메뉴 건너뛰기




Volumn 50, Issue 11, 2011, Pages 1647-1658

Cell sensitivity to oxidative stress is influenced by ferritin autophagy

Author keywords

Apoptosis; Autophagy; Ferritin; Free radicals; Lysosomes; Oxidative stress; Redox active iron

Indexed keywords

APOFERRITIN; CALCEIN; FERRITIN; HYDROGEN PEROXIDE; IRON;

EID: 79955588367     PISSN: 08915849     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.freeradbiomed.2011.03.014     Document Type: Article
Times cited : (66)

References (96)
  • 1
    • 0020362998 scopus 로고
    • The role of superoxide and hydroxyl radicals in phospholipid peroxidation catalysed by iron salts
    • DOI 10.1016/0014-5793(82)80788-6
    • J.M. Gutteridge The role of superoxide and hydroxyl radicals in phospholipid peroxidation catalysed by iron salts FEBS Lett. 150 1982 454 458 (Pubitemid 13184089)
    • (1982) FEBS Letters , vol.150 , Issue.2 , pp. 454-458
    • Gutteridge, J.M.C.1
  • 2
    • 0001951589 scopus 로고    scopus 로고
    • The chemistry of free radicals and related 'reactive species'
    • B. Halliwell, and J.M.C. Gutteridge The chemistry of free radicals and related 'reactive species' B. Halliwell, J.M.C. Gutteridge, Free Radicals in Biology and Medicine 2003 Oxford Univ. Press Oxford 36 104
    • (2003) Free Radicals in Biology and Medicine , pp. 36-104
    • Halliwell, B.1    Gutteridge, J.M.C.2
  • 3
    • 0036569986 scopus 로고    scopus 로고
    • Molecular bases of cellular iron toxicity
    • DOI 10.1016/S0891-5849(02)00772-4, PII S0891584902007724
    • J.W. Eaton, and M. Qian Molecular bases of cellular iron toxicity Free Radic. Biol. Med. 32 2002 833 840 (Pubitemid 34439254)
    • (2002) Free Radical Biology and Medicine , vol.32 , Issue.9 , pp. 833-840
    • Eaton, J.W.1    Qian, M.2
  • 4
    • 0030608152 scopus 로고    scopus 로고
    • The ferritins: Molecular properties, iron storage function and cellular regulation
    • DOI 10.1016/0005-2728(96)00022-9
    • P.M. Harrison, and P. Arosio The ferritins: molecular properties, iron storage function and cellular regulation Biochim. Biophys. Acta 1275 1996 161 203 (Pubitemid 26248989)
    • (1996) Biochimica et Biophysica Acta - Bioenergetics , vol.1275 , Issue.3 , pp. 161-203
    • Harrison, P.M.1    Arosio, P.2
  • 5
    • 33645048994 scopus 로고    scopus 로고
    • Cellular regulation and molecular interactions of the ferritins
    • K.J. Hintze, and E.C. Theil Cellular regulation and molecular interactions of the ferritins Cell. Mol. Life Sci. 63 2006 591 600
    • (2006) Cell. Mol. Life Sci. , vol.63 , pp. 591-600
    • Hintze, K.J.1    Theil, E.C.2
  • 6
    • 0037093202 scopus 로고    scopus 로고
    • Regulation of ferritin genes and protein
    • DOI 10.1182/blood.V99.10.3505
    • F.M. Torti, and S.V. Torti Regulation of ferritin genes and protein Blood 99 2002 3505 3516 (Pubitemid 34534516)
    • (2002) Blood , vol.99 , Issue.10 , pp. 3505-3516
    • Torti, F.M.1    Torti, S.V.2
  • 7
    • 34249686049 scopus 로고    scopus 로고
    • Ferritin and ferritin isoforms I: Structure-function relationships, synthesis, degradation and secretion
    • DOI 10.1080/13813450701318583, PII 779015334
    • A.M. Koorts, and M. Viljoen Ferritin and ferritin isoforms. I. Structure-function relationships, synthesis, degradation and secretion Arch. Physiol. Biochem. 113 2007 30 54 (Pubitemid 46825687)
    • (2007) Archives of Physiology and Biochemistry , vol.113 , Issue.1 , pp. 30-54
    • Koorts, A.M.1    Viljoen, M.2
  • 9
    • 0018236898 scopus 로고
    • Ferritin: Structure, biosynthesis, and role in iron metabolism
    • H.N. Munro, and M.C. Linder Ferritin: structure, biosynthesis, and role in iron metabolism Physiol. Rev. 58 1978 317 396 (Pubitemid 9097033)
    • (1978) Physiological Reviews , vol.58 , Issue.2 , pp. 317-396
    • Munro, H.N.1    Linder, M.C.2
  • 10
    • 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
    • I. De Domenico, M.B. Vaughn, L. Li, D. Bagley, G. Musci, D.M. Ward, and J. Kaplan Ferroportin-mediated mobilization of ferritin iron precedes ferritin degradation by the proteasome EMBO J. 25 2006 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
  • 11
    • 0041940266 scopus 로고    scopus 로고
    • Iron, manganese, and cobalt transport by Nramp1 (Slc11a1) and Nramp2 (Slc11a2) expressed at the plasma membrane
    • DOI 10.1182/blood-2003-02-0425
    • J.R. Forbes, and P. Gros Iron, manganese, and cobalt transport by Nramp1 (Slc11a1) and Nramp2 (Slc11a2) expressed at the plasma membrane Blood 102 2003 1884 1892 (Pubitemid 37022588)
    • (2003) Blood , vol.102 , Issue.5 , pp. 1884-1892
    • Forbes, J.R.1    Gros, P.2
  • 12
    • 0037126002 scopus 로고    scopus 로고
    • Previously uncharacterized isoforms of divalent metal transporter (DMT)-1: Implications for regulation and cellular function
    • N. Hubert, and M.W. Hentze Previously uncharacterized isoforms of divalent metal transporter (DMT)-1: implications for regulation and cellular function Proc. Natl Acad. Sci. U. S. A. 99 2002 12345 12350
    • (2002) Proc. Natl Acad. Sci. U. S. A. , vol.99 , pp. 12345-12350
    • Hubert, N.1    Hentze, M.W.2
  • 13
    • 54049156405 scopus 로고    scopus 로고
    • The type IV mucolipidosis-associated protein TRPML1 is an endolysosomal iron release channel
    • X.P. Dong, X. Cheng, E. Mills, M. Delling, F. Wang, T. Kurz, and H. Xu The type IV mucolipidosis-associated protein TRPML1 is an endolysosomal iron release channel Nature 455 2008 992 996
    • (2008) Nature , vol.455 , pp. 992-996
    • Dong, X.P.1    Cheng, X.2    Mills, E.3    Delling, M.4    Wang, F.5    Kurz, T.6    Xu, H.7
  • 14
    • 2042546096 scopus 로고    scopus 로고
