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Volumn 13, Issue 7, 2010, Pages 999-1009

Lysosomal proteolysis is the primary degradation pathway for cytosolic ferritin and cytosolic ferritin degradation is necessary for iron exit

Author keywords

[No Author keywords available]

Indexed keywords

CYTOSOLIC FERRITIN; FERRIC AMMONIUM CITRATE; FERRITIN; IRON; IRON BINDING PROTEIN; LEUPEPTIN; LYSOSOMAL PROTEASE; MITOCHONDRIAL FERRITIN; PROTEASOME; PROTEINASE; PROTEINASE INHIBITOR; UNCLASSIFIED DRUG;

EID: 77955871827     PISSN: 15230864     EISSN: None     Source Type: Journal    
DOI: 10.1089/ars.2010.3129     Document Type: Article
Times cited : (97)

References (55)
  • 3
    • 67349100157 scopus 로고    scopus 로고
    • Ferritins: A family of molecules for iron storage, antioxidation and more
    • Arosio P, Ingrassia R, and Cavadini P. Ferritins: A family of molecules for iron storage, antioxidation and more. Biochim Biophys Acta 1790: 589-599, 2009.
    • (2009) Biochim Biophys Acta , vol.1790 , pp. 589-599
    • Arosio, P.1    Ingrassia, R.2    Cavadini, P.3
  • 4
    • 0023162026 scopus 로고
    • Ascorbic acid inhibits lysosomal autophagy of ferritin
    • Bridges KR. Ascorbic acid inhibits lysosomal autophagy of ferritin. J Biol Chem 262: 14773-14778, 1987.
    • (1987) J Biol Chem , vol.262 , pp. 14773-14778
    • Bridges, K.R.1
  • 5
    • 34447629519 scopus 로고    scopus 로고
    • A novel deletion in the FTL gene causes hereditary hyperferritinemia cataract syndrome (HHCS) by alteration of the transcription start site
    • Burdon KP, Sharma S, Chen CS, Dimasi DP, Mackey DA, and Craig JE. A novel deletion in the FTL gene causes hereditary hyperferritinemia cataract syndrome (HHCS) by alteration of the transcription start site. Hum Mutat 28: 742, 2007.
    • (2007) Hum Mutat , vol.28 , pp. 742
    • Burdon, K.P.1    Sharma, S.2    Chen, C.S.3    Dimasi, D.P.4    MacKey, D.A.5    Craig, J.E.6
  • 8
    • 33747154110 scopus 로고    scopus 로고
    • Characterization of the l-ferritin variant 460InsA responsible of a hereditary ferritinopathy disorder
    • Cozzi A, Santambrogio P, Corsi B, Campanella A, Arosio P, and Levi S. Characterization of the l-ferritin variant 460InsA responsible of a hereditary ferritinopathy disorder. Neurobiol Dis 23: 644-652, 2006.
    • (2006) Neurobiol Dis , vol.23 , pp. 644-652
    • Cozzi, A.1    Santambrogio, P.2    Corsi, B.3    Campanella, A.4    Arosio, P.5    Levi, S.6
  • 9
    • 33751103909 scopus 로고    scopus 로고
    • Ferroportin-mediated mobilization of ferritin iron precedes ferritin degradation by the proteasome
    • Domenico ID, Vaughn MB, Li L, Bagley D, Musci G, Ward DM, and Kaplan J. Ferroportin-mediated mobilization of ferritin iron precedes ferritin degradation by the proteasome. EMBO J 25: 5396-5404, 2006.
    • (2006) EMBO J , vol.25 , pp. 5396-5404
    • Domenico, I.D.1    Vaughn, M.B.2    Li, L.3    Bagley, D.4    Musci, G.5    Ward, D.M.6    Kaplan, J.7
  • 10
    • 73349099034 scopus 로고    scopus 로고
    • Specific iron chela-tors determine the route of ferritin degradation
    • Domenico ID, Ward DM, and Kaplan J. Specific iron chela-tors determine the route of ferritin degradation. Blood 114: 4546-4551, 2009.
