메뉴 건너뛰기




Volumn 4, Issue 6, 2002, Pages 915-924

Apoptotic pathways of oxidative damage to renal tubular epithelial cells

Author keywords

[No Author keywords available]

Indexed keywords

AMINOGLYCOSIDE ANTIBIOTIC AGENT; BENZOIC ACID; BENZYLOXYCARBONYLVALYLALANYLASPARTYL FLUOROMETHYL KETONE; CASPASE; CASPASE 3 INHIBITOR; CASPASE INHIBITOR; CERAMIDE; CISPLATIN; CONTRAST MEDIUM; DIMETHYL SULFOXIDE; DIMETHYLTHIOUREA; DNA FRAGMENT; ENDONUCLEASE; GENTAMICIN; GLYCEROL; HYDROGEN PEROXIDE; MANNITOL; REACTIVE OXYGEN METABOLITE; SCAVENGER; TOXIN;

EID: 0036936654     PISSN: 15230864     EISSN: None     Source Type: Journal    
DOI: 10.1089/152308602762197452     Document Type: Review
Times cited : (64)

References (92)
  • 1
    • 0025000771 scopus 로고
    • Vitamin E and selenium in gentamicin nephrotoxicity
    • Ademuyiwa O, Ngaha EO, and Ubah FO. Vitamin E and selenium in gentamicin nephrotoxicity. Hum Exp Toxicol 9: 281-288, 1990.
    • (1990) Hum Exp Toxicol , vol.9 , pp. 281-288
    • Ademuyiwa, O.1    Ngaha, E.O.2    Ubah, F.O.3
  • 2
    • 12244273453 scopus 로고    scopus 로고
    • Acute renal failure associated with cancer chemotherapy
    • edited by Molitoris BA and Finn WE Philadelphia, PA: W.B. Saunders Company, Chapter 28
    • Agraharkar M, Guba SC, and Safirstein RL. Acute renal failure associated with cancer chemotherapy. In: Acute Renal Failure: A Companion to Brenner and Rector's The Kidney, edited by Molitoris BA and Finn WE Philadelphia, PA: W.B. Saunders Company, 2001, Chapter 28, pp. 365-375.
    • (2001) Acute Renal Failure: A Companion to Brenner and Rector's The Kidney , pp. 365-375
    • Agraharkar, M.1    Guba, S.C.2    Safirstein, R.L.3
  • 3
    • 0025247903 scopus 로고
    • Apoptosis. The role of the endonuclease
    • Arends MJ, Morris RG, and Wyllie AH. Apoptosis. The role of the endonuclease. Am J Pathol 136: 593-608, 1990.
    • (1990) Am J Pathol , vol.136 , pp. 593-608
    • Arends, M.J.1    Morris, R.G.2    Wyllie, A.H.3
  • 5
    • 12244299611 scopus 로고    scopus 로고
    • Acute renal failure associated with occupational and environmental settings
    • Philadelphia, PA: W.B. Saunders Company
    • Bach PH. Acute renal failure associated with occupational and environmental settings. In: Acute Renal Failure: A Companion to Brenner and Rector's The Kidney, Philadelphia, PA: W.B. Saunders Company, 2001, pp. 414-424.
    • (2001) Acute Renal Failure: A Companion to Brenner and Rector's The Kidney , pp. 414-424
    • Bach, P.H.1
  • 6
    • 0031933285 scopus 로고    scopus 로고
    • In vitro and in vivo evidence suggesting a role for iron in cisplatin-induced nephrotoxicity
    • Baliga R, Zhang Z, Baliga M, Ueda N, and Shah SV In vitro and in vivo evidence suggesting a role for iron in cisplatin-induced nephrotoxicity. Kidney Int 53: 394-401, 1998.
    • (1998) Kidney Int , vol.53 , pp. 394-401
    • Baliga, R.1    Zhang, Z.2    Baliga, M.3    Ueda, N.4    Shah, S.V.5
  • 7
  • 8
    • 0030848745 scopus 로고    scopus 로고
    • Expression of bcl-2 and bax in regenerating rat renal tubules following ischemic injury
    • Basile DP, Liapis H, and Hammerman MR. Expression of bcl-2 and bax in regenerating rat renal 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
  • 9
    • 0036205657 scopus 로고    scopus 로고
    • DNase I-like endonuclease in rat kidney cortex activated during ischemia/reperfusion injury
    • Basnakian AG, Ueda N, Kaushal GP, Mikhailova MV, and Shah SV. DNase I-like endonuclease in rat kidney cortex activated during ischemia/reperfusion injury. J Am Soc Nephrol 13: 1000-1007, 2002.
