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Volumn 151, Issue 4, 2010, Pages 473-479

Levels of plasma ceruloplasmin protein are markedly lower following dietary copper deficiency in rodents

Author keywords

Assay; Ceruloplasmin; Copper deficient; Ferroxidase; Mouse; Rat

Indexed keywords

AMINE OXIDASE (COPPER CONTAINING); BIOLOGICAL MARKER; CERULOPLASMIN; COPPER; DIAMINE DERIVATIVE; DIANISIDINE; IRON; PARAPHENYLENE DIAMINE; RNA; UNCLASSIFIED DRUG;

EID: 77949288230     PISSN: 15320456     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cbpc.2010.02.005     Document Type: Article
Times cited : (38)

References (33)
  • 1
    • 33646386896 scopus 로고    scopus 로고
    • Decreased hephaestin activity in the intestine of copper-deficient mice causes systemic iron deficiency
    • Chen H., Huang G., Su T., Gao H., Attieh Z.K., McKie A.T., Anderson G.J., and Vulpe C.D. Decreased hephaestin activity in the intestine of copper-deficient mice causes systemic iron deficiency. J. Nutr. 136 (2006) 1236-1241
    • (2006) J. Nutr. , vol.136 , pp. 1236-1241
    • Chen, H.1    Huang, G.2    Su, T.3    Gao, H.4    Attieh, Z.K.5    McKie, A.T.6    Anderson, G.J.7    Vulpe, C.D.8
  • 2
    • 7444243833 scopus 로고    scopus 로고
    • Anemia and impaired stress-induced erythropoiesis in aceruloplasminemic mice
    • Cherukuri S., Tripoulas N.A., Nurko S., and Fox P.L. Anemia and impaired stress-induced erythropoiesis in aceruloplasminemic mice. Blood Cells Mol. Dis. 33 (2004) 346-355
    • (2004) Blood Cells Mol. Dis. , vol.33 , pp. 346-355
    • Cherukuri, S.1    Tripoulas, N.A.2    Nurko, S.3    Fox, P.L.4
  • 3
    • 0037354169 scopus 로고    scopus 로고
    • The copper-iron chronicles: the story of an intimate relationship
    • Fox P.L. The copper-iron chronicles: the story of an intimate relationship. Biometals 16 (2003) 9-40
    • (2003) Biometals , vol.16 , pp. 9-40
    • Fox, P.L.1
  • 4
    • 0016908351 scopus 로고
    • Ceruloplasmin: the copper transport protein with essential oxidase activity
    • Frieden E., and Hsieh H.S. Ceruloplasmin: the copper transport protein with essential oxidase activity. Adv. Enzymol. Rel. Areas Mol. Biol. 44 (1976) 187-236
    • (1976) Adv. Enzymol. Rel. Areas Mol. Biol. , vol.44 , pp. 187-236
    • Frieden, E.1    Hsieh, H.S.2
  • 5
    • 0026521529 scopus 로고
    • Mechanisms of caeruloplasmin biosynthesis in normal and copper-deficient rats
    • Gitlin J.D., Schroeder J.J., Lee-Ambrose L.M., and Cousins R.J. Mechanisms of caeruloplasmin biosynthesis in normal and copper-deficient rats. Biochem. J. 282 (1992) 835-839
    • (1992) Biochem. J. , vol.282 , pp. 835-839
    • Gitlin, J.D.1    Schroeder, J.J.2    Lee-Ambrose, L.M.3    Cousins, R.J.4
  • 7
    • 0032875387 scopus 로고    scopus 로고
    • Targeted gene disruption reveals an essential role for ceruloplasmin in cellular iron efflux
    • Harris Z.L., Durley A.P., Man T.K., and Gitlin J.D. Targeted gene disruption reveals an essential role for ceruloplasmin in cellular iron efflux. Proc. Natl Acad. Sci. USA 96 (1999) 10812-10817
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 10812-10817
    • Harris, Z.L.1    Durley, A.P.2    Man, T.K.3    Gitlin, J.D.4
  • 8
    • 0036400025 scopus 로고    scopus 로고
