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Volumn 31, Issue 10, 1999, Pages 1111-1137

The transferrin receptor: Role in health and disease

Author keywords

[No Author keywords available]

Indexed keywords

CYTOKINE; FERRIC ION; IRON REGULATORY FACTOR; LYMPHOKINE; REPRESSOR PROTEIN; TRANSFERRIN; TRANSFERRIN RECEPTOR;

EID: 0032830130     PISSN: 13572725     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1357-2725(99)00070-9     Document Type: Article
Times cited : (481)

References (185)
  • 1
    • 0000622023 scopus 로고
    • Iron-transferrin requirements and transferrin receptor expression in proliferating cells
    • P. Ponka, H.M. Schulman, & R.C. Woodworth. Boca Raton, FL: CRC
    • Kühn L.C., Schulman H.M., Ponka P. Iron-transferrin requirements and transferrin receptor expression in proliferating cells. Ponka P., Schulman H.M., Woodworth R.C. Iron Transport and Storage. 1990;149-191 CRC, Boca Raton, FL.
    • (1990) Iron Transport and Storage , pp. 149-191
    • Kühn, L.C.1    Schulman, H.M.2    Ponka, P.3
  • 3
    • 0031567095 scopus 로고    scopus 로고
    • The molecular mechanisms of the metabolism and transport of iron in normal and neoplastic cells
    • Richardson D.R., Ponka P. The molecular mechanisms of the metabolism and transport of iron in normal and neoplastic cells. Biochimica et Biophysica Acta. 1331:1997;1-40.
    • (1997) Biochimica et Biophysica Acta , vol.1331 , pp. 1-40
    • Richardson, D.R.1    Ponka, P.2
  • 4
    • 0011224256 scopus 로고
    • Iron metabolism in relation to heme synthesis
    • H.A. Dailey. New York: McGraw-Hill Publishing Company
    • Ponka P., Schulman H.M., Cox T.M. Iron metabolism in relation to heme synthesis. Dailey H.A. Biosynthesis of Heme and Chlorophylls. 1990;393-434 McGraw-Hill Publishing Company, New York.
    • (1990) Biosynthesis of Heme and Chlorophylls , pp. 393-434
    • Ponka, P.1    Schulman, H.M.2    Cox, T.M.3
  • 6
    • 0028850367 scopus 로고
    • Siderophores: Structure and function of microbial iron transport compounds
    • Neilands J.B. Siderophores: structure and function of microbial iron transport compounds. Journal of Biological Chemistry. 270:1995;26,723-26,726.
    • (1995) Journal of Biological Chemistry , vol.270 , pp. 26
    • Neilands, J.B.1
  • 10
    • 0030561519 scopus 로고    scopus 로고
    • Cockroach transferrin closely resembles vertebrate transferrins in its metal ion-binding properties: A spectroscopic study
    • Gasdaska J.R., Law J.H., Bender C.J., Aisen P. Cockroach transferrin closely resembles vertebrate transferrins in its metal ion-binding properties: a spectroscopic study. Journal of Inorganic Biochemistry. 64:1996;247-258.
    • (1996) Journal of Inorganic Biochemistry , vol.64 , pp. 247-258
    • Gasdaska, J.R.1    Law, J.H.2    Bender, C.J.3    Aisen, P.4
  • 11
    • 0025695557 scopus 로고
    • Isolation and molecular cloning of transferrin from the tobacco hornwork, Manduca sexta. Sequence similarity to the vertebrate transferrins
    • Bartfeld N.S., Law J.H. Isolation and molecular cloning of transferrin from the tobacco hornwork, Manduca sexta. Sequence similarity to the vertebrate transferrins. Journal of Biological Chemistry. 265:1990;21,684-21,691.
    • (1990) Journal of Biological Chemistry , vol.265 , pp. 21
    • Bartfeld, N.S.1    Law, J.H.2
  • 13
    • 0031019989 scopus 로고    scopus 로고
    • A structurally novel transferrin-like protein accumulates in the plasma membrane of the unicellular green alga Dunaliella salina grown in high salinities
    • Fisher M., Gokhman I., Pick U., Zamir A. A structurally novel transferrin-like protein accumulates in the plasma membrane of the unicellular green alga Dunaliella salina grown in high salinities. Journal of Biological Chemistry. 272:1997;1565-1570.
    • (1997) Journal of Biological Chemistry , vol.272 , pp. 1565-1570
    • Fisher, M.1    Gokhman, I.2    Pick, U.3    Zamir, A.4
  • 14
    • 0032504198 scopus 로고    scopus 로고
    • Iron uptake by the halotolerant alga Dunaliella is mediated by a plasma membrane transferrrin
    • Fisher M., Zamir A., Pick U. Iron uptake by the halotolerant alga Dunaliella is mediated by a plasma membrane transferrrin. Journal of Biological Chemistry. 273:1998;17,553-17,558.
    • (1998) Journal of Biological Chemistry , vol.273 , pp. 17
    • Fisher, M.1    Zamir, A.2    Pick, U.3
  • 16
    • 0018180264 scopus 로고
    • Molecular characteristics of the transferrin-receptor complex of the rabbit reticulocyte
    • Hu H-Y.Y., Aisen P. Molecular characteristics of the transferrin-receptor complex of the rabbit reticulocyte. Journal of Supramolecular Structure. 8:1978;349-360.
    • (1978) Journal of Supramolecular Structure , vol.8 , pp. 349-360
    • Hu, H.-Y.Y.1    Aisen, P.2
  • 17
    • 0018137392 scopus 로고
    • Identification of the transferrin receptor of the rabbit reticulocyte
    • Witt D.P., Woodworth R.C. Identification of the transferrin receptor of the rabbit reticulocyte. Biochemistry. 17:1978;438-448.
    • (1978) Biochemistry , vol.17 , pp. 438-448
    • Witt, D.P.1    Woodworth, R.C.2
  • 19
    • 0019773013 scopus 로고
    • Physical characterization of the transferrin receptor in human placentae
    • Enns C.A., Sussman H.H. Physical characterization of the transferrin receptor in human placentae. Journal of Biological Chemistry. 255:1981;9820-9823.
    • (1981) Journal of Biological Chemistry , vol.255 , pp. 9820-9823
    • Enns, C.A.1    Sussman, H.H.2
  • 21
    • 0019570604 scopus 로고
    • Human cell surface glycoprotein related to cell proliferation is the receptor for transferrin
    • Trowbridge I.S., Omary M.B. Human cell surface glycoprotein related to cell proliferation is the receptor for transferrin. Proceedings of the National Academy of Sciences USA. 78:1981;3039-3043.
    • (1981) Proceedings of the National Academy of Sciences USA , vol.78 , pp. 3039-3043
    • Trowbridge, I.S.1    Omary, M.B.2
  • 22
    • 0021685289 scopus 로고
    • The human transferrin receptor gene: Genomic organization and the complete primary structure of the receptor deduced from a cDNA sequence
    • McClelland A., Kühn L.C., Ruddle F.H. The human transferrin receptor gene: Genomic organization and the complete primary structure of the receptor deduced from a cDNA sequence. Cell. 39:1984;267-274.
    • (1984) Cell , vol.39 , pp. 267-274
    • McClelland, A.1    Kühn, L.C.2    Ruddle, F.H.3
  • 23
    • 0021130929 scopus 로고
    • Primary structure of human transferrin receptor deduced from the mRNA sequence
    • C. Schneider, M.J. Owen, D. Banville, J.G. Williams, Primary structure of human transferrin receptor deduced from the mRNA sequence. Nature (1984) 675-678.
    • (1984) Nature , pp. 675-678
    • Schneider, C.1    Owen, M.J.2    Banville, D.3    Williams, J.G.4
  • 24
    • 0023282177 scopus 로고
    • Identification of the intermolecular disulfide bonds of the human transferrin receptor and its lipid-attachment site
    • Jing S., Trowbridge I.S. Identification of the intermolecular disulfide bonds of the human transferrin receptor and its lipid-attachment site. EMBO Journal. 6:1987;327-331.
    • (1987) EMBO Journal , vol.6 , pp. 327-331
    • Jing, S.1    Trowbridge, I.S.2
  • 25
    • 0019804406 scopus 로고
    • Biosynthesis of the human transferrin receptor in cultured cells
    • Omary M.B., Trowbridge I.S. Biosynthesis of the human transferrin receptor in cultured cells. Journal of Biological Chemistry. 256:1981;12,888-12,892.
