메뉴 건너뛰기




Volumn 31, Issue 10, 1999, Pages 1139-1152

Iron-regulatory proteins, iron-responsive elements and ferritin mRNA translation

Author keywords

Ferritin; Iron regulatory proteins; Iron responsive element; Posttranscriptional regulation; RNA binding proteins

Indexed keywords

CYTOKINE; ERYTHROPOIETIN; IRON REGULATORY FACTOR; LIOTHYRONINE; LYMPHOKINE; MESSENGER RNA; NITRIC OXIDE; RNA BINDING PROTEIN; TRANSFERRIN; TRANSFERRIN RECEPTOR;

EID: 0032878232     PISSN: 13572725     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1357-2725(99)00080-1     Document Type: Article
Times cited : (196)

References (61)
  • 1
    • 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
  • 2
    • 0025823445 scopus 로고
    • Transferrin receptors promote formation of clathrin lattices
    • Miller K., Shipman M., Trowbridge I.S., Hopkins C.R. Transferrin receptors promote formation of clathrin lattices. Cell. 65:1991;621-631.
    • (1991) Cell , vol.65 , pp. 621-631
    • Miller, K.1    Shipman, M.2    Trowbridge, I.S.3    Hopkins, C.R.4
  • 3
    • 0032530340 scopus 로고    scopus 로고
    • Iron is hot: An update on the pathophysiology of hemachromatosis
    • Andrews N.C., Levy J. Iron is hot: an update on the pathophysiology of hemachromatosis. Blood. 92:1998;1845-1851.
    • (1998) Blood , vol.92 , pp. 1845-1851
    • Andrews, N.C.1    Levy, J.2
  • 5
    • 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
  • 6
    • 0031605379 scopus 로고    scopus 로고
    • Iron-responsive element (IRE) family of mRNA regulators. Regulation of iron transport and uptake in animals, plants and microorganisms
    • Theil E.C. Iron-responsive element (IRE) family of mRNA regulators. Regulation of iron transport and uptake in animals, plants and microorganisms. Metal Ions in Biological Systems. 35:1998;403-434.
    • (1998) Metal Ions in Biological Systems , vol.35 , pp. 403-434
    • Theil, E.C.1
  • 7
    • 0032103264 scopus 로고    scopus 로고
    • Iron-regulatory protein-1 (IRP-1) is highly conserved in two invertebrate species. Characterisation of IRP-1 homologues in Drosophila melanogaster and Caenorhabditis elegans
    • Muckenthaler M., Gunkel N., Frishman D., Cyrklaff A., Tomancak P., Hentze M.W. Iron-regulatory protein-1 (IRP-1) is highly conserved in two invertebrate species. Characterisation of IRP-1 homologues in Drosophila melanogaster and Caenorhabditis elegans. European Journal of Biochemistry. 254:1998;230-237.
    • (1998) European Journal of Biochemistry , vol.254 , pp. 230-237
    • Muckenthaler, M.1    Gunkel, N.2    Frishman, D.3    Cyrklaff, A.4    Tomancak, P.5    Hentze, M.W.6
  • 8
    • 0025811624 scopus 로고
    • Human erythroid 5-aminolevulinate synthase: Promotor analysis and identification of an iron-responsive element in the mRNA
    • Cox T.C., Bawden M.J., Martin A., May B.K. Human erythroid 5-aminolevulinate synthase: promotor analysis and identification of an iron-responsive element in the mRNA. The EMBO Journal. 10:1991;1891-1892.
    • (1991) The EMBO Journal , vol.10 , pp. 1891-1892
    • Cox, T.C.1    Bawden, M.J.2    Martin, A.3    May, B.K.4
  • 10
    • 0029557688 scopus 로고
    • Succinate dehydrogenase b mRNA of Drosophila melanogaster has a functional iron-responsive element in its 5′-untranslated region
    • Kohler S.A., Henderson B.R., Kühn L.C. Succinate dehydrogenase b mRNA of Drosophila melanogaster has a functional iron-responsive element in its 5′-untranslated region. The Journal of Biological Chemistry. 270:1995;30,781-30,786.
