메뉴 건너뛰기




Volumn 178, Issue 3, 2011, Pages 1316-1328

Blood-brain barrier disruption and oxidative stress in guinea pig after systemic exposure to modified cell-free hemoglobin

Author keywords

[No Author keywords available]

Indexed keywords

4 HYDROXYNONENAL; 8 HYDROXYDEOXYGUANOSINE; ACTIN; CASPASE 3; CD163 ANTIGEN; CLAUDIN 5; GLIAL FIBRILLARY ACIDIC PROTEIN; HEME OXYGENASE; IMMUNOGLOBULIN G; IRON; OCCLUDIN; POLYMERIZED HEMOGLOBIN; PROTEIN ZO1;

EID: 79952763426     PISSN: 00029440     EISSN: 15252191     Source Type: Journal    
DOI: 10.1016/j.ajpath.2010.12.006     Document Type: Article
Times cited : (65)

References (63)
  • 1
    • 1842556541 scopus 로고    scopus 로고
    • Hematoma removal, heme, and heme oxygenase following hemorrhagic stroke
    • DOI 10.1196/annals.1306.020
    • Wagner KR, Dwyer BE: Hematoma removal, heme, and heme oxygenase following hemorrhagic stroke. Ann N Y Acad Sci 2004, 1012:237-251 (Pubitemid 38453529)
    • (2004) Annals of the New York Academy of Sciences , vol.1012 , pp. 237-251
    • Wagner, K.R.1    Dwyer, B.E.2
  • 2
    • 73949099862 scopus 로고    scopus 로고
    • Hemin toxicity: A preventable source of brain damage following hemorrhagic stroke
    • Robinson SR, Dang TN, Dringen R, Bishop GM: Hemin toxicity: a preventable source of brain damage following hemorrhagic stroke. Redox Rep 2009, 14:228-235
    • (2009) Redox Rep , vol.14 , pp. 228-235
    • Robinson, S.R.1    Dang, T.N.2    Dringen, R.3    Bishop, G.M.4
  • 4
    • 1142298608 scopus 로고    scopus 로고
    • Experimental subarachnoid hemorrhage: Cerebral blood flow and brain metabolism during the acute phase in three different models in the rat
    • Prunell GF, Mathiesen T, Svendgaard NA: Experimental subarachnoid hemorrhage: cerebral blood flow and brain metabolism during the acute phase in three different models in the rat. Neurosurgery 2004, 54:426-436
    • (2004) Neurosurgery , vol.54 , pp. 426-436
    • Prunell, G.F.1    Mathiesen, T.2    Svendgaard, N.A.3
  • 5
    • 77956501969 scopus 로고    scopus 로고
    • Hemoglobin-induced oxidative stress contributes to matrix metalloproteinase activation and blood-brain barrier dysfunction in vivo
    • Katsu M, Niizuma K, Yoshioka H, Okami N, Sakata H, Chan PH: Hemoglobin-induced oxidative stress contributes to matrix metalloproteinase activation and blood-brain barrier dysfunction in vivo. J Cereb Blood Flow Metab 2010, 30:1939-1950
    • (2010) J Cereb Blood Flow Metab , vol.30 , pp. 1939-1950
    • Katsu, M.1    Niizuma, K.2    Yoshioka, H.3    Okami, N.4    Sakata, H.5    Chan, P.H.6
  • 6
    • 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: Brain edema after experimental intracerebral hemorrhage: role of hemoglobin degradation products. J Neurosurg 2002, 96:287-293 (Pubitemid 34230243)
    • (2002) Journal of Neurosurgery , vol.96 , Issue.2 , pp. 287-293
    • Huang, F.-P.1    Xi, G.2    Keep, R.F.3    Hua, Y.4    Nemoianu, A.5    Hoff, J.T.6
  • 7
    • 34250782407 scopus 로고    scopus 로고
    • Heme oxygenase-1 exacerbates early brain injury after intracerebral haemorrhage
    • DOI 10.1093/brain/awm095
    • Wang J, Doré S: Heme oxygenase-1 exacerbates early brain injury after intracerebral haemorrhage. Brain 2007, 130:1643-1652 (Pubitemid 47355932)
    • (2007) Brain , vol.130 , Issue.6 , pp. 1643-1652
    • Wang, J.1    Dore, S.2
  • 9
    • 77949513218 scopus 로고    scopus 로고
