23 , pp. 91-98
    • Prohaska, J.R.1    Wells, W.W.2
  • 28
    • 0018734969 scopus 로고
    • Changes in activity of the Cu-Zn superoxide dismutase enzyme in tissues of the rat with changes in dietary copper
    • Paynter DI, Moir RJ, Underwood EJ. Changes in activity of the Cu-Zn superoxide dismutase enzyme in tissues of the rat with changes in dietary copper. J Nutr 109:1570-1576, 1979.
    • (1979) J Nutr , vol.109 , pp. 1570-1576
    • Paynter, D.I.1    Moir, R.J.2    Underwood, E.J.3
  • 29
    • 0025755648 scopus 로고
    • Changes in Cu,Zn-superoxide dismutase, cytochrome c oxidase, glutathione peroxidase and glutathione transferase activities in copper-deficient mice and rats
    • Prohaska JR. Changes in Cu,Zn-superoxide dismutase, cytochrome c oxidase, glutathione peroxidase and glutathione transferase activities in copper-deficient mice and rats. J Nutr 121:355-363, 1991.
    • (1991) J Nutr , vol.121 , pp. 355-363
    • Prohaska, J.R.1
  • 32
    • 0030200643 scopus 로고    scopus 로고
    • Proteasome inhibition enhances the stability of mouse Cu/Zn superoxide dismutase with mutations linked to familial amyotrophic lateral sclerosis
    • Hoffman EK, Wilcox HM, Scott RW, Siman R. Proteasome inhibition enhances the stability of mouse Cu/Zn superoxide dismutase with mutations linked to familial amyotrophic lateral sclerosis. J Neurol Sci 139:15-20, 1996.
    • (1996) J Neurol Sci , vol.139 , pp. 15-20
    • Hoffman, E.K.1    Wilcox, H.M.2    Scott, R.W.3    Siman, R.4
  • 33
    • 0014939521 scopus 로고
    • Studies on the rate of release and turnover of ceruloplasmin and apoceruloplasmin in rat plasma
    • Holtzman NA, Gaumnitz BM. Studies on the rate of release and turnover of ceruloplasmin and apoceruloplasmin in rat plasma. J Biol Chem 245:2354-2358, 1970.
    • (1970) J Biol Chem , vol.245 , pp. 2354-2358
    • Holtzman, N.A.1    Gaumnitz, B.M.2
  • 34
    • 0031149967 scopus 로고    scopus 로고
    • Cardiac nuclear encoded cytochrome c oxidase subunits are decreased with copper restriction but not iron restriction: Gene expression, protein synthesis and heat shock protein aspects
    • Medeiros DM, Shiry L, Samelman T. Cardiac nuclear encoded cytochrome c oxidase subunits are decreased with copper restriction but not iron restriction: gene expression, protein synthesis and heat shock protein aspects. Comp Biochem Physiol A Physiol 117:77-87, 1997.
    • (1997) Comp Biochem Physiol A Physiol , vol.117 , pp. 77-87
    • Medeiros, D.M.1    Shiry, L.2    Samelman, T.3
  • 35
    • 0034721928 scopus 로고    scopus 로고
    • Copper activation of superoxide dismutase I (SOD 1) in vivo. Role for protein-protein interactions with the copper chaperone for SODI
    • Schmidt PJ, Kunst C, Culotta VC. Copper activation of superoxide dismutase I (SOD 1) in vivo. Role for protein-protein interactions with the copper chaperone for SODI. J Biol Chem 275:33771-33776, 2000.
    • (2000) J Biol Chem , vol.275 , pp. 33771-33776
    • Schmidt, P.J.1    Kunst, C.2    Culotta, V.C.3
  • 36
    • 0037224817 scopus 로고    scopus 로고
    • Copper deficiency induces the upregulation of the copper chaperone for Cu/Zn superoxide dismutase in weanling male rats
    • Bertinato J, Iskandar M. L'Abbe MR. Copper deficiency induces the upregulation of the copper chaperone for Cu/Zn superoxide dismutase in weanling male rats. J Nutr 133:28-31, 2003.
    • (2003) J Nutr , vol.133 , pp. 28-31
    • Bertinato, J.1    Iskandar, M.2    L'Abbe, M.R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.