메뉴 건너뛰기




Volumn 293, Issue 4, 2007, Pages

Non-transferrin-bound iron reaches mitochondria by a chelator-inaccessible mechanism: Biological and clinical implications

Author keywords

Fluorescence; Oxidative stress; Transport

Indexed keywords

AMMONIUM SULFATE; CALCEIN; CHELATING AGENT; DEFEROXAMINE; ETHYLENE GLYCOL 1,2 BIS(2 AMINOPHENYL) ETHER N,N,N',N' TETRAACETIC ACID; FERRIC AMMONIUM CITRATE; FERRIC CITRATE; FERRIC HYDROXYQUINOLINE; FERROUS AMMONIUM SULFATE; IRON; QUINOLINOL DERIVATIVE; REACTIVE OXYGEN METABOLITE; RHODAMINE B; TRANSFERRIN; UNCLASSIFIED DRUG;

EID: 35048833703     PISSN: 03636143     EISSN: 15221563     Source Type: Journal    
DOI: 10.1152/ajpcell.00054.2007     Document Type: Article
Times cited : (71)

References (44)
  • 2
    • 14544268521 scopus 로고    scopus 로고
    • Molecular control of iron metabolism
    • Andrews NC. Molecular control of iron metabolism. Best Pract Res Clin Haematol 18: 159-169, 2005.
    • (2005) Best Pract Res Clin Haematol , vol.18 , pp. 159-169
    • Andrews, N.C.1
  • 4
    • 0028834446 scopus 로고
    • Iron acquired from transferrin by K562 cells is delivered into a cytoplasmic pool of chelatable iron(II)
    • Breuer W, Epzstejn S, Cabantchik ZI. Iron acquired from transferrin by K562 cells is delivered into a cytoplasmic pool of chelatable iron(II). J Biol Chem 270: 24209-24215, 1995.
    • (1995) J Biol Chem , vol.270 , pp. 24209-24215
    • Breuer, W.1    Epzstejn, S.2    Cabantchik, Z.I.3
  • 5
    • 0032007849 scopus 로고    scopus 로고
    • Binding of iron and inhibition of iron-dependent oxidative cell injury by the "calcium chelator" 1,2-bis(2-aminophenoxy)ethane N,N,N′,N′-tetraacetic acid (BAPTA)
    • Britigan BE, Rasmussen GT, Cox CD. Binding of iron and inhibition of iron-dependent oxidative cell injury by the "calcium chelator" 1,2-bis(2-aminophenoxy)ethane N,N,N′,N′-tetraacetic acid (BAPTA). Biochem Pharmacol 55: 287-295, 1998.
    • (1998) Biochem Pharmacol , vol.55 , pp. 287-295
    • Britigan, B.E.1    Rasmussen, G.T.2    Cox, C.D.3
  • 7
    • 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
    • Cozzi A, Corsi B, Levi S, Santambrogio P, Albertini A, Arosio P. Overexpression of wild type and mutated human ferritin H-chain in HeLa cells: in vivo role of ferritin ferroxidase activity. J Biol Chem 275: 25122-25129, 2000.
    • (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
  • 8
    • 0037173578 scopus 로고    scopus 로고
    • Molecular and cellular mechanisms of iron homeostasis and toxicity in mammalian cells
    • Crichton RR, Wilmet S, Legssyer R, Ward RJ. Molecular and cellular mechanisms of iron homeostasis and toxicity in mammalian cells. J Inorg Biochem 91: 9-18, 2002.
    • (2002) J Inorg Biochem , vol.91 , pp. 9-18
    • Crichton, R.R.1    Wilmet, S.2    Legssyer, R.3    Ward, R.J.4
  • 9
    • 0034069008 scopus 로고    scopus 로고
    • Preparation, properties, and reactions of metal-containing heterocycles. 101. Inclusion of copper(I) into a novel bipyridine containing tetraphosphadiplatinacyclophane
    • Ekkehard L, Veigel R, Ortner K, Nachtigal C, Steimann M. Preparation, properties, and reactions of metal-containing heterocycles. 101. Inclusion of copper(I) into a novel bipyridine containing tetraphosphadiplatinacyclophane. Eur J Inorg Chem 5: 959-969, 2000.