    • Toxicological consequences of extracellular hemoglobin: Biochemical and physiological perspectives
    • Buehler PW, D'Agnillo F: Toxicological consequences of extracellular hemoglobin: biochemical and physiological perspectives. Antioxid Redox Signal 2010, 12:275-291
    • (2010) Antioxid Redox Signal , vol.12 , pp. 275-291
    • Buehler, P.W.1    D'Agnillo, F.2
  • 10
    • 0035760898 scopus 로고    scopus 로고
    • Redox cycling of diaspirin cross-linked hemoglobin induces G2/M arrest and apoptosis in cultured endothelial cells
    • D'Agnillo F, Alayash AI: Redox cycling of diaspirin cross-linked hemoglobin induces G2/M arrest and apoptosis in cultured endothelial cells. Blood 2001, 98:3315-3323
    • (2001) Blood , vol.98 , pp. 3315-3323
    • D'Agnillo, F.1    Alayash, A.I.2
  • 11
    • 15944398355 scopus 로고    scopus 로고
    • The clinical sequelae of intravascular hemolysis and extracellular plasma hemoglobin: A novel mechanism of human disease
    • DOI 10.1001/jama.293.13.1653
    • Rother RP, Bell L, Hillmen P, Gladwin MT: The clinical sequelae of intravascular hemolysis and extracellular plasma hemoglobin: a novel mechanism of human disease. JAMA 2005, 293:1653-1662 (Pubitemid 40471796)
    • (2005) Journal of the American Medical Association , vol.293 , Issue.13 , pp. 1653-1662
    • Rother, R.P.1    Bell, L.2    Hillmen, P.3    Gladwin, M.T.4
  • 12
    • 69549107429 scopus 로고    scopus 로고
    • Vasculopathy in sickle cell disease: Biology, pathophysiology, genetics, translational medicine, and new research directions
    • Kato GJ, Hebbel RP, Steinberg MH, Gladwin MT: Vasculopathy in sickle cell disease: biology, pathophysiology, genetics, translational medicine, and new research directions. Am J Hematol 2009, 84:618-625
    • (2009) Am J Hematol , vol.84 , pp. 618-625
    • Kato, G.J.1    Hebbel, R.P.2    Steinberg, M.H.3    Gladwin, M.T.4
  • 13
    • 70449127973 scopus 로고    scopus 로고
    • Hemoglobin-based oxygen carriers: Current status and future directions
    • Silverman TA, Weiskopf RB: Hemoglobin-based oxygen carriers: current status and future directions. Transfusion 2009, 49:2495-2515
    • (2009) Transfusion , vol.49 , pp. 2495-2515
    • Silverman, T.A.1    Weiskopf, R.B.2
  • 14
    • 59649121245 scopus 로고    scopus 로고
    • Cerebral malaria and the hemolysis/methemoglobin/heme hypothesis: Shedding new light on an old disease
    • Pamplona A, Hanscheid T, Epiphanio S, Mota MM, Vigário AM: Cerebral malaria and the hemolysis/methemoglobin/heme hypothesis: shedding new light on an old disease. Int J Biochem Cell Biol 2009, 41:711-716
    • (2009) Int J Biochem Cell Biol , vol.41 , pp. 711-716
    • Pamplona, A.1    Hanscheid, T.2    Epiphanio, S.3    Mota, M.M.4    Vigário, A.M.5
  • 16
    • 0031008410 scopus 로고    scopus 로고
    • A proposed biochemical mechanism involving hemoglobin for blast overpressure-induced injury
    • DOI 10.1016/S0300-483X(97)03657-3, PII S0300483X97036573
    • Elsayed NM, Gorbunov NV, Kagan VE: A proposed biochemical mechanism involving hemoglobin for blast overpressure-induced injury. Toxicology 1997, 121:81-90 (Pubitemid 27259676)
    • (1997) Toxicology , vol.121 , Issue.1 , pp. 81-90
    • Elsayed, N.M.1    Gorbunov, N.V.2    Kagan, V.E.3
  • 19
