메뉴 건너뛰기




Volumn 77, Issue 8, 1999, Pages 577-592

Therapeutic approaches for ischemia/reperfusion injury in the liver

Author keywords

AP 1; Gene therapy; Ischemia Reperfusion; Liver; NF B; Reactive oxygen species; Signal transduction; Superoxide dismutase

Indexed keywords

CATALASE; GAMMA INTERFERON; GRANULOCYTE MACROPHAGE COLONY STIMULATING FACTOR; HEAT SHOCK PROTEIN; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; LYMPHOTOXIN; NITRIC OXIDE; SUPEROXIDE DISMUTASE; TRANSCRIPTION FACTOR; XANTHINE OXIDASE;

EID: 0032881237     PISSN: 09462716     EISSN: None     Source Type: Journal    
DOI: 10.1007/s001099900029     Document Type: Review
Times cited : (208)

References (162)
  • 1
    • 0032429362 scopus 로고    scopus 로고
    • Ischemia reperfusion injury and chronic allograft rejection
    • 1. Szabo A, Heemann U (1998) Ischemia reperfusion injury and chronic allograft rejection. Transplant Proc 30:4281-4284
    • (1998) Transplant Proc , vol.30 , pp. 4281-4284
    • Szabo, A.1    Heemann, U.2
  • 2
    • 0031664426 scopus 로고    scopus 로고
    • Ischemia and reperfusion injury. The ultimate pathophysiologic paradox
    • 2. Hammerman C, Kaplan M (1998) Ischemia and reperfusion injury. The ultimate pathophysiologic paradox. Clin Perinatol 25:757-777
    • (1998) Clin Perinatol , vol.25 , pp. 757-777
    • Hammerman, C.1    Kaplan, M.2
  • 4
    • 0029295095 scopus 로고
    • Auxiliary liver transplantation for acute liver failure
    • 4. Shaw BW Jr (1995) Auxiliary liver transplantation for acute liver failure. Liver Transplant Surg 1:194-200
    • (1995) Liver Transplant Surg , vol.1 , pp. 194-200
    • Shaw B.W., Jr.1
  • 6
    • 0026310875 scopus 로고
    • Superoxide generation by Kupffer cells and priming of neutrophils during reperfusion after hepatic ischemia
    • 6. Jacschke H, Bautista AP, Spolarics Z, Spitzer JJ (1991) Superoxide generation by Kupffer cells and priming of neutrophils during reperfusion after hepatic ischemia. Free Radic Res Commun 15:277-284
    • (1991) Free Radic Res Commun , vol.15 , pp. 277-284
    • Jacschke, H.1    Bautista, A.P.2    Spolarics, Z.3    Spitzer, J.J.4
  • 7
    • 0026518746 scopus 로고
    • Contribution of no-reflow phenomenon to hepatic injury after ischemia-reperfusion: Evidence for a role for superoxide anion
    • 7. Koo A, Komatsu H, Tao G, Inoue M, Guth PH, Kaplowitz N (1992) Contribution of no-reflow phenomenon to hepatic injury after ischemia-reperfusion: evidence for a role for superoxide anion. Hepatology 15:507-514
    • (1992) Hepatology , vol.15 , pp. 507-514
    • Koo, A.1    Komatsu, H.2    Tao, G.3    Inoue, M.4    Guth, P.H.5    Kaplowitz, N.6
  • 8
    • 0028128730 scopus 로고
    • The potential role of reactive oxygen species in liver ischemia/reperfusion injury following liver surgery
    • 8. Rauen U, Viebahn R, Lauchart W, de Groot H (1994) The potential role of reactive oxygen species in liver ischemia/reperfusion injury following liver surgery. Hepatogastroenterology 41:333-336
    • (1994) Hepatogastroenterology , vol.41 , pp. 333-336
    • Rauen, U.1    Viebahn, R.2    Lauchart, W.3    De Groot, H.4
  • 9
    • 0023758565 scopus 로고
    • Ischemia-reperfusion injury: A radical view
    • 9. Parks DA, Granger DN (1988) Ischemia-reperfusion injury: a radical view. Hepatology 8:680-682
    • (1988) Hepatology , vol.8 , pp. 680-682
    • Parks, D.A.1    Granger, D.N.2
  • 12
    • 0030220572 scopus 로고    scopus 로고
    • Mechanisms of inflammatory liver injury: Adhesion molecules and cytotoxicity of neutrophils
    • 12. Jaeschke H, Smith CW, Clemens MG, Ganey PE, Roth RA (1996) Mechanisms of inflammatory liver injury: adhesion molecules and cytotoxicity of neutrophils. Toxicol Appl Pharmacol 139:213-226
    • (1996) Toxicol Appl Pharmacol , vol.139 , pp. 213-226
    • Jaeschke, H.1    Smith, C.W.2    Clemens, M.G.3    Ganey, P.E.4    Roth, R.A.5
  • 14
    • 0026163812 scopus 로고
    • Hypoxia increases production of interleukin-1 and tumor necrosis factor by human mononuclear cells
    • 14. Ghezzi P, Dinarello CA, Bianchi M, Rosandich ME, Repine JE, White CW (1991) Hypoxia increases production of interleukin-1 and tumor necrosis factor by human mononuclear cells. Cytokine 3:189-194
    • (1991) Cytokine , vol.3 , pp. 189-194
    • Ghezzi, P.1    Dinarello, C.A.2    Bianchi, M.3    Rosandich, M.E.4    Repine, J.E.5    White, C.W.6
  • 15
    • 0026470632 scopus 로고
    • Inflammation and platelet-activating factor production during hepatic ischemia/reperfusion
    • 15. Zhou W, McCollum MO, Levine BA, Olson MS (1992) Inflammation and platelet-activating factor production during hepatic ischemia/reperfusion. Hepatology 16:1236-1240
    • (1992) Hepatology , vol.16 , pp. 1236-1240
    • Zhou, W.1    McCollum, M.O.2    Levine, B.A.3    Olson, M.S.4
  • 17
    • 0025756580 scopus 로고
    • Neutrophil and Kupffer cell-induced oxidant stress and ischemia-reperfusion injury in rat liver
    • 17. Jaeschke H, Farhood A (1991) Neutrophil and Kupffer cell-induced oxidant stress and ischemia-reperfusion injury in rat liver. Am J Physiol 260:G355-G362
    • (1991) Am J Physiol , vol.260
    • Jaeschke, H.1    Farhood, A.2
  • 18
    • 0029204907 scopus 로고
    • Activation of Kupffer cells and neutrophils for reactive oxygen formation is responsible for endotoxin-enhanced liver injury after hepatic ischemia
    • 18. Liu P, McGuire GM, Fisher MA, Farhood A, Smith CW, Jaeschke H (1995) Activation of Kupffer cells and neutrophils for reactive oxygen formation is responsible for endotoxin-enhanced liver injury after hepatic ischemia. Shock 3:56-62
    • (1995) Shock , vol.3 , pp. 56-62
    • Liu, P.1    McGuire, G.M.2    Fisher, M.A.3    Farhood, A.4    Smith, C.W.5    Jaeschke, H.6
  • 19
    • 0028527530 scopus 로고
    • Glycolysis and energy metabolism in rat liver during warm and cold ischemia: Evidence of an activation of the regulatory enzyme phosphofructokinase
    • 19. Churchill TA, Cheetham KM, Fuller BJ (1994) Glycolysis and energy metabolism in rat liver during warm and cold ischemia: evidence of an activation of the regulatory enzyme phosphofructokinase. Cryobiology 31:441-452
    • (1994) Cryobiology , vol.31 , pp. 441-452
    • Churchill, T.A.1    Cheetham, K.M.2    Fuller, B.J.3
  • 20
    • 0024369853 scopus 로고
    • Effects of warm and cold ischemia on mitochondrial functions in brain, liver and kidney
    • 20. Baumann M, Bender E, Stommer G, Gross G, Brand K (1989) Effects of warm and cold ischemia on mitochondrial functions in brain, liver and kidney. Mol Cell Biochem 87:137-145
    • (1989) Mol Cell Biochem , vol.87 , pp. 137-145
    • Baumann, M.1    Bender, E.2    Stommer, G.3    Gross, G.4    Brand, K.5
  • 21
    • 0028130441 scopus 로고
    • Oxidative stress in hepatocytes and stimulatory state of Kupffer cells after reperfusion differ between warm and cold ischemia in rats
    • 21. Mochida S, Arai M, Ohno A, Masaki N, Ogata I, Fujiwara K (1994) Oxidative stress in hepatocytes and stimulatory state of Kupffer cells after reperfusion differ between warm and cold ischemia in rats. Liver 14:234-240
    • (1994) Liver , vol.14 , pp. 234-240
    • Mochida, S.1    Arai, M.2    Ohno, A.3    Masaki, N.4    Ogata, I.5    Fujiwara, K.6
  • 22
    • 0026748407 scopus 로고
    • Ischemic injury in liver transplantation: Difference in injury sites between warm and cold ischemia in rats
    • 22. Ikeda T, Yanaga K, Kishikawa K, Kakizoe S, Shimada M, Sugimachi K (1992) Ischemic injury in liver transplantation: difference in injury sites between warm and cold ischemia in rats. Hepatology 16:454-461
    • (1992) Hepatology , vol.16 , pp. 454-461
    • Ikeda, T.1    Yanaga, K.2    Kishikawa, K.3    Kakizoe, S.4    Shimada, M.5    Sugimachi, K.6
  • 23
    • 0018880938 scopus 로고
    • Plasma hypoxanthine concentrations in pigs. A prognostic aid in hypoxia
    • 23. Saugstad OD, Aasen AO (1980) Plasma hypoxanthine concentrations in pigs. A prognostic aid in hypoxia. Eur Surg Res 12:123-129
    • (1980) Eur Surg Res , vol.12 , pp. 123-129
    • Saugstad, O.D.1    Aasen, A.O.2
  • 24
    • 0030002692 scopus 로고    scopus 로고
    • Role of xanthine oxidase and its inhibitor in hypoxia: Reoxygenation injury
    • 24. Saugstad OD (1996) Role of xanthine oxidase and its inhibitor in hypoxia: reoxygenation injury. Pediatrics 98:103-107
    • (1996) Pediatrics , vol.98 , pp. 103-107
    • Saugstad, O.D.1
  • 25
    • 0030716904 scopus 로고    scopus 로고
    • The oxidative half-reaction of xanthine dehydrogenase with NAD; reaction kinetics and steady-state mechanism
    • 25. Harris CM, Massey V (1997) The oxidative half-reaction of xanthine dehydrogenase with NAD; reaction kinetics and steady-state mechanism. J Biol Chem 272:28335-28341
    • (1997) J Biol Chem , vol.272 , pp. 28335-28341
    • Harris, C.M.1    Massey, V.2
  • 26
    • 0014690734 scopus 로고
    • The regulation of rat liver xanthine oxidase. Conversion in vitro of the enzyme activity from dehydrogenase (type D) to oxidase (type O)
    • 26. Stirpe F, Della Corte E (1969) The regulation of rat liver xanthine oxidase. Conversion in vitro of the enzyme activity from dehydrogenase (type D) to oxidase (type O). J Biol Chem 244:3855-3863
    • (1969) J Biol Chem , vol.244 , pp. 3855-3863
    • Stirpe, F.1    Della Corte, E.2
  • 27
    • 0023910116 scopus 로고
    • Hypoxanthine as an indicator of hypoxia: Its role in health and disease through free radical production
    • 27. Saugstad OD (1988) Hypoxanthine as an indicator of hypoxia: its role in health and disease through free radical production. Pediatr Res 23:143-150
    • (1988) Pediatr Res , vol.23 , pp. 143-150
    • Saugstad, O.D.1
  • 28
    • 0021141108 scopus 로고
    • Hypoxanthine and oxygen induced lung injury: A possible basic mechanism of tissue damage?
