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Volumn 73, Issue 1, 2003, Pages 113-121

Hemin induces an iron-dependent, oxidative injury to human neuron-like cells

Author keywords

CNS hemorrhage; Free radical; Hemoglobin toxicity; Neuron

Indexed keywords

BRAIN DERIVED NEUROTROPHIC FACTOR; CASPASE INHIBITOR; DEFEROXAMINE; GLUTATHIONE; HEME OXYGENASE 1; HEME OXYGENASE 2; HEMIN; HEMOGLOBIN; IRON; IRON CHELATE; MERCAPTOETHANOL; PHENANTHROLINE DERIVATIVE; REACTIVE OXYGEN METABOLITE; RETINOIC ACID; THIOL DERIVATIVE; UNCLASSIFIED DRUG;

EID: 0037716283     PISSN: 03604012     EISSN: None     Source Type: Journal    
DOI: 10.1002/jnr.10633     Document Type: Article
Times cited : (138)

References (62)
  • 3
    • 0021322523 scopus 로고
    • Hemin-mediated oxidative degradation of proteins
    • Aft RL, Mueller GC. 1984. Hemin-mediated oxidative degradation of proteins. J Biol Chem 259:301-305.
    • (1984) J Biol Chem , vol.259 , pp. 301-305
    • Aft, R.L.1    Mueller, G.C.2
  • 4
    • 0028828562 scopus 로고
    • Heme degradation in the presence of glutathione. A proposed mechanism to account for the high levels of nonheme iron found in the membranes of hemoglobinopathic red blood cells
    • Atamna H, Ginsberg, H. 1995. Heme degradation in the presence of glutathione. A proposed mechanism to account for the high levels of nonheme iron found in the membranes of hemoglobinopathic red blood cells. J Biol Chem 270:24876-24883.
    • (1995) J Biol Chem , vol.270 , pp. 24876-24883
    • Atamna, H.1    Ginsberg, H.2
  • 5
    • 0021330045 scopus 로고
    • The interaction of hemin with skeletal muscle actin
    • Avissar N, Shaklai M, Shaklai N. 1984. The interaction of hemin with skeletal muscle actin. Biochim Biophys Acta 786:179-187.
    • (1984) Biochim Biophys Acta , vol.786 , pp. 179-187
    • Avissar, N.1    Shaklai, M.2    Shaklai, N.3
  • 7
    • 0018117240 scopus 로고
    • Binding of protoporphyrin and haemin to human spectrin
    • Beaven GH, Gratzer WB. 1978. Binding of protoporphyrin and haemin to human spectrin. Acta Haematol 60:321-328.
    • (1978) Acta Haematol , vol.60 , pp. 321-328
    • Beaven, G.H.1    Gratzer, W.B.2
  • 9
    • 0029598771 scopus 로고
    • Hemin toxicity in a human epithelioid sarcoma cell line
    • Braverman S, Helson C, Helson L. 1995. Hemin toxicity in a human epithelioid sarcoma cell line. Anticancer Res 15:1963-1967.
    • (1995) Anticancer Res , vol.15 , pp. 1963-1967
    • Braverman, S.1    Helson, C.2    Helson, L.3
  • 10
    • 0038653828 scopus 로고
    • Rahway, NJ: Merck and Co.
    • Budavari S, editor. 1989. The Merck index. Rahway, NJ: Merck and Co. p1606.
    • (1989) The Merck Index , pp. 1606
    • Budavari, S.1
  • 11
    • 0014408353 scopus 로고
    • Exchange of heme along hemoglobins and between hemoglobin and albumin
    • Bunn HF, Jandl JH. 1967. Exchange of heme along hemoglobins and between hemoglobin and albumin. J Biol Chem 243:465-475.
    • (1967) J Biol Chem , vol.243 , pp. 465-475
    • Bunn, H.F.1    Jandl, J.H.2
  • 12
    • 0033066791 scopus 로고    scopus 로고
    • Cellular uptake and release of two contrasting iron chelators
    • Cable H, Lloyd JB. 1998. Cellular uptake and release of two contrasting iron chelators. J Pharm Pharmacol 51:131-134.
