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Volumn 125, Issue 1, 2013, Pages 89-101

Mechanisms of neuroprotection by hemopexin: Modeling the control of heme and iron homeostasis in brain neurons in inflammatory states

Author keywords

APP; heme; hemopexin; iron; neuroprotection; stroke

Indexed keywords

ALBUMIN; AMYLOID PRECURSOR PROTEIN; HEME; HEME OXYGENASE 1; HEMOPEXIN; HYDROGEN PEROXIDE; HYPOCHLOROUS ACID; IRON; MESSENGER RNA; REACTIVE OXYGEN METABOLITE; TERT BUTYL HYDROPEROXIDE;

EID: 84875258941     PISSN: 00223042     EISSN: 14714159     Source Type: Journal    
DOI: 10.1111/jnc.12165     Document Type: Article
Times cited : (58)

References (73)
  • 1
    • 0024427488 scopus 로고
    • Receptor-mediated transport of heme by hemopexin regulates gene expression in mammalian cells
    • Alam J., and, Smith A., (1989) Receptor-mediated transport of heme by hemopexin regulates gene expression in mammalian cells. J. Biol. Chem. 264, 17637-17640.
    • (1989) J. Biol. Chem. , vol.264 , pp. 17637-17640
    • Alam, J.1    Smith, A.2
  • 2
    • 0033543566 scopus 로고    scopus 로고
    • Nrf2, a Cap'n'Collar transcription factor, regulates induction of the heme oxygenase-1 gene
    • Alam J., Stewart D., Touchard C., Boinapally S., Choi A. M., and, Cook J. L., (1999) Nrf2, a Cap'n'Collar transcription factor, regulates induction of the heme oxygenase-1 gene. J. Biol. Chem. 274, 26071-26078.
    • (1999) J. Biol. Chem. , vol.274 , pp. 26071-26078
    • Alam, J.1    Stewart, D.2    Touchard, C.3    Boinapally, S.4    Choi, A.M.5    Cook, J.L.6
  • 5
    • 0015993964 scopus 로고
    • A spectroscopic study of the haemin-human-serum-albumin system
    • Beaven G. H., Chen S.-H., D'Albis A., and, Gratzer W. B., (1974) A spectroscopic study of the haemin-human-serum-albumin system. Eur. J. Biochem. 41, 539-546.
    • (1974) Eur. J. Biochem. , vol.41 , pp. 539-546
    • Beaven, G.H.1    Chen, S.-H.2    D'Albis, A.3    Gratzer, W.B.4
  • 6
    • 38149013161 scopus 로고    scopus 로고
    • Neurovascular unit dysfunction: A vascular component of Alzheimer disease?
    • Brenner S. R., (2008) Neurovascular unit dysfunction: a vascular component of Alzheimer disease? Neurology 70, 243-244.
    • (2008) Neurology , vol.70 , pp. 243-244
    • Brenner, S.R.1
  • 7
    • 63849094585 scopus 로고    scopus 로고
    • Haptoglobin preserves the CD163 hemoglobin scavenger pathway by shielding hemoglobin from peroxidative modification
    • Buehler P. W., Abraham B., Vallelian F., et al,. (2009) Haptoglobin preserves the CD163 hemoglobin scavenger pathway by shielding hemoglobin from peroxidative modification. Blood 113, 2578-2586.
    • (2009) Blood , vol.113 , pp. 2578-2586
    • Buehler, P.W.1    Abraham, B.2    Vallelian, F.3
  • 8
    • 1942471844 scopus 로고    scopus 로고
    • Heme oxygenase-2 gene deletion increases astrocyte vulnerability to hemin
    • Chen J., and, Regan R. F., (2004) Heme oxygenase-2 gene deletion increases astrocyte vulnerability to hemin. Biochem. Biophys. Res. Commun. 318, 88-94.
    • (2004) Biochem. Biophys. Res. Commun. , vol.318 , pp. 88-94
    • Chen, J.1    Regan, R.F.2
  • 9
    • 79953726765 scopus 로고    scopus 로고
    • Increased striatal injury and behavioral deficits after intracerebral hemorrhage in hemopexin knockout mice
    • Chen L., Zhang X., Chen-Roetling J., and, Regan R. F., (2010) Increased striatal injury and behavioral deficits after intracerebral hemorrhage in hemopexin knockout mice. J. Neurosurg. 114, 1159-1167.