    • Balancing acts: Molecular control of mammalian iron metabolism
    • DOI 10.1016/S0092-8674(04)00343-5, PII S0092867404003435
    • M.W. Hentze, M.U. Muckenthaler, and N.C. Andrews Balancing acts: molecular control of mammalian iron metabolism Cell 117 2004 285 297 (Pubitemid 38534536)
    • (2004) Cell , vol.117 , Issue.3 , pp. 285-297
    • Hentze, M.W.1    Muckenthaler, M.U.2    Andrews, N.C.3
  • 15
    • 33846691564 scopus 로고    scopus 로고
    • Iron uptake and metabolism in the new millennium
    • DOI 10.1016/j.tcb.2006.12.003, PII S0962892406003400
    • L.L. Dunn, Y.S. Rahmanto, and D.R. Richardson Iron uptake and metabolism in the new millennium Trends Cell Biol. 17 2007 93 100 (Pubitemid 46199183)
    • (2007) Trends in Cell Biology , vol.17 , Issue.2 , pp. 93-100
    • Dunn, L.L.1    Rahmanto, Y.S.2    Richardson, D.R.3
  • 16
    • 29844457587 scopus 로고    scopus 로고
    • The evolution of iron chelators for the treatment of iron overload disease and cancer
    • DOI 10.1124/pr.57.4.2
    • D.S. Kalinowski, and D.R. Richardson The evolution of iron chelators for the treatment of iron overload disease and cancer Pharmacol. Rev. 57 2005 547 583 (Pubitemid 43036441)
    • (2005) Pharmacological Reviews , vol.57 , Issue.4 , pp. 547-583
    • Kalinowski, D.S.1    Richardson, D.R.2
  • 17
    • 0031567095 scopus 로고    scopus 로고
    • The molecular mechanisms of the metabolism and transport of iron in normal and neoplastic cells
    • DOI 10.1016/S0304-4157(96)00014-7, PII S0304415796000147
    • D.R. Richardson, and P. Ponka The molecular mechanisms of the metabolism and transport of iron in normal and neoplastic cells Biochim. Biophys. Acta 1331 1997 1 40 (Pubitemid 27168147)
    • (1997) Biochimica et Biophysica Acta - Reviews on Biomembranes , vol.1331 , Issue.1 , pp. 1-40
    • Richardson, D.R.1    Ponka, P.2
  • 20
    • 0014878377 scopus 로고
    • Histochemical indications for lysosomal localization of heavy metals in normal rat brain and liver
    • A. Brun, and U. Brunk Histochemical indications for lysosomal localization of heavy metals in normal rat brain and liver J. Histochem. Cytochem. 18 1970 820 827
    • (1970) J. Histochem. Cytochem. , vol.18 , pp. 820-827
    • Brun, A.1    Brunk, U.2
  • 21
    • 33644641768 scopus 로고    scopus 로고
    • Oxidative stress, accumulation of biological 'garbage', and aging
    • DOI 10.1089/ars.2006.8.197
    • A. Terman, and U.T. Brunk Oxidative stress, accumulation of biological 'garbage', and aging Antioxid. Redox Signal. 8 2006 197 204 (Pubitemid 43324546)
    • (2006) Antioxidants and Redox Signaling , vol.8 , Issue.1-2 , pp. 197-204
    • Terman, A.1    Brunk, U.T.2
  • 22
    • 34249815482 scopus 로고    scopus 로고
    • Autophagy, ageing and apoptosis: The role of oxidative stress and lysosomal iron
    • DOI 10.1016/j.abb.2007.01.013, PII S000398610700029X, Highlight Issue: Pro- and antiapoptotic Signalling
    • T. Kurz, A. Terman, and U.T. Brunk Autophagy, ageing and apoptosis: the role of oxidative stress and lysosomal iron Arch. Biochem. Biophys. 462 2007 220 230 (Pubitemid 46856317)
    • (2007) Archives of Biochemistry and Biophysics , vol.462 , Issue.2 , pp. 220-230
    • Kurz, T.1    Terman, A.2    Brunk, U.T.3
  • 24
    • 0142200240 scopus 로고    scopus 로고
    • Iron as the malignant spirit in successful ageing
    • DOI 10.1016/S1568-1637(02)00048-X, PII S156816370200048X
    • A.S. Polla, L.L. Polla, and B.S. Polla Iron as the malignant spirit in successful ageing Ageing Res. Rev. 2 2003 25 37 (Pubitemid 37443916)
    • (2003) Ageing Research Reviews , vol.2 , Issue.1 , pp. 25-37
    • Polla, A.S.1    Polla, L.L.2    Polla, B.S.3
  • 25
    • 34247564692 scopus 로고    scopus 로고
    • Role of iron in neurodegenerative disorders
    • DOI 10.1097/01.rmr.0000245461.90406.ad, PII 0000214220060200000002
    • D. Berg, and M.B. Youdim Role of iron in neurodegenerative disorders Top. Magn. Reson. Imaging 17 2006 5 17 (Pubitemid 46672929)
    • (2006) Topics in Magnetic Resonance Imaging , vol.17 , Issue.1 , pp. 5-17
    • Berg, D.1    Youdim, M.B.H.2
  • 26
    • 34247143301 scopus 로고    scopus 로고
    • Iron induced oxidative damage as a potential factor in age-related macular degeneration: The Cogan lecture
    • DOI 10.1167/iovs.06-0568
    • J.L. Dunaief Iron induced oxidative damage as a potential factor in age-related macular degeneration: the Cogan Lecture Invest. Ophthalmol. Vis. Sci. 47 2006 4660 4664 (Pubitemid 46586359)
    • (2006) Investigative Ophthalmology and Visual Science , vol.47 , Issue.11 , pp. 4660-4664
    • Dunaief, J.L.1
  • 27
    • 34249104544 scopus 로고    scopus 로고
    • Oxidative stress and aberrant signaling in aging and cognitive decline
    • DOI 10.1111/j.1474-9726.2007.00294.x
    • W. Dröge, and H.M. Schipper Oxidative stress and aberrant signaling in aging and cognitive decline Aging Cell 6 2007 361 370 (Pubitemid 46785141)
    • (2007) Aging Cell , vol.6 , Issue.3 , pp. 361-370
    • Droge, W.1    Schipper, H.M.2
  • 28
    • 65449120792 scopus 로고    scopus 로고
    • Iron behaving badly: Inappropriate iron chelation as a major contributor to the aetiology of vascular and other progressive inflammatory and degenerative diseases
    • D.B. Kell Iron behaving badly: inappropriate iron chelation as a major contributor to the aetiology of vascular and other progressive inflammatory and degenerative diseases BMC Med. Genomics 2 2009 2
    • (2009) BMC Med. Genomics , vol.2 , pp. 2
    • Kell, D.B.1
  • 29
    • 0032563119 scopus 로고    scopus 로고
    • Localized unfolding at the junction of three ferritin subunits: A mechanism for iron release?
