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Volumn 105, Issue 6, 2005, Pages 2564-2570

The hereditary hemochromatosis protein, HFE, lowers intracellular iron levels independently of transferrin receptor 1 in TRVb cells

Author keywords

[No Author keywords available]

Indexed keywords

FERRITIN; HEREDITARY HEMOCHROMATOSIS PROTEIN; MACROGLOBULIN; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 1; MONOCLONAL ANTIBODY; PROTEIN; TRANSFERRIN RECEPTOR; UNCLASSIFIED DRUG;

EID: 15244342393     PISSN: 00064971     EISSN: None     Source Type: Journal    
DOI: 10.1182/blood-2004-03-1204     Document Type: Article
Times cited : (23)

References (41)
  • 2
    • 0031984370 scopus 로고    scopus 로고
    • Hereditary hemochromatosis: Etiologic, pathologic, and clinical aspects
    • Bothwell TH, MacPhail AP. Hereditary hemochromatosis: etiologic, pathologic, and clinical aspects. Semin Hematol. 1998;35:55-71.
    • (1998) Semin Hematol , vol.35 , pp. 55-71
    • Bothwell, T.H.1    MacPhail, A.P.2
  • 3
    • 9344224529 scopus 로고    scopus 로고
    • A novel MHC class I-like gene is mutated in patients with hereditary haemochromatosis
    • Feder JN, Gnirke A, Thomas W, et al. A novel MHC class I-like gene is mutated in patients with hereditary haemochromatosis. Nat Genet. 1996;13:399-408.
    • (1996) Nat Genet , vol.13 , pp. 399-408
    • Feder, J.N.1    Gnirke, A.2    Thomas, W.3
  • 4
    • 17644434333 scopus 로고    scopus 로고
    • The hemochromatosis founder mutation in HLA-H disrupts β2-microglobulin interaction and cell surface expression
    • Feder JN, Tsuchihashi Z, Irrinki A, et al. The hemochromatosis founder mutation in HLA-H disrupts β2-microglobulin interaction and cell surface expression. J Biol Chem. 1997;272:14025-14028.
    • (1997) J Biol Chem , vol.272 , pp. 14025-14028
    • Feder, J.N.1    Tsuchihashi, Z.2    Irrinki, A.3
  • 5
    • 0001376313 scopus 로고    scopus 로고
    • HFE gene knockout produces mouse model of hereditary hemochromatosis
    • Zhou XY, Tomatsu S, Fleming RE, et al. HFE gene knockout produces mouse model of hereditary hemochromatosis. Proc Natl Acad Sci U S A. 1998;95:2492-2497.
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 2492-2497
    • Zhou, X.Y.1    Tomatsu, S.2    Fleming, R.E.3
  • 6
    • 0034062537 scopus 로고    scopus 로고
    • Genes that modify the hemochromatosis phenotype in mice
    • Levy JE, Montross LK, Andrews NC. Genes that modify the hemochromatosis phenotype in mice. J Clin Invest. 2000;105:1209-1216.
    • (2000) J Clin Invest , vol.105 , pp. 1209-1216
    • Levy, J.E.1    Montross, L.K.2    Andrews, N.C.3
  • 7
    • 13144282684 scopus 로고    scopus 로고
    • The hemochromatosis gene product complexes with the transferrin receptor and lowers its affinity for ligand binding
    • Feder JN, Penny DM, Irrinki A, et al. The hemochromatosis gene product complexes with the transferrin receptor and lowers its affinity for ligand binding. Proc Natl Acad Sci U S A. 1998;95: 1472-1477.
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 1472-1477
    • Feder, J.N.1    Penny, D.M.2    Irrinki, A.3
  • 8
    • 0032478524 scopus 로고    scopus 로고
    • Crystal structure of the hemochromatosis protein HFE and characterization of its interaction with transferrin receptor
    • Lebron JA, Bennett MJ, Vaughn DE, et al. Crystal structure of the hemochromatosis protein HFE and characterization of its interaction with transferrin receptor. Cell. 1998;93:111-123.