    • (1995) The Journal of Biological Chemistry , vol.270 , pp. 30
    • Kohler, S.A.1    Henderson, B.R.2    Kühn, L.C.3
  • 11
    • 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
  • 12
    • 0029927715 scopus 로고    scopus 로고
    • Differential regulation of IRP1 and IRP2 by nitric oxide in rat hepatoma cells
    • Phillips J.D., Kinikini D.V., Yu Y., Guo B., Leibold E.A. Differential regulation of IRP1 and IRP2 by nitric oxide in rat hepatoma cells. Blood. 87:1996;2983-2992.
    • (1996) Blood , vol.87 , pp. 2983-2992
    • Phillips, J.D.1    Kinikini, D.V.2    Yu, Y.3    Guo, B.4    Leibold, E.A.5
  • 14
    • 0032571304 scopus 로고    scopus 로고
    • Regulation of iron regulatory protein 1 during hypoxia and hypoxia/reoxygenation
    • Hanson E.S., Leibold E.A. Regulation of iron regulatory protein 1 during hypoxia and hypoxia/reoxygenation. The Journal of Biological Chemistry. 273:1998;7588-7593.
    • (1998) The Journal of Biological Chemistry , vol.273 , pp. 7588-7593
    • Hanson, E.S.1    Leibold, E.A.2
  • 15
    • 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., Jöhrer K., Grünewald 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    Jöhrer, K.4    Grünewald, K.5    Brock, J.H.6
  • 16
    • 0030820438 scopus 로고    scopus 로고
    • Unidirectional upregulation of the synthesis of the major iron proteins, transferrin-receptor and ferritin, in HepG2 cells by the acute-phase protein α1-antitrypsin
    • Graziadei I., Weiss G., Bohm A., Werner-Felmayer G., Vogel W. Unidirectional upregulation of the synthesis of the major iron proteins, transferrin-receptor and ferritin, in HepG2 cells by the acute-phase protein α1-antitrypsin. Journal of Hepatology. 27:1997;716-725.
    • (1997) Journal of Hepatology , vol.27 , pp. 716-725
    • Graziadei, I.1    Weiss, G.2    Bohm, A.3    Werner-Felmayer, G.4    Vogel, W.5
  • 17
    • 0029914953 scopus 로고    scopus 로고
    • Phosphorylation and activation of both iron regulatory proteins 1 and 2 in HL-60 cells
    • Schalinske K.L., Eisenstein R.S. Phosphorylation and activation of both iron regulatory proteins 1 and 2 in HL-60 cells. The Journal of Biological Chemistry. 271:1996;7168-7176.
    • (1996) The Journal of Biological Chemistry , vol.271 , pp. 7168-7176
    • Schalinske, K.L.1    Eisenstein, R.S.2
  • 18
    • 15844363742 scopus 로고    scopus 로고
    • Thyroid hormone modulates the interaction between iron regulatory proteins and the ferritin mRNA iron-responsive element
    • Leedman P.J., Stein A.R., Chin W.W., Rogers J.T. Thyroid hormone modulates the interaction between iron regulatory proteins and the ferritin mRNA iron-responsive element. The Journal of Biological Chemistry. 271:1996;12,017-12,023.
    • (1996) The Journal of Biological Chemistry , vol.271 , pp. 12
    • Leedman, P.J.1    Stein, A.R.2    Chin, W.W.3    Rogers, J.T.4
  • 20
    • 0026729483 scopus 로고
    • Position is the determinant for function of the iron-responsive elements as translational enhancers
    • Goossen B., Hentze M.W. Position is the determinant for function of the iron-responsive elements as translational enhancers. Molecular and Cellular Biology. 12:1992;1959-1966.
    • (1992) Molecular and Cellular Biology , vol.12 , pp. 1959-1966
    • Goossen, B.1    Hentze, M.W.2
  • 21
    • 0030731419 scopus 로고    scopus 로고
    • Starting at the beginning, middle, and end: Translation initiation in eukaryotes
    • Sachs A.B., Sarnow P., Hentze M.W. Starting at the beginning, middle, and end: translation initiation in eukaryotes. Cell. 89:1997;831-838.
    • (1997) Cell , vol.89 , pp. 831-838
    • Sachs, A.B.1    Sarnow, P.2    Hentze, M.W.3
  • 22
    • 0032160381 scopus 로고    scopus 로고
    • IRP1 binding to ferritin mRNA prevents the recruitment of small ribosomal subunit by the cap-binding complex
    • Muckenthaler M., Gray N.K., Hentze M.W. IRP1 binding to ferritin mRNA prevents the recruitment of small ribosomal subunit by the cap-binding complex. Molecular Cell. 2:1998;383-388.