    • (1981) Journal of Biological Chemistry , vol.256 , pp. 12
    • Omary, M.B.1    Trowbridge, I.S.2
  • 26
    • 0026767382 scopus 로고
    • Identification of the O-linked glycosylation site of the human transferrin receptor
    • Hayes G.R., Enns C.A., Lucas J.J. Identification of the O-linked glycosylation site of the human transferrin receptor. Glycobiology. 2:1992;355-359.
    • (1992) Glycobiology , vol.2 , pp. 355-359
    • Hayes, G.R.1    Enns, C.A.2    Lucas, J.J.3
  • 27
    • 0026014164 scopus 로고
    • Mutated transferrin receptor lacking asparagine-linked glycoprotein sites shows reduced functionality and an association with binding immunoglobulin protein
    • Williams A.M., Enns C.A. Mutated transferrin receptor lacking asparagine-linked glycoprotein sites shows reduced functionality and an association with binding immunoglobulin protein. Journal of Biological Chemistry. 266:1991;17,648-17,654.
    • (1991) Journal of Biological Chemistry , vol.266 , pp. 17
    • Williams, A.M.1    Enns, C.A.2
  • 28
    • 0027976177 scopus 로고
    • Elimination of the O-linked glycosylation site at Thr 104 results in the generation of a soluble human-transferrin recptor
    • Rutledge E.A., Root B.J., Lucas J.J., Enns C.A. Elimination of the O-linked glycosylation site at Thr 104 results in the generation of a soluble human-transferrin recptor. Blood. 83:1994;580-586.
    • (1994) Blood , vol.83 , pp. 580-586
    • Rutledge, E.A.1    Root, B.J.2    Lucas, J.J.3    Enns, C.A.4
  • 29
    • 0030064479 scopus 로고    scopus 로고
    • Functional analysis of human/chicken transferrin receptor chimeras indicates that the carboxy-terminal region is important for ligand binding
    • Buchegger F., Trowbridge I.S., Liu L.F., White S., Collawn J.F. Functional analysis of human/chicken transferrin receptor chimeras indicates that the carboxy-terminal region is important for ligand binding. European Journal of Biochemistry. 235:1996;9-17.
    • (1996) European Journal of Biochemistry , vol.235 , pp. 9-17
    • Buchegger, F.1    Trowbridge, I.S.2    Liu, L.F.3    White, S.4    Collawn, J.F.5
  • 30
    • 0022749229 scopus 로고
    • The transmembrane segment of the human transferrin receptor functions as a signal peptide
    • Zerial M., Melancon P., Schneider C., Garoff H. The transmembrane segment of the human transferrin receptor functions as a signal peptide. EMBO Journal. 5:1986;1543-1550.
    • (1986) EMBO Journal , vol.5 , pp. 1543-1550
    • Zerial, M.1    Melancon, P.2    Schneider, C.3    Garoff, H.4
  • 31
    • 0023657394 scopus 로고
    • Foreign transmembrane peptides replacing the internal signal sequence of transferrin receptor allow its translocation and membrane binding
    • Zerial M., Haylbroek D., Garoff H. Foreign transmembrane peptides replacing the internal signal sequence of transferrin receptor allow its translocation and membrane binding. Cell. 48:1987;147-155.
    • (1987) Cell , vol.48 , pp. 147-155
    • Zerial, M.1    Haylbroek, D.2    Garoff, H.3
  • 32
    • 0025315963 scopus 로고
    • Nonacylated human transferrin receptors are rapidly internalized and mediate iron uptake
    • Jing S., Trowbridge I.S. Nonacylated human transferrin receptors are rapidly internalized and mediate iron uptake. Journal of Biological Chemistry. 265:1990;11,555-11,559.
    • (1990) Journal of Biological Chemistry , vol.265 , pp. 11
    • Jing, S.1    Trowbridge, I.S.2
  • 33
    • 0020447793 scopus 로고
    • Structural features of the cell surface receptor for transferrin that is recognized by the monoclonal antibody OKT9
    • Schneider C.R., Sutherland R., Newman R., Greaves M. Structural features of the cell surface receptor for transferrin that is recognized by the monoclonal antibody OKT9. Journal of Biological Chemistry. 257:1982;8516-8522.
    • (1982) Journal of Biological Chemistry , vol.257 , pp. 8516-8522
    • Schneider, C.R.1    Sutherland, R.2    Newman, R.3    Greaves, M.4
  • 34
    • 0023648008 scopus 로고
    • Endocytosis of the transferrin receptor requires the cytoplasmic domain but not its phosphorylation site
    • Rothenberger S., Iacopetta B.J., Kühn L.C. Endocytosis of the transferrin receptor requires the cytoplasmic domain but not its phosphorylation site. Cell. 49:1987;423-431.
    • (1987) Cell , vol.49 , pp. 423-431
    • Rothenberger, S.1    Iacopetta, B.J.2    Kühn, L.C.3
  • 35
    • 0022407991 scopus 로고
    • Hemin inhibits internalization of transferrin by reticulocytes and promotes phosphorylation of the membrane transferrin receptor
    • Cox T.M., O'Donnell M.W., Aisen P., London I.M. Hemin inhibits internalization of transferrin by reticulocytes and promotes phosphorylation of the membrane transferrin receptor. Proceedings of the National Academy of Sciences USA. 82:1985;5170-5174.
    • (1985) Proceedings of the National Academy of Sciences USA , vol.82 , pp. 5170-5174
    • Cox, T.M.1    O'Donnell, M.W.2    Aisen, P.3    London, I.M.4
  • 36
    • 0025276236 scopus 로고
    • A point mutation in the cytoplasmic domain of the transferrin receptor inhibits endocytosis
    • Alvarez E., Girones N., Davis R.J. A point mutation in the cytoplasmic domain of the transferrin receptor inhibits endocytosis. Biochemical Journal. 267:1990;31-35.
    • (1990) Biochemical Journal , vol.267 , pp. 31-35
    • Alvarez, E.1    Girones, N.2    Davis, R.J.3
  • 37
    • 0025635559 scopus 로고
    • Transferrin receptor internalization sequence YXRF implicates a tight turn as the structural recognition motif for endocytosis
    • Collawn J.F., Stangel M., Kühn L.A., Esekogwu V., Jing S.Q., Trowbridge I.S., Tainer J.A. Transferrin receptor internalization sequence YXRF implicates a tight turn as the structural recognition motif for endocytosis. Cell. 63:1990;1061-1072.
    • (1990) Cell , vol.63 , pp. 1061-1072
    • Collawn, J.F.1    Stangel, M.2    Kühn, L.A.3    Esekogwu, V.4    Jing, S.Q.5    Trowbridge, I.S.6    Tainer, J.A.7
  • 38
    • 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 J.F., Lai A., Domingo D., Fitch M., Hatton S., Trowbridge I.S. YTRF is the conserved internalization signal of the transferrin receptor, and a second YTRF signal at position 31-34 enhances endocytosis. Journal of Biological Chemistry. 268:1993;21,686-21,692.
    • (1993) Journal of Biological Chemistry , vol.268 , pp. 21
    • Collawn, J.F.1    Lai, A.2    Domingo, D.3    Fitch, M.4    Hatton, S.5    Trowbridge, I.S.6
  • 39
    • 0032530340 scopus 로고    scopus 로고
    • Iron is hot: An update on the pathophysiology of hemochromatosis
    • Andrews N.C., Levy J.E. Iron is hot: an update on the pathophysiology of hemochromatosis. Blood. 92:1998;1845-1851.
    • (1998) Blood , vol.92 , pp. 1845-1851
    • Andrews, N.C.1    Levy, J.E.2
  • 43
    • 0032478524 scopus 로고    scopus 로고
    • Crystal structure of the hemochromatosis protein HFE and characterization of its interaction with transferrin receptor
    • Lebrón J.A., Bennett M.J., Vaughn D.E., Chirino A.J., Snow P.M., Mintier G.A., Feder J.N., Bjorkman P.J. Crystal structure of the hemochromatosis protein HFE and characterization of its interaction with transferrin receptor. Cell. 93:1998;111-123.
    • (1998) Cell , vol.93 , pp. 111-123
    • Lebrón, 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
  • 44
    • 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 C.N., Irrinki A., Feder J.N., Enns C.A. Co-trafficking of HFE, a nonclassical major histocompatibility complex class I protein, with the transferrin receptor implies a role in intracellular iron regulation. Journal of Biological Chemistry. 273:1998;22,068-22,074.