    • (2009) Blood , vol.114 , pp. 4546-4551
    • Domenico, I.D.1    Ward, D.M.2    Kaplan, J.3
  • 12
    • 0033826764 scopus 로고    scopus 로고
    • Iron regulatory proteins and the molecular control of mammalian iron metabolism
    • Eisenstein RS. Iron regulatory proteins and the molecular control of mammalian iron metabolism. Annu Rev Nutr 20: 627-662, 2000.
    • (2000) Annu Rev Nutr , vol.20 , pp. 627-662
    • Eisenstein, R.S.1
  • 13
    • 0036799489 scopus 로고    scopus 로고
    • The genetics of inherited sideroblastic anemias
    • Fleming MD. The genetics of inherited sideroblastic anemias. Semin Hematol 39: 270-281, 2002.
    • (2002) Semin Hematol , vol.39 , pp. 270-281
    • Fleming, M.D.1
  • 14
    • 0031455120 scopus 로고    scopus 로고
    • On the cytoprotec-tive role of ferritin in macrophages and its ability to enhance lysosomal stability
    • Garner B, Li W, Roberg K, and Brunk UT. On the cytoprotec-tive role of ferritin in macrophages and its ability to enhance lysosomal stability. Free Radical Research 27: 487-500, 1997.
    • (1997) Free Radical Research , vol.27 , pp. 487-500
    • Garner, B.1    Li, W.2    Roberg, K.3    Brunk, U.T.4
  • 15
    • 0031709850 scopus 로고    scopus 로고
    • Endogenous ferritin protects cells with iron-laden lysosomes against oxidative stress
    • Garner B, Roberg K, and Brunk UT. Endogenous ferritin protects cells with iron-laden lysosomes against oxidative stress. Free Radical Research 29: 103-114, 1998.
    • (1998) Free Radical Research , vol.29 , pp. 103-114
    • Garner, B.1    Roberg, K.2    Brunk, U.T.3
  • 16
    • 0028788201 scopus 로고
    • Molecular basis for the recently described hereditary hyperferritinemia-cataract syndrome: A mutation in the iron-responsive element of ferritin L-subunit gene (the "verona mutation")
    • Girelli D, Corrocher R, Bisceglia L, Olivieri O, De Franceschi L, Zelante L, and Gasparini P. Molecular basis for the recently described hereditary hyperferritinemia-cataract syndrome: A mutation in the iron-responsive element of ferritin L-subunit gene (the "Verona mutation"). Blood 86: 4050-4053, 1995.
    • (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
  • 17
    • 32944482461 scopus 로고    scopus 로고
    • Differential degradation of ferritin H-and L-chains: Accumulation of L-chain-rich ferritin in lens epithelial cells
    • Goralska M, Nagar S, Fleisher LN, and McGahan MC. Differential degradation of ferritin H-and L-chains: Accumulation of L-chain-rich ferritin in lens epithelial cells. Invest Ophthalmol Vis Sci 46: 3521-3529, 2005.
    • (2005) Invest Ophthalmol Vis Sci , vol.46 , pp. 3521-3529
    • Goralska, M.1    Nagar, S.2    Fleisher, L.N.3    McGahan, M.C.4
  • 18
    • 0030608152 scopus 로고    scopus 로고
    • The ferritins: Molecular properties, iron storage function and cellular regulation
    • Harrison PM and Arosio P. The ferritins: Molecular properties, iron storage function and cellular regulation. Biochim Biophys Acta 1275: 161-203, 1996.
    • (1996) Biochim Biophys Acta , vol.1275 , pp. 161-203
    • Harrison, P.M.1    Arosio, P.2
  • 19
    • 0016287813 scopus 로고
    • Ferritin iron uptake and release. Structure-function relationships
    • Harrison PM, Hoy TG, Macara IG, and Hoare RJ. Ferritin iron uptake and release. Structure-function relationships. Biochem J 143: 445-451, 1974.