    • (1998) Molecular Cell , vol.2 , pp. 383-388
    • Muckenthaler, M.1    Gray, N.K.2    Hentze, M.W.3
  • 23
    • 0031869508 scopus 로고    scopus 로고
    • Translational activation of uncapped mRNAs by the central part of human eIF4G is 5′ end-dependent
    • De Gregorio E., Preiss T., Hentze M.W. Translational activation of uncapped mRNAs by the central part of human eIF4G is 5′ end-dependent. RNA. 4:1998;828-836.
    • (1998) RNA , vol.4 , pp. 828-836
    • De Gregorio, E.1    Preiss, T.2    Hentze, M.W.3
  • 24
    • 0029960279 scopus 로고    scopus 로고
    • Ferritin translation by interleukin-1 and interleukin-6: The role of sequences upstream of the start codons of the heavy and light subunit genes
    • Rogers J.T. Ferritin translation by interleukin-1 and interleukin-6: the role of sequences upstream of the start codons of the heavy and light subunit genes. Blood. 87:1996;2525-2537.
    • (1996) Blood , vol.87 , pp. 2525-2537
    • Rogers, J.T.1
  • 25
    • 0029861968 scopus 로고    scopus 로고
    • A model of the iron responsive element RNA hairpin loop structure determined from NMR and thermodynamic data
    • Laing L.G., Hall K.B. A model of the iron responsive element RNA hairpin loop structure determined from NMR and thermodynamic data. Biochemistry. 35:1996;13,586-13,596.
    • (1996) Biochemistry , vol.35 , pp. 13
    • Laing, L.G.1    Hall, K.B.2
  • 27
    • 0031917173 scopus 로고    scopus 로고
    • Translational regulation of mRNAs with distinct IRE sequences by iron regulatory proteins 1 and 2
    • Menotti E., Henderson B.R., Kühn L.C. Translational regulation of mRNAs with distinct IRE sequences by iron regulatory proteins 1 and 2. The Journal of Biological Chemistry. 273:1998;1821-1824.
    • (1998) The Journal of Biological Chemistry , vol.273 , pp. 1821-1824
    • Menotti, E.1    Henderson, B.R.2    Kühn, L.C.3
  • 28
    • 0028788201 scopus 로고
    • Molecular basis for recently described hereditary hyperferritinemia-cataract syndrome: A mutation in the iron-responsive element of ferritin 1-subunit gene (the "verona Mutation")
    • Girelli D., Corrocher R., Bisceglia L., Olivieri O., De Franceschi L., Zelante L., Gasparini P. Molecular basis for recently described hereditary hyperferritinemia-cataract syndrome: a mutation in the iron-responsive element of ferritin 1-subunit gene (the "Verona Mutation"). Blood. 86:1995;4050-4053.
    • (1995) Blood , vol.86 , pp. 4050-4053
    • Girelli, D.1    Corrocher, R.2    Bisceglia, L.3    Olivieri, O.4    De Franceschi, L.5    Zelante, L.6    Gasparini, P.7
  • 29
    • 0032508548 scopus 로고    scopus 로고
    • Loops and bulge/loops in iron-responsive element isoforms influence iron regulatory protein binding
    • Ke Y., Wu J., Leibold E.A., Walden W.E., Theil E. Loops and bulge/loops in iron-responsive element isoforms influence iron regulatory protein binding. The Journal of Biological Chemistry. 273:1998;23,637-23,640.
    • (1998) The Journal of Biological Chemistry , vol.273 , pp. 23
    • Ke, Y.1    Wu, J.2    Leibold, E.A.3    Walden, W.E.4    Theil, E.5
  • 31
    • 0031033691 scopus 로고    scopus 로고
    • The aconitase family: Three structural variations on a common theme
    • Gruer M.J., Artymiuk P.J., Guest J.R. The aconitase family: three structural variations on a common theme. Trends in Biochemistry. 22:1997;3-6.
    • (1997) Trends in Biochemistry , vol.22 , pp. 3-6
    • Gruer, M.J.1    Artymiuk, P.J.2    Guest, J.R.3
  • 32
    • 0030600134 scopus 로고    scopus 로고
    • Iron-sulphur clusters as genetic regulatory switches: The bifunctional iron regulatory protein-1
    • Paraskeva E., Hentze M.W. Iron-sulphur clusters as genetic regulatory switches: the bifunctional iron regulatory protein-1. FEBS Letters. 389:1996;40-43.