    • (2010) J. Neurosurg. , vol.114 , pp. 1159-1167
    • Chen, L.1    Zhang, X.2    Chen-Roetling, J.3    Regan, R.F.4
  • 10
    • 77957771842 scopus 로고    scopus 로고
    • Selective translational control of the Alzheimer amyloid precursor protein transcript by iron regulatory protein-1
    • Cho H. H., Cahill C. M., Vanderburg C. R., Scherzer C. R., Wang B., Huang X., and, Rogers J. T., (2010) Selective translational control of the Alzheimer amyloid precursor protein transcript by iron regulatory protein-1. J. Biol. Chem. 285, 31217-31232.
    • (2010) J. Biol. Chem. , vol.285 , pp. 31217-31232
    • Cho, H.H.1    Cahill, C.M.2    Vanderburg, C.R.3    Scherzer, C.R.4    Wang, B.5    Huang, X.6    Rogers, J.T.7
  • 11
    • 79551713201 scopus 로고    scopus 로고
    • Brain microbleeds and Alzheimer's disease: Innocent observation or key player?
    • Cordonnier C., and, van der Flier W. M., (2011) Brain microbleeds and Alzheimer's disease: innocent observation or key player? Brain 134, 335-344.
    • (2011) Brain , vol.134 , pp. 335-344
    • Cordonnier, C.1    Van Der Flier, W.M.2
  • 13
    • 0018582274 scopus 로고
    • Hepatic subcellular metabolism of heme from heme-hemopexin: Incorporation of iron into ferritin
    • Davies D. M., Smith A., Muller-Eberhard U., and, Morgan W. T., (1979) Hepatic subcellular metabolism of heme from heme-hemopexin: incorporation of iron into ferritin. Biochem. Biophys. Res. Commun. 91, 1504-1511.
    • (1979) Biochem. Biophys. Res. Commun. , vol.91 , pp. 1504-1511
    • Davies, D.M.1    Smith, A.2    Muller-Eberhard, U.3    Morgan, W.T.4
  • 14
    • 77956647381 scopus 로고    scopus 로고
    • Iron-export ferroxidase activity of beta-amyloid precursor protein is inhibited by zinc in Alzheimer's disease
    • Duce J. A., Tsatsanis A., Cater M. A., et al,. (2010) Iron-export ferroxidase activity of beta-amyloid precursor protein is inhibited by zinc in Alzheimer's disease. Cell 142, 857-867.
    • (2010) Cell , vol.142 , pp. 857-867
    • Duce, J.A.1    Tsatsanis, A.2    Cater, M.A.3
  • 15
    • 0033534451 scopus 로고    scopus 로고
    • Cellular protection mechanisms against extracellular heme: Heme- hemopexin, but not free heme, activates the N-terminal c-Jun kinase
    • Eskew J. D., Vanacore R. M., Sung L., Morales P. J., and, Smith A., (1999) Cellular protection mechanisms against extracellular heme: heme- hemopexin, but not free heme, activates the N-terminal c-Jun kinase. J. Biol. Chem. 274, 638-648.
    • (1999) J. Biol. Chem. , vol.274 , pp. 638-648
    • Eskew, J.D.1    Vanacore, R.M.2    Sung, L.3    Morales, P.J.4    Smith, A.5
  • 17
    • 42549165093 scopus 로고    scopus 로고
    • An investigation of hemopexin redox properties by spectroelectrochemistry: Biological relevance for heme uptake
    • Flaherty M. M., Rish K. R., Smith A., and, Crumbliss A. L., (2008) An investigation of hemopexin redox properties by spectroelectrochemistry: biological relevance for heme uptake. Biometals 21, 239-248.
    • (2008) Biometals , vol.21 , pp. 239-248
    • Flaherty, M.M.1    Rish, K.R.2    Smith, A.3    Crumbliss, A.L.4
  • 18
    • 0024232736 scopus 로고
    • Oxidation of proteins in rat heart and lungs by polymorphonuclear leukocyte oxidants
    • Fliss H., (1988) Oxidation of proteins in rat heart and lungs by polymorphonuclear leukocyte oxidants. Mol. Cell. Biochem. 84, 177-188.
