메뉴 건너뛰기




Volumn 448, Issue , 1999, Pages 1-16

Copper transport in mammals

Author keywords

[No Author keywords available]

Indexed keywords

ALBUMIN; CARRIER PROTEIN; CERULOPLASMIN; COPPER; TRANSCUPREIN; UNCLASSIFIED DRUG;

EID: 0033278330     PISSN: 00652598     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-1-4615-4859-1_1     Document Type: Conference Paper
Times cited : (41)

References (46)
  • 1
    • 0017730323 scopus 로고
    • Binding of zinc to alpha-2-macroglobulin and its role in enzyme binding activity
    • Adham, N.F., Song, M.K., and Rinderknecht, H. (1977). Binding of zinc to alpha-2-macroglobulin and its role in enzyme binding activity. Biochim. Biophys. Acta 495, 212-219
    • (1977) Biochim. Biophys. Acta , vol.495 , pp. 212-219
    • Adham, N.F.1    Song, M.K.2    Rinderknecht, H.3
  • 3
    • 0028058038 scopus 로고
    • The FET3 gene of S. Cerevisiae encodes a multicopper oxidase required for ferrous ion uptake
    • Askwith, C.E., Eide, D., Van Ho, A., et al. (1994). The FET3 gene of S. cerevisiae encodes a multicopper oxidase required for ferrous ion uptake. Cell 76, 403-410.
    • (1994) Cell , vol.76 , pp. 403-410
    • Askwith, C.E.1    Eide, D.2    Van Ho, A.3
  • 4
    • 0024271290 scopus 로고
    • Copper distribution among serum proteins in paediatric liver disorders and malignancies
    • Barrow, L., and Tanner, M.S. (1988). Copper distribution among serum proteins in paediatric liver disorders and malignancies. Eur. J. Clin. Invest. 18, 555-560
    • (1988) Eur. J. Clin. Invest. , vol.18 , pp. 555-560
    • Barrow, L.1    Tanner, M.S.2
  • 5
    • 84960996051 scopus 로고
    • 64Cu in serum fractions following oral administration: An alteration in Wilson's disease
    • 64Cu in serum fractions following oral administration: an alteration in Wilson's disease. Proc. Soc. Exp. Biol. Med. 85, 44-48
    • (1954) Proc. Soc. Exp. Biol. Med. , vol.85 , pp. 44-48
    • Bearn, A.G.1    Kunkel, H.G.2
  • 6
    • 0000028169 scopus 로고
    • Comparison of cupric ion-binding sites in myoglobin derivatives and serum albumin
    • Breslow, E. (1964). Comparison of cupric ion-binding sites in myoglobin derivatives and serum albumin. J. Biol. Chem. 239, 3252-3259
    • (1964) J. Biol. Chem. , vol.239 , pp. 3252-3259
    • Breslow, E.1
  • 8
    • 0028010889 scopus 로고
    • Molecular characterization of a copper transport protein in S. Cerevisiae: An unexpected role for copper in iron transport
    • Dancis, A., Yuan, D.S., Moehle, C., et al. (1994). Molecular characterization of a copper transport protein in S. cerevisiae: an unexpected role for copper in iron transport. Cell 76, 393-402
    • (1994) Cell , vol.76 , pp. 393-402
    • Dancis, A.1    Yuan, D.S.2    Moehle, C.3
  • 9
    • 0026321921 scopus 로고
    • Sequence of rat alpha-1-macroglobulin, a broad-range proteinase inihibitor from the alpha macroglobulin-complement family
    • Eggertsen, G., Hudson, G., Shiels, B., Reed, D., and Fey, G.H. (1991). Sequence of rat alpha-1-macroglobulin, a broad-range proteinase inihibitor from the alpha macroglobulin-complement family. Mol. Biol. Med. 8, 287-302
    • (1991) Mol. Biol. Med. , vol.8 , pp. 287-302
    • Eggertsen, G.1    Hudson, G.2    Shiels, B.3    Reed, D.4    Fey, G.H.5
  • 10
    • 0014440941 scopus 로고
    • The identification of metal-protein complexes by gel chromatography and neutron activation analysis