    • 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 OI, Buehler PW, D'Agnillo F: Differential induction of renal heme oxygenase and ferritin in ascorbate and nonascorbate producing species transfused with modified cell-free hemoglobin. Antioxid Redox Signal 2010, 12:199-208
    • (2010) Antioxid Redox Signal , vol.12 , pp. 199-208
    • Butt, O.I.1    Buehler, P.W.2    D'Agnillo, F.3
  • 20
    • 41149177025 scopus 로고    scopus 로고
    • Pharmacological and clinical aspects of heme oxygenase
    • DOI 10.1124/pr.107.07104
    • Abraham NG, Kappas A: Pharmacological and clinical aspects of heme oxygenase. Pharmacol Rev 2008, 60:79-127 (Pubitemid 351439218)
    • (2008) Pharmacological Reviews , vol.60 , Issue.1 , pp. 79-127
    • Abraham, N.G.1    Kappas, A.2
  • 21
    • 67649628772 scopus 로고    scopus 로고
    • Heme oxygenase-1 and neurodegeneration: Expanding frontiers of engagement
    • Schipper HM, Song W, Zukor H, Hascalovici JR, Zeligman D: Heme oxygenase-1 and neurodegeneration: expanding frontiers of engagement. Neurochem 2009, 110:469-485
    • (2009) Neurochem , vol.110 , pp. 469-485
    • Schipper, H.M.1    Song, W.2    Zukor, H.3    Hascalovici, J.R.4    Zeligman, D.5
  • 24
    • 0032972686 scopus 로고    scopus 로고
    • Overexpression of heme oxygenase-1 is neuroprotective in a model of permanent middle cerebral artery occlusion in transgenic mice
    • Panahian N, Yoshiura M, Maines MD: Overexpression of heme oxygenase-1 is neuroprotective in a model of permanent middle cerebral artery occlusion in transgenic mice. J Neurochem 1999, 72:1187-1203 (Pubitemid 29085035)
    • (1999) Journal of Neurochemistry , vol.72 , Issue.3 , pp. 1187-1203
    • Panahian, N.1    Yoshiura, M.2    Maines, M.D.3
  • 25
    • 67649958020 scopus 로고    scopus 로고
    • Induction of heme oxygenase-1 with hemin attenuates hippocampal injury in rats after acute carbon monoxide poisoning
    • Guan L, Wen T, Zhang Y, Wang X, Zhao J: Induction of heme oxygenase-1 with hemin attenuates hippocampal injury in rats after acute carbon monoxide poisoning. Toxicology 2009, 262:146-152
    • (2009) Toxicology , vol.262 , pp. 146-152
    • Guan, L.1    Wen, T.2    Zhang, Y.3    Wang, X.4    Zhao, J.5
  • 26
    • 85052609611 scopus 로고    scopus 로고
    • Systemic zinc protoporphyrin administration reduces intracerebral hemorrhage-induced brain injury
    • Gong Y, Tian H, Xi G, Keep RF, Hoff JT, Hua Y: Systemic zinc protoporphyrin administration reduces intracerebral hemorrhage-induced brain injury. Acta Neurochir Suppl 2006, 96:232-236
    • (2006) Acta Neurochir Suppl , vol.96 , pp. 232-236
    • Gong, Y.1    Tian, H.2    Xi, G.3    Keep, R.F.4    Hoff, J.T.5    Hua, Y.6
  • 27
    • 36249027101 scopus 로고    scopus 로고
    • Time course of increased heme oxygenase activity and expression after experimental intracerebral hemorrhage: Correlation with oxidative injury
    • DOI 10.1111/j.1471-4159.2007.04885.x
    • Chen M, Regan RF: Time course of increased heme oxygenase activity and expression after experimental intracerebral hemorrhage: correlation with oxidative injury. J Neurochem 2007, 103:2015-2021 (Pubitemid 350126616)
    • (2007) Journal of Neurochemistry , vol.103 , Issue.5 , pp. 2015-2021
    • Chen, M.1    Regan, R.F.2
  • 28
    • 22944483792 scopus 로고    scopus 로고
    • The blood-brain barrier/neurovascular unit in health and disease
    • DOI 10.1124/pr.57.2.4