    • (2000) Eur J Inorg Chem , vol.5 , pp. 959-969
    • Ekkehard, L.1    Veigel, R.2    Ortner, K.3    Nachtigal, C.4    Steimann, M.5
  • 10
    • 0036570964 scopus 로고    scopus 로고
    • A review of fluorescence methods for assessing labile iron in cells and biological fluids
    • Esposito BP, Epsztejn S, Breuer W, Cabantchik ZI. A review of fluorescence methods for assessing labile iron in cells and biological fluids. Anal Biochem 304: 1-18, 2002.
    • (2002) Anal Biochem , vol.304 , pp. 1-18
    • Esposito, B.P.1    Epsztejn, S.2    Breuer, W.3    Cabantchik, Z.I.4
  • 11
    • 0037993832 scopus 로고    scopus 로고
    • Transition metal speciation in the cell: Insights from the chemistry of metal ion receptors
    • Finney LA, O'Halloran TV. Transition metal speciation in the cell: insights from the chemistry of metal ion receptors. Science 300: 931-936, 2003.
    • (2003) Science , vol.300 , pp. 931-936
    • Finney, L.A.1    O'Halloran, T.V.2
  • 12
    • 27644539382 scopus 로고    scopus 로고
    • Intracellular labile iron pools as direct targets of iron chelators: A fluorescence study of chelator action in living cells
    • Glickstein H, Ben-El R, Shvartsman M, Cabantchik ZI. Intracellular labile iron pools as direct targets of iron chelators: a fluorescence study of chelator action in living cells. Blood 106: 3242-3250, 2005.
    • (2005) Blood , vol.106 , pp. 3242-3250
    • Glickstein, H.1    Ben-El, R.2    Shvartsman, M.3    Cabantchik, Z.I.4
  • 13
    • 33750001927 scopus 로고    scopus 로고
    • Action of chelators in iron-loaded cardiac cells: Accessibility to intracellular labile iron and functional consequences
    • Glickstein H, Ben-El R, Link G, Breuer W, Konijn AM, Hershko C, Nick H, Cabantchik ZI. Action of chelators in iron-loaded cardiac cells: accessibility to intracellular labile iron and functional consequences. Blood 108: 3195-3203, 2006.
    • (2006) Blood , vol.108 , pp. 3195-3203
    • Glickstein, H.1    Ben-El, R.2    Link, G.3    Breuer, W.4    Konijn, A.M.5    Hershko, C.6    Nick, H.7    Cabantchik, Z.I.8
  • 14
    • 2042546096 scopus 로고    scopus 로고
    • Balancing acts: Molecular control of mammalian iron metabolism
    • Hentze MW, Muckenthaler MU, Andrews NC. Balancing acts: molecular control of mammalian iron metabolism. Cell 117: 285-297, 2004.
    • (2004) Cell , vol.117 , pp. 285-297
    • Hentze, M.W.1    Muckenthaler, M.U.2    Andrews, N.C.3
  • 15
    • 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, Junod AF. Hydrogen peroxide-induced DNA damage is independent of nuclear calcium but dependent on redox-active ions. Biochem J 335: 85-94, 1998.
    • (1998) Biochem J , vol.335 , pp. 85-94
    • Jornot, L.1    Petersen, H.2    Junod, A.F.3
  • 16
    • 0033082143 scopus 로고    scopus 로고
    • Cardioprotective effect of α-tocopherol, ascorbate, deferoxamine, and deferiprone: Mitochondrial function in cultured, iron-loaded heart cells
    • Link G, Konijn AM, Hershko C. Cardioprotective effect of α-tocopherol, ascorbate, deferoxamine, and deferiprone: mitochondrial function in cultured, iron-loaded heart cells. J Lab Clin Med 133: 179-188, 1999.