    • (2002) J Am Soc Nephrol , vol.13 , pp. 1000-1007
    • Basnakian, A.G.1    Ueda, N.2    Kaushal, G.P.3    Mikhailova, M.V.4    Shah, S.V.5
  • 11
    • 0028099826 scopus 로고
    • Influence of iron, deferoxamine and ascorbic acid on gentamicin-induced nephrotoxicity in rats
    • Ben Ismail TH, Ali BH, and Bashir AA. Influence of iron, deferoxamine and ascorbic acid on gentamicin-induced nephrotoxicity in rats. Gen Pharmacol 25: 1249-1252, 1994.
    • (1994) Gen Pharmacol , vol.25 , pp. 1249-1252
    • Ben Ismail, T.H.1    Ali, B.H.2    Bashir, A.A.3
  • 12
    • 0029112931 scopus 로고
    • DNA strand breaks produced by oxidative stress in mammalian cells exhibit 3′-phosphoglycolate termini
    • Bertoncini CR and Meneghini R. DNA strand breaks produced by oxidative stress in mammalian cells exhibit 3′-phosphoglycolate termini. Nucleic Acids Res 23: 2995-3002, 1995.
    • (1995) Nucleic Acids Res , vol.23 , pp. 2995-3002
    • Bertoncini, C.R.1    Meneghini, R.2
  • 14
    • 51149212381 scopus 로고
    • Oxidation of α-diketones and α-keto-acids by hydrogen peroxide
    • Bunton CA. Oxidation of α-diketones and α-keto-acids by hydrogen peroxide. Nature 163: 444-451, 1949.
    • (1949) Nature , vol.163 , pp. 444-451
    • Bunton, C.A.1
  • 15
    • 84965248455 scopus 로고
    • Crush injuries with impairment of renal function
    • Bywaters EGL and Beall D. Crush injuries with impairment of renal function. Br Med J 1: 427-432, 1941.
    • (1941) Br Med J , vol.1 , pp. 427-432
    • Bywaters, E.G.L.1    Beall, D.2
  • 16
    • 0033105112 scopus 로고    scopus 로고
    • Removal by human apurinic/apyrimidinic endonuclease 1 (Ape 1) and Escherichia coli exonuclease III of 3′-phosphoglycolates from DNA treated with neocarzinostatin, calicheamicin, and gamma-radiation
    • Chaudhry MA, Dedon PC, Wilson DM 3rd, Demple B, and Weinfeld M. Removal by human apurinic/apyrimidinic endonuclease 1 (Ape 1) and Escherichia coli exonuclease III of 3′-phosphoglycolates from DNA treated with neocarzinostatin, calicheamicin, and gamma-radiation. Biochem Pharmacol 57: 531-538, 1999.
    • (1999) Biochem Pharmacol , vol.57 , pp. 531-538
    • Chaudhry, M.A.1    Dedon, P.C.2    Wilson D.M. III3    Demple, B.4    Weinfeld, M.5
  • 17
    • 0023655179 scopus 로고
    • Identification of a glucocorticoid-induced nuclease in thymocytes. A potential "lysis gene" product
    • Compton MM and Cidlowski JA. Identification of a glucocorticoid-induced nuclease in thymocytes. A potential "lysis gene" product. J Biol Chem 262: 8288-8292, 1987.
    • (1987) J Biol Chem , vol.262 , pp. 8288-8292
    • Compton, M.M.1    Cidlowski, J.A.2
  • 18
    • 0034717184 scopus 로고    scopus 로고
    • Involvement of sphingosine in mitochondria-dependent Fas-induced apoptosis of type II Jurkat T cells
    • Cuvillier O, Edsall L, and Spiegel S. Involvement of sphingosine in mitochondria-dependent Fas-induced apoptosis of type II Jurkat T cells. J Biol Chem 275: 15691-15700, 2000.