    • (1998) Journal of Biological Chemistry , vol.273 , pp. 22
    • Gross, C.N.1    Irrinki, A.2    Feder, J.N.3    Enns, C.A.4
  • 46
    • 0024348472 scopus 로고
    • Model of reticuloendothelial iron metabolism in humans: Abnormal behavior in idiopathic hemochromatosis and in inflammation
    • Fillet G., Beguin Y., Baldelli L. Model of reticuloendothelial iron metabolism in humans: abnormal behavior in idiopathic hemochromatosis and in inflammation. Blood. 74:1989;844-851.
    • (1989) Blood , vol.74 , pp. 844-851
    • Fillet, G.1    Beguin, Y.2    Baldelli, L.3
  • 47
    • 0032532742 scopus 로고    scopus 로고
    • Structural model of phospholipid-reconstituted human transferrin receptor derived by electron microscopy
    • Fuchs H., Lucken U., Tauber R., Engel A., Gessner R. Structural model of phospholipid-reconstituted human transferrin receptor derived by electron microscopy. Structure. 6:1998;1235-1243.
    • (1998) Structure , vol.6 , pp. 1235-1243
    • Fuchs, H.1    Lucken, U.2    Tauber, R.3    Engel, A.4    Gessner, R.5
  • 49
    • 0021330893 scopus 로고
    • A highly cytotoxic human transferrin-ricin A chain conjugate used to select receptor-modified cells
    • Raso V., Basala M. A highly cytotoxic human transferrin-ricin A chain conjugate used to select receptor-modified cells. Journal of Biological Chemistry. 259:1984;1143-1149.
    • (1984) Journal of Biological Chemistry , vol.259 , pp. 1143-1149
    • Raso, V.1    Basala, M.2
  • 50
    • 0023243675 scopus 로고
    • Functional expression of the human transferrin receptor cDNA in Chinese hamster ovary cells deficient in endogenous transferrin receptor
    • McGraw T.E., Greenfield L., Maxfield F.R. Functional expression of the human transferrin receptor cDNA in Chinese hamster ovary cells deficient in endogenous transferrin receptor. Journal of Cell Biology. 105:1987;207-214.
    • (1987) Journal of Cell Biology , vol.105 , pp. 207-214
    • McGraw, T.E.1    Greenfield, L.2    Maxfield, F.R.3
  • 51
    • 0026770143 scopus 로고
    • Transferrin-receptor-independent but iron-dependent proliferation of variant Chinese hamster ovary cells
    • Chan R.Y., Ponka P., Schulman H.M. Transferrin-receptor-independent but iron-dependent proliferation of variant Chinese hamster ovary cells. Experimental Cell Research. 202:1992;326-336.
    • (1992) Experimental Cell Research , vol.202 , pp. 326-336
    • Chan, R.Y.1    Ponka, P.2    Schulman, H.M.3
  • 52
    • 0021265943 scopus 로고
    • The effect of the iron saturation of transferrin on its binding and uptake by rabbit reticulocytes
    • Young S.P., Bomford A., Williams R. The effect of the iron saturation of transferrin on its binding and uptake by rabbit reticulocytes. Biochemical Journal. 219:1984;505-510.
    • (1984) Biochemical Journal , vol.219 , pp. 505-510
    • Young, S.P.1    Bomford, A.2    Williams, R.3
  • 53
    • 0002159387 scopus 로고
    • Iron transport
    • J.H. Brock, J.W. Halliday, M.J. Pippard, & L.W. Powell. W.B. Saunders Company Ltd
    • Baker E., Morgan E.H. Iron transport. Brock J.H., Halliday J.W., Pippard M.J., Powell L.W. Iron Metabolism in Health and Disease. 1994;63-95 W.B. Saunders Company Ltd.
    • (1994) Iron Metabolism in Health and Disease , pp. 63-95
    • Baker, E.1    Morgan, E.H.2
  • 54
    • 0025924788 scopus 로고
    • A new role for the transferrin receptor in the release of iron from transferrin
    • Bali P.K., Zak O., Aisen P. 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
  • 55
    • 0025744263 scopus 로고
    • Binding to cellular receptors results in increased iron release from transferrin at mildly acidic pH
    • Sipe D.M., Murphy R.F. Binding to cellular receptors results in increased iron release from transferrin at mildly acidic pH. Journal of Biological Chemistry. 266:1991;8002-8007.
    • (1991) Journal of Biological Chemistry , vol.266 , pp. 8002-8007
    • Sipe, D.M.1    Murphy, R.F.2
  • 59
    • 0028120808 scopus 로고
    • Interactive endocytosis of transferrin by K562 cells
    • Young S.P., Bomford A. Interactive endocytosis of transferrin by K562 cells. Biochemical Journal. 298:1994;165-170.
    • (1994) Biochemical Journal , vol.298 , pp. 165-170
    • Young, S.P.1    Bomford, A.2
  • 60
    • 0029865751 scopus 로고    scopus 로고
    • Distribution of iron in reticulocytes after inhibition of heme synthesis with succinylacetone. Examination of cytoplasmic and mitochondrial intermediates involved in iron metabolism
    • Richardson D.R., Ponka P., Vyoral D. Distribution of iron in reticulocytes after inhibition of heme synthesis with succinylacetone. Examination of cytoplasmic and mitochondrial intermediates involved in iron metabolism. Blood. 87:1996;3477-3488.
    • (1996) Blood , vol.87 , pp. 3477-3488
    • Richardson, D.R.1    Ponka, P.2    Vyoral, D.3
  • 61
    • 0031028178 scopus 로고    scopus 로고
    • Tissue-specific regulation of iron metabolism and heme synthesis: Distinct control mechanisms in erythroid cells
    • Ponka P. Tissue-specific regulation of iron metabolism and heme synthesis: distinct control mechanisms in erythroid cells. Blood. 89:1997;1-25.
    • (1997) Blood , vol.89 , pp. 1-25
    • Ponka, P.1
  • 62
    • 0027237639 scopus 로고
    • Role of microtubules in transferrin receptor transport from the cell surface to endosomes and the Golgi complex
    • Jin M., Snider M.D. Role of microtubules in transferrin receptor transport from the cell surface to endosomes and the Golgi complex. Journal of Biological Chemistry. 268:1993;18,390-18,397.
    • (1993) Journal of Biological Chemistry , vol.268 , pp. 18
    • Jin, M.1    Snider, M.D.2
  • 63
    • 0032488507 scopus 로고    scopus 로고
    • Two distinct kinds of tubular organelles involved in the rapid recycling and slow processing of endocytosed transferrin
    • Sakai T., Mizuno T., Miyamoto H., Kawasaki K. Two distinct kinds of tubular organelles involved in the rapid recycling and slow processing of endocytosed transferrin. Biochemical and Biophysical Research Communications. 242:1998;151-157.
    • (1998) Biochemical and Biophysical Research Communications , vol.242 , pp. 151-157
    • Sakai, T.1    Mizuno, T.2    Miyamoto, H.3    Kawasaki, K.4
  • 64
    • 0031816990 scopus 로고    scopus 로고
    • Oxidative stress leads to a rapid alteration of transferrin receptor intravesicular trafficking
    • Malorni W., Testa U., Rainaldi G., Tritarelli E., Peschle C. Oxidative stress leads to a rapid alteration of transferrin receptor intravesicular trafficking. Experimental Cell Research. 241:1998;102-116.
    • (1998) Experimental Cell Research , vol.241 , pp. 102-116
    • Malorni, W.1    Testa, U.2    Rainaldi, G.3    Tritarelli, E.4    Peschle, C.5
  • 65
    • 0032959574 scopus 로고    scopus 로고
    • Transferrin receptor is necessary for development of erythrocytes and the nervous system
    • Levy J.E., Jin O., Fujiwara Y., Kuo F., Andrews N.C. Transferrin receptor is necessary for development of erythrocytes and the nervous system. Nature Genetics. 21:1999;396-399.
    • (1999) Nature Genetics , vol.21 , pp. 396-399
    • Levy, J.E.1    Jin, O.2    Fujiwara, Y.3    Kuo, F.4    Andrews, N.C.5
  • 66
    • 0026674282 scopus 로고
    • Exogenous transferrin is taken up and localized by the neurulation-stage mouse embryo in vitro
    • Copp A.J., Estibeiro J.P., Brook F.A., Downs K.M. Exogenous transferrin is taken up and localized by the neurulation-stage mouse embryo in vitro. Developmental Biology. 153:1992;312-323.
