메뉴 건너뛰기




Volumn 429, Issue 3, 2010, Pages 463-471

Ferritin does not donate its iron for haem synthesis in macrophages

Author keywords

Aminolevulinic acid; Ferritin; Haem synthesis; Iron metabolism

Indexed keywords

5-AMINOLAEVULINIC ACID; AMINOLEVULINIC ACID; ERYTHROID CELLS; FERRITIN; HAEM SYNTHESIS; IRON METABOLISM; METABOLIC FUNCTION; MURINE MACROPHAGES; SINGLE CELLS;

EID: 77955082503     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20100346     Document Type: Article
Times cited : (8)

References (51)
  • 1
    • 37549059612 scopus 로고    scopus 로고
    • Regulation of iron acquisition and storage: Consequences for iron-linked disorders
    • De Domenico, I., McVey Ward, D. and Kaplan, J. (2008) Regulation of iron acquisition and storage: consequences for iron-linked disorders. Nat. Rev. Mol. Cell Biol. 9, 72-81
    • (2008) Nat. Rev. Mol. Cell Biol. , vol.9 , pp. 72-81
    • De Domenico, I.1    McVey Ward, D.2    Kaplan, J.3
  • 2
    • 0031567095 scopus 로고    scopus 로고
    • The molecular mechanisms of the metabolism and transport of iron in normal and neoplastic cells
    • Richardson, D. R. and Ponka, P. (1997) The molecular mechanisms of the metabolism and transport of iron in normal and neoplastic cells. Biochim. Biophys. Acta 1331, 1-40
    • (1997) Biochim. Biophys. Acta , vol.1331 , pp. 1-40
    • Richardson, D.R.1    Ponka, P.2
  • 3
    • 0036569986 scopus 로고    scopus 로고
    • Molecular bases of cellular iron toxicity
    • Eaton, J. W. and Qian, M. (2002) Molecular bases of cellular iron toxicity. Free Radical Biol. Med. 32, 833-840
    • (2002) Free Radical Biol. Med. , vol.32 , pp. 833-840
    • Eaton, J.W.1    Qian, M.2
  • 4
    • 0037101879 scopus 로고    scopus 로고
    • Ferritin, iron homeostasis, and oxidative damage
    • Arosio, P. and Levi, S. (2002) Ferritin, iron homeostasis, and oxidative damage. Free Radical Biol. Med. 33, 457-463
    • (2002) Free Radical Biol. Med. , vol.33 , pp. 457-463
    • Arosio, P.1    Levi, S.2
  • 5
    • 0030608152 scopus 로고    scopus 로고
    • The ferritins: Molecular properties, iron storage function and cellular regulation
    • Harrison, P. M. and Arosio, P. (1996) The ferritins: molecular properties, iron storage function and cellular regulation. Biochim. Biophys. Acta 1275, 161-203
    • (1996) Biochim. Biophys. Acta , vol.1275 , pp. 161-203
    • Harrison, P.M.1    Arosio, P.2
  • 8
    • 0000010870 scopus 로고
    • Relation of ferritin iron to heme synthesis in marrow and reticulocytes
    • Mazur, A. and Carleton, A. (1963) Relation of ferritin iron to heme synthesis in marrow and reticulocytes. J. Biol. Chem. 238, 1817-1824
    • (1963) J. Biol. Chem. , vol.238 , pp. 1817-1824
    • Mazur, A.1    Carleton, A.2
  • 9
    • 0018100135 scopus 로고
    • Mobilization of iron from the plasma membrane of the murine reticulocyte. The role of ferritin
    • Nunez, M. T., Glass, J. and Robinson, S. H. (1978) Mobilization of iron from the plasma membrane of the murine reticulocyte. The role of ferritin. Biochim. Biophys. Acta 509, 170-180
    • (1978) Biochim. Biophys. Acta , vol.509 , pp. 170-180
