메뉴 건너뛰기




Volumn 378, Issue 3, 2004, Pages 1039-1045

Relocalized redox-active lysosomal iron is an important mediator of oxidative-stress-induced DNA damage

Author keywords

DNA damage; Hydrogen peroxide; Lysosomal iron; Lysosome; Oxidative stress; Telomere

Indexed keywords

CELLS; CHELATION; DNA; IRON; REDOX REACTIONS; TRANSITION METALS;

EID: 1642463971     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20031029     Document Type: Article
Times cited : (96)

References (46)
  • 1
    • 0027171266 scopus 로고
    • Oxidants, antioxidants, and the degenerative diseases of aging
    • Ames, B. N., Shigenaga, M. K. and Hagen, T. M. (1993) Oxidants, antioxidants, and the degenerative diseases of aging. Proc. Natl. Acad. Sci. U.S.A. 90, 7915-7922
    • (1993) Proc. Natl. Acad. Sci. U.S.A. , vol.90 , pp. 7915-7922
    • Ames, B.N.1    Shigenaga, M.K.2    Hagen, T.M.3
  • 2
    • 0025972738 scopus 로고
    • DNA damage by oxygen-derived species. Its mechanism and measurement in mammalian systems
    • Halliwell, B. and Aruoma, O. I. (1991) DNA damage by oxygen-derived species. Its mechanism and measurement in mammalian systems. FEBS Lett. 281, 9-19
    • (1991) FEBS Lett. , vol.281 , pp. 9-19
    • Halliwell, B.1    Aruoma, O.I.2
  • 3
    • 0025126555 scopus 로고
    • Role of free radicals and catalytic metal ions in human disease: An overview
    • Halliwell, B. and Gutteridge, J. M. (1990) Role of free radicals and catalytic metal ions in human disease: an overview. Methods Enzymol. 186, 1-85
    • (1990) Methods Enzymol. , vol.186 , pp. 1-85
    • Halliwell, B.1    Gutteridge, J.M.2
  • 4
    • 0030857377 scopus 로고    scopus 로고
    • Iron homeostasis, oxidative stress, and DNA damage
    • Meneghini, R. (1997) Iron homeostasis, oxidative stress, and DNA damage. Free Radical Biol. Med. 23, 783-792
    • (1997) Free Radical Biol. Med. , vol.23 , pp. 783-792
    • Meneghini, R.1
  • 5
    • 0034881032 scopus 로고    scopus 로고
    • Free radicals associated with DNA damage
    • Chatgilialoglu, C. and O'Neill, P. (2001) Free radicals associated with DNA damage. Exp. Gerontol. 36, 1459-1471
    • (2001) Exp. Gerontol. , vol.36 , pp. 1459-1471
    • Chatgilialoglu, C.1    O'Neill, P.2
  • 6
    • 0030797051 scopus 로고    scopus 로고
    • Formation, prevention, and repair of DNA damage by iron/hydrogen peroxide
    • Henle, E. S. and Linn, S. (1997) Formation, prevention, and repair of DNA damage by iron/hydrogen peroxide. J. Biol. Chem. 272, 19095-19098
    • (1997) J. Biol. Chem. , vol.272 , pp. 19095-19098
    • Henle, E.S.1    Linn, S.2
  • 8
    • 0036829433 scopus 로고    scopus 로고
    • Rate of generation of oxidative stress-related damage and animal longevity
    • Barja, G. (2002) Rate of generation of oxidative stress-related damage and animal longevity. Free Radical Biol. Med. 33, 1167-1172
    • (2002) Free Radical Biol. Med. , vol.33 , pp. 1167-1172
    • Barja, G.1
  • 9
    • 0037366104 scopus 로고    scopus 로고
    • Oxidative stress, cell cycle, and neurodegeneration
    • Klein, J. A. and Ackerman, S. L. (2003) Oxidative stress, cell cycle, and neurodegeneration. J. Clin. Invest. 111, 785-793
    • (2003) J. Clin. Invest. , vol.111 , pp. 785-793
    • Klein, J.A.1    Ackerman, S.L.2
  • 10
    • 0006348848 scopus 로고    scopus 로고
    • Potential use of iron chelators against oxidative damage
