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Volumn 18, Issue 2, 2007, Pages 401-406

Renal iron metabolism: Transferrin iron delivery and the role of iron regulatory proteins

Author keywords

[No Author keywords available]

Indexed keywords

IRON; IRON REGULATORY FACTOR; IRON REGULATORY PROTEIN 1; IRON REGULATORY PROTEIN 2; MESSENGER RNA; TRANSFERRIN; TRANSFERRIN RECEPTOR;

EID: 33846706460     PISSN: 10466673     EISSN: None     Source Type: Journal    
DOI: 10.1681/ASN.2006080908     Document Type: Review
Times cited : (87)

References (52)
  • 1
    • 29144450958 scopus 로고    scopus 로고
    • Divalent metal transporter 1
    • Mims MP, Prchal JT: Divalent metal transporter 1. Hematology 10: 339-345, 2005
    • (2005) Hematology , vol.10 , pp. 339-345
    • Mims, M.P.1    Prchal, J.T.2
  • 4
    • 33644792074 scopus 로고    scopus 로고
    • Iron imports. III. Transfer of iron from the mucosa into circulation
    • Wessling-Resnick M: Iron imports. III. Transfer of iron from the mucosa into circulation. Am J Physiol Gastrointest Liver Physiol 290: G1-G6, 2006
    • (2006) Am J Physiol Gastrointest Liver Physiol , vol.290
    • Wessling-Resnick, M.1
  • 5
    • 0031605219 scopus 로고    scopus 로고
    • Transferrin, the transferrin receptor, and the uptake of iron by cells
    • Aisen P: Transferrin, the transferrin receptor, and the uptake of iron by cells. Met Ions Biol Syst 35: 585-631, 1998
    • (1998) Met Ions Biol Syst , vol.35 , pp. 585-631
    • Aisen, P.1
  • 6
    • 0030608152 scopus 로고    scopus 로고
    • The ferritins: Molecular properties, iron storage function and cellular regulation
    • Harrison PM, Arosio P: The ferritins: Molecular properties, iron storage function and cellular regulation. Biochim Biophys Acta 1275: 161-203, 1996
    • (1996) Biochim Biophys Acta , vol.1275 , pp. 161-203
    • Harrison, P.M.1    Arosio, P.2
  • 8
    • 0035954391 scopus 로고    scopus 로고
    • Opening the ferritin pore for iron release by mutation of conserved amino acids at interhelix and loop sites
    • Jin W, Takagi H, Pancorbo B, Theil EC: "Opening" the ferritin pore for iron release by mutation of conserved amino acids at interhelix and loop sites. Biochemistry 40: 7525-7532, 2001
    • (2001) Biochemistry , vol.40 , pp. 7525-7532
    • Jin, W.1    Takagi, H.2    Pancorbo, B.3    Theil, E.C.4
  • 9
    • 4143051431 scopus 로고    scopus 로고
    • Transferrin receptor 1
    • Aisen P: Transferrin receptor 1. Int J Biochem Cell Biol 36: 2137-2143, 2004
    • (2004) Int J Biochem Cell Biol , vol.36 , pp. 2137-2143
    • Aisen, P.1
  • 12
    • 0026476257 scopus 로고
    • Transferrin (TF) typing from semen stains using isoelectric focusing and immunoblotting: Correlation of TF types among blood, semen, urine, and vaginal secretion
    • Sawazaki K, Yasuda T, Nadano D, Iida R, Kishi K: Transferrin (TF) typing from semen stains using isoelectric focusing and immunoblotting: correlation of TF types among blood, semen, urine, and vaginal secretion. J Forensic Sci 37: 1514-1524, 1992
    • (1992) J Forensic Sci , vol.37 , pp. 1514-1524
    • Sawazaki, K.1    Yasuda, T.2    Nadano, D.3    Iida, R.4    Kishi, K.5
  • 14
    • 0003179404 scopus 로고