    • (1999) J Lab Clin Med , vol.133 , pp. 179-188
    • Link, G.1    Konijn, A.M.2    Hershko, C.3
  • 17
    • 0036136401 scopus 로고    scopus 로고
    • Design of clinically useful iron(III)-selective chelators
    • Liu ZD, Hider RC. Design of clinically useful iron(III)-selective chelators. Med Res Rev 22: 26-64, 2002.
    • (2002) Med Res Rev , vol.22 , pp. 26-64
    • Liu, Z.D.1    Hider, R.C.2
  • 18
    • 0344420004 scopus 로고    scopus 로고
    • The many highways for intracellular trafficking of metals
    • Luk E, Jensen LT, Culotta VC. The many highways for intracellular trafficking of metals. J Biol Inorg Chem 8: 803-809, 2003.
    • (2003) J Biol Inorg Chem , vol.8 , pp. 803-809
    • Luk, E.1    Jensen, L.T.2    Culotta, V.C.3
  • 20
    • 33748711220 scopus 로고    scopus 로고
    • PANK2 gene analysis confirms genetic heterogeneity in neurodegeneration with brain iron accumulation (NBIA), but mutations are rare in other types of adult neurodegenerative disease
    • Matarin MM, Singleton AB, Houlden H. PANK2 gene analysis confirms genetic heterogeneity in neurodegeneration with brain iron accumulation (NBIA), but mutations are rare in other types of adult neurodegenerative disease. Neurosci Lett 407: 162-165, 2006.
    • (2006) Neurosci Lett , vol.407 , pp. 162-165
    • Matarin, M.M.1    Singleton, A.B.2    Houlden, H.3
  • 21
    • 0037202135 scopus 로고    scopus 로고
    • Synthesis and evaluation of iron chelators with masked hydrophilic moieties
    • Meijler MM, Arad-Yellin R, Cabantchik ZI, Shanzer A. Synthesis and evaluation of iron chelators with masked hydrophilic moieties. J Am Chem Soc 124: 12666-12667, 2002.
    • (2002) J Am Chem Soc , vol.124 , pp. 12666-12667
    • Meijler, M.M.1    Arad-Yellin, R.2    Cabantchik, Z.I.3    Shanzer, A.4
  • 22
    • 33644869168 scopus 로고    scopus 로고
    • Vesicular transport and apotransferrin in intestinal iron absorption, as shown in the Caco-2 cell model
    • Moriya M, Linder MC. Vesicular transport and apotransferrin in intestinal iron absorption, as shown in the Caco-2 cell model. Am J Physiol Gastrointest Liver Physiol 290: G301-G309, 2006.
    • (2006) Am J Physiol Gastrointest Liver Physiol , vol.290
    • Moriya, M.1    Linder, M.C.2
  • 24
    • 14944387002 scopus 로고    scopus 로고
    • Iron trafficking in the mitochondrion: Novel pathways revealed by disease
    • Napier I, Ponka P, Richardson DR. Iron trafficking in the mitochondrion: novel pathways revealed by disease. Blood 105: 1867-1874, 2005.
    • (2005) Blood , vol.105 , pp. 1867-1874
    • Napier, I.1    Ponka, P.2    Richardson, D.R.3
  • 26
    • 1242317666 scopus 로고    scopus 로고
    • The mitochondrial transporter family (SLC25): Physiological and pathological implications
    • Palmieri F. The mitochondrial transporter family (SLC25): physiological and pathological implications. Pflügers Arch 447: 689-709, 2004.