    • (1998) Cell , vol.93 , pp. 111-123
    • Lebron, J.A.1    Bennett, M.J.2    Vaughn, D.E.3
  • 9
    • 0034610781 scopus 로고    scopus 로고
    • Crystal structure of the hereditary haemochromatosis protein HFE complexed with transferrin receptor
    • Bennett MJ, Lebron JA, Bjorkman PJ. Crystal structure of the hereditary haemochromatosis protein HFE complexed with transferrin receptor. Nature. 2000;403:46-53.
    • (2000) Nature , vol.403 , pp. 46-53
    • Bennett, M.J.1    Lebron, J.A.2    Bjorkman, P.J.3
  • 10
    • 0033574075 scopus 로고    scopus 로고
    • Association of HFE protein with transferrin receptor in crypt enterocytes of human duodenum
    • Waheed A, Parkkila S, Saarnio J, et al. Association of HFE protein with transferrin receptor in crypt enterocytes of human duodenum. Proc Natl Acad Sci U S A. 1999;96:1579-1584.
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 1579-1584
    • Waheed, A.1    Parkkila, S.2    Saarnio, J.3
  • 11
    • 0033585129 scopus 로고    scopus 로고
    • The hemochromatosis protein HFE competes with transferrin for binding to the transferrin receptor
    • Lebron JA, West AP Jr, Bjorkman PJ. The hemochromatosis protein HFE competes with transferrin for binding to the transferrin receptor. J Mol Biol. 1999;294:239-245.
    • (1999) J Mol Biol , vol.294 , pp. 239-245
    • Lebron, J.A.1    West Jr., A.P.2    Bjorkman, P.J.3
  • 12
    • 0035914480 scopus 로고    scopus 로고
    • Mutational analysis of the transferrin receptor reveals overlapping HFE and transferrin binding sites
    • West AP Jr, Giannetti AM, Herr AB, et al. Mutational analysis of the transferrin receptor reveals overlapping HFE and transferrin binding sites. J Mol Biol. 2001;313:385-397.
    • (2001) J Mol Biol , vol.313 , pp. 385-397
    • West Jr., A.P.1    Giannetti, A.M.2    Herr, A.B.3
  • 13
    • 2442657217 scopus 로고    scopus 로고
    • Mechanism for multiple ligand recognition by the human transferrin receptor
    • Giannetti AM, Snow PM, Zak O, Bjorkman PJ. Mechanism for multiple ligand recognition by the human transferrin receptor. PLoS Biol. 2003;1:341-350.
    • (2003) PLoS Biol , vol.1 , pp. 341-350
    • Giannetti, A.M.1    Snow, P.M.2    Zak, O.3    Bjorkman, P.J.4
  • 14
    • 0032555601 scopus 로고    scopus 로고
    • Co-trafficking of HFE, a nonclassical major histocompatibility complex class I protein, with the transferrin receptor implies a role in intracellular iron regulation
    • Gross CN, Irrinki A, Feder JN, Enns CA. Co-trafficking of HFE, a nonclassical major histocompatibility complex class I protein, with the transferrin receptor implies a role in intracellular iron regulation. J Biol Chem. 1998;273:22068-22074.
    • (1998) J Biol Chem , vol.273 , pp. 22068-22074
    • Gross, C.N.1    Irrinki, A.2    Feder, J.N.3    Enns, C.A.4
  • 15
    • 0033605595 scopus 로고    scopus 로고
    • The hereditary hemochromatosis protein, HFE, specifically regulates transferrin-mediated iron uptake in HeLa cells
    • Roy CN, Penny DM, Feder JN, Enns CA. The hereditary hemochromatosis protein, HFE, specifically regulates transferrin-mediated iron uptake in HeLa cells. J Biol Chem. 1999;274:9022-9028.
    • (1999) J Biol Chem , vol.274 , pp. 9022-9028
    • Roy, C.N.1    Penny, D.M.2    Feder, J.N.3    Enns, C.A.4
  • 16
    • 0037444795 scopus 로고    scopus 로고
    • The haemochromatosis protein HFE induces an apparent iron-deficient phenotype in H1299 cells that is not corrected by co-expression of beta 2-microglobulin
    • Wang J, Chen G, Pantopoulos K. The haemochromatosis protein HFE induces an apparent iron-deficient phenotype in H1299 cells that is not corrected by co-expression of beta 2-microglobulin. Biochem J. 2003;370:891-899.