    • (1996) FEBS Letters , vol.389 , pp. 40-43
    • Paraskeva, E.1    Hentze, M.W.2
  • 34
    • 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., Steffen D.W., Chen O.S., Eisenstein R. 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.2    Steffen, D.W.3    Chen, O.S.4    Eisenstein, R.5
  • 36
    • 0028009430 scopus 로고
    • Mutational analysis of the [4Fe-4S]-cluster converting iron-regulatory factor from its RNA-binding form to cytoplasmic aconitase
    • Hirling H., Henderson B.R., Kühn L.C. Mutational analysis of the [4Fe-4S]-cluster converting iron-regulatory factor from its RNA-binding form to cytoplasmic aconitase. The EMBO Journal. 13:1994;453-461.
    • (1994) The EMBO Journal , vol.13 , pp. 453-461
    • Hirling, H.1    Henderson, B.R.2    Kühn, L.C.3
  • 37
    • 0026511260 scopus 로고
    • Modulation of the RNA-binding activity of a regulatory protein by iron in vitro: Switching between enzymatic and genetic function?
    • Constable A., Quick S., Gray N.K., Hentze M.W. Modulation of the RNA-binding activity of a regulatory protein by iron in vitro: switching between enzymatic and genetic function? Proceedings of the National Academy of Sciences USA. 89:1992;4554-4558.
    • (1992) Proceedings of the National Academy of Sciences USA , vol.89 , pp. 4554-4558
    • Constable, A.1    Quick, S.2    Gray, N.K.3    Hentze, M.W.4
  • 39
    • 0031002851 scopus 로고    scopus 로고
    • The iron-sulfur cluster of iron regulatory protein 1 modulates the accessibility of RNA binding and phosphorylation sites
    • Schalinske K.L., Anderson S.A., Tuazon P.T., Chen O.S., Kennedy M.C., Eisenstein R.S. The iron-sulfur cluster of iron regulatory protein 1 modulates the accessibility of RNA binding and phosphorylation sites. Biochemistry. 36:1997;3950-3958.
    • (1997) Biochemistry , vol.36 , pp. 3950-3958
    • Schalinske, K.L.1    Anderson, S.A.2    Tuazon, P.T.3    Chen, O.S.4    Kennedy, M.C.5    Eisenstein, R.S.6
  • 42
    • 0345408097 scopus 로고
    • Translational control of mRNAs coding for both heavy and light subunits of ferritin in rat hepatoma cells is regulated by chelateable intracellular iron pools
    • Rogers J.T., Munro H.N. Translational control of mRNAs coding for both heavy and light subunits of ferritin in rat hepatoma cells is regulated by chelateable intracellular iron pools. Proceedings of the National Academy of Sciences USA. 84:1987;2277-2281.
    • (1987) Proceedings of the National Academy of Sciences USA , vol.84 , pp. 2277-2281
    • Rogers, J.T.1    Munro, H.N.2
  • 43
    • 0026976944 scopus 로고
    • Subunit structure and transmembrane signalling of the erythropoietin receptor
    • Showers M.O., D'Andrea A.D. Subunit structure and transmembrane signalling of the erythropoietin receptor. International Review of Cytology. 137B:1992;99-120.
    • (1992) International Review of Cytology , vol.137 , pp. 99-120
    • Showers, M.O.1    D'Andrea, A.D.2
  • 44
    • 0031068834 scopus 로고    scopus 로고
    • The role of nitric oxide in the regulation of cellular iron metabolism
    • Domachowske J.B. The role of nitric oxide in the regulation of cellular iron metabolism. Biochemical and Molecular Medicine. 60:1997;1-7.
    • (1997) Biochemical and Molecular Medicine , vol.60 , pp. 1-7
    • Domachowske, J.B.1
  • 47
    • 0344911532 scopus 로고    scopus 로고
    • Iron and gene expression: Molecular mechanisms regulating cellular iron homeostasis
    • Kühn L.C. Iron and gene expression: molecular mechanisms regulating cellular iron homeostasis. Nutrition Reviews. 56:1998;S11-S19.
    • (1998) Nutrition Reviews , vol.56
    • Kühn, L.C.1
  • 48
    • 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. The EMBO Journal. 14:1995;2917-2924.