    • (2000) J Biol Chem , vol.275 , pp. 15691-15700
    • Cuvillier, O.1    Edsall, L.2    Spiegel, S.3
  • 20
    • 0033136706 scopus 로고    scopus 로고
    • Ischemia/reperfusion-induced IFN-gamma up-regulation: Involvement of IL-12 and IL-18
    • Daemen MA, van't Veer C, Wolfs TG, and Buurman WA. Ischemia/reperfusion-induced IFN-gamma up-regulation: Involvement of IL-12 and IL-18. J Immunol 162: 5506-5510, 1999.
    • (1999) J Immunol , vol.162 , pp. 5506-5510
    • Daemen, M.A.1    Van't Veer, C.2    Wolfs, T.G.3    Buurman, W.A.4
  • 21
    • 0032780169 scopus 로고    scopus 로고
    • Role of caspases in hypoxia-induced necrosis of rat renal proximal tubules
    • Edelstein CL, Shi Y, and Schrier RW. Role of caspases in hypoxia-induced necrosis of rat renal proximal tubules. J Am Soc Nephrol 10: 1940-1949, 1999.
    • (1999) J Am Soc Nephrol , vol.10 , pp. 1940-1949
    • Edelstein, C.L.1    Shi, Y.2    Schrier, R.W.3
  • 22
    • 0031888955 scopus 로고    scopus 로고
    • A caspase-activated DNase that degrades DNA during apoptosis, and its inhibitor ICAD
    • Enari M, Sakahira H, Yokoyama H, Okawa K, Iwamatsu A, and Nagata S. A caspase-activated DNase 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    Yokoyama, H.3    Okawa, K.4    Iwamatsu, A.5    Nagata, S.6
  • 23
    • 0033000804 scopus 로고    scopus 로고
    • Partial ATP depletion induces Fas- and caspase-mediated apoptosis in MDCK cells
    • Renal Physiol 45
    • Feldenberg LR, Thevananther S, Del Rio M, DeLeon M, and Devarajan P. Partial ATP depletion induces Fas- and caspase-mediated apoptosis in MDCK cells. Am J Physiol 276 (Renal Physiol 45): F837-F846, 1999.
    • (1999) Am J Physiol , vol.276
    • Feldenberg, L.R.1    Thevananther, S.2    Del Rio, M.3    DeLeon, M.4    Devarajan, P.5
  • 24
    • 0018263443 scopus 로고
    • The biology of oxygen radicals. The superoxide radical is an agent of oxygen toxicity; superoxide dismutases provide an important defense
    • Fridovich I. The biology of oxygen radicals. The superoxide radical is an agent of oxygen toxicity; superoxide dismutases provide an important defense. Science 201: 875-880, 1978.
    • (1978) Science , vol.201 , pp. 875-880
    • Fridovich, I.1
  • 27
    • 0024343694 scopus 로고
    • 2 generation by rat kidney in glycerol-induced renal failure
    • 2 generation by rat kidney in glycerol-induced renal failure. Am J Physiol 257: F440-F445, 1989.
    • (1989) Am J Physiol , vol.257
    • Guidet, B.1    Shah, S.V.2
  • 28
    • 0030034283 scopus 로고    scopus 로고
    • Endonuclease-induced DNA damage and cell death in chemical hypoxic injury to LLC-PK1 cells
    • Hagar H, Ueda N, and Shah SV. Endonuclease-induced DNA damage and cell death in chemical hypoxic injury to LLC-PK1 cells. Kidney Int 49: 355-361, 1996.
    • (1996) Kidney Int , vol.49 , pp. 355-361
    • Hagar, H.1    Ueda, N.2    Shah, S.V.3
  • 29
    • 0029736434 scopus 로고    scopus 로고
    • Role of reactive oxygen metabolites in DNA damage and cell death in chemical hypoxic injury to LLC-PK1 cells
    • Hagar H, Ueda N, and Shah SV. Role of reactive oxygen metabolites in DNA damage and cell death in chemical hypoxic injury to LLC-PK1 cells. Am J Physiol 271: F209-F215, 1996.
    • (1996) Am J Physiol , vol.271
    • Hagar, H.1    Ueda, N.2    Shah, S.V.3
  • 30
    • 0018856912 scopus 로고
    • Mitochondrial pyruvate transport and its hormonal regulation
    • Halestrap AP, Scott RD, and Thomas AP. Mitochondrial pyruvate transport and its hormonal regulation. Int J Biochem 11: 97-105, 1980.