    • Hawkins BT, Davis TP: The blood-brain barrier/neurovascular unit in health and disease. Pharmacol Rev 2005, 57:173-185 (Pubitemid 41043883)
    • (2005) Pharmacological Reviews , vol.57 , Issue.2 , pp. 173-185
    • Hawkins, B.T.1    Davis, T.P.2
  • 29
    • 33747368249 scopus 로고    scopus 로고
    • Blood-brain barrier: Structural components and function under physiologic and pathologic conditions
    • DOI 10.1007/s11481-006-9025-3
    • Persidsky Y, Ramirez SH, Haorah J, Kanmogne GD: Blood-brain barrier: structural components and function under physiologic and pathologic conditions. J Neuroimmune Pharmacol 2006, 1:223-236 (Pubitemid 44244128)
    • (2006) Journal of Neuroimmune Pharmacology , vol.1 , Issue.3 , pp. 223-236
    • Persidsky, Y.1    Ramirez, S.H.2    Haorah, J.3    Kanmogne, G.D.4
  • 30
    • 33750546285 scopus 로고    scopus 로고
    • Hypoxia-induced astrocytic reaction and increased vascular permeability in the rat cerebellum
    • DOI 10.1002/glia.20420
    • Kaur C, Sivakumar V, Zhang Y, Ling EA: Hypoxia-induced astrocytic reaction and increased vascular permeability in the rat cerebellum. Glia 2006, 54:826-839 (Pubitemid 44671988)
    • (2006) GLIA , vol.54 , Issue.8 , pp. 826-839
    • Kaur, C.1    Sivakumar, V.2    Zhang, Y.3    Ling, E.A.4
  • 31
    • 0031027062 scopus 로고    scopus 로고
    • Morphological and immunophenotypic microglial changes in the denervated fascia dentata of adult rats: Correlation with blood-brain barrier damage and astroglial reactions
    • DOI 10.1006/exnr.1996.6337
    • Jensen MB, Finsen B, Zimmer J: Morphological and immunophenotypic microglial changes in the denervated fascia dentata of adult rats: correlation with blood-brain barrier damage and astroglial reactions. Exp Neurol 1997, 143:103-116 (Pubitemid 27049135)
    • (1997) Experimental Neurology , vol.143 , Issue.1 , pp. 103-116
    • Jensen, M.B.1    Finsen, B.2    Zimmer, J.3
  • 32
    • 1542373666 scopus 로고    scopus 로고
    • Microglia, macrophages, perivascular macrophages, and pericytes: A review of function and identification
    • DOI 10.1189/jlb.0303114
    • Guillemin GJ, Brew BJ: Microglia, macrophages, perivascular macrophages, and pericytes: a review of function and identification. J Leukoc Biol 2004, 75:388-397 (Pubitemid 38316367)
    • (2004) Journal of Leukocyte Biology , vol.75 , Issue.3 , pp. 388-397
    • Guillemin, G.J.1    Brew, B.J.2
  • 33
    • 73349140140 scopus 로고    scopus 로고
    • CNS pericytes: Concepts, misconceptions, and a way out
    • Krueger M, Bechmann I: CNS pericytes: concepts, misconceptions, and a way out. Glia 2010, 58:1-10
    • (2010) Glia , vol.58 , pp. 1-10
    • Krueger, M.1    Bechmann, I.2
  • 34
    • 34548842263 scopus 로고    scopus 로고
    • Effects of endogenous ascorbate on oxidation, oxygenation, and toxicokinetics of cell-free modified hemoglobin after exchange transfusion in rat and guinea pig
    • DOI 10.1124/jpet.107.126409
    • Buehler PW, D'Agnillo F, Hoffman V, Alayash AI: Effects of endogenous ascorbate on oxidation, oxygenation, and toxicokinetics of cellfree modified hemoglobin after exchange transfusion in rat and guinea pig. J Pharmacol Exp Ther 2007, 323:49-60 (Pubitemid 47443285)
    • (2007) Journal of Pharmacology and Experimental Therapeutics , vol.323 , Issue.1 , pp. 49-60
    • Buehler, P.W.1    D'Agnillo, F.2    Hoffman, V.3    Alayash, A.I.4
  • 35
    • 20444385158 scopus 로고    scopus 로고