    • 28. Saugstad OD, Hallman M, Abraham JL, Epstein B, Cochrane C, Gluck L (1984) Hypoxanthine and oxygen induced lung injury: a possible basic mechanism of tissue damage? Pediatr Res 18:501-504
    • (1984) Pediatr Res , vol.18 , pp. 501-504
    • Saugstad, O.D.1    Hallman, M.2    Abraham, J.L.3    Epstein, B.4    Cochrane, C.5    Gluck, L.6
  • 30
    • 0030997261 scopus 로고    scopus 로고
    • Activation of CPP32-like protease in tumor necrosis factor-induced apoptosis is dependent on mitochondrial function
    • 30. Higuchi M, Aggarwal BB, Yeh ET (1997) Activation of CPP32-like protease in tumor necrosis factor-induced apoptosis is dependent on mitochondrial function. J Clin Invest 99:1751-1758
    • (1997) J Clin Invest , vol.99 , pp. 1751-1758
    • Higuchi, M.1    Aggarwal, B.B.2    Yeh, E.T.3
  • 31
    • 1842375100 scopus 로고    scopus 로고
    • Implication of mitochondrial hydrogen peroxide generation in ceramide-induced apoptosis
    • 31. Quillet-Mary A, Jaffrezou JP, Mansat V, Bordier C, Naval J, Laurent G (1997) Implication of mitochondrial hydrogen peroxide generation in ceramide-induced apoptosis. J Biol Chem 272:21388-21395
    • (1997) J Biol Chem , vol.272 , pp. 21388-21395
    • Quillet-Mary, A.1    Jaffrezou, J.P.2    Mansat, V.3    Bordier, C.4    Naval, J.5    Laurent, G.6
  • 32
    • 0030477745 scopus 로고    scopus 로고
    • Mammalian peroxisomes: Metabolism of oxygen and reactive oxygen species
    • 32. Singh T (1996) Mammalian peroxisomes: metabolism of oxygen and reactive oxygen species. Ann N Y Acad Sci 804:612-627
    • (1996) Ann N Y Acad Sci , vol.804 , pp. 612-627
    • Singh, T.1
  • 33
    • 0031049745 scopus 로고    scopus 로고
    • The cytochrome P450 4 (CYP4) family
    • 33. Simpson AE (1997) The cytochrome P450 4 (CYP4) family. Gen Pharmacol 28:351-359
    • (1997) Gen Pharmacol , vol.28 , pp. 351-359
    • Simpson, A.E.1
  • 34
    • 0026502540 scopus 로고
    • Identification of superoxide dismutase in rat liver peroxisomes
    • 34. Wanders RJ, Denis S (1992) Identification of superoxide dismutase in rat liver peroxisomes. Biochim Biophys Acta 1115:259-262
    • (1992) Biochim Biophys Acta , vol.1115 , pp. 259-262
    • Wanders, R.J.1    Denis, S.2
  • 35
    • 0030881997 scopus 로고    scopus 로고
    • Cytochrome P450 2E1 in rat liver peroxisomes: Downregulation by ischemia/reperfusion-induced oxidative stress
    • 35. Pahan K, Smith BT, Singh AK, Singh I (1997) Cytochrome P450 2E1 in rat liver peroxisomes: downregulation by ischemia/reperfusion-induced oxidative stress. Free Radic Biol Med 23:963-971
    • (1997) Free Radic Biol Med , vol.23 , pp. 963-971
    • Pahan, K.1    Smith, B.T.2    Singh, A.K.3    Singh, I.4
  • 36
    • 0026335622 scopus 로고
    • Regulation of phagocyte oxygen radical production by the GTP-binding protein Rac 2
    • 36. Knaus UG, Heyworth PG, Evans T, Curnutte JT, Bokoch GM (1991) Regulation of phagocyte oxygen radical production by the GTP-binding protein Rac 2. Science 254:1512-1515
    • (1991) Science , vol.254 , pp. 1512-1515
    • Knaus, U.G.1    Heyworth, P.G.2    Evans, T.3    Curnutte, J.T.4    Bokoch, G.M.5
  • 37
    • 0023268486 scopus 로고
    • Free radicals and myocardial ischemia and reperfusion injury
    • 37. Simpson PJ, Lucchesi BR (1987) Free radicals and myocardial ischemia and reperfusion injury. J Lab Clin Med 110:13-30
    • (1987) J Lab Clin Med , vol.110 , pp. 13-30
    • Simpson, P.J.1    Lucchesi, B.R.2
  • 38
    • 0029173888 scopus 로고
    • Toxicity of oxygen from naturally occurring redox-active pro-oxidants
    • 38. Pardini RS (1995) Toxicity of oxygen from naturally occurring redox-active pro-oxidants. Arch Insect Biochem Physiol 29:101-118
    • (1995) Arch Insect Biochem Physiol , vol.29 , pp. 101-118
    • Pardini, R.S.1
  • 39
    • 0030452899 scopus 로고    scopus 로고
    • Mechanisms of liver damage
    • 39. Losser MR, Payen D (1996) Mechanisms of liver damage. Semin Liver Dis 16:357-367
    • (1996) Semin Liver Dis , vol.16 , pp. 357-367
    • Losser, M.R.1    Payen, D.2
  • 40
    • 0029929112 scopus 로고    scopus 로고
    • Mechanism and prevention of ischemia-reperfusion injury of the liver
    • 40. Kurokawa T, Nonami T, Harada A, Nakao A, Takagi H (1996) Mechanism and prevention of ischemia-reperfusion injury of the liver. Semin Surg Oncol 12:179-182
    • (1996) Semin Surg Oncol , vol.12 , pp. 179-182
    • Kurokawa, T.1    Nonami, T.2    Harada, A.3    Nakao, A.4    Takagi, H.5
  • 41
    • 0025745032 scopus 로고
    • Reactive oxygen and ischemia/reperfusion injury of the liver
    • 41. Jaeschke H (1991) Reactive oxygen and ischemia/reperfusion injury of the liver. Chem Biol Interact 79:115-136
    • (1991) Chem Biol Interact , vol.79 , pp. 115-136
    • Jaeschke, H.1
  • 42
    • 0031032046 scopus 로고    scopus 로고
    • Interleukin 1 receptor blockade reduces tumor necrosis factor production, tissue injury, and mortality after hepatic ischemia-reperfusion in the rat
    • 42. Shito M, Wakabayashi G, Ueda M, Shimazu M, Shirasugi N, Endo M, Mukai M, Kitajimu M (1997) Interleukin 1 receptor blockade reduces tumor necrosis factor production, tissue injury, and mortality after hepatic ischemia-reperfusion in the rat. Transplantation 63:143-148
    • (1997) Transplantation , vol.63 , pp. 143-148
    • Shito, M.1    Wakabayashi, G.2    Ueda, M.3    Shimazu, M.4    Shirasugi, N.5    Endo, M.6    Mukai, M.7    Kitajimu, M.8
  • 43
    • 0032162130 scopus 로고    scopus 로고
    • Tumor necrosis factor up-regulates intercellular adhesion molecule 1, which is important in the neutrophil-dependent lung and liver injury associated with hepatic ischemia and reperfusion in the rat
    • 43. Colletti LM, Cortis A, Lukacs N, Kunkel SL, Green M, Strieter RM (1998) Tumor necrosis factor up-regulates intercellular adhesion molecule 1, which is important in the neutrophil-dependent lung and liver injury associated with hepatic ischemia and reperfusion in the rat. Shock 10:182-191
    • (1998) Shock , vol.10 , pp. 182-191
    • Colletti, L.M.1    Cortis, A.2    Lukacs, N.3    Kunkel, S.L.4    Green, M.5    Strieter, R.M.6
  • 46
    • 0029894286 scopus 로고    scopus 로고
    • Involvement of platelet-activating factor in cytokine production and neutrophil activation after hepatic ischemia-reperfusion
    • 46. Serizawa A, Nakamura S, Suzuki, Baba S, Nakano M (1996) Involvement of platelet-activating factor in cytokine production and neutrophil activation after hepatic ischemia-reperfusion. Hepatology 23:1656-1663
    • (1996) Hepatology , vol.23 , pp. 1656-1663
    • Serizawa, A.1    Nakamura, S.2    Suzuki3    Baba, S.4    Nakano, M.5
  • 47
    • 0029096916 scopus 로고
    • Activation of dual T cell signaling pathways by the chemokine RANTES
    • 47. Bacon KB, Premack BA, Gardner P, Schall TJ (1995) Activation of dual T cell signaling pathways by the chemokine RANTES. Science 269:1727-1730
    • (1995) Science , vol.269 , pp. 1727-1730
    • Bacon, K.B.1    Premack, B.A.2    Gardner, P.3    Schall, T.J.4
  • 48
    • 0030905186 scopus 로고    scopus 로고
    • Biochemistry and autoimmune response to the 2-oxoacid dehydrogenase complexes in primary biliary cirrhosis
