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Volumn 288, Issue 24, 2013, Pages 17932-17940

Ferroportin and exocytoplasmic ferroxidase activity are required for brain microvascular endothelial cell iron efflux

Author keywords

[No Author keywords available]

Indexed keywords

BLOOD-BRAIN BARRIER; BRAIN MICROVASCULAR ENDOTHELIAL CELLS; CERULOPLASMINS; COPPER CHELATIONS; EXOCYTOPLASMIC; FERROXIDASE ACTIVITY; INDIRECT IMMUNOFLUORESCENCE; MICRO-VASCULATURE;

EID: 84879053438     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.455428     Document Type: Article
Times cited : (69)

References (40)
  • 1
    • 77951137998 scopus 로고    scopus 로고
    • Iron in neuronal function and dysfunction
    • Salvador, G. A. (2010) Iron in neuronal function and dysfunction. Bio- Factors 36, 103-110
    • (2010) Bio- Factors , vol.36 , pp. 103-110
    • Salvador, G.A.1
  • 3
    • 26944441309 scopus 로고    scopus 로고
    • Cellular iron: Ferroportin is the only way out
    • Ganz, T. (2005) Cellular iron: ferroportin is the only way out. Cell Metab. 1, 155-157
    • (2005) Cell Metab. , vol.1 , pp. 155-157
    • Ganz, T.1
  • 6
    • 79151477094 scopus 로고    scopus 로고
    • Transient expression of iron transport proteins in the capillary of the developing rat brain
    • Yang, W., Jung, K., Lee, M., Lee, Y., Nakagawa, S., Niwa, M., Cho, S., and Kim, D. (2011) Transient expression of iron transport proteins in the capillary of the developing rat brain. Cell Mol. Neurobiol. 31, 93-99
    • (2011) Cell Mol. Neurobiol. , vol.31 , pp. 93-99
    • Yang, W.1    Jung, K.2    Lee, M.3    Lee, Y.4    Nakagawa, S.5    Niwa, M.6    Cho, S.7    Kim, D.8
  • 7
    • 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
    • Jeong, S. Y., and David, S. (2003) Glycosylphosphatidylinositol-anchored ceruloplasmin is required for iron efflux from cells in the central nervous system. J. Biol. Chem. 278, 27144-27148 (Pubitemid 36876870)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.29 , pp. 27144-27148
    • Jeong, S.Y.1    David, S.2
  • 8
    • 34250800318 scopus 로고    scopus 로고
    • Ferroxidase activity is required for the stability of cell surface ferroportin in cells expressing GPI-ceruloplasmin
    • DOI 10.1038/sj.emboj.7601735, PII 7601735
    • De Domenico, I., Ward, D. M., di Patti, M. C., Jeong, S. Y., David, S., Musci, G., and Kaplan, J. (2007) Ferroxidase activity is required for the stability of cell surface ferroportin in cells expressing GPI-ceruloplasmin. EMBO J. 26, 2823-2831 (Pubitemid 46975784)
    • (2007) EMBO Journal , vol.26 , Issue.12 , pp. 2823-2831
    • De Domenico, I.1    Ward, D.M.2    Di, P.M.C.B.3    Jeong, S.Y.4    David, S.5    Musci, G.6    Kaplan, J.7
  • 9
    • 0032909207 scopus 로고    scopus 로고
    • Hephaestin, a ceruloplasmin homologue implicated in intestinal iron transport, is defective in the sla mouse
    • DOI 10.1038/5979
    • Vulpe, C. D., Kuo, Y. M., Murphy, T. L., Cowley, L., Askwith, C., Libina, N., Gitschier, J., and Anderson, G. J. (1999) Hephaestin, a ceruloplasmin homologue implicated in intestinal iron transport, is defective in the sla mouse. Nat. Genet. 21, 195-199 (Pubitemid 29070366)
    • (1999) Nature Genetics , vol.21 , Issue.2 , pp. 195-199
    • Vulpe, C.D.1    Kuo, Y.-M.2    Murphy, T.L.3    Cowley, L.4    Askwith, C.5    Libina, N.6    Gitschier, J.7    Anderson, G.I.8
  • 11
    • 34447263598 scopus 로고    scopus 로고
    • Colocalization of ferroportin-1 with hephaestin on the basolateral membrane of human intestinal absorptive cells
    • DOI 10.1002/jcb.21392
