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Volumn 139, Issue 4, 2016, Pages 586-595

Haptoglobin increases the vulnerability of CD163-expressing neurons to hemoglobin

Author keywords

intracerebral hemorrhage; iron; neurotoxicity; stroke; subarachnoid hemorrhage

Indexed keywords

CD163 ANTIGEN; FERRITIN; HAPTOGLOBIN; HEMOGLOBIN; CELL SURFACE RECEPTOR; DIFFERENTIATION ANTIGEN; LEUKOCYTE ANTIGEN;

EID: 84979080282     PISSN: 00223042     EISSN: 14714159     Source Type: Journal    
DOI: 10.1111/jnc.13720     Document Type: Article
Times cited : (44)

References (47)
  • 1
    • 0037101879 scopus 로고    scopus 로고
    • Ferritin, iron homeostasis, and oxidative damage
    • Arosio P. and Levi S. (2002) Ferritin, iron homeostasis, and oxidative damage. Free Radic. Biol. Med. 33, 457–463.
    • (2002) Free Radic. Biol. Med. , vol.33 , pp. 457-463
    • Arosio, P.1    Levi, S.2
  • 2
    • 84995342830 scopus 로고    scopus 로고
    • ARUP Lab Tests
    • ARUP (2016) Haptoglobin: ARUP Lab Tests.
    • (2016) Haptoglobin
  • 3
    • 33645862596 scopus 로고    scopus 로고
    • Haptoglobin and the development of cerebral artery vasospasm after subarachnoid hemorrhage
    • Borsody M., Burke A., Coplin W., Miller-Lotan R. and Levy A. (2006) Haptoglobin and the development of cerebral artery vasospasm after subarachnoid hemorrhage. Neurology 66, 634–640.
    • (2006) Neurology , vol.66 , pp. 634-640
    • Borsody, M.1    Burke, A.2    Coplin, W.3    Miller-Lotan, R.4    Levy, A.5
  • 4
    • 0028868824 scopus 로고
    • Serum-free B27/neurobasal medium supports differentiated growth of neurons from the striatum, substantia nigra, septum, cerebral cortex, cerebellum, and dentate gyrus
    • Brewer G. J. (1995) Serum-free B27/neurobasal medium supports differentiated growth of neurons from the striatum, substantia nigra, septum, cerebral cortex, cerebellum, and dentate gyrus. J. Neurosci. Res. 42, 674–683.
    • (1995) J. Neurosci. Res. , vol.42 , pp. 674-683
    • Brewer, G.J.1
  • 5
    • 33749080071 scopus 로고    scopus 로고
    • Effect of heme oxygenase-1 on the vulnerability of astrocytes and neurons to hemoglobin
    • Chen-Roetling J. and Regan R. F. (2006) Effect of heme oxygenase-1 on the vulnerability of astrocytes and neurons to hemoglobin. Biochem. Biophys. Res. Commun. 350, 233–237.
    • (2006) Biochem. Biophys. Res. Commun. , vol.350 , pp. 233-237
    • Chen-Roetling, J.1    Regan, R.F.2
  • 6
    • 63049135004 scopus 로고    scopus 로고
    • Heme oxygenase activity and hemoglobin neurotoxicity are attenuated by inhibitors of the MEK/ERK pathway
    • Chen-Roetling J., Li Z., Chen M., Awe O. O. and Regan R. F. (2009) Heme oxygenase activity and hemoglobin neurotoxicity are attenuated by inhibitors of the MEK/ERK pathway. Neuropharmacology 56, 922–928.
    • (2009) Neuropharmacology , vol.56 , pp. 922-928
    • Chen-Roetling, J.1    Li, Z.2    Chen, M.3    Awe, O.O.4    Regan, R.F.5
  • 7
    • 78650839740 scopus 로고    scopus 로고
    • Apotransferrin protects cortical neurons from hemoglobin toxicity
    • Chen-Roetling J., Chen L. and Regan R. F. (2011) Apotransferrin protects cortical neurons from hemoglobin toxicity. Neuropharmacology 60, 423–431.