    • (1980) Int J Biochem , vol.11 , pp. 97-105
    • Halestrap, A.P.1    Scott, R.D.2    Thomas, A.P.3
  • 31
    • 0025126555 scopus 로고
    • Role of free radicals and catalytic metal ions in human disease: An overview
    • Halliwell B and Gutteridge JMC. Role of free radicals and catalytic metal ions in human disease: An overview. Methods Enzymol 186: 1-85, 1990.
    • (1990) Methods Enzymol , vol.186 , pp. 1-85
    • Halliwell, B.1    Gutteridge, J.M.C.2
  • 33
    • 0002518026 scopus 로고
    • Renal circulatory and nephron function in experimental acute renal failure
    • edited by Brenner BM and Lazarus JM. Philadelphia, PA: W.B. Saunders Company
    • Hostetter TH, Wilkes BM, and Brenner BM. Renal circulatory and nephron function in experimental acute renal failure. In: Acute Renal Failure, edited by Brenner BM and Lazarus JM. Philadelphia, PA: W.B. Saunders Company, 1983, pp. 99-115.
    • (1983) Acute Renal Failure , pp. 99-115
    • Hostetter, T.H.1    Wilkes, B.M.2    Brenner, B.M.3
  • 34
    • 0000483242 scopus 로고
    • Toxic nephropathies
    • edited by Brenner BM and Rector J. Philadelphia, PA: W.B. Saunders Company
    • Humes HD and Weinberg JM. Toxic nephropathies. In: The Kidney, edited by Brenner BM and Rector J. Philadelphia, PA: W.B. Saunders Company, 1986, pp. 1491-1532.
    • (1986) The Kidney , pp. 1491-1532
    • Humes, H.D.1    Weinberg, J.M.2
  • 35
    • 0028706978 scopus 로고
    • An evaluation of renal tubular DNA laddering in response to oxygen deprivation and oxidant injury
    • Iwata M, Myerson D, Torok-Storb B, and Zager RA. An evaluation of renal tubular DNA laddering in response to oxygen deprivation and oxidant injury. J Am Soc Nephrol 5: 1307-1313, 1994.
    • (1994) J Am Soc Nephrol , vol.5 , pp. 1307-1313
    • Iwata, M.1    Myerson, D.2    Torok-Storb, B.3    Zager, R.A.4
  • 36
    • 0030798072 scopus 로고    scopus 로고
    • Role of caspases (ICE/CED 3 proteases) in DNA damage and cell death in response to a mitochondrial inhibitor, antimycin A
    • Kaushal GP, Ueda N, and Shah SV. Role of caspases (ICE/CED 3 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, G.P.1    Ueda, N.2    Shah, S.V.3
  • 37
    • 0031919843 scopus 로고    scopus 로고
    • Identification of caspase (ICE-like proteases) gene family in rat kidney and altered expression in ischemia/reperfusion injury
    • Renal Physiol 43
    • Kaushal GP, Singh AB, and Shah SV. Identification of caspase (ICE-like proteases) gene family in rat kidney and altered expression in ischemia/reperfusion injury. Am J Physiol 274 (Renal Physiol 43): F587-F595, 1998.
    • (1998) Am J Physiol , vol.274
    • Kaushal, G.P.1    Singh, A.B.2    Shah, S.V.3
  • 38
    • 0034778721 scopus 로고    scopus 로고
    • Role of caspases and their regulation by Akt/protein kinase B phosphorylation pathway in cisplatin-induced injury to renal tubular epithelial cells
    • Kaushal GP, Kaushal V, Hong X, and Shah SV. Role of caspases and their regulation by Akt/protein kinase B phosphorylation pathway in cisplatin-induced injury to renal tubular epithelial cells. Kidney Int 60: 1726-1736, 2001.
    • (2001) Kidney Int , vol.60 , pp. 1726-1736
    • Kaushal, G.P.1    Kaushal, V.2    Hong, X.3    Shah, S.V.4
  • 39
    • 0026336631 scopus 로고
    • Iron supplementation increases gentamicin nephrotoxicity in rats
    • Kays SE, Crowell WA, and Johnson MA. Iron supplementation increases gentamicin nephrotoxicity in rats. J Nutr 121: 1869-1875, 1991.