    • DOI 10.1074/jbc.273.30.18685
    • H. Takagi, D. Shi, Y. Ha, N.M. Allewell, and E.C. Theil Localized unfolding at the junction of three ferritin subunits: a mechanism for iron release? J. Biol. Chem. 273 1998 18685 18688 (Pubitemid 28366247)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.30 , pp. 18685-18688
    • Takagi, H.1    Shi, D.2    Ha, Y.3    Allewell, N.M.4    Theil, E.C.5
  • 31
    • 0022973969 scopus 로고
    • The effects of ascorbic acid on the intracellular metabolism of iron and ferritin
    • K.R. Bridges, and K.E. Hoffman The effects of ascorbic acid on the intracellular metabolism of iron and ferritin J. Biol. Chem. 261 1986 14273 14277 (Pubitemid 17196337)
    • (1986) Journal of Biological Chemistry , vol.261 , Issue.30 , pp. 14273-14277
    • Bridges, K.R.1    Hoffman, K.E.2
  • 32
    • 0024238392 scopus 로고
    • Ferritin iron kinetics and protein turnover in K562 cells
    • S. Roberts, and A. Bomford Ferritin iron kinetics and protein turnover in K562 cells J. Biol. Chem. 263 1988 19181 19187 (Pubitemid 19016387)
    • (1988) Journal of Biological Chemistry , vol.263 , Issue.35 , pp. 19181-19187
    • Roberts, S.1    Bomford, A.2
  • 33
    • 0025238656 scopus 로고
    • Autophagic degradation of protein generates a pool of ferric iron required for the killing of cultured hepatocytes by an oxidative stress
    • I. Sakaida, M.E. Kyle, and J.L. Farber Autophagic degradation of protein generates a pool of ferric iron required for the killing of cultured hepatocytes by an oxidative stress Mol. Pharmacol. 37 1990 435 442 (Pubitemid 20115603)
    • (1990) Molecular Pharmacology , vol.37 , Issue.3 , pp. 435-442
    • Sakaida, I.1    Kyle, M.E.2    Farber, J.L.3
  • 34
    • 0030854921 scopus 로고    scopus 로고
    • Utilization of intracellular ferritin iron for hemoglobin synthesis in developing human erythroid precursors
    • B. Vaisman, E. Fibach, and A.M. Konijn Utilization of intracellular ferritin iron for hemoglobin synthesis in developing human erythroid precursors Blood 90 1997 831 838 (Pubitemid 27299124)
    • (1997) Blood , vol.90 , Issue.2 , pp. 831-838
    • Vaisman, B.1    Fibach, E.2    Konijn, A.M.3
  • 35
    • 0032533549 scopus 로고    scopus 로고
    • Iron in cytosolic ferritin can be recycled through lysosomal degradation in human fibroblasts
    • D.C. Radisky, and J. Kaplan Iron in cytosolic ferritin can be recycled through lysosomal degradation in human fibroblasts Biochem. J. 336 1998 201 205 (Pubitemid 28532577)
    • (1998) Biochemical Journal , vol.336 , Issue.1 , pp. 201-205
    • Radisky, D.C.1    Kaplan, J.2
  • 37
    • 1642576976 scopus 로고    scopus 로고
    • Examination of the Mechanism(s) Involved in Doxorubicin-Mediated Iron Accumulation in Ferritin: Studies Using Metabolic Inhibitors, Protein Synthesis Inhibitors, and Lysosomotropic Agents
    • DOI 10.1124/mol.65.1.181
    • J.C. Kwok, and D.R. Richardson Examination of the mechanism(s) involved in doxorubicin-mediated iron accumulation in ferritin: studies using metabolic inhibitors, protein synthesis inhibitors, and lysosomotropic agents Mol. Pharmacol. 65 2004 181 195 (Pubitemid 38113899)
    • (2004) Molecular Pharmacology , vol.65 , Issue.1 , pp. 181-195
    • Kwok, J.C.1    Richardson, D.R.2
  • 38
    • 18844425714 scopus 로고    scopus 로고
    • Role of compartmentalized redox-active iron in hydrogen peroxide-induced DNA damage and apoptosis
    • DOI 10.1042/BJ20041650
    • M. Tenopoulou, P.T. Doulias, A. Barbouti, U. Brunk, and D. Galaris Role of compartmentalized redox-active iron in hydrogen peroxide-induced DNA damage and apoptosis Biochem. J. 387 2005 703 710 (Pubitemid 40685704)
    • (2005) Biochemical Journal , vol.387 , Issue.3 , pp. 703-710
    • Tenopoulou, M.1    Doulias, P.-T.2    Barbouti, A.3    Brunk, U.4    Galaris, D.5
  • 39
    • 0037448105 scopus 로고    scopus 로고
    • Intralysosomal iron: A major determinant of oxidant-induced cell death
    • DOI 10.1016/S0891-5849(03)00109-6
    • Z. Yu, H.L. Persson, J.W. Eaton, and U.T. Brunk Intralysosomal iron: a major determinant of oxidant-induced cell death Free Radic. Biol. Med. 34 2003 1243 1252 (Pubitemid 36513967)