    • Structural and functional characterization of glutaraldehyde-polymerized bovine hemoglobin and its isolated fractions
    • DOI 10.1021/ac050064y
    • Buehler PW, Boykins RA, Jia Y, Norris S, Freedberg DI, Alayash AI: Structural and functional characterization of glutaraldehyde-polymerized bovine hemoglobin and its isolated fractions. Anal Chem 2005, 77:3466-3478 (Pubitemid 40799835)
    • (2005) Analytical Chemistry , vol.77 , Issue.11 , pp. 3466-3478
    • Buehler, P.W.1    Boykins, R.A.2    Jia, Y.3    Norris, S.4    Freedberg, D.I.5    Alayash, A.I.6
  • 37
    • 0029799191 scopus 로고    scopus 로고
    • Carbon monoxide and nitric oxide homology: Differential modulation of heme oxygenases in brain and detection of protein and activity
    • Maines M: Carbon monoxide and nitric oxide homology: differential modulation of heme oxygenases in brain and detection of protein and activity. Methods Enzymol 1996, 268:473-488
    • (1996) Methods Enzymol , vol.268 , pp. 473-488
    • Maines, M.1
  • 38
    • 0015040637 scopus 로고
    • Spectrophotometric determination of serum iron at the submicrogram level with a new reagent (ferrozine)
    • Carter P: Spectrophotometric determination of serum iron at the submicrogram level with a new reagent (ferrozine). Anal Biochem 1971, 40:450-458
    • (1971) Anal Biochem , vol.40 , pp. 450-458
    • Carter, P.1
  • 39
    • 34250367117 scopus 로고    scopus 로고
    • Nonheme-iron histochemistry for light and electron microscopy: A historical, theoretical and technical review
    • DOI 10.1679/aohc.70.1
    • Meguro R, Asano Y, Odagiri S, Li C, Iwatsuki H, Shoumura K: Nonheme-iron histochemistry for light and electron microscopy: a historical, theoretical and technical review. Arch Histol Cytol 2007, 70:1-19 (Pubitemid 46917489)
    • (2007) Archives of Histology and Cytology , vol.70 , Issue.1 , pp. 1-19
    • Meguro, R.1    Asano, Y.2    Odagiri, S.3    Li, C.4    Iwatsuki, H.5    Shoumura, K.6
  • 40
    • 18844455657 scopus 로고
    • On the selective staining of the erythrocyte
    • Okajima K: On the selective staining of the erythrocyte. Anat Rec 1916, 11:295-296
    • (1916) Anat Rec , vol.11 , pp. 295-296
    • Okajima, K.1
  • 41
    • 0030250260 scopus 로고    scopus 로고
    • CNS microvascular pericytes express macrophage-like function, cell surface integrin alpha M, and macrophage marker ED-2
    • DOI 10.1006/mvre.1996.0049
    • Balabanov R, Washington R, Wagnerova J, Dore-Duffy P: CNS microvascular pericytes express macrophage-like function, cell surface integrin alpha M, and macrophage marker ED-2. Microvasc Res 1996, 52:127-142 (Pubitemid 26344909)
    • (1996) Microvascular Research , vol.52 , Issue.2 , pp. 127-142
    • Balabanov, R.1    Washington, R.2    Wagnerova, J.3    Dore-Duffy, P.4
  • 42
    • 77950627035 scopus 로고    scopus 로고
    • Scavenger receptor CD163, a Jack-of-all-trades and potential target for cell-directed therapy
    • Van Gorp H, Delputte PL, Nauwynck HJ: Scavenger receptor CD163, a Jack-of-all-trades and potential target for cell-directed therapy. Mol Immunol 2010, 47:1650-1660
    • (2010) Mol Immunol , vol.47 , pp. 1650-1660
    • Van Gorp, H.1    Delputte, P.L.2    Nauwynck, H.J.3
  • 44
    • 77449152992 scopus 로고    scopus 로고
    • Oxidative stress and its role in the pathogenesis of ischaemic stroke