    • Iron metabolism: An evolutionary perspective
    • edited by Brock JH, Halliday, Pippard MJ, Powell LW, Philadelphia, W.B. Saunders
    • Aisen P: Iron metabolism: An evolutionary perspective. In: Iron Metabolism in Health and Disease, edited by Brock JH, Halliday, Pippard MJ, Powell LW, Philadelphia, W.B. Saunders, 1994, pp 1-30
    • (1994) Iron Metabolism in Health and Disease , pp. 1-30
    • Aisen, P.1
  • 16
    • 0036310725 scopus 로고    scopus 로고
    • Expression of the iron transporter DMT1 in kidney from normal and anemic mk mice
    • Canonne-Hergaux F, Gros P: Expression of the iron transporter DMT1 in kidney from normal and anemic mk mice. Kidney Int 62: 147-156, 2002
    • (2002) Kidney Int , vol.62 , pp. 147-156
    • Canonne-Hergaux, F.1    Gros, P.2
  • 19
    • 33744812973 scopus 로고    scopus 로고
    • Divalent metal transporter 1 in the kidney proximal tubule is expressed in late endosomes/lysosomal membranes: Implications for renal handling of protein-metal complexes
    • Abouhamed M, Gburek J, Liu W, Torchalski B, Wilhelm A, Wolff NA, Christensen EI, Thevenod F, Smith CP: Divalent metal transporter 1 in the kidney proximal tubule is expressed in late endosomes/lysosomal membranes: Implications for renal handling of protein-metal complexes. Am J Physiol Renal Physiol 290: F1525-F1533, 2006
    • (2006) Am J Physiol Renal Physiol , vol.290
    • Abouhamed, M.1    Gburek, J.2    Liu, W.3    Torchalski, B.4    Wilhelm, A.5    Wolff, N.A.6    Christensen, E.I.7    Thevenod, F.8    Smith, C.P.9
  • 20
    • 0024953316 scopus 로고
    • Transferrin receptor expression in normal, iron-deficient and iron-overloaded rats
    • Lu JP, Hayashi K, Awai M: Transferrin receptor expression in normal, iron-deficient and iron-overloaded rats. Acta Pathol Jpn 39: 759-764, 1989
    • (1989) Acta Pathol Jpn , vol.39 , pp. 759-764
    • Lu, J.P.1    Hayashi, K.2    Awai, M.3
  • 21
    • 0020597630 scopus 로고
    • Transferrin receptors in human tissues: Their distribution and possible clinical relevance
    • Gatter KC, Brown G, Trowbridge B, Woolston RE, Mason DY: Transferrin receptors in human tissues: Their distribution and possible clinical relevance. J Clin Pathol 36: 539-545, 1983
    • (1983) J Clin Pathol , vol.36 , pp. 539-545
    • Gatter, K.C.1    Brown, G.2    Trowbridge, B.3    Woolston, R.E.4    Mason, D.Y.5
  • 22
    • 0020598381 scopus 로고
    • Transferrin as a fetal growth factor: Acquisition of responsiveness related to embryonic induction
    • Ekblom P, Thesleff I, Saxen L, Miettinen A, Timpl R: Transferrin as a fetal growth factor: Acquisition of responsiveness related to embryonic induction. Proc Natl Acad Sci U S A 80: 2651-2655, 1983
    • (1983) Proc Natl Acad Sci U S A , vol.80 , pp. 2651-2655
    • Ekblom, P.1    Thesleff, I.2    Saxen, L.3    Miettinen, A.4    Timpl, R.5
  • 23
    • 0030905888 scopus 로고    scopus 로고
    • Structural requirements for basolateral sorting of the human transferrin receptor in the biosynthetic and endocytic pathways of Madin-Darby canine kidney cells
    • Odorizzi G, Trowbridge IS: Structural requirements for basolateral sorting of the human transferrin receptor in the biosynthetic and endocytic pathways of Madin-Darby canine kidney cells. J Cell Biol 137: 1255-1264, 1997