    • (2004) Pflügers Arch , vol.447 , pp. 689-709
    • Palmieri, F.1
  • 27
    • 0642287902 scopus 로고    scopus 로고
    • Iron metabolism and mitochondrial abnormalities in Friedreich ataxia
    • Pandolfo M. Iron metabolism and mitochondrial abnormalities in Friedreich ataxia. Blood Cells Mol Dis 29: 536-552, 2002.
    • (2002) Blood Cells Mol Dis , vol.29 , pp. 536-552
    • Pandolfo, M.1
  • 28
    • 1842608845 scopus 로고    scopus 로고
    • Iron metabolism and the IRE/IRP regulatory system: An update
    • Pantopoulos K. Iron metabolism and the IRE/IRP regulatory system: an update. Ann NY Acad Sci 1012: 1-13, 2004.
    • (2004) Ann NY Acad Sci , vol.1012 , pp. 1-13
    • Pantopoulos, K.1
  • 29
    • 0037083893 scopus 로고    scopus 로고
    • Selective determination of mitochondrial chelatable iron in viable cells with a new fluorescent sensor
    • Petrat F, Weisheit D, Lensen M, De Groot H, Sustmann R, Rauen U. Selective determination of mitochondrial chelatable iron in viable cells with a new fluorescent sensor. Biochem J 362: 137-147, 2002.
    • (2002) Biochem J , vol.362 , pp. 137-147
    • Petrat, F.1    Weisheit, D.2    Lensen, M.3    De Groot, H.4    Sustmann, R.5    Rauen, U.6
  • 30
    • 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 MW, Grandchamp B, Beaumont C. Overexpression of the ferritin H subunit in cultured erythroid cells changes the intracellular iron distribution. Blood 87: 2057-2064, 1996.
    • (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
  • 31
    • 0032546922 scopus 로고    scopus 로고
    • Role of ferritin in the control of the labile iron pool in murine erythroleukemia cells
    • Picard V, Epsztejn S, Santambrogio P, Cabantchik ZI, Beaumont C. Role of ferritin in the control of the labile iron pool in murine erythroleukemia cells. J Biol Chem 273: 15382-15386, 1998.
    • (1998) J Biol Chem , vol.273 , pp. 15382-15386
    • Picard, V.1    Epsztejn, S.2    Santambrogio, P.3    Cabantchik, Z.I.4    Beaumont, C.5
  • 33
    • 0031028178 scopus 로고    scopus 로고
    • Tissue-specific regulation of iron metabolism and heme synthesis: Distinct control mechanisms in erythroid cells
    • Ponka P. Tissue-specific regulation of iron metabolism and heme synthesis: distinct control mechanisms in erythroid cells. Blood 90: 1-25, 1997.
    • (1997) Blood , vol.90 , pp. 1-25
    • Ponka, P.1
  • 34
    • 0021676080 scopus 로고
    • The effect of various chelating agents on the mobilization of iron from reticulocytes in the presence and absence of pyridoxal isonicotinoyl hydrazone
    • Ponka P, Grady RW, Wilczynska A, Schulman HM. The effect of various chelating agents on the mobilization of iron from reticulocytes in the presence and absence of pyridoxal isonicotinoyl hydrazone. Biochim Biophys Acta 802: 477-489, 1984.
    • (1984) Biochim Biophys Acta , vol.802 , pp. 477-489
    • Ponka, P.1    Grady, R.W.2    Wilczynska, A.3    Schulman, H.M.4
  • 35
    • 0035978474 scopus 로고    scopus 로고
    • Development of potential iron chelators for the treatment of Friedreich's ataxia: Ligands that mobilize mitochondrial iron
    • Richardson DR, Mouralian C, Ponka P, Becker E. Development of potential iron chelators for the treatment of Friedreich's ataxia: ligands that mobilize mitochondrial iron. Biochim Biophys Acta 1536: 133-140, 2001.