    • Ceruloplasmin metabolism and function
    • Hellman N.E., and Gitlin J.D. Ceruloplasmin metabolism and function. Annu. Rev. Nutr. 22 (2002) 439-458
    • (2002) Annu. Rev. Nutr. , vol.22 , pp. 439-458
    • Hellman, N.E.1    Gitlin, J.D.2
  • 9
    • 0014939589 scopus 로고
    • Identification of an apoceruloplasmin-like substance in the plasma of copper-deficient rats
    • Holtzman N.A., and Gaumnitz B.M. Identification of an apoceruloplasmin-like substance in the plasma of copper-deficient rats. J. Biol. Chem. 245 (1970) 2350-2353
    • (1970) J. Biol. Chem. , vol.245 , pp. 2350-2353
    • Holtzman, N.A.1    Gaumnitz, B.M.2
  • 10
    • 0014939521 scopus 로고
    • Studies on the rate of release and turnover of ceruloplasmin and apoceruloplasmin in rat plasma
    • Holtzman N.A., and Gaumnitz B.M. Studies on the rate of release and turnover of ceruloplasmin and apoceruloplasmin in rat plasma. J. Biol. Chem. 245 (1970) 2354-2358
    • (1970) J. Biol. Chem. , vol.245 , pp. 2354-2358
    • Holtzman, N.A.1    Gaumnitz, B.M.2
  • 12
    • 0026321799 scopus 로고
    • Immunoquantitation of rat erythrocyte superoxide dismutase: its use in copper deficiency
    • Levieux A., Levieux D., and Lab C. Immunoquantitation of rat erythrocyte superoxide dismutase: its use in copper deficiency. Free Radic. Biol. Med. 11 (1991) 589-595
    • (1991) Free Radic. Biol. Med. , vol.11 , pp. 589-595
    • Levieux, A.1    Levieux, D.2    Lab, C.3
  • 13
    • 0018178434 scopus 로고
    • A modification of the Lowry procedure to simplify protein determination in membrane and lipoprotein samples
    • Markwell M.A., Haas S.M., Bieber L.L., and Tolbert N.E. A modification of the Lowry procedure to simplify protein determination in membrane and lipoprotein samples. Anal. Biochem. 87 (1978) 206-210
    • (1978) Anal. Biochem. , vol.87 , pp. 206-210
    • Markwell, M.A.1    Haas, S.M.2    Bieber, L.L.3    Tolbert, N.E.4
  • 14
    • 0031571216 scopus 로고    scopus 로고
    • Induction of ceruloplasmin synthesis by IFN-gamma in human monocytic cells
    • Mazumder B., Mukhopadhyay C.K., Prok A., Cathcart M.K., and Fox P.L. Induction of ceruloplasmin synthesis by IFN-gamma in human monocytic cells. J. Immunol. 159 (1997) 1938-1944
    • (1997) J. Immunol. , vol.159 , pp. 1938-1944
    • Mazumder, B.1    Mukhopadhyay, C.K.2    Prok, A.3    Cathcart, M.K.4    Fox, P.L.5
  • 15
    • 0025600909 scopus 로고
    • Effects of cellular copper content on copper uptake and metallothionein and ceruloplasmin mRNA levels in mouse hepatocytes
    • McArdle H.J., Mercer J.F., Sargeson A.M., and Danks D.M. Effects of cellular copper content on copper uptake and metallothionein and ceruloplasmin mRNA levels in mouse hepatocytes. J. Nutr. 120 (1990) 1370-1375
    • (1990) J. Nutr. , vol.120 , pp. 1370-1375
    • McArdle, H.J.1    Mercer, J.F.2    Sargeson, A.M.3    Danks, D.M.4
  • 16
    • 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 D.M., Shiry L., and 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 (1997) 77-87
    • (1997) Comp. Biochem. Physiol. A Physiol. , vol.117 , pp. 77-87
    • Medeiros, D.M.1    Shiry, L.2    Samelman, T.3
  • 17
    • 0028092782 scopus 로고
    • Assessment of copper nutritional status
