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Volumn 18, Issue 5, 1998, Pages 505-518

Necrosis and apoptosis in acute renal failure

Author keywords

[No Author keywords available]

Indexed keywords

PHOSPHATIDYLSERINE; VITRONECTIN RECEPTOR;

EID: 0031657367     PISSN: 02709295     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Review
Times cited : (204)

References (103)
  • 1
    • 0026389838 scopus 로고
    • Dissociation of tubular cell detachment and tubular cell death in clinical and experimental "acute tubular necrosis"
    • Racusen L, Fivush B, Li Y-L, et al: Dissociation of tubular cell detachment and tubular cell death in clinical and experimental "acute tubular necrosis". Lab Invest 64:546-556, 1991
    • (1991) Lab Invest , vol.64 , pp. 546-556
    • Racusen, L.1    Fivush, B.2    Li, Y.-L.3
  • 2
    • 0018667528 scopus 로고
    • The morphology of "acute tubular necrosis" in man: Analysis of 57 renal biopsies and a comparison with the glycerol model
    • Solez K, Morel-Moroger L, Sraer JD: The morphology of "acute tubular necrosis" in man: Analysis of 57 renal biopsies and a comparison with the glycerol model. Medicine 58:362-376, 1979
    • (1979) Medicine , vol.58 , pp. 362-376
    • Solez, K.1    Morel-Moroger, L.2    Sraer, J.D.3
  • 3
    • 0000656242 scopus 로고    scopus 로고
    • Acute renal failure
    • Brenner B (ed): Philadelphia, PA, Saunders
    • Brady H, Brenner B, Lieberthal W: Acute renal failure, in Brenner B (ed): The Kidney. Philadelphia, PA, Saunders, 1996, pp 1200-1252
    • (1996) The Kidney , pp. 1200-1252
    • Brady, H.1    Brenner, B.2    Lieberthal, W.3
  • 4
    • 0030769161 scopus 로고    scopus 로고
    • Biology of acute renal failure: Therapeutic implications
    • Lieberthal W: Biology of acute renal failure: Therapeutic implications. Kidney Int 52:1102-1115, 1997
    • (1997) Kidney Int , vol.52 , pp. 1102-1115
    • Lieberthal, W.1
  • 5
    • 0029821680 scopus 로고    scopus 로고
    • Mechanisms of apoptosis and its potential role in renal tubular epithelial cell injury
    • Lieberthal W, Levine J: Mechanisms of apoptosis and its potential role in renal tubular epithelial cell injury. Am J Physiol 27:F477-F488, 1996
    • (1996) Am J Physiol , vol.27
    • Lieberthal, W.1    Levine, J.2
  • 6
    • 0015383455 scopus 로고
    • Apoptosis: A basic biologic phenomenon with wide ranging implications in tissue kinetics
    • Kerr JFR, Wyllie AH, Currie AR: Apoptosis: A basic biologic phenomenon with wide ranging implications in tissue kinetics. Br J Cancer 26:239-257, 1972
    • (1972) Br J Cancer , vol.26 , pp. 239-257
    • Kerr, J.F.R.1    Wyllie, A.H.2    Currie, A.R.3
  • 7
    • 43949172708 scopus 로고
    • Phagocyte recognition of cells undergoing apoptosis
    • Savill J, Fadok V, Henson P, et al: Phagocyte recognition of cells undergoing apoptosis. Immunology Today 14:131-136, 1993
    • (1993) Immunology Today , vol.14 , pp. 131-136
    • Savill, J.1    Fadok, V.2    Henson, P.3
  • 8
    • 0028473454 scopus 로고
    • Apoptosis and the kidney
    • Savill J: Apoptosis and the kidney. J Am Soc Nephrol 5:12-21, 1994
    • (1994) J Am Soc Nephrol , vol.5 , pp. 12-21
    • Savill, J.1
  • 9
    • 0028054017 scopus 로고
    • T-cell apoptosis detected in situ during positive and neative selection in the thymus
    • Surh CD, Sprent J: T-cell apoptosis detected in situ during positive and neative selection in the thymus. Nature 372:100-103, 1994
    • (1994) Nature , vol.372 , pp. 100-103
    • Surh, C.D.1    Sprent, J.2
  • 10
    • 0028058936 scopus 로고
    • Apoptotic neutrophils are phagocytosed by fibroblasts with participation of the fibroblast vitronectin receptor and involvement of a mannose/fucose-specific lectin
    • Hall SE, Savill JS, Henson PM, et al: Apoptotic neutrophils are phagocytosed by fibroblasts with participation of the fibroblast vitronectin receptor and involvement of a mannose/fucose-specific lectin. J Immunol 153:3218-3227, 1994
    • (1994) J Immunol , vol.153 , pp. 3218-3227
    • Hall, S.E.1    Savill, J.S.2    Henson, P.M.3
  • 11
    • 0021275785 scopus 로고
    • Hormoneinduced cell death. Surface changes in thymocytes undergoing apoptosis
    • Morris RG, Hargreaves AD, Duvall E, et al: Hormoneinduced cell death. Surface changes in thymocytes undergoing apoptosis. Am J Pathol 115:426-436, 1984
    • (1984) Am J Pathol , vol.115 , pp. 426-436
    • Morris, R.G.1    Hargreaves, A.D.2    Duvall, E.3
  • 12
    • 0021926813 scopus 로고
    • Macrophage recognition of cells undergoing programmed cell death (apoptosis)