    • Nunez, M.T.1    Glass, J.2    Robinson, S.H.3
  • 11
    • 0030854921 scopus 로고    scopus 로고
    • Utilization of intracellular ferritin iron for hemoglobin synthesis in developing human erythroid precursors
    • Vaisman, B., Fibach, E. and Konijn, A. M. (1997) Utilization of intracellular ferritin iron for hemoglobin synthesis in developing human erythroid precursors. Blood 90, 831-838
    • (1997) Blood , vol.90 , pp. 831-838
    • Vaisman, B.1    Fibach, E.2    Konijn, A.M.3
  • 12
    • 0015893042 scopus 로고
    • Study of intracellular iron distribution in rabbit reticulocytes with normal and inhibited heme synthesis
    • Borova, J., Ponka, P. and Neuwirt, J. (1973) Study of intracellular iron distribution in rabbit reticulocytes with normal and inhibited heme synthesis. Biochim. Biophys. Acta 320, 143-156
    • (1973) Biochim. Biophys. Acta , vol.320 , pp. 143-156
    • Borova, J.1    Ponka, P.2    Neuwirt, J.3
  • 13
    • 0030895693 scopus 로고    scopus 로고
    • Can ferritin provide iron for hemoglobin synthesis?
    • Ponka, P. and Richardson, D. R. (1997) Can ferritin provide iron for hemoglobin synthesis? Blood 89, 2611-2613
    • (1997) Blood , vol.89 , pp. 2611-2613
    • Ponka, P.1    Richardson, D.R.2
  • 14
    • 0024329963 scopus 로고
    • The effects of inhibition of heme synthesis on the intracellular localization of iron in rat reticulocytes
    • Adams, M. L., Ostapiuk, I. and Grasso, J. A. (1989) The effects of inhibition of heme synthesis on the intracellular localization of iron in rat reticulocytes. Biochim. Biophys. Acta 1012, 243-253
    • (1989) Biochim. Biophys. Acta , vol.1012 , pp. 243-253
    • Adams, M.L.1    Ostapiuk, I.2    Grasso, J.A.3
  • 15
    • 0021324643 scopus 로고
    • Ferritin is not a required intermediate for iron utilization in heme synthesis
    • Grasso, J. A., Hillis, T. J. and Mooney-Frank, J. A. (1984) Ferritin is not a required intermediate for iron utilization in heme synthesis. Biochim. Biophys. Acta 797, 247-255
    • (1984) Biochim. Biophys. Acta , vol.797 , pp. 247-255
    • Grasso, J.A.1    Hillis, T.J.2    Mooney-Frank, J.A.3
  • 16
    • 0020050144 scopus 로고
    • Iron utilization in rabbit reticulocytes. A study using succinylacetone as an inhibitor or heme synthesis
    • Ponka, P., Wilczynska, A. and Schulman, H. M. (1982) Iron utilization in rabbit reticulocytes. A study using succinylacetone as an inhibitor or heme synthesis. Biochim. Biophys. Acta 720, 96-105
    • (1982) Biochim. Biophys. Acta , vol.720 , pp. 96-105
    • Ponka, P.1    Wilczynska, A.2    Schulman, H.M.3
  • 17
    • 0014310585 scopus 로고
    • Studies on the partition of iron in bone marrow cells
    • Primosigh, J. V. and Thomas, E. D. (1968) Studies on the partition of iron in bone marrow cells. J. Clin. Invest. 47, 1473-1482
    • (1968) J. Clin. Invest. , vol.47 , pp. 1473-1482
    • Primosigh, J.V.1    Thomas, E.D.2
  • 18
    • 0029865751 scopus 로고    scopus 로고
    • Distribution of iron in reticulocytes after inhibition of heme synthesis with succinylacetone: Examination of the intermediates involved in iron metabolism