    • Evans, D.J.R., and Fritze, K. (1969). The identification of metal-protein complexes by gel chromatography and neutron activation analysis. Anal. Chim. Acta 44, 1-7
    • (1969) Anal. Chim. Acta , vol.44 , pp. 1-7
    • Evans, D.J.R.1    Fritze, K.2
  • 11
    • 0022634321 scopus 로고
    • Perspectives in copper biochemistry
    • Frieden, E. (1986). Perspectives in copper biochemistry. Clin. Physiol. Biochem. 4, 11-19
    • (1986) Clin. Physiol. Biochem. , vol.4 , pp. 11-19
    • Frieden, E.1
  • 12
    • 0023897894 scopus 로고
    • Transcriptional regulation of ceruloplasmin gene expression during inflammation
    • Gitlin, J.D. (1988). Transcriptional regulation of ceruloplasmin gene expression during inflammation. J. Biol. Chem. 263, 6281-6287
    • (1988) J. Biol. Chem. , vol.263 , pp. 6281-6287
    • Gitlin, J.D.1
  • 13
    • 0000429702 scopus 로고
    • Ceruloplasmin: An acute phase reactant and anti-oxidant
    • Goldstein, I.M. and Charo, I.F. (1982). Ceruloplasmin: An acute phase reactant and anti-oxidant. Lymphokines 8, 373-411
    • (1982) Lymphokines , vol.8 , pp. 373-411
    • Goldstein, I.M.1    Charo, I.F.2
  • 14
    • 0026335256 scopus 로고
    • Tissue-specific ceruloplasmin gene expression in the mammary gland
    • Jaeger, J.L., Shimizu, N., and Gitlin, J.D. (1991). Tissue-specific ceruloplasmin gene expression in the mammary gland. Biochem. J. 280, 671-677
    • (1991) Biochem. J. , vol.280 , pp. 671-677
    • Jaeger, J.L.1    Shimizu, N.2    Gitlin, J.D.3
  • 15
    • 0017703490 scopus 로고
    • Ferritin synthesis in inflammation. I. Pathogenesis of impaired iron release
    • Konijn, A.M., and Hershko, C. (1977). Ferritin synthesis in inflammation. I. Pathogenesis of impaired iron release. Brit. J. Haematol. 37, 7-16.
    • (1977) Brit. J. Haematol. , vol.37 , pp. 7-16
    • Konijn, A.M.1    Hershko, C.2
  • 16
    • 0019439290 scopus 로고
    • Ferritin synthesis in inflammation. II. Mechanism of increased ferritin synthesis
    • Konijn, A.M., and Hershko, C. (1981), Ferritin synthesis in inflammation. II. Mechanism of increased ferritin synthesis. Brit. J. Haematol. 49, 361-370.
    • (1981) Brit. J. Haematol. , vol.49 , pp. 361-370
    • Konijn, A.M.1    Hershko, C.2
  • 17
    • 0015218694 scopus 로고
    • Ternary coordination complex between human serum albumin, copper (II) and L-histidine
    • Lau, S., and Sarkar, B. (1971). Ternary coordination complex between human serum albumin, copper (II) and L-histidine. J. Biol. Chem. 246, 5938-5943
    • (1971) J. Biol. Chem. , vol.246 , pp. 5938-5943
    • Lau, S.1    Sarkar, B.2
  • 18
    • 0027272944 scopus 로고
    • Ceruloplasmin and copper transport during the latter part of gestation in the rat
    • Lee, S.H., Lancey, R., Montaser, A., Madani. N, and Linder, M.C. (1993), Ceruloplasmin and copper transport during the latter part of gestation in the rat. Proc. Soc. Exp. Biol. Med. 203, 428-439
    • (1993) Proc. Soc. Exp. Biol. Med. , vol.203 , pp. 428-439
    • Lee, S.H.1    Lancey, R.2    Montaser, A.3    Madani, N.4    Linder, M.C.5
  • 20
    • 0000152032 scopus 로고
    • Nutrition and metabolism of the trace elements
    • M.C. Linder, ed, (New York, New York: Elsevier Medical Publishers)
    • Linder, M.C. (1991b). Nutrition and metabolism of the trace elements. In Nutritional Biochemistry and Metabolism, M.C. Linder, ed, (New York, New York: Elsevier Medical Publishers), pp. 215-276
    • (1991) Nutritional Biochemistry and Metabolism , pp. 215-276
    • Linder, M.C.1
  • 21
    • 0001856378 scopus 로고