    • Han, O., and Kim, E. Y. (2007) Colocalization of ferroportin-1 with hephaestin on the basolateral membrane of human intestinal absorptive cells. J. Cell Biochem. 101, 1000-1010 (Pubitemid 47040880)
    • (2007) Journal of Cellular Biochemistry , vol.101 , Issue.4 , pp. 1000-1010
    • Han, O.1    Kim, E.-Y.2
  • 12
    • 34249305881 scopus 로고    scopus 로고
    • Brain iron toxicity: Differential responses of astrocytes, neurons, and endothelial cells
    • DOI 10.1007/s11064-007-9290-4
    • Gaasch, J. A., Lockman, P. R., Geldenhuys, W. J., Allen, D. D., and Van der Schyf, C. J. (2007) Brain iron toxicity: differential responses of astrocytes, neurons, and endothelial cells. Neurochem. Res. 32, 1196-1208 (Pubitemid 46817469)
    • (2007) Neurochemical Research , vol.32 , Issue.7 , pp. 1196-1208
    • Gaasch, J.A.1    Lockman, P.R.2    Geldenhuys, W.J.3    Allen, D.D.4    Van Der, S.C.J.5
  • 13
    • 80052923220 scopus 로고    scopus 로고
    • Iron efflux from oligodendrocytes is differentially regulated in gray and white matter
    • Schulz, K., Vulpe, C. D., Harris, L. Z., and David, S. (2011) Iron efflux from oligodendrocytes is differentially regulated in gray and white matter. J. Neurosci. 31, 13301-13311
    • (2011) J. Neurosci. , vol.31 , pp. 13301-13311
    • Schulz, K.1    Vulpe, C.D.2    Harris, L.Z.3    David, S.4
  • 14
    • 77952083750 scopus 로고    scopus 로고
    • Quantitative mass spectrometry-based proteomics reveals the dynamic range of primary mouse astrocyte protein secretion
    • Greco, T. M., Seeholzer, S. H., Mak, A., Spruce, L., and Ischiropoulos, H. (2010) Quantitative mass spectrometry-based proteomics reveals the dynamic range of primary mouse astrocyte protein secretion. J. Proteome Res. 9, 2764-2774
    • (2010) J. Proteome Res. , vol.9 , pp. 2764-2774
    • Greco, T.M.1    Seeholzer, S.H.2    Mak, A.3    Spruce, L.4    Ischiropoulos, H.5
  • 15
    • 0030856558 scopus 로고    scopus 로고
    • A novel glycosylphosphatidylinositol-anchored form of ceruloplasmin is expressed by mammalian astrocytes
    • DOI 10.1074/jbc.272.32.20185
    • Patel, B. N., and David, S. (1997) A novel glycosylphosphatidylinositol- anchored form of ceruloplasmin is expressed by mammalian astrocytes. J. Biol. Chem. 272, 20185-20190 (Pubitemid 27340128)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.32 , pp. 20185-20190
    • Patel, B.N.1    David, S.2
  • 17
    • 84875697145 scopus 로고    scopus 로고
    • Metal dyshomeostasis and oxidative stress in Alzheimer's disease
    • Greenough, M. A., Camakaris, J., and Bush, A. I. (2013) Metal dyshomeostasis and oxidative stress in Alzheimer's disease. Neurochem. Int. 62, 540-555
    • (2013) Neurochem. Int. , vol.62 , pp. 540-555
    • Greenough, M.A.1    Camakaris, J.2    Bush, A.I.3
  • 18
    • 84867132546 scopus 로고    scopus 로고
    • Impairment of interrelated iron- and copper homeostatic mechanisms in brain contributes to the pathogenesis of neurodegenerative disorders
    • Skjørringe, T., Møller, L. B., and Moos, T. (2012) Impairment of interrelated iron- and copper homeostatic mechanisms in brain contributes to the pathogenesis of neurodegenerative disorders. Front. Pharmacol. 3, 169
    • (2012) Front. Pharmacol. , vol.3 , pp. 169
    • Skjørringe, T.1    Møller, L.B.2    Moos, T.3
  • 19
    • 36248942024 scopus 로고    scopus 로고
    • Iron trafficking inside the brain
    • DOI 10.1111/j.1471-4159.2007.04976.x
    • Moos, T., Rosengren Nielsen, T., Skjørringe, T., and Morgan, E. H. (2007) Iron trafficking inside the brain. J. Neurochem. 103, 1730-1740 (Pubitemid 350126643)
    • (2007) Journal of Neurochemistry , vol.103 , Issue.5 , pp. 1730-1740
    • Moos, T.1    Nielsen, T.R.2    Skjorringe, T.3    Morgan, E.H.4
