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Volumn 38, Issue 4, 2010, Pages 947-951

Interactions of caeruloplasmin with other proteins participating in inflammation

Author keywords

Caeruloplasmin; Inflammation; Lactoferrin; Myeloperoxidase; Protein protein interaction

Indexed keywords

CERULOPLASMIN; LACTOFERRIN; MYELOPEROXIDASE;

EID: 77955936131     PISSN: 03005127     EISSN: 14708752     Source Type: Journal    
DOI: 10.1042/BST0380947     Document Type: Review
Times cited : (24)

References (50)
  • 1
    • 15844384254 scopus 로고    scopus 로고
    • Genetic and molecular basis for copper toxicity
    • Harris, Z.L. and Gitlin, J.D. (1996) Genetic and molecular basis for copper toxicity. Am. J. Clin. Nutr. 63, 836S-841S
    • (1996) Am. J. Clin. Nutr. , vol.63
    • Harris, Z.L.1    Gitlin, J.D.2
  • 2
    • 0001036447 scopus 로고
    • Investigations in serum copper. II. Isolation of the copper-containing protein and a description of some of its properties
    • Holmberg, C.G. and Laurell, C.B. (1948) Investigations in serum copper. II. Isolation of the copper-containing protein and a description of some of its properties. Acta Chem. Scand. 2, 550-556
    • (1948) Acta Chem. Scand. , vol.2 , pp. 550-556
    • Holmberg, C.G.1    Laurell, C.B.2
  • 3
    • 0023664014 scopus 로고
    • Rat ceruloplasmin: Molecular cloning and gene expression in choroids plexus, yolk sac, placenta, and testis
    • Aldred, A.R., Grimes, A., Schreiber, G. and Mercer, J.F. (1987) Rat ceruloplasmin: molecular cloning and gene expression in choroids plexus, yolk sac, placenta, and testis. J. Biol. Chem. 262, 2875-2878
    • (1987) J. Biol. Chem. , vol.262 , pp. 2875-2878
    • Aldred, A.R.1    Grimes, A.2    Schreiber, G.3    Mercer, J.F.4
  • 4
    • 0030036172 scopus 로고    scopus 로고
    • Ceruloplasmin gene expression in the murine central nervous system
    • Klomp, L.W.J., Farhangrazi, Z.S., Dugan, L.L. and Gitlin, J.D. (1996) Ceruloplasmin gene expression in the murine central nervous system. J. Clin. Invest. 98, 207-215
    • (1996) J. Clin. Invest. , vol.98 , pp. 207-215
    • Klomp, L.W.J.1    Farhangrazi, Z.S.2    Dugan, L.L.3    Gitlin, J.D.4
  • 6
    • 0006615873 scopus 로고
    • Structural model of human ceruloplasmin based on internal triplication, hydrophilic/hydrophobic character, and secondary structure of domains
    • Ortel, T.L., Takahashi, N. and Putnam, F.W. (1984) Structural model of human ceruloplasmin based on internal triplication, hydrophilic/hydrophobic character, and secondary structure of domains. Proc. Natl. Acad. Sci. U.S.A. 81, 4761-4765
    • (1984) Proc. Natl. Acad. Sci. U.S.A. , vol.81 , pp. 4761-4765
    • Ortel, T.L.1    Takahashi, N.2    Putnam, F.W.3
  • 8
    • 0001159410 scopus 로고
    • Quantitative electron spin resonance studies on native and denatured ceruloplasmin and laccase
    • Broman, L., Malmstrom, B.G., Aasa, R. and Vanngard, T. (1962) Quantitative electron spin resonance studies on native and denatured ceruloplasmin and laccase. J. Mol. Biol. 5, 301-310
    • (1962) J. Mol. Biol. , vol.5 , pp. 301-310
    • Broman, L.1    Malmstrom, B.G.2    Aasa, R.3    Vanngard, T.4
  • 9