    • (2011) Neuropharmacology , vol.60 , pp. 423-431
    • Chen-Roetling, J.1    Chen, L.2    Regan, R.F.3
  • 8
    • 84946195292 scopus 로고    scopus 로고
    • Different target specificities of haptoglobin and hemopexin define a sequential protection system against vascular hemoglobin toxicity
    • Deuel J. W., Vallelian F., Schaer C. A., Puglia M., Buehler P. W. and Schaer D. J. (2015) Different target specificities of haptoglobin and hemopexin define a sequential protection system against vascular hemoglobin toxicity. Free Radic. Biol. Med. 89, 931–943.
    • (2015) Free Radic. Biol. Med. , vol.89 , pp. 931-943
    • Deuel, J.W.1    Vallelian, F.2    Schaer, C.A.3    Puglia, M.4    Buehler, P.W.5    Schaer, D.J.6
  • 9
  • 10
    • 0027054312 scopus 로고
    • In situ hybridization and immunohistochemical localization of heme oxygenase-2 mRNA and protein in normal rat brain: differential distribution of isozyme 1 and 2
    • Ewing J. F. and Maines M. D. (1992) In situ hybridization and immunohistochemical localization of heme oxygenase-2 mRNA and protein in normal rat brain: differential distribution of isozyme 1 and 2. Mol. Cell Neurosci. 3, 559–570.
    • (1992) Mol. Cell Neurosci. , vol.3 , pp. 559-570
    • Ewing, J.F.1    Maines, M.D.2
  • 12
    • 84866007988 scopus 로고    scopus 로고
    • Macrophages and systemic iron homeostasis
    • Ganz T. (2012) Macrophages and systemic iron homeostasis. J. Innate. Immun. 4, 446–453.
    • (2012) J. Innate. Immun. , vol.4 , pp. 446-453
    • Ganz, T.1
  • 13
    • 84959530084 scopus 로고    scopus 로고
    • Hemoglobin-induced neuronal degeneration in the neonatal hippocampus after intraventricular hemorrhage
    • Garton T., He Y., Garton H. J., Keep R. F., Xi G. and Strahle J. M. (2016) Hemoglobin-induced neuronal degeneration in the neonatal hippocampus after intraventricular hemorrhage. Brain Res. 1635, 86–94.
    • (2016) Brain Res. , vol.1635 , pp. 86-94
    • Garton, T.1    He, Y.2    Garton, H.J.3    Keep, R.F.4    Xi, G.5    Strahle, J.M.6
  • 14
    • 77952083750 scopus 로고    scopus 로고
    • Quantitative mass spectrometry-based proteomics reveals the dynamic range of primary mouse astrocyte protein secretion
    • Greco T. M., Seeholzer S. H., Mak A., Spruce L. and Ischiropoulos H. (2010) Quantitative mass spectrometry-based proteomics reveals the dynamic range of primary mouse astrocyte protein secretion. J. Proteome Res. 9, 2764–2774.
    • (2010) J. Proteome Res. , vol.9 , pp. 2764-2774
    • Greco, T.M.1    Seeholzer, S.H.2    Mak, A.3    Spruce, L.4    Ischiropoulos, H.5
  • 15
    • 84887959333 scopus 로고    scopus 로고
    • Uptake and metabolism of iron and iron oxide nanoparticles in brain astrocytes
    • Hohnholt M. C. and Dringen R. (2013) Uptake and metabolism of iron and iron oxide nanoparticles in brain astrocytes. Biochem. Soc. Trans. 41, 1588–1592.
