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Volumn 1651, Issue 1-2, 2003, Pages 116-123

Stromal cell-derived receptor 2 and cytochrome b561 are functional ferric reductases

Author keywords

Cytochrome b561; Ferric reductase; hpx; sdr2

Indexed keywords

CYTOCHROME; CYTOCHROME B; CYTOCHROME B561; IRON REGULATORY FACTOR; OXIDOREDUCTASE; RECEPTOR; STROMAL CELL DERIVED RECEPTOR 2; UNCLASSIFIED DRUG; CELL SURFACE RECEPTOR; CYBRD1 PROTEIN, HUMAN; CYBRD1 PROTEIN, MOUSE; FERRIC CITRATE IRON REDUCTASE; FLAVINE MONONUCLEOTIDE REDUCTASE; IRON; STROMAL CELL DERIVED RECEPTOR 2, MOUSE; STROMAL CELL-DERIVED RECEPTOR 2, MOUSE;

EID: 0642341947     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1570-9639(03)00242-5     Document Type: Article
Times cited : (78)

References (43)
  • 2
    • 0027314995 scopus 로고
    • Impact of iron deficiency on cognition in infancy and childhood
    • Walter T. Impact of iron deficiency on cognition in infancy and childhood. Eur. J. Clin. Nutr. 47:1993;307-316.
    • (1993) Eur. J. Clin. Nutr. , vol.47 , pp. 307-316
    • Walter, T.1
  • 3
    • 0027218690 scopus 로고
    • Iron deficiency and cognitive function
    • Pollitt E. Iron deficiency and cognitive function. Annu. Rev. Nutr. 13:1993;521-537.
    • (1993) Annu. Rev. Nutr. , vol.13 , pp. 521-537
    • Pollitt, E.1
  • 4
    • 0022586095 scopus 로고
    • Behavioral aspects of iron deficiency
    • Lozoff B., Brittenham G.M. Behavioral aspects of iron deficiency. Prog. Hematol. 14:1986;23-53.
    • (1986) Prog. Hematol. , vol.14 , pp. 23-53
    • Lozoff, B.1    Brittenham, G.M.2
  • 6
    • 0024540920 scopus 로고
    • The reflection of histology in MR imaging of Pelizaeus-Merzbacher disease
    • van der Knaap M.S., Valk J. The reflection of histology in MR imaging of Pelizaeus-Merzbacher disease. AJNR, Am. J. Neuroradiol. 10:1989;99-103.
    • (1989) AJNR, Am. J. Neuroradiol. , vol.10 , pp. 99-103
    • Van Der Knaap, M.S.1    Valk, J.2
  • 7
    • 0031947244 scopus 로고    scopus 로고
    • Iron metabolism and Parkinson's disease
    • Hirsch E.C., Faucheux B.A. Iron metabolism and Parkinson's disease. Mov. Disord. 13:1998;39-45.
    • (1998) Mov. Disord. , vol.13 , pp. 39-45
    • Hirsch, E.C.1    Faucheux, B.A.2
  • 8
    • 0028000825 scopus 로고
    • Altered brain metabolism of iron as a cause of neurodegenerative diseases?
    • Gerlach M., Ben-Shachar D., Riederer P., Youdim M.B. Altered brain metabolism of iron as a cause of neurodegenerative diseases? J. Neurochem. 63:1994;793-807.
    • (1994) J. Neurochem. , vol.63 , pp. 793-807
    • Gerlach, M.1    Ben-Shachar, D.2    Riederer, P.3    Youdim, M.B.4
  • 9
    • 0027497409 scopus 로고
    • The possible role of iron in the etiopathology of Parkinson's disease
    • Youdim M.B., Ben-Shachar D., Riederer P. The possible role of iron in the etiopathology of Parkinson's disease. Mov. Disord. 8:1993;1-12.
    • (1993) Mov. Disord. , vol.8 , pp. 1-12
    • Youdim, M.B.1    Ben-Shachar, D.2    Riederer, P.3
  • 11
    • 0025314685 scopus 로고
    • Role of oxygen free radicals in carcinogenesis and brain ischemia
    • Floyd R.A. Role of oxygen free radicals in carcinogenesis and brain ischemia. FASEB J. 4:1990;2587-2597.
    • (1990) FASEB J. , vol.4 , pp. 2587-2597
    • Floyd, R.A.1
  • 12
    • 0026754574 scopus 로고
    • Reactive oxygen species and the central nervous system
    • Halliwell B. Reactive oxygen species and the central nervous system. J. Neurochem. 59:1992;1609-1623.
    • (1992) J. Neurochem. , vol.59 , pp. 1609-1623
    • Halliwell, B.1
  • 13
    • 0030598917 scopus 로고    scopus 로고
    • Dopamine, 6-hydroxydopamine, iron, and dioxygen-their mutual interactions and possible implication in the development of Parkinson's disease
    • Linert W., Herlinger E., Jameson R.F., Kienzl E., Jellinger K., Youdim M.B. Dopamine, 6-hydroxydopamine, iron, and dioxygen-their mutual interactions and possible implication in the development of Parkinson's disease. Biochim. Biophys. Acta. 1316:1996;160-168.