    • (1988) Mol. Cell. Biochem. , vol.84 , pp. 177-188
    • Fliss, H.1
  • 19
    • 84863813088 scopus 로고    scopus 로고
    • Hypochlorous acid-induced heme damage of hemoglobin and its inhibition by flavonoids
    • Gebicka L., and, Banasiak E., (2012) Hypochlorous acid-induced heme damage of hemoglobin and its inhibition by flavonoids. Toxicol. In Vitro 26, 924-929.
    • (2012) Toxicol. in Vitro , vol.26 , pp. 924-929
    • Gebicka, L.1    Banasiak, E.2
  • 21
    • 0032800507 scopus 로고    scopus 로고
    • The effects of heme-binding proteins on the peroxidative and catalatic activities of hemin
    • Grinberg L. N., O'Brien P. J., and, Hrkal Z., (1999) The effects of heme-binding proteins on the peroxidative and catalatic activities of hemin. Free Radic. Biol. Med. 27, 214-219.
    • (1999) Free Radic. Biol. Med. , vol.27 , pp. 214-219
    • Grinberg, L.N.1    O'Brien, P.J.2    Hrkal, Z.3
  • 22
    • 0028949268 scopus 로고
    • HOCl effects on tracheal epithelium: Conductance and permeability measurements
    • Guo Y., Schneider L. A., and, Wangensteen O. D., (1995) HOCl effects on tracheal epithelium: conductance and permeability measurements. J. Appl. Physiol. 78, 1330-1338.
    • (1995) J. Appl. Physiol. , vol.78 , pp. 1330-1338
    • Guo, Y.1    Schneider, L.A.2    Wangensteen, O.D.3
  • 23
    • 80052698422 scopus 로고    scopus 로고
    • Clinical usefulness of haptoglobin levels to evaluate hemolysis in recently transfused patients
    • Gupta S., Ahern K., Nakhl F., and, Forte F., (2011) Clinical usefulness of haptoglobin levels to evaluate hemolysis in recently transfused patients. Adv. Hematol. 2011, 389854.
    • (2011) Adv. Hematol. , vol.2011 , pp. 389854
    • Gupta, S.1    Ahern, K.2    Nakhl, F.3    Forte, F.4
  • 24
    • 0024241523 scopus 로고
    • Antioxidant protection by haemopexin of haem-stimulated lipid peroxidation
    • Gutteridge J. M., and, 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.1    Smith, A.2
  • 25
    • 38549164231 scopus 로고    scopus 로고
    • Mechanism of iron toxicity
    • Hershko C., (2007) Mechanism of iron toxicity. Food Nutr. Bull. 28, S500-S509.
    • (2007) Food Nutr. Bull. , vol.28
    • Hershko, C.1
  • 26
    • 0015980699 scopus 로고
    • Transfer of heme from ferrihemoglobin and ferrihemoglobin isolated chains to hemopexin
    • Hrkal Z., Vodrazka Z., and, Kalousek I., (1974) Transfer of heme from ferrihemoglobin and ferrihemoglobin isolated chains to hemopexin. Eur. J. Biochem. 43, 73-78.
    • (1974) Eur. J. Biochem. , vol.43 , pp. 73-78
    • Hrkal, Z.1    Vodrazka, Z.2    Kalousek, I.3
  • 27
    • 0030017012 scopus 로고    scopus 로고
    • Haem exacerbates reactive oxygen species toxicity to human retinal pigment epithelial cells while the haem-binding protein, haemopexin, is protective
    • Hunt R. C., Handy I., and, Smith A., (1996a) Haem exacerbates reactive oxygen species toxicity to human retinal pigment epithelial cells while the haem-binding protein, haemopexin, is protective. J. Cell. Physiol. 168, 81-86.
    • (1996) J. Cell. Physiol. , vol.168 , pp. 81-86
    • Hunt, R.C.1    Handy, I.2    Smith, A.3
  • 28
    • 0030017273 scopus 로고    scopus 로고
    • Hemopexin in the human retina: Protection of the retina against heme- mediated toxicity
    • Hunt R. C., Hunt D. M., Gaur N., and, Smith A., (1996b) Hemopexin in the human retina: protection of the retina against heme- mediated toxicity. J. Cell. Physiol. 168, 71-80.
