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Volumn 6, Issue JAN, 2015, Pages

The pathophysiology of extracellular hemoglobin associated with enhanced oxidative reactions

Author keywords

Extracellular hemoglobin; Fe(IV)hemoglobins; Heme; Hemoglobin autoxidation; Hydrogen peroxide; Oxidative reactions; proinflammatory reactions

Indexed keywords

FERRIC ION HEMOGLOBIN; FERRYL HEMOGLOBIN; HEME; HEMOGLOBIN; HYDROGEN PEROXIDE; LIPOPROTEIN; OXYFERRYL HEMOGLOBIN; PORPHYRIN DERIVATIVE; UNCLASSIFIED DRUG;

EID: 84926484061     PISSN: None     EISSN: 1664042X     Source Type: Journal    
DOI: 10.3389/fphys.2014.00500     Document Type: Review
Times cited : (107)

References (52)
  • 1
    • 77951796238 scopus 로고    scopus 로고
    • Glucose-6-phosphate dehydrogenase and red cell pyruvate kinase deficiency in neonatal jaundice cases in egypt Pediatr
    • Abdel, F. M., Abdel, G. E., Adel, A., Mosallam, D., and Kamal, S. (2010). Glucose-6-phosphate dehydrogenase and red cell pyruvate kinase deficiency in neonatal jaundice cases in egypt. Pediatr. Hematol. Oncol. 27, 262-271. doi: 10.3109/08880011003639986
    • (2010) Hematol. Oncol. , vol.27 , pp. 262-271
    • Abdel, F.M.1    Abdel, G.E.2    Adel, A.3    Mosallam, D.4    Kamal, S.5
  • 2
    • 0001412393 scopus 로고
    • The linkage between oxygenation and subunit dissociation in human hemoglobin
    • Ackers, G. K., and Halvorson, H. R. (1974). The linkage between oxygenation and subunit dissociation in human hemoglobin. Proc. Natl. Acad. Sci. U.S.A. 71, 4312-4316. doi: 10.1073/pnas.71.11.4312
    • (1974) Proc. Natl. Acad. Sci. U. S. A. , vol.71 , pp. 4312-4316
    • Ackers, G.K.1    Halvorson, H.R.2
  • 3
    • 0026318447 scopus 로고
    • Hemin: a possible physiological mediator of low density lipoprotein oxidation and endothelial injury
    • Balla, G., Jacob, H. S., Eaton, J. W., Belcher, J. D., and Vercellotti, G. M. (1991). Hemin: a possible physiological mediator of low density lipoprotein oxidation and endothelial injury. Arterioscler. Thromb. 11, 1700-1711. doi: 10.1161/01.ATV.11.6.1700
    • (1991) Arterioscler. Thromb. , vol.11 , pp. 1700-1711
    • Balla, G.1    Jacob, H.S.2    Eaton, J.W.3    Belcher, J.D.4    Vercellotti, G.M.5
  • 4
    • 77955204547 scopus 로고    scopus 로고
    • Erythrocyte membrane defects and asymmetry in paroxysmal nocturnal hemoglobinuria and myelodysplastic syndrome
    • Basu, S., Banerjee, D., Ghosh, M., and Chakrabarti, A. (2010). Erythrocyte membrane defects and asymmetry in paroxysmal nocturnal hemoglobinuria and myelodysplastic syndrome. Hematology 15, 236-239. doi: 10.1179/102453309X12583347114095
    • (2010) Hematology , vol.15 , pp. 236-239
    • Basu, S.1    Banerjee, D.2    Ghosh, M.3    Chakrabarti, A.4
  • 5
    • 68849086892 scopus 로고    scopus 로고
    • Sequestration of extracellular hemoglobin within a haptoglobin complex decreases its hypertensive and oxidative effects in dogs and guinea pigs
    • Boretti, F. S., Buehler, P. W., D'Agnillo, F., Kluge, K., Glaus, T., Butt, O. I., et al. (2009). Sequestration of extracellular hemoglobin within a haptoglobin complex decreases its hypertensive and oxidative effects in dogs and guinea pigs. J. Clin. Invest. 119, 2271-2280. doi: 10.1172/JCI39115
    • (2009) J. Clin. Invest. , vol.119 , pp. 2271-2280
    • Boretti, F.S.1    Buehler, P.W.2    D'Agnillo, F.3    Kluge, K.4    Glaus, T.5    Butt, O.I.6
  • 6
    • 0014408353 scopus 로고
    • Exchange of heme among hemoglobins and between hemoglobin and albumin
    • Bunn, H. F., and Jandl, J. H. (1968). Exchange of heme among hemoglobins and between hemoglobin and albumin. J. Biol. Chem. 243, 465-475.