    • (1991) J Nutr , vol.121 , pp. 1869-1875
    • Kays, S.E.1    Crowell, W.A.2    Johnson, M.A.3
  • 40
    • 0030912483 scopus 로고    scopus 로고
    • Up-regulation of the Nedd2 gene encoding an ICE/Ced-3-like cysteine protease in the gerbil brain after transient global ischemia
    • Kinoshita M, Tomimoto H, Kinoshita A, Kumar S, and Noda M. Up-regulation of the Nedd2 gene encoding an ICE/Ced-3-like cysteine protease in the gerbil brain after transient global ischemia. J Cereb Blood Flow Metab 17: 507-514, 1997.
    • (1997) J Cereb Blood Flow Metab , vol.17 , pp. 507-514
    • Kinoshita, M.1    Tomimoto, H.2    Kinoshita, A.3    Kumar, S.4    Noda, M.5
  • 41
    • 0032553416 scopus 로고    scopus 로고
    • The cloning and expression of human deoxyribonuclease II. A possible role in apoptosis
    • Krieser RJ and Eastman A. The cloning and expression of human deoxyribonuclease II. A possible role in apoptosis. J Biol Chem 273: 30909-30914, 1998.
    • (1998) J Biol Chem , vol.273 , pp. 30909-30914
    • Krieser, R.J.1    Eastman, A.2
  • 42
    • 0017069532 scopus 로고
    • Acute renal failure due to nontraumatic rhabdomyolysis
    • Koffler A, Friedler RM, and Massry SG. Acute renal failure due to nontraumatic rhabdomyolysis. Ann Intern Med 85: 23-28, 1976.
    • (1976) Ann Intern Med , vol.85 , pp. 23-28
    • Koffler, A.1    Friedler, R.M.2    Massry, S.G.3
  • 43
    • 0019887828 scopus 로고
    • Deoxyribonuclease I in mammalian tissues. Specificity of inhibition by actin
    • Lacks SA. Deoxyribonuclease I in mammalian tissues. Specificity of inhibition by actin. J Biol Chem 256: 2644-2648, 1981.
    • (1981) J Biol Chem , vol.256 , pp. 2644-2648
    • Lacks, S.A.1
  • 44
    • 0016170149 scopus 로고
    • Free radicals and inflammation: Protection of synovial fluid by superoxide dismutase
    • McCord JM. Free radicals and inflammation: Protection of synovial fluid by superoxide dismutase. Science 185: 529-531, 1974.
    • (1974) Science , vol.185 , pp. 529-531
    • McCord, J.M.1
  • 45
    • 0021984681 scopus 로고
    • Oxygen-derived free radicals in postischemic tissue injury
    • McCord JM. Oxygen-derived free radicals in postischemic tissue injury. N Engl J Med 312: 159-163, 1985.
    • (1985) N Engl J Med , vol.312 , pp. 159-163
    • McCord, J.M.1
  • 46
    • 0014691242 scopus 로고
    • Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein)
    • McCord JM and Fridovich I. Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein). J Biol Chem 244: 6049-6055, 1969.
    • (1969) J Biol Chem , vol.244 , pp. 6049-6055
    • McCord, J.M.1    Fridovich, I.2
  • 49
    • 0020669768 scopus 로고
    • Membrane transport of anions across epithelia of mammalian small intestine and kidney proximal tubule
    • Murer H and Burckhardt G. Membrane transport of anions across epithelia of mammalian small intestine and kidney proximal tubule. Rev Physiol Biochem Pharmacol 96: 1-51, 1983.
    • (1983) Rev Physiol Biochem Pharmacol , vol.96 , pp. 1-51
    • Murer, H.1    Burckhardt, G.2
  • 50
    • 0034630317 scopus 로고    scopus 로고
    • Apoptotic DNA fragmentation
    • Nagata S. Apoptotic DNA fragmentation. Exp Cell Res 256: 12-18, 2000.
    • (2000) Exp Cell Res , vol.256 , pp. 12-18
    • Nagata, S.1
  • 51
    • 0028213114 scopus 로고
    • Mechanisms for protective effects of free radical scavengers on gentamicin-mediated nephropathy in rats
    • Nakajima T, Hishida A, and Kato A. Mechanisms for protective effects of free radical scavengers on gentamicin-mediated nephropathy in rats. Am J Physiol 266: F425-F431, 1994.