    • (1996) J. Cell. Physiol. , vol.168 , pp. 71-80
    • Hunt, R.C.1    Hunt, D.M.2    Gaur, N.3    Smith, A.4
  • 29
    • 0001094560 scopus 로고
    • Molecular weight studies on human serum albumin after reduction and alkylation of disulfide bonds
    • Hunter M. J., and, McDuffie F. C., (1959) Molecular weight studies on human serum albumin after reduction and alkylation of disulfide bonds. J. Am. Chem. Soc. 81, 1400-1406.
    • (1959) J. Am. Chem. Soc. , vol.81 , pp. 1400-1406
    • Hunter, M.J.1    McDuffie, F.C.2
  • 30
    • 0025293777 scopus 로고
    • Hydrogen peroxide production during experimental protein glycation
    • Jiang Z.-Y., Woollard A. C. S., and, Wolff S. P., (1990) Hydrogen peroxide production during experimental protein glycation. FEBS Lett. 268, 69-71.
    • (1990) FEBS Lett. , vol.268 , pp. 69-71
    • Jiang, Z.-Y.1    Woollard, A.C.S.2    Wolff, S.P.3
  • 31
    • 0028233559 scopus 로고
    • Assays for the chlorination activity of myeloperoxidase
    • Kettle A. J., and, Winterbourn C. C., (1994) Assays for the chlorination activity of myeloperoxidase. Methods Enzymol. 233, 502-512.
    • (1994) Methods Enzymol. , vol.233 , pp. 502-512
    • Kettle, A.J.1    Winterbourn, C.C.2
  • 32
    • 77958023093 scopus 로고    scopus 로고
    • A central role for free heme in the pathogenesis of severe sepsis
    • Larsen R., Gozzelino R., Jeney V., et al,. (2010) A central role for free heme in the pathogenesis of severe sepsis. Sci. Transl. Med. 2, 51ra71.
    • (2010) Sci. Transl. Med. , vol.2
    • Larsen, R.1    Gozzelino, R.2    Jeney, V.3
  • 34
    • 84867854041 scopus 로고    scopus 로고
    • Coordinated expression of 6-phosphofructo-2-kinase/fructose-2,6- bisphosphatase 4 and heme oxygenase 2: Evidence for a regulatory link between glycolysis and heme catabolism
    • Li B., Takeda K., Ishikawa K., Yoshizawa M., Sato M., Shibahara S., and, Furuyama K., (2012) Coordinated expression of 6-phosphofructo-2-kinase/fructose- 2,6-bisphosphatase 4 and heme oxygenase 2: evidence for a regulatory link between glycolysis and heme catabolism. Tohoku J. Exp. Med. 228, 27-41.
    • (2012) Tohoku J. Exp. Med. , vol.228 , pp. 27-41
    • Li, B.1    Takeda, K.2    Ishikawa, K.3    Yoshizawa, M.4    Sato, M.5    Shibahara, S.6    Furuyama, K.7
  • 36
    • 34547135735 scopus 로고    scopus 로고
    • Heme oxygenase-1 protein localizes to the nucleus and activates transcription factors important in oxidative stress
    • Lin Q., Weis S., Yang G., et al,. (2007) Heme oxygenase-1 protein localizes to the nucleus and activates transcription factors important in oxidative stress. J. Biol. Chem. 282, 20621-20633.
    • (2007) J. Biol. Chem. , vol.282 , pp. 20621-20633
    • Lin, Q.1    Weis, S.2    Yang, G.3
  • 37
    • 84864809340 scopus 로고    scopus 로고
    • Identification of hemopexin as an anti-inflammatory factor that inhibits synergy of hemoglobin with HMGB1 in sterile and infectious inflammation
    • Lin T., Sammy F., Yang H., Thundivalappil S., Hellman J., Tracey K. J., and, Warren H. S., (2012) Identification of hemopexin as an anti-inflammatory factor that inhibits synergy of hemoglobin with HMGB1 in sterile and infectious inflammation. J. Immunol. 189, 2017-2022.
    • (2012) J. Immunol. , vol.189 , pp. 2017-2022
    • Lin, T.1    Sammy, F.2    Yang, H.3    Thundivalappil, S.4    Hellman, J.5    Tracey, K.J.6    Warren, H.S.7
  • 38
    • 0035478537 scopus 로고    scopus 로고
    • A real-time electrochemical technique for measurement of cellular hydrogen peroxide generation and consumption: Evaluation in human polymorphonuclear leukocytes
    • Liu X., and, Zweier J. L., (2001) A real-time electrochemical technique for measurement of cellular hydrogen peroxide generation and consumption: evaluation in human polymorphonuclear leukocytes. Free Radic. Biol. Med. 31, 894-901.