    • (1968) J. Biol. Chem. , vol.243 , pp. 465-475
    • Bunn, H.F.1    Jandl, J.H.2
  • 7
    • 77949499744 scopus 로고    scopus 로고
    • Differential induction of renal heme oxygenase and ferritin in ascorbate and nonascorbate producing species transfused with modified cell-free hemoglobin
    • Butt, O. I., Buehler, P. W., and D'Agnillo, F. (2010). Differential induction of renal heme oxygenase and ferritin in ascorbate and nonascorbate producing species transfused with modified cell-free hemoglobin. Antioxid. Redox Signal. 12, 199-208. doi: 10.1089/ars.2009.2798
    • (2010) Antioxid. Redox Signal. , vol.12 , pp. 199-208
    • Butt, O.I.1    Buehler, P.W.2    D'Agnillo, F.3
  • 8
    • 70349610358 scopus 로고    scopus 로고
    • Nitrite enhances RBC hypoxic ATP synthesis and the release of ATP into the vasculature: a new mechanism for nitrite-induced vasodilation
    • Cao, Z., Bell, J. B., Mohanty, J. G., Nagababu, E., and Rifkind, J. M. (2009). Nitrite enhances RBC hypoxic ATP synthesis and the release of ATP into the vasculature: a new mechanism for nitrite-induced vasodilation. Am. J. Physiol. Heart Circ. Physiol. 297, H1494-H1503. doi: 10.1152/ajpheart.01233.2008
    • (2009) Am. J. Physiol. Heart Circ. Physiol. , vol.297 , pp. H1494-H1503
    • Cao, Z.1    Bell, J.B.2    Mohanty, J.G.3    Nagababu, E.4    Rifkind, J.M.5
  • 9
    • 84881376528 scopus 로고    scopus 로고
    • Hereditary spherocytosis, elliptocytosis, and other red cell membrane disorders
    • Da, C. L., Galimand, J., Fenneteau, O., and Mohandas, N. (2013). Hereditary spherocytosis, elliptocytosis, and other red cell membrane disorders. Blood Rev. 27, 167-178. doi: 10.1016/j.blre.2013.04.003
    • (2013) Blood Rev , vol.27 , pp. 167-178
    • Da, C.L.1    Galimand, J.2    Fenneteau, O.3    Mohandas, N.4
  • 10
    • 1642483018 scopus 로고    scopus 로고
    • Identification of free radicals on hemoglobin from its self-peroxidation using mass spectrometry and immuno-spin trapping: observation of a histidinyl radical
    • Deterding, L. J., Ramirez, D. C., Dubin, J. R., Mason, R. P., and Tomer, K. B. (2004). Identification of free radicals on hemoglobin from its self-peroxidation using mass spectrometry and immuno-spin trapping: observation of a histidinyl radical. J. Biol. Chem. 279, 11600-11607. doi: 10.1074/jbc.M310704200
    • (2004) J. Biol. Chem. , vol.279 , pp. 11600-11607
    • Deterding, L.J.1    Ramirez, D.C.2    Dubin, J.R.3    Mason, R.P.4    Tomer, K.B.5
  • 11
    • 52549119182 scopus 로고    scopus 로고