    • Richardson, D. R., Ponka, P. and Vyoral, D. (1996) Distribution of iron in reticulocytes after inhibition of heme synthesis with succinylacetone: examination of the intermediates involved in iron metabolism. Blood 87, 3477-3488 (Pubitemid 26115381)
    • (1996) Blood , vol.87 , Issue.8 , pp. 3477-3488
    • Richardson, D.R.1    Ponka, P.2    Vyoral, D.3
  • 19
    • 0016266968 scopus 로고
    • The mechanism of iron exchange between synthetic iron chelators and rabbit reticulocytes
    • Hemmaplardh, D. and Morgan, E. H. (1974) The mechanism of iron exchange between synthetic iron chelators and rabbit reticulocytes. Biochim. Biophys. Acta 373, 84-99
    • (1974) Biochim. Biophys. Acta , vol.373 , pp. 84-99
    • Hemmaplardh, D.1    Morgan, E.H.2
  • 20
    • 11144226961 scopus 로고    scopus 로고
    • Intracellular kinetics of iron in reticulocytes: Evidence for endosome involvement in iron targeting to mitochondria
    • Zhang, A. S., Sheftel, A. D. and Ponka, P. (2005) Intracellular kinetics of iron in reticulocytes: evidence for endosome involvement in iron targeting to mitochondria. Blood 105, 368-375
    • (2005) Blood , vol.105 , pp. 368-375
    • Zhang, A.S.1    Sheftel, A.D.2    Ponka, P.3
  • 21
    • 34347375300 scopus 로고    scopus 로고
    • Direct interorganellar transfer of iron from endosome to mitochondrion
    • DOI 10.1182/blood-2007-01-068148
    • Sheftel, A. D., Zhang, A. S., Brown, C., Shirihai, O. S. and Ponka, P. (2007) Direct interorganellar transfer of iron from endosome to mitochondrion. Blood 110, 125-132 (Pubitemid 47026827)
    • (2007) Blood , vol.110 , Issue.1 , pp. 125-132
    • Sheftel, A.D.1    Zhang, A.-S.2    Brown, C.3    Shirihai, O.S.4    Ponka, P.5
  • 22
    • 0030060705 scopus 로고    scopus 로고
    • Overexpression of the ferritin H subunit in cultured erythroid cells changes the intracellular iron distribution
    • Picard, V., Renaudie, F., Porcher, C., Hentze, M. W., Grandchamp, B. and Beaumont, C. (1996) Overexpression of the ferritin H subunit in cultured erythroid cells changes the intracellular iron distribution. Blood 87, 2057-2064
    • (1996) Blood , vol.87 , pp. 2057-2064
    • Picard, V.1    Renaudie, F.2    Porcher, C.3    Hentze, M.W.4    Grandchamp, B.5    Beaumont, C.6
  • 23
    • 70349237065 scopus 로고    scopus 로고
    • Conditional deletion of ferritin H in mice induces loss of iron storage and liver damage
    • Darshan, D., Vanoaica, L., Richman, L., Beermann, F. and Kühn, L.C. (2009) Conditional deletion of ferritin H in mice induces loss of iron storage and liver damage. Hepatology 50, 852-860
    • (2009) Hepatology , vol.50 , pp. 852-860
    • Darshan, D.1    Vanoaica, L.2    Richman, L.3    Beermann, F.4    Kühn, L.C.5
  • 25
    • 33748102856 scopus 로고    scopus 로고
    • Hepcidin: A peptide hormone at the interface of innate immunity and iron metabolism
    • Ganz, T. (2006) Hepcidin: a peptide hormone at the interface of innate immunity and iron metabolism. Curr. Top. Microbiol. Immunol. 306, 183-198
    • (2006) Curr. Top. Microbiol. Immunol. , vol.306 , pp. 183-198
    • Ganz, T.1
  • 26
    • 0034733635 scopus 로고    scopus 로고