    • (2001) Biochim Biophys Acta , vol.1536 , pp. 133-140
    • Richardson, D.R.1    Mouralian, C.2    Ponka, P.3    Becker, E.4
  • 36
    • 0033559011 scopus 로고    scopus 로고
    • Influence of calcium and iron on cell death and mitochondrial function in oxidatively stressed astrocytes
    • Robb SJ, Robb-Gaspers LD, Scaduto RC, Thomas AP, Connor JR. Influence of calcium and iron on cell death and mitochondrial function in oxidatively stressed astrocytes. J Neurosci Res 55: 674-686, 1999.
    • (1999) J Neurosci Res , vol.55 , pp. 674-686
    • Robb, S.J.1    Robb-Gaspers, L.D.2    Scaduto, R.C.3    Thomas, A.P.4    Connor, J.R.5
  • 37
    • 33644555509 scopus 로고    scopus 로고
    • Mitochondrial carriers in the cytoplasmic state have a common substrate binding site
    • Robinson AJ, Kunji ERS. Mitochondrial carriers in the cytoplasmic state have a common substrate binding site. Proc Natl Acad Sci USA 103: 2617-2622, 2006.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 2617-2622
    • Robinson, A.J.1    Kunji, E.R.S.2
  • 38
    • 0035964737 scopus 로고    scopus 로고
    • The iron chelator pyridoxal isonicotinoyl hydrazone inhibits mitochondrial lipid peroxidation induced by Fe(II)-citrate
    • Santos NCF, Castilho RF, Meinicke AR, Hermes-Lima M. The iron chelator pyridoxal isonicotinoyl hydrazone inhibits mitochondrial lipid peroxidation induced by Fe(II)-citrate. Eur J Pharmacol 428: 37-44, 2001.
    • (2001) Eur J Pharmacol , vol.428 , pp. 37-44
    • Santos, N.C.F.1    Castilho, R.F.2    Meinicke, A.R.3    Hermes-Lima, M.4
  • 39
    • 0032958211 scopus 로고    scopus 로고
    • Schubert US, Eschbaumer C, Hochwimmer G. High yield synthesis of 5,5′-dimethyl-2,2′-bipyridine and 5,5″-dimethyl-2,2′: 6′,2″-terpyridine and some bisfunctionalization reactions using N-bromosuccinimide. Synthesis 5: 779-782, 1999.
    • Schubert US, Eschbaumer C, Hochwimmer G. High yield synthesis of 5,5′-dimethyl-2,2′-bipyridine and 5,5″-dimethyl-2,2′: 6′,2″-terpyridine and some bisfunctionalization reactions using N-bromosuccinimide. Synthesis 5: 779-782, 1999.
  • 41
    • 34347375300 scopus 로고    scopus 로고
    • Ponka P. Direct interorganellar transfer of iron from endosome to mitochondrion
    • Sheftel AD, Zhang AS, Brown C, Shirihai OS, 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
  • 42
    • 0037944100 scopus 로고    scopus 로고
    • Involvement of ABC7 in the biosynthesis of heme in erythroid cells: Interaction of ABC7 with ferrochelatase
    • Taketani S, Kakimoto K, Ueta H, Masaki R, Furukawa T. Involvement of ABC7 in the biosynthesis of heme in erythroid cells: interaction of ABC7 with ferrochelatase. Blood 101: 3274-3280, 2003.
    • (2003) Blood , vol.101 , pp. 3274-3280
    • Taketani, S.1    Kakimoto, K.2    Ueta, H.3    Masaki, R.4    Furukawa, T.5
  • 44
    • 11144226961 scopus 로고    scopus 로고
    • Ponka P. Intracellular kinetics of iron in reticulocytes: Evidence for endosome involvement in iron targeting to mitochondria
    • Zhang AS, Sheftel AD, Ponka P. Intracellular kinetics of iron in reticulocytes: evidence for endosome involvement in iron targeting to mitochondria. Blood 105: 368-375, 2005.
    • (2005) Blood , vol.105 , pp. 368-375
    • Zhang, A.S.1    Sheftel, A.D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.