메뉴 건너뛰기




Volumn 131, Issue 5, 1998, Pages 432-441

Hepatic inflammatory responses to αα-cross-linked hemoglobin infusion in rats

Author keywords

[No Author keywords available]

Indexed keywords


EID: 0032078273     PISSN: 00222143     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-2143(98)90144-5     Document Type: Article
Times cited : (4)

References (54)
  • 1
    • 0029112589 scopus 로고
    • The development of hemoglobin solutions as red cell substitutes
    • Ogden JE, Parry ES. The development of hemoglobin solutions as red cell substitutes. Int Anesthesiol Clin 1995;33:115-29.
    • (1995) Int Anesthesiol Clin , vol.33 , pp. 115-129
    • Ogden, J.E.1    Parry, E.S.2
  • 2
    • 0026731665 scopus 로고
    • Potential clinical applications for blood substitutes
    • Winslow RM. Potential clinical applications for blood substitutes. Biomater Artif Cells Immobil Biotechnol 1992;20:205-17.
    • (1992) Biomater Artif Cells Immobil Biotechnol , vol.20 , pp. 205-217
    • Winslow, R.M.1
  • 3
    • 0028472303 scopus 로고
    • Alternatives to regular blood transfusions
    • Farley D. Alternatives to regular blood transfusions. FDA Consumer 1994;28:5-9.
    • (1994) FDA Consumer , vol.28 , pp. 5-9
    • Farley, D.1
  • 4
    • 0005597394 scopus 로고    scopus 로고
    • Blood substitutes: What is the target?
    • Winslow RM, Vandegriff KD, Intaglietta M, editors. Boston: Birkhauser
    • Joyner MJ, Faust RJ. Blood substitutes: what is the target? In: Winslow RM, Vandegriff KD, Intaglietta M, editors. Blood substitutes: new challenges. Boston: Birkhauser, 1996:15-33.
    • (1996) Blood Substitutes: New Challenges , pp. 15-33
    • Joyner, M.J.1    Faust, R.J.2
  • 5
    • 0023428522 scopus 로고
    • HbXL99 alpha: A hemoglobin derivative that is cross-linked between the alpha subunits is useful as a blood substitute
    • Snyder SR, Welty EV, Walder RY, Williams LA, Walder JA. HbXL99 alpha: a hemoglobin derivative that is cross-linked between the alpha subunits is useful as a blood substitute. Proc Natl Acad Sci U S A 1987;84:7280-4.
    • (1987) Proc Natl Acad Sci U S A , vol.84 , pp. 7280-7284
    • Snyder, S.R.1    Welty, E.V.2    Walder, R.Y.3    Williams, L.A.4    Walder, J.A.5
  • 6
    • 0026344691 scopus 로고
    • Preparation, properties, and plasma retention of human hemoglobin derivatives: Comparison of uncross-linked carboxymethylated hemoglobin with cross-linked tetrameric hemoglobin
    • Manning LR, Morgan S, Beavis RC, et al. Preparation, properties, and plasma retention of human hemoglobin derivatives: comparison of uncross-linked carboxymethylated hemoglobin with cross-linked tetrameric hemoglobin. Proc Natl Acad Sci U S A 1991;88:3329-33.
    • (1991) Proc Natl Acad Sci U S A , vol.88 , pp. 3329-3333
    • Manning, L.R.1    Morgan, S.2    Beavis, R.C.3
  • 7
    • 0027471148 scopus 로고
    • The use of hemoglobin as a blood substitute
    • Bunn HF. The use of hemoglobin as a blood substitute. Am J Hematol 1993;42:112-7.
    • (1993) Am J Hematol , vol.42 , pp. 112-117
    • Bunn, H.F.1
  • 8
    • 0028121992 scopus 로고
    • Regional circulatory and systemic hemodynamic effects of diaspirin cross-linked hemoglobin in the rat
    • Sharma AC, Rebello S, Gulati A. Regional circulatory and systemic hemodynamic effects of diaspirin cross-linked hemoglobin in the rat. Artif Cells Blood Substit Immobil Biotechnol 1994;22:593-602.
    • (1994) Artif Cells Blood Substit Immobil Biotechnol , vol.22 , pp. 593-602
    • Sharma, A.C.1    Rebello, S.2    Gulati, A.3
  • 10
    • 0030945979 scopus 로고    scopus 로고
    • Use of donor blood in the surgical setting: Potentials for application of blood substitutes
    • Greenburg AG, Kim HW. Use of donor blood in the surgical setting: potentials for application of blood substitutes. Artif Cells Blood Substit Immobil Biotechnol 1997;25:25-9.