    • (1998) J Pharm Pharmacol , vol.51 , pp. 131-134
    • Cable, H.1    Lloyd, J.B.2
  • 13
    • 0032511729 scopus 로고    scopus 로고
    • Cellular distribution of ferritin subunits in postnatal rat brain
    • Cheepsunthorn P, Palmer C, Connor JR. 1998. Cellular distribution of ferritin subunits in postnatal rat brain. J Comp Neurol 400:73-86.
    • (1998) J Comp Neurol , vol.400 , pp. 73-86
    • Cheepsunthorn, P.1    Palmer, C.2    Connor, J.R.3
  • 14
    • 0024600910 scopus 로고
    • Oxidative hemoglobin denaturation and RBC destruction: The effect of heme on red cell membranes
    • Chiu D, Lubin B. 1989. Oxidative hemoglobin denaturation and RBC destruction: the effect of heme on red cell membranes. Semin Hematol 26:128-135.
    • (1989) Semin Hematol , vol.26 , pp. 128-135
    • Chiu, D.1    Lubin, B.2
  • 15
    • 0030843570 scopus 로고    scopus 로고
    • Hemin-induced membrane sulfhydryl oxidation: Possible involvement of thiyl radicals
    • Chiu DT, Huang TY, Hung IJ, Wei JS, Liu TZ, Stern A. 1997. Hemin-induced membrane sulfhydryl oxidation: possible involvement of thiyl radicals. Free Radic Res 27:55-62.
    • (1997) Free Radic Res , vol.27 , pp. 55-62
    • Chiu, D.T.1    Huang, T.Y.2    Hung, I.J.3    Wei, J.S.4    Liu, T.Z.5    Stern, A.6
  • 16
    • 0019355321 scopus 로고
    • Mechanism of hemolysis induced by ferriprotoporphyrin IX
    • Chou AC, Fitch CD. 1981. Mechanism of hemolysis induced by ferriprotoporphyrin IX. J Clin Invest 68:672-677.
    • (1981) J Clin Invest , vol.68 , pp. 672-677
    • Chou, A.C.1    Fitch, C.D.2
  • 20
    • 0031792792 scopus 로고    scopus 로고
    • Protective properties of tin- and manganese-centered porphyrins against hydrogen peroxide-mediated injury in rat astroglial cells
    • Dwyer BE, Lu SY, Laitinen JT, Nishimura RN. 1998. Protective properties of tin- and manganese-centered porphyrins against hydrogen peroxide-mediated injury in rat astroglial cells. J Neurochem 71:2497-2504.
    • (1998) J Neurochem , vol.71 , pp. 2497-2504
    • Dwyer, B.E.1    Lu, S.Y.2    Laitinen, J.T.3    Nishimura, R.N.4
  • 21
    • 0033844835 scopus 로고    scopus 로고
    • Sequential treatment of SH-SY5Y cells with retinoic acid and brain-derived neurotrophic factor gives rise to fully differentiated, neurotrophic factor-dependent, human neuron-like cells
    • Encinas M, Iglesias M, Liu Y, Wang H, Muhaisen A, Cena V, Gallego C, Comella JX. 2000. Sequential treatment of SH-SY5Y cells with retinoic acid and brain-derived neurotrophic factor gives rise to fully differentiated, neurotrophic factor-dependent, human neuron-like cells. J Neurochem 75:993-1003.
    • (2000) J Neurochem , vol.75 , pp. 993-1003
    • Encinas, M.1    Iglesias, M.2    Liu, Y.3    Wang, H.4    Muhaisen, A.5    Cena, V.6    Gallego, C.7    Comella, J.X.8
  • 22
    • 0030834118 scopus 로고    scopus 로고
    • Pitfalls using metalloporphyrins in carbon monoxide research
    • Grundemar L, Ny L. 1997. Pitfalls using metalloporphyrins in carbon monoxide research. Trends Pharmacol Sci 18:193-195.