    • (1992) Developmental Biology , vol.153 , pp. 312-323
    • Copp, A.J.1    Estibeiro, J.P.2    Brook, F.A.3    Downs, K.M.4
  • 67
    • 0021186059 scopus 로고
    • Acquired iron-deficiency anemia caused by an antibody against the transferrin receptor
    • Larrick J.W., Hyman E.S. Acquired iron-deficiency anemia caused by an antibody against the transferrin receptor. New England Journal of Medicine. 311:1984;214-218.
    • (1984) New England Journal of Medicine , vol.311 , pp. 214-218
    • Larrick, J.W.1    Hyman, E.S.2
  • 68
    • 0021174049 scopus 로고
    • Gene transfer, expression and molecular cloning of the human transferrin receptor gene
    • Kühn J.C., McClelland A., Ruddle F.H. Gene transfer, expression and molecular cloning of the human transferrin receptor gene. Cell. 37:1984;95-103.
    • (1984) Cell , vol.37 , pp. 95-103
    • Kühn, J.C.1    McClelland, A.2    Ruddle, F.H.3
  • 71
    • 0023336087 scopus 로고
    • Noncoding 3′ sequences of the transferrin receptor gene are required for mRNA regulation by iron
    • Owen D., Kühn L.C. Noncoding 3′ sequences of the transferrin receptor gene are required for mRNA regulation by iron. EMBO Journal. 6:1987;1287-1293.
    • (1987) EMBO Journal , vol.6 , pp. 1287-1293
    • Owen, D.1    Kühn, L.C.2
  • 72
    • 0030852440 scopus 로고    scopus 로고
    • Exon/intron structure of the human transferrin receptor gene
    • Evans P., Kemp J. Exon/intron structure of the human transferrin receptor gene. Gene. 199:1997;123-131.
    • (1997) Gene , vol.199 , pp. 123-131
    • Evans, P.1    Kemp, J.2
  • 73
    • 0027500319 scopus 로고
    • Molecular cloning of a complementary DNA encoding a prostate-specific membrane antigen
    • Israeli R.S., Powell C.T., Fair W.R., Heston W.D. Molecular cloning of a complementary DNA encoding a prostate-specific membrane antigen. Cancer Research. 53:1993;227-230.
    • (1993) Cancer Research , vol.53 , pp. 227-230
    • Israeli, R.S.1    Powell, C.T.2    Fair, W.R.3    Heston, W.D.4
  • 74
  • 75
    • 0024365045 scopus 로고
    • A specific mRNA-binding factor regulates the iron-dependent stability of cytoplasmic transferrin receptor mRNA
    • Müllner E.W., Neupert B., Kühn L.C. A specific mRNA-binding factor regulates the iron-dependent stability of cytoplasmic transferrin receptor mRNA. Cell. 58:1989;373-382.
    • (1989) Cell , vol.58 , pp. 373-382
    • Müllner, E.W.1    Neupert, B.2    Kühn, L.C.3
  • 76
    • 0024819020 scopus 로고
    • Iron regulation of transferrin receptor mRNA levels required iron-responsive elements and a rapid turnover determinants in the 3′ untranslated region of the mRNA
    • Casey J.L., Koeller D.M., Rawin V.R., Klausner R.D., Harford J.B. Iron regulation of transferrin receptor mRNA levels required iron-responsive elements and a rapid turnover determinants in the 3′ untranslated region of the mRNA. EMBO Journal. 8:1989;3693-3699.
    • (1989) EMBO Journal , vol.8 , pp. 3693-3699
    • Casey, J.L.1    Koeller, D.M.2    Rawin, V.R.3    Klausner, R.D.4    Harford, J.B.5
  • 79
    • 0023037147 scopus 로고
    • Cell proliferation and expression of the transferrin receptor gene: Promoter sequence homologies and protein interactions
    • Miskimins W.K., McClelland A., Roberts M.P., Ruddle F.H. Cell proliferation and expression of the transferrin receptor gene: promoter sequence homologies and protein interactions. Journal of Cell Biology. 103:1986;1781-1788.
    • (1986) Journal of Cell Biology , vol.103 , pp. 1781-1788
    • Miskimins, W.K.1    McClelland, A.2    Roberts, M.P.3    Ruddle, F.H.4
  • 80
    • 0027502185 scopus 로고
    • A mitogen-responsive promoter region that is synergistically activated through multiple signalling pathways
    • Ouyang Q., Bommakanti M., Miskimins W.K. A mitogen-responsive promoter region that is synergistically activated through multiple signalling pathways. Molecular and Cellular Biology. 13:1993;1796-1804.
    • (1993) Molecular and Cellular Biology , vol.13 , pp. 1796-1804
    • Ouyang, Q.1    Bommakanti, M.2    Miskimins, W.K.3
  • 81
    • 0029005532 scopus 로고
    • Mitogen induction of nuclear factors that interact with a delayed responsive region of the transferrin receptor gene promoter
    • Hirsch S., Miskinins W.K. Mitogen induction of nuclear factors that interact with a delayed responsive region of the transferrin receptor gene promoter. Cell Growth and Differentiation. 6:1995;719-726.
    • (1995) Cell Growth and Differentiation , vol.6 , pp. 719-726
    • Hirsch, S.1    Miskinins, W.K.2
  • 82
    • 0021840709 scopus 로고
    • Sequential expression of genes involved in human T lymphocyte growth and differentiation
    • Kronke M., Leonard W., Depper J.M., Greene W.C. Sequential expression of genes involved in human T lymphocyte growth and differentiation. Journal of Experimental Medicine. 161:1985;1593-1598.
    • (1985) Journal of Experimental Medicine , vol.161 , pp. 1593-1598
    • Kronke, M.1    Leonard, W.2    Depper, J.M.3    Greene, W.C.4
  • 83
    • 0024996685 scopus 로고
    • Gene transcription during in vitro activation of human B lymphocytes with Staphylococcus aureus Cowan I strain
    • Boumpas D.T., Anastassiou E.D., Tsokos G.C., Thyphronitis G., Balow J.E. Gene transcription during in vitro activation of human B lymphocytes with Staphylococcus aureus Cowan I strain. Journal of Immunology. 145:1990;2701-2705.
    • (1990) Journal of Immunology , vol.145 , pp. 2701-2705
    • Boumpas, D.T.1    Anastassiou, E.D.2    Tsokos, G.C.3    Thyphronitis, G.4    Balow, J.E.5
  • 84
    • 0027364195 scopus 로고
    • Interleukin-2-dependent transcriptional and post-transcriptional regulation of transferrin receptor mRNA
    • Seiser C., Texieira S., Kühn L.C. Interleukin-2-dependent transcriptional and post-transcriptional regulation of transferrin receptor mRNA. Journal of Biological Chemistry. 268:1993;13,074-13,080.
    • (1993) Journal of Biological Chemistry , vol.268 , pp. 13
    • Seiser, C.1    Texieira, S.2    Kühn, L.C.3
  • 85
    • 0026352922 scopus 로고
    • SV40 activates transcription from the transferrin receptor promoter by inducing a factor which binds to the CRE/AP-1 recognition sequence
    • Beard P., Offord E., Paduwat N., Bruggmann H. SV40 activates transcription from the transferrin receptor promoter by inducing a factor which binds to the CRE/AP-1 recognition sequence. Nucleic Acids Research. 25:1991;7117-7123.
    • (1991) Nucleic Acids Research , vol.25 , pp. 7117-7123
    • Beard, P.1    Offord, E.2    Paduwat, N.3    Bruggmann, H.4
  • 87
    • 0024550991 scopus 로고
    • Transcriptional regulation of transferrin receptor expression by cultured lymphoblastoid T cells treated with phorbol esters
    • Alcantara O., Denham C.A., Phillips J.L., Boldt D.H. Transcriptional regulation of transferrin receptor expression by cultured lymphoblastoid T cells treated with phorbol esters. Journal of Immunology. 142:1989;1719-1725.
    • (1989) Journal of Immunology , vol.142 , pp. 1719-1725
    • Alcantara, O.1    Denham, C.A.2    Phillips, J.L.3    Boldt, D.H.4
  • 88
    • 0029877060 scopus 로고    scopus 로고
    • Transcriptional regulation of transferrin receptor gene expression during phorbol ester-induced HL-60 cell differentiation
    • Lok C.N., Chan K.F., Loh T.T. Transcriptional regulation of transferrin receptor gene expression during phorbol ester-induced HL-60 cell differentiation. European Journal of Biochemistry. 236:1996;614-619.