    • (2003) Biochem J , vol.370 , pp. 891-899
    • Wang, J.1    Chen, G.2    Pantopoulos, K.3
  • 17
    • 0041422148 scopus 로고    scopus 로고
    • Mechanisms of HFE-induced regulation of iron homeostasis: Insights from the W81A HFE mutation
    • Zhang AS, Davies PS, Carlson HL, Enns CA. Mechanisms of HFE-induced regulation of iron homeostasis: insights from the W81A HFE mutation. Proc Natl Acad Sci U S A. 2003;100:9500-9505.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 9500-9505
    • Zhang, A.S.1    Davies, P.S.2    Carlson, H.L.3    Enns, C.A.4
  • 18
    • 0033020518 scopus 로고    scopus 로고
    • The transferrin receptor binding site on HFE, the class I MHC-related protein mutated in hereditary hemochromatosis
    • Lebron JA, Bjorkman PJ. The transferrin receptor binding site on HFE, the class I MHC-related protein mutated in hereditary hemochromatosis. J Mol Biol. 1999;289:1109-1118.
    • (1999) J Mol Biol , vol.289 , pp. 1109-1118
    • Lebron, J.A.1    Bjorkman, P.J.2
  • 19
    • 0023243675 scopus 로고
    • Functional expression of the human transferrin receptor cDNA in Chinese hamster ovary cells deficient in endogenous transferrin receptor
    • McGraw T, Greenfield L, Maxfield FR. Functional expression of the human transferrin receptor cDNA in Chinese hamster ovary cells deficient in endogenous transferrin receptor. J Cell Biol. 1987;105:207-214.
    • (1987) J Cell Biol , vol.105 , pp. 207-214
    • McGraw, T.1    Greenfield, L.2    Maxfield, F.R.3
  • 20
    • 0028938965 scopus 로고
    • An internalization motif is created in the cytoplasmic domain of the transferrin receptor by substitution of a tyrosine at the first position of a predicted tight turn
    • Pytowski B, Judge TW, McGraw TE. An internalization motif is created in the cytoplasmic domain of the transferrin receptor by substitution of a tyrosine at the first position of a predicted tight turn. J Biol Chem. 1995;270:9067-9073.
    • (1995) J Biol Chem , vol.270 , pp. 9067-9073
    • Pytowski, B.1    Judge, T.W.2    McGraw, T.E.3
  • 21
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970;227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 22
    • 0026014164 scopus 로고
    • A mutated transferrin receptor lacking asparagine-linked glycosylation sites shows reduced functionality and an association with binding immunoglobulin protein
    • Williams AM, Enns CA. A mutated transferrin receptor lacking asparagine-linked glycosylation sites shows reduced functionality and an association with binding immunoglobulin protein. J Biol Chem. 1991;266:17648-17654.
    • (1991) J Biol Chem , vol.266 , pp. 17648-17654
    • Williams, A.M.1    Enns, C.A.2
  • 23
    • 0034634505 scopus 로고    scopus 로고
    • Interactions of the ectodomain of HFE with the transferrin receptor are critical for iron homeostasis in cells
    • Roy CN, Carlson EJ, Anderson EL, et al. Interactions of the ectodomain of HFE with the transferrin receptor are critical for iron homeostasis in cells. FEBS Lett. 2000;484:271-274.
    • (2000) FEBS Lett , vol.484 , pp. 271-274
    • Roy, C.N.1    Carlson, E.J.2    Anderson, E.L.3
  • 24
    • 0036135887 scopus 로고    scopus 로고
    • Increased IRP1 and IRP2 RNA binding activity accompanies a reduction of the labile iron pool in HFE-expressing cells
    • Roy CN, Blemings KP, Deck KM, et al. Increased IRP1 and IRP2 RNA binding activity accompanies a reduction of the labile iron pool in HFE-expressing cells. J Cell Physiol. 2002;190:218-226.