    • (1997) Artif Cells Blood Substit Immobil Biotechnol , vol.25 , pp. 25-29
    • Greenburg, A.G.1    Kim, H.W.2
  • 11
    • 0029004672 scopus 로고
    • Review of modified hemoglobin research at Letterman: Attempts to delineate the toxicity of cell-free tetrameric hemoglobin
    • Hess JR. Review of modified hemoglobin research at Letterman: attempts to delineate the toxicity of cell-free tetrameric hemoglobin. Artif Cells Blood Substit Immobil Biotechnol 1995;23:277-89.
    • (1995) Artif Cells Blood Substit Immobil Biotechnol , vol.23 , pp. 277-289
    • Hess, J.R.1
  • 13
    • 0031056208 scopus 로고    scopus 로고
    • The toxicities of native and modified hemoglobins
    • Everse J, Hsia N. The toxicities of native and modified hemoglobins. Free Radic Biol Med 1997;22:1075-99.
    • (1997) Free Radic Biol Med , vol.22 , pp. 1075-1099
    • Everse, J.1    Hsia, N.2
  • 15
    • 0030248134 scopus 로고    scopus 로고
    • The cytotoxic activities of human hemoglobin and diaspirin cross-linked hemoglobin
    • Hsia N, Everse J. The cytotoxic activities of human hemoglobin and diaspirin cross-linked hemoglobin. Artif Cells Blood Substit Immobil Biotechnol 1996;24:533-51.
    • (1996) Artif Cells Blood Substit Immobil Biotechnol , vol.24 , pp. 533-551
    • Hsia, N.1    Everse, J.2
  • 16
    • 0026716352 scopus 로고
    • Differential regulation of heme oxygenase isozymes by Sn- and Zn-protoporphyrins: Possible relevance to suppression of hyperbilirubinemia
    • Maines MD, Trakshel GM. Differential regulation of heme oxygenase isozymes by Sn- and Zn-protoporphyrins: possible relevance to suppression of hyperbilirubinemia. Biochim Biophys Acta 1992;1131:166-74.
    • (1992) Biochim Biophys Acta , vol.1131 , pp. 166-174
    • Maines, M.D.1    Trakshel, G.M.2
  • 17
    • 0021351203 scopus 로고
    • Oxygen radicals, transition metals and disease
    • Halliwell B, Gutteridge JM. Oxygen radicals, transition metals and disease. Biochem J 1984;219:1-14.
    • (1984) Biochem J , vol.219 , pp. 1-14
    • Halliwell, B.1    Gutteridge, J.M.2
  • 18
    • 0027170781 scopus 로고
    • Catabolism of heme moiety of hemoglobin haptoglobin in rat liver cells in vivo
    • Takami M. Catabolism of heme moiety of hemoglobin haptoglobin in rat liver cells in vivo. J Biol Chem 1993;268:20335-42.
    • (1993) J Biol Chem , vol.268 , pp. 20335-20342
    • Takami, M.1
  • 19
    • 0025666366 scopus 로고
    • Nonparenchymal cells and hepatotoxicity
    • Laskin DL. Nonparenchymal cells and hepatotoxicity. Semin Liver Dis 1990;10:293-304.
    • (1990) Semin Liver Dis , vol.10 , pp. 293-304
    • Laskin, D.L.1
  • 20
    • 0023147156 scopus 로고
    • Secretory products of macrophages
    • Nathan CF. Secretory products of macrophages. J Clin Invest 1987;79:319-26.
    • (1987) J Clin Invest , vol.79 , pp. 319-326
    • Nathan, C.F.1
  • 21
    • 0025051058 scopus 로고
    • Biologically active products of stimulated liver macrophages (Kupffer cells)
    • Decker K. Biologically active products of stimulated liver macrophages (Kupffer cells). Eur J Biochem 1990;192:245-61.
    • (1990) Eur J Biochem , vol.192 , pp. 245-261
    • Decker, K.1
  • 22
    • 0029204907 scopus 로고
    • Activation of Kupffer cells and neutrophils for reactive oxygen formation is responsible for endotoxin-enhanced liver injury after hepatic ischemia
    • Liu P, McGuire GM, Fisher MA, Farhood A, Smith CW, Jaeschke H. Activation of Kupffer cells and neutrophils for reactive oxygen formation is responsible for endotoxin-enhanced liver injury after hepatic ischemia. Shock 1995;3:56-62.
