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Volumn 207, Issue 1-2, 2003, Pages 108-109

Aceruloplasminemia

Author keywords

[No Author keywords available]

Indexed keywords

CERULOPLASMIN; FERROUS ION; GLYCOPROTEIN; IRON BINDING PROTEIN;

EID: 12244281826     PISSN: 0022510X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-510X(02)00434-3     Document Type: Conference Paper
Times cited : (25)

References (24)
  • 1
    • 0023240051 scopus 로고
    • Familial apoceruloplasmin deficiency associated with blepharospasm and retinal degeneration
    • Miyajima H., Nishimura Y., Mizoguchi K.et al. Familial apoceruloplasmin deficiency associated with blepharospasm and retinal degeneration. Neurology. 37:1987;761-767.
    • (1987) Neurology , vol.37 , pp. 761-767
    • Miyajima, H.1    Nishimura, Y.2    Mizoguchi, K.3
  • 2
    • 0028903259 scopus 로고
    • Aceruloplasminemia: Molecular characterization of this disorder of iron metabolism
    • Harris Z.L., Takahashi Y., Miyajima H.et al. Aceruloplasminemia: molecular characterization of this disorder of iron metabolism. Proc. Natl. Acad. Sci. U. S. A. 92:1995;2539-2543.
    • (1995) Proc. Natl. Acad. Sci. U. S. A. , vol.92 , pp. 2539-2543
    • Harris, Z.L.1    Takahashi, Y.2    Miyajima, H.3
  • 3
    • 0028895749 scopus 로고
    • A mutation in the ceruloplasmin gene is associated with systemic hemosiderosis in humans
    • Yoshida K., Furihata K., Takeda S.et al. A mutation in the ceruloplasmin gene is associated with systemic hemosiderosis in humans. Nat. Genet. 9:1995;267-272.
    • (1995) Nat. Genet. , vol.9 , pp. 267-272
    • Yoshida, K.1    Furihata, K.2    Takeda, S.3
  • 4
    • 0029618814 scopus 로고
    • A nonsense mutation of the ceruloplasmin gene in hereditary ceruloplasmin deficiency with diabetes mellitus
    • Daimon M., Kato T., Kawanami T., Tominaga M.et al. A nonsense mutation of the ceruloplasmin gene in hereditary ceruloplasmin deficiency with diabetes mellitus. Biochem. Biophys. Res. Commun. 217:1995;89-95.
    • (1995) Biochem. Biophys. Res. Commun. , vol.217 , pp. 89-95
    • Daimon, M.1    Kato, T.2    Kawanami, T.3    Tominaga, M.4
  • 5
    • 0030014701 scopus 로고    scopus 로고
    • Familial dementia due to a frameshift mutation in the ceruloplasmin gene
    • Harris Z.L., Migas M.D., Hughes A.E.et al. Familial dementia due to a frameshift mutation in the ceruloplasmin gene. Q. J. Med. 89:1996;355-359.
    • (1996) Q. J. Med. , vol.89 , pp. 355-359
    • Harris, Z.L.1    Migas, M.D.2    Hughes, A.E.3
  • 6
    • 0029872996 scopus 로고    scopus 로고
    • Hereditary ceruloplasmin deficiency with hemosiderosis
    • Okamoto N., Wada S., Oga T., Kawabata Y.et al. Hereditary ceruloplasmin deficiency with hemosiderosis. Hum. Genet. 97:1996;755-778.
    • (1996) Hum. Genet. , vol.97 , pp. 755-778
    • Okamoto, N.1    Wada, S.2    Oga, T.3    Kawabata, Y.4
  • 7
    • 0037059741 scopus 로고    scopus 로고
    • Biochemical analysis of a missense mutation in aceruloplasminemia
    • Hellman N.E., Kono S., Miyajima H., Gitlin J.D. Biochemical analysis of a missense mutation in aceruloplasminemia. J. Biol. Chem. 277:2002;1375-1380.