    • (1997) Trends Pharmacol Sci , vol.18 , pp. 193-195
    • Grundemar, L.1    Ny, L.2
  • 23
    • 0022469346 scopus 로고
    • Iron promoters of the Fenton reaction and lipid peroxidation can be released from haemoglobin by peroxides
    • Gutteridge JMC. 1986. Iron promoters of the Fenton reaction and lipid peroxidation can be released from haemoglobin by peroxides. FEBS Lett 201:291-295.
    • (1986) FEBS Lett , vol.201 , pp. 291-295
    • Gutteridge, J.M.C.1
  • 24
    • 0024241523 scopus 로고
    • Antioxidant protection by haemopexin of haem-stimulated lipid peroxidation
    • Gutteridge JMC, Smith A. 1988. Antioxidant protection by haemopexin of haem-stimulated lipid peroxidation. Biochem J 256:861-865.
    • (1988) Biochem J , vol.256 , pp. 861-865
    • Gutteridge, J.M.C.1    Smith, A.2
  • 25
    • 0024790459 scopus 로고
    • Protection against tissue damage in vivo by desferrioxamine: What is its mechanism of action?
    • Halliwell B. 1989. Protection against tissue damage in vivo by desferrioxamine: what is its mechanism of action? Free Radic Biol Med 7:645-651.
    • (1989) Free Radic Biol Med , vol.7 , pp. 645-651
    • Halliwell, B.1
  • 27
    • 0027525152 scopus 로고
    • Changes in intracellular pH associated with glutamate excitotoxicity
    • Hartley Z, Dubinsky JM. 1993. Changes in intracellular pH associated with glutamate excitotoxicity. J Neurosci 13:4690-4699.
    • (1993) J Neurosci , vol.13 , pp. 4690-4699
    • Hartley, Z.1    Dubinsky, J.M.2
  • 28
    • 0024551404 scopus 로고
    • Pathobiology of heme interaction with the erythrocyte membrane
    • Hebbel RP, Eaton JW. 1989. Pathobiology of heme interaction with the erythrocyte membrane. Semin Hematol 26:136-149.
    • (1989) Semin Hematol , vol.26 , pp. 136-149
    • Hebbel, R.P.1    Eaton, J.W.2
  • 29
    • 0034128227 scopus 로고    scopus 로고
    • Complement activation in the brain after experimental intracerebral hemorrhage
    • Hua Y, Xi G, Keep RF, Hoff JT. 2000. Complement activation in the brain after experimental intracerebral hemorrhage. J Neurosurg 92:1016-1022.
    • (2000) J Neurosurg , vol.92 , pp. 1016-1022
    • Hua, Y.1    Xi, G.2    Keep, R.F.3    Hoff, J.T.4
  • 30
    • 0036120064 scopus 로고    scopus 로고
    • Brain edema after experimental intracerebral hemorrhage: Role of hemoglobin degradation products
    • Huang FP, Xi G, Keep RF, Hua Y, Nemoianu A, Hoff JT. 2002. Brain edema after experimental intracerebral hemorrhage: role of hemoglobin degradation products. J Neurosurg 96:287-293.
    • (2002) J Neurosurg , vol.96 , pp. 287-293
    • Huang, F.P.1    Xi, G.2    Keep, R.F.3    Hua, Y.4    Nemoianu, A.5    Hoff, J.T.6
  • 32
    • 0032579512 scopus 로고    scopus 로고
    • Characterization and biological significance of immunosuppressive peptide D2702.75-84 (E→V)
    • Iyer S, Woo J, Cornejo MC, Gao L, McCoubrey W, Maines M, Buelow R. 1998. Characterization and biological significance of immunosuppressive peptide D2702.75-84 (E→V). J Biol Chem 273:2692-2697.
    • (1998) J Biol Chem , vol.273 , pp. 2692-2697
    • Iyer, S.1    Woo, J.2    Cornejo, M.C.3    Gao, L.4    McCoubrey, W.5    Maines, M.6    Buelow, R.7
  • 36
    • 0027234437 scopus 로고
    • Hemin: Levels in experimental subarachnoid hematoma and effects on dissociated vascular smooth muscle cells
    • Letarte PB, Lieberman K, Nagatani K, Haworth RA, Odell GB, Duff TA. 1993. Hemin: levels in experimental subarachnoid hematoma and effects on dissociated vascular smooth muscle cells. J Neurosurg 79:252-255.