    • (2013) Biochem. Soc. Trans. , vol.41 , pp. 1588-1592
    • Hohnholt, M.C.1    Dringen, R.2
  • 16
    • 0036120064 scopus 로고    scopus 로고
    • Brain edema after experimental intracerebral hemorrhage: role of hemoglobin degradation products
    • Huang F. P., Xi G., Keep R. F., Hua Y., Nemoianu A. and Hoff J. T. (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
  • 17
    • 77954704729 scopus 로고    scopus 로고
    • Accelerated hemolysis and neurotoxicity in neuron-glia-blood clot Co-cultures
    • Jaremko K. M., Chen-Roetling J., Chen L. and Regan R. F. (2010) Accelerated hemolysis and neurotoxicity in neuron-glia-blood clot Co-cultures. J. Neurochem. 114, 1063–1073.
    • (2010) J. Neurochem. , vol.114 , pp. 1063-1073
    • Jaremko, K.M.1    Chen-Roetling, J.2    Chen, L.3    Regan, R.F.4
  • 18
    • 0001699857 scopus 로고
    • The effect of haptoglobin polymer size on hemoglobin binding capacity
    • Javid J. (1965) The effect of haptoglobin polymer size on hemoglobin binding capacity. Vox Sang. 10, 320–325.
    • (1965) Vox Sang. , vol.10 , pp. 320-325
    • Javid, J.1
  • 19
    • 79955809197 scopus 로고    scopus 로고
    • Extracellular hemoglobin polarizes the macrophage proteome toward Hb-clearance, enhanced antioxidant capacity and suppressed HLA class 2 expression
    • Kaempfer T., Duerst E., Gehrig P., Roschitzki B., Rutishauser D., Grossmann J., Schoedon G., Vallelian F. and Schaer D. J. (2011) Extracellular hemoglobin polarizes the macrophage proteome toward Hb-clearance, enhanced antioxidant capacity and suppressed HLA class 2 expression. J. Proteome Res. 10, 2397–2408.
    • (2011) J. Proteome Res. , vol.10 , pp. 2397-2408
    • Kaempfer, T.1    Duerst, E.2    Gehrig, P.3    Roschitzki, B.4    Rutishauser, D.5    Grossmann, J.6    Schoedon, G.7    Vallelian, F.8    Schaer, D.J.9
  • 20
    • 84893307785 scopus 로고    scopus 로고
    • Haptoglobin genotype and functional outcome after aneurysmal subarachnoid hemorrhage
    • Kantor E., Bayir H., Ren D., et al. (2014) Haptoglobin genotype and functional outcome after aneurysmal subarachnoid hemorrhage. J. Neurosurg. 120, 386–390.
    • (2014) J. Neurosurg. , vol.120 , pp. 386-390
    • Kantor, E.1    Bayir, H.2    Ren, D.3
  • 21
    • 71049127348 scopus 로고    scopus 로고
    • Peroxidase activity of hemoglobin-haptoglobin complexes: covalent aggregation and oxidative stress in plasma and macrophages
    • Kapralov A., Vlasova I. I., Feng W., et al. (2009) Peroxidase activity of hemoglobin-haptoglobin complexes: covalent aggregation and oxidative stress in plasma and macrophages. J. Biol. Chem. 284, 30395–30407.
    • (2009) J. Biol. Chem. , vol.284 , pp. 30395-30407
    • Kapralov, A.1    Vlasova, I.I.2    Feng, W.3
  • 22
    • 0023877523 scopus 로고
    • Vulnerability of cultured cortical neurons to damage by excitotoxins: differential susceptibility of neurons containing NADPH-diaphorase
    • Koh J. Y. and Choi D. W. (1988) Vulnerability of cultured cortical neurons to damage by excitotoxins: differential susceptibility of neurons containing NADPH-diaphorase. J. Neurosci. 8, 2153–2163.
    • (1988) J. Neurosci. , vol.8 , pp. 2153-2163
    • Koh, J.Y.1    Choi, D.W.2
  • 23
    • 0037101622 scopus 로고    scopus 로고
    • The relationship between intracellular free iron and cell injury in cultured neurons, astrocytes, and oligodendrocytes
    • Kress G. J., Dineley K. E. and Reynolds I. J. (2002) The relationship between intracellular free iron and cell injury in cultured neurons, astrocytes, and oligodendrocytes. J. Neurosci. 22, 5848–5855.
