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Volumn 1820, Issue 3, 2012, Pages 393-402

Functional roles of transferrin in the brain

Author keywords

Blood brain barrier; Choroid plexus; Iron; Neuron; Oligodendrocyte; Transferrin

Indexed keywords

TRANSFERRIN;

EID: 84857373169     PISSN: 03044165     EISSN: 18728006     Source Type: Journal    
DOI: 10.1016/j.bbagen.2011.10.016     Document Type: Review
Times cited : (123)

References (172)
  • 1
    • 0017885589 scopus 로고
    • Stoichiometric and site characteristics of the binding of iron to human transferrin
    • P. Aisen, A. Leibman, and J. Zweier Stoichiometric and site characteristics of the binding of iron to human transferrin J. Biol. Chem. 253 1978 1930 1937 (Pubitemid 8299518)
    • (1978) Journal of Biological Chemistry , vol.253 , Issue.6 , pp. 1930-1937
    • Aisen, P.1    Leibman, A.2    Zweier, J.3
  • 4
    • 57349091759 scopus 로고    scopus 로고
    • Why iron deficiency is important in infant development
    • J.L. Beard Why iron deficiency is important in infant development J. Nutr. 138 2008 2534 2536
    • (2008) J. Nutr. , vol.138 , pp. 2534-2536
    • Beard, J.L.1
  • 5
    • 77951137998 scopus 로고    scopus 로고
    • Iron in neuronal function and dysfunction
    • G.A. Salvador Iron in neuronal function and dysfunction Biofactors 36 2010 103 110
    • (2010) Biofactors , vol.36 , pp. 103-110
    • Salvador, G.A.1
  • 6
    • 0041792815 scopus 로고
    • Transferrin gene expression visualized in oligodendrocytes of the rat brain by using in situ hybridization and immunohistochemistry
    • DOI 10.1073/pnas.82.19.6706
    • B. Bloch, T. Popovici, M.J. Levin, D. Tuil, and A. Kahn Transferrin gene expression visualized in oligodendrocytes of the rat brain by using in situ hybridization and immunohistochemistry Proc. Natl. Acad. Sci. U. S. A. 82 1985 6706 6710 (Pubitemid 16228889)
    • (1985) Proceedings of the National Academy of Sciences of the United States of America , vol.82 , Issue.19 , pp. 6706-6710
    • Bloch, B.1    Popovici, T.2    Levin, M.J.3
  • 7
    • 0022508973 scopus 로고
    • The distribution of transferrin immunoreactivity in the rat central nervous system
    • DOI 10.1016/0006-8993(86)90576-7
    • J.R. Connor, and R.E. Fine The distribution of transferrin immunoreactivity in the rat central nervous system Brain Res. 368 1986 319 328 (Pubitemid 16046183)
    • (1986) Brain Research , vol.368 , Issue.2 , pp. 319-328
    • Connor, J.R.1    Fine, R.E.2
  • 8
    • 12244310166 scopus 로고    scopus 로고
    • Brain iron uptake in hypotransferrinemic mice: Influence of systemic iron status
    • DOI 10.1002/jnr.20324, Brain Energy Metabolism: Transporters, Mitochondria and Neurodegeneration
    • J.L. Beard, J.A. Wiesinger, N. Li, and J.R. Connor Brain iron uptake in hypotransferrinemic mice: influence of systemic iron status J. Neurosci. Res. 79 2005 254 261 (Pubitemid 40116443)
    • (2005) Journal of Neuroscience Research , vol.79 , Issue.1-2 , pp. 254-261
    • Beard, J.L.1    Wiesinger, J.A.2    Li, N.3    Connor, J.R.4
  • 9
    • 0019453395 scopus 로고
    • Sciatin: Immunocytochemical localization of a myotrophic protein in chicken neural tissues
    • T.H. Oh, C.A. Sofia, Y.C. Kim, C. Carroll, H.H. Kim, G.J. Markelonis, and P.J. Reier Sciatin: immunocytochemical localization of a myotrophic protein in chicken neural tissues J. Histochem. Cytochem. 29 1981 1205 1212 (Pubitemid 11061055)
    • (1981) Journal of Histochemistry and Cytochemistry , vol.29 , Issue.10 , pp. 1205-1212
    • Oh, T.H.1    Sofia, C.A.2    Kim, Y.C.3
  • 10
    • 0020313092 scopus 로고
    • Sciatin is a transferrin-like polypeptide
    • DOI 10.1111/j.1471-4159.1982.tb03949.x
    • G.J. Markelonis, R.A. Bradshaw, T.H. Oh, J.L. Johnson, and O.J. Bates Sciatin is a transferrin-like polypeptide J. Neurochem. 39 1982 315 320 (Pubitemid 12013607)
    • (1982) Journal of Neurochemistry , vol.39 , Issue.2 , pp. 315-320
    • Markelonis, G.J.1    Bradshaw, R.A.2    Oh, T.H.3
  • 11
    • 0026635457 scopus 로고
    • Iron regulation in the brain: Histochemical, biochemical, and molecular considerations
    • Suppl.
    • J.R. Connor, and S.A. Benkovic Iron regulation in the brain: histochemical, biochemical, and molecular considerations Ann. Neurol. 32 1992 S51 S61 Suppl.
    • (1992) Ann. Neurol. , vol.32
    • Connor, J.R.1    Benkovic, S.A.2
  • 12
    • 0026590705 scopus 로고
    • Regional distribution of iron and iron-regulatory proteins in the brain in aging and Alzheimer's disease
    • J.R. Connor, B.S. Snyder, J.L. Beard, R.E. Fine, and E.J. Mufson Regional distribution of iron and iron-regulatory proteins in the brain in aging and Alzheimer's disease J. Neurosci. Res. 31 1992 327 335
    • (1992) J. Neurosci. Res. , vol.31 , pp. 327-335
    • Connor, J.R.1    Snyder, B.S.2    Beard, J.L.3    Fine, R.E.4    Mufson, E.J.5
  • 13
    • 0033597780 scopus 로고    scopus 로고
    • Molecular cloning of transferrin receptor 2. A new member of the transferrin receptor-like family
    • H. Kawabata, R. Yang, T. Hirama, P.T. Vuong, S. Kawano, A.F. Gombart, and H.P. Koeffler Molecular cloning of transferrin receptor 2. A new member of the transferrin receptor-like family J. Biol. Chem. 274 1999 20826 20832
    • (1999) J. Biol. Chem. , vol.274 , pp. 20826-20832
    • Kawabata, H.1    Yang, R.2    Hirama, T.3    Vuong, P.T.4    Kawano, S.5    Gombart, A.F.6    Koeffler, H.P.7
  • 15
    • 0020511115 scopus 로고
    • Transferrin recycling in reticulocytes: pH and iron are important determinants of ligand binding and processing
    • C. Harding, and P. Stahl Transferrin recycling in reticulocytes: pH and iron are important determinants of ligand binding and processing Biochem. Biophys. Res. Commun. 113 1983 650 658 (Pubitemid 13058481)
    • (1983) Biochemical and Biophysical Research Communications , vol.113 , Issue.2 , pp. 650-658
    • Harding, C.1    Stahl, P.2
  • 16
    • 0026055852 scopus 로고
    • Recycling kinetics and transcytosis of transferrin in primary cultures of bovine brain microvessel endothelial cells
    • T.J. Raub, and C.R. Newton Recycling kinetics and transcytosis of transferrin in primary cultures of bovine brain microvessel endothelial cells J. Cell. Physiol. 149 1991 141 151 (Pubitemid 21910175)
    • (1991) Journal of Cellular Physiology , vol.149 , Issue.1 , pp. 141-151
    • Raub, T.J.1    Newton, C.R.2
  • 17
    • 0021675792 scopus 로고
    • Acidification of endocytic compartments and the intracellular pathways of ligands and receptors
    • DOI 10.1002/jcb.240260404
    • D.J. Yamashiro, and F.R. Maxfield Acidification of endocytic compartments and the intracellular pathways of ligands and receptors J. Cell. Biochem. 26 1984 231 246 (Pubitemid 15168551)
    • (1984) Journal of Cellular Biochemistry , vol.26 , Issue.4 , pp. 231-246
    • Yamashiro, D.J.1    Maxfield, F.R.2
  • 18
    • 0025744263 scopus 로고
    • Binding to cellular receptors results in increased iron release from transferrin at mildly acidic pH
    • D.M. Sipe, and R.F. Murphy Binding to cellular receptors results in increased iron release from transferrin at mildly acidic pH J. Biol. Chem. 266 1991 8002 8007 (Pubitemid 21906466)
    • (1991) Journal of Biological Chemistry , vol.266 , Issue.13 , pp. 8002-8007
    • Sipe, D.M.1    Murphy, R.F.2
  • 19
    • 0025924788 scopus 로고
    • A new role for the transferrin receptor in the release of iron from transferrin
    • P.K. Bali, O. Zak, and P. Aisen A new role for the transferrin receptor in the release of iron from transferrin Biochemistry 30 1991 324 328
    • (1991) Biochemistry , vol.30 , pp. 324-328