    • Duvall E, Wyllie A, Morris R: Macrophage recognition of cells undergoing programmed cell death (apoptosis). Immunology 56:351-358, 1985
    • (1985) Immunology , vol.56 , pp. 351-358
    • Duvall, E.1    Wyllie, A.2    Morris, R.3
  • 14
    • 0026508561 scopus 로고
    • Exposure of phosphatidylserine on the surface of apoptotic lymphocytes triggers specific recognition and removal by macrophages
    • Fadok VA, Voelker DR, Campbell PA, et al: Exposure of phosphatidylserine on the surface of apoptotic lymphocytes triggers specific recognition and removal by macrophages. J Immunol 148:2207-2216, 1992
    • (1992) J Immunol , vol.148 , pp. 2207-2216
    • Fadok, V.A.1    Voelker, D.R.2    Campbell, P.A.3
  • 15
    • 0029043888 scopus 로고
    • A novel assay for apoptosis. Flow cytometric detection of phosphotidylserine expression on early apoptotic cells using fluorescein labelled annexin V
    • Vermes I, Haanen C, Steffens-Naakken H, et al: A novel assay for apoptosis. Flow cytometric detection of phosphotidylserine expression on early apoptotic cells using fluorescein labelled annexin V. J Immun Methods 184:39-51, 1995
    • (1995) J Immun Methods , vol.184 , pp. 39-51
    • Vermes, I.1    Haanen, C.2    Steffens-Naakken, H.3
  • 16
    • 0030240765 scopus 로고    scopus 로고
    • Anti-phospholipid autoantibodies bind to apoptotic, but not viable, thymocytes in a β2-gIycoprotein 1-dependent manner
    • Price B, Rauch J, Shia M, et al: Anti-phospholipid autoantibodies bind to apoptotic, but not viable, thymocytes in a β2-gIycoprotein 1-dependent manner. J Immunol 157:2201-2208, 1996
    • (1996) J Immunol , vol.157 , pp. 2201-2208
    • Price, B.1    Rauch, J.2    Shia, M.3
  • 17
    • 0026527846 scopus 로고
    • The clearance of apoptotic cells in the liver is mediated by the asialoglycoprotein receptor
    • Dini L, Autuori F, Lentini A: The clearance of apoptotic cells in the liver is mediated by the asialoglycoprotein receptor. FEBS lett 296:174-178, 1992
    • (1992) FEBS Lett , vol.296 , pp. 174-178
    • Dini, L.1    Autuori, F.2    Lentini, A.3
  • 18
    • 0025164935 scopus 로고
    • Vitronectin receptor-mediated phagocytosis of cells undergoing apoptosis
    • Savill J, Dransfield I, Hogg N, et al: Vitronectin receptor-mediated phagocytosis of cells undergoing apoptosis. Nature 343:170-173, 1990
    • (1990) Nature , vol.343 , pp. 170-173
    • Savill, J.1    Dransfield, I.2    Hogg, N.3
  • 19
    • 0027057502 scopus 로고
    • Different populations of macrophages use either the vitronectin receptor or the phosphatidylserine receptor to recognize and remove apoptotic cells
    • Fadok V, Savill J, Haslett C, et al: Different populations of macrophages use either the vitronectin receptor or the phosphatidylserine receptor to recognize and remove apoptotic cells. J Immunol 149:4029-4035, 1992
    • (1992) J Immunol , vol.149 , pp. 4029-4035
    • Fadok, V.1    Savill, J.2    Haslett, C.3
  • 20
    • 0026453281 scopus 로고
    • Thrombospondin cooperates with CD36 and the vitronectin receptor in macrophage recognition of neutrophils undergoing apoptosis
    • Savill J, Hogg N, Ren Y, et al: Thrombospondin cooperates with CD36 and the vitronectin receptor in macrophage recognition of neutrophils undergoing apoptosis. J Clin Invest 90:1513-1522, 1992
    • (1992) J Clin Invest , vol.90 , pp. 1513-1522
    • Savill, J.1    Hogg, N.2    Ren, Y.3
  • 21
    • 0029960471 scopus 로고    scopus 로고
    • Role for the class a macrophage scavenger receptor in the phagocytosis of apoptotic thymocytes in vitro
    • Platt N, Suzuki H, Kurihara Y, et al: Role for the class A macrophage scavenger receptor in the phagocytosis of apoptotic thymocytes in vitro. Proc Natl Acad Sci USA 93:12456-12460, 1996
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 12456-12460
    • Platt, N.1    Suzuki, H.2    Kurihara, Y.3
  • 22
    • 0030858968 scopus 로고    scopus 로고
    • Macrophages lacking scavenger receptor a show a decrease in binding and uptake of acetylated low-density lipoprotein and of apoptotic thymocytes, but not of oxidatively damaged red blood cells
    • Terpstra V, Kondratenko N, Steinberg D: Macrophages lacking scavenger receptor A show a decrease in binding and uptake of acetylated low-density lipoprotein and of apoptotic thymocytes, but not of oxidatively damaged red blood cells. Proc Natl Acad Sci USA 94:8127-8131, 1997
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 8127-8131
    • Terpstra, V.1    Kondratenko, N.2    Steinberg, D.3