    • (1996) European Journal of Biochemistry , vol.236 , pp. 614-619
    • Lok, C.N.1    Chan, K.F.2    Loh, T.T.3
  • 89
    • 0026646606 scopus 로고
    • Transferrin receptor gene is hyperexpressed and transcriptionally regulated in differentiating erythroid cells
    • Chan L.N., Gerhardt E.M. Transferrin receptor gene is hyperexpressed and transcriptionally regulated in differentiating erythroid cells. Journal of Biological Chemistry. 267:1992;8254-8259.
    • (1992) Journal of Biological Chemistry , vol.267 , pp. 8254-8259
    • Chan, L.N.1    Gerhardt, E.M.2
  • 90
    • 0028269856 scopus 로고
    • Regulation of transferrin receptor mRNA expression: Distinct regulatory features in erythroid cells
    • Chan R.Y.Y., Seiser C., Schulman H.M., Kühn L.C., Ponka P. Regulation of transferrin receptor mRNA expression: distinct regulatory features in erythroid cells. European Journal of Biochemistry. 220:1994;683-692.
    • (1994) European Journal of Biochemistry , vol.220 , pp. 683-692
    • Chan, R.Y.Y.1    Seiser, C.2    Schulman, H.M.3    Kühn, L.C.4    Ponka, P.5
  • 93
    • 0028198767 scopus 로고
    • A DNA-binding activity, TRAC, specific for the TRA element of the transferrin receptor gene copurifies with the Ku autoantigen
    • Roberts M.R., Han Y., Fienberg A., Hunihan L., Ruddle F.H. A DNA-binding activity, TRAC, specific for the TRA element of the transferrin receptor gene copurifies with the Ku autoantigen. Proceedings of the National Academy of Sciences USA. 91:1994;6354-6358.
    • (1994) Proceedings of the National Academy of Sciences USA , vol.91 , pp. 6354-6358
    • Roberts, M.R.1    Han, Y.2    Fienberg, A.3    Hunihan, L.4    Ruddle, F.H.5
  • 94
    • 0030917505 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-kinase inhibitor wortmannin blocks mitogenic activation of the transferrin receptor gene promoter in late G1
    • Miskimins W.K., King F., Miskimins R. Phosphatidylinositol 3-kinase inhibitor wortmannin blocks mitogenic activation of the transferrin receptor gene promoter in late G1. Cell Growth and Differentiation. 8:1997;565-570.
    • (1997) Cell Growth and Differentiation , vol.8 , pp. 565-570
    • Miskimins, W.K.1    King, F.2    Miskimins, R.3
  • 95
    • 0029870839 scopus 로고    scopus 로고
    • MafB is an interaction partner and repressor of Ets-1 that inhibits erythroid differentiation
    • Sieweke M.H., Tekotte J., Frampton J., Graf T. MafB is an interaction partner and repressor of Ets-1 that inhibits erythroid differentiation. Cell. 85:1996;49-60.
    • (1996) Cell , vol.85 , pp. 49-60
    • Sieweke, M.H.1    Tekotte, J.2    Frampton, J.3    Graf, T.4
  • 96
    • 85058252845 scopus 로고    scopus 로고
    • Analysis of transferrin receptor promoter activity in erythroid cells
    • Lok C.N., Ponka P. Analysis of transferrin receptor promoter activity in erythroid cells. Blood. 90:1997;7a.
    • (1997) Blood , vol.90
    • Lok, C.N.1    Ponka, P.2
  • 97
    • 0026684574 scopus 로고
    • Iron-dependent regulation of ferritin and transferrin receptor expression by the iron-responsive element binding protein
    • Liebold E.A., Guo B. Iron-dependent regulation of ferritin and transferrin receptor expression by the iron-responsive element binding protein. Annual Review of Nutrition. 12:1992;345-368.
    • (1992) Annual Review of Nutrition , vol.12 , pp. 345-368
    • Liebold, E.A.1    Guo, B.2
  • 98
    • 0028114730 scopus 로고
    • Iron regulatory elements (IREs): A family of mRNA non-coding sequences
    • Theil E.C. Iron regulatory elements (IREs): a family of mRNA non-coding sequences. Biochemical Journal. 304:1994;1-11.
    • (1994) Biochemical Journal , vol.304 , pp. 1-11
    • Theil, E.C.1
  • 99
    • 0027452550 scopus 로고
    • Regulating the fate of mRNA: The control of cellular iron metabolism
    • Klausner R.D., Rouault T.A., Harford J.B. Regulating the fate of mRNA: the control of cellular iron metabolism. Cell. 72:1993;19-28.
    • (1993) Cell , vol.72 , pp. 19-28
    • Klausner, R.D.1    Rouault, T.A.2    Harford, J.B.3
  • 100
    • 0029758487 scopus 로고    scopus 로고
    • Molecular control of vertebrate iron metabolism: MRNA-based regulatory circuits operated by iron, nitric oxide, and oxidative stress
    • Hentze M.W., Kühn L.C. Molecular control of vertebrate iron metabolism: mRNA-based regulatory circuits operated by iron, nitric oxide, and oxidative stress. Proceedings of the National Academy of Sciences USA. 93:1996;8175-8182.
    • (1996) Proceedings of the National Academy of Sciences USA , vol.93 , pp. 8175-8182
    • Hentze, M.W.1    Kühn, L.C.2
  • 101
    • 0028143071 scopus 로고
    • Molecular characterization of a second iron-responsive element binding protein, iron regulatory protein 2. Structure, function and post-translational regulation
    • Samaniego F., Chin J., Iwai K., Rouault T.A., Klausner R.D. Molecular characterization of a second iron-responsive element binding protein, iron regulatory protein 2. Structure, function and post-translational regulation. Journal of Biological Chemistry. 269:1994;30,904-30,910.
    • (1994) Journal of Biological Chemistry , vol.269 , pp. 30
    • Samaniego, F.1    Chin, J.2    Iwai, K.3    Rouault, T.A.4    Klausner, R.D.5
  • 102
    • 0028982262 scopus 로고
    • Iron regulates the intracellular degradation of iron regulatory protein 2 by the proteasome
    • Guo B., Phillips J.D., Yu Y., Leibold E.A. Iron regulates the intracellular degradation of iron regulatory protein 2 by the proteasome. Journal of Biological Chemistry. 270:1995;21,645-21,651.
    • (1995) Journal of Biological Chemistry , vol.270 , pp. 21
    • Guo, B.1    Phillips, J.D.2    Yu, Y.3    Leibold, E.A.4
  • 103
    • 0028788316 scopus 로고
    • Requirements for iron-regulated degradation of the RNA binding protein, iron regulatory protein 2
    • Iwai K., Klausner R.D., Rouault T.A. Requirements for iron-regulated degradation of the RNA binding protein, iron regulatory protein 2. EMBO Journal. 14:1995;5350-5357.
    • (1995) EMBO Journal , vol.14 , pp. 5350-5357
    • Iwai, K.1    Klausner, R.D.2    Rouault, T.A.3
  • 106
    • 77957057022 scopus 로고    scopus 로고
    • Effects of nitrogen monoxide on cellular iron metabolism
    • Richardson D.R., Ponka P. Effects of nitrogen monoxide on cellular iron metabolism. Methods in Neurosciences. 31:1996;329-345.
    • (1996) Methods in Neurosciences , vol.31 , pp. 329-345
    • Richardson, D.R.1    Ponka, P.2
  • 107
    • 0027301897 scopus 로고
    • Biosynthesis of nitric oxide activates iron regulatory factor in macrophages
    • Drapier J.C., Hirling H., Wietzerbin J., Kaldy P., Kühn L.C. Biosynthesis of nitric oxide activates iron regulatory factor in macrophages. EMBO Journal. 12:1993;3643-3649.
    • (1993) EMBO Journal , vol.12 , pp. 3643-3649
    • Drapier, J.C.1    Hirling, H.2    Wietzerbin, J.3    Kaldy, P.4    Kühn, L.C.5
  • 109
    • 0028784211 scopus 로고
    • The effect of redox-related species of nitrogen monoxide on transferrin and iron uptake and cellular proliferation of erythroleukemia (K562) cells
    • Richardson D.R., Neumannova V., Nagy E., Ponka P. The effect of redox-related species of nitrogen monoxide on transferrin and iron uptake and cellular proliferation of erythroleukemia (K562) cells. Blood. 86:1995;3211-3219.