    • A central role for free heme in the pathogenesis of severe malaria: the missing link? J
    • Ferreira, A., Balla, J., Jeney, V., Balla, G., and Soares, M. P. (2008). A central role for free heme in the pathogenesis of severe malaria: the missing link? J. Mol. Med. (Berl.) 86, 1097-1111. doi: 10.1007/s00109-008-0368-5
    • (2008) Mol. Med. (Berl. ) , vol.86 , pp. 1097-1111
    • Ferreira, A.1    Balla, J.2    Jeney, V.3    Balla, G.4    Soares, M.P.5
  • 12
    • 84858017083 scopus 로고    scopus 로고
    • Heme induces programmed necrosis on macrophages through autocrine TNF and ROS production
    • Fortes, G. B., Alves, L. S., de Oliveira, R., Dutra, F. F., Rodrigues, D., Fernandez, P. L., et al. (2012). Heme induces programmed necrosis on macrophages through autocrine TNF and ROS production. Blood 119, 2368-2375. doi: 10.1182/blood-2011-08-375303
    • (2012) Blood , vol.119 , pp. 2368-2375
    • Fortes, G.B.1    Alves, L.S.2    de Oliveira, R.3    Dutra, F.F.4    Rodrigues, D.5    Fernandez, P.L.6
  • 13
    • 0021131198 scopus 로고
    • Superoxide dismutase, catalase, and glutathione peroxidase in red blood cells from patients with malignant diseases
    • Gonzales, R., Auclair, C., Voisin, E., Gautero, H., Dhermy, D., and Boivin, P. (1984). Superoxide dismutase, catalase, and glutathione peroxidase in red blood cells from patients with malignant diseases. Cancer Res. 44, 4137-4139.
    • (1984) Cancer Res , vol.44 , pp. 4137-4139
    • Gonzales, R.1    Auclair, C.2    Voisin, E.3    Gautero, H.4    Dhermy, D.5    Boivin, P.6
  • 14
    • 77952522924 scopus 로고    scopus 로고
    • Extracellular haemoglobin, oxidative stress and quality of red blood cells relative to perioperative blood salvage
    • Gueye, P. M., Bertrand, F., Duportail, G., and Lessinger, J. M. (2010). Extracellular haemoglobin, oxidative stress and quality of red blood cells relative to perioperative blood salvage. Clin. Chem. Lab. Med. 48, 677-683. doi: 10.1515/CCLM.2010.106
    • (2010) Clin. Chem. Lab. Med. , vol.48 , pp. 677-683
    • Gueye, P.M.1    Bertrand, F.2    Duportail, G.3    Lessinger, J.M.4
  • 15
    • 0022021390 scopus 로고
    • Auto-oxidation and a membrane-associated 'Fenton reagent': a possible explanation for development of membrane lesions in sickle erythrocytes
    • Hebbel, R. P. (1985). Auto-oxidation and a membrane-associated 'Fenton reagent': a possible explanation for development of membrane lesions in sickle erythrocytes. Clin. Haematol. 14, 129-140.