    • (2001) Free Radic. Biol. Med. , vol.31 , pp. 894-901
    • Liu, X.1    Zweier, J.L.2
  • 39
    • 0035715444 scopus 로고    scopus 로고
    • Ldl modified by hypochlorous acid is a potent inhibitor of lecithin-cholesterol acyltransferase activity
    • McCall M. R., Carr A. C., Forte T. M., and, Frei B., (2001) Ldl modified by hypochlorous acid is a potent inhibitor of lecithin-cholesterol acyltransferase activity. Arterioscler. Thromb. Vasc. Biol. 21, 1040-1045.
    • (2001) Arterioscler. Thromb. Vasc. Biol. , vol.21 , pp. 1040-1045
    • McCall, M.R.1    Carr, A.C.2    Forte, T.M.3    Frei, B.4
  • 40
    • 58149357031 scopus 로고    scopus 로고
    • Systemic inflammation alters the kinetics of cerebrovascular tight junction disruption after experimental stroke in mice
    • McColl B. W., Rothwell N. J., and, Allan S. M., (2008) Systemic inflammation alters the kinetics of cerebrovascular tight junction disruption after experimental stroke in mice. J. Neurosci. 28, 9451-9462.
    • (2008) J. Neurosci. , vol.28 , pp. 9451-9462
    • McColl, B.W.1    Rothwell, N.J.2    Allan, S.M.3
  • 41
    • 0015524032 scopus 로고
    • Interactions of porphyrins with rabbit hemopexin
    • Morgan W. T., and, Muller-Eberhard U., (1972) Interactions of porphyrins with rabbit hemopexin. J. Biol. Chem. 247, 7181-7187.
    • (1972) J. Biol. Chem. , vol.247 , pp. 7181-7187
    • Morgan, W.T.1    Muller-Eberhard, U.2
  • 42
    • 0011045635 scopus 로고    scopus 로고
    • Binding and transport of iron-porphyrins by hemopexin
    • in (Mauk G. and Sykes A. G. eds), Academic Press, London, UK & San Diego, CA, USA.
    • Morgan W., and, Smith A,. (2001). Binding and transport of iron-porphyrins by hemopexin, in Advances in Inorganic Chemistry (, Mauk G., and, Sykes A. G.,eds), pp. 205-241. Academic Press, London, UK & San Diego, CA, USA.
    • (2001) Advances in Inorganic Chemistry , pp. 205-241
    • Morgan, W.1    Smith, A.2
  • 44
    • 8544251150 scopus 로고
    • The Acid Ionization Constant of HOCl from 5 to 35°
    • Morris J. C., (1966). The Acid Ionization Constant of HOCl from 5 to 35°. J. Phys. Chem. 70, 3798-3805.
    • (1966) J. Phys. Chem. , vol.70 , pp. 3798-3805
    • Morris, J.C.1
  • 45
    • 0035983247 scopus 로고    scopus 로고
    • Heme oxygenase-1: The "emerging molecule" has arrived
    • Morse D., and, Choi A. M., (2002) Heme oxygenase-1: the "emerging molecule" has arrived. Am. J. Respir. Cell Mol. Biol. 27, 8-16.
    • (2002) Am. J. Respir. Cell Mol. Biol. , vol.27 , pp. 8-16
    • Morse, D.1    Choi, A.M.2
  • 46
    • 80052300274 scopus 로고    scopus 로고
    • Heme oxygenase-1 and carbon monoxide modulate DNA repair through ataxia-telangiectasia mutated (ATM) protein
    • Otterbein L. E., Hedblom A., Harris C., Csizmadia E., Gallo D., and, Wegiel B., (2011) Heme oxygenase-1 and carbon monoxide modulate DNA repair through ataxia-telangiectasia mutated (ATM) protein. Proc. Natl Acad. Sci. USA 108, 14491-14496.
    • (2011) Proc. Natl Acad. Sci. USA , vol.108 , pp. 14491-14496
    • Otterbein, L.E.1    Hedblom, A.2    Harris, C.3    Csizmadia, E.4    Gallo, D.5    Wegiel, B.6
  • 50
    • 34548159927 scopus 로고    scopus 로고
    • Evidence that heme and heme-hemopexin interact with cell growth-associated plasma membrane electron transport
    • Rish K. R., Swartzlander R., Sadikot T. N., Berridge M. V., and, Smith A., (2007) Evidence that heme and heme-hemopexin interact with cell growth-associated plasma membrane electron transport. Biochem. Biophys. Acta Bioenerg. 1767, 1107-1117.