    • Allen CL, Bayraktutan U: Oxidative stress and its role in the pathogenesis of ischaemic stroke. Int J Stroke 2009, 4:461-470
    • (2009) Int J Stroke , vol.4 , pp. 461-470
    • Allen, C.L.1    Bayraktutan, U.2
  • 45
    • 67650153191 scopus 로고    scopus 로고
    • Involvement of ROS in BBB dysfunction
    • Pun PB, Lu J, Moochhala S: Involvement of ROS in BBB dysfunction. Free Radic Res 2009, 43:348-364
    • (2009) Free Radic Res , vol.43 , pp. 348-364
    • Pun, P.B.1    Lu, J.2    Moochhala, S.3
  • 47
    • 33845776568 scopus 로고    scopus 로고
    • Alcohol-induced blood-brain barrier dysfunction is mediated via inositol 1,4,5-triphosphate receptor (IP3R)-gated intracellular calcium release
    • Haorah J, Knipe B, Gorantla S, Zheng J, Persidsky Y: Alcohol-induced blood-brain barrier dysfunction is mediated via inositol 1,4,5-triphosphate receptor (IP3R)-gated intracellular calcium release. J Neurochem 2007, 100:324-336
    • (2007) J Neurochem , vol.100 , pp. 324-336
    • Haorah, J.1    Knipe, B.2    Gorantla, S.3    Zheng, J.4    Persidsky, Y.5
  • 48
    • 0036901407 scopus 로고    scopus 로고
    • Tyrosine phosphorylation and dissociation of occludin-ZO-1 and E-cadherin-beta-catenin complexes from the cytoskeleton by oxidative stress
    • DOI 10.1042/BJ20011804
    • Rao RK, Basuroy S, Rao VU, Karnaky KJ Jr, Gupta A: Tyrosine phosphorylation and dissociation of occludin-ZO-1 and E-cadherin-beta-catenin complexes from the cytoskeleton by oxidative stress. Biochem J 2002, 368:471-481 (Pubitemid 35454525)
    • (2002) Biochemical Journal , vol.368 , Issue.2 , pp. 471-481
    • Rao, R.K.1    Basuroy, S.2    Rao, V.U.3    Karnaky Jr., K.J.4    Gupta, A.5
  • 49
  • 50
    • 40449135547 scopus 로고    scopus 로고
    • Cellular and molecular mechanisms of heat stress-induced up-regulation of occludin protein expression: Regulatory role of heat shock factor-1
    • DOI 10.2353/ajpath.2008.070522
    • Dokladny K, Ye D, Kennedy JC, Moseley PL, Ma TY: Cellular and molecular mechanisms of heat stress-induced up-regulation of occludin protein expression regulatory role of heat shock factor-1. Am J Pathol 2008, 172:659-670 (Pubitemid 351354539)
    • (2008) American Journal of Pathology , vol.172 , Issue.3 , pp. 659-670
    • Dokladny, K.1    Ye, D.2    Kennedy, J.C.3    Moseley, P.L.4    Ma, T.Y.5
  • 52
    • 28544449134 scopus 로고    scopus 로고
    • Cultured astrocytes from heme oxygenase-1 knockout mice are more vulnerable to heme-mediated oxidative injury
    • DOI 10.1002/jnr.20681
    • Chen-Roetling J, Benvenisti-Zarom L, Regan RF: Cultured astrocytes from heme oxygenase-1 knockout mice are more vulnerable to hememediated oxidative injury. J Neurosci Res 2005, 82:802-810 (Pubitemid 41746493)
    • (2005) Journal of Neuroscience Research , vol.82 , Issue.6 , pp. 802-810
    • Chen-Roetling, J.1    Benvenisti-Zarom, L.2    Regan, R.F.3
  • 53
    • 0034677855 scopus 로고    scopus 로고
    • Heme oxygenase-1 induction protects murine cortical astrocytes from hemoglobin toxicity
    • DOI 10.1016/S0304-3940(00)00817-X, PII S030439400000817X
    • Regan RF, Guo Y, Kumar N: Heme oxygenase-1 induction protects murine cortical astrocytes from hemoglobin toxicity. Neurosci Lett 2000, 282:1-4 (Pubitemid 30129154)
    • (2000) Neuroscience Letters , vol.282 , Issue.1-2 , pp. 1-4
    • Regan, R.F.1    Guo, Y.2    Kumar, N.3
  • 54
    • 0029868298 scopus 로고    scopus 로고