  • 23
    • 0030878251 scopus 로고    scopus 로고
    • Characterization of CLA-1, a human homologue of rodent scavenger receptor Bl, as a receptor for high density lipoprotein and apoptotic thymocytes
    • Murao K, Terpstra V, Green SR, et al: Characterization of CLA-1, a human homologue of rodent scavenger receptor Bl, as a receptor for high density lipoprotein and apoptotic thymocytes. J Biol Chem 272:17551-17557, 1997
    • (1997) J Biol Chem , vol.272 , pp. 17551-17557
    • Murao, K.1    Terpstra, V.2    Green, S.R.3
  • 24
    • 0028929745 scopus 로고
    • Recognition of oxidatively damaged and apoptotic cells by an oxidized low density lipoprotein receptor on mouse peritoneal macrophages: A role of membrane phopshatidylserine
    • Sambrano GR, Steinberg D: Recognition of oxidatively damaged and apoptotic cells by an oxidized low density lipoprotein receptor on mouse peritoneal macrophages: A role of membrane phopshatidylserine. Proc Natl Acad Sci USA 92:1396-1400, 1995
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 1396-1400
    • Sambrano, G.R.1    Steinberg, D.2
  • 25
    • 0028972471 scopus 로고
    • β2-Glycoprotein I is a major protein associated with very rapidly cleared liposomes in vivo, suggesting a significant role in the immune clearance of "non-self" particles
    • Chonn A, Semple SC, Cullis PR: β2-Glycoprotein I is a major protein associated with very rapidly cleared liposomes in vivo, suggesting a significant role in the immune clearance of "non-self" particles. J Biol Chem 25845-25849, 1995
    • (1995) J Biol Chem 25845-25849
    • Chonn, A.1    Semple, S.C.2    Cullis, P.R.3
  • 26
    • 0028891783 scopus 로고
    • Apoptosis, oncosis, and necrosis: An overview of cell death
    • Majno G, Joris I: Apoptosis, oncosis, and necrosis: An overview of cell death. Am J Pathol 146:3-15, 1995
    • (1995) Am J Pathol , vol.146 , pp. 3-15
    • Majno, G.1    Joris, I.2
  • 27
    • 0010431403 scopus 로고
    • Cell death in embryonic development
    • Potten CS (ed): New York, NY, Oxford University Press
    • Snow MHL: Cell death in embryonic development, in Potten CS (ed): Perspectives in Mammalian Cell Death. New York, NY, Oxford University Press, 1987, pp 202-287.
    • (1987) Perspectives in Mammalian Cell Death , pp. 202-287
    • Snow, M.H.L.1
  • 28
    • 0028818755 scopus 로고
    • Signals for cell death and survival: A two step mechanism for cavitation in the vertebrate embryo
    • Coucouvanis E, Martin OH: Signals for cell death and survival: A two step mechanism for cavitation in the vertebrate embryo. Cell 83:279-400, 1995
    • (1995) Cell , vol.83 , pp. 279-400
    • Coucouvanis, E.1    Martin, O.H.2
  • 29
    • 0026504147 scopus 로고
    • Social controls on cell survival and cell death
    • Raff M: Social controls on cell survival and cell death. Nature 356:397-400, 1992
    • (1992) Nature , vol.356 , pp. 397-400
    • Raff, M.1
  • 30
    • 33645870788 scopus 로고
    • Apoptosis in metanephric development
    • Koseki C, Herzlinger D, Al-Awqati Q: Apoptosis in metanephric development. Cell 81:9-12, 1992
    • (1992) Cell , vol.81 , pp. 9-12
    • Koseki, C.1    Herzlinger, D.2    Al-Awqati, Q.3
  • 31
    • 0030892234 scopus 로고    scopus 로고
    • Apoptosis by death factor
    • Nagata S: Apoptosis by death factor. Cell 88:355-365, 1997
    • (1997) Cell , vol.88 , pp. 355-365
    • Nagata, S.1
  • 32
    • 0028932731 scopus 로고
    • The CTL's kiss of death
    • Berke G: The CTL's kiss of death. Cell 81:9-12, 1995
    • (1995) Cell , vol.81 , pp. 9-12
    • Berke, G.1
  • 33
    • 0028362689 scopus 로고
    • Apoptosis and steroid hormones
    • Thompson E: Apoptosis and steroid hormones. Mol Endocrinol 8:665-673, 1994
    • (1994) Mol Endocrinol , vol.8 , pp. 665-673
    • Thompson, E.1
  • 34
    • 0026769457 scopus 로고
    • Induction of apoptosis in cultured hepatocytes and in regressing liver by transforming growth factor β1
    • Oberhammer F, Pavelka M, Sharma S, et al: Induction of apoptosis in cultured hepatocytes and in regressing liver by transforming growth factor β1. Proc Natl Acad Sci 89:5408-5412, 1992
    • (1992) Proc Natl Acad Sci , vol.89 , pp. 5408-5412
    • Oberhammer, F.1    Pavelka, M.2    Sharma, S.3
  • 35
    • 0030031398 scopus 로고    scopus 로고
    • Angiotensin type 2 receptor mediates programmed cell death
    • Yamada T, Horiuchi M, Dzau VJ: Angiotensin type 2 receptor mediates programmed cell death. Proc Natl Acad Sci USA 93:156-160, 1996
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 156-160