    • (1993) J Neurosurg , vol.79 , pp. 252-255
    • Letarte, P.B.1    Lieberman, K.2    Nagatani, K.3    Haworth, R.A.4    Odell, G.B.5    Duff, T.A.6
  • 38
    • 0027738889 scopus 로고
    • Protoporphyrins modulate voltage-gated calcium current in AtT-20 pituitary cells
    • Linden DJ, Narisimhan K, Gurfel D. 1993. Protoporphyrins modulate voltage-gated calcium current in AtT-20 pituitary cells. J Neurophysiol 70:2673-2677.
    • (1993) J Neurophysiol , vol.70 , pp. 2673-2677
    • Linden, D.J.1    Narisimhan, K.2    Gurfel, D.3
  • 39
    • 0028176233 scopus 로고
    • Metalloporphyrins inhibit nitric oxide-dependent cGMP formation in vivo
    • Luo D, Vincent SR. 1994. Metalloporphyrins inhibit nitric oxide-dependent cGMP formation in vivo. Eur J Pharmacol 267:263-267.
    • (1994) Eur J Pharmacol , vol.267 , pp. 263-267
    • Luo, D.1    Vincent, S.R.2
  • 40
    • 1842330947 scopus 로고    scopus 로고
    • Heme oxygenase-2 is a hemoprotein and binds heme through heme regulatory motifs that are not involved in heme catalysis
    • McCoubrey WK, Huang TJ, Maines MD. 1997. Heme oxygenase-2 is a hemoprotein and binds heme through heme regulatory motifs that are not involved in heme catalysis. J Biol Chem 272:12568-12574.
    • (1997) J Biol Chem , vol.272 , pp. 12568-12574
    • McCoubrey, W.K.1    Huang, T.J.2    Maines, M.D.3
  • 41
    • 0028067882 scopus 로고
    • Inhibition of hippocampal heme oxygenase, nitric oxide synthase, and long-term potentiation by metalloporphyrins
    • Meffert MK, Haley JE, Schuman EM, Schulman H, Madison DV. 1994. Inhibition of hippocampal heme oxygenase, nitric oxide synthase, and long-term potentiation by metalloporphyrins. Neuron 13:1225-1233.
    • (1994) Neuron , vol.13 , pp. 1225-1233
    • Meffert, M.K.1    Haley, J.E.2    Schuman, E.M.3    Schulman, H.4    Madison, D.V.5
  • 42
    • 0015502066 scopus 로고
    • The generation of superoxide radical during the autoxidation of hemoglobin
    • Misra HP, Fridovich I. 1972. The generation of superoxide radical during the autoxidation of hemoglobin. J Biol Chem 247:6960-6962.
    • (1972) J Biol Chem , vol.247 , pp. 6960-6962
    • Misra, H.P.1    Fridovich, I.2
  • 43
    • 0014511563 scopus 로고
    • Intracellular mechanisms for the decomposition of a lipid peroxide. 1. Decomposition of a lipid peroxide by metal ions, heme compounds, and nucleophiles
    • O'Brien PJ. 1969. Intracellular mechanisms for the decomposition of a lipid peroxide. 1. Decomposition of a lipid peroxide by metal ions, heme compounds, and nucleophiles. Can J Biochem 47:485-492.
    • (1969) Can J Biochem , vol.47 , pp. 485-492
    • O'Brien, P.J.1
  • 44
    • 0030886054 scopus 로고    scopus 로고
    • Reduced stress defense in heme oxygenase 1-deficient cells
    • Poss KD, Tonegawa S. 1997. Reduced stress defense in heme oxygenase 1-deficient cells. Proc Natl Acad Sci USA 94:10925-10930.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 10925-10930
    • Poss, K.D.1    Tonegawa, S.2
  • 45
    • 0034677855 scopus 로고    scopus 로고
    • Heme oxygenase-1 induction protects murine cortical astrocytes from hemoglobin toxicity
    • Regan RF, Guo YP, Kumar N. 2000. Heme oxygenase-1 induction protects murine cortical astrocytes from hemoglobin toxicity. Neurosci Lett 282:1-4.