    • (2002) J. Biol. Chem. , vol.277 , pp. 1375-1380
    • Hellman, N.E.1    Kono, S.2    Miyajima, H.3    Gitlin, J.D.4
  • 8
    • 0014027719 scopus 로고
    • The possible significance of the ferrous oxidase activity of ceruloplasmin in normal human serum
    • Osaki S., Johnson D., Frieden E. The possible significance of the ferrous oxidase activity of ceruloplasmin in normal human serum. J. Biol. Chem. 241:1966;2746-2757.
    • (1966) J. Biol. Chem. , vol.241 , pp. 2746-2757
    • Osaki, S.1    Johnson, D.2    Frieden, E.3
  • 11
    • 0015217690 scopus 로고
    • The mobilization of iron from the perfused mammalian liver by a serum copper enzyme, ferroxidase
    • Osaki S., Johnson D.A., Frieden E. The mobilization of iron from the perfused mammalian liver by a serum copper enzyme, ferroxidase. J. Biol. Chem. 246:1971;3018-3023.
    • (1971) J. Biol. Chem. , vol.246 , pp. 3018-3023
    • Osaki, S.1    Johnson, D.A.2    Frieden, E.3
  • 12
    • 0028058038 scopus 로고
    • The FET3 gene of S. cerevisiae encodes a multicopper oxidase required for ferrous iron uptake
    • Askwith C., Eide D., VanHo A., Bernard P.S.et al. The FET3 gene of S. cerevisiae encodes a multicopper oxidase required for ferrous iron uptake. Cell. 76:1994;403-410.
    • (1994) Cell , vol.76 , pp. 403-410
    • Askwith, C.1    Eide, D.2    VanHo, A.3    Bernard, P.S.4
  • 13
    • 0029921680 scopus 로고    scopus 로고
    • A permease-oxidase complex involved in high-affinity iron uptake in yeast
    • Stearman R., Yuan D., Yamaguchi-Iwa Y.et al. A permease-oxidase complex involved in high-affinity iron uptake in yeast. Science. 271:1996;1552-1557.
    • (1996) Science , vol.271 , pp. 1552-1557
    • Stearman, R.1    Yuan, D.2    Yamaguchi-Iwa, Y.3
  • 14
    • 0029800745 scopus 로고    scopus 로고
    • Expression of the ceruloplasmin gene in the human retina and brain: Implications for the pathogenic model in aceruloplasminemia
    • Klomp L.W.J., Gitlin J.D. Expression of the ceruloplasmin gene in the human retina and brain: implications for the pathogenic model in aceruloplasminemia. Hum. Mol. Genet. 5:1996;1989-1996.
    • (1996) Hum. Mol. Genet. , vol.5 , pp. 1989-1996
    • Klomp, L.W.J.1    Gitlin, J.D.2
  • 15
    • 0030856558 scopus 로고    scopus 로고
    • A novel glycophosphatidylinositol-anchored form of ceruloplasmin is expressed by mammalian astrocytes
    • Patel B.N., David S. A novel glycophosphatidylinositol-anchored form of ceruloplasmin is expressed by mammalian astrocytes. J. Biol. Chem. 272:1997;20185-20190.
    • (1997) J. Biol. Chem. , vol.272 , pp. 20185-20190
    • Patel, B.N.1    David, S.2
  • 16
    • 0032532332 scopus 로고    scopus 로고
    • Ran-2, a glial lineage marker, is a GPI-anchored form of ceruloplasmin
    • Salzer J.L., Lovejoy L., Linder M.C., Rosen C. Ran-2, a glial lineage marker, is a GPI-anchored form of ceruloplasmin. J. Neurosci. Res. 54:1998;147-157.
    • (1998) J. Neurosci. Res. , vol.54 , pp. 147-157
    • Salzer, J.L.1    Lovejoy, L.2    Linder, M.C.3    Rosen, C.4
  • 17
    • 0032881432 scopus 로고    scopus 로고
    • Glycosyl phosphatidylinositol-anchored ceruloplasmin is expressed in Sertoli cells and is concentrated in detergent-insoluble membrane fractions