    • 48. Bassendine MF, Jones DE, Yeaman SJ (1997) Biochemistry and autoimmune response to the 2-oxoacid dehydrogenase complexes in primary biliary cirrhosis. Semin Liver Dis 17:49-60
    • (1997) Semin Liver Dis , vol.17 , pp. 49-60
    • Bassendine, M.F.1    Jones, D.E.2    Yeaman, S.J.3
  • 49
    • 0028034751 scopus 로고
    • Nitric oxide attenuates leukocyte-endothelial interaction via P-selectin in splanchnic ischemia-reperfusion
    • 49. Gauthier TW, Davenpeck KL, Lefer AM (1994) Nitric oxide attenuates leukocyte-endothelial interaction via P-selectin in splanchnic ischemia-reperfusion. Am J Physiol 267:G562-G568
    • (1994) Am J Physiol , vol.267
    • Gauthier, T.W.1    Davenpeck, K.L.2    Lefer, A.M.3
  • 50
    • 17644445227 scopus 로고    scopus 로고
    • CD18/ICAM-1-dependent oxidative NF-kappaB activation leading to nitric oxide production in rat Kupffer cells cocultured with syngeneic hepatoma cells
    • 50. Kurose I, Saito H, Miura S, Ebinuma H, Higuchi H, Watanabe N, Zeki S, Nakamura T, Takaishi M, Ishii H (1997) CD18/ICAM-1-dependent oxidative NF-kappaB activation leading to nitric oxide production in rat Kupffer cells cocultured with syngeneic hepatoma cells. J Clin Invest 99:867-878
    • (1997) J Clin Invest , vol.99 , pp. 867-878
    • Kurose, I.1    Saito, H.2    Miura, S.3    Ebinuma, H.4    Higuchi, H.5    Watanabe, N.6    Zeki, S.7    Nakamura, T.8    Takaishi, M.9    Ishii, H.10
  • 51
    • 0031911630 scopus 로고    scopus 로고
    • Inhibition of nitric oxide synthase attenuates peroxynitrite generation, but augments neutrophil accumulation in hepatic ischemia-reperfusion in rats
    • 51. Liu P, Yin K, Nagele R, Wong PY (1998) Inhibition of nitric oxide synthase attenuates peroxynitrite generation, but augments neutrophil accumulation in hepatic ischemia-reperfusion in rats. J Pharmacol Exp Ther 284:1139-1146
    • (1998) J Pharmacol Exp Ther , vol.284 , pp. 1139-1146
    • Liu, P.1    Yin, K.2    Nagele, R.3    Wong, P.Y.4
  • 52
    • 0025189864 scopus 로고
    • Apparent hydroxyl radical production by peroxynitrite: Implications for endothelial injury from nitric oxide and superoxide
    • 52. Beckman JS, Beckman TW, Chen J, Marshall PA, Freeman BA (1990) Apparent hydroxyl radical production by peroxynitrite: implications for endothelial injury from nitric oxide and superoxide. Proc Natl Acad Sci U S A 87:1620-1624
    • (1990) Proc Natl Acad Sci U S A , vol.87 , pp. 1620-1624
    • Beckman, J.S.1    Beckman, T.W.2    Chen, J.3    Marshall, P.A.4    Freeman, B.A.5
  • 53
    • 0030203367 scopus 로고    scopus 로고
    • The pathophysiological role of peroxynitrite in shock, inflammation, and ischemia-reperfusion injury
    • 53. Szabo C (1996) The pathophysiological role of peroxynitrite in shock, inflammation, and ischemia-reperfusion injury. Shock 6:79-88
    • (1996) Shock , vol.6 , pp. 79-88
    • Szabo, C.1
  • 54
    • 0027325255 scopus 로고
    • Nitric oxide synthase structure and mechanism
    • 54. Marletta MA (1993) Nitric oxide synthase structure and mechanism. J Biol Chem 268:12231-12234
    • (1993) J Biol Chem , vol.268 , pp. 12231-12234
    • Marletta, M.A.1
  • 56
    • 0030668380 scopus 로고    scopus 로고
    • Reactive oxygen species and antioxidants in signal transduction and gene expression
    • 56. Palmer HJ, Paulson KE (1997) Reactive oxygen species and antioxidants in signal transduction and gene expression. Nutr Rev 55:353-361
    • (1997) Nutr Rev , vol.55 , pp. 353-361
    • Palmer, H.J.1    Paulson, K.E.2
  • 58
    • 0025739254 scopus 로고
    • Reactive oxygen intermediates as apparently widely used messengers in the activation of the NF-kappa B transcription factor and HIV-1
    • 58. Schreck R, Rieber P, Baeuerle PA (1991) Reactive oxygen intermediates as apparently widely used messengers in the activation of the NF-kappa B transcription factor and HIV-1. EMBO J 10:2247-2258
    • (1991) EMBO J , vol.10 , pp. 2247-2258
    • Schreck, R.1    Rieber, P.2    Baeuerle, P.A.3
  • 59
    • 0026590541 scopus 로고
    • Dithiocarbamates as potent inhibitors of nuclear factor kappa B activation in intact cells
    • 59. Schreck R, Meier B, Mannel DN, Droge W, Baeuerle PA (1992) Dithiocarbamates as potent inhibitors of nuclear factor kappa B activation in intact cells. J Exp Med 175:1181-1194
    • (1992) J Exp Med , vol.175 , pp. 1181-1194
    • Schreck, R.1    Meier, B.2    Mannel, D.N.3    Droge, W.4    Baeuerle, P.A.5
  • 61
    • 0031706322 scopus 로고    scopus 로고
    • Ischemia/reperfusion injury in the liver of BALB/c mice activates AP-1 and nuclear factor kappaB independently of IkappaB degradation
    • 61. Zwacka RM, Zhang Y, Zhou W, Halldorson J, Engelhardt JF (1998) Ischemia/reperfusion injury in the liver of BALB/c mice activates AP-1 and nuclear factor kappaB independently of IkappaB degradation. Hepatology 28:1022-1030
    • (1998) Hepatology , vol.28 , pp. 1022-1030
    • Zwacka, R.M.1    Zhang, Y.2    Zhou, W.3    Halldorson, J.4    Engelhardt, J.F.5
  • 62
    • 0028174061 scopus 로고
    • Function and activation of NF-kappa B in the immune system
    • 62. Baeuerle PA, Henkel T (1994) Function and activation of NF-kappa B in the immune system. Annu Rev Immunol 12:141-179
    • (1994) Annu Rev Immunol , vol.12 , pp. 141-179
    • Baeuerle, P.A.1    Henkel, T.2
  • 63
    • 0031596596 scopus 로고    scopus 로고
    • Blocking NF-kappaB in the liver: The good and bad news
    • 63. Taub R (1998) Blocking NF-kappaB in the liver: the good and bad news. Hepatology 27:1445-1446
    • (1998) Hepatology , vol.27 , pp. 1445-1446
    • Taub, R.1
  • 65
    • 0025726646 scopus 로고
    • Isolation of a rel-related human cDNA that potentially encodes the 65-kD subunit of NF-kappa B
    • published erratum 254:11
    • 65. Ruben SM, Dillon PJ, Schreck R, Henkel T, Chen CH, Maher M, Baeuerle PA, Rosen CA (1991) Isolation of a rel-related human cDNA that potentially encodes the 65-kD subunit of NF-kappa B. Science 251:1490-1493 (published erratum 254:11)
    • (1991) Science , vol.251 , pp. 1490-1493
    • Ruben, S.M.1    Dillon, P.J.2    Schreck, R.3    Henkel, T.4    Chen, C.H.5    Maher, M.6    Baeuerle, P.A.7    Rosen, C.A.8
  • 66
    • 0025078530 scopus 로고
    • Cloning of the p50 DNA binding subunit of NF-kappa B: Homology to rel and dorsal
    • 66. Ghosh S, Gifford AM, Riviere LR, Tempst P, Nolan GP, Baltimore D (1990) Cloning of the p50 DNA binding subunit of NF-kappa B: homology to rel and dorsal. Cell 62:1019-1029
    • (1990) Cell , vol.62 , pp. 1019-1029
    • Ghosh, S.1    Gifford, A.M.2    Riviere, L.R.3    Tempst, P.4    Nolan, G.P.5    Baltimore, D.6
  • 67
    • 0028971289 scopus 로고
    • Rel/NF-kappa B/I kappa B family: Intimate tales of association and dissociation
    • 67. Verma IM, Stevenson JK, Schwarz EM, Van Antwerp D, Miyamoto S (1995) Rel/NF-kappa B/I kappa B family: intimate tales of association and dissociation. Genes Dev 9:2723-2735
    • (1995) Genes Dev , vol.9 , pp. 2723-2735
    • Verma, I.M.1    Stevenson, J.K.2    Schwarz, E.M.3    Van Antwerp, D.4    Miyamoto, S.5
  • 69
    • 0030613551 scopus 로고    scopus 로고
    • The IkappaB kinase complex (IKK) contains two kinase subunits, IKKalpha and IKKbeta, necessary for IkappaB phosphorylation and NF-kappaB activation
