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Volumn 229, Issue 8, 2004, Pages 756-764

Cu,Zn-Superoxide dismutase is lower and copper chaperone CCS is higher in erythrocytes of copper-deficient rats and mice

Author keywords

Chaperone CCS; Copper deficient; Erythrocytes; Superoxide dismutase

Indexed keywords

BIOLOGICAL MARKER; CHAPERONE; COPPER; COPPER ZINC SUPEROXIDE DISMUTASE; IRON;

EID: 4444274953     PISSN: 15353702     EISSN: None     Source Type: Journal    
DOI: 10.1177/153537020422900807     Document Type: Article
Times cited : (74)

References (32)
  • 1
    • 0037354169 scopus 로고    scopus 로고
    • The copper-iron chronicles: The story of an intimate relationship
    • Fox PL. The copper-iron chronicles: the story of an intimate relationship. Biometals 16:9-40, 2003.
    • (2003) Biometals , vol.16 , pp. 9-40
    • Fox, P.L.1
  • 2
    • 0035458898 scopus 로고    scopus 로고
    • Aluminum, boron, calcium, copper, iron, magnesium, manganese, molybdenum, phosphorus, potassium, sodium, and zinc: Concentrations in common western foods and estimated daily intakes by infants; toddlers; and male and female adolescents, adults, and seniors in the United States
    • Hunt CD, Meacham SL. Aluminum, boron, calcium, copper, iron, magnesium, manganese, molybdenum, phosphorus, potassium, sodium, and zinc: concentrations in common western foods and estimated daily intakes by infants; toddlers; and male and female adolescents, adults, and seniors in the United States. J Am Diet Assoc 101:1058-1060, 2001.
    • (2001) J Am Diet Assoc , vol.101 , pp. 1058-1060
    • Hunt, C.D.1    Meacham, S.L.2
  • 4
    • 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
  • 6
    • 0017125356 scopus 로고
    • Copper deficiency and erythrocuprein (2Cu, 2Zn-superoxide dismutase)
    • Bohnenkamp W, Weser U. Copper deficiency and erythrocuprein (2Cu, 2Zn-superoxide dismutase). Biochim Biophys Acta 444:396-406, 1976.
    • (1976) Biochim Biophys Acta , vol.444 , pp. 396-406
    • Bohnenkamp, W.1    Weser, U.2
  • 7
    • 0018744336 scopus 로고
    • Effects of dietary copper and zinc on erythrocyte superoxide dismutase activity in the chick
    • Bettger WJ, Savage JE, O'Dell BL. Effects of dietary copper and zinc on erythrocyte superoxide dismutase activity in the chick. Nutr Rep Intl 19:893-900, 1979.
    • (1979) Nutr Rep Intl , vol.19 , pp. 893-900
    • Bettger, W.J.1    Savage, J.E.2    O'Dell, B.L.3
  • 8
    • 0018873422 scopus 로고
    • Effects of changes in nutritional copper on erythrocyte superoxide dismutase activity in sheep
    • Andrewartha KA, Caple IW. Effects of changes in nutritional copper on erythrocyte superoxide dismutase activity in sheep. Res Vet Sci 28:101-104, 1980.
    • (1980) Res Vet Sci , vol.28 , pp. 101-104
    • Andrewartha, K.A.1    Caple, I.W.2
  • 9
    • 0018935455 scopus 로고
    • Changes in erythrocyte superoxide dismutase in a patient with copper deficiency
    • Okahata S, Nishi Y, Hatano S, Kobayashi Y, Usui T. Changes in erythrocyte superoxide dismutase in a patient with copper deficiency. Eur J Pediatr 134:121-124, 1980.
    • (1980) Eur J Pediatr , vol.134 , pp. 121-124
    • Okahata, S.1    Nishi, Y.2    Hatano, S.3    Kobayashi, Y.4    Usui, T.5
  • 10
    • 0022374676 scopus 로고
    • Red cell superoxide dismutase activity as an index of human copper nutrition
    • Uauy R, Castillo-Duran C, Fisberg M, Fernandez N, Valenzuela A. Red cell superoxide dismutase activity as an index of human copper nutrition. J Nutr 115:1650-1655, 1985.
    • (1985) J Nutr , vol.115 , pp. 1650-1655
    • Uauy, R.1    Castillo-Duran, C.2    Fisberg, M.3    Fernandez, N.4    Valenzuela, A.5
  • 11
    • 0028092782 scopus 로고
    • Assessment of copper nutritional status
    • Milne DB. Assessment of copper nutritional status. Clin Chem 40:1479-1484, 1994.