    • (1995) Shock , vol.3 , pp. 56-62
    • Liu, P.1    McGuire, G.M.2    Ma, F.3    Farhood, A.4    Smith, C.W.5    Jaeschke, H.6
  • 23
    • 0025819677 scopus 로고
    • Exposure of endothelial cells to free heme potentiates damage mediated by granulocytes and toxic oxygen species
    • Balla G, Vercellotti GM, Muller-Eberhard U, Eaton J, Jacob HS. Exposure of endothelial cells to free heme potentiates damage mediated by granulocytes and toxic oxygen species. Lab Invest 1991;64:648-55.
    • (1991) Lab Invest , vol.64 , pp. 648-655
    • Balla, G.1    Vercellotti, G.M.2    Muller-Eberhard, U.3    Eaton, J.4    Jacob, H.S.5
  • 24
    • 0029051189 scopus 로고
    • Mechanisms of oxidant stress-induced acute tissue injury
    • Jaeschke H. Mechanisms of oxidant stress-induced acute tissue injury. Proc Soc Exp Biol Med 1995;209:104-11.
    • (1995) Proc Soc Exp Biol Med , vol.209 , pp. 104-111
    • Jaeschke, H.1
  • 25
    • 0028347865 scopus 로고
    • Macrophage activation revisted
    • Celada A, Nathan CF. Macrophage activation revisted. Immunol Today 1994;15:100-2.
    • (1994) Immunol Today , vol.15 , pp. 100-102
    • Celada, A.1    Nathan, C.F.2
  • 26
    • 0025687478 scopus 로고
    • Neutrophils contribute to ischemia/reperfusion injury in rat liver in vivo
    • Jaeschke H, Farhood A, Smith CW. Neutrophils contribute to ischemia/reperfusion injury in rat liver in vivo. FASEB J 1990;4:3355-9.
    • (1990) FASEB J , vol.4 , pp. 3355-3359
    • Jaeschke, H.1    Farhood, A.2    Smith, C.W.3
  • 27
    • 0000076470 scopus 로고
    • Esterase activity in leukocytes demonstrated by the use of naphthol AS-D chloroacetate substrate
    • Maloney WC, McPherson K, Fliegelman L. Esterase activity in leukocytes demonstrated by the use of naphthol AS-D chloroacetate substrate. J Histochem Cytochem 1960;8:200-7.
    • (1960) J Histochem Cytochem , vol.8 , pp. 200-207
    • Maloney, W.C.1    McPherson, K.2    Fliegelman, L.3
  • 28
    • 0022632224 scopus 로고
    • Characterization of two constitutive forms of rat liver microsomal heme oxygenase
    • Maines MD, Trakshel GM, Kutty RK. Characterization of two constitutive forms of rat liver microsomal heme oxygenase. J Biol Chem 1986;261:411-9.
    • (1986) J Biol Chem , vol.261 , pp. 411-419
    • Maines, M.D.1    Trakshel, G.M.2    Kutty, R.K.3
  • 30
    • 0022474482 scopus 로고
    • The role of mitochondrial glutathione and cellular protein sulfhydryls in formaldehyde toxicity in glutathione depleted rat hepatocytes
    • Ku RH, Billings RE. The role of mitochondrial glutathione and cellular protein sulfhydryls in formaldehyde toxicity in glutathione depleted rat hepatocytes. Arch Biochem Biophys 1986;247:183-9.
    • (1986) Arch Biochem Biophys , vol.247 , pp. 183-189
    • Ku, R.H.1    Billings, R.E.2
  • 31
    • 0019887888 scopus 로고
    • Purification and characterization of biliverdin reductase from rat liver
    • Kutty RK, Maines MD. Purification and characterization of biliverdin reductase from rat liver. J Biol Chem 1981;-256:3956-62.
    • (1981) J Biol Chem , vol.256 , pp. 3956-3962
    • Kutty, R.K.1    Maines, M.D.2
  • 33
    • 0016838104 scopus 로고
    • Cobalt stimulation of heme degradation in the liver
    • Maines MD, Kappas A. Cobalt stimulation of heme degradation in the liver. J Biol Chem 1975;250:4171-7.