    • Milne D.B. Assessment of copper nutritional status. Clin. Chem. 40 (1994) 1479-1484
    • (1994) Clin. Chem. , vol.40 , pp. 1479-1484
    • Milne, D.B.1
  • 18
    • 2942588454 scopus 로고    scopus 로고
    • Role of copper in the proteosome-mediated degradation of the multicopper oxidase hephaestin
    • Nittis T., and Gitlin J.D. Role of copper in the proteosome-mediated degradation of the multicopper oxidase hephaestin. J. Biol. Chem. 279 (2004) 25696-25702
    • (2004) J. Biol. Chem. , vol.279 , pp. 25696-25702
    • Nittis, T.1    Gitlin, J.D.2
  • 19
    • 0014027719 scopus 로고
    • The possible significance of the ferrous oxidase activity of ceruloplasmin in normal human serum
    • Osaki S., Johnson D.A., and Frieden E. The possible significance of the ferrous oxidase activity of ceruloplasmin in normal human serum. J. Biol. Chem. 241 (1966) 2746-2751
    • (1966) J. Biol. Chem. , vol.241 , pp. 2746-2751
    • Osaki, S.1    Johnson, D.A.2    Frieden, E.3
  • 20
    • 0040369657 scopus 로고
    • Comparison between dietary and genetic copper deficiency in mice: copper-dependent anemia
    • Prohaska J.R. Comparison between dietary and genetic copper deficiency in mice: copper-dependent anemia. Nutr. Res. 1 (1981) 159-167
    • (1981) Nutr. Res. , vol.1 , pp. 159-167
    • Prohaska, J.R.1
  • 21
    • 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 J.R. 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 (1983) 2048-2058
    • (1983) J. Nutr. , vol.113 , pp. 2048-2058
    • Prohaska, J.R.1
  • 22
    • 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 J.R. Changes in Cu, Zn-superoxide dismutase, cytochrome c oxidase, glutathione peroxidase and glutathione transferase activities in copper-deficient mice and rats. J. Nutr. 121 (1991) 355-363
    • (1991) J. Nutr. , vol.121 , pp. 355-363
    • Prohaska, J.R.1
  • 23
    • 33847369883 scopus 로고    scopus 로고
    • Copper
    • Bowman B.A., and Russell R.M. (Eds), International Life Sciences Institute, Washington, DC
    • Prohaska J.R. Copper. In: Bowman B.A., and Russell R.M. (Eds). Present Knowledge In Nutrition, vol. 1 (2006), International Life Sciences Institute, Washington, DC 458-470
    • (2006) Present Knowledge In Nutrition, vol. 1 , pp. 458-470
    • Prohaska, J.R.1
  • 24
    • 0034993967 scopus 로고    scopus 로고
    • Dietary copper deficiency alters protein levels of rat dopamine-beta-monooxygenase and tyrosine monooxygenase
    • Prohaska J.R., and Brokate B. Dietary copper deficiency alters protein levels of rat dopamine-beta-monooxygenase and tyrosine monooxygenase. Exp. Biol. Med. 226 (2001) 199-207
    • (2001) Exp. Biol. Med. , vol.226 , pp. 199-207
    • Prohaska, J.R.1    Brokate, B.2
  • 25
    • 11144285379 scopus 로고    scopus 로고
    • Peptidylglycine-alpha-amidating monooxygenase activity and protein are lower in copper-deficient rats and suckling copper-deficient mice
    • Prohaska J.R., Gybina A.A., Broderius M., and Brokate B. Peptidylglycine-alpha-amidating monooxygenase activity and protein are lower in copper-deficient rats and suckling copper-deficient mice. Arch. Biochem. Biophys. 434 (2005) 212-220
    • (2005) Arch. Biochem. Biophys. , vol.434 , pp. 212-220