    • Yamada, T.1    Horiuchi, M.2    Dzau, V.J.3
  • 36
    • 0026713818 scopus 로고
    • Cytotoxic activity of tumor necrosis factor is mediated by early damage of mitochondrial functions: Evidence for the involvement of mitochondrial radical generation
    • Schulze-Osthoff K, Bakker A, Vanhaesebroeck B, et al: Cytotoxic activity of tumor necrosis factor is mediated by early damage of mitochondrial functions: Evidence for the involvement of mitochondrial radical generation. J Biol Chem 267:5317-5323, 1992
    • (1992) J Biol Chem , vol.267 , pp. 5317-5323
    • Schulze-Osthoff, K.1    Bakker, A.2    Vanhaesebroeck, B.3
  • 38
    • 0026048714 scopus 로고
    • The pathogenesis of sepsis
    • Bone R: The pathogenesis of sepsis. Ann Int Med 115:457-469, 1991
    • (1991) Ann Int Med , vol.115 , pp. 457-469
    • Bone, R.1
  • 39
    • 0030460595 scopus 로고    scopus 로고
    • Regulation of Fas and Fas ligand expression in cultured murine renal cells and in the kidney during endotoxemia
    • Ortiz-Arduan A, Danoff TM, Kalluri R, et al: Regulation of Fas and Fas ligand expression in cultured murine renal cells and in the kidney during endotoxemia. Am J Physiol 271:F1193-F1201, 1996
    • (1996) Am J Physiol , vol.271
    • Ortiz-Arduan, A.1    Danoff, T.M.2    Kalluri, R.3
  • 40
    • 0031062401 scopus 로고    scopus 로고
    • Expression of apoptosis-regulatory genes in renal proximal tubular epithelial cells exposed to high ambient glucose and in diabetic kidneys
    • Ortiz A, Ziyadeh F, Neilson E: Expression of apoptosis-regulatory genes in renal proximal tubular epithelial cells exposed to high ambient glucose and in diabetic kidneys. J Inv Med 45:50-56, 1997
    • (1997) J Inv Med , vol.45 , pp. 50-56
    • Ortiz, A.1    Ziyadeh, F.2    Neilson, E.3
  • 41
    • 0026612306 scopus 로고
    • ras by transforming growth factor β in epithelial cells
    • ras by transforming growth factor β in epithelial cells. J Biol Chem 267:5029-5031, 1992
    • (1992) J Biol Chem , vol.267 , pp. 5029-5031
    • Morris Sl, M.K.M.1
  • 42
    • 0028337567 scopus 로고
    • The emerging role of transforming growth factor-β in kidney diseases
    • Sharma K, Ziyadeh F: The emerging role of transforming growth factor-β in kidney diseases. Am J Physiol 266:F829-F842, 1994
    • (1994) Am J Physiol , vol.266
    • Sharma, K.1    Ziyadeh, F.2
  • 43
    • 0005600787 scopus 로고
    • The TNFR2-TRAF signaling complex contains two novel proteins related to baculoviral inhibitors of apoptosis
    • Rothe M, Pan M-G, Wenzel WJ, et al: The TNFR2-TRAF signaling complex contains two novel proteins related to baculoviral inhibitors of apoptosis. Cell 274:782-784, 1995
    • (1995) Cell , vol.274 , pp. 782-784
    • Rothe, M.1    Pan, M.-G.2    Wenzel, W.J.3
  • 44
    • 0026642195 scopus 로고
    • Induction of apoptosis in fibroblasts by c-myc protein
    • Evan G, Wyllie A, Gilbert C, et al: Induction of apoptosis in fibroblasts by c-myc protein. Cell 69:119-128, 1992
    • (1992) Cell , vol.69 , pp. 119-128
    • Evan, G.1    Wyllie, A.2    Gilbert, C.3
  • 45
    • 0022996750 scopus 로고
    • IL-2 addiction: Withdrawal of growth factor activates a suicide program in dependent T cells
    • Duke RC, Cohen JJ: IL-2 addiction: Withdrawal of growth factor activates a suicide program in dependent T cells. Lymphokine Res 5:289-299, 1986
    • (1986) Lymphokine Res , vol.5 , pp. 289-299
    • Duke, R.C.1    Cohen, J.J.2
  • 46
    • 0027516937 scopus 로고
    • Role of growth factors in regulation of renal growth
    • Hammerman M, O'Shea M, Miller S: Role of growth factors in regulation of renal growth. Annu Rev Physiol 55:305-321, 1993
    • (1993) Annu Rev Physiol , vol.55 , pp. 305-321
    • Hammerman, M.1    O'Shea, M.2    Miller, S.3
  • 47
    • 0030665658 scopus 로고    scopus 로고
    • Lysophosphatidic acid: A novel growth and survival factor for renal proximal tubular cells
    • Levine JS, Koh JS, Triaca V, et al: Lysophosphatidic acid: a novel growth and survival factor for renal proximal tubular cells. Am J Physiol 273:F575-F585, 1997
    • (1997) Am J Physiol , vol.273
    • Levine, J.S.1    Koh, J.S.2    Triaca, V.3
  • 48
    • 0028803728 scopus 로고
    • Alterations in cellular adhesion and apoptosis in epithelial cells overexpressing prostaglandin endoperoxide synthase 2
    • Tsujii M, DuBois R: Alterations in cellular adhesion and apoptosis in epithelial cells overexpressing prostaglandin endoperoxide synthase 2. Cell 83:493-501, 1995
    • (1995) Cell , vol.83 , pp. 493-501
    • Tsujii, M.1    DuBois, R.2