    • (1974) Biochem J , vol.143 , pp. 445-451
    • Harrison, P.M.1    Hoy, T.G.2    MacAra, I.G.3    Hoare, R.J.4
  • 20
    • 33645553357 scopus 로고    scopus 로고
    • Hereditary hyperferritinemia cataract syndrome: Ocular, genetic, and biochemical findings
    • Ismail AR, Lachlan KL, Mumford AD, Temple IK, and Hodgkins PR. Hereditary hyperferritinemia cataract syndrome: Ocular, genetic, and biochemical findings. Eur J Ophthalmol 16: 153-160, 2006.
    • (2006) Eur J Ophthalmol , vol.16 , pp. 153-160
    • Ismail, A.R.1    Lachlan, K.L.2    Mumford, A.D.3    Temple, I.K.4    Hodgkins, P.R.5
  • 21
    • 0035954391 scopus 로고    scopus 로고
    • "Opening" the ferritin pore for iron release by mutation of conserved amino acids at interhelix and loop sites
    • Jin W, Takagi H, Pancorbo B, and Theil EC. "Opening" the ferritin pore for iron release by mutation of conserved amino acids at interhelix and loop sites. Biochemistry 40: 7525-7532, 2001.
    • (2001) Biochemistry , vol.40 , pp. 7525-7532
    • Jin, W.1    Takagi, H.2    Pancorbo, B.3    Theil, E.C.4
  • 23
    • 58149398237 scopus 로고    scopus 로고
    • Autophagy of HSP70 and chelation of lysosomal iron in a non-redox-active form
    • Kurz T and Brunk UT. Autophagy of HSP70 and chelation of lysosomal iron in a non-redox-active form. Autophagy 5: 93-95, 2009.
    • (2009) Autophagy , vol.5 , pp. 93-95
    • Kurz, T.1    Brunk, U.T.2
  • 24
    • 0037379680 scopus 로고    scopus 로고
    • Anthracyclines induce accumulation of iron in ferritin in myocardial and neoplastic cells: Inhibition of the ferritin iron mobilization pathway
    • Kwok JC and Richardson DR. Anthracyclines induce accumulation of iron in ferritin in myocardial and neoplastic cells: Inhibition of the ferritin iron mobilization pathway. Mol Pharmacol 63: 849-861, 2003.
    • (2003) Mol Pharmacol , vol.63 , pp. 849-861
    • Kwok, J.C.1    Richardson, D.R.2
  • 25
    • 1642576976 scopus 로고    scopus 로고
    • Examination of the mecha-nism(s) involved in doxorubicin-mediated iron accumulation in ferritin: Studies using metabolic inhibitors, protein synthesis inhibitors, and lysosomotropic agents
    • Kwok JC and Richardson DR. Examination of the mecha-nism(s) involved in doxorubicin-mediated iron accumulation in ferritin: Studies using metabolic inhibitors, protein synthesis inhibitors, and lysosomotropic agents. Mol Pharmacol 65: 181-195, 2004.
    • (2004) Mol Pharmacol , vol.65 , pp. 181-195
    • Kwok, J.C.1    Richardson, D.R.2
  • 26
    • 0032189348 scopus 로고    scopus 로고
    • Proteasome inhibitors: Valuable new tools for cell biologists
    • Lee DH and Goldberg AL. Proteasome inhibitors: Valuable new tools for cell biologists. Trends Cell Biol 8: 397-403, 1998.
    • (1998) Trends Cell Biol , vol.8 , pp. 397-403
    • Lee, D.H.1    Goldberg, A.L.2
  • 27
    • 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 EA and Munro HN. 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 USA 85: 2171-2175, 1988.
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 2171-2175
    • Leibold, E.A.1    Munro, H.N.2
  • 30
    • 15244339209 scopus 로고    scopus 로고
    • Ferritins: Dynamic management of biological iron and oxygen chemistry
    • Liu X and Theil EC. Ferritins: Dynamic management of biological iron and oxygen chemistry. Acc Chem Res 38: 167-175, 2005.
    • (2005) Acc Chem Res , vol.38 , pp. 167-175
    • Liu, X.1    Theil, E.C.2
  • 31
    • 67650229951 scopus 로고    scopus 로고
    • Overexpression of mitochondrial fer-ritin sensitizes cells to oxidative stress via an iron-mediated mechanism
    • Lu Z, Nie G, Li Y, Soe-Lin S, Tao Y, Cao Y, Zhang Z, Liu N, Ponka P, and Zhao B. Overexpression of mitochondrial fer-ritin sensitizes cells to oxidative stress via an iron-mediated mechanism. Antioxid Redox Signal 11: 1791-1803, 2009.