    • Galey, J. B. (1997) Potential use of iron chelators against oxidative damage. Adv. Pharmacol. 38, 167-203
    • (1997) Adv. Pharmacol. , vol.38 , pp. 167-203
    • Galey, J.B.1
  • 11
    • 0023732274 scopus 로고
    • A site-specific mechanism for free radical induced biological damage: The essential role of redox-active transition metals
    • Chevion, M. (1988) A site-specific mechanism for free radical induced biological damage: the essential role of redox-active transition metals. Free Radical Biol. Med. 5, 27-37
    • (1988) Free Radical Biol. Med. , vol.5 , pp. 27-37
    • Chevion, M.1
  • 12
    • 0014878377 scopus 로고
    • Histochemical indications for lysosomal localization of heavy metals in normal rat brain and liver
    • Brun, A. and Brunk, U. (1970) Histochemical indications for lysosomal localization of heavy metals in normal rat brain and liver. J. Histochem. Cytochem. 18, 820-827
    • (1970) J. Histochem. Cytochem. , vol.18 , pp. 820-827
    • Brun, A.1    Brunk, U.2
  • 13
    • 0022336763 scopus 로고
    • Lysosomal origin of the ferric iron required for cell killing by hydrogen peroxide
    • Starke, P. E., Gilbertson, J. D. and Farber, J. L (1985) Lysosomal origin of the ferric iron required for cell killing by hydrogen peroxide. Biochem. Biophys. Res. Commun. 133, 371-379
    • (1985) Biochem. Biophys. Res. Commun. , vol.133 , pp. 371-379
    • Starke, P.E.1    Gilbertson, J.D.2    Farber, J.L.3
  • 14
    • 0027180710 scopus 로고
    • Visualization of iron in cultured macrophages: A cytochemical light and electron microscopic study using autometallography
    • Zdolsek, J. M., Roberg, K. and Brunk, U. T. (1993) Visualization of iron in cultured macrophages: a cytochemical light and electron microscopic study using autometallography. Free Radical Biol. Med. 15, 1-11
    • (1993) Free Radical Biol. Med. , vol.15 , pp. 1-11
    • Zdolsek, J.M.1    Roberg, K.2    Brunk, U.T.3
  • 15
    • 0035874476 scopus 로고    scopus 로고
    • Subcellular distribution of chelatable iron: A laser scanning microscopic study in isolated hepatocytes and liver endothelial cells
    • Petrat, F., de Groot, H. and Rauen, U. (2001) Subcellular distribution of chelatable iron: a laser scanning microscopic study in isolated hepatocytes and liver endothelial cells. Biochem. J. 356, 61-69
    • (2001) Biochem. J. , vol.356 , pp. 61-69
    • Petrat, F.1    De Groot, H.2    Rauen, U.3
  • 16
    • 0037448105 scopus 로고    scopus 로고
    • Intralysosomal iron: A major determinant of oxidant-inducedcell death
    • Yu, Z., Persson, H. L., Eaton, J. W. and Brunk, U. T. (2003) Intralysosomal iron: a major determinant of oxidant-inducedcell death. Free Radical Biol. Med. 34, 1243-1252
    • (2003) Free Radical Biol. Med. , vol.34 , pp. 1243-1252
    • Yu, Z.1    Persson, H.L.2    Eaton, J.W.3    Brunk, U.T.4
  • 17
    • 0037448064 scopus 로고    scopus 로고
    • Prevention of oxidant-induced cell death by lysosomotropic iron chelators
    • Persson, H. L., Yu, Z., Tirosh, O., Eaton, J. W. and Brunk, U. T. (2003) Prevention of oxidant-induced cell death by lysosomotropic iron chelators. Free Radical Biol. Med. 34, 1295-1305
    • (2003) Free Radical Biol. Med. , vol.34 , pp. 1295-1305
    • Persson, H.L.1    Yu, Z.2    Tirosh, O.3    Eaton, J.W.4    Brunk, U.T.5
  • 19
    • 0029133790 scopus 로고
    • Cellular injury induced by oxidative stress is mediated through lysosomal damage