    • (1975) J Biol Chem , vol.250 , pp. 4171-4177
    • Maines, M.D.1    Kappas, A.2
  • 34
    • 0025647389 scopus 로고
    • Laboratory methods: A simplified method for the preparation of transcriptionally active liver nuclear extracts
    • Hattori M, Tugores A, Veloz L, Karin M, Brenner DA. Laboratory methods: a simplified method for the preparation of transcriptionally active liver nuclear extracts. DNA Cell Biol 1990;9:777-81.
    • (1990) DNA Cell Biol , vol.9 , pp. 777-781
    • Hattori, M.1    Tugores, A.2    Veloz, L.3    Karin, M.4    Brenner, D.A.5
  • 35
    • 0029789321 scopus 로고    scopus 로고
    • Characterization of hepatic nitric oxide synthase: Identification as the cytokine-inducible form primarily regulated by oxidants
    • Duval DL, Miller DR, Collier J, Billings RE. Characterization of hepatic nitric oxide synthase: identification as the cytokine-inducible form primarily regulated by oxidants. Mol Pharmacol 1996;50:1-8.
    • (1996) Mol Pharmacol , vol.50 , pp. 1-8
    • Duval, D.L.1    Miller, D.R.2    Collier, J.3    Billings, R.E.4
  • 36
    • 0022186670 scopus 로고
    • Measurement of protein using bicinchoninic acid
    • Smith PK, Krohn RI, Hermanson GT, et al. Measurement of protein using bicinchoninic acid. Anal Biochem 1985;-150:76-85.
    • (1985) Anal Biochem , vol.150 , pp. 76-85
    • Smith, P.K.1    Krohn, R.I.2    Hermanson, G.T.3
  • 37
    • 0024362683 scopus 로고
    • Generation and characterization of hamster monoclonal antibodies that neutralize murine tumor necrosis factors
    • Sheehan KCF, Ruddle NH, Schreiber RD. Generation and characterization of hamster monoclonal antibodies that neutralize murine tumor necrosis factors. J Immunol 1989;-142:3884-93.
    • (1989) J Immunol , vol.142 , pp. 3884-3893
    • Sheehan, K.C.F.1    Ruddle, N.H.2    Schreiber, R.D.3
  • 41
    • 0027944068 scopus 로고
    • Hemoglobin stimulates mononuclear leukocytes to release interleukin-8 and tumor necrosis factor α
    • McFaul SJ, Bowman PD, Villa VM, Gutierrez-Ibanez MJ, Johnson M, Smith D. Hemoglobin stimulates mononuclear leukocytes to release interleukin-8 and tumor necrosis factor α. Blood 1994;9:3175-81.
    • (1994) Blood , vol.9 , pp. 3175-3181
    • McFaul, S.J.1    Bowman, P.D.2    Villa, V.M.3    Gutierrez-Ibanez, M.J.4    Johnson, M.5    Smith, D.6
  • 42
    • 0023982676 scopus 로고
    • The role of tumor necrosis factor and interleukin 1 in the immunoinflammatory response
    • Larrick JW, Kunkel SL. The role of tumor necrosis factor and interleukin 1 in the immunoinflammatory response. Pharm Res 1988;5:129-39.
    • (1988) Pharm Res , vol.5 , pp. 129-139
    • Larrick, J.W.1    Kunkel, S.L.2
  • 43
    • 0000784043 scopus 로고
    • The physiology of the NF-κB transcription factor
    • Cohen P, Foulkes JG, editors. Amsterdam: Biomedical Press Elsevier
    • Baeuerle PA, Baltimore D. The physiology of the NF-κB transcription factor. In: Cohen P, Foulkes JG, editors. Hormonal control regulation of gene expression. Amsterdam: Biomedical Press Elsevier, 1991:409-32.
    • (1991) Hormonal Control Regulation of Gene Expression , pp. 409-432
    • Baeuerle, P.A.1    Baltimore, D.2
  • 44
    • 0028946614 scopus 로고
    • Transcriptional inhibition of the inducible nitric oxide synthase gene by competitive binding of NF-κB /Rel protein
    • Goldring C, Narayana R, Lagadec P, Jeannin J. Transcriptional inhibition of the inducible nitric oxide synthase gene by competitive binding of NF-κB /Rel protein. Biochem Biophys Res Commun 1995;209:73-9.