    • (2003) Free Radical Biology and Medicine , vol.34 , Issue.10 , pp. 1243-1252
    • Yu, Z.1    Persson, H.L.2    Eaton, J.W.3    Brunk, U.T.4
  • 40
    • 0037448064 scopus 로고    scopus 로고
    • Prevention of oxidant-induced cell death by lysosomotropic iron chelators
    • DOI 10.1016/S0891-5849(03)00106-0
    • H.L. Persson, Z. Yu, O. Tirosh, J.W. Eaton, and U.T. Brunk Prevention of oxidant-induced cell death by lysosomotropic iron chelators Free Radic. Biol. Med. 34 2003 1295 1305 (Pubitemid 36513971)
    • (2003) Free Radical Biology and Medicine , vol.34 , Issue.10 , pp. 1295-1305
    • Persson, H.L.1    Yu, Z.2    Tirosh, O.3    Eaton, J.W.4    Brunk, U.T.5
  • 41
    • 0031709850 scopus 로고    scopus 로고
    • Endogenous ferritin protects cells with iron-laden lysosomes against oxidative stress
    • DOI 10.1080/10715769800300121
    • B. Garner, K. Roberg, and U.T. Brunk Endogenous ferritin protects cells with iron-laden lysosomes against oxidative stress Free Radic. Res. 29 1998 103 114 (Pubitemid 28451389)
    • (1998) Free Radical Research , vol.29 , Issue.2 , pp. 103-114
    • Garner, B.1    Roberg, K.2    Brunk, U.T.3
  • 42
    • 77955871827 scopus 로고    scopus 로고
    • Lysosomal proteolysis is the primary degradation pathway for cytosolic ferritin and cytosolic ferritin degradation is necessary for iron exit
    • Y. Zhang, M. Mikhael, D. Xu, Y. Li, S. Soe-Lin, B. Ning, W. Li, G. Nie, Y. Zhao, and P. Ponka Lysosomal proteolysis is the primary degradation pathway for cytosolic ferritin and cytosolic ferritin degradation is necessary for iron exit Antioxid. Redox Signal. 13 2010 999 1009
    • (2010) Antioxid. Redox Signal. , vol.13 , pp. 999-1009
    • Zhang, Y.1    Mikhael, M.2    Xu, D.3    Li, Y.4    Soe-Lin, S.5    Ning, B.6    Li, W.7    Nie, G.8    Zhao, Y.9    Ponka, P.10
  • 43
    • 73349099034 scopus 로고    scopus 로고
    • Specific iron chelators determine the route of ferritin degradation
    • I. De Domenico, D.M. Ward, and J. Kaplan Specific iron chelators determine the route of ferritin degradation Blood 114 2009 4546 4551
    • (2009) Blood , vol.114 , pp. 4546-4551
    • De Domenico, I.1    Ward, D.M.2    Kaplan, J.3
  • 44
    • 8344242220 scopus 로고    scopus 로고
    • Autophagy in health and disease: A double-edged sword
    • DOI 10.1126/science.1099993
    • T. Shintani, and D.J. Klionsky Autophagy in health and disease: a double-edged sword Science 306 2004 990 995 (Pubitemid 39482894)
    • (2004) Science , vol.306 , Issue.5698 , pp. 990-995
    • Shintani, T.1    Klionsky, D.J.2
  • 45
    • 27644484061 scopus 로고    scopus 로고
    • Autophagy: Molecular machinery for self-eating
    • DOI 10.1038/sj.cdd.4401765, PII 4401765
    • T. Yorimitsu, and D.J. Klionsky Autophagy: molecular machinery for self-eating Cell Death Differ. 12 Suppl. 2 2005 1542 1552 (Pubitemid 41553991)
    • (2005) Cell Death and Differentiation , vol.12 , Issue.SUPPL. 2 , pp. 1542-1552
    • Yorimitsu, T.1    Klionsky, D.J.2
  • 46
    • 34248139628 scopus 로고    scopus 로고
    • Molecular machinery of autophagosome formation in yeast, Saccharomyces cerevisiae
    • DOI 10.1016/j.febslet.2007.01.096, PII S0014579307002554, Membrane Trafficking
    • K. Suzuki, and Y. Ohsumi Molecular machinery of autophagosome formation in yeast. Saccharomyces cerevisiae FEBS Lett. 581 2007 2156 2161 (Pubitemid 46709906)
    • (2007) FEBS Letters , vol.581 , Issue.11 , pp. 2156-2161
    • Suzuki, K.1    Ohsumi, Y.2
  • 47
    • 1842583789 scopus 로고    scopus 로고
    • Development by self-digestion: Molecular mechanisms and biological functions of autophagy
    • DOI 10.1016/S1534-5807(04)00099-1, PII S1534580704000991
    • B. Levine, and D.J. Klionsky Development by self-digestion: molecular mechanisms and biological functions of autophagy Dev. Cell 6 2004 463 477 (Pubitemid 38456176)
    • (2004) Developmental Cell , vol.6 , Issue.4 , pp. 463-477
    • Levine, B.1    Klionsky, D.J.2
  • 48
    • 33745026738 scopus 로고    scopus 로고
    • Ffrench, M.; Terman, A. Autophagy and aging: The importance of maintaining "clean" cells