    • (1996) Biochim. Biophys. Acta , vol.1316 , pp. 160-168
    • Linert, W.1    Herlinger, E.2    Jameson, R.F.3    Kienzl, E.4    Jellinger, K.5    Youdim, M.B.6
  • 14
    • 0031283221 scopus 로고    scopus 로고
    • Indices of oxidative stress in Parkinson's disease, Alzheimer's disease and dementia with Lewy bodies
    • Owen A.D., Schapira A.H., Jenner P., Marsden C.D. Indices of oxidative stress in Parkinson's disease, Alzheimer's disease and dementia with Lewy bodies. J. Neural Transm., Suppl. 51:1997;167-173.
    • (1997) J. Neural Transm., Suppl. , vol.51 , pp. 167-173
    • Owen, A.D.1    Schapira, A.H.2    Jenner, P.3    Marsden, C.D.4
  • 17
    • 0033961913 scopus 로고    scopus 로고
    • Transferrin and transferrin receptor function in brain barrier systems
    • Moos T., Morgan E.H. Transferrin and transferrin receptor function in brain barrier systems. Cell. Mol. Neurobiol. 20:2000;77-95.
    • (2000) Cell. Mol. Neurobiol. , vol.20 , pp. 77-95
    • Moos, T.1    Morgan, E.H.2
  • 21
    • 0015214389 scopus 로고
    • Cytochrome b561 of the bovine adrenal chromaffin granules. A high potential b-type cytochrome
    • Flatmark T., Terland O. Cytochrome b561 of the bovine adrenal chromaffin granules. A high potential b-type cytochrome. Biochim. Biophys. Acta. 253:1971;487-491.
    • (1971) Biochim. Biophys. Acta , vol.253 , pp. 487-491
    • Flatmark, T.1    Terland, O.2
  • 22
    • 0035880488 scopus 로고    scopus 로고
    • Domain homologues of dopamine beta-hydroxylase and ferric reductase: Roles for iron metabolism in neurodegenerative disorders?
    • Ponting C.P. Domain homologues of dopamine beta-hydroxylase and ferric reductase: roles for iron metabolism in neurodegenerative disorders? Hum. Mol. Genet. 10:2001;1853-1858.
    • (2001) Hum. Mol. Genet. , vol.10 , pp. 1853-1858
    • Ponting, C.P.1
  • 25
    • 0023522698 scopus 로고
    • Hereditary hypotransferrinemia with hemosiderosis, a murine disorder resembling human atransferrinemia
    • Bernstein S.E. Hereditary hypotransferrinemia with hemosiderosis, a murine disorder resembling human atransferrinemia. J. Lab. Clin. Med. 110:1987;690-705.
    • (1987) J. Lab. Clin. Med. , vol.110 , pp. 690-705
    • Bernstein, S.E.1
  • 27
    • 0035823348 scopus 로고    scopus 로고
    • Abnormal iron accumulation in the brain of neonatal hypotransferrinemic mice
    • Takeda A., Takatsuka K., Connor J.R., Oku N. Abnormal iron accumulation in the brain of neonatal hypotransferrinemic mice. Brain Res. 912:2001;154-161.
    • (2001) Brain Res. , vol.912 , pp. 154-161
    • Takeda, A.1    Takatsuka, K.2    Connor, J.R.3    Oku, N.4
  • 28
    • 0029065064 scopus 로고
    • Cellular distribution of iron, transferrin, and ferritin in the hypotransferrinemic (Hp) mouse brain
    • Dickinson T.K., Connor J.R. Cellular distribution of iron, transferrin, and ferritin in the hypotransferrinemic (Hp) mouse brain. J. Comp. Neurol. 355:1995;67-80.
    • (1995) J. Comp. Neurol. , vol.355 , pp. 67-80
    • Dickinson, T.K.1    Connor, J.R.2
  • 29
    • 0032746341 scopus 로고    scopus 로고
    • Transferrin is required for normal distribution of 59 Fe and 54 Mn in mouse brain
    • Malecki E.A., Cook B.M., Devenyi A.G., Beard J.L., Connor J.R. Transferrin is required for normal distribution of 59 Fe and 54 Mn in mouse brain. J. Neurol. Sci. 170:1999;112-118.
    • (1999) J. Neurol. Sci. , vol.170 , pp. 112-118
    • Malecki, E.A.1    Cook, B.M.2    Devenyi, A.G.3    Beard, J.L.4    Connor, J.R.5
  • 30
    • 0034669060 scopus 로고    scopus 로고
    • Anthelmintic actions on homomer-forming nicotinic acetylcholine receptor subunits: Chicken alpha7 and ACR-16 from the nematode Caenorhabditis elegans
    • Raymond V., Mongan N.P., Sattelle D.B. Anthelmintic actions on homomer-forming nicotinic acetylcholine receptor subunits: chicken alpha7 and ACR-16 from the nematode Caenorhabditis elegans. Neuroscience. 101:2000;785-791.