    • (2000) Neurosci Lett , vol.282 , pp. 1-4
    • Regan, R.F.1    Guo, Y.P.2    Kumar, N.3
  • 46
    • 0034765001 scopus 로고    scopus 로고
    • Activation of extracellular signal-regulated kinases potentiates hemin toxicity in astrocyte cultures
    • Regan RF, Wang Y, Ma X, Chong A, Guo Y. 2001. Activation of extracellular signal-regulated kinases potentiates hemin toxicity in astrocyte cultures. J Neurochem 79:545-555.
    • (2001) J Neurochem , vol.79 , pp. 545-555
    • Regan, R.F.1    Wang, Y.2    Ma, X.3    Chong, A.4    Guo, Y.5
  • 47
    • 0029064518 scopus 로고
    • Glutamate induces the production of reactive oxygen species in cultured forebrain neurons following NMDA receptor activation
    • Reynolds IJ, Hastings T. 1995. Glutamate induces the production of reactive oxygen species in cultured forebrain neurons following NMDA receptor activation. J Neurosci 15:3318-3327.
    • (1995) J Neurosci , vol.15 , pp. 3318-3327
    • Reynolds, I.J.1    Hastings, T.2
  • 48
    • 0021045327 scopus 로고
    • On the cytotoxicity of vitamin C and metal ions. A site-specific Fenton mechanism
    • Samuni A, Aronivitch J, Godinger G, Chevion M, Czapski G. 1983. On the cytotoxicity of vitamin C and metal ions. A site-specific Fenton mechanism. Eur J Biochem 137:119-124.
    • (1983) Eur J Biochem , vol.137 , pp. 119-124
    • Samuni, A.1    Aronivitch, J.2    Godinger, G.3    Chevion, M.4    Czapski, G.5
  • 49
    • 0030994406 scopus 로고    scopus 로고
    • Effects of pyrroloquinoline quinone on glutamate-induced production of reactive oxygen species in neurons
    • Scanlon JM, Aizenman E, Reynolds IJ. 1997. Effects of pyrroloquinoline quinone on glutamate-induced production of reactive oxygen species in neurons. Eur J Pharmacol 326:67-74.
    • (1997) Eur J Pharmacol , vol.326 , pp. 67-74
    • Scanlon, J.M.1    Aizenman, E.2    Reynolds, I.J.3
  • 50
    • 0026499957 scopus 로고
    • Retinal cell and photoreceptor transplantation between adult New Zealand red rabbit retinas
    • Schuschereba ST, Silverman MS. 1992. Retinal cell and photoreceptor transplantation between adult New Zealand red rabbit retinas. Exp Neurol 115:95-99.
    • (1992) Exp Neurol , vol.115 , pp. 95-99
    • Schuschereba, S.T.1    Silverman, M.S.2
  • 52
    • 0023472083 scopus 로고
    • Glutathione as a scavenger of free hemin. A mechanism of preventing red cell membrane damage
    • Shviro Y, Shaklai N. 1987. Glutathione as a scavenger of free hemin. A mechanism of preventing red cell membrane damage. Biochem Pharmacol 36:3801-3807.
    • (1987) Biochem Pharmacol , vol.36 , pp. 3801-3807
    • Shviro, Y.1    Shaklai, N.2
  • 54
    • 0033582784 scopus 로고    scopus 로고
    • Anti-oxidants prevent focal rat brain injury as assessed by induction of heat shock proteins (HSP70, HO-1/HSP32, HSP47) following subarachnoid injection of lysed blood
    • Turner CP, Panter SS, Sharp FR. 1999. Anti-oxidants prevent focal rat brain injury as assessed by induction of heat shock proteins (HSP70, HO-1/HSP32, HSP47) following subarachnoid injection of lysed blood. Brain Res Mol Brain Res 65:87-102.