  • 20
    • 84864915735 scopus 로고    scopus 로고
    • Mechanistic analysis of iron accumulation by endothelial cells of the BBB
    • McCarthy, R. C., and Kosman, D. J. (2012) Mechanistic analysis of iron accumulation by endothelial cells of the BBB. Biometals 25, 665-675
    • (2012) Biometals , vol.25 , pp. 665-675
    • McCarthy, R.C.1    Kosman, D.J.2
  • 21
    • 67650034287 scopus 로고    scopus 로고
    • Decreased hephaestin expression and activity leads to decreased iron efflux from differentiated Caco2 cells
    • Chen, H., Attieh, Z. K., Dang, T., Huang, G., van der Hee, R. M., and Vulpe, C. (2009) Decreased hephaestin expression and activity leads to decreased iron efflux from differentiated Caco2 cells. J. Cell Biochem. 107, 803- 808
    • (2009) J. Cell Biochem. , vol.107 , pp. 803-808
    • Chen, H.1    Attieh, Z.K.2    Dang, T.3    Huang, G.4    Van Der Hee, R.M.5    Vulpe, C.6
  • 24
    • 0346461664 scopus 로고    scopus 로고
    • Ferroportin/IREG-1/MTP-1/SLC40A1 modulates the uptake of iron at the apical membrane of enterocytes
    • DOI 10.1136/gut.53.1.44
    • Thomas, C., and Oates, P. S. (2004) Ferroportin/IREG-1/MTP-1/SLC40A1 modulates the uptake of iron at the apical membrane of enterocytes. Gut. 53, 44-49 (Pubitemid 38083009)
    • (2004) Gut , vol.53 , Issue.1 , pp. 44-49
    • Thomas, C.1    Oates, P.S.2
  • 25
    • 67749109895 scopus 로고    scopus 로고
    • Hepcidin decreases iron transporter expression in vivo in mouse duodenum and spleen and in vitro in THP-1 macrophages and intestinal Caco-2 cells
    • Chung, B., Chaston, T., Marks, J., Srai, S. K., and Sharp, P. A. (2009) Hepcidin decreases iron transporter expression in vivo in mouse duodenum and spleen and in vitro in THP-1 macrophages and intestinal Caco-2 cells. J. Nutr. 139, 1457-1462
    • (2009) J. Nutr. , vol.139 , pp. 1457-1462
    • Chung, B.1    Chaston, T.2    Marks, J.3    Srai, S.K.4    Sharp, P.A.5
  • 26
    • 84856370491 scopus 로고    scopus 로고
    • Immune cells and hepatocytes express gly-cosylphosphatidylinositol- anchored ceruloplasmin at their cell surface
    • Marques, L., Auriac, A., Willemetz, A., Banha, J., Silva, B., Canonne-Hergaux, F., and Costa, L. (2012) Immune cells and hepatocytes express gly-cosylphosphatidylinositol- anchored ceruloplasmin at their cell surface. Blood Cells Mol. Dis. 48, 110-120
    • (2012) Blood Cells Mol. Dis. , vol.48 , pp. 110-120
    • Marques, L.1    Auriac, A.2    Willemetz, A.3    Banha, J.4    Silva, B.5    Canonne-Hergaux, F.6    Costa, L.7
  • 28
    • 38949166834 scopus 로고    scopus 로고
    • Role of copper in thermal stability of human ceruloplasmin
    • Sedlák, E., Žoldák, G., and Wittung-Stafshede, P. (2008) Role of copper in thermal stability of human ceruloplasmin. Biophys. J. 94, 1384-1391
    • (2008) Biophys. J. , vol.94 , pp. 1384-1391
    • Sedlák, E.1    Žoldák, G.2    Wittung-Stafshede, P.3
  • 29
    • 34250014148 scopus 로고    scopus 로고
    • Ferroportin1 and hephaestin are involved in the nigral iron accumulation of 6-OHDA-lesioned rats
    • DOI 10.1111/j.1460-9568.2007.05515.x
    • Wang, J., Jiang, H., and Xie, J. X. (2007) Ferroportin1 and hephaestin are involved in the nigral iron accumulation of 6-OHDA-lesioned rats. Eur. J. Neurosci. 25, 2766-2772 (Pubitemid 46888831)
    • (2007) European Journal of Neuroscience , vol.25 , Issue.9 , pp. 2766-2772
    • Wang, J.1    Jiang, H.2    Xie, J.-X.3
  • 30
    • 2942588454 scopus 로고    scopus 로고
    • Role of copper in the proteosome-mediated degradation of the multicopper oxidase hephaestin
    • DOI 10.1074/jbc.M401151200
