메뉴 건너뛰기




Volumn 1840, Issue 10, 2014, Pages 3138-3144

Hypoxia controls iron metabolism and glutamate secretion in retinal pigmented epithelial cells

Author keywords

Blood ocular barriers; Glutamate; Hypoxia; Iron transport

Indexed keywords

GLUTAMIC ACID; IRON 59; TRANSFERRIN;

EID: 84907863413     PISSN: 03044165     EISSN: 18728006     Source Type: Journal    
DOI: 10.1016/j.bbagen.2014.06.012     Document Type: Article
Times cited : (12)

References (35)
  • 1
    • 0026561842 scopus 로고
    • Does the lens serve as a 'sink' for iron during ocular inflammation?
    • M.C. McGahan Does the lens serve as a 'sink' for iron during ocular inflammation? Exp. Eye Res. 54 1992 525 530
    • (1992) Exp. Eye Res. , vol.54 , pp. 525-530
    • McGahan, M.C.1
  • 2
    • 0022451765 scopus 로고
    • A micromethod for the determination of iron and total iron-binding capacity in intraocular fluids and plasma using electrothermal atomic absorption spectroscopy
    • M.C. McGahan, and L.N. Fleisher A micromethod for the determination of iron and total iron-binding capacity in intraocular fluids and plasma using electrothermal atomic absorption spectroscopy Anal. Biochem. 156 1986 397 402
    • (1986) Anal. Biochem. , vol.156 , pp. 397-402
    • McGahan, M.C.1    Fleisher, L.N.2
  • 4
    • 0034536030 scopus 로고    scopus 로고
    • Distribution of ferritin and redox-active transition metals in normal and cataractous human lenses
    • B. Garner, K. Roberg, M. Qian, J.W. Eaton, and R.J. Truscott Distribution of ferritin and redox-active transition metals in normal and cataractous human lenses Exp. Eye Res. 71 2000 599 607
    • (2000) Exp. Eye Res. , vol.71 , pp. 599-607
    • Garner, B.1    Roberg, K.2    Qian, M.3    Eaton, J.W.4    Truscott, R.J.5
  • 5
    • 0028224873 scopus 로고
    • Transferrin inhibits the ocular inflammatory response
    • M.C. McGahan, A.M. Grimes, and L.N. Fleisher Transferrin inhibits the ocular inflammatory response Exp. Eye Res. 58 1994 509 511
    • (1994) Exp. Eye Res. , vol.58 , pp. 509-511
    • McGahan, M.C.1    Grimes, A.M.2    Fleisher, L.N.3
  • 6
    • 84883495401 scopus 로고    scopus 로고
    • Retinal iron homeostasis in health and disease
    • D. Song, and J.L. Dunaief Retinal iron homeostasis in health and disease Front. Aging Neurosci. 5 2013 1 13
    • (2013) Front. Aging Neurosci. , vol.5 , pp. 1-13
    • Song, D.1    Dunaief, J.L.2
  • 7
    • 4644293303 scopus 로고    scopus 로고
    • Disruption of ceruloplasmin and hephaestin in mice causes retinal iron overload and retinal degeneration with features of age-related macular degeneration
    • P. Hahn, Y. Qian, T. Dentchev, L. Chen, J. Beard, and Z.L. Harris et al. Disruption of ceruloplasmin and hephaestin in mice causes retinal iron overload and retinal degeneration with features of age-related macular degeneration Proc. Natl. Acad. Sci. U. S. A. 101 2004 13850 13855
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 13850-13855
    • Hahn, P.1    Qian, Y.2    Dentchev, T.3    Chen, L.4    Beard, J.5    Harris, Z.L.6
  • 8
    • 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
  • 10
    • 0034733635 scopus 로고    scopus 로고
    • A novel mammalian iron-regulated protein involved in intracellular iron metabolism
    • S. Abboud, and D.J. Haile A novel mammalian iron-regulated protein involved in intracellular iron metabolism J. Biol. Chem. 275 2000 19906 19912