    • (2009) Antioxid Redox Signal , vol.11 , pp. 1791-1803
    • Lu, Z.1    Nie, G.2    Li, Y.3    Soe-Lin, S.4    Tao, Y.5    Cao, Y.6    Zhang, Z.7    Liu, N.8    Ponka, P.9    Zhao, B.10
  • 33
    • 10644232372 scopus 로고    scopus 로고
    • Oxidation-induced ferritin turnover in microglial cells: Role of proteasome
    • Mehlhase J, Sandig G, Pantopoulos K, and Grune T. Oxidation-induced ferritin turnover in microglial cells: role of proteasome. Free Radic Biol Med 38: 276-285, 2005.
    • (2005) Free Radic Biol Med , vol.38 , pp. 276-285
    • Mehlhase, J.1    Sandig, G.2    Pantopoulos, K.3    Grune, T.4
  • 34
    • 0032513215 scopus 로고    scopus 로고
    • Pro-teasome inhibitors activate stress kinases and induce Hsp72. Diverse effects on apoptosis
    • Meriin A, Gabai V, Yaglom J, Shifrin V, and Sherman M. Pro-teasome inhibitors activate stress kinases and induce Hsp72. Diverse effects on apoptosis. J Biol Chem 273: 6373, 1998.
    • (1998) J Biol Chem , vol.273 , pp. 6373
    • Meriin, A.1    Gabai, V.2    Yaglom, J.3    Shifrin, V.4    Sherman, M.5
  • 35
    • 0032736896 scopus 로고    scopus 로고
    • Post-transcriptional control via iron-responsive elements: The impact of aberrations in hereditary disease
    • Mikulits W, Schranzhofer M, Beug H, and Mullner EW. Post-transcriptional control via iron-responsive elements: The impact of aberrations in hereditary disease. Mutat Res 437: 219-230, 1999.
    • (1999) Mutat Res , vol.437 , pp. 219-230
    • Mikulits, W.1    Schranzhofer, M.2    Beug, H.3    Mullner, E.W.4
  • 36
    • 33749334487 scopus 로고    scopus 로고
    • In vivo tumor growth is inhibited by cytosolic iron deprivation caused by the expression of mitochondrial ferritin
    • Nie G, Chen G, Sheftel AD, Pantopoulos K, and Ponka P. In vivo tumor growth is inhibited by cytosolic iron deprivation caused by the expression of mitochondrial ferritin. Blood 108: 2428-2434, 2006.
    • (2006) Blood , vol.108 , pp. 2428-2434
    • Nie, G.1    Chen, G.2    Sheftel, A.D.3    Pantopoulos, K.4    Ponka, P.5
  • 37
    • 14944358625 scopus 로고    scopus 로고
    • Overexpression of mitochondrial ferritin causes cytosolic iron depletion and changes cellular iron homeostasis
    • Nie G, Sheftel AD, Kim SF, and Ponka P. Overexpression of mitochondrial ferritin causes cytosolic iron depletion and changes cellular iron homeostasis. Blood 105: 2161-2167, 2005.
    • (2005) Blood , vol.105 , pp. 2161-2167
    • Nie, G.1    Sheftel, A.D.2    Kim, S.F.3    Ponka, P.4
  • 38
    • 0031370708 scopus 로고    scopus 로고
    • Starvation-induced autophagocytosis paradoxically decreases the susceptibility to oxidative stress of the extremely oxidative stress-sensitive NIT insulinoma cells
    • Olejnicka BT, Dalen H, Baranowski MM, and Brunk UT. Starvation-induced autophagocytosis paradoxically decreases the susceptibility to oxidative stress of the extremely oxidative stress-sensitive NIT insulinoma cells. Redox Rep 3: 311-318, 1997.