    • Prohaska, J.R.1    Gybina, A.A.2    Broderius, M.3    Brokate, B.4
  • 26
    • 33847410167 scopus 로고    scopus 로고
    • Rodent brain and heart catecholamine levels are altered by different models of copper deficiency
    • Pyatskowit J.W., and Prohaska J.R. Rodent brain and heart catecholamine levels are altered by different models of copper deficiency. Comp. Biochem. Physiol. C 145 (2007) 275-281
    • (2007) Comp. Biochem. Physiol. C , vol.145 , pp. 275-281
    • Pyatskowit, J.W.1    Prohaska, J.R.2
  • 27
    • 39749157811 scopus 로고    scopus 로고
    • Copper deficient rats and mice both develop anemia but only rats have lower plasma and brain iron levels
    • Pyatskowit J.W., and Prohaska J.R. Copper deficient rats and mice both develop anemia but only rats have lower plasma and brain iron levels. Comp. Biochem. Physiol. C 147 (2008) 316-323
    • (2008) Comp. Biochem. Physiol. C , vol.147 , pp. 316-323
    • Pyatskowit, J.W.1    Prohaska, J.R.2
  • 28
    • 42549139465 scopus 로고    scopus 로고
    • Multiple mechanisms account for lower plasma iron in young copper deficient rats
    • Pyatskowit J.W., and Prohaska J.R. Multiple mechanisms account for lower plasma iron in young copper deficient rats. Biometals 21 (2008) 343-352
    • (2008) Biometals , vol.21 , pp. 343-352
    • Pyatskowit, J.W.1    Prohaska, J.R.2
  • 29
    • 11844282820 scopus 로고    scopus 로고
    • Dietary copper deficiency reduces iron absorption and duodenal enterocyte hephaestin protein in male and female rats
    • Reeves P.G., Demars L.C., Johnson W.T., and Lukaski H.C. Dietary copper deficiency reduces iron absorption and duodenal enterocyte hephaestin protein in male and female rats. J. Nutr. 135 (2005) 92-98
    • (2005) J. Nutr. , vol.135 , pp. 92-98
    • Reeves, P.G.1    Demars, L.C.2    Johnson, W.T.3    Lukaski, H.C.4
  • 30
    • 0000554334 scopus 로고
    • Standardization of ceruloplasmin activity in terms of International Enzyme Units. Oxidative formation of "Bandrowski's base" from p-phenylenediamine by ceruloplasmin
    • Rice E.W. Standardization of ceruloplasmin activity in terms of International Enzyme Units. Oxidative formation of "Bandrowski's base" from p-phenylenediamine by ceruloplasmin. Anal. Biochem. 3 (1962) 452-456
    • (1962) Anal. Biochem. , vol.3 , pp. 452-456
    • Rice, E.W.1
  • 31
    • 0016331976 scopus 로고
    • Measurement of ceruloplasmin from its oxidase activity in serum by use of o-dianisidine dihydrochloride
    • Schosinsky K.H., Lehmann H.P., and Beeler M.F. Measurement of ceruloplasmin from its oxidase activity in serum by use of o-dianisidine dihydrochloride. Clin. Chem. 20 (1974) 1556-1563
    • (1974) Clin. Chem. , vol.20 , pp. 1556-1563
    • Schosinsky, K.H.1    Lehmann, H.P.2    Beeler, M.F.3
  • 33
    • 77949292454 scopus 로고    scopus 로고
    • Identification of human plasma proteins as major clients for the extracellular chaperone clusterin
    • Wyatt A.R., and Wilson M.R. Identification of human plasma proteins as major clients for the extracellular chaperone clusterin. J. Biol. Chem. 285 (2010) 3532-3539
    • (2010) J. Biol. Chem. , vol.285 , pp. 3532-3539
    • Wyatt, A.R.1    Wilson, M.R.2


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