    • (2000) J. Biol. Chem. , vol.275 , pp. 19906-19912
    • Abboud, S.1    Haile, D.J.2
  • 11
    • 0242521527 scopus 로고    scopus 로고
    • The role of the iron responsive element in the control of ferroportin1/IREG1/MTP1 gene expression
    • A. Lymboussaki, E. Pignatti, G. Montosi, C. Garuti, D.J. Haile, and A. Pietrangelo The role of the iron responsive element in the control of ferroportin1/IREG1/MTP1 gene expression J. Hepatol. 39 2003 710 715
    • (2003) J. Hepatol. , vol.39 , pp. 710-715
    • Lymboussaki, A.1    Pignatti, E.2    Montosi, G.3    Garuti, C.4    Haile, D.J.5    Pietrangelo, A.6
  • 13
    • 10844258104 scopus 로고    scopus 로고
    • Hepcidin regulates cellular iron efflux by binding to ferroportin and inducing its internalization
    • E. Nemeth, M.S. Tuttle, J. Powelson, M.B. Vaughn, A. Donovan, and D.M. Ward et al. Hepcidin regulates cellular iron efflux by binding to ferroportin and inducing its internalization Science 306 2004 2090 2093
    • (2004) Science , vol.306 , pp. 2090-2093
    • Nemeth, E.1    Tuttle, M.S.2    Powelson, J.3    Vaughn, M.B.4    Donovan, A.5    Ward, D.M.6
  • 15
    • 34250800318 scopus 로고    scopus 로고
    • Ferroxidase activity is required for the stability of cell surface ferroportin in cells expressing GPI-ceruloplasmin
    • I. De Domenico, D.M. Ward, M.C. di Patti, S.Y. Jeong, S. David, and G. Musci et al. Ferroxidase activity is required for the stability of cell surface ferroportin in cells expressing GPI-ceruloplasmin EMBO J. 26 2007 2823 2831
    • (2007) EMBO J. , vol.26 , pp. 2823-2831
    • De Domenico, I.1    Ward, D.M.2    Di Patti, M.C.3    Jeong, S.Y.4    David, S.5    Musci, G.6
  • 16
    • 79951679054 scopus 로고    scopus 로고
    • Regulation of iron pathways in response to hypoxia
    • N.L. Chepelev, and W.G. Willmore Regulation of iron pathways in response to hypoxia Free Radic. Biol. Med. 50 2011 645 666
    • (2011) Free Radic. Biol. Med. , vol.50 , pp. 645-666
    • Chepelev, N.L.1    Willmore, W.G.2
  • 17
    • 0035917313 scopus 로고    scopus 로고
    • HIFα ταργεted for VHL-mediated destruction by proline hydroxylation: Implications for O2 sensing
    • M. Ivan, K. Kondo, H. Yang, W. Kim, J. Valiando, and M. Ohh et al. HIFα ταργεted for VHL-mediated destruction by proline hydroxylation: implications for O2 sensing Science 292 2001 464 468
    • (2001) Science , vol.292 , pp. 464-468
    • Ivan, M.1    Kondo, K.2    Yang, H.3    Kim, W.4    Valiando, J.5    Ohh, M.6
  • 18
    • 0035917808 scopus 로고    scopus 로고
    • Targeting of HIF-α to the von Hippel-Lindau ubiquitylation complex by O2-regulated prolyl hydroxylation
    • P. Jaakkola, D.R. Mole, Y.-M. Tian, M.I. Wilson, J. Gielbert, and S.J. Gaskell et al. Targeting of HIF-α to the von Hippel-Lindau ubiquitylation complex by O2-regulated prolyl hydroxylation Science 292 2001 468 472
    • (2001) Science , vol.292 , pp. 468-472
    • Jaakkola, P.1    Mole, D.R.2    Tian, Y.-M.3    Wilson, M.I.4    Gielbert, J.5    Gaskell, S.J.6
  • 19
    • 40949126440 scopus 로고    scopus 로고
    • Mitochondrial complex III regulates hypoxic activation of HIF
    • T. Klimova, and N.S. Chandel Mitochondrial complex III regulates hypoxic activation of HIF Cell Death Differ. 15 2008 660 666