    • (1997) Redox Rep , vol.3 , pp. 311-318
    • Olejnicka, B.T.1    Dalen, H.2    Baranowski, M.M.3    Brunk, U.T.4
  • 39
    • 0035057746 scopus 로고    scopus 로고
    • Novel cellular defenses against iron and oxidation: Ferritin and autophago-cytosis preserve lysosomal stability in airway epithelium
    • Persson HL, Nilsson KJ, and Brunk UT. Novel cellular defenses against iron and oxidation: Ferritin and autophago-cytosis preserve lysosomal stability in airway epithelium. Redox Report 6: 57-63, 2001.
    • (2001) Redox Report , vol.6 , pp. 57-63
    • Persson, H.L.1    Nilsson, K.J.2    Brunk, U.T.3
  • 40
    • 0018798539 scopus 로고
    • A study of intracellular iron metabolism using pyridoxal iso-nicotinoyl hydrazone and other synthetic chelating agents
    • Ponka P, Borova J, Neuwirt J, Fuchs O, and Necas E. A study of intracellular iron metabolism using pyridoxal iso-nicotinoyl hydrazone and other synthetic chelating agents. Biochim Biophys Acta 586: 278-297, 1979.
    • (1979) Biochim Biophys Acta , vol.586 , pp. 278-297
    • Ponka, P.1    Borova, J.2    Neuwirt, J.3    Fuchs, O.4    Necas, E.5
  • 41
    • 0030895693 scopus 로고    scopus 로고
    • Can ferritin provide iron for hemoglobin synthesis?
    • Ponka P and Richardson DR. Can ferritin provide iron for hemoglobin synthesis? Blood 89: 2611-2613, 1997.
    • (1997) Blood , vol.89 , pp. 2611-2613
    • Ponka, P.1    Richardson, D.R.2
  • 42
    • 0022406630 scopus 로고
    • Acquisition of iron from transferrin regulates reticulocyte heme synthesis
    • Ponka P and Schulman HM. Acquisition of iron from transferrin regulates reticulocyte heme synthesis. J Biol Chem 260: 14717-14721, 1985.
    • (1985) J Biol Chem , vol.260 , pp. 14717-14721
    • Ponka, P.1    Schulman, H.M.2
  • 43
    • 0032533549 scopus 로고    scopus 로고
    • Iron in cytosolic ferritin can be recycled through lysosomal degradation in human fibro-blasts
    • Radisky DC and Kaplan J. Iron in cytosolic ferritin can be recycled through lysosomal degradation in human fibro-blasts. Biochem J 336: 201-205, 1998.
    • (1998) Biochem J , vol.336 , pp. 201-205
    • Radisky, D.C.1    Kaplan, J.2
  • 44
    • 0029865751 scopus 로고    scopus 로고
    • Distribution of iron in reticulocytes after inhibition of heme synthesis with suc-cinylacetone: Examination of the intermediates involved in iron metabolism
    • Richardson DR, Ponka P, and Vyoral D. Distribution of iron in reticulocytes after inhibition of heme synthesis with suc-cinylacetone: Examination of the intermediates involved in iron metabolism. Blood 87: 3477-3488, 1996.
    • (1996) Blood , vol.87 , pp. 3477-3488
    • Richardson, D.R.1    Ponka, P.2    Vyoral, D.3
  • 45
    • 0024238392 scopus 로고
    • Ferritin iron kinetics and protein turnover in K562 cells
    • Roberts S and Bomford A. Ferritin iron kinetics and protein turnover in K562 cells. J Biol Chem 263: 19181-19187, 1988.
    • (1988) J Biol Chem , vol.263 , pp. 19181-19187
    • Roberts, S.1    Bomford, A.2
  • 46
    • 33750363298 scopus 로고    scopus 로고
    • The roles of intracellular protein-degradation pathways in neurodegeneration
    • Rubinsztein DC. The roles of intracellular protein-degradation pathways in neurodegeneration. Nature 443: 780-786, 2006.
    • (2006) Nature , vol.443 , pp. 780-786
    • Rubinsztein, D.C.1
  • 47
    • 0033938488 scopus 로고    scopus 로고
    • Ferritin oxidation in vitro: Implication of iron release and degradation by the 20S proteasome
    • Rudeck M, Volk T, Sitte N, and Grune T. Ferritin oxidation in vitro: Implication of iron release and degradation by the 20S proteasome. IUBMB Life 49: 451-456, 2000.