    • A.M. Cuervo, E. Bergamini, U.T. Brunk, and W. Dröge ffrench, M.; Terman, A. Autophagy and aging: the importance of maintaining "clean" cells Autophagy 1 2005 131 140
    • (2005) Autophagy , vol.1 , pp. 131-140
    • Cuervo, A.M.1    Bergamini, E.2    Brunk, U.T.3    Dröge, W.4
  • 49
    • 21244476364 scopus 로고    scopus 로고
    • The aging myocardium: Roles of mitochondrial damage and lysosomal degradation
    • DOI 10.1016/j.hlc.2004.12.023
    • A. Terman, and U.T. Brunk The aging myocardium: roles of mitochondrial damage and lysosomal degradation Heart Lung Circ. 14 2005 107 114 (Pubitemid 40895299)
    • (2005) Heart Lung and Circulation , vol.14 , Issue.2 , pp. 107-114
    • Terman, A.1    Brunk, U.T.2
  • 50
    • 0027180710 scopus 로고
    • Visualization of iron in cultured macrophages: A cytochemical light and electron microscopic study using autometallography
    • DOI 10.1016/0891-5849(93)90120-J
    • J.M. Zdolsek, K. Roberg, and U.T. Brunk Visualization of iron in cultured macrophages: a cytochemical light and electron microscopic study using autometallography Free Radic. Biol. Med. 15 1993 1 11 (Pubitemid 23171438)
    • (1993) Free Radical Biology and Medicine , vol.15 , Issue.1 , pp. 1-11
    • Zdolsek, J.M.1    Roberg, K.2    Brunk, U.T.3
  • 51
    • 0031889998 scopus 로고    scopus 로고
    • Lipofuscin: Mechanisms of formation and increase with age
    • A. Terman, and U.T. Brunk Lipofuscin: mechanisms of formation and increase with age APMIS 106 1998 265 276 (Pubitemid 28131355)
    • (1998) APMIS , vol.106 , Issue.2 , pp. 265-276
    • Terman, A.1    Brunk, U.T.2
  • 52
    • 0036710928 scopus 로고    scopus 로고
    • Lipofuscin: Mechanisms of age-related accumulation and influence on cell function
    • DOI 10.1016/S0891-5849(02)00959-0, PII S0891584902009590
    • U.T. Brunk, and A. Terman Lipofuscin: mechanisms of age-related accumulation and influence on cell function Free Radic. Biol. Med. 33 2002 611 619 (Pubitemid 35245833)
    • (2002) Free Radical Biology and Medicine , vol.33 , Issue.5 , pp. 611-619
    • Brunk, U.T.1    Terman, A.2
  • 53
    • 1642463971 scopus 로고    scopus 로고
    • Relocalized redox-active lysosomal iron is an important mediator of oxidative-stress-induced DNA damage
    • DOI 10.1042/BJ20031029
    • T. Kurz, A. Leake, T. Von Zglinicki, and U.T. Brunk Relocalized redox-active lysosomal iron is an important mediator of oxidative-stress-induced DNA damage Biochem. J. 378 2004 1039 1045 (Pubitemid 38406883)
    • (2004) Biochemical Journal , vol.378 , Issue.3 , pp. 1039-1045
    • Kurz, T.1    Leake, A.2    Von Zglinicki, T.3    Brunk, U.T.4
  • 54
    • 33749146320 scopus 로고    scopus 로고
    • Lysosomal labilization
    • DOI 10.1080/15216540600904885, PII J375811642077257
    • A. Terman, T. Kurz, B. Gustafsson, and U.T. Brunk Lysosomal labilization IUBMB Life 58 2006 531 539 (Pubitemid 44470239)
    • (2006) IUBMB Life , vol.58 , Issue.9 , pp. 531-539
    • Terman, A.1    Kurz, T.2    Gustafsson, B.3    Brunk, U.T.4
  • 55
    • 0141447370 scopus 로고    scopus 로고
    • Lysosomal enzymes promote mitochondrial oxidant production, cytochrome c release and apoptosis
    • DOI 10.1046/j.1432-1033.2003.03765.x
    • M. Zhao, F. Antunes, J.W. Eaton, and U.T. Brunk Lysosomal enzymes promote mitochondrial oxidant production, cytochrome c release and apoptosis Eur. J. Biochem. 270 2003 3778 3786 (Pubitemid 37123249)
    • (2003) European Journal of Biochemistry , vol.270 , Issue.18 , pp. 3778-3786
    • Zhao, M.1    Antunes, F.2    Eaton, J.W.3    Brunk, U.T.4
  • 56
    • 0032988381 scopus 로고    scopus 로고
    • Oxidative stress, growth factor starvation and Fas activation may all cause apoptosis through lysosomal leak
    • U.T. Brunk, and I. Svensson Oxidative stress, growth factor starvation and Fas activation may all cause apoptosis through lysosomal leak Redox Rep. 4 1999 3 11 (Pubitemid 29296774)
    • (1999) Redox Report , vol.4 , Issue.1-2 , pp. 3-11
    • Brunk, U.T.1    Svensson, I.2
  • 57
    • 33747600931 scopus 로고    scopus 로고
    • Do lysosomes induce cell death?