    • Bali, P.K.1    Zak, O.2    Aisen, P.3
  • 21
    • 0021130764 scopus 로고
    • Transferrin receptor on endothelium of brain capillaries
    • DOI 10.1038/312162a0
    • W.A. Jefferies, M.R. Brandon, S.V. Hunt, A.F. Williams, K.C. Gatter, and D.Y. Mason Transferrin receptor on endothelium of brain capillaries Nature 312 1984 162 163 (Pubitemid 14000081)
    • (1984) Nature , vol.312 , Issue.5990 , pp. 162-163
    • Jefferies, W.A.1    Brandon, M.R.2    Hunt, S.V.3
  • 23
    • 0025354340 scopus 로고
    • Developmental changes in transferrin and iron uptake by the brain in the rat
    • DOI 10.1016/0165-3806(90)90103-6
    • E.M. Taylor, and E.H. Morgan Developmental changes in transferrin and iron uptake by the brain in the rat Brain Res. Dev. Brain Res. 55 1990 35 42 (Pubitemid 20241301)
    • (1990) Developmental Brain Research , vol.55 , Issue.1 , pp. 35-42
    • Taylor, E.M.1    Morgan, E.H.2
  • 24
    • 0026794561 scopus 로고
    • Iron uptake in relation to transferrin degradation in brain and other tissues of rats
    • M.E. Strahan, A. Crowe, and E.H. Morgan Iron uptake in relation to transferrin degradation in brain and other tissues of rats Am. J. Physiol. 263 1992 R924 R929
    • (1992) Am. J. Physiol. , vol.263
    • Strahan, M.E.1    Crowe, A.2    Morgan, E.H.3
  • 25
    • 0022466364 scopus 로고
    • Three-dimensional reconstruction of vesicles in endothelium of blood-brain barrier versus highly permeable microvessels
    • B.L. Coomber, and P.A. Stewart Three-dimensional reconstruction of vesicles in endothelium of blood-brain barrier versus highly permeable microvessels Anat. Rec. 215 1986 256 261 (Pubitemid 16058751)
    • (1986) Anatomical Record , vol.215 , Issue.3 , pp. 256-261
    • Coomber, B.L.1    Stewart, P.A.2
  • 26
    • 0031039178 scopus 로고    scopus 로고
    • Ultrastructural and morphometric investigation of human brain capillaries in normal and peritumoral tissues
    • M. Bertossi, D. Virgintino, E. Maiorano, M. Occhiogrosso, and L. Roncali Ultrastructural and morphometric investigation of human brain capillaries in normal and peritumoral tissues Ultrastruct. Pathol. 21 1997 41 49 (Pubitemid 27099728)
    • (1997) Ultrastructural Pathology , vol.21 , Issue.1 , pp. 41-49
    • Bertossi, M.1    Maiorano, E.2    Occhiogrosso, M.3    Roncali, L.4
  • 27
    • 0142185331 scopus 로고    scopus 로고
    • Mechanisms and regulation of transferrin and iron transport in a model blood-brain barrier system
    • DOI 10.1016/S0306-4522(03)00590-6
    • J.R. Burdo, D.A. Antonetti, E.B. Wolpert, and J.R. Connor Mechanisms and regulation of transferrin and iron transport in a model blood-brain barrier system Neuroscience 121 2003 883 890 (Pubitemid 37324587)
    • (2003) Neuroscience , vol.121 , Issue.4 , pp. 883-890
    • Burdo, J.R.1    Antonetti, D.A.2    Wolpert, E.B.3    Connor, J.R.4
  • 29
    • 1442323987 scopus 로고    scopus 로고
    • Iron accumulation, iron-mediated toxicity and altered levels of ferritin and transferrin receptor in cultured astrocytes during incubation with ferric ammonium citrate
    • DOI 10.1046/j.1471-4159.2003.02236.x
    • H.H. Hoepken, T. Korten, S.R. Robinson, and R. Dringen Iron accumulation, iron-mediated toxicity and altered levels of ferritin and transferrin receptor in cultured astrocytes during incubation with ferric ammonium citrate J. Neurochem. 88 2004 1194 1202 (Pubitemid 38280687)
    • (2004) Journal of Neurochemistry , vol.88 , Issue.5 , pp. 1194-1202
    • Hoepken, H.H.1    Korten, T.2    Robinsont, S.R.3    Dringen, R.4
  • 30
    • 0033548410 scopus 로고    scopus 로고
    • Increased expression of transferrin receptors and iron in amoeboid microglial cells in postnatal rats following an exposure to hypoxia
    • DOI 10.1016/S0304-3940(99)00075-0, PII S0304394099000750
    • C. Kaur, and E.A. Ling Increased expression of transferrin receptors and iron in amoeboid microglial cells in postnatal rats following an exposure to hypoxia Neurosci. Lett. 262 1999 183 186 (Pubitemid 29136800)
    • (1999) Neuroscience Letters , vol.262 , Issue.3 , pp. 183-186
    • Kaur, C.1    Ling, E.A.2
  • 31
    • 0032504563 scopus 로고    scopus 로고
    • Immunohistochemical analysis of transferrin receptor: Regional and cellular distribution in the hypotransferrinemic (hpx) mouse brain
    • DOI 10.1016/S0006-8993(98)00575-7, PII S0006899398005757
    • T.K. Dickinson, and J.R. Connor Immunohistochemical analysis of transferrin receptor: regional and cellular distribution in the hypotransferrinemic (hpx) mouse brain Brain Res. 801 1998 171 181 (Pubitemid 28401661)
    • (1998) Brain Research , vol.801 , Issue.1-2 , pp. 171-181
    • Dickinson, T.K.1    Connor, J.R.2
  • 32
    • 0029976834 scopus 로고    scopus 로고
    • Immunohistochemical localization of intraneuronal transferrin receptor immunoreactivity in the adult mouse central nervous system
    • DOI 10.1002/(SICI)1096-9861(19961125)375:4<675::AID-CNE8>3.0.CO;2-Z
    • T. Moos Immunohistochemical localization of intraneuronal transferrin receptor immunoreactivity in the adult mouse central nervous system J. Comp. Neurol. 375 1996 675 692 (Pubitemid 26398347)
    • (1996) Journal of Comparative Neurology , vol.375 , Issue.4 , pp. 675-692
    • Moos, T.1
  • 33
    • 0023252003 scopus 로고
    • MHC antigen expression on bulk isolated macrophage-microglia from newborn mouse brain: Induction of Ia antigen expression by γ-interferon
    • DOI 10.1016/0165-5728(87)90121-4
    • A. Suzumura, S.G. Mezitis, N.K. Gonatas, and D.H. Silberberg MHC antigen expression on bulk isolated macrophage-microglia from newborn mouse brain: induction of Ia antigen expression by gamma-interferon J. Neuroimmunol. 15 1987 263 278 (Pubitemid 17108036)
    • (1987) Journal of Neuroimmunology , vol.15 , Issue.3 , pp. 263-278
    • Suzumura, A.1    Mezitis, S.G.E.2    Gonatas, N.K.3    Silberberg, D.H.4
  • 36
    • 0034595856 scopus 로고    scopus 로고
    • Transferrin receptor 2-α supports cell growth both in iron-chelated cultured cells and in vivo
    • DOI 10.1074/jbc.M908846199
    • H. Kawabata, R.S. Germain, P.T. Vuong, T. Nakamaki, J.W. Said, and H.P. Koeffler Transferrin receptor 2-alpha supports cell growth both in iron-chelated cultured cells and in vivo J. Biol. Chem. 275 2000 16618 16625 (Pubitemid 30398888)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.22 , pp. 16618-16625
    • Kawabata, H.1    Germain, R.S.2    Vuong, P.T.3    Nakamaki, T.4    Said, J.W.5    Koeffler, H.P.6
  • 37
    • 19944427107 scopus 로고    scopus 로고
    • Expression of hepcidin is down-regulated in TfR2 mutant mice manifesting a phenotype of hereditary hemochromatosis
    • DOI 10.1182/blood-2004-04-1416
    • H. Kawabata, R.E. Fleming, D. Gui, S.Y. Moon, T. Saitoh, J. O'Kelly, Y. Umehara, Y. Wano, J.W. Said, and H.P. Koeffler Expression of hepcidin is down-regulated in TfR2 mutant mice manifesting a phenotype of hereditary hemochromatosis Blood 105 2005 376 381 (Pubitemid 40053107)
    • (2005) Blood , vol.105 , Issue.1 , pp. 376-381
    • Kawabata, H.1    Fleming, R.E.2    Gui, D.3    Moon, S.Y.4    Saitoh, T.5    O'Kelly, J.6    Umehara, Y.7    Wano, Y.8    Said, J.W.9    Koeffler, H.P.10
  • 38
    • 0026458234 scopus 로고
    • Regulation of transferrin gene expression
    • M.M. Zakin Regulation of transferrin gene expression FASEB J. 6 1992 3253 3258
    • (1992) FASEB J. , vol.6 , pp. 3253-3258
    • Zakin, M.M.1
  • 39
    • 0033588021 scopus 로고    scopus 로고
    • Transferrin receptor induction by hypoxia. HIF-1-mediated transcriptional activation and cell-specific post-transcriptional regulation