    • (1985) Clin. Haematol. , vol.14 , pp. 129-140
    • Hebbel, R.P.1
  • 16
    • 0018723614 scopus 로고
    • Pathophysiology of Tamm-Horsfall protein
    • Hoyer, J. R., and Seiler, M. W. (1979). Pathophysiology of Tamm-Horsfall protein. Kidney Int. 16, 279-289. doi: 10.1038/ki.1979.130
    • (1979) Kidney Int , vol.16 , pp. 279-289
    • Hoyer, J.R.1    Seiler, M.W.2
  • 18
    • 0020611314 scopus 로고
    • Intraoperative autotransfusion. Experience in 725 consecutive cases
    • Keeling, M. M., Gray, L. A. Jr., Brink, M. A., Hillerich, V. K., and Bland, K. I. (1983). Intraoperative autotransfusion. Experience in 725 consecutive cases. Ann. Surg. 197, 536-541. doi: 10.1097/00000658-198305000-00006
    • (1983) Ann. Surg. , vol.197 , pp. 536-541
    • Keeling, M.M.1    Gray Jr, L.A.2    Brink, M.A.3    Hillerich, V.K.4    Bland, K.I.5
  • 19
    • 0034842052 scopus 로고    scopus 로고
    • Oligomerization and ligand binding in a homotetrameric hemoglobin: two high-resolution crystal structures of hemoglobin Bart's (gamma(4)), a marker for alpha-thalassemia
    • Kidd, R. D., Baker, H. M., Mathews, A. J., Brittain, T., and Baker, E. N. (2001). Oligomerization and ligand binding in a homotetrameric hemoglobin: two high-resolution crystal structures of hemoglobin Bart's (gamma(4)), a marker for alpha-thalassemia. Protein Sci. 10, 1739-1749. doi: 10.1110/ps.11701
    • (2001) Protein Sci , vol.10 , pp. 1739-1749
    • Kidd, R.D.1    Baker, H.M.2    Mathews, A.J.3    Brittain, T.4    Baker, E.N.5
  • 20
    • 10744233389 scopus 로고    scopus 로고
    • Peroxiredoxin II is essential for sustaining life span of erythrocytes in mice
    • Lee, T. H., Kim, S. U., Yu, S. L., Kim, S. H., Park, D. S., Moon, H. B., et al. (2003). Peroxiredoxin II is essential for sustaining life span of erythrocytes in mice. Blood 101, 5033-5038. doi: 10.1182/blood-2002-08-2548
    • (2003) Blood , vol.101 , pp. 5033-5038
    • Lee, T.H.1    Kim, S.U.2    Yu, S.L.3    Kim, S.H.4    Park, D.S.5    Moon, H.B.6
  • 21
    • 84862822312 scopus 로고    scopus 로고
    • Microglial TIR-domain-containing adapter-inducing interferon-beta (TRIF) deficiency promotes retinal ganglion cell survival and axon regeneration via nuclear factor-kappaB
    • Lin, S., Liang, Y., Zhang, J., Bian, C., Zhou, H., Guo, Q., et al. (2012). Microglial TIR-domain-containing adapter-inducing interferon-beta (TRIF) deficiency promotes retinal ganglion cell survival and axon regeneration via nuclear factor-kappaB. J. Neuroinflammation 9, 39. doi: 10.1186/1742-2094-9-39
    • (2012) J. Neuroinflammation , vol.9 , pp. 39
    • Lin, S.1    Liang, Y.2    Zhang, J.3    Bian, C.4    Zhou, H.5    Guo, Q.6
  • 22
    • 0142116222 scopus 로고    scopus 로고
    • Methemoglobin is a potent activator of endothelial cells by stimulating IL-6 and IL-8 production and E-selectin membrane expression
    • Liu, X., and Spolarics, Z. (2003). Methemoglobin is a potent activator of endothelial cells by stimulating IL-6 and IL-8 production and E-selectin membrane expression. Am. J. Physiol. Cell Physiol. 285, C1036-C1046. doi: 10.1152/ajpcell.00164.2003
    • (2003) Am. J. Physiol. Cell Physiol. , vol.285 , pp. C1036-C1046