    • Öllinger, K. and Brunk, U. T. (1995) Cellular injury induced by oxidative stress is mediated through lysosomal damage. Free Radical Biol. Med. 19, 565-574
    • (1995) Free Radical Biol. Med. , vol.19 , pp. 565-574
    • Öllinger, K.1    Brunk, U.T.2
  • 20
    • 0034983544 scopus 로고    scopus 로고
    • Lysosomal involvement in apoptosis
    • Brunk, U. T., Neuzil, J. and Eaton, J. W. (2001) Lysosomal involvement in apoptosis. Redox Rep. 6, 91-97
    • (2001) Redox Rep. , vol.6 , pp. 91-97
    • Brunk, U.T.1    Neuzil, J.2    Eaton, J.W.3
  • 22
    • 0035887215 scopus 로고    scopus 로고
    • Sphingosine-induced apoptosis is dependent on lysosomal proteases
    • Kågedal, K., Zhao, M., Svensson, I. and Brunk, U. T. (2001) Sphingosine-induced apoptosis is dependent on lysosomal proteases. Biochem. J. 359, 335-343
    • (2001) Biochem. J. , vol.359 , pp. 335-343
    • Kågedal, K.1    Zhao, M.2    Svensson, I.3    Brunk, U.T.4
  • 24
    • 0021337104 scopus 로고
    • Iron-catalyzed hydroxyl radical formation. Stringent requirement for free iron coordination site
    • Graf, E., Mahoney, J. R., Bryant, R. G. and Eaton, J. W. (1984) Iron-catalyzed hydroxyl radical formation. Stringent requirement for free iron coordination site. J. Biol. Chem. 259, 3620-3624
    • (1984) J. Biol. Chem. , vol.259 , pp. 3620-3624
    • Graf, E.1    Mahoney, J.R.2    Bryant, R.G.3    Eaton, J.W.4
  • 25
    • 0021813287 scopus 로고
    • Cellular pharmacology of deferrioxamine B and derivatives in cultured rat hepatocytes in relation to iron mobilization
    • Laub, R., Schneider, Y. J., Octave, J. N., Trouet, A. and Crichton, R. R. (1985) Cellular pharmacology of deferrioxamine B and derivatives in cultured rat hepatocytes in relation to iron mobilization. Biochem. Pharmacol. 34, 1175-1183
    • (1985) Biochem. Pharmacol. , vol.34 , pp. 1175-1183
    • Laub, R.1    Schneider, Y.J.2    Octave, J.N.3    Trouet, A.4    Crichton, R.R.5
  • 26
    • 0033066791 scopus 로고    scopus 로고
    • Cellular uptake and release of two contrasting iron chelators
    • Cable, H. and Lloyd, J. B. (1999) Cellular uptake and release of two contrasting iron chelators. J. Pharm. Pharmacol. 51, 131-134
    • (1999) J. Pharm. Pharmacol. , vol.51 , pp. 131-134
    • Cable, H.1    Lloyd, J.B.2
  • 27
    • 0025974150 scopus 로고
    • Evidence that desferrioxamine cannot enter cells by passive diffusion
    • Lloyd, J. B., Cable, H. and Rice-Evans, C. (1991) Evidence that desferrioxamine cannot enter cells by passive diffusion. Biochem. Pharmacol. 41, 1361-1363
    • (1991) Biochem. Pharmacol. , vol.41 , pp. 1361-1363
    • Lloyd, J.B.1    Cable, H.2    Rice-Evans, C.3
  • 28
    • 0142227699 scopus 로고    scopus 로고
    • Endosomal and lysosomal effects of desferrioxamine: Protection of HeLa cells from hydrogen peroxide-induced DNA damage and induction of cell-cycle arrest
    • Doulias, P. T., Christoforidis, S., Brunk, U. T. and Galaris, D. (2003) Endosomal and lysosomal effects of desferrioxamine: protection of HeLa cells from hydrogen peroxide-induced DNA damage and induction of cell-cycle arrest. Free Radical Biol. Med. 35, 719-728
    • (2003) Free Radical Biol. Med. , vol.35 , pp. 719-728
    • Doulias, P.T.1    Christoforidis, S.2    Brunk, U.T.3    Galaris, D.4
  • 29
    • 0041430881 scopus 로고    scopus 로고
    • I-selegiline potentiates the cellular poly(ADP-ribosyl)ation response to ionizing radiation