    • L. Tacchini, L. Bianchi, A. Bernelli-Zazzera, and G. Cairo Transferrin receptor induction by hypoxia. HIF-1-mediated transcriptional activation and cell-specific post-transcriptional regulation J. Biol. Chem. 274 1999 24142 24146
    • (1999) J. Biol. Chem. , vol.274 , pp. 24142-24146
    • Tacchini, L.1    Bianchi, L.2    Bernelli-Zazzera, A.3    Cairo, G.4
  • 40
    • 0000655498 scopus 로고    scopus 로고
    • Identification of a hypoxia response element in the transferrin receptor gene
    • C.N. Lok, and P. Ponka Identification of a hypoxia response element in the transferrin receptor gene J. Biol. Chem. 274 1999 24147 24152
    • (1999) J. Biol. Chem. , vol.274 , pp. 24147-24152
    • Lok, C.N.1    Ponka, P.2
  • 41
    • 0033230181 scopus 로고    scopus 로고
    • HIF-1-mediated activation of transferrin receptor gene transcription by iron chelation
    • DOI 10.1093/nar/27.21.4223
    • L. Bianchi, L. Tacchini, and G. Cairo HIF-1-mediated activation of transferrin receptor gene transcription by iron chelation Nucleic Acids Res. 27 1999 4223 4227 (Pubitemid 29500256)
    • (1999) Nucleic Acids Research , vol.27 , Issue.21 , pp. 4223-4227
    • Bianchi, L.1    Tacchini, L.2    Cairo, G.3
  • 44
    • 0030792094 scopus 로고    scopus 로고
    • Oxygen-regulated transferrin expression is mediated by hypoxia-inducible factor-1
    • DOI 10.1074/jbc.272.32.20055
    • A. Rolfs, I. Kvietikova, M. Gassmann, and R.H. Wenger Oxygen-regulated transferrin expression is mediated by hypoxia-inducible factor-1 J. Biol. Chem. 272 1997 20055 20062 (Pubitemid 27340110)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.32 , pp. 20055-20062
    • Rolfs, A.1    Kvietikova, I.2    Gassmann, M.3    Wenger, R.H.4
  • 47
    • 0346881343 scopus 로고    scopus 로고
    • Thrombin Preconditioning Attenuates Brain Edema Induced by Erythrocytes and Iron
    • Y. Hua, R.F. Keep, J.T. Hoff, and G. Xi Thrombin preconditioning attenuates brain edema induced by erythrocytes and iron J. Cereb. Blood Flow Metab. 23 2003 1448 1454 (Pubitemid 38018263)
    • (2003) Journal of Cerebral Blood Flow and Metabolism , vol.23 , Issue.12 , pp. 1448-1454
    • Hua, Y.1    Keep, R.F.2    Hoff, J.T.3    Xi, G.4
  • 48
    • 0343060358 scopus 로고    scopus 로고
    • Roles of nitric oxide in brain hypoxia-ischemia
    • DOI 10.1016/S0005-2728(99)00030-4, PII S0005272899000304
    • J.P. Bolaños, and A. Almeida Roles of nitric oxide in brain hypoxia-ischemia Biochim. Biophys. Acta 1411 1999 415 436 (Pubitemid 29221965)
    • (1999) Biochimica et Biophysica Acta - Bioenergetics , vol.1411 , Issue.2-3 , pp. 415-436
    • Bolanos, J.P.1    Almeida, A.2
  • 49
    • 51049103235 scopus 로고    scopus 로고
    • Role of HIF-1 and NF-kappaB transcription factors in the modulation of transferrin receptor by inflammatory and anti-inflammatory signals
    • L. Tacchini, E. Gammella, C. De Ponti, S. Recalcati, and G. Cairo Role of HIF-1 and NF-kappaB transcription factors in the modulation of transferrin receptor by inflammatory and anti-inflammatory signals J. Biol. Chem. 283 2008 20674 20686
    • (2008) J. Biol. Chem. , vol.283 , pp. 20674-20686
    • Tacchini, L.1    Gammella, E.2    De Ponti, C.3    Recalcati, S.4    Cairo, G.5
  • 50
    • 0029850677 scopus 로고    scopus 로고
    • Rab11 regulates recycling through the pericentriolar recycling endosome
    • O. Ullrich, S. Reinsch, S. Urbé, M. Zerial, and R.G. Parton Rab11 regulates recycling through the pericentriolar recycling endosome J. Cell Biol. 135 1996 913 924 (Pubitemid 26403768)
    • (1996) Journal of Cell Biology , vol.135 , Issue.4 , pp. 913-924
    • Ullrich, O.1    Reinsch, S.2    Urbe, S.3    Zerial, M.4    Parton, R.G.5
  • 53
    • 0030697289 scopus 로고    scopus 로고
    • Functional expression cloning and characterization of SFT, a stimulator of Fe transport
    • DOI 10.1083/jcb.139.4.895
    • J.A. Gutierrez, J. Yu, S. Rivera, and M. Wessling-Resnick Functional expression cloning and characterization of SFT, a stimulator of Fe transport J. Cell Biol. 139 1997 895 905 (Pubitemid 27508560)
    • (1997) Journal of Cell Biology , vol.139 , Issue.4 , pp. 895-905
    • Gutierrez, J.A.1    Yu, J.2    Rivera, S.3    Wessling-Resnick, M.4
  • 54
    • 0032478524 scopus 로고    scopus 로고
    • Crystal structure of the hemochromatosis protein HFE and characterization of its interaction with transferrin receptor
    • DOI 10.1016/S0092-8674(00)81151-4
    • J.A. Lebrón, M.J. Bennett, D.E. Vaughn, A.J. Chirino, P.M. Snow, G.A. Mintier, J.N. Feder, and P.J. Bjorkman Crystal structure of the hemochromatosis protein HFE and characterization of its interaction with transferrin receptor Cell 93 1998 111 123 (Pubitemid 28173557)
    • (1998) Cell , vol.93 , Issue.1 , pp. 111-123
    • Lebron, J.A.1    Bennett, M.J.2    Vaughn, D.E.3    Chirino, A.J.4    Snow, P.M.5    Mintier, G.A.6    Feder, J.N.7    Bjorkman, P.J.8
  • 55
    • 0033605595 scopus 로고    scopus 로고
    • The hereditary hemochromatosis protein, HFE, specifically regulates transferrin-mediated iron uptake in HeLa cells
    • DOI 10.1074/jbc.274.13.9022
    • C.N. Roy, D.M. Penny, J.N. Feder, and C.A. Enns The hereditary hemochromatosis protein, HFE, specifically regulates transferrin-mediated iron uptake in HeLa cells J. Biol. Chem. 274 1999 9022 9028 (Pubitemid 29164707)
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.13 , pp. 9022-9028
    • Roy, C.N.1    Penny, D.M.2    Feder, J.N.3    Enns, C.A.4
  • 58
    • 79955492902 scopus 로고    scopus 로고
    • HFE gene variants affect iron in the brain
    • W. Nandar, and J.R. Connor HFE gene variants affect iron in the brain J. Nutr. 141 2011 729S 739S
    • (2011) J. Nutr. , vol.141
    • Nandar, W.1    Connor, J.R.2
  • 59
    • 0019138448 scopus 로고
    • Iron transferrin receptors in rat and human cerebrum
    • P. Angelova-Gateva Iron transferrin receptors in rat and human cerebrum Agressologie 21 1980 27 30 (Pubitemid 11207172)
    • (1980) Agressologie , vol.21 , Issue.1 , pp. 27-30
    • Angelova-Gateva, P.1
  • 63
    • 0347993815 scopus 로고    scopus 로고
    • The significance of the mutated divalent metal transporter (DMT1) on iron transport into the Belgrade rat brain
    • T. Moos, and E.H. Morgan The significance of the mutated divalent metal transporter (DMT1) on iron transport into the Belgrade rat brain J. Neurochem. 88 2004 233 245 (Pubitemid 38030226)
    • (2004) Journal of Neurochemistry , vol.88 , Issue.1 , pp. 233-245
    • Moos, T.1    Morgan, E.H.2
  • 64
    • 33748090285 scopus 로고    scopus 로고
    • Brain capillary endothelial cells mediate iron transport into the brain by segregating iron from transferrin without the involvement of divalent metal transporter 1
    • DOI 10.1111/j.1471-4159.2006.04023.x
    • T. Moos, T. Skjoerringe, S. Gosk, and E.H. Morgan Brain capillary endothelial cells mediate iron transport into the brain by segregating iron from transferrin without the involvement of divalent metal transporter 1 J. Neurochem. 98 2006 1946 1958 (Pubitemid 44298257)
    • (2006) Journal of Neurochemistry , vol.98 , Issue.6 , pp. 1946-1958
    • Moos, T.1    Skjoerringe, T.2    Gosk, S.3    Morgan, E.H.4
  • 66
    • 0030739637 scopus 로고    scopus 로고
    • Transport of iron in the blood-brain-cerebrospinal fluid system
    • M.W. Bradbury Transport of iron in the blood-brain-cerebrospinal fluid system J. Neurochem. 69 1997 443 454 (Pubitemid 27327945)
    • (1997) Journal of Neurochemistry , vol.69 , Issue.2 , pp. 443-454
    • Bradbury, M.W.B.1
  • 67
    • 0037354170 scopus 로고    scopus 로고
    • Brain iron uptake and homeostatic mechanisms: An overview
    • DOI 10.1023/A:1020718718550