  • 49
    • 0028057613 scopus 로고
    • Disruption of epithelial cell-matrix interactions induces apoptosis
    • Frisch SM, Francis H: Disruption of epithelial cell-matrix interactions induces apoptosis. J Cell Biol 124:619-626, 1994
    • (1994) J Cell Biol , vol.124 , pp. 619-626
    • Frisch, S.M.1    Francis, H.2
  • 51
    • 0027451706 scopus 로고
    • The extracellular matrix as a survival factor
    • Meredith J, Fazeli B, Schwartz M: The extracellular matrix as a survival factor. Mol Biol Cell 4:953-961, 1993
    • (1993) Mol Biol Cell , vol.4 , pp. 953-961
    • Meredith, J.1    Fazeli, B.2    Schwartz, M.3
  • 52
    • 0028987936 scopus 로고
    • Integrins and signal transduction pathways: The road taken
    • Clark EA, Brugge JS: Integrins and signal transduction pathways: The road taken. Science 268:233-239, 1995
    • (1995) Science , vol.268 , pp. 233-239
    • Clark, E.A.1    Brugge, J.S.2
  • 53
    • 0031452520 scopus 로고    scopus 로고
    • Effect of integrins on proliferation and apoptosis of renal epithelial cells after acute injury
    • Wijesekara DS, Zamara MJ, Palier MS: Effect of integrins on proliferation and apoptosis of renal epithelial cells after acute injury. Kidney Int 52:1511-1520, 1997
    • (1997) Kidney Int , vol.52 , pp. 1511-1520
    • Wijesekara, D.S.1    Zamara, M.J.2    Palier, M.S.3
  • 54
    • 33645857467 scopus 로고    scopus 로고
    • Apoptosis of renal tubular cells in suspension is prevented by cadherin-mediated aggregation: Implications for cast formation in acute renal failure
    • abstr
    • Bergin E, Levine JS, Lieberthal W: Apoptosis of renal tubular cells in suspension is prevented by cadherin-mediated aggregation: Implications for cast formation in acute renal failure. J Am Soc Nephrol 8:583a, 1997 (abstr)
    • (1997) J Am Soc Nephrol , vol.8
    • Bergin, E.1    Levine, J.S.2    Lieberthal, W.3
  • 55
    • 0028258533 scopus 로고
    • Apoptosis induced by inhibition of intercellular contact
    • Bates R, Buret A, Helden KV, et al: Apoptosis induced by inhibition of intercellular contact. J Cell Biol 125:403-415, 1994
    • (1994) J Cell Biol , vol.125 , pp. 403-415
    • Bates, R.1    Buret, A.2    Helden, K.V.3
  • 56
    • 0028918891 scopus 로고
    • In vivo analysis of cadherin function in the mouse intestinal epithelium: Essential roles in adhesion, maintenance of differentiation, and regulation of programmed cell death
    • Hermiston ML, Gordon JI: In vivo analysis of cadherin function in the mouse intestinal epithelium: Essential roles in adhesion, maintenance of differentiation, and regulation of programmed cell death. J Cell Biol 129:489-506, 1995
    • (1995) J Cell Biol , vol.129 , pp. 489-506
    • Hermiston, M.L.1    Gordon, J.I.2
  • 57
    • 0028910006 scopus 로고
    • Regulation of transcription by the rat EOF gene promoter in normal and ischemic murine kidney cells
    • Price PM, Megyesi J, Saggi S, et al: Regulation of transcription by the rat EOF gene promoter in normal and ischemic murine kidney cells. Am J Physiol 268:F664-F670, 1995
    • (1995) Am J Physiol , vol.268
    • Price, P.M.1    Megyesi, J.2    Saggi, S.3
  • 58
    • 0026329275 scopus 로고
    • Expression of cytokine-like genes JE and KC is increased during renal ischemia
    • Safirstein R, Megyesi J, Saggi SJ, et al: Expression of cytokine-like genes JE and KC is increased during renal ischemia. Am J Physiol 261:F1095-F1101, 1991
    • (1991) Am J Physiol , vol.261
    • Safirstein, R.1    Megyesi, J.2    Saggi, S.J.3
  • 59
    • 0028471151 scopus 로고
    • Therapeutic use of growth factors in renal failure
    • Hammerman MR, Miller SB: Therapeutic use of growth factors in renal failure. J Am Soc Nephrol 5:1-11, 1994
    • (1994) J Am Soc Nephrol , vol.5 , pp. 1-11
    • Hammerman, M.R.1    Miller, S.B.2
  • 60
    • 0028055171 scopus 로고
    • Functional and cytoskeletal changes induced by sublethal injury in proximal tubular epithelial cells
    • Kroshian VM, Sheridan A, Lieberthal W: Functional and cytoskeletal changes induced by sublethal injury in proximal tubular epithelial cells. Am J Physiol 266:F21-F30, 1994
    • (1994) Am J Physiol , vol.266
    • Kroshian, V.M.1    Sheridan, A.2    Lieberthal, W.3
  • 61
    • 0031452520 scopus 로고    scopus 로고
    • Effects of integrins on proliferation and apoptosis of renal epithelial cells after acute injury
    • Wijesekera DS, Zarama MJ, Palier MS: Effects of integrins on proliferation and apoptosis of renal epithelial cells after acute injury. Kidney Int 52:1511-1520, 1996