    • (2002) J. Neurosci. , vol.22 , pp. 5848-5855
    • Kress, G.J.1    Dineley, K.E.2    Reynolds, I.J.3
  • 24
    • 67349265621 scopus 로고    scopus 로고
    • On the fate of extracellular hemoglobin and heme in brain
    • Lara F. A., Kahn S. A., da Fonseca A. C., et al. (2009) On the fate of extracellular hemoglobin and heme in brain. J. Cereb. Blood Flow Metab. 29, 1109–1120.
    • (2009) J. Cereb. Blood Flow Metab. , vol.29 , pp. 1109-1120
    • Lara, F.A.1    Kahn, S.A.2    da Fonseca, A.C.3
  • 25
    • 84921770260 scopus 로고    scopus 로고
    • Haptoglobin phenotype predicts the development of focal and global cerebral vasospasm and may influence outcomes after aneurysmal subarachnoid hemorrhage
    • Leclerc J. L., Blackburn S., Neal D., Mendez N. V., Wharton J. A., Waters M. F. and Dore S. (2015) Haptoglobin phenotype predicts the development of focal and global cerebral vasospasm and may influence outcomes after aneurysmal subarachnoid hemorrhage. Proc. Natl Acad. Sci. USA 112, 1155–1160.
    • (2015) Proc. Natl Acad. Sci. USA , vol.112 , pp. 1155-1160
    • Leclerc, J.L.1    Blackburn, S.2    Neal, D.3    Mendez, N.V.4    Wharton, J.A.5    Waters, M.F.6    Dore, S.7
  • 26
    • 0034786775 scopus 로고    scopus 로고
    • Role of haptoglobin in free hemoglobin metabolism
    • Lim S. K., Ferraro B., Moore K. and Halliwell B. (2001) Role of haptoglobin in free hemoglobin metabolism. Redox Rep. 6, 219–227.
    • (2001) Redox Rep. , vol.6 , pp. 219-227
    • Lim, S.K.1    Ferraro, B.2    Moore, K.3    Halliwell, B.4
  • 27
    • 84878741762 scopus 로고    scopus 로고
    • Human Hp1-1 and Hp2-2 phenotype-specific haptoglobin therapeutics are both effective in vitro and in guinea pigs to attenuate hemoglobin toxicity
    • Lipiski M., Deuel J. W., Baek J. H., Engelsberger W. R., Buehler P. W. and Schaer D. J. (2013) Human Hp1-1 and Hp2-2 phenotype-specific haptoglobin therapeutics are both effective in vitro and in guinea pigs to attenuate hemoglobin toxicity. Antioxid. Redox Signal. 19, 1619–1633.
    • (2013) Antioxid. Redox Signal. , vol.19 , pp. 1619-1633
    • Lipiski, M.1    Deuel, J.W.2    Baek, J.H.3    Engelsberger, W.R.4    Buehler, P.W.5    Schaer, D.J.6
  • 28
    • 1842504357 scopus 로고    scopus 로고
    • The metabolism of neuronal iron and its pathogenic role in neurological disease: review
    • Moos T. and Morgan E. H. (2004) The metabolism of neuronal iron and its pathogenic role in neurological disease: review. Ann. N. Y. Acad. Sci. 1012, 14–26.
    • (2004) Ann. N. Y. Acad. Sci. , vol.1012 , pp. 14-26
    • Moos, T.1    Morgan, E.H.2
  • 32
    • 0033033374 scopus 로고    scopus 로고
    • Iron proteins of duodenal enterocytes isolated from mice with genetically and experimentally altered iron metabolism
    • Pountney D. J., Konijn A. M., McKie A. T., Peters T. J., Raja K. B., Salisbury J. R. and Simpson R. J. (1999) Iron proteins of duodenal enterocytes isolated from mice with genetically and experimentally altered iron metabolism. Br. J. Haematol. 105, 1066–1073.