    • (1995) The EMBO Journal , vol.14 , pp. 2917-2924
    • Pantopoulos, K.1    Hentze, M.W.2
  • 49
    • 0028131454 scopus 로고
    • Iron regulates cytoplasmic levels of a novel iron-responsive element binding protein without aconitase activity
    • Guo B., Yu Y., Leibold E. Iron regulates cytoplasmic levels of a novel iron-responsive element binding protein without aconitase activity. The Journal of Biological Chemistry. 269:1994;24,252-24,260.
    • (1994) The Journal of Biological Chemistry , vol.269 , pp. 24
    • Guo, B.1    Yu, Y.2    Leibold, E.3
  • 50
    • 0027717217 scopus 로고
    • Characterisation of a second RNA-binding protein in rodents with specificity for iron responsive elements
    • Henderson B.R., Seiser C., Kühn L.C. Characterisation of a second RNA-binding protein in rodents with specificity for iron responsive elements. The Journal of Biological Chemistry. 268:1993;27,327-27,334.
    • (1993) The Journal of Biological Chemistry , vol.268 , pp. 27
    • Henderson, B.R.1    Seiser, C.2    Kühn, L.C.3
  • 51
    • 0028143071 scopus 로고
    • Molecular characterisation of a second iron-responsive element binding protein, iron-regulatory protein 2
    • Samaniego F., Chin J., Iwai K., Roualt T.A., Klausner R.D. Molecular characterisation of a second iron-responsive element binding protein, iron-regulatory protein 2. The Journal of Biological Chemistry. 269:1994;30,904-30,910.
    • (1994) The Journal of Biological Chemistry , vol.269 , pp. 30
    • Samaniego, F.1    Chin, J.2    Iwai, K.3    Roualt, T.A.4    Klausner, R.D.5
  • 52
    • 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. The EMBO Journal. 14:1995;5350-5357.
    • (1995) The EMBO Journal , vol.14 , pp. 5350-5357
    • Iwai, K.1    Klausner, R.D.2    Rouault, T.A.3
  • 54
    • 0028982262 scopus 로고
    • Iron regulates the intracellular degradation of iron-regulatory protein 2 by the proteosome
    • Guo B., Phillips J.D., Yu T., Leibold E.A. Iron regulates the intracellular degradation of iron-regulatory protein 2 by the proteosome. The Journal of Biological Chemistry. 270:1995;21,645-21,651.
    • (1995) The Journal of Biological Chemistry , vol.270 , pp. 21
    • Guo, B.1    Phillips, J.D.2    Yu, T.3    Leibold, E.A.4
  • 55
    • 0024360593 scopus 로고
    • Chromosomal localisation of nucleic acid-binding proteins by affinity mapping: Assignment of the IRE-binding protein gene to human chromosome 9
    • Hentze M.W., Seuanez H.N., O'Brien S.J., Harford J.B., Klausner R.D. Chromosomal localisation of nucleic acid-binding proteins by affinity mapping: assignment of the IRE-binding protein gene to human chromosome 9. Nucleic Acids Research. 17:1989;6103-6108.
    • (1989) Nucleic Acids Research , vol.17 , pp. 6103-6108
    • Hentze, M.W.1    Seuanez, H.N.2    O'Brien, S.J.3    Harford, J.B.4    Klausner, R.D.5
  • 56
    • 85052903769 scopus 로고
    • Genetic regulation of the iron transport and storage genes: Links with acute phase response
    • R.B. Lauffer. Boca Raton: CRC Press
    • Rogers J.T. Genetic regulation of the iron transport and storage genes: links with acute phase response. Lauffer R.B. Iron and human disease. 1992;78-104 CRC Press, Boca Raton.
    • (1992) Iron and Human Disease , pp. 78-104
    • Rogers, J.T.1
  • 61
    • 0028302350 scopus 로고
    • Translational enhancement of H-ferritin mRNA by interleukin-1β acts through 5′-leader sequences distinct from the iron-responsive element
    • Rogers J.T., Andriotakis J., Lacroix L., Kasschau K., Durmowicz G., Bridges K. Translational enhancement of H-ferritin mRNA by interleukin-1β acts through 5′-leader sequences distinct from the iron-responsive element. Nucleic Acids Research. 22:1994;2678-2686.
    • (1994) Nucleic Acids Research , vol.22 , pp. 2678-2686
    • Rogers, J.T.1    Andriotakis, J.2    Lacroix, L.3    Kasschau, K.4    Durmowicz, G.5    Bridges, K.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.