    • 69. Zandi E, Rothwarf DM, Delhase M, Hayakawa M, Karin M (1997) The IkappaB kinase complex (IKK) contains two kinase subunits, IKKalpha and IKKbeta, necessary for IkappaB phosphorylation and NF-kappaB activation. Cell 91:243-252
    • (1997) Cell , vol.91 , pp. 243-252
    • Zandi, E.1    Rothwarf, D.M.2    Delhase, M.3    Hayakawa, M.4    Karin, M.5
  • 70
    • 0027536852 scopus 로고
    • The inducible transcription factor NF-kappa B: Structure-function relationship of its protein subunits
    • 70. Grimm S, Baeuerle PA (1993) The inducible transcription factor NF-kappa B: structure-function relationship of its protein subunits. Biochem J 290:297-308
    • (1993) Biochem J , vol.290 , pp. 297-308
    • Grimm, S.1    Baeuerle, P.A.2
  • 71
    • 0032583949 scopus 로고    scopus 로고
    • Differential regulation of IkappaB kinase alpha and beta by two upstream kinases, NF-kappaB-inducing kinase and mitogen-activated protein kinase/ERK kinase kinase-1
    • 71. Nakano H, Shindo M, Sakon S, Nishinaka S, Mihara M, Yagita H, Okumura K (1998) Differential regulation of IkappaB kinase alpha and beta by two upstream kinases, NF-kappaB-inducing kinase and mitogen-activated protein kinase/ERK kinase kinase-1. Proc Natl Acad Sci USA 95: 3537-3542
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 3537-3542
    • Nakano, H.1    Shindo, M.2    Sakon, S.3    Nishinaka, S.4    Mihara, M.5    Yagita, H.6    Okumura, K.7
  • 72
  • 73
    • 0031285250 scopus 로고    scopus 로고
    • Activation of the IkappaB alpha kinase complex by MEKK1, a kinase of the JNK pathway
    • 73. Lee FS, Hagler J, Chen ZJ, Maniatis T (1997) Activation of the IkappaB alpha kinase complex by MEKK1, a kinase of the JNK pathway. Cell 88:213-222
    • (1997) Cell , vol.88 , pp. 213-222
    • Lee, F.S.1    Hagler, J.2    Chen, Z.J.3    Maniatis, T.4
  • 74
    • 0028268629 scopus 로고
    • Hypoxia causes the activation of nuclear factor kappa B through the phosphorylation of I kappa B alpha on tyrosine residues
    • 74. Koong AC, Chen EY, Giaccia AJ (1994) Hypoxia causes the activation of nuclear factor kappa B through the phosphorylation of I kappa B alpha on tyrosine residues. Cancer Res 54:1425-1430
    • (1994) Cancer Res , vol.54 , pp. 1425-1430
    • Koong, A.C.1    Chen, E.Y.2    Giaccia, A.J.3
  • 76
    • 0030298294 scopus 로고    scopus 로고
    • Dissection of TNF receptor 1 effector functions: JNK activation is not linked to apoptosis while NF-kappaB activation prevents cell death
    • 76. Liu ZG, Hsu H, Goeddel DV, Karin M (1996) Dissection of TNF receptor 1 effector functions: JNK activation is not linked to apoptosis while NF-kappaB activation prevents cell death. Cell 87:565-576
    • (1996) Cell , vol.87 , pp. 565-576
    • Liu, Z.G.1    Hsu, H.2    Goeddel, D.V.3    Karin, M.4
  • 77
    • 0029858387 scopus 로고    scopus 로고
    • TNF- and cancer therapy-induced apoptosis: Potentiation by inhibition of NF-kappaB
    • 77. Wang CY, Mayo MW, Baldwin AS Jr (1996) TNF- and cancer therapy-induced apoptosis: potentiation by inhibition of NF-kappaB. Science 274:784-787
    • (1996) Science , vol.274 , pp. 784-787
    • Wang, C.Y.1    Mayo, M.W.2    Baldwin A.S., Jr.3
  • 82
    • 0028201023 scopus 로고
    • Oncogenic Ras activates c-Jun via a separate pathway from the activation of extracellular signal-regulated kinases
    • 82. Westwick JK, Cox AD, Der CJ, Cobb MH, Hibi M, Karin M, Brenner DA (1994) Oncogenic Ras activates c-Jun via a separate pathway from the activation of extracellular signal-regulated kinases. Proc Natl Acad Sci U S A 91:6030-6034
    • (1994) Proc Natl Acad Sci U S A , vol.91 , pp. 6030-6034
    • Westwick, J.K.1    Cox, A.D.2    Der, C.J.3    Cobb, M.H.4    Hibi, M.5    Karin, M.6    Brenner, D.A.7
  • 83
    • 0030883604 scopus 로고    scopus 로고
    • Opposing activities of c-Fos and Fra-2 on AP-1 regulated transcriptional activity in mouse keratinocytes induced to differentiate by calcium and phorbol esters
    • 83. Rutberg SE, Saez E, Lo S, Jang SI, Markova N, Spiegelman BM, Yuspa SH (1997) Opposing activities of c-Fos and Fra-2 on AP-1 regulated transcriptional activity in mouse keratinocytes induced to differentiate by calcium and phorbol esters. Oncogene 15:1337-1346
    • (1997) Oncogene , vol.15 , pp. 1337-1346
    • Rutberg, S.E.1    Saez, E.2    Lo, S.3    Jang, S.I.4    Markova, N.5    Spiegelman, B.M.6    Yuspa, S.H.7
  • 84
    • 0032539001 scopus 로고    scopus 로고
    • The transcription factor AP-1 is required for EGF-induced activation of rho-like GTPases, cytoskeletal rearrangements, motility, and in vitro invasion of A431 cells
    • 84. Malliri A, Symons M, Hennigan RF, Hurlstone AF, Lamb RF, Wheeler T, Ozanne BW (1998) The transcription factor AP-1 is required for EGF-induced activation of rho-like GTPases, cytoskeletal rearrangements, motility, and in vitro invasion of A431 cells. J Cell Biol 143:1087-1099
    • (1998) J Cell Biol , vol.143 , pp. 1087-1099
    • Malliri, A.1    Symons, M.2    Hennigan, R.F.3    Hurlstone, A.F.4    Lamb, R.F.5    Wheeler, T.6    Ozanne, B.W.7
  • 85
    • 0032483808 scopus 로고    scopus 로고
    • H2O2 and tumor necrosis factor-alpha induce differential binding of the redox-responsive transcription factors AP-1 and NF-kappaB to the interleukin-8 promoter in endothelial and epithelial cells
    • 85. Lakshminarayanan V, Drab-Weiss EA, Roebuck KA (1998) H2O2 and tumor necrosis factor-alpha induce differential binding of the redox-responsive transcription factors AP-1 and NF-kappaB to the interleukin-8 promoter in endothelial and epithelial cells. J Biol Chem 273:32670-32678
    • (1998) J Biol Chem , vol.273 , pp. 32670-32678
    • Lakshminarayanan, V.1    Drab-Weiss, E.A.2    Roebuck, K.A.3
  • 86
    • 0031450154 scopus 로고    scopus 로고
    • MEKK1 binds directly to the c-Jun N-terminal kinases/stress-activated protein kinases
    • 86. Xu S, Cobb MH (1997) MEKK1 binds directly to the c-Jun N-terminal kinases/stress-activated protein kinases. J Biol Chem 272:32056-32060
    • (1997) J Biol Chem , vol.272 , pp. 32056-32060
    • Xu, S.1    Cobb, M.H.2
  • 87
    • 0028329953 scopus 로고
    • JNK1: A protein kinase stimulated by UV light and Ha-Ras that binds and phosphorylates the c-Jun activation domain
    • 87. Derijard B, Hibi M, Wu TH, Barrett T, Su B, Deng T, Karin M, Davis RJ (1994) JNK1: a protein kinase stimulated by UV light and Ha-Ras that binds and phosphorylates the c-Jun activation domain. Cell 76:1025-1037
    • (1994) Cell , vol.76 , pp. 1025-1037
    • Derijard, B.1    Hibi, M.2    Wu, T.H.3    Barrett, T.4    Su, B.5    Deng, T.6    Karin, M.7    Davis, R.J.8
  • 88
    • 0028061674 scopus 로고
    • Signal transduction by tumor necrosis factor mediated by JNK protein kinases
    • 88. Sluss HK, Barrett T, Derijard B, Davis RJ (1994) Signal transduction by tumor necrosis factor mediated by JNK protein kinases. Mol Cell Biol 14:8376-8384
    • (1994) Mol Cell Biol , vol.14 , pp. 8376-8384
    • Sluss, H.K.1    Barrett, T.2    Derijard, B.3    Davis, R.J.4
  • 89
    • 0025788098 scopus 로고
    • Oncogenic and transcriptional cooperation with Ha-Ras requires phosphorylation of c-Jun on serines 63 and 73