    • (2000) IUBMB Life , vol.49 , pp. 451-456
    • Rudeck, M.1    Volk, T.2    Sitte, N.3    Grune, T.4
  • 48
    • 0027198736 scopus 로고
    • Production and characterization of recombinant heteropolymers of human ferritin H and L chains
    • Santambrogio P, Levi S, Cozzi A, Rovida E, Albertini A, and Arosio P. Production and characterization of recombinant heteropolymers of human ferritin H and L chains. J Biol Chem 268: 12744-12748, 1993.
    • (1993) J Biol Chem , vol.268 , pp. 12744-12748
    • Santambrogio, P.1    Levi, S.2    Cozzi, A.3    Rovida, E.4    Albertini, A.5    Arosio, P.6
  • 49
    • 34347375300 scopus 로고    scopus 로고
    • Direct interorganellar transfer of iron from endosome to mitochondrion
    • Sheftel AD, Zhang AS, Brown C, Shirihai OS, and Ponka P. Direct interorganellar transfer of iron from endosome to mitochondrion. Blood 110: 125-132, 2007.
    • (2007) Blood , vol.110 , pp. 125-132
    • Sheftel, A.D.1    Zhang, A.S.2    Brown, C.3    Shirihai, O.S.4    Ponka, P.5
  • 50
    • 0032563119 scopus 로고    scopus 로고
    • Localized unfolding at the junction of three ferritin subunits. A mechanism for iron release?
    • Takagi H, Shi D, Ha Y, Allewell NM, and Theil EC. Localized unfolding at the junction of three ferritin subunits. A mechanism for iron release? J Biol Chem 273: 18685-18688, 1998.
    • (1998) J Biol Chem , vol.273 , pp. 18685-18688
    • Takagi, H.1    Shi, D.2    Ha, Y.3    Allewell, N.M.4    Theil, E.C.5
  • 51
    • 0037093202 scopus 로고    scopus 로고
    • Regulation of ferritin genes and protein
    • Torti FM and Torti SV. Regulation of ferritin genes and protein. Blood 99: 3505-3516, 2002.
    • (2002) Blood , vol.99 , pp. 3505-3516
    • Torti, F.M.1    Torti, S.V.2
  • 52
    • 0035966122 scopus 로고    scopus 로고
    • Iron prevents ferri-tin turnover in hepatic cells
    • Truty J, Malpe R, and Linder MC. Iron prevents ferri-tin turnover in hepatic cells. J Biol Chem 276: 48775-48780, 2001.
    • (2001) J Biol Chem , vol.276 , pp. 48775-48780
    • Truty, J.1    Malpe, R.2    Linder, M.C.3
  • 53
    • 0032557816 scopus 로고    scopus 로고
    • Iron transport in K562 cells: A kinetic study using native gel electrophoresis and 59Fe autoradi-ography
    • Vyoral D and Petrak J. Iron transport in K562 cells: A kinetic study using native gel electrophoresis and 59Fe autoradi-ography. Biochim Biophys Acta 1403: 179-188, 1998.
    • (1998) Biochim Biophys Acta , vol.1403 , pp. 179-188
    • Vyoral, D.1    Petrak, J.2
  • 54
    • 0347579854 scopus 로고    scopus 로고
    • Expressed sequence tag analysis of adult human lens for the NEIBank Project: Over 2000 non-redundant transcripts, novel genes and splice variants
    • Wistow G, Bernstein SL, Wyatt MK, Behal A, Touchman JW, Bouffard G, Smith D, and Peterson K. Expressed sequence tag analysis of adult human lens for the NEIBank Project: over 2000 non-redundant transcripts, novel genes and splice variants. Mol Vis 8: 171-184, 2002. (Pubitemid 36153607)
    • (2002) Molecular Vision , vol.8 , pp. 171-184
    • Wistow, G.1    Bernstein, S.L.2    Wyatt, M.K.3    Behal, A.4    Touchman, J.W.5    Bouffard, G.6    Smith, D.7    Peterson, K.8


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