    • (1997) J Cell Biol , vol.137 , pp. 1255-1264
    • Odorizzi, G.1    Trowbridge, I.S.2
  • 24
    • 0030660482 scopus 로고    scopus 로고
    • Structure and dynamics of the iron responsive element RNA: Implications for binding of the RNA by iron regulatory proteins
    • Addess KJ, Basilion JP, Klausner RD, Rouault TA, Pardi AJ: Structure and dynamics of the iron responsive element RNA: Implications for binding of the RNA by iron regulatory proteins. J Mol Biol 274: 72-83, 1997
    • (1997) J Mol Biol , vol.274 , pp. 72-83
    • Addess, K.J.1    Basilion, J.P.2    Klausner, R.D.3    Rouault, T.A.4    Pardi, A.J.5
  • 25
    • 0032501997 scopus 로고    scopus 로고
    • Iron regulatory element and internal loop/bulge structure for ferritin mRNA studied by cobalt(III) hexamine binding, molecular modeling, and NMR spectroscopy
    • Gdaniec Z, Sierzputowska-Gracz H, Theil EC: Iron regulatory element and internal loop/bulge structure for ferritin mRNA studied by cobalt(III) hexamine binding, molecular modeling, and NMR spectroscopy. Biochemistry 37: 1505-1512, 1998
    • (1998) Biochemistry , vol.37 , pp. 1505-1512
    • Gdaniec, Z.1    Sierzputowska-Gracz, H.2    Theil, E.C.3
  • 27
    • 2042546096 scopus 로고    scopus 로고
    • Balancing acts: Molecular control of mammalian iron metabolism
    • Hentze MW, Muckenthaler MU, Andrews NC: Balancing acts: Molecular control of mammalian iron metabolism. Cell 117: 285-297, 2004
    • (2004) Cell , vol.117 , pp. 285-297
    • Hentze, M.W.1    Muckenthaler, M.U.2    Andrews, N.C.3
  • 28
    • 33746361251 scopus 로고    scopus 로고
    • The role of iron regulatory proteins in mammalian iron homeostasis and disease
    • Rouault TA: The role of iron regulatory proteins in mammalian iron homeostasis and disease. Nat Chem Biol 2: 406-414, 2006
    • (2006) Nat Chem Biol , vol.2 , pp. 406-414
    • Rouault, T.A.1
  • 29
    • 17144378216 scopus 로고    scopus 로고
    • Opinion: Iron-sulphur cluster biogenesis and mitochondrial iron homeostasis
    • Rouault TA, Tong WH: Opinion: Iron-sulphur cluster biogenesis and mitochondrial iron homeostasis. Nat Rev Mol Cell Biol 6: 345-351, 2005
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 345-351
    • Rouault, T.A.1    Tong, W.H.2
  • 30
    • 14244254585 scopus 로고    scopus 로고
    • Down-regulation of iron regulatory protein 1 activities and expression in superoxide dismutase 1 knock-out mice is not associated with alterations in iron metabolism
    • Starzynski RR, Lipinski P, Drapier JC, Diet A, Smuda E, Bartlomiejczyk T, Gralak MA, Kruszewski M: Down-regulation of iron regulatory protein 1 activities and expression in superoxide dismutase 1 knock-out mice is not associated with alterations in iron metabolism. J Biol Chem 280: 4207-4212, 2005
    • (2005) J Biol Chem , vol.280 , pp. 4207-4212
    • Starzynski, R.R.1    Lipinski, P.2    Drapier, J.C.3    Diet, A.4    Smuda, E.5    Bartlomiejczyk, T.6    Gralak, M.A.7    Kruszewski, M.8
  • 32
    • 0028266818 scopus 로고
    • Evidence that the pathway of transferrin receptor mRNA degradation involves an endonucleolytic cleavage within the 3′UTR and does not involve poly(A) tail shortening