    • Liu, X.1    Spolarics, Z.2
  • 23
    • 0032997659 scopus 로고    scopus 로고
    • Kinetics of hemin distribution in plasma reveals its role in lipoprotein oxidation
    • Miller, Y. I., and Shaklai, N. (1999). Kinetics of hemin distribution in plasma reveals its role in lipoprotein oxidation. Biochim. Biophys. Acta 1454, 153-164. doi: 10.1016/S0925-4439(99)00027-7
    • (1999) Biochim. Biophys. Acta , vol.1454 , pp. 153-164
    • Miller, Y.I.1    Shaklai, N.2
  • 24
    • 3242735024 scopus 로고    scopus 로고
    • Hydrogen-peroxide-induced heme degradation in red blood cells: the protective roles of catalase and glutathione peroxidase
    • Nagababu, E., Chrest, F. J., and Rifkind, J. M. (2003). Hydrogen-peroxide-induced heme degradation in red blood cells: the protective roles of catalase and glutathione peroxidase. Biochim. Biophys. Acta 1620, 211-217. doi: 10.1016/S0304-4165(02)00537-8
    • (2003) Biochim. Biophys. Acta , vol.1620 , pp. 211-217
    • Nagababu, E.1    Chrest, F.J.2    Rifkind, J.M.3
  • 25
    • 44649126828 scopus 로고    scopus 로고
    • Heme degradation and oxidative stress in murine models for hemoglobinopathies: thalassemia, sickle cell disease and hemoglobin C disease
    • Nagababu, E., Fabry, M. E., Nagel, R. L., and Rifkind, J. M. (2008a). Heme degradation and oxidative stress in murine models for hemoglobinopathies: thalassemia, sickle cell disease and hemoglobin C disease. Blood Cells Mol. Dis. 41, 60-66. doi: 10.1016/j.bcmd.2007.12.003
    • (2008) Blood Cells Mol. Dis. , vol.41 , pp. 60-66
    • Nagababu, E.1    Fabry, M.E.2    Nagel, R.L.3    Rifkind, J.M.4
  • 27
    • 84873683820 scopus 로고    scopus 로고
    • Role of peroxiredoxin-2 in protecting RBCs from hydrogen peroxide-induced oxidative stress
    • Nagababu, E., Mohanty, J. G., Friedman, J. S., and Rifkind, J. M. (2013). Role of peroxiredoxin-2 in protecting RBCs from hydrogen peroxide-induced oxidative stress. Free Radic. Res. 47, 164-171. doi: 10.3109/10715762.2012.756138
    • (2013) Free Radic. Res. , vol.47 , pp. 164-171
    • Nagababu, E.1    Mohanty, J.G.2    Friedman, J.S.3    Rifkind, J.M.4
  • 28
    • 0032577878 scopus 로고    scopus 로고
    • Formation of fluorescent heme degradation products during the oxidation of hemoglobin by hydrogen peroxide
    • Nagababu, E., and Rifkind, J. M. (1998). Formation of fluorescent heme degradation products during the oxidation of hemoglobin by hydrogen peroxide. Biochem. Biophys. Res. Commun. 247, 592-596. doi: 10.1006/bbrc.1998.8846
    • (1998) Biochem. Biophys. Res. Commun. , vol.247 , pp. 592-596
    • Nagababu, E.1    Rifkind, J.M.2
  • 29
    • 0034633998 scopus 로고    scopus 로고
    • Reaction of hydrogen peroxide with ferrylhemoglobin: superoxide production and heme degradation
    • Nagababu, E., and Rifkind, J. M. (2000). Reaction of hydrogen peroxide with ferrylhemoglobin: superoxide production and heme degradation. Biochemistry 39, 12503-12511. doi: 10.1021/bi992170y
    • (2000) Biochemistry , vol.39 , pp. 12503-12511
    • Nagababu, E.1    Rifkind, J.M.2
  • 31
    • 0031888839 scopus 로고    scopus 로고
    • Intracellular targets in heme protein-induced renal injury