    • J.R. Burdo, and J.R. Connor Brain iron uptake and homeostatic mechanisms: an overview Biometals 16 2003 63 75 (Pubitemid 36140216)
    • (2003) BioMetals , vol.16 , Issue.1 , pp. 63-75
    • Burdo, J.R.1    Connor, J.R.2
  • 69
    • 0024159960 scopus 로고
    • Studies of the slow bidirectional transport of iron and transferrin across the blood-brain barrier
    • DOI 10.1016/0361-9230(88)90021-4
    • W.A. Banks, A.J. Kastin, M.B. Fasold, C.M. Barrera, and G. Augereau Studies of the slow bidirectional transport of iron and transferrin across the blood-brain barrier Brain Res. Bull. 21 1988 881 885 (Pubitemid 19266486)
    • (1988) Brain Research Bulletin , vol.21 , Issue.6 , pp. 881-885
    • Banks, W.A.1    Kastin, A.J.2    Fasold, M.B.3    Barrera, C.M.4    Augereau, G.5
  • 71
    • 1042301280 scopus 로고    scopus 로고
    • Brain capillary endothelium and choroid plexus epithelium regulate transport of transferrin-bound and free iron into the rat brain
    • R. Deane, W. Zheng, and B.V. Zlokovic Brain capillary endothelium and choroid plexus epithelium regulate transport of transferrin-bound and free iron into the rat brain J. Neurochem. 88 2004 813 820 (Pubitemid 38199301)
    • (2004) Journal of Neurochemistry , vol.88 , Issue.4 , pp. 813-820
    • Deane, R.1    Zheng, W.2    Zlokovic, B.V.3
  • 73
    • 0032549868 scopus 로고    scopus 로고
    • 125I]transferrin injected into the ventricular system of the rat
    • DOI 10.1016/S0006-8993(98)00055-9, PII S0006899398000559
    • T. Moos, and E.H. Morgan Kinetics and distribution of [59Fe-125I]transferrin injected into the ventricular system of the rat Brain Res. 790 1998 115 128 (Pubitemid 28234495)
    • (1998) Brain Research , vol.790 , Issue.1-2 , pp. 115-128
    • Moos, T.1    Morgan, E.H.2
  • 74
    • 34548168838 scopus 로고    scopus 로고
    • Properties of the lymphatic cerebrospinal fluid transport system in the rat: Impact of elevated intracranial pressure
    • DOI 10.1159/000104255
    • L. Koh, G. Nagra, and M. Johnston Properties of the lymphatic cerebrospinal fluid transport system in the rat: impact of elevated intracranial pressure J. Vasc. Res. 44 2007 423 432 (Pubitemid 47312663)
    • (2007) Journal of Vascular Research , vol.44 , Issue.5 , pp. 423-432
    • Koh, L.1    Nagra, G.2    Johnston, M.3
  • 75
    • 0014481056 scopus 로고
    • Junctions between intimately apposed cell membranes in the vertebrate brain
    • M.W. Brightman, and T.S. Reese Junctions between intimately apposed cell membranes in the vertebrate brain J. Cell Biol. 40 1969 648 677
    • (1969) J. Cell Biol. , vol.40 , pp. 648-677
    • Brightman, M.W.1    Reese, T.S.2
  • 76
    • 0023654529 scopus 로고
    • Distribution of transferrin synthesis in brain and other tissues in the rat
    • A.R. Aldred, P.W. Dickson, P.D. Marley, and G. Schreiber Distribution of transferrin synthesis in brain and other tissues in the rat J. Biol. Chem. 262 1987 5293 5297
    • (1987) J. Biol. Chem. , vol.262 , pp. 5293-5297
    • Aldred, A.R.1    Dickson, P.W.2    Marley, P.D.3    Schreiber, G.4
  • 77
    • 0024354993 scopus 로고
    • Developmental patterns of gene expression of secreted proteins in brain and choroid plexus
    • T. Thomas, G. Schreiber, and A. Jaworowski Developmental patterns of gene expression of secreted proteins in brain and choroid plexus Dev. Biol. 134 1989 38 47 (Pubitemid 19176468)
    • (1989) Developmental Biology , vol.134 , Issue.1 , pp. 38-47
    • Thomas, T.1    Schreiber, G.2    Jaworowski, A.3
  • 78
    • 58649108784 scopus 로고    scopus 로고
    • Diurnal cycle influences peripheral and brain iron levels in mice
    • E.L. Unger, C.J. Earley, and J.L. Beard Diurnal cycle influences peripheral and brain iron levels in mice J. Appl. Physiol. 106 2009 187 193
    • (2009) J. Appl. Physiol. , vol.106 , pp. 187-193
    • Unger, E.L.1    Earley, C.J.2    Beard, J.L.3
  • 79
    • 40349112963 scopus 로고    scopus 로고
    • The blood-CSF barrier explained: When development is not immaturity
    • DOI 10.1002/bies.20718
    • P.A. Johansson, K.M. Dziegielewska, S.A. Liddelow, and N.R. Saunders The blood-CSF barrier explained: when development is not immaturity Bioessays 30 2008 237 248 (Pubitemid 351341128)
    • (2008) BioEssays , vol.30 , Issue.3 , pp. 237-248
    • Johansson, P.A.1    Dziegielewska, K.M.2    Liddelow, S.A.3    Saunders, N.R.4
  • 80
    • 67449123256 scopus 로고    scopus 로고
    • Brain iron homeostasis and neurodegenerative disease
    • E.E. Benarroch Brain iron homeostasis and neurodegenerative disease Neurology 72 2009 1436 1440
    • (2009) Neurology , vol.72 , pp. 1436-1440
    • Benarroch, E.E.1
  • 81
    • 74449085808 scopus 로고    scopus 로고
    • Brain iron homeostasis, the choroid plexus, and localization of iron transport proteins
    • T.A. Rouault, D.L. Zhang, and S.Y. Jeong Brain iron homeostasis, the choroid plexus, and localization of iron transport proteins Metab. Brain Dis. 24 2009 673 684
    • (2009) Metab. Brain Dis. , vol.24 , pp. 673-684
    • Rouault, T.A.1    Zhang, D.L.2    Jeong, S.Y.3
  • 83
    • 0032701114 scopus 로고    scopus 로고
    • Transferrin receptors on the plasma membrane of cultured rat astrocytes
    • Z.M. Qian, Y. To, P.L. Tang, and Y.M. Feng Transferrin receptors on the plasma membrane of cultured rat astrocytes Exp. Brain Res. 129 1999 473 476 (Pubitemid 29537620)
    • (1999) Experimental Brain Research , vol.129 , Issue.3 , pp. 473-476
    • Zhong, M.Q.1    To, Y.2    Pak, L.T.3    You, M.F.4
  • 84
    • 33750709690 scopus 로고    scopus 로고
    • Brain Iron Metabolism
    • DOI 10.1016/j.spen.2006.08.002, PII S107190910600101X
    • T.A. Rouault, and S. Cooperman Brain iron metabolism Semin. Pediatr. Neurol. 13 2006 142 148 (Pubitemid 44709651)
    • (2006) Seminars in Pediatric Neurology , vol.13 , Issue.3 , pp. 142-148
    • Rouault, T.A.1    Cooperman, S.2
  • 85
    • 34547782810 scopus 로고    scopus 로고
    • Copper and iron disorders of the brain
    • DOI 10.1146/annurev.neuro.30.051606.094232
    • E. Madsen, and J.D. Gitlin Copper and iron disorders of the brain Annu. Rev. Neurosci. 30 2007 317 337 (Pubitemid 47224759)
    • (2007) Annual Review of Neuroscience , vol.30 , pp. 317-337
    • Madsen, E.1    Gitlin, J.D.2
  • 86
    • 0038711587 scopus 로고    scopus 로고
    • Glycosylphosphatidylinositol-anchored ceruloplasmin is required for iron efflux from cells in the central nervous system
    • DOI 10.1074/jbc.M301988200
    • S.Y. Jeong, and S. David Glycosylphosphatidylinositol-anchored ceruloplasmin is required for iron efflux from cells in the central nervous system J. Biol. Chem. 278 2003 27144 27148 (Pubitemid 36876870)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.29 , pp. 27144-27148
    • Jeong, S.Y.1    David, S.2
  • 87
    • 33748889489 scopus 로고    scopus 로고
    • Age-related changes in iron homeostasis and cell death in the cerebellum of ceruloplasmin-deficient mice
    • DOI 10.1523/JNEUROSCI.2922-06.2006
    • S.Y. Jeong, and S. David Age-related changes in iron homeostasis and cell death in the cerebellum of ceruloplasmin-deficient mice J. Neurosci. 26 2006 9810 9819 (Pubitemid 44427720)
    • (2006) Journal of Neuroscience , vol.26 , Issue.38 , pp. 9810-9819
    • Suh, Y.J.1    David, S.2
  • 88
    • 0029433318 scopus 로고
    • Cellular management of iron in the brain
    • Suppl
    • J.R. Connor, and S.L. Menzies Cellular management of iron in the brain J. Neurol. Sci. 134 1995 33 44 Suppl
    • (1995) J. Neurol. Sci. , vol.134 , pp. 33-44
    • Connor, J.R.1    Menzies, S.L.2
  • 89
    • 0031581351 scopus 로고    scopus 로고
    • Nutrition. from 'whither' to 'wither' micronutrient malnutrition?