    • (1996) Kidney Int , vol.52 , pp. 1511-1520
    • Wijesekera, D.S.1    Zarama, M.J.2    Palier, M.S.3
  • 62
    • 0030941458 scopus 로고    scopus 로고
    • P53, the cellular gatekeeper for growth and division
    • Levine A: p53, the cellular gatekeeper for growth and division. Cell 323-331, 1997
    • (1997) Cell , pp. 323-331
    • Levine, A.1
  • 63
    • 0027319521 scopus 로고
    • P53 is required for radiation-induced apoptosis in mouse thymocytes
    • Lowe S, Schmitt E, Smith S, et al: p53 is required for radiation-induced apoptosis in mouse thymocytes. Nature 362:847-862, 1993
    • (1993) Nature , vol.362 , pp. 847-862
    • Lowe, S.1    Schmitt, E.2    Smith, S.3
  • 64
    • 0027258466 scopus 로고
    • Thymocyte apoptosis induced by p53-dependent and independent pathways
    • Clarke AR, Purdie CA, Harrison DJ, et al: Thymocyte apoptosis induced by p53-dependent and independent pathways. Nature 362:849-852, 1993
    • (1993) Nature , vol.362 , pp. 849-852
    • Clarke, A.R.1    Purdie, C.A.2    Harrison, D.J.3
  • 65
    • 0029881461 scopus 로고    scopus 로고
    • Mechanisms of death induced by cisplatin in proximal tubular epithelial cells: Apoptosis vs. necrosis
    • Lieberthal W, Triaca V, Levine J: Mechanisms of death induced by cisplatin in proximal tubular epithelial cells: Apoptosis vs. necrosis. Am J Physiol 270:F700-708, 1996
    • (1996) Am J Physiol , vol.270
    • Lieberthal, W.1    Triaca, V.2    Levine, J.3
  • 66
    • 0028943734 scopus 로고
    • Apoptosis in the pathogenesis and treatment of disease
    • Thompson C: Apoptosis in the pathogenesis and treatment of disease. Science 267:1456-1462, 1995
    • (1995) Science , vol.267 , pp. 1456-1462
    • Thompson, C.1
  • 68
    • 0027967063 scopus 로고
    • Reperfusion injury induces apoptosis in rabbit cardiomyocytes
    • Gottlieb RA, Burleson KO, Kloner RA, et al: Reperfusion injury induces apoptosis in rabbit cardiomyocytes. J Clin Invest 94:1621-1628, 1994
    • (1994) J Clin Invest , vol.94 , pp. 1621-1628
    • Gottlieb, R.A.1    Burleson, K.O.2    Kloner, R.A.3
  • 69
    • 0031989121 scopus 로고    scopus 로고
    • Graded ATP depletion can induce apoptosis or necrosis of cultured mouse proximal tubular cells
    • Lieberthal W, Menza SA, Levine JS: Graded ATP depletion can induce apoptosis or necrosis of cultured mouse proximal tubular cells. Am J Phyiol 274:F315-F327, 1998
    • (1998) Am J Phyiol , vol.274
    • Lieberthal, W.1    Menza, S.A.2    Levine, J.S.3
  • 70
    • 0023861035 scopus 로고
    • Energy thresholds that determine membrane integrity and injury in a renal epithelial cell line (LLC-PK1)
    • Venkatachalam MA, Patel YJ, Kreisberg JI, et al: Energy thresholds that determine membrane integrity and injury in a renal epithelial cell line (LLC-PK1). J Clin Invest 81:745-759, 1988
    • (1988) J Clin Invest , vol.81 , pp. 745-759
    • Venkatachalam, M.A.1    Patel, Y.J.2    Kreisberg, J.I.3
  • 71
    • 0027378020 scopus 로고
    • Renal mouse proximal tubular cells are more susceptible than MDCK cells to chemical anoxia
    • Sheridan A, Schwanz J, Kroshian V, et al: Renal mouse proximal tubular cells are more susceptible than MDCK cells to chemical anoxia. Am J Physiol 265:F323-F350, 1993
    • (1993) Am J Physiol , vol.265
    • Sheridan, A.1    Schwanz, J.2    Kroshian, V.3
  • 72
    • 0031888955 scopus 로고    scopus 로고
    • A caspase-activated endonuclease that degrades DNA during apoptosis, and its inhibitor ICAD
    • Enari M, Sakahira H, Yokayama H, et al: A caspase-activated endonuclease that degrades DNA during apoptosis, and its inhibitor ICAD. Nature 391:43-50, 1998
    • (1998) Nature , vol.391 , pp. 43-50
    • Enari, M.1    Sakahira, H.2    Yokayama, H.3
  • 73
    • 0031938419 scopus 로고    scopus 로고
    • An endonuclease at last
    • Wyllie A: An endonuclease at last. Nature 391:20-21, 1998
    • (1998) Nature , vol.391 , pp. 20-21
    • Wyllie, A.1
  • 74
    • 0021346318 scopus 로고
    • Chromatin cleavage in apoptosis: Association with condensed chromatin morphology and dependence on macromolecular sythnesis
    • Wyllie A, Morris R, Smith A, et al: Chromatin cleavage in apoptosis: Association with condensed chromatin morphology and dependence on macromolecular sythnesis. J Pathol 142:67-77, 1984
    • (1984) J Pathol , vol.142 , pp. 67-77
    • Wyllie, A.1    Morris, R.2    Smith, A.3
  • 75
    • 0029042718 scopus 로고
    • Nuclear changes in apoptosis
    • Earnshaw W: Nuclear changes in apoptosis. Curr Opin Cell Biol 7:337-343, 1995