    • Nath, K. A., Grande, J. P., Croatt, A. J., Likely, S., Hebbel, R. P., and Enright, H. (1998). Intracellular targets in heme protein-induced renal injury. Kidney Int. 53, 100-111. doi: 10.1046/j.1523-1755.1998.00731.x
    • (1998) Kidney Int , vol.53 , pp. 100-111
    • Nath, K.A.1    Grande, J.P.2    Croatt, A.J.3    Likely, S.4    Hebbel, R.P.5    Enright, H.6
  • 32
    • 0036424313 scopus 로고    scopus 로고
    • Severe alloimmune hemolytic anemia after renal transplantation
    • Odabas, A. R., Tutucu, K. N., Turkmen, A., Keskin, H., and Sever, M. S. (2002). Severe alloimmune hemolytic anemia after renal transplantation. Nephron 92, 743-745. doi: 10.1159/000064093
    • (2002) Nephron , vol.92 , pp. 743-745
    • Odabas, A.R.1    Tutucu, K.N.2    Turkmen, A.3    Keskin, H.4    Sever, M.S.5
  • 33
    • 0020409958 scopus 로고
    • Use of haemonetics Cell Saver for autotransfusion in cardiovascular surgery Scand
    • Ottesen, S., and Froysaker, T. (1982). Use of haemonetics Cell Saver for autotransfusion in cardiovascular surgery. Scand. J. Thorac. Cardiovasc. Surg. 16, 263-268. doi: 10.3109/14017438209101060
    • (1982) J. Thorac. Cardiovasc. Surg. , vol.16 , pp. 263-268
    • Ottesen, S.1    Froysaker, T.2
  • 34
  • 35
    • 84886415336 scopus 로고    scopus 로고
    • Humanized mouse model of glucose 6-phosphate dehydrogenase deficiency for in vivo assessment of hemolytic toxicity
    • Rochford, R., Ohrt, C., Baresel, P. C., Campo, B., Sampath, A., Magill, A. J., et al. (2013). Humanized mouse model of glucose 6-phosphate dehydrogenase deficiency for in vivo assessment of hemolytic toxicity. Proc. Natl. Acad. Sci. U.S.A. 110, 17486-17491. doi: 10.1073/pnas.1310402110
    • (2013) Proc. Natl. Acad. Sci. U. S. A. , vol.110 , pp. 17486-17491
    • Rochford, R.1    Ohrt, C.2    Baresel, P.C.3    Campo, B.4    Sampath, A.5    Magill, A.J.6
  • 36
    • 15944398355 scopus 로고    scopus 로고
    • The clinical sequelae of intravascular hemolysis and extracellular plasma hemoglobin: a novel mechanism of human disease
    • Rother, R. P., Bell, L., Hillmen, P., and Gladwin, M. T. (2005). The clinical sequelae of intravascular hemolysis and extracellular plasma hemoglobin: a novel mechanism of human disease. JAMA 293, 1653-1662. doi: 10.1001/jama.293.13.1653
    • (2005) JAMA , vol.293 , pp. 1653-1662
    • Rother, R.P.1    Bell, L.2    Hillmen, P.3    Gladwin, M.T.4
  • 37
    • 0024242512 scopus 로고
    • Hemoglobin-mediated oxidant damage to the central nervous system requires endogenous ascorbate
    • Sadrzadeh, S. M., and Eaton, J. W. (1988). Hemoglobin-mediated oxidant damage to the central nervous system requires endogenous ascorbate. J. Clin. Invest. 82, 1510-1515. doi: 10.1172/JCI113759
    • (1988) J. Clin. Invest. , vol.82 , pp. 1510-1515
    • Sadrzadeh, S.M.1    Eaton, J.W.2
  • 39
    • 84874439878 scopus 로고    scopus 로고
    • Hemolysis and free hemoglobin revisited: exploring hemoglobin and hemin scavengers as a novel class of therapeutic proteins
    • Schaer, D. J., Buehler, P. W., Alayash, A. I., Belcher, J. D., and Vercellotti, G. M. (2013). Hemolysis and free hemoglobin revisited: exploring hemoglobin and hemin scavengers as a novel class of therapeutic proteins. Blood 121, 1276-1284. doi: 10.1182/blood-2012-11-451229