    • (1999) Br. J. Haematol. , vol.105 , pp. 1066-1073
    • Pountney, D.J.1    Konijn, A.M.2    McKie, A.T.3    Peters, T.J.4    Raja, K.B.5    Salisbury, J.R.6    Simpson, R.J.7
  • 33
    • 0027298460 scopus 로고
    • Neurotoxicity of hemoglobin in cortical cell culture
    • Regan R. F. and Panter S. S. (1993) Neurotoxicity of hemoglobin in cortical cell culture. Neurosci. Lett. 153, 219–222.
    • (1993) Neurosci. Lett. , vol.153 , pp. 219-222
    • Regan, R.F.1    Panter, S.S.2
  • 34
    • 0037263625 scopus 로고    scopus 로고
    • Delayed treatment of hemoglobin neurotoxicity
    • Regan R. F. and Rogers B. (2003) Delayed treatment of hemoglobin neurotoxicity. J. Neurotrauma 20, 111–120.
    • (2003) J. Neurotrauma , vol.20 , pp. 111-120
    • Regan, R.F.1    Rogers, B.2
  • 35
    • 0037055997 scopus 로고    scopus 로고
    • Ferritin induction protects cortical astrocytes from heme-mediated oxidative injury
    • Regan R. F., Kumar N., Gao F. and Guo Y. P. (2002) Ferritin induction protects cortical astrocytes from heme-mediated oxidative injury. Neuroscience 113, 985–994.
    • (2002) Neuroscience , vol.113 , pp. 985-994
    • Regan, R.F.1    Kumar, N.2    Gao, F.3    Guo, Y.P.4
  • 36
    • 47149093139 scopus 로고    scopus 로고
    • Neurons lacking iron regulatory protein-2 are highly resistant to the toxicity of hemoglobin
    • Regan R. F., Chen M., Li Z., Zhang X., Benvenisti-Zarom L. and Chen-Roetling J. (2008) Neurons lacking iron regulatory protein-2 are highly resistant to the toxicity of hemoglobin. Neurobiol. Dis. 31, 242–249.
    • (2008) Neurobiol. Dis. , vol.31 , pp. 242-249
    • Regan, R.F.1    Chen, M.2    Li, Z.3    Zhang, X.4    Benvenisti-Zarom, L.5    Chen-Roetling, J.6
  • 37
    • 0141749478 scopus 로고    scopus 로고
    • Heme oxygenase-2 knockout neurons are less vulnerable to hemoglobin toxicity
    • Rogers B., Yakopson V., Teng Z. P., Guo Y. and Regan R. F. (2003) Heme oxygenase-2 knockout neurons are less vulnerable to hemoglobin toxicity. Free Rad. Biol. Med. 35, 872–881.
    • (2003) Free Rad. Biol. Med. , vol.35 , pp. 872-881
    • Rogers, B.1    Yakopson, V.2    Teng, Z.P.3    Guo, Y.4    Regan, R.F.5
  • 39
    • 0035072165 scopus 로고    scopus 로고
    • Molecular cloning and characterization of the mouse CD163 homologue, a highly glucocorticoid-inducible member of the scavenger receptor cysteine-rich family
    • Schaer D. J., Boretti F. S., Hongegger A., Poehler D., Linnscheid P., Staege H., Muller C., Schoedon G. and Schaffner A. (2001) Molecular cloning and characterization of the mouse CD163 homologue, a highly glucocorticoid-inducible member of the scavenger receptor cysteine-rich family. Immunogenetics 53, 170–177.
    • (2001) Immunogenetics , vol.53 , pp. 170-177
    • Schaer, D.J.1    Boretti, F.S.2    Hongegger, A.3    Poehler, D.4    Linnscheid, P.5    Staege, H.6    Muller, C.7    Schoedon, G.8    Schaffner, A.9
  • 40
    • 33750451990 scopus 로고    scopus 로고
    • Constitutive endocytosis of CD163 mediates hemoglobin-heme uptake and determines the noninflammatory and protective transcriptional response of macrophages to hemoglobin
    • Schaer C. A., Schoedon G., Imhof A., Kurrer M. O. and Schaer D. J. (2006a) Constitutive endocytosis of CD163 mediates hemoglobin-heme uptake and determines the noninflammatory and protective transcriptional response of macrophages to hemoglobin. Circ. Res. 99, 943–950.