    • (2007) Biochem. Biophys. Acta Bioenerg. , vol.1767 , pp. 1107-1117
    • Rish, K.R.1    Swartzlander, R.2    Sadikot, T.N.3    Berridge, M.V.4    Smith, A.5
  • 51
    • 0347928847 scopus 로고    scopus 로고
    • An iron-responsive element type II in the 5'-untranslated region of the Alzheimer's amyloid precursor protein transcript
    • Rogers J. T., Randall J. D., Cahill C. M., et al,. (2002) An iron-responsive element type II in the 5'-untranslated region of the Alzheimer's amyloid precursor protein transcript. J. Biol. Chem. 277, 45518-45528.
    • (2002) J. Biol. Chem. , vol.277 , pp. 45518-45528
    • Rogers, J.T.1    Randall, J.D.2    Cahill, C.M.3
  • 52
    • 1842608814 scopus 로고    scopus 로고
    • Heme oxygenase-1: Transducer of pathological brain iron sequestration under oxidative stress
    • Schipper H. M., (2004) Heme oxygenase-1: transducer of pathological brain iron sequestration under oxidative stress. Ann. N. Y. Acad. Sci. 1012, 84-93.
    • (2004) Ann. N. Y. Acad. Sci. , vol.1012 , pp. 84-93
    • Schipper, H.M.1
  • 53
    • 67649617842 scopus 로고    scopus 로고
    • Suppression of glial HO-1 activity as a potential neurotherapeutic intervention in AD
    • Schipper H. M., Gupta A., and, Szarek W. A., (2009a) Suppression of glial HO-1 activity as a potential neurotherapeutic intervention in AD. Curr. Alzheimer Res. 6, 424-430.
    • (2009) Curr. Alzheimer Res. , vol.6 , pp. 424-430
    • Schipper, H.M.1    Gupta, A.2    Szarek, W.A.3
  • 54
    • 67649628772 scopus 로고    scopus 로고
    • Heme oxygenase-1 and neurodegeneration: Expanding frontiers of engagement
    • Schipper H. M., Song W., Zukor H., Hascalovici J. R., and, Zeligman D., (2009b) Heme oxygenase-1 and neurodegeneration: expanding frontiers of engagement. J. Neurochem. 110, 469-485.
    • (2009) J. Neurochem. , vol.110 , pp. 469-485
    • Schipper, H.M.1    Song, W.2    Zukor, H.3    Hascalovici, J.R.4    Zeligman, D.5
  • 55
    • 33644532847 scopus 로고    scopus 로고
    • Expression cloning screen for modifiers of amyloid precursor protein shedding
    • Schobel S., Neumann S., Seed B., and, Lichtenthaler S. F., (2006) Expression cloning screen for modifiers of amyloid precursor protein shedding. Int. J. Dev. Neurosci. 24, 141-148.
    • (2006) Int. J. Dev. Neurosci. , vol.24 , pp. 141-148
    • Schobel, S.1    Neumann, S.2    Seed, B.3    Lichtenthaler, S.F.4
  • 56
    • 40849135997 scopus 로고    scopus 로고
    • Hydrogen peroxide as an endogenous mediator and exogenous tool in cardiovascular research: Issues and considerations
    • Schroder E., and, Eaton P., (2008) Hydrogen peroxide as an endogenous mediator and exogenous tool in cardiovascular research: issues and considerations. Curr. Opin. Pharmacol. 8, 153-159.
    • (2008) Curr. Opin. Pharmacol. , vol.8 , pp. 153-159
    • Schroder, E.1    Eaton, P.2
  • 58
    • 84875250524 scopus 로고    scopus 로고
    • Mechanisms of Cytoprotection by Hemopexin
    • in (Kadish K. M. Smith K. M. and Guilard R. eds), World Scientific Publishing Co. Pte. Ltd., Singapore.
    • Smith A., (2011). Mechanisms of Cytoprotection by Hemopexin, in Handbook of Porphyrin Science. Biochemistry of Tetrapyrroles (, Kadish K. M., Smith K. M., and, Guilard R., eds), pp. 217-356. World Scientific Publishing Co. Pte. Ltd., Singapore.