    • Fortna R.R., Watson H.A., Nyquist S.E. Glycosyl phosphatidylinositol-anchored ceruloplasmin is expressed in Sertoli cells and is concentrated in detergent-insoluble membrane fractions. Biol. Reprod. 61:1999;1042-1049.
    • (1999) Biol. Reprod. , vol.61 , pp. 1042-1049
    • Fortna, R.R.1    Watson, H.A.2    Nyquist, S.E.3
  • 18
    • 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., Gitlin J.D. Targeted gene disruption reveals an essential role for ceruloplasmin in cellular iron efflux. Proc. Natl. Acad. Sci. U. S. A. 96:1999;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
  • 19
    • 0035965212 scopus 로고    scopus 로고
    • Copper transport and metabolism are normal in aceruloplasminemic mice
    • Meyer L.A., Durley A.P., Prohaska J.R., Harris Z.L. Copper transport and metabolism are normal in aceruloplasminemic mice. J. Biol. Chem. 276:2001;36857-36861.
    • (2001) J. Biol. Chem. , vol.276 , pp. 36857-36861
    • Meyer, L.A.1    Durley, A.P.2    Prohaska, J.R.3    Harris, Z.L.4
  • 20
    • 0036703490 scopus 로고    scopus 로고
    • Ceruloplasmin regulates iron levels in the CNS and prevents free radical injury
    • Patel B.N., Dunn R.J., Jeong S.Y.et al. Ceruloplasmin regulates iron levels in the CNS and prevents free radical injury. J. Neurosci. 22:2002;6578-6586.
    • (2002) J. Neurosci. , vol.22 , pp. 6578-6586
    • Patel, B.N.1    Dunn, R.J.2    Jeong, S.Y.3
  • 21
    • 0030003830 scopus 로고    scopus 로고
    • Increased plasma lipid peroxidation in patients with aceruloplasminemia
    • Miyajima H., Takahashi Y., Serizawa M.et al. Increased plasma lipid peroxidation in patients with aceruloplasminemia. Free Radic. Biol. Med. 20:1996;757-760.
    • (1996) Free Radic. Biol. Med. , vol.20 , pp. 757-760
    • Miyajima, H.1    Takahashi, Y.2    Serizawa, M.3
  • 22
    • 0034656236 scopus 로고    scopus 로고
    • Increased lipid peroxidation in the brains of aceruloplasminemic patients
    • Yoshida K., Kaneko K., Miyajima H.et al. Increased lipid peroxidation in the brains of aceruloplasminemic patients. J. Neurol. Sci. 175:2000;91-95.
    • (2000) J. Neurol. Sci. , vol.175 , pp. 91-95
    • Yoshida, K.1    Kaneko, K.2    Miyajima, H.3
  • 23
    • 0034672736 scopus 로고    scopus 로고
    • Defective electron transfer in complexes I and IV in patients with aceruloplasminemia
    • Kohno S., Miyajima H., Takahashi Y.et al. Defective electron transfer in complexes I and IV in patients with aceruloplasminemia. J. Neurol. Sci. 182:2000;57-60.
    • (2000) J. Neurol. Sci. , vol.182 , pp. 57-60
    • Kohno, S.1    Miyajima, H.2    Takahashi, Y.3
  • 24
    • 0036522005 scopus 로고    scopus 로고
    • Glial fibrillary acidic protein is greatly modified by oxidative stress in aceruloplasminemia brain
    • Kaneko K., Nakamura A., Yoshida K.et al. Glial fibrillary acidic protein is greatly modified by oxidative stress in aceruloplasminemia brain. Free Radic. Res. 36:2002;303-306.
    • (2002) Free Radic. Res. , vol.36 , pp. 303-306
    • Kaneko, K.1    Nakamura, A.2    Yoshida, K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.