    • Heme-oxygenase-1 induction in glia throughout rat brain following experimental subarachnoid hemorrhage
    • DOI 10.1016/0006-8993(95)01511-6
    • Matz P, Turner C, Weinstein PR, Massa SM, Panter SS, Sharp FR: Heme-oxygenase-1 induction in glia throughout rat brain following experimental subarachnoid hemorrhage. Brain Res 1996, 713:211-222 (Pubitemid 26114842)
    • (1996) Brain Research , vol.713 , Issue.1-2 , pp. 211-222
    • Matz, P.1    Turner, C.2    Weinstein, P.R.3    Massa, S.M.4    Panter, S.S.5    Sharp, F.R.6
  • 56
    • 0014408353 scopus 로고
    • Exchange of heme among hemoglobins and between hemoglobin and albumin
    • Bunn HF, Jandl JH: Exchange of heme among hemoglobins and between hemoglobin and albumin. J Biol Chem 1968, 243:465-475
    • (1968) J Biol Chem , vol.243 , pp. 465-475
    • Bunn, H.F.1    Jandl, J.H.2
  • 57
    • 0031906718 scopus 로고    scopus 로고
    • Chemical, biological and clinical aspects of dexrazoxane and other bisdioxopiperazines
    • Hasinoff BB, Hellmann K, Herman EH, Ferrans VJ: Chemical, biological and clinical aspects of dexrazoxane and other bisdioxopiperazines. Curr Med Chem 1998, 5:1-28 (Pubitemid 28083490)
    • (1998) Current Medicinal Chemistry , vol.5 , Issue.1 , pp. 1-28
    • Hasinoff, B.B.1    Hellmann, K.2    Herman, E.H.3    Ferrans, V.J.4
  • 59
    • 0033866453 scopus 로고    scopus 로고
    • Monocyte infiltration is highly associated with loss of the tight junction protein zonula occludens in HIV-1-associated dementia
    • DOI 10.1046/j.1365-2990.2000.00255.x
    • Boven LA, Middel J, Verhoef J, De Groot CJ, Nottet HS: Monocyte infiltration is highly associated with loss of the tight junction protein zonula occludens in HIV-1-associated dementia. Neuropathol Appl Neurobiol 2000, 26:356-360 (Pubitemid 30609431)
    • (2000) Neuropathology and Applied Neurobiology , vol.26 , Issue.4 , pp. 356-360
    • Boven, L.A.1    Middel, J.2    Verhoef, J.3    De Groot, C.J.A.4    Nottet, H.S.L.M.5
  • 60
    • 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, Soares MP: Oxidized hemoglobin is an endogenous proinflammatory agonist that targets vascular endothelial cells. J Biol Chem 2009, 284:29582-29595
    • (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
  • 61
    • 0030734872 scopus 로고    scopus 로고
    • Heme induces the expression of adhesion molecules ICAM-1, VCAM-1, and E selectin in vascular endothelial cells
    • Wagener FA, Feldman E, de Witte T, Abraham NG: Heme induces the expression of adhesion molecules ICAM-1, VCAM-1, and E selectin in vascular endothelial cells. Proc Soc Exp Biol Med 1997, 216:456-463
    • (1997) Proc Soc Exp Biol Med , vol.216 , pp. 456-463
    • Wagener, F.A.1    Feldman, E.2    De Witte, T.3    Abraham, N.G.4
  • 62
    • 34249305881 scopus 로고    scopus 로고
    • Brain iron toxicity: Differential responses of astrocytes, neurons, and endothelial cells
    • DOI 10.1007/s11064-007-9290-4
    • Gaasch JA, Lockman PR, Geldenhuys WJ, Allen DD, Van der Schyf CJ: Brain iron toxicity: differential responses of astrocytes, neurons, and endothelial cells. Neurochem Res 2007, 32:1196-1208 (Pubitemid 46817469)
    • (2007) Neurochemical Research , vol.32 , Issue.7 , pp. 1196-1208
    • Gaasch, J.A.1    Lockman, P.R.2    Geldenhuys, W.J.3    Allen, D.D.4    Van Der, S.C.J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.