    • Brabeck, C., Pfeiffer, R., Leake, A., Beneke, S., Meyer, R. and Bürkle, A. (2003) I-selegiline potentiates the cellular poly(ADP-ribosyl)ation response to ionizing radiation. J. Pharmacol. Exp. Ther. 306, 973-979
    • (2003) J. Pharmacol. Exp. Ther. , vol.306 , pp. 973-979
    • Brabeck, C.1    Pfeiffer, R.2    Leake, A.3    Beneke, S.4    Meyer, R.5    Bürkle, A.6
  • 30
    • 0019476174 scopus 로고
    • Fluorometric method for rapid detection of DNA strand breaks in human white blood cells produced by low doses of radiation
    • Birnboim, H. C. and Jevcak, J. J. (1981) Fluorometric method for rapid detection of DNA strand breaks in human white blood cells produced by low doses of radiation. Cancer Res. 41, 1889-1892
    • (1981) Cancer Res. , vol.41 , pp. 1889-1892
    • Birnboim, H.C.1    Jevcak, J.J.2
  • 31
    • 0033954684 scopus 로고    scopus 로고
    • Accumulation of single-strand breaks is the major cause of telomere shortening in human fibroblasts
    • von Zglinicki, T., Pilger, R. and Sitte, N. (2000) Accumulation of single-strand breaks is the major cause of telomere shortening in human fibroblasts. Free Radical Biol. Med. 28, 64-74
    • (2000) Free Radical Biol. Med. , vol.28 , pp. 64-74
    • Von Zglinicki, T.1    Pilger, R.2    Sitte, N.3
  • 32
    • 0031821009 scopus 로고    scopus 로고
    • Preferential accumulation of single-stranded regions in telomeres of human fibroblasts
    • Petersen, S., Saretzki, G. and von Zglinicki, T. (1998) Preferential accumulation of single-stranded regions in telomeres of human fibroblasts. Exp. Cell Res. 239, 152-160
    • (1998) Exp. Cell Res. , vol.239 , pp. 152-160
    • Petersen, S.1    Saretzki, G.2    Von Zglinicki, T.3
  • 33
    • 0032054781 scopus 로고    scopus 로고
    • Accelerated telomere shortening in fibroblasts after extended periods of confluency
    • Sitte, N., Saretzki, G. and von Zglinicki, T. (1998) Accelerated telomere shortening in fibroblasts after extended periods of confluency. Free Radical Biol. Med. 24, 885-893
    • (1998) Free Radical Biol. Med. , vol.24 , pp. 885-893
    • Sitte, N.1    Saretzki, G.2    Von Zglinicki, T.3
  • 34
    • 0025279931 scopus 로고
    • Telomeres shorten during ageing of human fibroblasts
    • Harley, C. B., Futcher, A. B. and Greider, C. W. (1990) Telomeres shorten during ageing of human fibroblasts. Nature (London) 345, 458-460
    • (1990) Nature (London) , vol.345 , pp. 458-460
    • Harley, C.B.1    Futcher, A.B.2    Greider, C.W.3
  • 35
    • 0035861903 scopus 로고    scopus 로고
    • Delayed oxidant-induced cell death involves activation of phospholipase A2
    • Zhao, M., Brunk, U. T. and Eaton, J. W. (2001) Delayed oxidant-induced cell death involves activation of phospholipase A2. FEBS Lett. 509, 399-404
    • (2001) FEBS Lett. , vol.509 , pp. 399-404
    • Zhao, M.1    Brunk, U.T.2    Eaton, J.W.3
  • 36
    • 0035057746 scopus 로고    scopus 로고
    • Novel cellular defenses against iron and oxidation: Ferritin and autophagocytosis preserve lysosomal stability in airway epithelium
    • Persson, H. L., Nilsson, K. J. and Brunk, U. T. (2001) Novel cellular defenses against iron and oxidation: ferritin and autophagocytosis preserve lysosomal stability in airway epithelium. Redox Rep. 6, 57-63
    • (2001) Redox Rep. , vol.6 , pp. 57-63
    • Persson, H.L.1    Nilsson, K.J.2    Brunk, U.T.3
  • 38
    • 0036629255 scopus 로고    scopus 로고