    • (2002) J Cell Physiol , vol.190 , pp. 218-226
    • Roy, C.N.1    Blemings, K.P.2    Deck, K.M.3
  • 26
    • 0023938640 scopus 로고
    • Carrier mediated iron transport through erythroid cell membrane
    • Egyed A. Carrier mediated iron transport through erythroid cell membrane. Br J Haematol. 1988;68:483-486.
    • (1988) Br J Haematol , vol.68 , pp. 483-486
    • Egyed, A.1
  • 27
    • 0023850270 scopus 로고
    • Effect of osmolar ionic composition of the extracellular fluid on transferrin endocytosis and exocytosis and iron uptake by reticulocytes
    • Bowen BJ, Morgan EH. Effect of osmolar ionic composition of the extracellular fluid on transferrin endocytosis and exocytosis and iron uptake by reticulocytes. J Cell Phys. 1988:1-12.
    • (1988) J Cell Phys , pp. 1-12
    • Bowen, B.J.1    Morgan, E.H.2
  • 28
    • 0025014580 scopus 로고
    • Role of the human transferrin receptor cytoplasmic domain in endocytosis: Localization of a specific signal sequence for internalization
    • Jing S, Spencer T, Miller K, Hopkins C, Trowbridge IS. Role of the human transferrin receptor cytoplasmic domain in endocytosis: localization of a specific signal sequence for internalization. J Cell Biol. 1990;110:283-294.
    • (1990) J Cell Biol , vol.110 , pp. 283-294
    • Jing, S.1    Spencer, T.2    Miller, K.3    Hopkins, C.4    Trowbridge, I.S.5
  • 29
    • 0025402516 scopus 로고
    • Human transferrin receptor internalization is partially dependent upon an aromatic amino acid on the cytoplasmic domain
    • McGraw T, Maxfield FR. Human transferrin receptor internalization is partially dependent upon an aromatic amino acid on the cytoplasmic domain. Cell Regulation. 1990;1:369-377.
    • (1990) Cell Regulation , vol.1 , pp. 369-377
    • McGraw, T.1    Maxfield, F.R.2
  • 30
    • 0027493023 scopus 로고
    • YTRF is the conserved internalization signal of the transferrin receptor, and a second YTRF signal at position 31-34 enhances endocytosis
    • Collawn JF, Lai A, Domingo D, Fitch M, Hatton S, Trowbridge IS. YTRF is the conserved internalization signal of the transferrin receptor, and a second YTRF signal at position 31-34 enhances endocytosis. J Biol Chem. 1993;268:21686-21692.
    • (1993) J Biol Chem , vol.268 , pp. 21686-21692
    • Collawn, J.F.1    Lai, A.2    Domingo, D.3    Fitch, M.4    Hatton, S.5    Trowbridge, I.S.6
  • 31
    • 0037180545 scopus 로고    scopus 로고
    • The hemochromatosis protein HFE inhibits iron export from macrophages
    • Drakesmith H, Sweetland E, Schimanski L, et al. The hemochromatosis protein HFE inhibits iron export from macrophages. Proc Natl Acad Sci U S A. 2002;99:15602-15607.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 15602-15607
    • Drakesmith, H.1    Sweetland, E.2    Schimanski, L.3
  • 32
    • 2942537827 scopus 로고    scopus 로고
    • Expression of the hereditary hemochromatosis protein HFE increases ferritin levels by inhibiting iron export in HT29 cells
    • Davies PS, Enns CA. Expression of the hereditary hemochromatosis protein HFE increases ferritin levels by inhibiting iron export in HT29 cells. J Biol Chem. 2004;279:25085-25092.
    • (2004) J Biol Chem , vol.279 , pp. 25085-25092
    • Davies, P.S.1    Enns, C.A.2
  • 33
    • 0029758487 scopus 로고    scopus 로고
    • Molecular control of vertebrate iron metabolism: MRNA-based regulatory circuits operated by iron, nitric oxide, and oxidative stress
    • Hentze MW, Kuhn LC. Molecular control of vertebrate iron metabolism: mRNA-based regulatory circuits operated by iron, nitric oxide, and oxidative stress. Proc Natl Acad Sci U S A. 1996;93: 8175-8182.