    • (2013) Blood , vol.121 , pp. 1276-1284
    • Schaer, D.J.1    Buehler, P.W.2    Alayash, A.I.3    Belcher, J.D.4    Vercellotti, G.M.5
  • 40
    • 70350418736 scopus 로고    scopus 로고
    • Oxidized hemoglobin is an endogenous proinflammatory agonist that targets vascular endothelial cells
    • Silva, G., Jeney, V., Chora, A., Larsen, R., Balla, J., and Soares, M. P. (2009). Oxidized hemoglobin is an endogenous proinflammatory agonist that targets vascular endothelial cells. J. Biol. Chem. 284, 29582-29595. doi: 10.1074/jbc.M109.045344
    • (2009) J. Biol. Chem. , vol.284 , pp. 29582-29595
    • Silva, G.1    Jeney, V.2    Chora, A.3    Larsen, R.4    Balla, J.5    Soares, M.P.6
  • 41
    • 84877305820 scopus 로고    scopus 로고
    • Proinflammatory responses of heme in alveolar macrophages: repercussion in lung hemorrhagic episodes
    • Simoes, R. L., Arruda, M. A., Canetti, C., Serezani, C. H., Fierro, I. M., and Barja-Fidalgo, C. (2013). Proinflammatory responses of heme in alveolar macrophages: repercussion in lung hemorrhagic episodes. Mediators Inflamm. 2013:946878. doi: 10.1155/2013/946878
    • (2013) Mediators Inflamm , vol.2013
    • Simoes, R.L.1    Arruda, M.A.2    Canetti, C.3    Serezani, C.H.4    Fierro, I.M.5    Barja-Fidalgo, C.6
  • 42
    • 0000061171 scopus 로고
    • Modification of low density lipoprotein by endothelial cells involves lipid peroxidation and degradation of low density lipoprotein phospholipids
    • Steinbrecher, U. P., Parthasarathy, S., Leake, D. S., Witztum, J. L., and Steinberg, D. (1984). Modification of low density lipoprotein by endothelial cells involves lipid peroxidation and degradation of low density lipoprotein phospholipids. Proc. Natl. Acad. Sci. U.S.A. 81, 3883-3887. doi: 10.1073/pnas.81.12.3883
    • (1984) Proc. Natl. Acad. Sci. U.S.A. , vol.81 , pp. 3883-3887
    • Steinbrecher, U.P.1    Parthasarathy, S.2    Leake, D.S.3    Witztum, J.L.4    Steinberg, D.5
  • 43
    • 0023132858 scopus 로고
    • Bilirubin is an antioxidant of possible physiological importance
    • Stocker, R., Yamamoto, Y., McDonagh, A. F., Glazer, A. N., and Ames, B. N. (1987). Bilirubin is an antioxidant of possible physiological importance. Science 235, 1043-1046. doi: 10.1126/science.3029864
    • (1987) Science , vol.235 , pp. 1043-1046
    • Stocker, R.1    Yamamoto, Y.2    McDonagh, A.F.3    Glazer, A.N.4    Ames, B.N.5
  • 44
    • 76749153419 scopus 로고    scopus 로고
    • Activation of TLR4-mediated NFkappaB signaling in hemorrhagic brain in rats
    • Teng, W., Wang, L., Xue, W., and Guan, C. (2009). Activation of TLR4-mediated NFkappaB signaling in hemorrhagic brain in rats. Mediators Inflamm. 2009:473276. doi: 10.1155/2009/473276
    • (2009) Mediators Inflamm
    • Teng, W.1    Wang, L.2    Xue, W.3    Guan, C.4
  • 45
    • 33846664696 scopus 로고    scopus 로고
    • Physiology and pathophysiology of heme: implications for kidney disease
    • Tracz, M. J., Alam, J., and Nath, K. A. (2007). Physiology and pathophysiology of heme: implications for kidney disease. J. Am. Soc. Nephrol. 18, 414-420. doi: 10.1681/ASN.2006080894
    • (2007) J. Am. Soc. Nephrol. , vol.18 , pp. 414-420