    • Oxidative stress shortens telomeres
    • von Zglinicki, T. (2002) Oxidative stress shortens telomeres. Trends Biochem. Sci. 27, 339-344
    • (2002) Trends Biochem. Sci. , vol.27 , pp. 339-344
    • Von Zglinicki, T.1
  • 39
    • 0021348493 scopus 로고
    • Cell killing and DNA damage by hydrogen peroxide are mediated by intracellular iron
    • Mello Filho, A. C., Hoffmann, M. E. and Meneghini, R. (1984) Cell killing and DNA damage by hydrogen peroxide are mediated by intracellular iron. Biochem. J. 218, 273-275
    • (1984) Biochem. J. , vol.218 , pp. 273-275
    • Mello Filho, A.C.1    Hoffmann, M.E.2    Meneghini, R.3
  • 40
    • 0023886170 scopus 로고
    • DNA damage and oxygen radical toxicity
    • Imlay, J. A. and Linn, S. (1988) DNA damage and oxygen radical toxicity. Science 240, 1302-1309
    • (1988) Science , vol.240 , pp. 1302-1309
    • Imlay, J.A.1    Linn, S.2
  • 41
    • 0028575839 scopus 로고
    • Three chemically distinct types of oxidants formed by iron-mediated Fenton reactions in the presence of DNA
    • Luo, Y., Han, Z., Chin, S. M. and Linn, S. (1994) Three chemically distinct types of oxidants formed by iron-mediated Fenton reactions in the presence of DNA. Proc. Natl. Acad. Sci. U.S.A. 91, 12438-12442
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 12438-12442
    • Luo, Y.1    Han, Z.2    Chin, S.M.3    Linn, S.4
  • 43
    • 0032189907 scopus 로고    scopus 로고
    • Hydrogen peroxide-induced DNA damage is independent of nuclear calcium but dependent on redox-active ions
    • Jornot, L., Petersen, H. and Junod, A. F. (1998) Hydrogen peroxide-induced DNA damage is independent of nuclear calcium but dependent on redox-active ions. Biochem. J. 335, 85-94
    • (1998) Biochem. J. , vol.335 , pp. 85-94
    • Jornot, L.1    Petersen, H.2    Junod, A.F.3
  • 44
    • 0035882247 scopus 로고    scopus 로고
    • Intracellular iron, but not copper, plays a critical role in hydrogen peroxide-induced DNA damage
    • Barbouti, A., Doulias, P. T., Zhu, B. Z., Frei, B. and Galaris, D. (2001) Intracellular iron, but not copper, plays a critical role in hydrogen peroxide-induced DNA damage. Free Radical Biol. Med. 31, 490-498
    • (2001) Free Radical Biol. Med. , vol.31 , pp. 490-498
    • Barbouti, A.1    Doulias, P.T.2    Zhu, B.Z.3    Frei, B.4    Galaris, D.5
  • 45
    • 0034656371 scopus 로고    scopus 로고
    • Acidic pH amplifies iron-mediated lipid peroxidation in cells
    • Schafer, F. Q. and Buettner, G. R. (2000) Acidic pH amplifies iron-mediated lipid peroxidation in cells. Free Radical Biol. Med. 28, 1175-1181
    • (2000) Free Radical Biol. Med. , vol.28 , pp. 1175-1181
    • Schafer, F.Q.1    Buettner, G.R.2
  • 46
    • 0025098737 scopus 로고
    • A cysteine-specific lysosomal transport system provides a major route for the delivery of thiol to human fibroblast lysosomes: Possible role in supporting lysosomal proteolysis
    • Pisoni, R. L., Acker, T. L., Lisowski, K. M., Lemons, R. M. and Thoene, J. G. (1990) A cysteine-specific lysosomal transport system provides a major route for the delivery of thiol to human fibroblast lysosomes: possible role in supporting lysosomal proteolysis. J. Cell Biol. 110, 327-335
    • (1990) J. Cell Biol. , vol.110 , pp. 327-335
    • Pisoni, R.L.1    Acker, T.L.2    Lisowski, K.M.3    Lemons, R.M.4    Thoene, J.G.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.