    • 89. Smeal T, Binetruy B, Mercola DA, Birrer M, Karin M (1991) Oncogenic and transcriptional cooperation with Ha-Ras requires phosphorylation of c-Jun on serines 63 and 73. Nature 354:494-496
    • (1991) Nature , vol.354 , pp. 494-496
    • Smeal, T.1    Binetruy, B.2    Mercola, D.A.3    Birrer, M.4    Karin, M.5
  • 90
    • 0029808748 scopus 로고    scopus 로고
    • Transcription factor AP-1 regulation by mitogen-activated protein kinase signal transduction pathways
    • 90. Whitmarsh AJ, Davis RJ (1996) Transcription factor AP-1 regulation by mitogen-activated protein kinase signal transduction pathways. J Mol Med 74:589-607
    • (1996) J Mol Med , vol.74 , pp. 589-607
    • Whitmarsh, A.J.1    Davis, R.J.2
  • 91
    • 0028908803 scopus 로고
    • Identification of the rel family members required for virus induction of the human beta interferon gene
    • 91. Thanos D, Maniatis T (1995) Identification of the rel family members required for virus induction of the human beta interferon gene. Mol Cell Biol 15:152-164
    • (1995) Mol Cell Biol , vol.15 , pp. 152-164
    • Thanos, D.1    Maniatis, T.2
  • 92
    • 0030922083 scopus 로고    scopus 로고
    • A novel mechanism of JNK1 activation. Nuclear translocation and activation of JNK1 during ischemia and reperfusion
    • 92. Mizukami Y, Yoshioka K, Morimoto S, Yoshida K (1997) A novel mechanism of JNK1 activation. Nuclear translocation and activation of JNK1 during ischemia and reperfusion. J Biol Chem 272:16657-16662
    • (1997) J Biol Chem , vol.272 , pp. 16657-16662
    • Mizukami, Y.1    Yoshioka, K.2    Morimoto, S.3    Yoshida, K.4
  • 93
    • 0026645859 scopus 로고
    • Expression and involvement of c-fos and c-jun protooncogenes in programmed cell death induced by growth factor deprivation in lymphoid cell lines
    • 93. Colotta F, Polentarutti N, Sironi M, Mantovani A (1992) Expression and involvement of c-fos and c-jun protooncogenes in programmed cell death induced by growth factor deprivation in lymphoid cell lines. J Biol Chem 267:18278-18283
    • (1992) J Biol Chem , vol.267 , pp. 18278-18283
    • Colotta, F.1    Polentarutti, N.2    Sironi, M.3    Mantovani, A.4
  • 94
    • 0029982563 scopus 로고    scopus 로고
    • Expression of c-fos and c-jun during hepatocellular remodeling following ischemia/reperfusion in mouse liver
    • 94. Schlossberg H, Zhang Y, Dudus L, Engelhardt JF (1996) Expression of c-fos and c-jun during hepatocellular remodeling following ischemia/reperfusion in mouse liver. Hepatology 23:1546-1555
    • (1996) Hepatology , vol.23 , pp. 1546-1555
    • Schlossberg, H.1    Zhang, Y.2    Dudus, L.3    Engelhardt, J.F.4
  • 95
    • 0028984775 scopus 로고
    • Activation of Jun kinase is an early event in hepatic regeneration
    • 95. Westwick JK, Weitzel C, Leffert HL, Brenner DA (1995) Activation of Jun kinase is an early event in hepatic regeneration. J Clin Invest 95:803-810
    • (1995) J Clin Invest , vol.95 , pp. 803-810
    • Westwick, J.K.1    Weitzel, C.2    Leffert, H.L.3    Brenner, D.A.4
  • 96
    • 0031030599 scopus 로고    scopus 로고
    • Induction of early-immediate genes by tumor necrosis factor alpha contribute to liver repair following chemical-induced hepatotoxicity
    • 96. Bruccoleri A, Gallucci R, Germolec DR, Blackshear P, Simeonova P, Thurman RG, Luster MI (1997) Induction of early-immediate genes by tumor necrosis factor alpha contribute to liver repair following chemical-induced hepatotoxicity. Hepatology 25:133-141
    • (1997) Hepatology , vol.25 , pp. 133-141
    • Bruccoleri, A.1    Gallucci, R.2    Germolec, D.R.3    Blackshear, P.4    Simeonova, P.5    Thurman, R.G.6    Luster, M.I.7
  • 97
    • 0028325891 scopus 로고
    • Mouse JunD negatively regulates fibroblast growth and antagonizes transformation by ras
    • 97. Pfarr CM, Mechta F, Spyrou G, Lallemand D, Carillo S, Yaniv M (1994) Mouse JunD negatively regulates fibroblast growth and antagonizes transformation by ras. Cell 76:747-760
    • (1994) Cell , vol.76 , pp. 747-760
    • Pfarr, C.M.1    Mechta, F.2    Spyrou, G.3    Lallemand, D.4    Carillo, S.5    Yaniv, M.6
  • 98
    • 0025015647 scopus 로고
    • Antitumor promotion and antiinflammation: Down-modulation of AP-1 (Fos/Jun) activity by glucocorticoid hormone
    • 98. Jonat C, Rahmsdorf HJ, Park KK, Cato AC, Gebel S, Ponta H, Herrlich P (1990) Antitumor promotion and antiinflammation: down-modulation of AP-1 (Fos/Jun) activity by glucocorticoid hormone. Cell 62:1189-1204
    • (1990) Cell , vol.62 , pp. 1189-1204
    • Jonat, C.1    Rahmsdorf, H.J.2    Park, K.K.3    Cato, A.C.4    Gebel, S.5    Ponta, H.6    Herrlich, P.7
  • 99
    • 0028986193 scopus 로고
    • NF-kappa B: A lesson in family values
    • 99. Thanos D, Maniatis T (1995) NF-kappa B: a lesson in family values. Cell 80:529-532
    • (1995) Cell , vol.80 , pp. 529-532
    • Thanos, D.1    Maniatis, T.2
  • 100
    • 0030961006 scopus 로고    scopus 로고
    • Hypoxia-inducible factor 1alpha (HIF-1alpha) protein is rapidly degraded by the ubiquitin-proteasome system under normoxic conditions. Its stabilization by hypoxia depends on redox-induced changes
    • 100. Salceda S, Caro J (1997) Hypoxia-inducible factor 1alpha (HIF-1alpha) protein is rapidly degraded by the ubiquitin-proteasome system under normoxic conditions. Its stabilization by hypoxia depends on redox-induced changes. J Biol Chem 272:22642-22647
    • (1997) J Biol Chem , vol.272 , pp. 22642-22647
    • Salceda, S.1    Caro, J.2
  • 101
    • 0028859483 scopus 로고
    • Hypoxia-induced protein binding to O2-responsive sequences on the tyrosine hydroxylase gene
    • 101. Norris ML, Millhorn DE (1995) Hypoxia-induced protein binding to O2-responsive sequences on the tyrosine hydroxylase gene. J Biol Chem 270:23774-23779
    • (1995) J Biol Chem , vol.270 , pp. 23774-23779
    • Norris, M.L.1    Millhorn, D.E.2
  • 102
    • 0029842459 scopus 로고    scopus 로고
    • Oxygen sensing and molecular adaptation to hypoxia
    • 102. Bunn HF, Poyton RO (1996) Oxygen sensing and molecular adaptation to hypoxia. Physiol Rev 76:839-885
    • (1996) Physiol Rev , vol.76 , pp. 839-885
    • Bunn, H.F.1    Poyton, R.O.2
  • 103
    • 0030963616 scopus 로고    scopus 로고
    • The hypoxic response: Huffing and HIFing
    • 103. Guillemin K, Krasnow MA (1997) The hypoxic response: huffing and HIFing. Cell 89:9-12
    • (1997) Cell , vol.89 , pp. 9-12
    • Guillemin, K.1    Krasnow, M.A.2
  • 104
    • 0023764626 scopus 로고
    • 1,25-Dihydroxy-vitamin D3 increases the toxicity of hydrogen peroxide in the human monocytic line U937: The role of calcium and heat shock
    • 104. Polla BS, Bonventre JV, Krane SM (1988) 1,25-Dihydroxy-vitamin D3 increases the toxicity of hydrogen peroxide in the human monocytic line U937: the role of calcium and heat shock. J Cell Riol 107:373-380
    • (1988) J Cell Riol , vol.107 , pp. 373-380
    • Polla, B.S.1    Bonventre, J.V.2    Krane, S.M.3
  • 105
    • 0032030809 scopus 로고    scopus 로고
    • Constitutive and inducible hsp70 s are involved in oxidative resistance evoked by heat shock or ethanol
    • 105. Su CY, Chong KY, Owen OE, Dillmann WH, Chang C, Lai CC (1998) Constitutive and inducible hsp70 s are involved in oxidative resistance evoked by heat shock or ethanol. J Mol Cell Cardiol 30:587-598