    • (1994) Am J Physiol , vol.266
    • Nakajima, T.1    Hishida, A.2    Kato, A.3
  • 53
    • 0012358348 scopus 로고
    • Induction of apoptosis in ischemia-reperfusion kidney model: Appearance of DNA strand breaks and expression of FAS mRNA
    • Nogae S, Koji T, Nakanishi Y, Saito T, Abe K, and Nakane PK. Induction of apoptosis in ischemia-reperfusion kidney model: Appearance of DNA strand breaks and expression of FAS mRNA. J Am Soc Nephrol 5: 905-910, 1994.
    • (1994) J Am Soc Nephrol , vol.5 , pp. 905-910
    • Nogae, S.1    Koji, T.2    Nakanishi, Y.3    Saito, T.4    Abe, K.5    Nakane, P.K.6
  • 55
    • 0033990535 scopus 로고    scopus 로고
    • Role of apoptosis in cisplatin-induced toxicity in the renal epithelial cell line LLC-PK1: Implication of the functions of apical membranes
    • Okuda M, Masaki K, Fukatsu S, Hashimoto Y, and Inui K. Role of apoptosis in cisplatin-induced toxicity in the renal epithelial cell line LLC-PK1: Implication of the functions of apical membranes. Biochem Pharmacol 59: 195-201, 2000.
    • (2000) Biochem Pharmacol , vol.59 , pp. 195-201
    • Okuda, M.1    Masaki, K.2    Fukatsu, S.3    Hashimoto, Y.4    Inui, K.5
  • 56
    • 0023755521 scopus 로고
    • Hemoglobin- and myoglobin-induced acute renal failure in rats: Role of iron in nephrotoxicity
    • Paller MS. Hemoglobin- and myoglobin-induced acute renal failure in rats: Role of iron in nephrotoxicity. Am J Physiol 255: F539-F544, 1988.
    • (1988) Am J Physiol , vol.255
    • Paller, M.S.1
  • 57
    • 0027745784 scopus 로고
    • Overexpression of deoxyribonuclease I (DNase I) transfected into COS-cells: Its distribution during apoptotic cell death
    • Polzar B, Peitsch MC, Loos R, Tschopp J, and Mannherz HG. Overexpression of deoxyribonuclease I (DNase I) transfected into COS-cells: Its distribution during apoptotic cell death. Eur J Cell Biol 62: 397-405, 1993.
    • (1993) Eur J Cell Biol , vol.62 , pp. 397-405
    • Polzar, B.1    Peitsch, M.C.2    Loos, R.3    Tschopp, J.4    Mannherz, H.G.5
  • 58
    • 0021888013 scopus 로고
    • The level of induced DNA double-strand breakage correlates with cell killing after X-irradiation
    • Radford IR. The level of induced DNA double-strand breakage correlates with cell killing after X-irradiation. Int J Radiat Biol Relat Stud Phys Chem Med 48: 45-54, 1985.
    • (1985) Int J Radiat Biol Relat Stud Phys Chem Med , vol.48 , pp. 45-54
    • Radford, I.R.1
  • 60
    • 0022469685 scopus 로고
    • Effects of diphenylphenylenediamine on gentamicin-induced lipid peroxidation and toxicity in rat renal cortex
    • Ramsammy LS, Josepovitz C, Ling KY, Lane BP, and Kaloyanides GJ. Effects of diphenylphenylenediamine on gentamicin-induced lipid peroxidation and toxicity in rat renal cortex. J Pharmacol Exp Ther 238: 83-88, 1986.
    • (1986) J Pharmacol Exp Ther , vol.238 , pp. 83-88
    • Ramsammy, L.S.1    Josepovitz, C.2    Ling, K.Y.3    Lane, B.P.4    Kaloyanides, G.J.5
  • 63
    • 0026326943 scopus 로고
    • Hydrogen peroxide-induced renal injury. A protective role for pyruvate in vitro and in vivo
    • Salahudeen AK, Clark EC, and Nath KA. Hydrogen peroxide-induced renal injury. A protective role for pyruvate in vitro and in vivo. J Clin Invest 88: 1886-1893, 1991.
    • (1991) J Clin Invest , vol.88 , pp. 1886-1893
    • Salahudeen, A.K.1    Clark, E.C.2    Nath, K.A.3
  • 64
    • 0027296679 scopus 로고
    • Absence of endonuclease activation during acute cell death in renal proximal tubules
    • Schnellmann RG, Swagler AR, and Compton MM. Absence of endonuclease activation during acute cell death in renal proximal tubules. Am J Physiol 265: C485-C490, 1993.