    • A novel mammalian iron-regulated protein involved in intracellular iron metabolism
    • Abboud, S. and Haile, D. J. (2000) A novel mammalian iron-regulated protein involved in intracellular iron metabolism. J. Biol. Chem. 275, 19906-19912
    • (2000) J. Biol. Chem. , vol.275 , pp. 19906-19912
    • Abboud, S.1    Haile, D.J.2
  • 28
    • 10844258104 scopus 로고    scopus 로고
    • Hepcidin regulates cellular iron efflux by binding to ferroportin and inducing its internalization
    • DOI 10.1126/science.1104742
    • Nemeth, E., Tuttle, M. S., Powelson, J., Vaughn, M. B., Donovan, A., Ward, D. M., Ganz, T. and Kaplan, J. (2004) Hepcidin regulates cellular iron efflux by binding to ferroportin and inducing its internalization. Science 306, 2090-2093 (Pubitemid 40007660)
    • (2004) Science , vol.306 , Issue.5704 , pp. 2090-2093
    • Nemeth, E.1    Tuttle, M.S.2    Powelson, J.3    Vaughn, M.D.4    Donovan, A.5    Ward, D.M.6    Ganz, T.7    Kaplan, J.8
  • 29
    • 0037125975 scopus 로고    scopus 로고
    • Nitrogen monoxide-mediated control of ferritin synthesis: Implications for macrophage iron homeostasis
    • Kim, S. and Ponka, P. (2002) Nitrogen monoxide-mediated control of ferritin synthesis: implications for macrophage iron homeostasis. Proc. Natl. Acad. Sci. U.S.A. 99, 12214-12219
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 12214-12219
    • Kim, S.1    Ponka, P.2
  • 30
    • 33746691267 scopus 로고    scopus 로고
    • Iron regulatory protein-independent regulation of ferritin synthesis by nitrogen monoxide
    • Mikhael, M., Kim, S. F., Schranzhofer, M., Soe-Lin, S., Sheftel, A. D., Mullner, E. W. and Ponka, P. (2006) Iron regulatory protein-independent regulation of ferritin synthesis by nitrogen monoxide. FEBS J. 273, 3828-3836
    • (2006) FEBS J. , vol.273 , pp. 3828-3836
    • Mikhael, M.1    Kim, S.F.2    Schranzhofer, M.3    Soe-Lin, S.4    Sheftel, A.D.5    Mullner, E.W.6    Ponka, P.7
  • 31
    • 0016221446 scopus 로고
    • Storage iron kinetics. VII. A biologic model for reticuloendothelial iron transport
    • Fillet, G., Cook, J. D. and Finch, C. A. (1974) Storage iron kinetics. VII. A biologic model for reticuloendothelial iron transport. J. Clin. Invest. 53, 1527-1533
    • (1974) J. Clin. Invest. , vol.53 , pp. 1527-1533
    • Fillet, G.1    Cook, J.D.2    Finch, C.A.3
  • 32
    • 0033511832 scopus 로고    scopus 로고
    • Cell biology of heme
    • Ponka, P. (1999) Cell biology of heme. Am. J. Med. Sci. 318, 241-256
    • (1999) Am. J. Med. Sci. , vol.318 , pp. 241-256
    • Ponka, P.1
  • 34
    • 33751103909 scopus 로고    scopus 로고
    • Ferroportin-mediated mobilization of ferritin iron precedes ferritin degradation by the proteasome
    • DOI 10.1038/sj.emboj.7601409, PII 7601409
    • De Domenico, I., Vaughn, M. B., Li, L., Bagley, D., Musci, G., Ward, D. M. and Kaplan, J. (2006) Ferroportin-mediated mobilization of ferritin iron precedes ferritin degradation by the proteasome. EMBO J. 25, 5396-5404 (Pubitemid 44764148)
    • (2006) EMBO Journal , vol.25 , Issue.22 , pp. 5396-5404
    • De Domenico, I.1    Vaughn, M.B.2    Li, L.3    Bagley, D.4    Musci, G.5    Ward, D.M.6    Kaplan, J.7