    • (2011) Handbook of Porphyrin Science. Biochemistry of Tetrapyrroles , pp. 217-356
    • Smith, A.1
  • 59
    • 0018634705 scopus 로고
    • Haem transport to the liver by haemopexin. Receptor-mediated uptake with recycling of the protein
    • Smith A., and, Morgan W. T., (1979) Haem transport to the liver by haemopexin. Receptor-mediated uptake with recycling of the protein. Biochem. J. 182, 47-54.
    • (1979) Biochem. J. , vol.182 , pp. 47-54
    • Smith, A.1    Morgan, W.T.2
  • 60
    • 31944431573 scopus 로고    scopus 로고
    • Over-expression of heme oxygenase-1 promotes oxidative mitochondrial damage in rat astroglia
    • Song W., Su H., Song S., Paudel H. K., and, Schipper H. M., (2006) Over-expression of heme oxygenase-1 promotes oxidative mitochondrial damage in rat astroglia. J. Cell. Physiol. 206, 655-663.
    • (2006) J. Cell. Physiol. , vol.206 , pp. 655-663
    • Song, W.1    Su, H.2    Song, S.3    Paudel, H.K.4    Schipper, H.M.5
  • 61
    • 84864836824 scopus 로고    scopus 로고
    • Schizophrenia-like features in transgenic mice overexpressing human HO-1 in the astrocytic compartment
    • Song W., Zukor H., Lin S. H., et al,. (2012) Schizophrenia-like features in transgenic mice overexpressing human HO-1 in the astrocytic compartment. J. Neurosci. 32, 10841-10853.
    • (2012) J. Neurosci. , vol.32 , pp. 10841-10853
    • Song, W.1    Zukor, H.2    Lin, S.H.3
  • 62
    • 0009296982 scopus 로고    scopus 로고
    • Defenses against extracellular heme-mediated oxidative damage: Use of iron and copper chelators to investigate the role of redox active iron, copper and heme in the hemopexin heme transport system
    • in (Badman D. G. Bergeron R. J. and Brittenham G. M. eds), Saratoga Publishing Group, Sarotoga, FL.
    • Sung L., Morales P., Shibata M., Shipulina N., and, Smith A., (2000). Defenses against extracellular heme-mediated oxidative damage: use of iron and copper chelators to investigate the role of redox active iron, copper and heme in the hemopexin heme transport system, in Iron Chelators: New Development Strategies (, Badman D. G., Bergeron R. J., and, Brittenham G. M., eds), pp. 67-86. Saratoga Publishing Group, Sarotoga, FL.
    • (2000) Iron Chelators: New Development Strategies , pp. 67-86
    • Sung, L.1    Morales, P.2    Shibata, M.3    Shipulina, N.4    Smith, A.5
  • 63
    • 0033638815 scopus 로고    scopus 로고
    • Amyloid precursor proteins inhibit heme oxygenase activity and augment neurotoxicity in Alzheimer's disease
    • Takahashi M., Dore S., Ferris C. D., et al,. (2000) Amyloid precursor proteins inhibit heme oxygenase activity and augment neurotoxicity in Alzheimer's disease. Neuron 28, 461-473.
    • (2000) Neuron , vol.28 , pp. 461-473
    • Takahashi, M.1    Dore, S.2    Ferris, C.D.3
  • 64
    • 0021338944 scopus 로고
    • Quantitative and temporal characterization of the extracellular H2O2 pool generated by human neutrophils
    • Test S. T., and, Weiss S. J., (1984) Quantitative and temporal characterization of the extracellular H2O2 pool generated by human neutrophils. J. Biol. Chem. 259, 399-405.
    • (1984) J. Biol. Chem. , vol.259 , pp. 399-405
    • Test, S.T.1    Weiss, S.J.2
  • 65
    • 0029437791 scopus 로고
    • EPR studies on the effects of complexation of heme by hemopexin upon its reactions with organic peroxides
    • Timmins G. S., Davies M. J., Song D. X., and, Muller-Eberhard U., (1995) EPR studies on the effects of complexation of heme by hemopexin upon its reactions with organic peroxides. Free Radic. Res. 23, 559-569.