    • C.E. West, and J.G. Hautvast Nutrition. From 'whither' to 'wither' micronutrient malnutrition? Lancet 350 Suppl. 3 1997 SIII15
    • (1997) Lancet , vol.350 , Issue.SUPPL. 3 , pp. 15
    • West, C.E.1    Hautvast, J.G.2
  • 90
    • 0026779475 scopus 로고
    • Axonal and dendritic endocytic pathways in cultured neurons
    • R.G. Parton, K. Simons, and C.G. Dotti Axonal and dendritic endocytic pathways in cultured neurons J. Cell Biol. 119 1992 123 137
    • (1992) J. Cell Biol. , vol.119 , pp. 123-137
    • Parton, R.G.1    Simons, K.2    Dotti, C.G.3
  • 91
    • 0026048669 scopus 로고
    • Colocalization of synaptophysin with transferrin receptors: Implications for synaptic vesicle biogenesis
    • P.L. Cameron, T.C. Südhof, R. Jahn, and P. De Camilli Colocalization of synaptophysin with transferrin receptors: implications for synaptic vesicle biogenesis J. Cell Biol. 115 1991 151 164 (Pubitemid 21909902)
    • (1991) Journal of Cell Biology , vol.115 , Issue.1 , pp. 151-164
    • Cameron, P.L.1    Sudhof, T.C.2    Jahn, R.3    De Camilli, P.4
  • 92
    • 0030684039 scopus 로고    scopus 로고
    • Dendroaxonal transcytosis of transferrin in cultured hippocampal and sympathetic neurons
    • A. Hémar, J.C. Olivo, E. Williamson, R. Saffrich, and C.G. Dotti Dendroaxonal transcytosis of transferrin in cultured hippocampal and sympathetic neurons J. Neurosci. 17 1997 9026 9034 (Pubitemid 27498430)
    • (1997) Journal of Neuroscience , vol.17 , Issue.23 , pp. 9026-9034
    • Hemar, A.1    Olivo, J.-C.2    Williamson, E.3    Saffrich, R.4    Dotti, C.G.5
  • 94
    • 0028243124 scopus 로고
    • Immunocytochemical analyses of distributions of Na, K-ATPase and GLUT1, insulin and transferrin receptors in the developing retinal pigment epithelial cells
    • K. Sugasawa, J. Deguchi, T. Okami, A. Yamamoto, K. Omori, M. Uyama, and Y. Tashiro Immunocytochemical analyses of distributions of Na, K-ATPase and GLUT1, insulin and transferrin receptors in the developing retinal pigment epithelial cells Cell Struct. Funct. 19 1994 21 28 (Pubitemid 24158525)
    • (1994) Cell Structure and Function , vol.19 , Issue.1 , pp. 21-28
    • Sugasawa, K.1    Deguchi, J.2    Okami, T.3    Yamamoto, A.4    Omori, K.5    Uyama, M.6    Tashiro, Y.7
  • 96
    • 79951858362 scopus 로고    scopus 로고
    • Developmental iron uptake and axonal transport in the retina of the rat
    • T. Moos, N. Bernth, Y. Courtois, and E.H. Morgan Developmental iron uptake and axonal transport in the retina of the rat Mol. Cell. Neurosci. 46 2011 607 613
    • (2011) Mol. Cell. Neurosci. , vol.46 , pp. 607-613
    • Moos, T.1    Bernth, N.2    Courtois, Y.3    Morgan, E.H.4
  • 97
    • 0242594002 scopus 로고    scopus 로고
    • Inhaled iron, unlike manganese, is not transported to the rat brain via the olfactory pathway
    • DOI 10.1016/S0041-008X(03)00340-5
    • D.B. Rao, B.A. Wong, B.E. McManus, A.M. McElveen, A.R. James, and D.C. Dorman Inhaled iron, unlike manganese, is not transported to the rat brain via the olfactory pathway Toxicol. Appl. Pharmacol. 193 2003 116 126 (Pubitemid 37373771)
    • (2003) Toxicology and Applied Pharmacology , vol.193 , Issue.1 , pp. 116-126
    • Rao, D.B.1    Wong, B.A.2    McManus, B.E.3    McElveen, A.M.4    James, A.R.5    Dorman, D.C.6
  • 99
    • 0034671436 scopus 로고    scopus 로고
    • 2) to the rat brain: Toxicokinetic investigations in a unilateral nasal occlusion model
    • DOI 10.1006/taap.2000.9073
    • K.A. Brenneman, B.A. Wong, M.A. Buccellato, E.R. Costa, E.A. Gross, and D.C. Dorman Direct olfactory transport of inhaled manganese ((54)MnCl(2)) to the rat brain: toxicokinetic investigations in a unilateral nasal occlusion model Toxicol. Appl. Pharmacol. 169 2000 238 248 (Pubitemid 32048501)
    • (2000) Toxicology and Applied Pharmacology , vol.169 , Issue.3 , pp. 238-248
    • Brenneman, K.A.1    Wong, B.A.2    Buccellato, M.A.3    Costa, E.R.4    Gross, E.A.5    Dorman, D.C.6
  • 101
    • 0025895433 scopus 로고
    • Manganese neurotoxicity: Cellular effects and blood-brain barrier transport
    • M. Aschner, and J.L. Aschner Manganese neurotoxicity: cellular effects and blood-brain barrier transport Neurosci. Biobehav. Rev. 15 1991 333 340
    • (1991) Neurosci. Biobehav. Rev. , vol.15 , pp. 333-340
    • Aschner, M.1    Aschner, J.L.2
  • 102
    • 0024462463 scopus 로고
    • Effect of latent iron deficiency on metal levels of rat brain regions
    • A. Shukla, K.N. Agarwal, and G.S. Shukla Effect of latent iron deficiency on metal levels of rat brain regions Biol. Trace Elem. Res. 22 1989 141 152 (Pubitemid 19267771)
    • (1989) Biological Trace Element Research , vol.22 , Issue.2 , pp. 141-152
    • Shukla, A.1    Agarwal, K.N.2    Shukla, G.S.3
  • 103
    • 0026324113 scopus 로고
    • Effect of dietary iron deficiency on mineral levels in tissues of rats
    • K. Yokoi, M. Kimura, and Y. Itokawa Effect of dietary iron deficiency on mineral levels in tissues of rats Biol. Trace Elem. Res. 29 1991 257 265
    • (1991) Biol. Trace Elem. Res. , vol.29 , pp. 257-265
    • Yokoi, K.1    Kimura, M.2    Itokawa, Y.3
  • 104
    • 0035986114 scopus 로고    scopus 로고
    • Manganese accumulates in iron-deficient rat brain regions in a heterogeneous fashion and is associated with neurochemical alterations
    • DOI 10.1385/BTER:87:1-3:143
    • K.M. Erikson, Z.K. Shihabi, J.L. Aschner, and M. Aschner Manganese accumulates in iron-deficient rat brain regions in a heterogeneous fashion and is associated with neurochemical alterations Biol. Trace Elem. Res. 87 2002 143 156 (Pubitemid 34721827)
    • (2002) Biological Trace Element Research , vol.87 , Issue.1-3 , pp. 143-156
    • Erikson, K.M.1    Shihabi, Z.K.2    Aschner, J.L.3    Aschner, M.4
  • 106
    • 0021107162 scopus 로고
    • Thermodynamic binding constants for gallium transferrin
    • W.R. Harris, and V.L. Pecoraro Thermodynamic binding constants for gallium transferrin Biochemistry 22 1983 292 299
    • (1983) Biochemistry , vol.22 , pp. 292-299
    • Harris, W.R.1    Pecoraro, V.L.2
  • 107
    • 0020972548 scopus 로고
    • Thermodynamic binding constant of the zinc-human serum transferrin complex
    • W.R. Harris Thermodynamic binding constants of the zinc-human serum transferrin complex Biochemistry 22 1983 3920 3926 (Pubitemid 13035561)
    • (1983) Biochemistry , vol.22 , Issue.16 , pp. 3920-3926
    • Harris, W.R.1
  • 108
    • 0024374606 scopus 로고
    • Effects of transferrin-indium on cellular proliferation of a human leukemia cell line
    • P.L. Moran, and P.A. Seligman Effects of transferrin-indium on cellular proliferation of a human leukemia cell line Cancer Res. 49 1989 4237 4241 (Pubitemid 19207266)
    • (1989) Cancer Research , vol.49 , Issue.15 , pp. 4237-4241
    • Moran, P.L.1    Seligman, P.A.2
  • 109
    • 0023819346 scopus 로고
    • Aluminum, chemical physiology, and Alzheimer's disease
    • J.D. Birchall, and J.S. Chappell Aluminum, chemical physiology, and Alzheimer's disease Lancet 2 1988 1008 1010
    • (1988) Lancet , vol.2 , pp. 1008-1010
    • Birchall, J.D.1    Chappell, J.S.2
  • 110
    • 77949347463 scopus 로고
    • Geographical relation between Alzheimer's disease and aluminium in drinking water
    • C.N. Martyn, D.J. Barker, C. Osmond, E.C. Harris, J.A. Edwardson, and R.F. Lacey Geographical relation between Alzheimer's disease and aluminum in drinking water Lancet 1 1989 59 62 (Pubitemid 19033991)
    • (1989) Lancet , vol.1 , Issue.8629 , pp. 59-62
    • Martyn, C.N.1    Osmond, C.2    Edwardson, J.A.3    Barker, D.J.P.4    Harris, E.C.5    Lacey, R.F.6
  • 111
    • 0018827099 scopus 로고