    • 0002160369 scopus 로고
    • Some aspects of structure and function in copper containing oxidases
    • Williams, R.J.P. and Da Silva, J.RR.F., eds Academic Press, New York
    • Malmstrom, B.G. (1978) Some aspects of structure and function in copper containing oxidases. in New Trends in Bioinorganic Chemistry (Williams, R.J.P. and Da Silva, J.RR.F., eds), pp. 59-77, Academic Press, New York
    • (1978) New Trends in Bioinorganic Chemistry , pp. 59-77
    • Malmstrom, B.G.1
  • 10
    • 0032758350 scopus 로고    scopus 로고
    • An X-ray crystallographic study of the binding center of azide inhibitor and organic substrates of ceruloplasmin, a multi-copper oxidase in plasma
    • Zaitsev, V.N., Zaitseva, I., Papiz, M. and Lindley, P.L. (1999) An X-ray crystallographic study of the binding center of azide inhibitor and organic substrates of ceruloplasmin, a multi-copper oxidase in plasma. J. Biol. Inorg. Chem. 4, 579-587
    • (1999) J. Biol. Inorg. Chem. , vol.4 , pp. 579-587
    • Zaitsev, V.N.1    Zaitseva, I.2    Papiz, M.3    Lindley, P.L.4
  • 11
    • 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
  • 12
    • 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
  • 13
    • 0036400025 scopus 로고    scopus 로고
    • Ceruloplasmin metabolism and function
    • Hellman, N.E. and Gitlin, J.D. (2002) Ceruloplasmin metabolism and function. Annu. Rev. Nutr. 22, 439-458
    • (2002) Annu. Rev. Nutr. , vol.22 , pp. 439-458
    • Hellman, N.E.1    Gitlin, J.D.2
  • 14
    • 0037354169 scopus 로고    scopus 로고
    • The copper-iron chronicles: The story of an intimate relationship
    • Fox, P.L. (2003) The copper-iron chronicles: the story of an intimate relationship. Biometals 16, 9-40
    • (2003) Biometals , vol.16 , pp. 9-40
    • Fox, P.L.1
  • 15
    • 47649126246 scopus 로고    scopus 로고
    • Forging a field: The golden age of iron biology
    • Andrews, N.C. (2008) Forging a field: the golden age of iron biology. Blood 112, 219-230
    • (2008) Blood , vol.112 , pp. 219-230
    • Andrews, N.C.1
  • 16
    • 0031981976 scopus 로고    scopus 로고
    • Aceruloplasminemia: An inherited neurodegenerative disease with impaired iron homeostasis
    • Harris, Z.L., Klomp, L.W. and Gitlin, J.D. (1998) Aceruloplasminemia: an inherited neurodegenerative disease with impaired iron homeostasis. Am. J. Clin. Nutr. 67, 972S-977S
    • (1998) Am. J. Clin. Nutr. , vol.67
    • Harris, Z.L.1    Klomp, L.W.2    Gitlin, J.D.3
  • 18
    • 0038711587 scopus 로고    scopus 로고
    • GPI-anchored ceruloplasmin is required for iron efflux from cells in the central nervous system
    • Jeong, S.Y. and David, S. (2003) GPI-anchored ceruloplasmin is required for iron efflux from cells in the central nervous system. J. Biol. Chem. 278, 27144-27148
    • (2003) J. Biol. Chem. , vol.278 , pp. 27144-27148
    • Jeong, S.Y.1    David, S.2
  • 19
    • 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. (1999) Targeted gene disruption reveals an essential role for ceruloplasmin in cellular iron efflux. Proc. Natl. Acad. Sci. U.S.A. 96, 10812-10817
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 10812-10817
    • Harris, Z.L.1    Durley, A.P.2    Man, T.K.3    Gitlin, J.D.4