    • (1995) Free Radic. Res. , vol.23 , pp. 559-569
    • Timmins, G.S.1    Davies, M.J.2    Song, D.X.3    Muller-Eberhard, U.4
  • 66
    • 30644465969 scopus 로고    scopus 로고
    • Vascular remodeling versus amyloid beta-induced oxidative stress in the cerebrovascular dysfunctions associated with Alzheimer's disease
    • Tong X. K., Nicolakakis N., Kocharyan A., and, Hamel E., (2005) Vascular remodeling versus amyloid beta-induced oxidative stress in the cerebrovascular dysfunctions associated with Alzheimer's disease. J. Neurosci. 25, 11165-11174.
    • (2005) J. Neurosci. , vol.25 , pp. 11165-11174
    • Tong, X.K.1    Nicolakakis, N.2    Kocharyan, A.3    Hamel, E.4
  • 67
    • 0034527607 scopus 로고    scopus 로고
    • Role for copper in transient oxidation and nuclear translocation of MTF-1, but not of NFkB, by the hemopexin heme transport system
    • Vanacore R., Eskew J., Morales P., Sung L., and, Smith A., (2000) Role for copper in transient oxidation and nuclear translocation of MTF-1, but not of NFkB, by the hemopexin heme transport system. Antioxid. Redox Signal. 2, 739-752.
    • (2000) Antioxid. Redox Signal. , vol.2 , pp. 739-752
    • Vanacore, R.1    Eskew, J.2    Morales, P.3    Sung, L.4    Smith, A.5
  • 68
    • 84861414390 scopus 로고    scopus 로고
    • Blood transfusions increase circulating plasma free hemoglobin levels and plasma nitric oxide consumption: A prospective observational pilot study
    • Vermeulen Windsant I. C., de Wit N. C., Sertorio J. T., Beckers E. A., Tanus-Santos J. E., Jacobs M. J., and, Buurman W. A., (2012) Blood transfusions increase circulating plasma free hemoglobin levels and plasma nitric oxide consumption: a prospective observational pilot study. Crit. Care 16, R95.
    • (2012) Crit. Care , vol.16
    • Vermeulen Windsant, I.C.1    De Wit, N.C.2    Sertorio, J.T.3    Beckers, E.A.4    Tanus-Santos, J.E.5    Jacobs, M.J.6    Buurman, W.A.7
  • 70
    • 0015935434 scopus 로고
    • Reversible denaturation of human serum albumin by pH, temperature, and guanidine hydrochloride followed by optical rotation
    • Wallevik K., (1973) Reversible denaturation of human serum albumin by pH, temperature, and guanidine hydrochloride followed by optical rotation. J. Biol. Chem. 248, 2650-2655.
    • (1973) J. Biol. Chem. , vol.248 , pp. 2650-2655
    • Wallevik, K.1
  • 71
    • 0024602827 scopus 로고
    • Tissue destruction by neutrophils
    • Weiss S. J., (1989) Tissue destruction by neutrophils. N. Engl. J. Med. 320, 365-376.
    • (1989) N. Engl. J. Med. , vol.320 , pp. 365-376
    • Weiss, S.J.1
  • 72
    • 0020479233 scopus 로고
    • The occurrence of molecular interactions among NADPH-cytochrome c reductase, heme oxygenase, and biliverdin reductase in heme degradation
    • Yoshinaga T., Sassa S., and, Kappas A., (1982) The occurrence of molecular interactions among NADPH-cytochrome c reductase, heme oxygenase, and biliverdin reductase in heme degradation. J. Biol. Chem. 257, 7786-7793.
    • (1982) J. Biol. Chem. , vol.257 , pp. 7786-7793
    • Yoshinaga, T.1    Sassa, S.2    Kappas, A.3
  • 73
    • 72749101173 scopus 로고    scopus 로고
    • Divalent metal transporter 1 is involved in amyloid precursor protein processing and Abeta generation
    • Zheng W., Xin N., Chi Z. H., Zhao B. L., Zhang J., Li J. Y., and, Wang Z. Y., (2009) Divalent metal transporter 1 is involved in amyloid precursor protein processing and Abeta generation. FASEB J. 23, 4207-4217.
    • (2009) FASEB J. , vol.23 , pp. 4207-4217
    • Zheng, W.1    Xin, N.2    Chi, Z.H.3    Zhao, B.L.4    Zhang, J.5    Li, J.Y.6    Wang, Z.Y.7


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