    • (1999) Brain Res Mol Brain Res , vol.65 , pp. 87-102
    • Turner, C.P.1    Panter, S.S.2    Sharp, F.R.3
  • 55
    • 0023789109 scopus 로고
    • The use of cis-parinaric acid to determine lipid peroxidation in human erythrocyte membranes: Comparison of normal and sickle erythrocyte membranes
    • Van den Berg JJ, Kuypers FA, Qju JH, Chiu D, Lubin B, Roelofsen B, Op den Kamp JA. 1988. The use of cis-parinaric acid to determine lipid peroxidation in human erythrocyte membranes: comparison of normal and sickle erythrocyte membranes. Biochim Biophys Acta 944:29-39.
    • (1988) Biochim Biophys Acta , vol.944 , pp. 29-39
    • Van den Berg, J.J.1    Kuypers, F.A.2    Qju, J.H.3    Chiu, D.4    Lubin, B.5    Roelofsen, B.6    Op den Kamp, J.A.7
  • 56
    • 0028300334 scopus 로고
    • Heme oxygenase 1 mediates an adaptive response to oxidative stress in human skin fibroblasts
    • Vile GF, Basu-Modak S, Waltner C, Tyrrell RM. 1994. Heme oxygenase 1 mediates an adaptive response to oxidative stress in human skin fibroblasts. Proc Natl Acad Sci USA 91:2607-2610.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 2607-2610
    • Vile, G.F.1    Basu-Modak, S.2    Waltner, C.3    Tyrrell, R.M.4
  • 58
    • 0036318246 scopus 로고    scopus 로고
    • Hemoglobin-induced cytotoxicity in rat cerebral cortical neurons: Caspase activation and oxidative stress
    • Wang X, Mori T, Sumii T, Lo EH. 2002. Hemoglobin-induced cytotoxicity in rat cerebral cortical neurons: caspase activation and oxidative stress. Stroke 33:1882-1888.
    • (2002) Stroke , vol.33 , pp. 1882-1888
    • Wang, X.1    Mori, T.2    Sumii, T.3    Lo, E.H.4
  • 59
    • 0031756092 scopus 로고    scopus 로고
    • Erythrocytes and delayed brain edema formation following intracerebral hemorrhage in rats
    • Xi GH, Keep RF, Hoff JT. 1998. Erythrocytes and delayed brain edema formation following intracerebral hemorrhage in rats. J Neurosurg 89:991-996.
    • (1998) J Neurosurg , vol.89 , pp. 991-996
    • Xi, G.H.1    Keep, R.F.2    Hoff, J.T.3
  • 60
    • 0026682896 scopus 로고
    • Screening of thiol compounds: Depolarization-induced release of glutathione and cysteine from rat brain slices
    • Zängerle L, Cuénod M, Winterhalter KH, Do KQ. 1992. Screening of thiol compounds: depolarization-induced release of glutathione and cysteine from rat brain slices. J Neurochem 59:181-189.
    • (1992) J Neurochem , vol.59 , pp. 181-189
    • Zängerle, L.1    Cuénod, M.2    Winterhalter, K.H.3    Do, K.Q.4
  • 61
    • 0029781732 scopus 로고    scopus 로고
    • Effects of glutathione and pH on the oxidation of biomarkers of cellular oxidative stress
    • Zhu H, He M, Bannenberg GL, Moldeus P, Shertzer HG. 1996. Effects of glutathione and pH on the oxidation of biomarkers of cellular oxidative stress. Arch Toxicol 70:628-634.
    • (1996) Arch Toxicol , vol.70 , pp. 628-634
    • Zhu, H.1    He, M.2    Bannenberg, G.L.3    Moldeus, P.4    Shertzer, H.G.5
  • 62
    • 0037103555 scopus 로고    scopus 로고
    • Enhancement of glutathione-dependent haemin degradation by ascorbic acid
    • Zou CG, Agar NS, Jones GL. 2002. Enhancement of glutathione-dependent haemin degradation by ascorbic acid. Biochem Pharmacol 64:565-572.
    • (2002) Biochem Pharmacol , vol.64 , pp. 565-572
    • Zou, C.G.1    Agar, N.S.2    Jones, G.L.3


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