    • Binder R, Horowitz JA, Basilion JP, Koeller DM, Klausner RD, Harford JB: Evidence that the pathway of transferrin receptor mRNA degradation involves an endonucleolytic cleavage within the 3′UTR and does not involve poly(A) tail shortening. EMBO J 13: 1969-1980, 1994
    • (1994) EMBO J , vol.13 , pp. 1969-1980
    • Binder, R.1    Horowitz, J.A.2    Basilion, J.P.3    Koeller, D.M.4    Klausner, R.D.5    Harford, J.B.6
  • 34
    • 23044503950 scopus 로고    scopus 로고
    • Microcytic anemia, erythropoietic protoporphyria, and neurodegeneration in mice with targeted deletion of iron-regulatory protein 2
    • Cooperman SS, Meyron-Holtz EG, Olivierre-Wilson H, Ghosh MC, McConnell JP, Rouault TA: Microcytic anemia, erythropoietic protoporphyria, and neurodegeneration in mice with targeted deletion of iron-regulatory protein 2. Blood 106: 1084-1091, 2005
    • (2005) Blood , vol.106 , pp. 1084-1091
    • Cooperman, S.S.1    Meyron-Holtz, E.G.2    Olivierre-Wilson, H.3    Ghosh, M.C.4    McConnell, J.P.5    Rouault, T.A.6
  • 35
  • 37
    • 33749418694 scopus 로고    scopus 로고
    • Mesenchymal cells from adult kidney support angiogenesis and differentiate into multiple interstitial cell types including erythropoietin-producing fibroblasts
    • Plotkin M, Goligorsky MS: Mesenchymal cells from adult kidney support angiogenesis and differentiate into multiple interstitial cell types including erythropoietin-producing fibroblasts. Am J Physiol Renal Physiol 291: F902-F912, 2006
    • (2006) Am J Physiol Renal Physiol , vol.291
    • Plotkin, M.1    Goligorsky, M.S.2
  • 38
    • 0027410945 scopus 로고
    • Co-localization of erythropoietin mRNA and ecto-5′-nucleotidase immunoreactivity in peritubular cells of rat renal cortex indicates that fibroblasts produce erythropoietin
    • Bachmann S, Le Hir M, Eckardt KU: Co-localization of erythropoietin mRNA and ecto-5′-nucleotidase immunoreactivity in peritubular cells of rat renal cortex indicates that fibroblasts produce erythropoietin. J Histochem Cytochem 41: 335-341, 1993
    • (1993) J Histochem Cytochem , vol.41 , pp. 335-341
    • Bachmann, S.1    Le Hir, M.2    Eckardt, K.U.3
  • 40
    • 33746655373 scopus 로고    scopus 로고
    • Hypoxia-inducible factors in the kidney
    • Haase VH: Hypoxia-inducible factors in the kidney. Am J Physiol Renal Physiol 291: F271-F281, 2006
    • (2006) Am J Physiol Renal Physiol , vol.291
    • Haase, V.H.1
  • 41
    • 2542450917 scopus 로고    scopus 로고
    • HIF hydroxylation and cellular oxygen sensing
    • Metzen E, Ratcliffe PJ: HIF hydroxylation and cellular oxygen sensing. Biol Chem 385: 223-230, 2004
    • (2004) Biol Chem , vol.385 , pp. 223-230
    • Metzen, E.1    Ratcliffe, P.J.2
  • 42
    • 0000655498 scopus 로고    scopus 로고
    • Identification of a hypoxia response element in the transferrin receptor gene
    • Lok CN, Ponka P: Identification of a hypoxia response element in the transferrin receptor gene. J Biol Chem 274: 24147-24152, 1999
    • (1999) J Biol Chem , vol.274 , pp. 24147-24152
    • Lok, C.N.1    Ponka, P.2
  • 43
    • 0033588021 scopus 로고    scopus 로고
    • Transferrin receptor induction by hypoxia. HIF-1-mediated transcriptional activation and cell-specific post-transcriptional regulation