    • Nittis, T., and Gitlin, J. D. (2004) Role of copper in the proteosome-mediated degradation of the multicopper oxidase hephaestin. J. Biol. Chem. 279, 25696-25702 (Pubitemid 38756833)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.24 , pp. 25696-25702
    • Nittis, T.1    Gitlin, J.D.2
  • 31
    • 18144405022 scopus 로고    scopus 로고
    • Rat brain iron concentration is lower following perinatal copper deficiency
    • DOI 10.1111/j.1471-4159.2005.03091.x
    • Prohaska, J. R., and Gybina, A. A. (2005) Rat brain iron concentration is lower following perinatal copper deficiency. J. Neurochem. 93, 698-705 (Pubitemid 40617629)
    • (2005) Journal of Neurochemistry , vol.93 , Issue.3 , pp. 698-705
    • Prohaska, J.R.1    Gybina, A.A.2
  • 32
    • 0034733635 scopus 로고    scopus 로고
    • A novel mammalian iron-regulated protein involved in intracellular iron metabolism
    • DOI 10.1074/jbc.M000713200
    • Abboud, S., and Haile, D. J. (2000) A novel mammalian iron-regulated protein involved in intracellular iron metabolism. J. Biol. Chem. 275, 19906-19912 (Pubitemid 30441595)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.26 , pp. 19906-19912
    • Abboud, S.1    Haile, D.J.2
  • 33
    • 38549133531 scopus 로고    scopus 로고
    • The family of iron responsive RNA structures regulated by changes in cellular iron and oxygen
    • DOI 10.1007/s00018-007-7198-4
    • Leipuviene, R., and Theil, E. (2007) The family of iron responsive RNA structures regulated by changes in cellular iron and oxygen. Cell Mol. Life Sci. 64, 2945-2955 (Pubitemid 351152243)
    • (2007) Cellular and Molecular Life Sciences , vol.64 , Issue.22 , pp. 2945-2955
    • Leipuviene, R.1    Theil, E.C.2
  • 36
    • 0034635402 scopus 로고    scopus 로고
    • Alternative rna splicing generates a glycosylphosphatidylinositol- anchored form of ceruloplasmin in mammalian brain
    • DOI 10.1074/jbc.275.6.4305
    • Patel, B. N., Dunn, R. J., and David, S. (2000) Alternative RNA splicing generates a glycosylphosphatidylinositol-anchored form of ceruloplasmin in mammalian brain. J. Biol. Chem. 275, 4305-4310 (Pubitemid 30094671)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.6 , pp. 4305-4310
    • Patel, B.N.1    Dunn, R.J.2    David, S.3
  • 37
    • 33750709690 scopus 로고    scopus 로고
    • Brain Iron Metabolism
    • DOI 10.1016/j.spen.2006.08.002, PII S107190910600101X
    • Rouault, T. A., and Cooperman, S. (2006) Brain iron metabolism. Semin. Pediatr. Neurol. 13, 142-148 (Pubitemid 44709651)
    • (2006) Seminars in Pediatric Neurology , vol.13 , Issue.3 , pp. 142-148
    • Rouault, T.A.1    Cooperman, S.2
  • 38
    • 34848815312 scopus 로고    scopus 로고
    • The pivotal role of astrocytes in the metabolism of iron in the brain
    • DOI 10.1007/s11064-007-9375-0
    • Dringen, R., Bishop, G. M., Koeppe, M., Dang, T. N., and Robinson, S. R. (2007) The pivotal role of astrocytes in the metabolism of iron in the brain. Neurochem. Res. 32, 1884-1890 (Pubitemid 47497889)
    • (2007) Neurochemical Research , vol.32 , Issue.11 , pp. 1884-1890
    • Dringen, R.1    Bishop, G.M.2    Koeppe, M.3    Dang, T.N.4    Robinson, S.R.5
  • 40
    • 0029800745 scopus 로고    scopus 로고
    • Expression of the ceruloplasmin gene in the human retina and brain: Implications for a pathogenic model in aceruloplasminemia
    • Klomp, L. W., and Gitlin, J. D. (1996) Expression of the ceruloplasmin gene in the human retina and brain: Implications for a pathogenic model in Aceruloplasminemia. Hum. Mol. Genet. 5, 1989-1996 (Pubitemid 26413644)
    • (1996) Human Molecular Genetics , vol.5 , Issue.12 , pp. 1989-1996
    • Klomp, L.W.J.1    Gitlin, J.D.2


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