  • 20
  • 21
    • 0034282914 scopus 로고    scopus 로고
    • Intact human ceruloplasmin is required for the incorporation of iron into human ferritin
    • Van Eden, M.E. and Aust, S.D. (2000) Intact human ceruloplasmin is required for the incorporation of iron into human ferritin. Arch. Biochem. Biophys. 381, 119-126
    • (2000) Arch. Biochem. Biophys. , vol.381 , pp. 119-126
    • Van Eden, M.E.1    Aust, S.D.2
  • 22
    • 0000852301 scopus 로고
    • Deficiency of ceruloplasmin in patients with hepatolenticular degeneration (Wilson's disease)
    • Scheinberg, I.H. and Gitlin, D. (1952) Deficiency of ceruloplasmin in patients with hepatolenticular degeneration (Wilson's disease). Science 116, 484-489
    • (1952) Science , vol.116 , pp. 484-489
    • Scheinberg, I.H.1    Gitlin, D.2
  • 23
    • 27544442658 scopus 로고    scopus 로고
    • Ceruloplasmin in neurodegenerative diseases
    • Vassiliev, V., Harris, Z.L. and Zatta, P. (2005) Ceruloplasmin in neurodegenerative diseases. Brain Res. Rev. 49, 633-640
    • (2005) Brain Res. Rev. , vol.49 , pp. 633-640
    • Vassiliev, V.1    Harris, Z.L.2    Zatta, P.3
  • 24
    • 0015311157 scopus 로고
    • Interaction of some centrally active drugs with ceruloplasmin
    • Barrass, B.C. and Coult, D.B. (1972) Interaction of some centrally active drugs with ceruloplasmin. Biochem. Pharmacol. 21, 677-685
    • (1972) Biochem. Pharmacol. , vol.21 , pp. 677-685
    • Barrass, B.C.1    Coult, D.B.2
  • 25
    • 0015354899 scopus 로고
    • 3-Hydroxy-4-methoxyphenethylamine: The endogeneous toxin of parkinsonism?
    • Barrass, B.C., Coult, D.B. and Pinder, R.M. (1972) 3-Hydroxy-4- methoxyphenethylamine: the endogeneous toxin of parkinsonism? J. Pharm. Pharmacol. 24, 499-500
    • (1972) J. Pharm. Pharmacol. , vol.24 , pp. 499-500
    • Barrass, B.C.1    Coult, D.B.2    Pinder, R.M.3
  • 26
    • 0015866638 scopus 로고
    • Substrate specificity of caeruloplasmin. Indoles and indole isosters
    • Barrass, B.C., Coult, D.B., Pinder, R.M. and Skeels, M. (1973) Substrate specificity of caeruloplasmin. Indoles and indole isosters. Biochem. Pharmacol. 22, 2891-2895
    • (1973) Biochem. Pharmacol. , vol.22 , pp. 2891-2895
    • Barrass, B.C.1    Coult, D.B.2    Pinder, R.M.3    Skeels, M.4
  • 27
    • 0015969693 scopus 로고
    • Substrate specificity of caeruloplasmin: Phenylalkylamine substrates
    • Barrass, B.C., Coult, D.B., Rich, P. and Tutt, K.J. (1974) Substrate specificity of caeruloplasmin: phenylalkylamine substrates. Biochem. Pharmacol. 23, 47-56
    • (1974) Biochem. Pharmacol. , vol.23 , pp. 47-56
    • Barrass, B.C.1    Coult, D.B.2    Rich, P.3    Tutt, K.J.4
  • 28
    • 0033570220 scopus 로고    scopus 로고
    • The multifunctional oxidase activity of ceruloplasmin as revealed by anion binding studies
    • Musci, G., Bellenchi, G.C. and Calabrese, L. (1999) The multifunctional oxidase activity of ceruloplasmin as revealed by anion binding studies. Eur. J. Biochem. 265, 589-597.
    • (1999) Eur. J. Biochem. , vol.265 , pp. 589-597
    • Musci, G.1    Bellenchi, G.C.2    Calabrese, L.3
  • 30
    • 0016378870 scopus 로고