    • Tacchini L, Bianchi L, Bernelli-Zazzera A, Cairo G: Transferrin receptor induction by hypoxia. HIF-1-mediated transcriptional activation and cell-specific post-transcriptional regulation. J Biol Chem 274: 24142-24146, 1999
    • (1999) J Biol Chem , vol.274 , pp. 24142-24146
    • Tacchini, L.1    Bianchi, L.2    Bernelli-Zazzera, A.3    Cairo, G.4
  • 44
    • 0030792094 scopus 로고    scopus 로고
    • Oxygen-regulated transferrin expression is mediated by hypoxia-inducible factor-1
    • Rolfs A, Kvietikova I, Gassmann M, Wenger RH: Oxygen-regulated transferrin expression is mediated by hypoxia-inducible factor-1. J Biol Chem 272: 20055-20062, 1997
    • (1997) J Biol Chem , vol.272 , pp. 20055-20062
    • Rolfs, A.1    Kvietikova, I.2    Gassmann, M.3    Wenger, R.H.4
  • 45
    • 10844282789 scopus 로고    scopus 로고
    • Mammalian tissue oxygen levels modulate iron-regulatory protein activities in vivo
    • Meyron-Holtz EG, Ghosh MC, Rouault TA: Mammalian tissue oxygen levels modulate iron-regulatory protein activities in vivo. Science 306: 2087-2090, 2004
    • (2004) Science , vol.306 , pp. 2087-2090
    • Meyron-Holtz, E.G.1    Ghosh, M.C.2    Rouault, T.A.3
  • 46
    • 0034682761 scopus 로고    scopus 로고
    • Overexpression of wild type and mutated human ferritin H-chain in HeLa cells: In vivo role of ferritin ferroxidase activity
    • Cozzi A, Corsi B, Levi S, Santambrogio P, Albertini A, Arosio P: Overexpression of wild type and mutated human ferritin H-chain in HeLa cells: In vivo role of ferritin ferroxidase activity. J Biol Chem 275: 25122-25129, 2000
    • (2000) J Biol Chem , vol.275 , pp. 25122-25129
    • Cozzi, A.1    Corsi, B.2    Levi, S.3    Santambrogio, P.4    Albertini, A.5    Arosio, P.6
  • 50
    • 0031046993 scopus 로고    scopus 로고
    • The rabbit kidney tubule simultaneously degrades and synthesizes glutamate. A 13C NMR study
    • Chauvin MF, Megnin-Chanet F, Martin G, Mispelter J, Baverel G: The rabbit kidney tubule simultaneously degrades and synthesizes glutamate. A 13C NMR study. J Biol Chem 272: 4705-4716, 1997
    • (1997) J Biol Chem , vol.272 , pp. 4705-4716
    • Chauvin, M.F.1    Megnin-Chanet, F.2    Martin, G.3    Mispelter, J.4    Baverel, G.5
  • 51
    • 24044554883 scopus 로고    scopus 로고
    • Loss of the von Hippel Lindau tumor suppressor disrupts iron homeostasis in renal carcinoma cells
    • Alberghini A, Recalcati S, Tacchini L, Santambrogio P, Campanella A, Cairo G: Loss of the von Hippel Lindau tumor suppressor disrupts iron homeostasis in renal carcinoma cells. J Biol Chem 280: 30120-30128, 2005
    • (2005) J Biol Chem , vol.280 , pp. 30120-30128
    • Alberghini, A.1    Recalcati, S.2    Tacchini, L.3    Santambrogio, P.4    Campanella, A.5    Cairo, G.6
  • 52
    • 0037354172 scopus 로고    scopus 로고
    • Prevention of free-radical mediated tissue damage and carcinogenesis induced by low-molecular-weight iron
    • Okada S: Prevention of free-radical mediated tissue damage and carcinogenesis induced by low-molecular-weight iron. Biometals 16: 99-101, 2003
    • (2003) Biometals , vol.16 , pp. 99-101
    • Okada, S.1


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