    • Tracz, M.J.1    Alam, J.2    Nath, K.A.3
  • 46
    • 0035252322 scopus 로고    scopus 로고
    • Heme-induced cell adhesion in the pathogenesis of sickle-cell disease and inflammation
    • Wagener, F. A., Abraham, N. G., van Kooyk, Y., de Witte, T., and Figdor, C. G. (2001a). Heme-induced cell adhesion in the pathogenesis of sickle-cell disease and inflammation. Trends Pharmacol. Sci. 22, 52-54. doi: 10.1016/S0165-6147(00)01609-6
    • (2001) Trends Pharmacol. Sci. , vol.22 , pp. 52-54
    • Wagener, F.A.1    Abraham, N.G.2    van Kooyk, Y.3    de Witte, T.4    Figdor, C.G.5
  • 47
    • 0035885926 scopus 로고    scopus 로고
    • Heme is a potent inducer of inflammation in mice and is counteracted by heme oxygenase
    • Wagener, F. A., Eggert, A., Boerman, O. C., Oyen, W. J., Verhofstad, A., Abraham, N. G., et al. (2001b). Heme is a potent inducer of inflammation in mice and is counteracted by heme oxygenase. Blood 98, 1802-1811. doi: 10.1182/blood.V98.6.1802
    • (2001) Blood , vol.98 , pp. 1802-1811
    • Wagener, F.A.1    Eggert, A.2    Boerman, O.C.3    Oyen, W.J.4    Verhofstad, A.5    Abraham, N.G.6
  • 48
    • 0023688353 scopus 로고
    • Autoantibody against erythrocyte protein 4 1 in a patient with autoimmune hemolytic anemia
    • Wakui, H., Imai, H., Kobayashi, R., Itoh, H., Notoya, T., Yoshida, K., et al. (1988). Autoantibody against erythrocyte protein 4.1 in a patient with autoimmune hemolytic anemia. Blood 72, 408-412.
    • (1988) Blood , vol.72 , pp. 408-412
    • Wakui, H.1    Imai, H.2    Kobayashi, R.3    Itoh, H.4    Notoya, T.5    Yoshida, K.6
  • 49
    • 84870976528 scopus 로고    scopus 로고
    • In reply to Transfusion of older blood and risk of death: unanswered questions
    • Wang, D., Sun, J., Solomon, S. B., Klein, H. G., and Natanson, C. (2012). In reply to Transfusion of older blood and risk of death: unanswered questions. Transfusion 52, 2724-2725. doi: 10.1111/j.1537-2995.2012.03913.x
    • (2012) Transfusion , vol.52 , pp. 2724-2725
    • Wang, D.1    Sun, J.2    Solomon, S.B.3    Klein, H.G.4    Natanson, C.5
  • 50
    • 1842431892 scopus 로고    scopus 로고
    • Biology of heme in health and disease
    • Wijayanti, N., Katz, N., and Immenschuh, S. (2004). Biology of heme in health and disease. Curr. Med. Chem. 11, 981-986. doi: 10.2174/0929867043455521
    • (2004) Curr. Med. Chem. , vol.11 , pp. 981-986
    • Wijayanti, N.1    Katz, N.2    Immenschuh, S.3
  • 51
    • 4243607831 scopus 로고
    • Toxicity of iron and hydrogen peroxide: the Fenton reaction
    • Winterbourn, C. C. (1995). Toxicity of iron and hydrogen peroxide: the Fenton reaction. Toxicol. Lett. 82-83, 969-974. doi: 10.1016/0378-4274(95)03532-X
    • (1995) Toxicol. Lett , pp. 82-83
    • Winterbourn, C.C.1
  • 52
    • 0026354021 scopus 로고
    • Autoxidation of hemoglobin enhanced by dissociation into dimers
    • Zhang, L., Levy, A., and Rifkind, J. M. (1991). Autoxidation of hemoglobin enhanced by dissociation into dimers. J. Biol. Chem. 266, 24698-24701.
    • (1991) J. Biol. Chem. , vol.266 , pp. 24698-24701
    • Zhang, L.1    Levy, A.2    Rifkind, J.M.3


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