    • Alzheimer's disease: X-ray spectrometric evidence of aluminum accumulation in neurofibrillary tangle-bearing neurons
    • D.P. Perl, and A.R. Brody Alzheimer's disease: X-ray spectrometric evidence of aluminum accumulation in neurofibrillary tangle-bearing neurons Science 208 1980 297 299 (Pubitemid 10075227)
    • (1980) Science , vol.208 , Issue.4441 , pp. 297-299
    • Perl, D.P.1    Brody, A.R.2
  • 112
    • 0028033537 scopus 로고
    • Brain-specific expression of the human transferrin gene. Similar elements govern transcription in oligodendrocytes and in a neuronal cell line
    • A. Espinosa de los Monteros, B.E. Sawaya, F. Guillou, M.M. Zakin, J. de Vellis, and E. Schaeffer Brain-specific expression of the human transferrin gene. Similar elements govern transcription in oligodendrocytes and in a neuronal cell line J. Biol. Chem. 269 1994 24504 24510
    • (1994) J. Biol. Chem. , vol.269 , pp. 24504-24510
    • Espinosa De Los Monteros, A.1    Sawaya, B.E.2    Guillou, F.3    Zakin, M.M.4    De Vellis, J.5    Schaeffer, E.6
  • 113
    • 0026059099 scopus 로고
    • Expression of transferrin mRNA in the CNS of normal and jimpy mice
    • W.P. Bartlett, X.S. Li, and J.R. Connor Expression of transferrin mRNA in the CNS of normal and jimpy mice J. Neurochem. 57 1991 318 322
    • (1991) J. Neurochem. , vol.57 , pp. 318-322
    • Bartlett, W.P.1    Li, X.S.2    Connor, J.R.3
  • 114
    • 0042626103 scopus 로고    scopus 로고
    • Neuropathological examination suggests impaired brain iron acquisition in restless legs syndrome
    • J.R. Connor, P.J. Boyer, S.L. Menzies, B. Dellinger, R.P. Allen, W.G. Ondo, and C.J. Earley Neuropathological examination suggests impaired brain iron acquisition in restless legs syndrome Neurology 61 2003 304 309 (Pubitemid 36975956)
    • (2003) Neurology , vol.61 , Issue.3 , pp. 304-309
    • Connor, J.R.1    Boyer, P.J.2    Menzies, S.L.3    Dellinger, B.4    Allen, R.P.5    Ondo, W.G.6    Earley, C.J.7
  • 115
    • 0026778299 scopus 로고
    • Transferrin receptor expression in myelin deficient (md) rats
    • A.J. Roskams, and J.R. Connor Transferrin receptor expression in myelin deficient (md) rats J. Neurosci. Res. 31 1992 421 427
    • (1992) J. Neurosci. Res. , vol.31 , pp. 421-427
    • Roskams, A.J.1    Connor, J.R.2
  • 117
    • 79954616688 scopus 로고    scopus 로고
    • H-ferritin is the major source of iron for oligodendrocytes
    • B. Todorich, X. Zhang, and J.R. Connor H-ferritin is the major source of iron for oligodendrocytes Glia 59 2011 927 935
    • (2011) Glia , vol.59 , pp. 927-935
    • Todorich, B.1    Zhang, X.2    Connor, J.R.3
  • 118
    • 0023941555 scopus 로고
    • Synthesis and localization of plasma proteins in the developing human brain. Integrity of the fetal blood-brain barrier to endogenous proteins of hepatic origin
    • K. Møllgård, K.M. Dziegielewska, N.R. Saunders, H. Zakut, and H. Soreq Synthesis and localization of plasma proteins in the developing human brain. Integrity of the fetal blood-brain barrier to endogenous proteins of hepatic origin Dev. Biol. 128 1988 207 221
    • (1988) Dev. Biol. , vol.128 , pp. 207-221
    • Møllgård, K.1    Dziegielewska, K.M.2    Saunders, N.R.3    Zakut, H.4    Soreq, H.5
  • 120
    • 0027548150 scopus 로고
    • Characterization of "plasma proteins" secreted by cultured rat macroglial cells
    • K.R. Zahs, V. Bigornia, and C.F. Deschepper Characterization of "plasma proteins" secreted by cultured rat macroglial cells Glia 7 1993 121 133
    • (1993) Glia , vol.7 , pp. 121-133
    • Zahs, K.R.1    Bigornia, V.2    Deschepper, C.F.3
  • 123
    • 0027448674 scopus 로고
    • Transferrin in the central nervous system of the shiverer mouse myelin mutant
    • DOI 10.1002/jnr.490360502
    • J.R. Connor, A.J. Roskams, S.L. Menzies, and M.E. Williams Transferrin in the central nervous system of the shiverer mouse myelin mutant J. Neurosci. Res. 36 1993 501 507 (Pubitemid 23354042)
    • (1993) Journal of Neuroscience Research , vol.36 , Issue.5 , pp. 501-507
    • Connor, J.R.1    Roskams, A.J.2    Menzies, S.L.3    Williams, M.E.4
  • 125
    • 0029065064 scopus 로고
    • Cellular distribution of iron, transferrin, and ferritin in the hypotransferrinemic (Hp) mouse brain
    • T.K. Dickinson, and J.R. Connor 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
  • 126
    • 0032519436 scopus 로고    scopus 로고
    • Evidence for non-transferrin-mediated uptake and release of iron and manganese in glial cell cultures from hypotransferrinemic mice
    • DOI 10.1002/(SICI)1097-4547(19980215)51:4<454::AID-JNR5>3.0.CO;2-B
    • A. Takeda, A. Devenyi, and J.R. Connor Evidence for non-transferrin- mediated uptake and release of iron and manganese in glial cell cultures from hypotransferrinemic mice J. Neurosci. Res. 51 1998 454 462 (Pubitemid 28106706)
    • (1998) Journal of Neuroscience Research , vol.51 , Issue.4 , pp. 454-462
    • Takeda, A.1    Devenyi, A.2    Connor, J.R.3
  • 127
    • 4444273210 scopus 로고    scopus 로고
    • Effect of manipulation of iron storage, transport, or availability on myelin composition and brain iron content in three different animal models
    • DOI 10.1002/jnr.20207
    • E. Ortiz, J.M. Pasquini, K. Thompson, B. Felt, G. Butkus, J. Beard, and J.R. Connor Effect of manipulation of iron storage, transport, or availability on myelin composition and brain iron content in three different animal models J. Neurosci. Res. 77 2004 681 689 (Pubitemid 39194609)
    • (2004) Journal of Neuroscience Research , vol.77 , Issue.5 , pp. 681-689
    • Ortiz, E.1    Pasquini, J.M.2    Thompson, K.3    Felt, B.4    Butkus, G.5    Beard, J.6    Connor, J.R.7
  • 130
    • 0030968309 scopus 로고    scopus 로고
    • Single intracranial injection of apotransferrin in young rats increases the expression of specific myelin protein mRNA
    • DOI 10.1002/(SICI)1097-4547(19970315)47:6<603::AID-JNR5>3.0.CO;2-H
    • O.E. Escobar Cabrera, M.M. Zakin, E.F. Soto, and J.M. Pasquini Single intracranial injection of apotransferrin in young rats increases the expression of specific myelin protein mRNA J. Neurosci. Res. 47 1997 603 608 (Pubitemid 27138742)
    • (1997) Journal of Neuroscience Research , vol.47 , Issue.6 , pp. 603-608
    • Cabrera, O.E.E.1    Zakin, M.M.2    Soto, E.F.3    Pasquini, J.M.4
  • 131
    • 0028662387 scopus 로고
    • Single intracerebral injection of apotransferrin in young rats induces increased myelination
    • O.E. Escobar Cabrera, E.R. Bongarzone, E.F. Soto, and J.M. Pasquini Single intracerebral injection of apotransferrin in young rats induces increased myelination Dev. Neurosci. 16 1994 248 254
    • (1994) Dev. Neurosci. , vol.16 , pp. 248-254
    • Escobar Cabrera, O.E.1    Bongarzone, E.R.2    Soto, E.F.3    Pasquini, J.M.4
  • 132
    • 0342514711 scopus 로고    scopus 로고
    • Myelin membranes isolated from rats intracranially injected with apoTransferrin are more susceptible to in vitro peroxidation
    • DOI 10.1023/A:1007543600609
    • O.E. Escobar Cabrera, E.F. Soto, and J.M. Pasquini Myelin membranes isolated from rats intracranially injected with apotransferrin are more susceptible to in vitro peroxidation Neurochem. Res. 25 2000 87 93 (Pubitemid 30074279)
    • (2000) Neurochemical Research , vol.25 , Issue.1 , pp. 87-93
    • Escobar Cabrera, O.E.1    Soto, E.F.2    Pasquini, J.M.3
  • 134
    • 0037309720 scopus 로고    scopus 로고
    • Gene expression of transferrin and tranferrin receptor in brains of control vs. iron-deficient rats
    • DOI 10.1080/1028415021000042811
    • J. Han, J.R. Day, J.R. Connor, and J.L. Beard Gene expression of transferrin and transferrin receptor in brains of control vs. iron-deficient rats Nutr. Neurosci. 6 2003 1 10 (Pubitemid 36157526)