    • (1994) Clin Chem , vol.40 , pp. 1479-1484
    • Milne, D.B.1
  • 12
    • 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
  • 13
    • 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 Radic Biol Med 11:589-595, 1991.
    • (1991) Free Radic Biol Med , vol.11 , pp. 589-595
    • Levieux, A.1    Levieux, D.2    Lab, C.3
  • 14
    • 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
  • 15
    • 0141736847 scopus 로고    scopus 로고
    • Copper,Zinc-superoxide dismutase protein but not mRNA is lower in copper-deficient mice and mice lacking the copper chaperone for superoxide dismutase
    • Prohaska JR, Geissler J, Brokate B, Broderius M. Copper,Zinc-superoxide dismutase protein but not mRNA is lower in copper-deficient mice and mice lacking the copper chaperone for superoxide dismutase. Exp Biol Med 228:959-966, 2003.
    • (2003) Exp Biol Med , vol.228 , pp. 959-966
    • Prohaska, J.R.1    Geissler, J.2    Brokate, B.3    Broderius, M.4
  • 16
    • 0043164959 scopus 로고    scopus 로고
    • Metallochaperone for Cu,Zn-superoxide dismutase (CCS) protein but not mRNA is higher in organs from copper-deficient mice and rats
    • Prohaska JR, Broderius M, Brokate B. Metallochaperone for Cu,Zn-superoxide dismutase (CCS) protein but not mRNA is higher in organs from copper-deficient mice and rats. Arch Biochem Biophys 417:227-234, 2003.
    • (2003) Arch Biochem Biophys , vol.417 , pp. 227-234
    • Prohaska, J.R.1    Broderius, M.2    Brokate, B.3
  • 17
    • 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
  • 18
    • 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
  • 19
    • 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
  • 20
    • 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
  • 22
    • 0021811365 scopus 로고
    • Binding of glycolytic enzymes to cardiac sarcolemmal and sarcoplasmic reticular membranes
    • Pierce GN, Philipson KD. Binding of glycolytic enzymes to cardiac sarcolemmal and sarcoplasmic reticular membranes. J Biol Chem 260:6862-6870, 1985.
    • (1985) J Biol Chem , vol.260 , pp. 6862-6870
    • Pierce, G.N.1    Philipson, K.D.2
  • 23
    • 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
  • 25
    • 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
  • 27
    • 0942279589 scopus 로고    scopus 로고
    • Contrasting and cooperative effects of copper and iron deficiencies in male rats fed different concentrations of manganese and different sources of sulfur amino acids in an AIN-93G-based diet
    • Reeves PG, Ralston NV, Idso JP, Lukaski HC. Contrasting and cooperative effects of copper and iron deficiencies in male rats fed different concentrations of manganese and different sources of sulfur amino acids in an AIN-93G-based diet. J Nutr 134:416-425, 2004.
    • (2004) J Nutr , vol.134 , pp. 416-425
    • Reeves, P.G.1    Ralston, N.V.2    Idso, J.P.3    Lukaski, H.C.4
  • 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
  • 30
    • 0042858163 scopus 로고    scopus 로고
    • Mechanisms of biosynthesis of mammalian copper/zinc superoxide dismutase
    • Bartnikas TB, Gitlin JD. Mechanisms of biosynthesis of mammalian copper/zinc superoxide dismutase. J Biol Chem 278:33602-33608, 2003.
    • (2003) J Biol Chem , vol.278 , pp. 33602-33608
    • Bartnikas, T.B.1    Gitlin, J.D.2
  • 32
    • 0042317107 scopus 로고    scopus 로고
    • Copper modulates the degradation of copper chaperone for Cu,Zn superoxide dismutase by the 26 S proteosome
    • Bertinato J, L'Abbe MR. Copper modulates the degradation of copper chaperone for Cu,Zn superoxide dismutase by the 26 S proteosome. J Biol Chem 278:35071-35078, 2003.
    • (2003) J Biol Chem , vol.278 , pp. 35071-35078
    • Bertinato, J.1    L'Abbe, M.R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.