    • DOI 10.1080/15216540600719630, PII L64007348Q613541
    • V. Stoka, V. Turk, and B. Turk Do lysosomes induce cell death? IUBMB Life 58 2006 493 494 (Pubitemid 44266911)
    • (2006) IUBMB Life , vol.58 , Issue.8 , pp. 493-494
    • Stoka, V.1    Turk, V.2    Turk, B.3
  • 58
    • 0031422255 scopus 로고    scopus 로고
    • Lysosomal heterogeneity between and within cells with respect to resistance against oxidative stress
    • E. Nilsson, R. Ghassemifar, and U.T. Brunk Lysosomal heterogeneity between and within cells with respect to resistance against oxidative stress Histochem. J. 29 1997 857 865 (Pubitemid 28062672)
    • (1997) Histochemical Journal , vol.29 , Issue.11-12 , pp. 857-865
    • Nilsson, E.1    Ghassemifar, R.2    Brunk, U.T.3
  • 59
    • 0036829433 scopus 로고    scopus 로고
    • Rate of generation of oxidative stress-related damage and animal longevity
    • DOI 10.1016/S0891-5849(02)00910-3, PII S0891584902009103
    • G. Barja Rate of generation of oxidative stress-related damage and animal longevity Free Radic. Biol. Med. 33 2002 1167 1172 (Pubitemid 35246584)
    • (2002) Free Radical Biology and Medicine , vol.33 , Issue.9 , pp. 1167-1172
    • Barja, G.1
  • 60
    • 0036628724 scopus 로고    scopus 로고
    • Role of oxidative stress and protein oxidation in the aging process
    • DOI 10.1016/S0891-5849(02)00856-0, PII S0891584902008560
    • R.S. Sohal Role of oxidative stress and protein oxidation in the aging process Free Radic. Biol. Med. 33 2002 37 44 (Pubitemid 34681004)
    • (2002) Free Radical Biology and Medicine , vol.33 , Issue.1 , pp. 37-44
    • Sohal, R.S.1
  • 61
    • 34347375300 scopus 로고    scopus 로고
    • Direct interorganellar transfer of iron from endosome to mitochondrion
    • DOI 10.1182/blood-2007-01-068148
    • A.D. Sheftel, A.S. Zhang, C. Brown, O.S. Shirihai, and P. Ponka Direct interorganellar transfer of iron from endosome to mitochondrion Blood 110 2007 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
  • 62
    • 0035366499 scopus 로고    scopus 로고
    • 2 is a consequence of lysosomal rupture
    • DOI 10.1042/0264-6021:3560549
    • 2 is a consequence of lysosomal rupture Biochem. J. 356 2001 549 555 (Pubitemid 32532368)
    • (2001) Biochemical Journal , vol.356 , Issue.2 , pp. 549-555
    • Antunes, F.1    Cadenas, E.2    Brunk, U.T.3
  • 63
    • 33745205646 scopus 로고    scopus 로고
    • Intralysosomal iron chelation protects against oxidative stress-induced cellular damage
    • T. Kurz, B. Gustafsson, and U.T. Brunk Intralysosomal iron chelation protects against oxidative stress-induced cellular damage FEBS J. 273 2006 3106 3117
    • (2006) FEBS J. , vol.273 , pp. 3106-3117
    • Kurz, T.1    Gustafsson, B.2    Brunk, U.T.3
  • 64
    • 0034677741 scopus 로고    scopus 로고
    • Induction of cell death by the lysosomotropic detergent MSDH
    • DOI 10.1016/S0014-5793(00)01286-2, PII S0014579300012862
    • W. Li, X. Yuan, G. Nordgren, H. Dalen, G.M. Dubowchik, R.A. Firestone, and U.T. Brunk Induction of cell death by the lysosomotropic detergent MSDH FEBS Lett. 470 2000 35 39 (Pubitemid 30155619)
    • (2000) FEBS Letters , vol.470 , Issue.1 , pp. 35-39
    • Li, W.1    Yuan, X.2    Nordgren, G.3    Dalen, H.4    Dubowchik, G.M.5    Firestone, R.A.6    Brunk, U.T.7
  • 65
    • 0035861903 scopus 로고    scopus 로고
    • Delayed oxidant-induced cell death involves activation of phospholipase A2
    • DOI 10.1016/S0014-5793(01)03184-2, PII S0014579301031842
    • M. Zhao, U.T. Brunk, and J.W. Eaton Delayed oxidant-induced cell death involves activation of phospholipase A2 FEBS Lett. 509 2001 399 404 (Pubitemid 34031968)
    • (2001) FEBS Letters , vol.509 , Issue.3 , pp. 399-404
    • Zhao, M.1    Brunk, U.T.2    Eaton, J.W.3
  • 67
    • 0001636281 scopus 로고
    • Histochemistry of heavy metals; The sulfide-silver procedure
    • F. Timm Histochemistry of heavy metals; the sulfide-silver procedure Dtsch. Z. Gesamte Gerichtl. Med. 46 1958 706 711
    • (1958) Dtsch. Z. Gesamte Gerichtl. Med. , vol.46 , pp. 706-711
    • Timm, F.1
  • 68
    • 0025726216 scopus 로고
    • A rapid and simple method for measuring thymocyte apoptosis by propidium iodide staining and flow cytometry
    • I. Nicoletti, G. Migliorati, M.C. Pagliacci, F. Grignani, and C. Riccardi A rapid and simple method for measuring thymocyte apoptosis by propidium iodide staining and flow cytometry J. Immunol. Methods 139 1991 271 279
    • (1991) J. Immunol. Methods , vol.139 , pp. 271-279
    • Nicoletti, I.1    Migliorati, G.2    Pagliacci, M.C.3    Grignani, F.4    Riccardi, C.5
  • 69
    • 33746108329 scopus 로고    scopus 로고
    • Lysosomal turnover, but not a cellular level, of endogenous LC3 is a marker for autophagy
    • I. Tanida, N. Minematsu-Ikeguchi, T. Ueno, and E. Kominami Lysosomal turnover, but not a cellular level, of endogenous LC3 is a marker for autophagy Autophagy 1 2005 84 91
    • (2005) Autophagy , vol.1 , pp. 84-91
    • Tanida, I.1    Minematsu-Ikeguchi, N.2    Ueno, T.3    Kominami, E.4
  • 70
    • 34247157226 scopus 로고    scopus 로고
    • Does the calcein-AM method assay the total cellular 'labile iron pool' or only a fraction of it?