    • (2003) Nutritional Neuroscience , vol.6 , Issue.1 , pp. 1-10
    • Han, J.1    Day, J.R.2    Connor, J.R.3    Beard, J.L.4
  • 135
    • 0037266963 scopus 로고    scopus 로고
    • Morphological changes of myelin sheaths in rats intracranially injected with apotransferrin
    • DOI 10.1023/A:1021604413737
    • C.B. Marta, P. Paez, M. Lopez, A. Pellegrino de Iraldi, E.F. Soto, and J.M. Pasquini Morphological changes of myelin sheaths in rats intracranially injected with apotransferrin Neurochem. Res. 28 2003 101 110 (Pubitemid 36173231)
    • (2003) Neurochemical Research , vol.28 , Issue.1 , pp. 101-110
    • Marta, C.B.1    Paez, P.2    Lopez, M.3    De Iraldi, A.P.4    Soto, E.F.5    Pasquini, J.M.6
  • 136
    • 24544471440 scopus 로고    scopus 로고
    • Observations from the anaesthetized rabbit, pertinent to the mechanism of iron transport into brain
    • M. Bradbury Observations from the anaesthetized rabbit, pertinent to the mechanism of iron transport into brain J. Physiol. 491 1996 30P
    • (1996) J. Physiol. , vol.491
    • Bradbury, M.1
  • 137
    • 0036970621 scopus 로고    scopus 로고
    • Apotransferrin decreases migration and enhances differentiation of oligodendroglial progenitor cells in an in vitro system
    • DOI 10.1159/000064945
    • P.M. Paez, C.B. Marta, M.B. Moreno, E.F. Soto, and J.M. Pasquini Apotransferrin decreases migration and enhances differentiation of oligodendroglial progenitor cells in an in vitro system Dev. Neurosci. 24 2002 47 58 (Pubitemid 36151217)
    • (2002) Developmental Neuroscience , vol.24 , Issue.1 , pp. 47-58
    • Paez, P.M.1    Marta, C.B.2    Moreno, M.B.3    Soto, E.F.4    Pasquini, J.M.5
  • 138
    • 0035198691 scopus 로고    scopus 로고
    • The neurotoxicant, cuprizone, as a model to study demyelination and remyelination in the central nervous system
    • G.K. Matsushima, and P. Morell The neurotoxicant, cuprizone, as a model to study demyelination and remyelination in the central nervous system Brain Pathol. 11 2001 107 116
    • (2001) Brain Pathol. , vol.11 , pp. 107-116
    • Matsushima, G.K.1    Morell, P.2
  • 139
    • 0037477740 scopus 로고    scopus 로고
    • A delicate balance: Homeostatic control of copper uptake and distribution
    • M.M. Peña, J. Lee, and D.J. Thiele A delicate balance: homeostatic control of copper uptake and distribution J. Nutr. 129 1999 1251 1260 (Pubitemid 29304971)
    • (1999) Journal of Nutrition , vol.129 , Issue.7 , pp. 1251-1260
    • Pena, M.M.O.1    Lee, J.2    Thiele, D.J.3
  • 142
    • 0036971447 scopus 로고    scopus 로고
    • Ferritin binding in the developing mouse brain follows a pattern similar to myelination and is unaffected by the jimpy mutation
    • DOI 10.1159/000065704
    • S.W. Hulet, S. Menzies, and J.R. Connor Ferritin binding in the developing mouse brain follows a pattern similar to myelination and is unaffected by the jimpy mutation Dev. Neurosci. 24 2002 208 213 (Pubitemid 36151451)
    • (2002) Developmental Neuroscience , vol.24 , Issue.2-3 , pp. 208-213
    • Hulet, S.W.1    Menzies, S.2    Connor, J.R.3
  • 143
    • 0024429492 scopus 로고
    • The development of the transferrin-transferrin receptor system in relation to astrocytes, MBP and galactocerebroside in normal and myelin-deficient rat optic nerves
    • DOI 10.1016/0165-3806(89)90029-1
    • H.H. Lin, and J.R. Connor The development of the transferrin-transferrin receptor system in relation to astrocytes, MBP and galactocerebroside in normal and myelin-deficient rat optic nerves Brain Res. Dev. Brain Res. 49 1989 281 293 (Pubitemid 19250379)
    • (1989) Developmental Brain Research , vol.49 , Issue.2 , pp. 281-293
    • Lin, H.H.1    Connor, J.R.2
  • 144
    • 0028911242 scopus 로고
    • Transient expression of transferrin receptors and localisation of iron in amoeboid microglia in postnatal rats
    • C. Kaur, and E.A. Ling Transient expression of transferrin receptors and localisation of iron in amoeboid microglia in postnatal rats J. Anat. 186 Pt 1 1995 165 173
    • (1995) J. Anat. , vol.186 , Issue.PART 1 , pp. 165-173
    • Kaur, C.1    Ling, E.A.2
  • 145
    • 0023638828 scopus 로고
    • Increased nigral iron content in postmortem Parkinsonian brain
    • D.T. Dexter, F.R. Wells, F. Agid, Y. Agid, A.J. Lees, P. Jenner, and C.D. Marsden Increased nigral iron content in postmortem parkinsonian brain Lancet 2 1987 1219 1220 (Pubitemid 17156630)
    • (1987) Lancet , vol.2 , Issue.8569 , pp. 1219-1220
    • Dexter, D.T.1    Wells, F.R.2    Agid, F.3    Agid, Y.4    Lees, A.J.5    Jenner, P.6    Marsden, C.D.7
  • 148
    • 0034102395 scopus 로고    scopus 로고
    • Abnormalities in CSF concentrations of ferritin and transferrin in restless legs syndrome
    • C.J. Earley, J.R. Connor, J.L. Beard, E.A. Malecki, D.K. Epstein, and R.P. Allen Abnormalities in CSF concentrations of ferritin and transferrin in restless legs syndrome Neurology 54 2000 1698 1700 (Pubitemid 30226823)
    • (2000) Neurology , vol.54 , Issue.8 , pp. 1698-1700
    • Earley, C.J.1    Connor, J.R.2    Beard, J.L.3    Malecki, E.A.4    Epstein, D.K.5    Allen, R.P.6
  • 149
    • 79952400329 scopus 로고    scopus 로고
    • Decreased CSF transferrin in sCJD: A potential pre-mortem diagnostic test for prion disorders
    • A. Singh, A.J. Beveridge, and N. Singh Decreased CSF transferrin in sCJD: a potential pre-mortem diagnostic test for prion disorders PLoS One 6 2011 e16804
    • (2011) PLoS One , vol.6 , pp. 16804
    • Singh, A.1    Beveridge, A.J.2    Singh, N.3
  • 151
    • 33745502924 scopus 로고    scopus 로고
    • Long-lasting neural and behavioral effects of iron deficiency in infancy
    • DOI 10.1301/nr.2006.may.S34-S43
    • B. Lozoff, J. Beard, J. Connor, F. Barbara, M. Georgieff, and T. Schallert Long-lasting neural and behavioral effects of iron deficiency in infancy Nutr. Rev. 64 2006 S34 S43 discussion S72-91 (Pubitemid 44606856)
    • (2006) Nutrition Reviews , vol.64 , Issue.SUPPL. 1
    • Lozoff, B.1    Beard, J.2    Connor, J.3    Felt, B.4    Georgieff, M.5    Schallert, T.6
  • 152
    • 0029070912 scopus 로고
    • Iron regulation in the developing rat brain: Effect of in utero ethanol exposure
    • M.W. Miller, A.J. Roskams, and J.R. Connor Iron regulation in the developing rat brain: effect of in utero ethanol exposure J. Neurochem. 65 1995 373 380
    • (1995) J. Neurochem. , vol.65 , pp. 373-380
    • Miller, M.W.1    Roskams, A.J.2    Connor, J.R.3
  • 153
    • 0025791960 scopus 로고
    • Effects of ethanol on the secretion of hepatic secretory protein in rat alcoholic liver injury
    • Y. Matsuda, A. Takada, S. Takase, and M. Yasuhara Effects of ethanol on the secretion of hepatic secretory protein in rat alcoholic liver injury Alcohol 8 1991 433 437
    • (1991) Alcohol , vol.8 , pp. 433-437
    • Matsuda, Y.1    Takada, A.2    Takase, S.3    Yasuhara, M.4
  • 154
    • 0025864470 scopus 로고
    • Accumulation of glycoprotein in the Golgi apparatus of hepatocytes in alcoholic liver injuries
    • Y. Matsuda, A. Takada, S. Takase, and H. Sato Accumulation of glycoprotein in the Golgi apparatus of hepatocytes in alcoholic liver injuries Am. J. Gastroenterol. 86 1991 854 860
    • (1991) Am. J. Gastroenterol. , vol.86 , pp. 854-860
    • Matsuda, Y.1    Takada, A.2    Takase, S.3    Sato, H.4
  • 156
    • 0032743724 scopus 로고    scopus 로고
    • Reference distributions for the negative acute-phase serum proteins, albumin, transferrin and transthyretin: A practical, simple and clinically relevant approach in a large cohort