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 8175-8182
    • Hentze, M.W.1    Kuhn, L.C.2
  • 34
    • 0033485885 scopus 로고    scopus 로고
    • HFE downregulates iron uptake from transferrin and induces iron-regulatory protein activity in stably transfected cells
    • Riedel HD, Muckenthaler MU, Gehrke SG, et al. HFE downregulates iron uptake from transferrin and induces iron-regulatory protein activity in stably transfected cells. Blood. 1999;94:3915-3921.
    • (1999) Blood , vol.94 , pp. 3915-3921
    • Riedel, H.D.1    Muckenthaler, M.U.2    Gehrke, S.G.3
  • 35
    • 0032866573 scopus 로고    scopus 로고
    • Overexpression of the hereditary hemochromatosis protein, HFE, in HeLa cells induces and iron-deficient phenotype
    • Corsi B, Levi S, Cozzi A, et al. Overexpression of the hereditary hemochromatosis protein, HFE, in HeLa cells induces and iron-deficient phenotype. FEBS Lett. 1999;460:149-152.
    • (1999) FEBS Lett , vol.460 , pp. 149-152
    • Corsi, B.1    Levi, S.2    Cozzi, A.3
  • 36
    • 0035938289 scopus 로고    scopus 로고
    • The effects of wild-type and mutant HFE expression upon cellular iron uptake in transfected human embryonic kidney cells
    • Feeney GP, Worwood M. The effects of wild-type and mutant HFE expression upon cellular iron uptake in transfected human embryonic kidney cells. Biochim Biophys Acta. 2001;1538: 242-251.
    • (2001) Biochim Biophys Acta , vol.1538 , pp. 242-251
    • Feeney, G.P.1    Worwood, M.2
  • 37
    • 0037022588 scopus 로고    scopus 로고
    • Regulation of transferrin-mediated iron uptake by HFE, the protein defective in hereditary hemochromatosis
    • Waheed A, Grubb JH, Zhou XY, et al. Regulation of transferrin-mediated iron uptake by HFE, the protein defective in hereditary hemochromatosis. Proc Natl Acad Sci U S A. 2002;99:3117-3122.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 3117-3122
    • Waheed, A.1    Grubb, J.H.2    Zhou, X.Y.3
  • 38
    • 0034254794 scopus 로고    scopus 로고
    • Wild-type HFE protein normalizes transferrin iron accumulation in macrophages from subjects with hereditary hemochromatosis
    • Montosi G, Paglia P, Garuti C, et al. Wild-type HFE protein normalizes transferrin iron accumulation in macrophages from subjects with hereditary hemochromatosis. Blood. 2000;96:1125-1129.
    • (2000) Blood , vol.96 , pp. 1125-1129
    • Montosi, G.1    Paglia, P.2    Garuti, C.3
  • 40
    • 0842263988 scopus 로고    scopus 로고
    • Localization of iron metabolism-related mRNAs in rat liver indicate that HFE is expressed predominantly in hepatocytes
    • Zhang AS, Xiong S, Tsukamoto H, Enns CA. Localization of iron metabolism-related mRNAs in rat liver indicate that HFE is expressed predominantly in hepatocytes. Blood. 2004;103:1509-1514.
    • (2004) Blood , vol.103 , pp. 1509-1514
    • Zhang, A.S.1    Xiong, S.2    Tsukamoto, H.3    Enns, C.A.4
  • 41
    • 10744230040 scopus 로고    scopus 로고
    • Structure and liver cell expression pattern of the HFE gene in the rat
    • Holmstrom P, Dzikaite V, Hultcrantz R, et al. Structure and liver cell expression pattern of the HFE gene in the rat. J Hepatol. 2003;39:308-314.
    • (2003) J Hepatol , vol.39 , pp. 308-314
    • Holmstrom, P.1    Dzikaite, V.2    Hultcrantz, R.3


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