    • Interactions between copper and iron in mammalian metabolism
    • B. Elsenhans, W. Forth, and K. Schumann, eds. (Gutersloh, Germany: Bertelsmann Foundation Publishers)
    • Linder, M.C. (1993). Interactions between copper and iron in mammalian metabolism. In Metal-Metal Initeractions, B. Elsenhans, W. Forth, and K. Schumann, eds. (Gutersloh, Germany: Bertelsmann Foundation Publishers), pp. 11-41
    • (1993) Metal-metal Initeractions , pp. 11-41
    • Linder, M.C.1
  • 22
    • 0029883795 scopus 로고    scopus 로고
    • Copper biochemistry and molecular biology
    • Linder, M.C., and Hazegh-Azam, M. (1996). Copper biochemistry and molecular biology. Am. J. Clin. Nutr. 63, 797S-811S
    • (1996) Am. J. Clin. Nutr. , vol.63
    • Linder, M.C.1    Hazegh-Azam, M.2
  • 26
    • 0027520019 scopus 로고
    • Intrinsic stoichiometric equilibrium constants for the binding of zinc(II) and copper(II) to the high affinity site of serum albumin
    • Masuoka, J., Hegenauer, J., Van Dyke, B.R., and Saltman, P. (1993). Intrinsic stoichiometric equilibrium constants for the binding of zinc(II) and copper(II) to the high affinity site of serum albumin. J. Biol. Chem. 268, 21533-21537
    • (1993) J. Biol. Chem. , vol.268 , pp. 21533-21537
    • Masuoka, J.1    Hegenauer, J.2    Van Dyke, B.R.3    Saltman, P.4
  • 27
    • 0027180288 scopus 로고
    • Synthesis and turnover of ceruloplasmin in rats treated with 17-beta-estradiol
    • Middleton, R.B., and Linder M.C., (1993). Synthesis and turnover of ceruloplasmin in rats treated with 17-beta-estradiol. Arch. Biochem. Biophys. 302, 362-368
    • (1993) Arch. Biochem. Biophys. , vol.302 , pp. 362-368
    • Middleton, R.B.1    Linder, M.C.2
  • 28
    • 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. (1966). The possible significance of the ferrous oxidase activity of ceruloplasmin in normal human serum. J. Biol. Chem. 241, 2746-2751
    • (1966) J. Biol. Chem. , vol.241 , pp. 2746-2751
    • Osaki, S.1    Johnson, D.A.2    Frieden, E.3
  • 29
    • 0015217690 scopus 로고
    • The mobilization of iron from the perfused mammalian liver by a serum copper enzyme, ferroxidase I
    • Osaki, S., Johnson, D.A. and Frieden, E. (1971). The mobilization of iron from the perfused mammalian liver by a serum copper enzyme, ferroxidase I. J. Biol. Chem. 246, 3018-3023
    • (1971) J. Biol. Chem. , vol.246 , pp. 3018-3023
    • Osaki, S.1    Johnson, D.A.2    Frieden, E.3
  • 31
    • 0021765981 scopus 로고
    • Methylamine-induced conformational change of alpha-2-macroglobulin and its zinc(II) binding capacity. An x-ray scattering study
    • Osterberg, R., and Malmensten, B., (1984). Methylamine-induced conformational change of alpha-2-macroglobulin and its zinc(II) binding capacity. An x-ray scattering study. Eur. J. Biochem. 143, 541-544
    • (1984) Eur. J. Biochem. , vol.143 , pp. 541-544
    • Osterberg, R.1    Malmensten, B.2
  • 32
  • 33
    • 0025907762 scopus 로고
    • Differential regulation of the two mRNA species of the rodent negative acute phase protein alpha-1-inhibitor 3
    • Regler, R., Sickinger, S., and Schweizer, M. (1991). Differential regulation of the two mRNA species of the rodent negative acute phase protein alpha-1-inhibitor 3. FEBS Lett. 282, 368-372
    • (1991) FEBS Lett. , vol.282 , pp. 368-372
    • Regler, R.1    Sickinger, S.2    Schweizer, M.3
  • 35
    • 0027480013 scopus 로고