    • DOI 10.1042/BJ20061840
    • M. Tenopoulou, T. Kurz, P.T. Doulias, D. Galaris, and U.T. Brunk Does the calcein-AM method assay the total cellular 'labile iron pool' or only a fraction of it? Biochem. J. 403 2007 261 266 (Pubitemid 46596581)
    • (2007) Biochemical Journal , vol.403 , Issue.2 , pp. 261-266
    • Tenopoulou, M.1    Kurz, T.2    Doulias, P.-T.3    Galaris, D.4    Brunk, U.T.5
  • 71
    • 75349112375 scopus 로고    scopus 로고
    • Mitochondrial turnover and aging of long-lived postmitotic cells: The mitochondrial-lysosomal axis theory of aging
    • A. Terman, T. Kurz, M. Navratil, E.A. Arriaga, and U.T. Brunk Mitochondrial turnover and aging of long-lived postmitotic cells: the mitochondrial-lysosomal axis theory of aging Antioxid. Redox Signal. 12 2010 503 535
    • (2010) Antioxid. Redox Signal. , vol.12 , pp. 503-535
    • Terman, A.1    Kurz, T.2    Navratil, M.3    Arriaga, E.A.4    Brunk, U.T.5
  • 73
    • 33846702991 scopus 로고    scopus 로고
    • Autophagy, organelles and ageing
    • DOI 10.1002/path.2094
    • A. Terman, B. Gustafsson, and U.T. Brunk Autophagy, organelles and ageing J. Pathol. 211 2007 134 143 (Pubitemid 46195512)
    • (2007) Journal of Pathology , vol.211 , Issue.2 , pp. 134-143
    • Terman, A.1    Gustafsson, B.2    Brunk, U.T.3
  • 75
    • 0036236006 scopus 로고    scopus 로고
    • The mitochondrial-lysosomal axis theory of aging: Accumulation of damaged mitochondria as a result of imperfect autophagocytosis
    • DOI 10.1046/j.1432-1033.2002.02869.x
    • U.T. Brunk, and A. Terman The mitochondrial-lysosomal axis theory of aging: accumulation of damaged mitochondria as a result of imperfect autophagocytosis Eur. J. Biochem. 269 2002 1996 2002 (Pubitemid 34437840)
    • (2002) European Journal of Biochemistry , vol.269 , Issue.8 , pp. 1996-2002
    • Brunk, U.T.1    Terman, A.2
  • 76
    • 0029563691 scopus 로고
    • Lipofuscin in bovine muscle and brain: A model for studying age pigment
    • R.D. Jolly, B.V. Douglas, P.M. Davey, and J.E. Roiri Lipofuscin in bovine muscle and brain: a model for studying age pigment Gerontology 41 1995 283 295 (Pubitemid 26019924)
    • (1995) Gerontology , vol.41 , Issue.SUPPL. 2 , pp. 283-295
    • Jolly, R.D.1    Douglas, B.V.2    Davey, P.M.3    Roiri, J.E.4
  • 79
    • 0027980319 scopus 로고
    • Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC class I molecules
    • DOI 10.1016/S0092-8674(94)90462-6
    • K.L. Rock, C. Gramm, L. Rothstein, K. Clark, R. Stein, L. Dick, D. Hwang, and A.L. Goldberg Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC class I molecules Cell 78 1994 761 771 (Pubitemid 24294452)
    • (1994) Cell , vol.78 , Issue.5 , pp. 761-771
    • Rock, K.L.1    Gramm, C.2    Rothstein, L.3    Clark, K.4    Stein, R.5    Dick, L.6    Hwang, D.7    Goldberg, A.L.8
  • 80
    • 0034983544 scopus 로고    scopus 로고
    • Lysosomal involvement in apoptosis
    • DOI 10.1179/135100001101536094
    • U.T. Brunk, J. Neuzil, and J.W. Eaton Lysosomal involvement in apoptosis Redox Rep. 6 2001 91 97 (Pubitemid 32519816)
    • (2001) Redox Report , vol.6 , Issue.2 , pp. 91-97
    • Brunk, U.T.1    Neuzil, J.2    Eaton, J.W.3
  • 81
    • 0031455120 scopus 로고    scopus 로고
    • On the cytoprotective role of ferritin in macrophages and its ability to enhance lysosomal stability
    • B. Garner, W. Li, K. Roberg, and U.T. Brunk On the cytoprotective role of ferritin in macrophages and its ability to enhance lysosomal stability Free Radic. Res. 27 1997 487 500 (Pubitemid 28026532)
    • (1997) Free Radical Research , vol.27 , Issue.5 , pp. 487-500
    • Garner, B.1    Li, W.2    Roberg, K.3    Brunk, U.T.4
  • 82
    • 32944481457 scopus 로고    scopus 로고
    • Metallothionein protects against oxidative stress-induced lysosomal destabilization
    • DOI 10.1042/BJ20051143
    • S.K. Baird, T. Kurz, and U.T. Brunk Metallothionein protects against oxidative stress-induced lysosomal destabilization Biochem. J. 394 2006 275 283 (Pubitemid 43259678)
    • (2006) Biochemical Journal , vol.394 , Issue.1 , pp. 275-283
    • Baird, S.K.1    Kurz, T.2    Brunk, U.T.3
  • 83
    • 58149398237 scopus 로고    scopus 로고
    • Autophagy of HSP70 and chelation of lysosomal iron in a non-redox-active form
    • T. Kurz, and U.T. Brunk Autophagy of HSP70 and chelation of lysosomal iron in a non-redox-active form Autophagy 5 2009 93 95
    • (2009) Autophagy , vol.5 , pp. 93-95
    • Kurz, T.1    Brunk, U.T.2
  • 85
    • 0033571363 scopus 로고    scopus 로고
    • H-ferritin subunit overexpression in erythroid cells reduces the oxidative stress response and induces multidrug resistance properties
    • S. Epsztejn, H. Glickstein, V. Picard, I.N. Slotki, W. Breuer, C. Beaumont, and Z.I. Cabantchik H-ferritin subunit overexpression in erythroid cells reduces the oxidative stress response and induces multidrug resistance properties Blood 94 1999 3593 3603 (Pubitemid 29536156)
    • (1999) Blood , vol.94 , Issue.10 , pp. 3593-3603
    • Epsztejn, S.1    Glickstein, H.2    Picard, V.3    Slotki, I.N.4    Breuer, W.5    Beaumont, C.6    Cabantchik, Z.I.7