    • The generation of hydrogen peroxide, superoxide radical, and hydroxyl radical by 6-hydroxydopamine, dialuric acid, and related cytotoxic agents
    • Cohen, G. and Heikkila, R.E. (1974) The generation of hydrogen peroxide, superoxide radical, and hydroxyl radical by 6-hydroxydopamine, dialuric acid, and related cytotoxic agents. J. Biol. Chem. 249, 2447-2452
    • (1974) J. Biol. Chem. , vol.249 , pp. 2447-2452
    • Cohen, G.1    Heikkila, R.E.2
  • 31
    • 0032126999 scopus 로고    scopus 로고
    • Studies on the interaction between ferritin and ceruloplasmin
    • Juan, S.-H. and Aust, S.D. (1998) Studies on the interaction between ferritin and ceruloplasmin. Arch. Biochem. Biophys. 355, 56-62
    • (1998) Arch. Biochem. Biophys. , vol.355 , pp. 56-62
    • Juan, S.-H.1    Aust, S.D.2
  • 32
    • 0030894460 scopus 로고    scopus 로고
    • Binding and inhibition of myeloperoxidase (MPO): A major function of ceruloplasmin?
    • Segelmark, M., Persson, B., Hellmark, T. and Wieslander, J. (1997) Binding and inhibition of myeloperoxidase (MPO): a major function of ceruloplasmin? Clin. Exp. Immunol. 108, 167-174
    • (1997) Clin. Exp. Immunol. , vol.108 , pp. 167-174
    • Segelmark, M.1    Persson, B.2    Hellmark, T.3    Wieslander, J.4
  • 34
    • 0036191387 scopus 로고    scopus 로고
    • The physiology of lactoferrin
    • Brock, J.H. (2002) The physiology of lactoferrin. Biochem. Cell Biol. 80, 1-6
    • (2002) Biochem. Cell Biol. , vol.80 , pp. 1-6
    • Brock, J.H.1
  • 35
    • 0018899060 scopus 로고
    • Lactoferrin in human milk: Its role in iron absorption and protection against enteric infection in the newborn infant
    • Brock, J.H. (1980) Lactoferrin in human milk: its role in iron absorption and protection against enteric infection in the newborn infant. Arch. Dis. Child. 55, 417-421
    • (1980) Arch. Dis. Child. , vol.55 , pp. 417-421
    • Brock, J.H.1
  • 36
    • 0018868141 scopus 로고
    • Bactericidal activity of human lactoferrin: Sensitivity of a variety of microorganisms
    • Arnold, R.R., Brewer, M. and Gauthier, J.J. (1980) Bactericidal activity of human lactoferrin: sensitivity of a variety of microorganisms. Infect. Immun. 28, 893-898
    • (1980) Infect. Immun. , vol.28 , pp. 893-898
    • Arnold, R.R.1    Brewer, M.2    Gauthier, J.J.3
  • 41
    • 0024991498 scopus 로고
    • Characterization of an interaction between Protein C and ceruloplasmin
    • Walker, F.J. and Fay, P.J. (1990) Characterization of an interaction between Protein C and ceruloplasmin. J. Biol. Chem. 265, 1834-1836
    • (1990) J. Biol. Chem. , vol.265 , pp. 1834-1836
    • Walker, F.J.1    Fay, P.J.2
  • 49
    • 70749099050 scopus 로고    scopus 로고
    • Study of interaction of ceruloplasmin, lactoferrin, and myeloperoxidase by photon correlation spectroscopy
    • Moscow
    • Sokolov, A.V., Prozorovskii, V.N. and Vasilyev, V.B. (2009) Study of interaction of ceruloplasmin, lactoferrin, and myeloperoxidase by photon correlation spectroscopy. Biochemistry (Moscow) 74, 1225-1227
    • (2009) Biochemistry , vol.74 , pp. 1225-1227
    • Sokolov, A.V.1    Prozorovskii, V.N.2    Vasilyev, V.B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.