    • (2000) Neuroscience , vol.101 , pp. 785-791
    • Raymond, V.1    Mongan, N.P.2    Sattelle, D.B.3
  • 32
    • 0023159107 scopus 로고
    • Properties of single sodium channels translated by Xenopus oocytes after injection with messenger ribonucleic acid
    • Sigel E. Properties of single sodium channels translated by Xenopus oocytes after injection with messenger ribonucleic acid. J. Physiol. 386:1987;73-90.
    • (1987) J. Physiol. , vol.386 , pp. 73-90
    • Sigel, E.1
  • 33
    • 0025078661 scopus 로고
    • Use of Xenopus oocytes for the functional expression of plasma membrane proteins
    • Sigel E. Use of Xenopus oocytes for the functional expression of plasma membrane proteins. J. Membr. Biol. 117:1990;201-221.
    • (1990) J. Membr. Biol. , vol.117 , pp. 201-221
    • Sigel, E.1
  • 34
    • 0034008744 scopus 로고    scopus 로고
    • The use of Xenopus laevis oocytes for the functional characterization of heterologously expressed membrane proteins
    • Wagner C.A., Friedrich B., Setiawan I., Lang F., Broer S. The use of Xenopus laevis oocytes for the functional characterization of heterologously expressed membrane proteins. Cell Physiol. Biochem. 10:2000;1-12.
    • (2000) Cell Physiol. Biochem. , vol.10 , pp. 1-12
    • Wagner, C.A.1    Friedrich, B.2    Setiawan, I.3    Lang, F.4    Broer, S.5
  • 35
    • 0022971533 scopus 로고
    • Functional coupling between enzymes of the chromaffin granule membrane
    • Wakefield L.M., Cass A.E., Radda G.K. Functional coupling between enzymes of the chromaffin granule membrane. J. Biol. Chem. 261:1986;9739-9745.
    • (1986) J. Biol. Chem. , vol.261 , pp. 9739-9745
    • Wakefield, L.M.1    Cass, A.E.2    Radda, G.K.3
  • 36
    • 0022972685 scopus 로고
    • Role of ascorbic acid in dopamine beta-hydroxylation. The endogenous enzyme cofactor and putative electron donor for cofactor regeneration
    • Menniti F.S., Knoth J., Diliberto E.J. Jr. Role of ascorbic acid in dopamine beta-hydroxylation. The endogenous enzyme cofactor and putative electron donor for cofactor regeneration. J. Biol. Chem. 261:1986;16901-16908.
    • (1986) J. Biol. Chem. , vol.261 , pp. 16901-16908
    • Menniti, F.S.1    Knoth, J.2    Diliberto, E.J.Jr.3
  • 38
    • 0022032020 scopus 로고
    • Regional specificity of iron uptake by small intestinal brush-border membranes from normal and iron-deficient mice
    • Muir A., Hopfer U. Regional specificity of iron uptake by small intestinal brush-border membranes from normal and iron-deficient mice. Am. J. Physiol. 248:1985;G376-G379.
    • (1985) Am. J. Physiol. , vol.248
    • Muir, A.1    Hopfer, U.2
  • 39
    • 0021474453 scopus 로고
    • Role of the liver in normal iron metabolism
    • Bacon B.R., Tavill A.S. Role of the liver in normal iron metabolism. Semin. Liver Dis. 4:1984;181-192.
    • (1984) Semin. Liver Dis. , vol.4 , pp. 181-192
    • Bacon, B.R.1    Tavill, A.S.2
  • 40
    • 0034655418 scopus 로고    scopus 로고
    • In vivo characterization of renal iron transport in the anaesthetized rat
    • Wareing M., Ferguson C.J., Green R., Riccardi D., Smith C.P. In vivo characterization of renal iron transport in the anaesthetized rat. J. Physiol. 524(Pt 2):2000;581-586.
    • (2000) J. Physiol. , vol.524 , Issue.PT 2 , pp. 581-586
    • Wareing, M.1    Ferguson, C.J.2    Green, R.3    Riccardi, D.4    Smith, C.P.5
  • 42
    • 0023665279 scopus 로고
    • NADH diferric transferrin reductase in liver plasma membrane
    • Sun I.L., Navas P., Crane F.L., Morre D.J., Low H. NADH diferric transferrin reductase in liver plasma membrane. J. Biol. Chem. 262:1987;15915-15921.
    • (1987) J. Biol. Chem. , vol.262 , pp. 15915-15921
    • Sun, I.L.1    Navas, P.2    Crane, F.L.3    Morre, D.J.4    Low, H.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.