  • 86
    • 0032694352 scopus 로고    scopus 로고
    • Adenovirus E1A blocks oxidant-dependent ferritin induction and sensitizes cells to pro-oxidant cytotoxicity
    • DOI 10.1016/S0014-5793(99)01443-X, PII S001457939901443X
    • K. Orino, Y. Tsuji, F.M. Torti, and S.V. Torti Adenovirus E1A blocks oxidant-dependent ferritin induction and sensitizes cells to pro-oxidant cytotoxicity FEBS Lett. 461 1999 334 338 (Pubitemid 29533358)
    • (1999) FEBS Letters , vol.461 , Issue.3 , pp. 334-338
    • Orino, K.1    Tsuji, Y.2    Torti, F.M.3    Torti, S.V.4
  • 87
    • 0033853838 scopus 로고    scopus 로고
    • Coordinate transcriptional and translational regulation of ferritin in response to oxidative stress
    • DOI 10.1128/MCB.20.16.5818-5827.2000
    • Y. Tsuji, H. Ayaki, S.P. Whitman, C.S. Morrow, S.V. Torti, and F.M. Torti Coordinate transcriptional and translational regulation of ferritin in response to oxidative stress Mol. Cell. Biol. 20 2000 5818 5827 (Pubitemid 30613031)
    • (2000) Molecular and Cellular Biology , vol.20 , Issue.16 , pp. 5818-5827
    • Tsuji, Y.1    Ayaki, H.2    Whitman, S.P.3    Morrow, C.S.4    Torti, S.V.5    Torti, F.M.6
  • 89
    • 28844490007 scopus 로고    scopus 로고
    • The lysosome-associated apoptosis-inducing protein containing the pleckstrin homology (PH) and FYVE domains (LAPF), representative of a novel family of PH and FYVE domain-containing proteins, induces caspase-independent apoptosis via the lysosomal-mitochondrial pathway
    • DOI 10.1074/jbc.M502190200
    • W. Chen, N. Li, T. Chen, Y. Han, C. Li, Y. Wang, W. He, L. Zhang, T. Wan, and X. Cao The lysosome-associated apoptosis-inducing protein containing the pleckstrin homology (PH) and FYVE domains (LAPF), representative of a novel family of PH and FYVE domain-containing proteins, induces caspase-independent apoptosis via the lysosomal-mitochondrial pathway J. Biol. Chem. 280 2005 40985 40995 (Pubitemid 41780594)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.49 , pp. 40985-40995
    • Chen, W.1    Li, N.2    Chen, T.3    Han, Y.4    Li, C.5    Wang, Y.6    He, W.7    Zhang, L.8    Wan, T.9    Cao, X.10
  • 90
    • 37048999377 scopus 로고    scopus 로고
    • Adaptor protein LAPF recruits phosphorylated p53 to lysosomes and triggers lysosomal destabilization in apoptosis
    • DOI 10.1158/0008-5472.CAN-07-2333
    • N. Li, Y. Zheng, W. Chen, C. Wang, X. Liu, W. He, H. Xu, and X. Cao Adaptor protein LAPF recruits phosphorylated p53 to lysosomes and triggers lysosomal destabilization in apoptosis Cancer Res. 67 2007 11176 11185 (Pubitemid 350248542)
    • (2007) Cancer Research , vol.67 , Issue.23 , pp. 11176-11185
    • Li, N.1    Zheng, Y.2    Chen, W.3    Wang, C.4    Liu, X.5    He, W.6    Xu, H.7    Cao, X.8
  • 91
    • 0034682761 scopus 로고    scopus 로고
    • Overexpression of wild type and mutated human ferritin H-chain in HeLa cells: In vivo role of ferritin ferroxidase activity
    • A. Cozzi, B. Corsi, S. Levi, P. Santambrogio, A. Albertini, and P. Arosio Overexpression of wild type and mutated human ferritin H-chain in HeLa cells: in vivo role of ferritin ferroxidase activity J. Biol. Chem. 275 2000 25122 25129
    • (2000) J. Biol. Chem. , vol.275 , pp. 25122-25129
    • Cozzi, A.1    Corsi, B.2    Levi, S.3    Santambrogio, P.4    Albertini, A.5    Arosio, P.6
  • 92
    • 1542373640 scopus 로고    scopus 로고
    • Analysis of the biologic functions of H- and L-ferritins in HeLa cells by transfection with siRNAs and cDNAs: Evidence for a proliferative role of L-ferritin
    • DOI 10.1182/blood-2003-06-1842
    • A. Cozzi, B. Corsi, S. Levi, P. Santambrogio, G. Biasiotto, and P. Arosio Analysis of the biologic functions of H- and L-ferritins in HeLa cells by transfection with siRNAs and cDNAs: evidence for a proliferative role of L-ferritin Blood 103 2004 2377 2383 (Pubitemid 38326261)
    • (2004) Blood , vol.103 , Issue.6 , pp. 2377-2383
    • Cozzi, A.1    Corsi, B.2    Levi, S.3    Santambrogio, P.4    Biasiotto, G.5    Arosio, P.6
  • 93
    • 0035353194 scopus 로고    scopus 로고
    • Repression of ferritin expression increases the labile iron pool, oxidative stress, and short-term growth of human erythroleukemia cells
    • O. Kakhlon, Y. Gruenbaum, and Z.I. Cabantchik Repression of ferritin expression increases the labile iron pool, oxidative stress, and short-term growth of human erythroleukemia cells Blood 97 2001 2863 2871
    • (2001) Blood , vol.97 , pp. 2863-2871
    • Kakhlon, O.1    Gruenbaum, Y.2    Cabantchik, Z.I.3
  • 94
  • 95
    • 77953810574 scopus 로고    scopus 로고
    • Cytosolic and mitochondrial ferritins in the regulation of cellular iron homeostasis and oxidative damage
    • P. Arosio, and S. Levi Cytosolic and mitochondrial ferritins in the regulation of cellular iron homeostasis and oxidative damage Biochim. Biophys. Acta 1800 2010 783 792
    • (2010) Biochim. Biophys. Acta , vol.1800 , pp. 783-792
    • Arosio, P.1    Levi, S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.