    • (1998) J Mol Cell Cardiol , vol.30 , pp. 587-598
    • Su, C.Y.1    Chong, K.Y.2    Owen, O.E.3    Dillmann, W.H.4    Chang, C.5    Lai, C.C.6
  • 106
  • 108
    • 0030995732 scopus 로고    scopus 로고
    • Differential activation of heat shock and nuclear factor kappaB transcription factors in postischemic reperfused rat liver
    • 108. Tacchini L, Radice L, Pogliaghi G, Bernelli-Zazzera A (1997) Differential activation of heat shock and nuclear factor kappaB transcription factors in postischemic reperfused rat liver. Hepatology 26:186-191
    • (1997) Hepatology , vol.26 , pp. 186-191
    • Tacchini, L.1    Radice, L.2    Pogliaghi, G.3    Bernelli-Zazzera, A.4
  • 110
    • 0031470969 scopus 로고    scopus 로고
    • A new platelet-activating factor antagonist (CV-6209) in preservation of heart and lung for transplantation
    • 110. Qayumi KA, English JC, Feelry EJ, Poostizadeh A, Nikbakht-Sangari M (1997) A new platelet-activating factor antagonist (CV-6209) in preservation of heart and lung for transplantation. Cardiovasc Drugs Ther 11:777-785
    • (1997) Cardiovasc Drugs Ther , vol.11 , pp. 777-785
    • Qayumi, K.A.1    English, J.C.2    Feelry, E.J.3    Poostizadeh, A.4    Nikbakht-Sangari, M.5
  • 111
    • 0030899606 scopus 로고    scopus 로고
    • Neutrophils accentuate renal cold ischemia-reperfusion injury. Dose-dependent protective effect of a platelet-activating factor receptor antagonist
    • 111. Riera M, Torras J, Herrero I, Valles J, Paubert-Braquet M, Cruzado JM, Alsina J, Grinyo JM (1997) Neutrophils accentuate renal cold ischemia-reperfusion injury. Dose-dependent protective effect of a platelet-activating factor receptor antagonist. J Pharmacol Exp Ther 280:786-794
    • (1997) J Pharmacol Exp Ther , vol.280 , pp. 786-794
    • Riera, M.1    Torras, J.2    Herrero, I.3    Valles, J.4    Paubert-Braquet, M.5    Cruzado, J.M.6    Alsina, J.7    Grinyo, J.M.8
  • 112
    • 0027764523 scopus 로고
    • Requirements for tumor necrosis factor-alpha and interleukin-1 in limb ischemia/reperfusion injury and associated lung injury
    • 112. Seekamp A, Warren JS, Remick DG, Till GO, Ward PA (1993) Requirements for tumor necrosis factor-alpha and interleukin-1 in limb ischemia/reperfusion injury and associated lung injury. Am J Pathol 143:453-463
    • (1993) Am J Pathol , vol.143 , pp. 453-463
    • Seekamp, A.1    Warren, J.S.2    Remick, D.G.3    Till, G.O.4    Ward, P.A.5
  • 113
    • 0026575932 scopus 로고
    • The mechanism of action of cyclosporin A and FK506
    • 113. Schreiber SL, Crabtree GR (1992) The mechanism of action of cyclosporin A and FK506. Immunol Today 13:136-142
    • (1992) Immunol Today , vol.13 , pp. 136-142
    • Schreiber, S.L.1    Crabtree, G.R.2
  • 115
    • 84945736046 scopus 로고
    • Atrial natriuretic peptide protects hepatocytes against damage induced by hypoxia and reactive oxygen. Possible role of intracellular free ionized calcium
    • 115. von Ruecker AA, Wild M, Rao GS, Bidlingmaier F (1989) Atrial natriuretic peptide protects hepatocytes against damage induced by hypoxia and reactive oxygen. Possible role of intracellular free ionized calcium. J Clin Chem Clin Biochem 27:531-537
    • (1989) J Clin Chem Clin Biochem , vol.27 , pp. 531-537
    • Von Ruecker, A.A.1    Wild, M.2    Rao, G.S.3    Bidlingmaier, F.4
  • 116
    • 0026032026 scopus 로고
    • The protective effect of atrial natriuretic peptide (ANP) on cells damaged by oxygen radicals is mediated through elevated CGMP-levels, reduction of calcium-inflow and probably G-proteins
    • 116. Pellav R (1991) The protective effect of atrial natriuretic peptide (ANP) on cells damaged by oxygen radicals is mediated through elevated CGMP-levels, reduction of calcium-inflow and probably G-proteins. Biochem Biophys Res Commun 174:549-555
    • (1991) Biochem Biophys Res Commun , vol.174 , pp. 549-555
    • Pellav, R.1
  • 117
    • 0032020204 scopus 로고    scopus 로고
    • Images in hepatology: Hepatic iron in hemochromatosis enhances hepatocellular carcinoma in magnetic resonance imaging
    • 117. Bilzer M, Helmberger T (1998) Images in hepatology: hepatic iron in hemochromatosis enhances hepatocellular carcinoma in magnetic resonance imaging. J Hepatol 28:523
    • (1998) J Hepatol , vol.28 , pp. 523
    • Bilzer, M.1    Helmberger, T.2
  • 118
    • 0023947833 scopus 로고
    • Principles of solid-organ preservation by cold storage
    • 118. Belzer FO, Southard JH (1988) Principles of solid-organ preservation by cold storage. Transplantation 45:673-676
    • (1988) Transplantation , vol.45 , pp. 673-676
    • Belzer, F.O.1    Southard, J.H.2
  • 119
    • 0031879552 scopus 로고    scopus 로고
    • Sinusoidal endothelial cell injury during hepatic preservation and reperfusion
    • 119. Clavien PA (1998) Sinusoidal endothelial cell injury during hepatic preservation and reperfusion. Hepatology 28:281-285
    • (1998) Hepatology , vol.28 , pp. 281-285
    • Clavien, P.A.1
  • 120
    • 0032988969 scopus 로고    scopus 로고
    • Early activation of transcription factor NF-kappaB during ischemia in perfused rat heart
    • 120. Li C, Browder W, Kao RL (1999) Early activation of transcription factor NF-kappaB during ischemia in perfused rat heart. Am J Physiol 276:H543-H552
    • (1999) Am J Physiol , vol.276
    • Li, C.1    Browder, W.2    Kao, R.L.3
  • 121
    • 0025973603 scopus 로고
    • Myocardial sulfhydryl pool alterations occur during reperfusion after brief and prolonged myocardial ischemia in vivo
    • 121. Lesnefsky EJ, Dauber IM, Horwitz LD (1991) Myocardial sulfhydryl pool alterations occur during reperfusion after brief and prolonged myocardial ischemia in vivo. Circ Res 68:605-613
    • (1991) Circ Res , vol.68 , pp. 605-613
    • Lesnefsky, E.J.1    Dauber, I.M.2    Horwitz, L.D.3
  • 123
    • 1842311445 scopus 로고
    • Nucleotide sequence and expression of human chromosome 21-encoded superoxide dismutase mRNA
    • 123. Sherman L, Dafni N, Lieman-Hurwitz J, Groner Y (1983) Nucleotide sequence and expression of human chromosome 21-encoded superoxide dismutase mRNA. Proc Natl Acad Sci U S A 80:5465-5469
    • (1983) Proc Natl Acad Sci U S A , vol.80 , pp. 5465-5469
    • Sherman, L.1    Dafni, N.2    Lieman-Hurwitz, J.3    Groner, Y.4
  • 124
    • 0023902809 scopus 로고
    • Isolation and characterization of complementary DNAs encoding human manganese-containing superoxide dismutase
    • 124. Ho YS, Crapo JD (1988) Isolation and characterization of complementary DNAs encoding human manganese-containing superoxide dismutase. FEBS Lett 229:256-260
    • (1988) FEBS Lett , vol.229 , pp. 256-260
    • Ho, Y.S.1    Crapo, J.D.2
  • 125
    • 1842709537 scopus 로고
    • Isolation and sequence of complementary DNA encoding human extracellular superoxide dismutase
    • 125. Hjalmarsson K, Marklund SL, Engstrom A, Edlund T (1987) Isolation and sequence of complementary DNA encoding human extracellular superoxide dismutase. Proc Natl Acad Sci U S A 84:6340-6344
    • (1987) Proc Natl Acad Sci U S A , vol.84 , pp. 6340-6344
    • Hjalmarsson, K.1    Marklund, S.L.2    Engstrom, A.3    Edlund, T.4
  • 127
    • 0025719649 scopus 로고