    • (1995) Curr Opin Cell Biol , vol.7 , pp. 337-343
    • Earnshaw, W.1
  • 76
    • 0029022365 scopus 로고
    • Involvement of an ICE-like protease in Fas-mediated apoptosis
    • Enari M, Hug H, Nagata S: Involvement of an ICE-like protease in Fas-mediated apoptosis. Nature 375:78-81, 1995
    • (1995) Nature , vol.375 , pp. 78-81
    • Enari, M.1    Hug, H.2    Nagata, S.3
  • 77
    • 0027513268 scopus 로고
    • Apoptosis
    • Cohen J: Apoptosis. Immunol Today 14:126-130, 1993
    • (1993) Immunol Today , vol.14 , pp. 126-130
    • Cohen, J.1
  • 78
    • 0032498625 scopus 로고    scopus 로고
    • Apoptotic membrane blebbing is regulated by myosin light chain phopshorylation
    • Mills JC, Stone NL, Erhardt J, et al: Apoptotic membrane blebbing is regulated by myosin light chain phopshorylation. J Cell Biol 140:627-635, 1998
    • (1998) J Cell Biol , vol.140 , pp. 627-635
    • Mills, J.C.1    Stone, N.L.2    Erhardt, J.3
  • 79
    • 0030918572 scopus 로고    scopus 로고
    • Membrane and morphologic changes in apoptotic cells regulated by caspase-mediated activation of PAK2
    • Rudel T, Bokoch GM: Membrane and morphologic changes in apoptotic cells regulated by caspase-mediated activation of PAK2. Science 276:1571-1574, 1997
    • (1997) Science , vol.276 , pp. 1571-1574
    • Rudel, T.1    Bokoch, G.M.2
  • 80
    • 0025761170 scopus 로고
    • The cell biology of ischemic renal injury
    • Weinberg JM: The cell biology of ischemic renal injury. Kidney Int 39:476-500, 1991
    • (1991) Kidney Int , vol.39 , pp. 476-500
    • Weinberg, J.M.1
  • 81
    • 0028149786 scopus 로고
    • Checkpoints of dueling dimers foil death wishes
    • Oltavi ZN, Korsmeyer SJ: Checkpoints of dueling dimers foil death wishes. Cell 79:189-192, 1994
    • (1994) Cell , vol.79 , pp. 189-192
    • Oltavi, Z.N.1    Korsmeyer, S.J.2
  • 82
    • 0028040019 scopus 로고
    • Bcl-2 and the regulation of programmed cell death
    • Reed J: Bcl-2 and the regulation of programmed cell death. J Cell Biol 124:1-6, 1994
    • (1994) J Cell Biol , vol.124 , pp. 1-6
    • Reed, J.1
  • 83
    • 0027318190 scopus 로고
    • BCl-2 inhibits death of central neural cells induced by multiple agents
    • Zhong L-T, Sarafian T, Kane D, et al: BCl-2 inhibits death of central neural cells induced by multiple agents. Proc Natl Acad Sci USA 90:4533-4537, 1993
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 4533-4537
    • Zhong, L.-T.1    Sarafian, T.2    Kane, D.3
  • 84
    • 0028847915 scopus 로고
    • Cloning and functional analysis of BAG-1: A novel Bcl-2 binding protein with anti-cell death activity
    • Takayama S, Sato T, Krajewski S, et al: Cloning and functional analysis of BAG-1: A novel Bcl-2 binding protein with anti-cell death activity. Cell 80:279-284, 1995
    • (1995) Cell , vol.80 , pp. 279-284
    • Takayama, S.1    Sato, T.2    Krajewski, S.3
  • 85
    • 0027282044 scopus 로고
    • Bcl-x, a Bcl-2 related gene that functions as a dominant regulator of apoptotic cell death
    • Boise LH, Gonzalez-Garcia M, Bostema CE, et al: Bcl-x, a Bcl-2 related gene that functions as a dominant regulator of apoptotic cell death. Cell 74:597-608, 1993
    • (1993) Cell , vol.74 , pp. 597-608
    • Boise, L.H.1    Gonzalez-Garcia, M.2    Bostema, C.E.3
  • 86
    • 0028809209 scopus 로고
    • Bad, a heterodimeric partner for Bcl-xL and Bcl-2 displaces Bax and promotes cell death
    • Yang E, Zha J, Jockei J, et al: Bad, a heterodimeric partner for Bcl-xL and Bcl-2 displaces Bax and promotes cell death. Cell 80:285-291, 1995
    • (1995) Cell , vol.80 , pp. 285-291
    • Yang, E.1    Zha, J.2    Jockei, J.3
  • 87
    • 0028904163 scopus 로고
    • Modulation of apoptosis by the widely distributed Bcl-2 homologue Bak
    • Kiefer MC, Brauer MJ, Powers VC, et al: Modulation of apoptosis by the widely distributed Bcl-2 homologue Bak. Nature 374:736-739, 1995
    • (1995) Nature , vol.374 , pp. 736-739
    • Kiefer, M.C.1    Brauer, M.J.2    Powers, V.C.3
  • 88
    • 0027166048 scopus 로고
    • Bcl-2 heterodimerizes in vivo with a conserved homolog, Bax, that accelerates programmed cell death
    • Oltavi ZN, Nilliman CL, Korsmeyer SJ: Bcl-2 heterodimerizes in vivo with a conserved homolog, Bax, that accelerates programmed cell death. Cell 74:609-619, 1993
    • (1993) Cell , vol.74 , pp. 609-619
    • Oltavi, Z.N.1    Nilliman, C.L.2    Korsmeyer, S.J.3
  • 89
    • 0029927422 scopus 로고
    • The role of proteases during apoptosis
    • Patel T, Gores GJ, Kaufmann SH: The role of proteases during apoptosis. FASEB 10:587-597, 1966