  • 35
    • 0015518342 scopus 로고
    • The kinetics of iron and transferrin incorporation into rabbit erythroid cells and the nature of stromal-bound iron
    • Martinez-Medellin, J. and Schulman, H. M. (1972) The kinetics of iron and transferrin incorporation into rabbit erythroid cells and the nature of stromal-bound iron. Biochim. Biophys. Acta 264, 272-274
    • (1972) Biochim. Biophys. Acta , vol.264 , pp. 272-274
    • Martinez-Medellin, J.1    Schulman, H.M.2
  • 36
    • 0022406630 scopus 로고
    • Acquisition of iron from transferrin regulates reticulocyte heme synthesis
    • Ponka, P. and Schulman, H. M. (1985) Acquisition of iron from transferrin regulates reticulocyte heme synthesis. J. Biol. Chem. 260, 14717-14721
    • (1985) J. Biol. Chem. , vol.260 , pp. 14717-14721
    • Ponka, P.1    Schulman, H.M.2
  • 37
    • 0018798539 scopus 로고
    • A study of intracellular iron metabolism using pyridoxal isonicotinoyl hydrazone and other synthetic chelating agents
    • Ponka, P., Borova, J., Neuwirt, J., Fuchs, O. and Necas, E. (1979) A study of intracellular iron metabolism using pyridoxal isonicotinoyl hydrazone and other synthetic chelating agents. Biochim. Biophys. Acta 586, 278-297
    • (1979) Biochim. Biophys. Acta , vol.586 , pp. 278-297
    • Ponka, P.1    Borova, J.2    Neuwirt, J.3    Fuchs, O.4    Necas, E.5
  • 38
    • 0024365045 scopus 로고
    • A specific mRNA binding factor regulates the iron-dependent stability of cytoplasmic transferrin receptor mRNA
    • Mullner, E. W., Neupert, B. and Kuhn, L. C. (1989) A specific mRNA binding factor regulates the iron-dependent stability of cytoplasmic transferrin receptor mRNA. Cell 58, 373-382
    • (1989) Cell , vol.58 , pp. 373-382
    • Mullner, E.W.1    Neupert, B.2    Kuhn, L.C.3
  • 39
    • 47149095786 scopus 로고    scopus 로고
    • Nramp1 equips macrophages for efficient iron recycling
    • Soe-Lin, S., Sheftel, A. D., Wasyluk, B. and Ponka, P. (2008) Nramp1 equips macrophages for efficient iron recycling. Exp. Hematol. 36, 929-937
    • (2008) Exp. Hematol. , vol.36 , pp. 929-937
    • Soe-Lin, S.1    Sheftel, A.D.2    Wasyluk, B.3    Ponka, P.4
  • 41
    • 0015939503 scopus 로고
    • The use of exogenous δ-aminolevulinic acid for the studies of the regulation of haem synthesis in rabbit reticulocytes
    • Ponka, P., Neuwirt, J. and Borova, J. (1973) The use of exogenous δ-aminolevulinic acid for the studies of the regulation of haem synthesis in rabbit reticulocytes. Biochim. Biophys. Acta 304, 123-131
    • (1973) Biochim. Biophys. Acta , vol.304 , pp. 123-131
    • Ponka, P.1    Neuwirt, J.2    Borova, J.3
  • 42
    • 28844432578 scopus 로고    scopus 로고
    • The heme oxygenase system: Update 2005
    • Maines, M. D. (2005) The heme oxygenase system: update 2005. Antioxid. Redox Signaling 7, 1761-1766
    • (2005) Antioxid. Redox Signaling , vol.7 , pp. 1761-1766
    • Maines, M.D.1
  • 43
    • 0024121621 scopus 로고
    • Cytoplasmic protein binds in vitro to a highly conserved sequence in the 5′ untranslated region of ferritin heavy- and light-subunit mRNAs