    • (1995) Blood , vol.86 , pp. 3211-3219
    • Richardson, D.R.1    Neumannova, V.2    Nagy, E.3    Ponka, P.4
  • 110
    • 0027104253 scopus 로고
    • Biochemistry of nitric oxide and its redox-activated forms
    • Stamler J.S., Singel D.J., Loscalzo J. Biochemistry of nitric oxide and its redox-activated forms. Science. 258:1992;1898-1902.
    • (1992) Science , vol.258 , pp. 1898-1902
    • Stamler, J.S.1    Singel, D.J.2    Loscalzo, J.3
  • 111
    • 0028132836 scopus 로고
    • Redox signaling: Nitrosylation and related target interactions of nitric oxide
    • Stamler J.S. Redox signaling: nitrosylation and related target interactions of nitric oxide. Cell. 78:1994;931-936.
    • (1994) Cell , vol.78 , pp. 931-936
    • Stamler, J.S.1
  • 112
    • 0342543576 scopus 로고    scopus 로고
    • Control of transferrin receptor and ferritin expression via nitric oxide (NO)-mediated degradation of IRP-2
    • Ponka P., Kim S. Control of transferrin receptor and ferritin expression via nitric oxide (NO)-mediated degradation of IRP-2. Nitric Oxide. 2:1998;104.
    • (1998) Nitric Oxide , vol.2 , pp. 104
    • Ponka, P.1    Kim, S.2
  • 113
    • 0030961083 scopus 로고    scopus 로고
    • Iron regulatory protein 1 is not required for the modulation of ferritin and transferrin receptor expression by iron in a murine pro-B lymphocyte cell line
    • Schalinske K.L., Blemings K.P., Steffen D.W., Chen O.S., Eisenstein R.S. Iron regulatory protein 1 is not required for the modulation of ferritin and transferrin receptor expression by iron in a murine pro-B lymphocyte cell line. Proceedings of the National Academy of Sciences USA. 94:1997;10,681-10,686.
    • (1997) Proceedings of the National Academy of Sciences USA , vol.94 , pp. 10
    • Schalinske, K.L.1    Blemings, K.P.2    Steffen, D.W.3    Chen, O.S.4    Eisenstein, R.S.5
  • 114
    • 0028799569 scopus 로고
    • Oxidative stress induces activation of a cytosolic protein responsible for control of iron uptake
    • Martins E.A., Robalinho R.L., Meneghini R. Oxidative stress induces activation of a cytosolic protein responsible for control of iron uptake. Archives of Biochemistry and Biophysics. 316:1995;128-134.
    • (1995) Archives of Biochemistry and Biophysics , vol.316 , pp. 128-134
    • Martins, E.A.1    Robalinho, R.L.2    Meneghini, R.3
  • 115
    • 0029055581 scopus 로고
    • Rapid responses to oxidative stress mediated by iron regulatory protein
    • Pantopoulos K., Hentze M.W. Rapid responses to oxidative stress mediated by iron regulatory protein. EMBO Journal. 14:1995;2917-2924.
    • (1995) EMBO Journal , vol.14 , pp. 2917-2924
    • Pantopoulos, K.1    Hentze, M.W.2
  • 120
    • 0019567178 scopus 로고
    • Specific membrane receptors for diferric-transferrin in cultured rat skeletal myocytes and chick-embryo cardiac myocytes
    • Fava R.A., Comeau R.D., Woodworth R.C. Specific membrane receptors for diferric-transferrin in cultured rat skeletal myocytes and chick-embryo cardiac myocytes. Bioscience Reports. 1:1981;377-385.
    • (1981) Bioscience Reports , vol.1 , pp. 377-385
    • Fava, R.A.1    Comeau, R.D.2    Woodworth, R.C.3
  • 121
  • 123
    • 0019975069 scopus 로고
    • Changes in cell surface antigen expression during hematopoietic differentiation
    • Siel C., Bicknell D., Cairne G., Robinson J., Lam G., Greaves M. Changes in cell surface antigen expression during hematopoietic differentiation. Blood. 60:1982;703-713.
    • (1982) Blood , vol.60 , pp. 703-713
    • Siel, C.1    Bicknell, D.2    Cairne, G.3    Robinson, J.4    Lam, G.5    Greaves, M.6
  • 124
    • 0021342268 scopus 로고
    • Expression of transferrin receptor on murine hematopoietic progenitors
    • Lesley J., Hyman R., Schulte R., Trotter J. Expression of transferrin receptor on murine hematopoietic progenitors. Cellular Immunology. 83:1984;14-25.
    • (1984) Cellular Immunology , vol.83 , pp. 14-25
    • Lesley, J.1    Hyman, R.2    Schulte, R.3    Trotter, J.4
  • 125
    • 0020354532 scopus 로고
    • Transferrin receptors and iron uptake during erythroid cell development
    • Iacopetta B.J., Morgan E.G., Yeoh G.C.T. Transferrin receptors and iron uptake during erythroid cell development. Biochimica et Biophysica Acta. 687:1982;204-210.
    • (1982) Biochimica et Biophysica Acta , vol.687 , pp. 204-210
    • Iacopetta, B.J.1    Morgan, E.G.2    Yeoh, G.C.T.3
  • 126
    • 0023019234 scopus 로고
    • Transferrin receptor number, synthesis, and endocytosis during erythropoietin-induced maturation of Friend virus-infected erythroid cells
    • Sawyer S.T., Krantz S.B. Transferrin receptor number, synthesis, and endocytosis during erythropoietin-induced maturation of Friend virus-infected erythroid cells. Journal of Biological Chemistry. 261:1986;9187-9195.
    • (1986) Journal of Biological Chemistry , vol.261 , pp. 9187-9195
    • Sawyer, S.T.1    Krantz, S.B.2
  • 128
    • 0017723977 scopus 로고
    • Inducibility of transferrin receptors of Friend erythroleukemia cells
    • Hu H.Y., Gardner J., Aisen P., Skoultchi A.I. Inducibility of transferrin receptors of Friend erythroleukemia cells. Science. 197:1977;559-561.
    • (1977) Science , vol.197 , pp. 559-561
    • Hu, H.Y.1    Gardner, J.2    Aisen, P.3    Skoultchi, A.I.4
  • 129
  • 130
    • 0023023013 scopus 로고
    • Control of heme synthesis during Friend cell differentiation: Role of iron and transferrin
    • Laskey J.D., Ponka P., Schulman H.M. Control of heme synthesis during Friend cell differentiation: role of iron and transferrin. Journal of Cellular Physiology. 129:1986;185-192.
    • (1986) Journal of Cellular Physiology , vol.129 , pp. 185-192
    • Laskey, J.D.1    Ponka, P.2    Schulman, H.M.3
  • 132
    • 0020687063 scopus 로고
    • Loss of the transferrin receptor during the maturation of sheep reticulocytes in vitro. An immunological approach
    • Pan B.T., Blostein R., Johnstone R.M. Loss of the transferrin receptor during the maturation of sheep reticulocytes in vitro. An immunological approach. Biochemical Journal. 210:1983;37-47.
    • (1983) Biochemical Journal , vol.210 , pp. 37-47
    • Pan, B.T.1    Blostein, R.2    Johnstone, R.M.3
  • 133
    • 0026691333 scopus 로고
    • GATA-binding transcription factors in hematopoietic cells
    • Orkin S.H. GATA-binding transcription factors in hematopoietic cells. Blood. 80:1992;575-581.
    • (1992) Blood , vol.80 , pp. 575-581
    • Orkin, S.H.1
  • 134
    • 4243652085 scopus 로고
    • Transcriptional regulation of the transferrin receptor gene in differentiating erythroid cells
    • Chan L-N.L., Shao J.Y. Transcriptional regulation of the transferrin receptor gene in differentiating erythroid cells. Blood. 82:1993;458a.
    • (1993) Blood , vol.82
    • Chan, L.-N.L.1    Shao, J.Y.2
  • 136
    • 0033566141 scopus 로고    scopus 로고
    • Gene expression in proliferating human erythroid cells
    • Gubin A.N., Njoroge J.M., Bouffard G.G., Miller J.L. Gene expression in proliferating human erythroid cells. Genomics. 59:1999;168-177.