    • (1966) FASEB , vol.10 , pp. 587-597
    • Patel, T.1    Gores, G.J.2    Kaufmann, S.H.3
  • 90
    • 0030702084 scopus 로고    scopus 로고
    • Caspases: Intracellular signalling by proteolysis
    • Salvesen GS, Dixit VM: Caspases: Intracellular signalling by proteolysis. Cell 91:443-446, 1997
    • (1997) Cell , vol.91 , pp. 443-446
    • Salvesen, G.S.1    Dixit, V.M.2
  • 93
    • 0029787268 scopus 로고    scopus 로고
    • Molecular ordering of apoptotic mammalian CED-3/ICE-like proteases
    • Orth K, O'Rourke K, Salvesen GS, et al: Molecular ordering of apoptotic mammalian CED-3/ICE-like proteases. J Biol Chem 271:20977-20980, 1996
    • (1996) J Biol Chem , vol.271 , pp. 20977-20980
    • Orth, K.1    O'Rourke, K.2    Salvesen, G.S.3
  • 94
    • 0032576641 scopus 로고    scopus 로고
    • Death cycle and swiss army knives
    • Hengartner MO: Death cycle and swiss army knives. Nature 391:441-442, 1998
    • (1998) Nature , vol.391 , pp. 441-442
    • Hengartner, M.O.1
  • 95
    • 0030581151 scopus 로고    scopus 로고
    • Induction of apoptotic program in cell-free extracts: Requirement for dATP and cytochrome c
    • Liu X, Naekyung C, Yang J, et al: Induction of apoptotic program in cell-free extracts: Requirement for dATP and cytochrome c. Cell 86:147-157, 1996
    • (1996) Cell , vol.86 , pp. 147-157
    • Liu, X.1    Naekyung, C.2    Yang, J.3
  • 96
    • 0032576757 scopus 로고    scopus 로고
    • Injected cytochrome c induced apoptosis
    • Zhivotovsky B, Orrenius S, Brustugun OT, et al: Injected cytochrome c induced apoptosis. Nature 391:449-450, 1998
    • (1998) Nature , vol.391 , pp. 449-450
    • Zhivotovsky, B.1    Orrenius, S.2    Brustugun, O.T.3
  • 97
    • 0029068871 scopus 로고
    • Identification and inhibition of the ICE/CED-3 protease necessary for mammalian apoptosis
    • Nicholson DW, Ali A, Thombeny NA, et al: Identification and inhibition of the ICE/CED-3 protease necessary for mammalian apoptosis. Nature 376:37-43, 1995
    • (1995) Nature , vol.376 , pp. 37-43
    • Nicholson, D.W.1    Ali, A.2    Thombeny, N.A.3
  • 98
    • 0030798072 scopus 로고    scopus 로고
    • Rple of caspases (ICE/CED3 proteases) in DNA damage and cell death in response to a mitochondrial inhibitor, antimycin a
    • Kaushal OP, Ueda N, Shah SV: Rple of caspases (ICE/CED3 proteases) in DNA damage and cell death in response to a mitochondrial inhibitor, antimycin A. Kidney Int 52:438-445, 1997
    • (1997) Kidney Int , vol.52 , pp. 438-445
    • Kaushal, O.P.1    Ueda, N.2    Shah, S.V.3
  • 99
    • 0026551591 scopus 로고
    • Morphologic, biochemical, and molecular evidence of apoptosis during the reperfusion phase after brief periods of renal ischemia
    • Schumer M, Colombel MC, Sawchuk TS, et al: Morphologic, biochemical, and molecular evidence of apoptosis during the reperfusion phase after brief periods of renal ischemia. Am J Pathol 140:831-838, 1992
    • (1992) Am J Pathol , vol.140 , pp. 831-838
    • Schumer, M.1    Colombel, M.C.2    Sawchuk, T.S.3
  • 100
    • 0027250758 scopus 로고
    • Apoptosis and cell desquamation in repair process of ischemic tubular necrosis
    • Shimizu A, Yamanaka N: Apoptosis and cell desquamation in repair process of ischemic tubular necrosis. Virchows Archiv Cell Pathol 64:171-180, 1993
    • (1993) Virchows Archiv Cell Pathol , vol.64 , pp. 171-180
    • Shimizu, A.1    Yamanaka, N.2
  • 101
    • 0030848745 scopus 로고    scopus 로고
    • Expression of bcl-2 and bax in regenerating rat remnal tubules following ischemic injury
    • Basile DP, Liapis H, Hammerman MR: Expression of bcl-2 and bax in regenerating rat remnal tubules following ischemic injury. Am J Physiol 272:F640-F647, 1997
    • (1997) Am J Physiol , vol.272
    • Basile, D.P.1    Liapis, H.2    Hammerman, M.R.3
  • 102
    • 0029957252 scopus 로고    scopus 로고
    • Uninephrectomy reduces apoptotic cell death and enhances renal tubular cell regeneration in ischemic ARF in rats
    • Nakajima T, Miyaji T, Kato A, et al: Uninephrectomy reduces apoptotic cell death and enhances renal tubular cell regeneration in ischemic ARF in rats. Am J Physiol 271:F846-F853, 1996
    • (1996) Am J Physiol , vol.271
    • Nakajima, T.1    Miyaji, T.2    Kato, A.3
  • 103
    • 0031605321 scopus 로고    scopus 로고
    • 1 angiotensin II receptors in renal ischemic injury
    • 1 angiotensin II receptors in renal ischemic injury. Am J Physiol 274:F79-F90, 1998
    • (1998) Am J Physiol , vol.274
    • Kontogiannis, J.1    Burns, K.D.2


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