    • Identification of monomeric alpha-macroglobulin proteinase inhibitors in birds, reptiles, amphibians and mammals, and purification and characterization of a monomeric alpha-macroglobulin proteinase inhibitor from the American bullfrog Rana catesbiana
    • Rubenstein, D.S., Thogersen, I.B., Pizzo, S.V., and Enghild, J.J. (1993). Identification of monomeric alpha-macroglobulin proteinase inhibitors in birds, reptiles, amphibians and mammals, and purification and characterization of a monomeric alpha-macroglobulin proteinase inhibitor from the American bullfrog Rana catesbiana. Biochem. J. 2990, 85-95
    • (1993) Biochem. J. , vol.2990 , pp. 85-95
    • Rubenstein, D.S.1    Thogersen, I.B.2    Pizzo, S.V.3    Enghild, J.J.4
  • 37
    • 0028119827 scopus 로고
    • Compartmental model of copper metabolism in adult men
    • Scott, K.C., and Turnlund, J.R. (1994). Compartmental model of copper metabolism in adult men. J. Nutr. Biochem. 5, 342-350
    • (1994) J. Nutr. Biochem. , vol.5 , pp. 342-350
    • Scott, K.C.1    Turnlund, J.R.2
  • 39
    • 0018102319 scopus 로고
    • Iron and infection
    • Weinberg, E.D. (1978). Iron and infection. Microbiol. Rev. 42, 45-66
    • (1978) Microbiol. Rev. , vol.42 , pp. 45-66
    • Weinberg, E.D.1
  • 40
    • 0022101878 scopus 로고
    • Copper transport in rats involving a new plasma protein
    • Weiss, K.C., and Linder, M.C. (1985). Copper transport in rats involving a new plasma protein. Am. J. Physiol. 249, E77-E88
    • (1985) Am. J. Physiol. , vol.249
    • Weiss, K.C.1    Linder, M.C.2
  • 41
    • 0021925472 scopus 로고
    • Distribution of copper among components of human serum
    • Wirth, P.L., and Linder, M.C. (1985). Distribution of copper among components of human serum. J. Nat. Cancer Inst. 75, 277-284
    • (1985) J. Nat. Cancer Inst. , vol.75 , pp. 277-284
    • Wirth, P.L.1    Linder, M.C.2
  • 42
    • 0027968625 scopus 로고
    • Copper transport in the nagase analbuminemic rat
    • Vargas, E.J., Shoho, A.R., and Linder, M.C. (1994). Copper transport in the Nagase analbuminemic rat. Am. J. Physiol. 267, G259-G269
    • (1994) Am. J. Physiol. , vol.267
    • Vargas, E.J.1    Shoho, A.R.2    Linder, M.C.3
  • 43
    • 0025069640 scopus 로고
    • The valency state of absorbed iron appearing in the portal blood and ceruloplasmin substitution
    • Wollenberg, P., Mahlberg, R. and Rummel, W. (1990). The valency state of absorbed iron appearing in the portal blood and ceruloplasmin substitution. Biol. Metals 3, 1-7.
    • (1990) Biol. Metals , vol.3 , pp. 1-7
    • Wollenberg, P.1    Mahlberg, R.2    Rummel, W.3
  • 44
    • 0030298057 scopus 로고    scopus 로고
    • Ceruloplasmin is found in milk and amniotic fluid and may have a nutritional role
    • Woolen, L., Shulze, R.A., Lacey, R.W., Lietzow, M., and Linder, M.C. (1996). Ceruloplasmin is found in milk and amniotic fluid and may have a nutritional role. J. Nutr. Biochem. 7, 632-639
    • (1996) J. Nutr. Biochem. , vol.7 , pp. 632-639
    • Woolen, L.1    Shulze, R.A.2    Lacey, R.W.3    Lietzow, M.4    Linder, M.C.5
  • 45
    • 0028895749 scopus 로고
    • A mutation in the ceruloplasmin gene is associated with systemic hemosiderosis in humans
    • Yoshida, K., Furihata, K., Takeda, S. (1995). A mutation in the ceruloplasmin gene is associated with systemic hemosiderosis in humans. Nature Genet. 9, 267-272
    • (1995) Nature Genet. , vol.9 , pp. 267-272
    • Yoshida, K.1    Furihata, K.2    Takeda, S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.