    • (1999) Genomics , vol.59 , pp. 168-177
    • Gubin, A.N.1    Njoroge, J.M.2    Bouffard, G.G.3    Miller, J.L.4
  • 137
    • 0031018874 scopus 로고    scopus 로고
    • Regulation of cellular iron metabolism by erythropoietin: Activation of iron-regulatory protein and upregulation of transferrin receptor expression in erythroid cells
    • Weiss G., Houston T., Kastner S., Johrer K., Grunenwald K., Brock J.H. Regulation of cellular iron metabolism by erythropoietin: activation of iron-regulatory protein and upregulation of transferrin receptor expression in erythroid cells. Blood. 89:1997;680-687.
    • (1997) Blood , vol.89 , pp. 680-687
    • Weiss, G.1    Houston, T.2    Kastner, S.3    Johrer, K.4    Grunenwald, K.5    Brock, J.H.6
  • 138
    • 0343744222 scopus 로고    scopus 로고
    • Regulation of transferrin receptor expression in erythroid cells: Erythropoietin does not affect iron-regulatory proteins
    • Ponka P., Nagy E., Zhang A-S, Koury M.J. Regulation of transferrin receptor expression in erythroid cells: erythropoietin does not affect iron-regulatory proteins. Blood. 90:(1):1997;6a.
    • (1997) Blood , vol.90 , Issue.1
    • Ponka, P.1    Nagy, E.2    Zhang A-S3    Koury, M.J.4
  • 141
    • 0029130335 scopus 로고
    • Regulation of iron metabolism: Translational effects mediated by iron, heme and cytokines
    • Mascotti D.P., Rup D., Thach R.E. Regulation of iron metabolism: translational effects mediated by iron, heme and cytokines. Annual Review of Nutrition. 15:1995;239-261.
    • (1995) Annual Review of Nutrition , vol.15 , pp. 239-261
    • Mascotti, D.P.1    Rup, D.2    Thach, R.E.3
  • 144
    • 0027267128 scopus 로고
    • Expression and loss of the transferrin receptor in growing and differentiating HD3 cells
    • Grdisa M., Mathew A., Johnstone R.M. Expression and loss of the transferrin receptor in growing and differentiating HD3 cells. Journal of Cellular Physiology. 155:1993;349-357.
    • (1993) Journal of Cellular Physiology , vol.155 , pp. 349-357
    • Grdisa, M.1    Mathew, A.2    Johnstone, R.M.3
  • 145
    • 0025941184 scopus 로고
    • Intracellular heme coordinately modulates globin chain synthesis, transferrin receptor numbers, and ferritin content in differentiating Friend erythroleukemia cells
    • Battistini A., Coccia E-M., Marziali G., Bulgarini D., Scalzo S., Fiorucci G., Romeo G., Affabris E., Testa U., Rossi G.B., Peschle C. Intracellular heme coordinately modulates globin chain synthesis, transferrin receptor numbers, and ferritin content in differentiating Friend erythroleukemia cells. Blood. 78:1991;2098-2103.
    • (1991) Blood , vol.78 , pp. 2098-2103
    • Battistini, A.1    Coccia, E.-M.2    Marziali, G.3    Bulgarini, D.4    Scalzo, S.5    Fiorucci, G.6    Romeo, G.7    Affabris, E.8    Testa, U.9    Rossi, G.B.10    Peschle, C.11
  • 146
    • 0026584401 scopus 로고
    • Inhibition of heme synthesis decreases transferrin receptor expression in mouse erythroleukemia cells
    • Hradilek A., Fuchs O., Neuwirt J. Inhibition of heme synthesis decreases transferrin receptor expression in mouse erythroleukemia cells. Journal of Cellular Physiology. 150:1992;327-333.
    • (1992) Journal of Cellular Physiology , vol.150 , pp. 327-333
    • Hradilek, A.1    Fuchs, O.2    Neuwirt, J.3
  • 147
    • 0343744222 scopus 로고    scopus 로고
    • Role of heme in transferrin receptor expression in erythroid cells
    • Lok C.N., Ponka P. Role of heme in transferrin receptor expression in erythroid cells. Blood. 90:(1):1997;6a.
    • (1997) Blood , vol.90 , Issue.1
    • Lok, C.N.1    Ponka, P.2
  • 151
    • 0025766759 scopus 로고
    • Differential regulation of iron regulatory element-binding protein(s) in cell extracts of activated lymphocytes versus monocytes-macrophages
    • Testa U., Kühn L., Petrini M., Quaranta M.T., Pelosi E., Peschle C. Differential regulation of iron regulatory element-binding protein(s) in cell extracts of activated lymphocytes versus monocytes-macrophages. Journal of Biological Chemistry. 266:1991;3925-3930.
    • (1991) Journal of Biological Chemistry , vol.266 , pp. 3925-3930
    • Testa, U.1    Kühn, L.2    Petrini, M.3    Quaranta, M.T.4    Pelosi, E.5    Peschle, C.6
  • 152
    • 0021688127 scopus 로고
    • Expression of the transferrin receptor on murine peritoneal macrophages is modulated by in vitro treatment with interferon gamma
    • Hamilton T.A., Gray P.W., Adams D.O. Expression of the transferrin receptor on murine peritoneal macrophages is modulated by in vitro treatment with interferon gamma. Cellular Immunology. 89:1984;478-488.
    • (1984) Cellular Immunology , vol.89 , pp. 478-488
    • Hamilton, T.A.1    Gray, P.W.2    Adams, D.O.3
  • 153
    • 0024555386 scopus 로고
    • Interferon gamma-activated human monocytes downregulate transferrin receptors and inhibits the intracellular multiplication of Legionella pneumophila by limiting the availability of iron
    • Byrd T.F., Horowitz M.A. Interferon gamma-activated human monocytes downregulate transferrin receptors and inhibits the intracellular multiplication of Legionella pneumophila by limiting the availability of iron. Journal of Clinical Investigation. 83:1989;1457-1465.
    • (1989) Journal of Clinical Investigation , vol.83 , pp. 1457-1465
    • Byrd, T.F.1    Horowitz, M.A.2
  • 155
    • 0019412449 scopus 로고
    • Expression of transferrin receptors on mitogen-stimulated human peripheral blood lymphocytes: Relation to cellular activation and related metabolic events
    • Galbraith R.M., Galbraith G.M. Expression of transferrin receptors on mitogen-stimulated human peripheral blood lymphocytes: relation to cellular activation and related metabolic events. Immunology. 133:1983;703-710.
    • (1983) Immunology , vol.133 , pp. 703-710
    • Galbraith, R.M.1    Galbraith, G.M.2
  • 156
    • 0020961467 scopus 로고
    • Transferrin receptor induction in mitogen-stimulated human T lymphocytes is required for DNA synthesis and cell division and is regulated by interleukin 2
    • Neckers L.M., Cossman J. Transferrin receptor induction in mitogen-stimulated human T lymphocytes is required for DNA synthesis and cell division and is regulated by interleukin 2. Proceedings of the National Academy of Sciences USA. 80:1983;3494-3498.
    • (1983) Proceedings of the National Academy of Sciences USA , vol.80 , pp. 3494-3498
    • Neckers, L.M.1    Cossman, J.2
  • 157
    • 0021689209 scopus 로고
    • The role of the transferrin receptor in human B lymphocyte activation
    • Neckers L.M., Yenokida G., James S.P. The role of the transferrin receptor in human B lymphocyte activation. Journal of Immunology. 133:1984;2437-2441.
    • (1984) Journal of Immunology , vol.133 , pp. 2437-2441
    • Neckers, L.M.1    Yenokida, G.2    James, S.P.3
  • 159
    • 0026346929 scopus 로고
    • Post-transcriptional regulation of the transferrin receptor and 4F2 antigen heavy chain mRNA during growth activation of spleen cells
    • Teixeira S., Kühn L.C. Post-transcriptional regulation of the transferrin receptor and 4F2 antigen heavy chain mRNA during growth activation of spleen cells. European Journal of Biochemistry. 202:1991;819-826.
    • (1991) European Journal of Biochemistry , vol.202 , pp. 819-826
    • Teixeira, S.1    Kühn, L.C.2
  • 160
    • 0023234092 scopus 로고
    • Replacement of transferrin in serum-free cultures of mitogen-stimulated mouse lymphocytes by a lipophilic iron chelator
    • Brock J.H., Stevenson J. Replacement of transferrin in serum-free cultures of mitogen-stimulated mouse lymphocytes by a lipophilic iron chelator. Immunological Letters. 15:1987;23-25.