    • Leibold, E. A. and Munro, H. N. (1988) Cytoplasmic protein binds in vitro to a highly conserved sequence in the 5′ untranslated region of ferritin heavy- and light-subunit mRNAs. Proc. Natl. Acad. Sci. U.S.A. 85, 2171-2175
    • (1988) Proc. Natl. Acad. Sci. U.S.A. , vol.85 , pp. 2171-2175
    • Leibold, E.A.1    Munro, H.N.2
  • 44
    • 0024369974 scopus 로고
    • Purification of a specific repressor of ferritin mRNA translation from rabbit liver
    • Walden, W. E., Patino, M. M. and Gaffield, L. (1989) Purification of a specific repressor of ferritin mRNA translation from rabbit liver. J. Biol. Chem. 264, 13765-13769
    • (1989) J. Biol. Chem. , vol.264 , pp. 13765-13769
    • Walden, W.E.1    Patino, M.M.2    Gaffield, L.3
  • 45
    • 0032524657 scopus 로고    scopus 로고
    • Involvement of heme in the degradation of iron-regulatory protein 2
    • Goessling, L. S., Mascotti, D. P. and Thach, R. E. (1998) Involvement of heme in the degradation of iron-regulatory protein 2. J. Biol. Chem. 273, 12555-12557
    • (1998) J. Biol. Chem. , vol.273 , pp. 12555-12557
    • Goessling, L.S.1    Mascotti, D.P.2    Thach, R.E.3
  • 46
    • 0031438147 scopus 로고    scopus 로고
    • Haem precursor delta-aminolaevulinic acid induces activation of the cytosolic iron regulatory protein 1
    • Carvalho, H., Bechara, E. J., Meneghini, R. and Demasi, M. (1997) Haem precursor delta-aminolaevulinic acid induces activation of the cytosolic iron regulatory protein 1. Biochem. J. 328, 827-832
    • (1997) Biochem. J. , vol.328 , pp. 827-832
    • Carvalho, H.1    Bechara, E.J.2    Meneghini, R.3    Demasi, M.4
  • 48
    • 33748370752 scopus 로고    scopus 로고
    • Ferritins: Iron/oxygen biominerals in protein nanocages
    • Theil, E. C., Matzapetakis, M. and Liu, X. (2006) Ferritins: iron/oxygen biominerals in protein nanocages. J. Biol. Inorg. Chem. 11, 803-810
    • (2006) J. Biol. Inorg. Chem. , vol.11 , pp. 803-810
    • Theil, E.C.1    Matzapetakis, M.2    Liu, X.3
  • 49
    • 34249857235 scopus 로고    scopus 로고
    • Non-heme induction of heme oxygenase-1 does not alter cellular iron metabolism
    • Sheftel, A. D., Kim, S. F. and Ponka, P. (2007) Non-heme induction of heme oxygenase-1 does not alter cellular iron metabolism. J. Biol. Chem. 282, 10480-10486
    • (2007) J. Biol. Chem. , vol.282 , pp. 10480-10486
    • Sheftel, A.D.1    Kim, S.F.2    Ponka, P.3
  • 50
    • 61349203895 scopus 로고    scopus 로고
    • The power plant of the cell is also a smithy: The emerging role of mitochondria in cellular iron homeostasis
    • Sheftel, A. D. and Lill, R. (2009) The power plant of the cell is also a smithy: the emerging role of mitochondria in cellular iron homeostasis. Ann. Med. 41, 82-99
    • (2009) Ann. Med. , vol.41 , pp. 82-99
    • Sheftel, A.D.1    Lill, R.2
  • 51
    • 33947192111 scopus 로고    scopus 로고
    • Erythropoietin and iron-restricted erythropoiesis
    • Goodnough, L. T. (2007) Erythropoietin and iron-restricted erythropoiesis. Exp. Hematol. 35, 167-172
    • (2007) Exp. Hematol. , vol.35 , pp. 167-172
    • Goodnough, L.T.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.