    • (2008) Cell Death Differ. , vol.15 , pp. 660-666
    • Klimova, T.1    Chandel, N.S.2
  • 20
    • 84888112364 scopus 로고    scopus 로고
    • Source-dependent intracellular distribution of iron in lens epithelial cells cultured under normoxic and hypoxic conditions
    • M. Goralska, S. Nagar, L.N. Fleisher, P. Mzyk, and M.C. McGahan Source-dependent intracellular distribution of iron in lens epithelial cells cultured under normoxic and hypoxic conditions Invest. Ophthalmol. Vis. Sci. 54 2013 7666 7673
    • (2013) Invest. Ophthalmol. Vis. Sci. , vol.54 , pp. 7666-7673
    • Goralska, M.1    Nagar, S.2    Fleisher, L.N.3    Mzyk, P.4    McGahan, M.C.5
  • 21
    • 70350365391 scopus 로고    scopus 로고
    • Inhibition of prolyl hydroxylase protects against 1-methyl-4-phenyl-1,2, 3,6-tetrahydropyridine-induced neurotoxicity: Model for the potential involvement of the hypoxia-inducible factor pathway in Parkinson Disease
    • D.W. Lee, S. Rajagopalan, A. Siddiq, R. Gwiazda, L. Yang, and M.F. Beal et al. Inhibition of prolyl hydroxylase protects against 1-methyl-4-phenyl-1,2, 3,6-tetrahydropyridine-induced neurotoxicity: model for the potential involvement of the hypoxia-inducible factor pathway in Parkinson Disease J. Biol. Chem. 284 2009 29065 29076
    • (2009) J. Biol. Chem. , vol.284 , pp. 29065-29076
    • Lee, D.W.1    Rajagopalan, S.2    Siddiq, A.3    Gwiazda, R.4    Yang, L.5    Beal, M.F.6
  • 22
    • 78751598932 scopus 로고    scopus 로고
    • Regulation of type II transmembrane serine proteinase TMPRSS6 by hypoxia-inducible factors: New link between hypoxia signaling and iron homeostasis
    • S. Lakhal, J. Schodel, A.R.M. Townsend, C.W. Pugh, P.J. Ratcliffe, and D.R. Mole Regulation of type II transmembrane serine proteinase TMPRSS6 by hypoxia-inducible factors: new link between hypoxia signaling and iron homeostasis J. Biol. Chem. 286 2011 4090 4097
    • (2011) J. Biol. Chem. , vol.286 , pp. 4090-4097
    • Lakhal, S.1    Schodel, J.2    Townsend, A.R.M.3    Pugh, C.W.4    Ratcliffe, P.J.5    Mole, D.R.6
  • 24
    • 39549114487 scopus 로고    scopus 로고
    • Iron regulates L-glutamate secretion, Xc- activity and glutathione levels in lens epithelial and retinal pigment epithelial cells by its effect on cytosolic aconitase
    • M.M. Lall, J.B. Ferrell, S. Nagar, L.N. Fleisher, and M.C. McGahan Iron regulates L-glutamate secretion, Xc- activity and glutathione levels in lens epithelial and retinal pigment epithelial cells by its effect on cytosolic aconitase Invest. Ophthalmol. Vis. Sci. 49 2008 310 319
    • (2008) Invest. Ophthalmol. Vis. Sci. , vol.49 , pp. 310-319
    • Lall, M.M.1    Ferrell, J.B.2    Nagar, S.3    Fleisher, L.N.4    McGahan, M.C.5
  • 25
    • 0024643741 scopus 로고
    • Transferrin receptors on the surfaces of retinal pigment epithelial cells are associated with the cytoskeleton
    • R.C. Hunt, A. Dewey, and A.A. Davis Transferrin receptors on the surfaces of retinal pigment epithelial cells are associated with the cytoskeleton J. Cell Sci. 92 1989 655 666
    • (1989) J. Cell Sci. , vol.92 , pp. 655-666
    • Hunt, R.C.1    Dewey, A.2    Davis, A.A.3
  • 27
    • 84857134714 scopus 로고    scopus 로고
    • Effects of hypoxic preconditioning on the expression of iron influx and efflux proteins in primary neuron culture