    • (2006) Circ. Res. , vol.99 , pp. 943-950
    • Schaer, C.A.1    Schoedon, G.2    Imhof, A.3    Kurrer, M.O.4    Schaer, D.J.5
  • 41
    • 30144435054 scopus 로고    scopus 로고
    • CD163 is the macrophage scavenger receptor for native and chemically modified hemoglobins in the absence of haptoglobin
    • Schaer D. J., Schaer C. A., Buehler P. W., Boykins R. A., Schoedon G., Alayash A. I. and Schaffner A. (2006b) CD163 is the macrophage scavenger receptor for native and chemically modified hemoglobins in the absence of haptoglobin. Blood 107, 373–380.
    • (2006) Blood , vol.107 , pp. 373-380
    • Schaer, D.J.1    Schaer, C.A.2    Buehler, P.W.3    Boykins, R.A.4    Schoedon, G.5    Alayash, A.I.6    Schaffner, A.7
  • 42
    • 47049108919 scopus 로고    scopus 로고
    • Breast cancer expression of CD163, a macrophage scavenger receptor, is related to early distant recurrence and reduced patient survival
    • Shabo I., Stal O., Olsson H., Dore S. and Svanvik J. (2008) Breast cancer expression of CD163, a macrophage scavenger receptor, is related to early distant recurrence and reduced patient survival. Int. J. Cancer 123, 780–786.
    • (2008) Int. J. Cancer , vol.123 , pp. 780-786
    • Shabo, I.1    Stal, O.2    Olsson, H.3    Dore, S.4    Svanvik, J.5
  • 43
    • 70349259469 scopus 로고    scopus 로고
    • Expression of the macrophage antigen CD163 in rectal cancer cells is associated with early local recurrence and reduced survival time
    • Shabo I., Olsson H., Sun X. F. and Svanvik J. (2009) Expression of the macrophage antigen CD163 in rectal cancer cells is associated with early local recurrence and reduced survival time. Int. J. Cancer 125, 1826–1831.
    • (2009) Int. J. Cancer , vol.125 , pp. 1826-1831
    • Shabo, I.1    Olsson, H.2    Sun, X.F.3    Svanvik, J.4
  • 44
    • 84891548265 scopus 로고    scopus 로고
    • Phenotypic transition of microglia into astrocyte-like cells associated with disease onset in a model of inherited ALS
    • Trias E., Diaz-Amarilla P., Olivera-Bravo S., et al. (2013) Phenotypic transition of microglia into astrocyte-like cells associated with disease onset in a model of inherited ALS. Front. Cell Neurosci. 7, 274.
    • (2013) Front. Cell Neurosci. , vol.7 , pp. 274
    • Trias, E.1    Diaz-Amarilla, P.2    Olivera-Bravo, S.3
  • 45
    • 0345599222 scopus 로고    scopus 로고
    • Iron and iron-handling proteins in the brain after intracerebral hemorrhage
    • Wu J., Hua Y., Keep R. F., Nakemura T., Hoff J. T. and Xi G. (2003) Iron and iron-handling proteins in the brain after intracerebral hemorrhage. Stroke 34, 2964–2969.
    • (2003) Stroke , vol.34 , pp. 2964-2969
    • Wu, J.1    Hua, Y.2    Keep, R.F.3    Nakemura, T.4    Hoff, J.T.5    Xi, G.6
  • 46
    • 0031756092 scopus 로고    scopus 로고
    • Erythrocytes and delayed brain edema formation following intracerebral hemorrhage in rats
    • Xi G. H., Keep R. F. and Hoff J. T. (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


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