    • R.F. Ritchie, G.E. Palomaki, L.M. Neveux, O. Navolotskaia, T.B. Ledue, and W.Y. Craig Reference distributions for the negative acute-phase serum proteins, albumin, transferrin and transthyretin: a practical, simple and clinically relevant approach in a large cohort J. Clin. Lab. Anal. 13 1999 273 279
    • (1999) J. Clin. Lab. Anal. , vol.13 , pp. 273-279
    • Ritchie, R.F.1    Palomaki, G.E.2    Neveux, L.M.3    Navolotskaia, O.4    Ledue, T.B.5    Craig, W.Y.6
  • 157
    • 0031911483 scopus 로고    scopus 로고
    • Mood disorders and dysfunction of the hypothalamic-pituitary-adrenal axis in multiple sclerosis: Association with cerebral inflammation
    • DOI 10.1001/archneur.55.1.66
    • K. Fassbender, R. Schmidt, R. Mössner, U. Kischka, J. Kühnen, A. Schwartz, and M. Hennerici Mood disorders and dysfunction of the hypothalamic-pituitary-adrenal axis in multiple sclerosis: association with cerebral inflammation Arch. Neurol. 55 1998 66 72 (Pubitemid 28139107)
    • (1998) Archives of Neurology , vol.55 , Issue.1 , pp. 66-72
    • Fassbender, K.1    Schmidt, R.2    Mossner, R.3    Kischka, U.4    Kuhnen, J.5    Schwarte, A.6    Hennerici, M.7
  • 158
    • 0035693924 scopus 로고    scopus 로고
    • Inflammation, autotoxicity and Alzheimer disease
    • DOI 10.1016/S0197-4580(01)00289-5, PII S0197458001002895
    • P.L. McGeer, and E.G. McGeer Inflammation, autotoxicity and Alzheimer disease Neurobiol. Aging 22 2001 799 809 (Pubitemid 34066546)
    • (2001) Neurobiology of Aging , vol.22 , Issue.6 , pp. 799-809
    • McGeer, P.L.1    McGeer, E.G.2
  • 160
    • 0034278467 scopus 로고    scopus 로고
    • Studies on oxidative stress, serum iron and iron binding capacity in subjects prone to the risk of coronary artery disease
    • S.B. Sharma, S. Dwivedi, N. Kumar, K.M. Prabhu, and N. Madan Studies on oxidative stress, serum iron and iron binding capacity in subjects prone to the risk of coronary artery disease Indian Heart J. 52 2000 583 586 (Pubitemid 33703184)
    • (2000) Indian Heart Journal , vol.52 , Issue.5 , pp. 583-586
    • Sharma, S.B.1    Dwivedi, S.2    Kumar, N.3    Prabhu, K.M.4    Madan, N.5
  • 161
    • 0019754340 scopus 로고
    • Serum supplements and serum-free media: Applicability for microcarrier culture of animal cells
    • J.M. Clark, C. Gebb, and M.D. Hirtenstein Serum supplements and serum-free media: applicability for microcarrier culture of animal cells Dev. Biol. Stand. 50 1981 81 91
    • (1981) Dev. Biol. Stand. , vol.50 , pp. 81-91
    • Clark, J.M.1    Gebb, C.2    Hirtenstein, M.D.3
  • 162
    • 0023830034 scopus 로고
    • Susceptibilities of lactoferrin and transferrin to myeloperoxidase- dependent loss of iron-binding capacity
    • C.C. Winterbourn, and A.L. Molloy Susceptibilities of lactoferrin and transferrin to myeloperoxidase-dependent loss of iron-binding capacity Biochem. J. 250 1988 613 616 (Pubitemid 18067912)
    • (1988) Biochemical Journal , vol.250 , Issue.2 , pp. 613-616
    • Winterbourn, C.C.1    Molloy, A.L.2
  • 163
    • 0021739838 scopus 로고
    • Oxidants from phagocytes: Agents of defense and destruction
    • B.M. Babior Oxidants from phagocytes: agents of defense and destruction Blood 64 1984 959 966 (Pubitemid 15212033)
    • (1984) Blood , vol.64 , Issue.5 , pp. 959-966
    • Babior, B.M.1
  • 164
    • 0019332452 scopus 로고
    • The effect of trypsin digestion on the structure and iron-donating properties of transferrins from several species
    • I. Esparza, and J.H. Brock The effect of trypsin digestion on the structure and iron-donating properties of transferrins from several species Biochim. Biophys. Acta 622 1980 297 307
    • (1980) Biochim. Biophys. Acta , vol.622 , pp. 297-307
    • Esparza, I.1    Brock, J.H.2
  • 165
    • 0016197623 scopus 로고
    • The formation of iron-binding fragments of hen ovotransferrin by limited proteolysis
    • J. Williams The formation of iron-binding fragments of hen ovotransferrin by limited proteolysis Biochem. J. 141 1974 745 752
    • (1974) Biochem. J. , vol.141 , pp. 745-752
    • Williams, J.1
  • 166
    • 0027428420 scopus 로고
    • Transferrin and lactoferrin undergo proteolytic cleavage in the Pseudomonas aeruginosa-infected lungs of patients with cystic fibrosis
    • B.E. Britigan, M.B. Hayek, B.N. Doebbeling, and R.B. Fick Transferrin and lactoferrin undergo proteolytic cleavage in the Pseudomonas aeruginosa-infected lungs of patients with cystic fibrosis Infect. Immun. 61 1993 5049 5055 (Pubitemid 23353879)
    • (1993) Infection and Immunity , vol.61 , Issue.12 , pp. 5049-5055
    • Britigan, B.E.1    Hayek, M.B.2    Doebbeling, B.N.3    Fick Jr., R.B.4
  • 167
    • 0023791265 scopus 로고
    • Isolation of a chymotrypsinlike enzyme from Treponema denticola
    • V.J. Uitto, D. Grenier, E.C. Chan, and B.C. McBride Isolation of a chymotrypsinlike enzyme from Treponema denticola Infect. Immun. 56 1988 2717 2722
    • (1988) Infect. Immun. , vol.56 , pp. 2717-2722
    • Uitto, V.J.1    Grenier, D.2    Chan, E.C.3    McBride, B.C.4
  • 168
    • 0024573192 scopus 로고
    • Equilibrium constants for the complexation of metal ions by serum transferrin
    • W.R. Harris Equilibrium constants for the complexation of metal ions by serum transferrin Adv. Exp. Med. Biol. 249 1989 67 93
    • (1989) Adv. Exp. Med. Biol. , vol.249 , pp. 67-93
    • Harris, W.R.1
  • 169
    • 0024390045 scopus 로고
    • Inactivation of transferrin iron binding capacity by the neutrophil myeloperoxidase system
    • R.A. Clark, and D.W. Pearson Inactivation of transferrin iron binding capacity by the neutrophil myeloperoxidase system J. Biol. Chem. 264 1989 9420 9427 (Pubitemid 19157584)
    • (1989) Journal of Biological Chemistry , vol.264 , Issue.16 , pp. 9420-9427
    • Clark, R.A.1    Pearson, D.W.2
  • 170
    • 3242707992 scopus 로고    scopus 로고
    • Biochemical model for inflammation of the brain: The effect of iron and transferrin on monocytes and lipid peroxidation
    • DOI 10.1023/B:MEBR.0000027421.33085.8b
    • S.J. van Rensburg, J. van Zyl, D. Hon, W. Daniels, J. Hendricks, F. Potocnik, and R. Erasmus Biochemical model for inflammation of the brain: the effect of iron and transferrin on monocytes and lipid peroxidation Metab. Brain Dis. 19 2004 97 112 (Pubitemid 39005629)
    • (2004) Metabolic Brain Disease , vol.19 , Issue.1-2 , pp. 97-112
    • Van Rensburg, S.J.1    Van Zyl, J.2    Hon, D.3    Daniels, W.4    Hendricks, J.5    Potocnik, F.6    Erasmus, R.7
  • 171
    • 0025298818 scopus 로고
    • Transferrin receptor in normal and neoplastic brain tissue: Implications for brain-tumor immunotherapy
    • L. Recht, C.O. Torres, T.W. Smith, V. Raso, and T.W. Griffin Transferrin receptor in normal and neoplastic brain tissue: implications for brain-tumor immunotherapy J. Neurosurg. 72 1990 941 945 (Pubitemid 20191521)
    • (1990) Journal of Neurosurgery , vol.72 , Issue.6 , pp. 941-945
    • Recht, L.1    Torres, C.O.2    Smith, T.W.3    Raso, V.4    Griffin, T.W.5
  • 172
    • 0042303765 scopus 로고    scopus 로고
    • Changes in expression of transferrin, insulin-like growth factor 1, and interleukin 4 receptors after irradiation of cells of primary malignant brain tumor cell lines
    • K.U. Kim, J. Xiao, H.T. Ni, K.H. Cho, S.R. Spellman, W.C. Low, and W.A. Hall Changes in expression of transferrin, insulin-like growth factor 1, and interleukin 4 receptors after irradiation of cells of primary malignant brain tumor cell lines Radiat. Res. 160 2003 224 231 (Pubitemid 36897503)
    • (2003) Radiation Research , vol.160 , Issue.2 , pp. 224-231
    • Kim, K.-U.1    Xiao, J.2    Ni, H.-T.3    Cho, K.H.4    Spellman, S.R.5    Low, W.C.6    Hall, W.A.7


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