    • F. Du, M. Fan, Q. Gong, Z.J. Zhu, L.L. Zhu, and L. Lu et al. Effects of hypoxic preconditioning on the expression of iron influx and efflux proteins in primary neuron culture Neurochem. Int. 60 2012 335 343
    • (2012) Neurochem. Int. , vol.60 , pp. 335-343
    • Du, F.1    Fan, M.2    Gong, Q.3    Zhu, Z.J.4    Zhu, L.L.5    Lu, L.6
  • 28
    • 84862808520 scopus 로고
    • Hypoxic preconditioning increases iron transport rate in astrocytes
    • L. Yang, M. Fan, F. Du, Q. Gong, Z.G. Bi, and Z.J. Zhu et al. Hypoxic preconditioning increases iron transport rate in astrocytes Biochim. Biophys. Acta 2012 1822 500 508
    • (1822) Biochim. Biophys. Acta , vol.2012 , pp. 500-508
    • Yang, L.1    Fan, M.2    Du, F.3    Gong, Q.4    Bi, Z.G.5    Zhu, Z.J.6
  • 29
    • 7044247550 scopus 로고    scopus 로고
    • Immunolocalization and regulation of iron handling proteins ferritin and ferroportin in the retina
    • P. Hahn, T. Dentchev, Y. Qian, T. Rouault, Z.L. Harris, and J.L. Dunaief Immunolocalization and regulation of iron handling proteins ferritin and ferroportin in the retina Mol. Vis. 10 2004 598 607
    • (2004) Mol. Vis. , vol.10 , pp. 598-607
    • Hahn, P.1    Dentchev, T.2    Qian, Y.3    Rouault, T.4    Harris, Z.L.5    Dunaief, J.L.6
  • 30
    • 0036791486 scopus 로고    scopus 로고
    • The gene encoding the iron regulatory peptide hepcidin is regulated by anemia, hypoxia and inflammation
    • G. Nicholas, C. Chauvet, L. Viatte, J.L. Danan, X. Bigard, and I. Devaux et al. The gene encoding the iron regulatory peptide hepcidin is regulated by anemia, hypoxia and inflammation J. Clin. Invest. 110 2002 1037 1044
    • (2002) J. Clin. Invest. , vol.110 , pp. 1037-1044
    • Nicholas, G.1    Chauvet, C.2    Viatte, L.3    Danan, J.L.4    Bigard, X.5    Devaux, I.6
  • 31
    • 84869014083 scopus 로고    scopus 로고
    • Hypoxia-induced oxidative stress in ischemic retinopathy
    • Article ID 426769, 10 pages
    • S.Y. Li, Z.J. Fu, and A.C.Y. Lo Hypoxia-induced oxidative stress in ischemic retinopathy Oxidative Med. Cell. Longev. 2012 Article ID 426769, 10 pages
    • (2012) Oxidative Med. Cell. Longev.
    • Li, S.Y.1    Fu, Z.J.2    Lo, A.C.Y.3
  • 33
    • 76349095132 scopus 로고    scopus 로고
    • Defining the role of hypoxia-inducible factor 1 in cancer biology and therapeutics
    • G.L. Semenza Defining the role of hypoxia-inducible factor 1 in cancer biology and therapeutics Oncogene 29 2010 625 634
    • (2010) Oncogene , vol.29 , pp. 625-634
    • Semenza, G.L.1
  • 34
    • 84856739946 scopus 로고    scopus 로고
    • Hypoxia-inducible factors in physiology and medicine
    • G.L. Semenza Hypoxia-inducible factors in physiology and medicine Cell Death Differ. 148 2012 399 408
    • (2012) Cell Death Differ. , vol.148 , pp. 399-408
    • Semenza, G.L.1
  • 35
    • 84925711068 scopus 로고    scopus 로고
    • Brain to blood glutamate scavenging as a novel therapeutic modality: A review
    • 10.1007/s00702-014-1181-7 (e-pub ahead of print)
    • M. Boyko, S.E. Gruenbaum, B.F. Gruenbaum, Y. Shapira, and A. Zlotnik Brain to blood glutamate scavenging as a novel therapeutic modality: a review J. Neural Transm. 2014 10.1007/s00702-014-1181-7 (e-pub ahead of print)
    • (2014) J. Neural Transm.
    • Boyko, M.1    Gruenbaum, S.E.2    Gruenbaum, B.F.3    Shapira, Y.4    Zlotnik, A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.