    • Manganese superoxide dismutase: A hepatic acute phase protein regulated by interleukin-6 and glucocorticoids
    • 127. Dougall WC, Nick HS (1991) Manganese superoxide dismutase: a hepatic acute phase protein regulated by interleukin-6 and glucocorticoids. Endocrinology 129:2376-2384
    • (1991) Endocrinology , vol.129 , pp. 2376-2384
    • Dougall, W.C.1    Nick, H.S.2
  • 128
    • 0032030789 scopus 로고    scopus 로고
    • Thiol redox modulation of tumor necrosis factor-alpha responsiveness in cultured AIDS-related Kaposi's sarcoma cells
    • 128. Mallery SR, Landwehr DJ, Ness GM, Clark YM, Hohl CM (1998) Thiol redox modulation of tumor necrosis factor-alpha responsiveness in cultured AIDS-related Kaposi's sarcoma cells. J Cell Biochem 68:339-354
    • (1998) J Cell Biochem , vol.68 , pp. 339-354
    • Mallery, S.R.1    Landwehr, D.J.2    Ness, G.M.3    Clark, Y.M.4    Hohl, C.M.5
  • 129
    • 0031044252 scopus 로고    scopus 로고
    • Iron modulation of LPS-induced manganese superoxide dismutase gene expression in rat tissues
    • 129. De Leo ME, Landriscina M, Palazzotti B, Borrello S, Galeotti T (1997) Iron modulation of LPS-induced manganese superoxide dismutase gene expression in rat tissues. FEBS Lett 403:131-135
    • (1997) FEBS Lett , vol.403 , pp. 131-135
    • De Leo, M.E.1    Landriscina, M.2    Palazzotti, B.3    Borrello, S.4    Galeotti, T.5
  • 130
    • 0029991725 scopus 로고    scopus 로고
    • Biochemical aspects of cellular antioxidant systems
    • 130. Fernandez V, Videla LA (1996) Biochemical aspects of cellular antioxidant systems. Biol Res 29:177-182
    • (1996) Biol Res , vol.29 , pp. 177-182
    • Fernandez, V.1    Videla, L.A.2
  • 131
    • 0028170326 scopus 로고
    • Importance of Se-glutathione peroxidase, catalase, Cu/Zn-SOD for cell survival against oxidative stress
    • 131. Michiels C, Raes M, Toussaint O, Remacle J (1994) Importance of Se-glutathione peroxidase, catalase, Cu/Zn-SOD for cell survival against oxidative stress. Free Radic Biol Med 17:235-248
    • (1994) Free Radic Biol Med , vol.17 , pp. 235-248
    • Michiels, C.1    Raes, M.2    Toussaint, O.3    Remacle, J.4
  • 132
    • 0031407777 scopus 로고    scopus 로고
    • Preventive effects of superoxide dismutase derivatives modified with monosaccharides on reperfusion injury in rat liver transplantation
    • 132. Mizoe A, Kondo S, Azuma T, Fujioka H, Tanaka K, Hashida M, Kanematsu T (1997) Preventive effects of superoxide dismutase derivatives modified with monosaccharides on reperfusion injury in rat liver transplantation. J Surg Res 73: 160-165
    • (1997) J Surg Res , vol.73 , pp. 160-165
    • Mizoe, A.1    Kondo, S.2    Azuma, T.3    Fujioka, H.4    Tanaka, K.5    Hashida, M.6    Kanematsu, T.7
  • 133
    • 0025257116 scopus 로고
    • Superoxide dismutase and catalase as therapeutic agents for human diseases. A critical review
    • 133. Greenwald RA (1990) Superoxide dismutase and catalase as therapeutic agents for human diseases. A critical review. Free Radic Biol Med 8:201-209
    • (1990) Free Radic Biol Med , vol.8 , pp. 201-209
    • Greenwald, R.A.1
  • 134
    • 0021352122 scopus 로고
    • Protection against oxygen toxicity by intravenous injection of liposome-entrapped catalase and superoxide dismutase
    • 134. Turrens JF, Crapo JD, Freeman BA (1984) Protection against oxygen toxicity by intravenous injection of liposome-entrapped catalase and superoxide dismutase. J Clin Invest 73:87-95
    • (1984) J Clin Invest , vol.73 , pp. 87-95
    • Turrens, J.F.1    Crapo, J.D.2    Freeman, B.A.3
  • 135
    • 0028844530 scopus 로고
    • Antioxidant-surfactant liposomes mitigate hyperoxic lung injury in premature rabbits
    • 135. Walther FJ, David-Cu R, Lopez SL (1995) Antioxidant-surfactant liposomes mitigate hyperoxic lung injury in premature rabbits. Am J Physiol 269:L613-L617
    • (1995) Am J Physiol , vol.269
    • Walther, F.J.1    David-Cu, R.2    Lopez, S.L.3
  • 136
    • 0027460226 scopus 로고
    • Polyethylene glycol-conjugated superoxide dismutase protects rats against oxygen toxicity
    • 136. Tang G, White JE, Gordon RJ, Lumb PD, Tsan MF (1993) Polyethylene glycol-conjugated superoxide dismutase protects rats against oxygen toxicity. J Appl Physiol 74:1425-1431
    • (1993) J Appl Physiol , vol.74 , pp. 1425-1431
    • Tang, G.1    White, J.E.2    Gordon, R.J.3    Lumb, P.D.4    Tsan, M.F.5
  • 137
    • 0027102397 scopus 로고
    • Therapeutic effects of superoxide dismutase derivatives modified with mono- or polysaccharides on hepatic injury induced by ischemia/reperfusion
    • 137. Fujita T, Furitsu H, Nishikawa M, Takakura Y, Sezaki H, Hashida M (1992) Therapeutic effects of superoxide dismutase derivatives modified with mono- or polysaccharides on hepatic injury induced by ischemia/reperfusion. Biochem Biophys Res Commun 189:191-196
    • (1992) Biochem Biophys Res Commun , vol.189 , pp. 191-196
    • Fujita, T.1    Furitsu, H.2    Nishikawa, M.3    Takakura, Y.4    Sezaki, H.5    Hashida, M.6
  • 138
    • 0026039253 scopus 로고
    • Targeting SOD by gene and protein engineering and inhibition of free radical injury
    • 138. Inoue M, Watanabe N, Utsumi T, Sasaki J (1991) Targeting SOD by gene and protein engineering and inhibition of free radical injury. Free Radic Res Commun 12-13:391-399
    • (1991) Free Radic Res Commun , vol.12-13 , pp. 391-399
    • Inoue, M.1    Watanabe, N.2    Utsumi, T.3    Sasaki, J.4
  • 139
    • 0029015757 scopus 로고
    • Antioxidant therapy in critical care medicine
    • 139. Tanswell AK, Freeman BA (1995) Antioxidant therapy in critical care medicine. New Horiz 3:330-341
    • (1995) New Horiz , vol.3 , pp. 330-341
    • Tanswell, A.K.1    Freeman, B.A.2
  • 140
    • 0032925686 scopus 로고    scopus 로고
    • Targeted delivery and improved therapeutic potential of catalase by chemical modification: Combination with superoxide dismutase derivatives
    • 140. Yabe Y, Nishikawa M, Tamada A, Takakura Y, Hashida M (1999) Targeted delivery and improved therapeutic potential of catalase by chemical modification: combination with superoxide dismutase derivatives. J Pharmacol Exp Ther 289:1176-1184
    • (1999) J Pharmacol Exp Ther , vol.289 , pp. 1176-1184
    • Yabe, Y.1    Nishikawa, M.2    Tamada, A.3    Takakura, Y.4    Hashida, M.5
  • 141
    • 0026501194 scopus 로고
    • Reduced expression of manganese superoxide dismutase in cells resistant to cytolysis by tumor necrosis factor
    • 141. Melendez JA, Baglioni C (1992) Reduced expression of manganese superoxide dismutase in cells resistant to cytolysis by tumor necrosis factor. Free Radic Biol Med 12:151-159
    • (1992) Free Radic Biol Med , vol.12 , pp. 151-159
    • Melendez, J.A.1    Baglioni, C.2
  • 142
    • 0026048173 scopus 로고
    • Overproduction of human Mn-superoxide dismutase modulates paraquat-mediated toxicity in mammalian cell
    • 142. St. Clair DK, Oberley TD, Ho YS (1991) Overproduction of human Mn-superoxide dismutase modulates paraquat-mediated toxicity in mammalian cell., FEBS Lett 293:199-203
    • (1991) FEBS Lett , vol.293 , pp. 199-203
    • St. Clair, D.K.1    Oberley, T.D.2    Ho, Y.S.3
  • 143
    • 0027394553 scopus 로고