    • (1987) Immunological Letters , vol.15 , pp. 23-25
    • Brock, J.H.1    Stevenson, J.2
  • 161
    • 0023900767 scopus 로고
    • Evidence that transferrin supports cell proliferation by supplying iron for DNA synthesis
    • Laskey J., Webb I., Schulman H.M., Ponka P. Evidence that transferrin supports cell proliferation by supplying iron for DNA synthesis. Experimental Cell Research. 176:1988;87-95.
    • (1988) Experimental Cell Research , vol.176 , pp. 87-95
    • Laskey, J.1    Webb, I.2    Schulman, H.M.3    Ponka, P.4
  • 162
    • 0028027726 scopus 로고
    • Inhibition of proliferation and differentiation during early T cell development by anti-transferrin receptor antibody
    • Brekelmans P., van Soest P., Leenen P.J., van Ewijk W. Inhibition of proliferation and differentiation during early T cell development by anti-transferrin receptor antibody. European Journal of Immunology. 24:1994;2896-2902.
    • (1994) European Journal of Immunology , vol.24 , pp. 2896-2902
    • Brekelmans, P.1    Van Soest, P.2    Leenen, P.J.3    Van Ewijk, W.4
  • 163
    • 0022636575 scopus 로고
    • A transferrin receptor antibody represents one signal for the induction of IL 2 production by a human T cell line
    • Manger B., Weiss A., Hardy K.J., Stobo J.D. A transferrin receptor antibody represents one signal for the induction of IL 2 production by a human T cell line. Journal of Immunology. 136:1986;532-538.
    • (1986) Journal of Immunology , vol.136 , pp. 532-538
    • Manger, B.1    Weiss, A.2    Hardy, K.J.3    Stobo, J.D.4
  • 165
    • 0020956787 scopus 로고
    • Fate of the transferrin receptor during maturation of sheep reticulocytes in vitro: Selective externalization of the receptor
    • Pan B.T., Johnstone R.M. Fate of the transferrin receptor during maturation of sheep reticulocytes in vitro: selective externalization of the receptor. Cell. 33:1983;967-978.
    • (1983) Cell , vol.33 , pp. 967-978
    • Pan, B.T.1    Johnstone, R.M.2
  • 166
    • 0022201056 scopus 로고
    • Electron microscopic evidence for externalization of the transferrin receptor in vesicular form in sheep reticulocytes
    • Pan B.T., Teng K., Wu C., Adam M., Johnstone R.M. Electron microscopic evidence for externalization of the transferrin receptor in vesicular form in sheep reticulocytes. Journal of Cell Biology. 101:1985;942-948.
    • (1985) Journal of Cell Biology , vol.101 , pp. 942-948
    • Pan, B.T.1    Teng, K.2    Wu, C.3    Adam, M.4    Johnstone, R.M.5
  • 167
    • 0027190608 scopus 로고
    • Origin of a soluble truncated transferrin receptor
    • Ahn J., Johnstone R.M. Origin of a soluble truncated transferrin receptor. Blood. 81:1993;2442-2451.
    • (1993) Blood , vol.81 , pp. 2442-2451
    • Ahn, J.1    Johnstone, R.M.2
  • 168
    • 0029775046 scopus 로고    scopus 로고
    • Cleavage of the transferrin receptor by human granulocytes: Differential proteolysis of the exosome-bound TfR
    • Johnstone R.M. Cleavage of the transferrin receptor by human granulocytes: differential proteolysis of the exosome-bound TfR. Journal of Cellular Physiology. 168:1996;333-345.
    • (1996) Journal of Cellular Physiology , vol.168 , pp. 333-345
    • Johnstone, R.M.1
  • 171
    • 0031812848 scopus 로고    scopus 로고
    • Diagnostic utility of serum transferrin receptors measurement in assessing iron status
    • Ahluwalia N. Diagnostic utility of serum transferrin receptors measurement in assessing iron status. Nutritional Review. 56:1998;133-141.
    • (1998) Nutritional Review , vol.56 , pp. 133-141
    • Ahluwalia, N.1
  • 174
    • 0031605219 scopus 로고    scopus 로고
    • Transferrin, the transferrin receptor, and the uptake of iron by cells
    • S. Sigel, Sigel H. New York: Marcel Dekker Inc
    • Aisen P. Transferrin, the transferrin receptor, and the uptake of iron by cells. Sigel S., Sigel H. Metal Ions in Biological Systems. vol. 35:1998;585-631 Marcel Dekker Inc, New York.
    • (1998) Metal Ions in Biological Systems , vol.35 , pp. 585-631
    • Aisen, P.1
  • 175
    • 0005237820 scopus 로고
    • Erythroid cell iron metabolism and heme synthesis
    • P. Ponka, H.M. Schulman, & R.D. Woodworth. Boca Raton, Florida: CRC
    • Cox T.M., Ponka P., Schulman H.M. Erythroid cell iron metabolism and heme synthesis. Ponka P., Schulman H.M., Woodworth R.D. Iron Transport and Storage. 1990;163-279 CRC, Boca Raton, Florida.
    • (1990) Iron Transport and Storage , pp. 163-279
    • Cox, T.M.1    Ponka, P.2    Schulman, H.M.3
  • 177
    • 0033166453 scopus 로고    scopus 로고
    • A conserved RGD (Arg=Gly-Asp) motif in the transferrin receptor is required for binding to transferrin
    • Dubljevic V., Sali A., Goding J.W. A conserved RGD (Arg=Gly-Asp) motif in the transferrin receptor is required for binding to transferrin. Biochemical Journal. 341:1999;11-14.
    • (1999) Biochemical Journal , vol.341 , pp. 11-14
    • Dubljevic, V.1    Sali, A.2    Goding, J.W.3
  • 178
    • 0033605595 scopus 로고    scopus 로고
    • The hereditary hemochromatosis protein, HFE, specifically regulates transferrin-mediated iron uptake in HeLa cells
    • Roy C.N., Penny D.M., Feder J.N., Enns C.A. The hereditary hemochromatosis protein, HFE, specifically regulates transferrin-mediated iron uptake in HeLa cells. Journal of Biological Chemistry. 274:1999;9022-9028.
    • (1999) Journal of Biological Chemistry , vol.274 , pp. 9022-9028
    • Roy, C.N.1    Penny, D.M.2    Feder, J.N.3    Enns, C.A.4
  • 181
    • 0033529669 scopus 로고    scopus 로고
    • Rab15 mediates an early endocytic event in Chinese hamster ovary cells
    • Zuk P.A., Elferink L.A. Rab15 mediates an early endocytic event in Chinese hamster ovary cells. Journal of Biological Chemistry. 274:1999;22303-22312.
    • (1999) Journal of Biological Chemistry , vol.274 , pp. 22303-22312
    • Zuk, P.A.1    Elferink, L.A.2
  • 183
    • 0000655498 scopus 로고    scopus 로고
    • Identification of a hypoxia response element in the transferrin receptor gene
    • Lok C.N., Ponka P. Identification of a hypoxia response element in the transferrin receptor gene. Journal of Biological Chemistry. 274:1999;24147-24152.
    • (1999) Journal of Biological Chemistry , vol.274 , pp. 24147-24152
    • Lok, C.N.1    Ponka, P.2
  • 184
    • 0033548410 scopus 로고    scopus 로고
    • Increased expression of transferrin receptors and iron in amoeboid microglial cells in postnatal rats following an exposure to hypoxia
    • Kaur C., Ling E.A. Increased expression of transferrin receptors and iron in amoeboid microglial cells in postnatal rats following an exposure to hypoxia. Neuroscience Letters. 262:1999;183-186.
    • (1999) Neuroscience Letters , vol.262 , pp. 183-186
    • Kaur, C.1    Ling, E.A.2
  • 185
    • 0032746973 scopus 로고    scopus 로고
    • Control of transferrin receptor expression via nitric oxide-mediated modulation of iron-regulatory protein 2
    • in press
    • S. Kim, P. Ponka, Control of transferrin receptor expression via nitric oxide-mediated modulation of iron-regulatory protein 2, Journal of Biological Chemistry 274 (1999) in press.
    • (1999) Journal of Biological Chemistry , vol.274
    • Kim, S.1    Ponka, P.2


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