    • (1995) Biochem Biophys Res Commun , vol.209 , pp. 73-79
    • Goldring, C.1    Narayana, R.2    Lagadec, P.3    Jeannin, J.4
  • 45
    • 0025739254 scopus 로고
    • Reactive oxygen intermediates as apparently widely used messengers in the activation of the NF-κB transcription and HIV-1
    • Schreck R, Rieber P, Baeuerle PA. Reactive oxygen intermediates as apparently widely used messengers in the activation of the NF-κB transcription and HIV-1. EMBO J 1991;10:2247-58.
    • (1991) EMBO J , vol.10 , pp. 2247-2258
    • Schreck, R.1    Rieber, P.2    Baeuerle, P.A.3
  • 46
    • 0027974133 scopus 로고
    • Assessing oxygen radicals as mediators in activation of inducible eukaryotic transcription factor NF-κB
    • Schreck R, Baeuerle PA. Assessing oxygen radicals as mediators in activation of inducible eukaryotic transcription factor NF-κB. Methods Enzymol 1994;234:151-63.
    • (1994) Methods Enzymol , vol.234 , pp. 151-163
    • Schreck, R.1    Baeuerle, P.A.2
  • 47
    • 0025201693 scopus 로고
    • Cytotoxic mechanism of tumor necrosis factor-α
    • Larrick JW, Wright SC. Cytotoxic mechanism of tumor necrosis factor-α. FASEB J 1990;4:3215-23.
    • (1990) FASEB J , vol.4 , pp. 3215-3223
    • Larrick, J.W.1    Wright, S.C.2
  • 48
    • 0028925023 scopus 로고
    • Regulation of hepatic nitric oxide synthase by reactive oxygen intermediates and glutathione
    • Duval DL, Sieg DJ, Billings RE. Regulation of hepatic nitric oxide synthase by reactive oxygen intermediates and glutathione. Arch Biochem Biophys 1994;316:699-706.
    • (1994) Arch Biochem Biophys , vol.316 , pp. 699-706
    • Duval, D.L.1    Sieg, D.J.2    Billings, R.E.3
  • 49
    • 0026657174 scopus 로고
    • Ferritin: A cytoprotective antioxidant stratagem of endothelium
    • Balla G, Jacob HS, Balla J, et al. Ferritin: a cytoprotective antioxidant stratagem of endothelium. J Biol Chem 1992;267:18148-53.
    • (1992) J Biol Chem , vol.267 , pp. 18148-18153
    • Balla, G.1    Jacob, H.S.2    Balla, J.3
  • 50
    • 0020479017 scopus 로고
    • Metal ion-mediated regulation of heme oxygenase induction in cultured avian liver cells
    • Sardana MK, Sassa S, Kappas A. Metal ion-mediated regulation of heme oxygenase induction in cultured avian liver cells. J Biol Chem 1982;257:4806-11.
    • (1982) J Biol Chem , vol.257 , pp. 4806-4811
    • Sardana, M.K.1    Sassa, S.2    Kappas, A.3
  • 51
    • 0026033907 scopus 로고
    • Induction of heme oxygenase: A general response to oxidant stress in cultured mammalian cells
    • Applegate LA, Luscher P, Tyrrell RM. Induction of heme oxygenase: a general response to oxidant stress in cultured mammalian cells. Cancer Res 1991;51:974-8.
    • (1991) Cancer Res , vol.51 , pp. 974-978
    • Applegate, L.A.1    Luscher, P.2    Tyrrell, R.M.3
  • 53
    • 0025368527 scopus 로고
    • Induction of haem oxygenase as a defence against oxidative stress
    • Stocker R. Induction of haem oxygenase as a defence against oxidative stress. Free Radic Res Commun 1990;9:101-12.
    • (1990) Free Radic Res Commun , vol.9 , pp. 101-112
    • Stocker, R.1
  • 54
    • 0029410648 scopus 로고
    • Hemoglobin provides protection against lethal endotoxemia in rats: The role of heme oxygenase-1
    • Otterbein L, Sylvester SL, Choi AMK. Hemoglobin provides protection against lethal endotoxemia in rats: the role of heme oxygenase-1. Am J Respir Cell Mol Biol 1995;13:595-601.
    • (1995) Am J Respir Cell Mol Biol , vol.13 , pp. 595-601
    • Otterbein, L.1    Sylvester, S.L.2    Choi, A.M.K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.