    • Overexpression of mitochondrial manganese superoxide dismutase promotes the survival of tumor cells exposed to interleukin-1, tumor necrosis factor, selected anticancer drugs, and ionizing radiation
    • 143. Hirose K, Longo DL, Oppenheim JJ, Matsushima K (1993) Overexpression of mitochondrial manganese superoxide dismutase promotes the survival of tumor cells exposed to interleukin-1, tumor necrosis factor, selected anticancer drugs, and ionizing radiation. Faseb J 7:361-368
    • (1993) Faseb J , vol.7 , pp. 361-368
    • Hirose, K.1    Longo, D.L.2    Oppenheim, J.J.3    Matsushima, K.4
  • 145
    • 0026700573 scopus 로고
    • Acute-phase induction of manganese superoxide dismutase in intestinal epithelial cell lines
    • 145. Valentine JF, Nick HS (1992) Acute-phase induction of manganese superoxide dismutase in intestinal epithelial cell lines. Gastroenterology 103:905-912
    • (1992) Gastroenterology , vol.103 , pp. 905-912
    • Valentine, J.F.1    Nick, H.S.2
  • 146
    • 0032125963 scopus 로고    scopus 로고
    • Gene therapy for oxidant injury-related diseases: Adenovirus-mediated transfer of superoxide dismutase and catalase cDNAs protects against hyperoxia but not against ischemia-reperfusion lung injury
    • 146. Danel C, Erzurum SC, Prayssac P, Eissa NT, Crystal RG, Herve P, Baudet B, Mazmanian M, Lemarchand P (1998) Gene therapy for oxidant injury-related diseases: adenovirus-mediated transfer of superoxide dismutase and catalase cDNAs protects against hyperoxia but not against ischemia-reperfusion lung injury. Hum Gene Ther 9:1487-1496
    • (1998) Hum Gene Ther , vol.9 , pp. 1487-1496
    • Danel, C.1    Erzurum, S.C.2    Prayssac, P.3    Eissa, N.T.4    Crystal, R.G.5    Herve, P.6    Baudet, B.7    Mazmanian, M.8    Lemarchand, P.9
  • 147
    • 0032487365 scopus 로고    scopus 로고
    • Transgenic mice with increased copper/zinc-superoxide dismutase activity are resistant to hepatic leukostasis and capillary no-reflow after gut ischemia/reperfusion
    • 147. Horie Y, Wolf R, Flores SC, McCord JM, Epstein CJ, Granger DN (1998) Transgenic mice with increased copper/zinc-superoxide dismutase activity are resistant to hepatic leukostasis and capillary no-reflow after gut ischemia/reperfusion. Circ Res 83:691-696
    • (1998) Circ Res , vol.83 , pp. 691-696
    • Horie, Y.1    Wolf, R.2    Flores, S.C.3    McCord, J.M.4    Epstein, C.J.5    Granger, D.N.6
  • 150
    • 0031918742 scopus 로고    scopus 로고
    • The mitochondrial death/life regulator in apoptosis and necrosis
    • 150. Kroemer G, Dallaporta B, Resche-Rigon M (1998) The mitochondrial death/life regulator in apoptosis and necrosis. Annu Rev Physiol 60:619-642
    • (1998) Annu Rev Physiol , vol.60 , pp. 619-642
    • Kroemer, G.1    Dallaporta, B.2    Resche-Rigon, M.3
  • 151
    • 0028306269 scopus 로고
    • Peroxynitrite causes calcium efflux from mitochondria which is prevented by cyclosporin A
    • 151. Packer MA, Murphy MP (1994) Peroxynitrite causes calcium efflux from mitochondria which is prevented by Cyclosporin A. FEBS Lett 345:237-240
    • (1994) FEBS Lett , vol.345 , pp. 237-240
    • Packer, M.A.1    Murphy, M.P.2
  • 152
    • 0028999212 scopus 로고
    • On the effects of paraquat on isolated mitochondria. Evidence that paraquat causes opening of the cyclosporin A-sensitive permeability transition pore synergistically with nitric oxide
    • 152. Costantini P, Petronilli V, Colonna R, Bernardi P (1995) On the effects of paraquat on isolated mitochondria. Evidence that paraquat causes opening of the cyclosporin A-sensitive permeability transition pore synergistically with nitric oxide. Toxicology 99:77-88
    • (1995) Toxicology , vol.99 , pp. 77-88
    • Costantini, P.1    Petronilli, V.2    Colonna, R.3    Bernardi, P.4
  • 153
    • 0021345968 scopus 로고
    • The role of glutathione in the retention of Ca2+ by liver mitochondria
    • 153. Beatrice MC, Stiers DL, Pfeiffer DR (1984) The role of glutathione in the retention of Ca2+ by liver mitochondria. J Biol Chem 259:1279-1287
    • (1984) J Biol Chem , vol.259 , pp. 1279-1287
    • Beatrice, M.C.1    Stiers, D.L.2    Pfeiffer, D.R.3
  • 154
    • 0032504709 scopus 로고    scopus 로고
    • Elucidating the molecular mechanism of the permeability transition pore and its role in reperfusion injury of the heart
    • 154. Halestrap AP, Kerr PM, Javadov S, Woodfield KY (1998) Elucidating the molecular mechanism of the permeability transition pore and its role in reperfusion injury of the heart. Biochim Biophys Acta 1366:79-94
    • (1998) Biochim Biophys Acta , vol.1366 , pp. 79-94
    • Halestrap, A.P.1    Kerr, P.M.2    Javadov, S.3    Woodfield, K.Y.4
  • 155
  • 156
    • 0032508486 scopus 로고    scopus 로고
    • Bcl-2 activates the transcription factor NFkappaB through the degradation of the cytoplasmic inhibitor IkappaBalpha
    • 156. de Moissac D, Mustapha S, Greenberg AH, Kirshenbaum LA (1998) Bcl-2 activates the transcription factor NFkappaB through the degradation of the cytoplasmic inhibitor IkappaBalpha. J Biol Chem 273:23946-23951
    • (1998) J Biol Chem , vol.273 , pp. 23946-23951
    • De Moissac, D.1    Mustapha, S.2    Greenberg, A.H.3    Kirshenbaum, L.A.4
  • 158
    • 0032573165 scopus 로고    scopus 로고
    • Ionizing radiation and short wavelength UV activate NF-kappaB through two distinct mechanisms
    • 158. Li N, Karin M (1998) Ionizing radiation and short wavelength UV activate NF-kappaB through two distinct mechanisms. Proc Natl Acad Sci U S A 95:13012-13017
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 13012-13017
    • Li, N.1    Karin, M.2
  • 159
    • 0031596594 scopus 로고    scopus 로고
    • Inhibition of NFkappaB in activated rat hepatic stellate cells by proteasome inhibitors and an IkappaB super-repressor
    • 159. Hellerbrand C, Jobin C, Iimuro Y, Licato L, Sartor RB, Brenner DA (1998) Inhibition of NFkappaB in activated rat hepatic stellate cells by proteasome inhibitors and an IkappaB super-repressor. Hepatology 27:1285-1295
    • (1998) Hepatology , vol.27 , pp. 1285-1295
    • Hellerbrand, C.1    Jobin, C.2    Iimuro, Y.3    Licato, L.4    Sartor, R.B.5    Brenner, D.A.6
  • 160
    • 0030613758 scopus 로고    scopus 로고
    • NF-kappaB activation: The I kappaB kinase revealed?
    • 160. Stancovski I, Baltimore D (1997) NF-kappaB activation: the I kappaB kinase revealed? Cell 91:299-302
    • (1997) Cell , vol.91 , pp. 299-302
    • Stancovski, I.1    Baltimore, D.2
  • 161
    • 0032557526 scopus 로고    scopus 로고
    • Multiple signalling pathways lead to the activation of the nuclear factor kappaB by the Rho family of GTPases
    • 161. Montaner S, Perona R, Saniger L, Lacal JC (1998) Multiple signalling pathways lead to the activation of the nuclear factor kappaB by the Rho family of GTPases. J Biol Chem 273:12779-12785
    • (1998) J Biol Chem , vol.273 , pp. 12779-12785
    • Montaner, S.1    Perona, R.2    Saniger, L.3    Lacal, J.C.4
  • 162
    • 0028926263 scopus 로고
    • Parallel signal processing among mammalian MAPKs
    • 162. Cano E, Mahadevan LC (1995) Parallel signal processing among mammalian MAPKs. Trends Biochem Sci 20:117-122
    • (1995) Trends Biochem Sci , vol.20 , pp. 117-122
    • Cano, E.1    Mahadevan, L.C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.