    • (1993) Am J Physiol , vol.265
    • Schnellmann, R.G.1    Swagler, A.R.2    Compton, M.M.3
  • 66
    • 0023707789 scopus 로고
    • Evidence suggesting a role for hydroxyl radical in glycerol-induced acute renal failure
    • Shah SV and Walker PD. Evidence suggesting a role for hydroxyl radical in glycerol-induced acute renal failure. Am J Physiol 255: F438-F443, 1988.
    • (1988) Am J Physiol , vol.255
    • Shah, S.V.1    Walker, P.D.2
  • 67
    • 0033826589 scopus 로고    scopus 로고
    • Down-regulation of the calpain inhibitor protein calpastatin by caspases during renal ischemia-reperfusion
    • Shi Y, Melnikov VY, Schrier RW, and Edelstein CL. Down-regulation of the calpain inhibitor protein calpastatin by caspases during renal ischemia-reperfusion. Am J Physiol Renal Physiol 279: F509-F517, 2000.
    • (2000) Am J Physiol Renal Physiol , vol.279
    • Shi, Y.1    Melnikov, V.Y.2    Schrier, R.W.3    Edelstein, C.L.4
  • 68
    • 0027250758 scopus 로고
    • Apoptosis and cell desquamation in repair process of ischemic tubular necrosis
    • Shimizu A, and Yamanaka N. Apoptosis and cell desquamation in repair process of ischemic tubular necrosis. Virchows Arch B Cell Pathol 64: 171-180, 1993.
    • (1993) Virchows Arch B Cell Pathol , vol.64 , pp. 171-180
    • Shimizu, A.1    Yamanaka, N.2
  • 69
    • 0014171369 scopus 로고
    • The effect of radiation on deoxyribonucleoproteins in animal tissue. 3. The character of the polydeoxyribonucleotides released from irradiated tissues
    • Skalka M and Matyasova J. The effect of radiation on deoxyribonucleoproteins in animal tissue. 3. The character of the polydeoxyribonucleotides released from irradiated tissues. Folia Biol (Praha) 13: 457-464, 1967.
    • (1967) Folia Biol (Praha) , vol.13 , pp. 457-464
    • Skalka, M.1    Matyasova, J.2
  • 70
    • 0029689954 scopus 로고    scopus 로고
    • Cisplatin-induced apoptosis in mouse proximal tubular cell line
    • Takeda M, Fukuoka K, and Endo H. Cisplatin-induced apoptosis in mouse proximal tubular cell line. Contrib Nephrol 118: 24-28, 1996.
    • (1996) Contrib Nephrol , vol.118 , pp. 24-28
    • Takeda, M.1    Fukuoka, K.2    Endo, H.3
  • 71
    • 0030801183 scopus 로고    scopus 로고
    • Cisplatin-induced apoptosis of immortalized mouse proximal tubule cells is mediated by interleukin-1beta converting enzyme (ICE) family of proteases but inhibited by overexpression of Bcl-2
    • Takeda M, Kobayashi M, Shirato I, Osaki T, and Endou H. Cisplatin-induced apoptosis of immortalized mouse proximal tubule cells is mediated by interleukin-1beta converting enzyme (ICE) family of proteases but inhibited by overexpression of Bcl-2. Arch Toxicol 71: 612-621, 1997.
    • (1997) Arch Toxicol , vol.71 , pp. 612-621
    • Takeda, M.1    Kobayashi, M.2    Shirato, I.3    Osaki, T.4    Endou, H.5
  • 72
    • 0034673555 scopus 로고    scopus 로고
    • Mammalian deoxyribonucleases I are classified into three types: Pancreas, parotid, and pancreas-parotid (mixed), based on differences in their tissue concentrations
    • Takeshita H, Mogi K, Yasuda T, Nakajima T, Nakashima Y, Mori S, Hoshino T, and Kishi K. Mammalian deoxyribonucleases I are classified into three types: Pancreas, parotid, and pancreas-parotid (mixed), based on differences in their tissue concentrations. Biochem Biophys Res Commun 269: 481-484, 2000.
    • (2000) Biochem Biophys Res Commun , vol.269 , pp. 481-484
    • Takeshita, H.1    Mogi, K.2    Yasuda, T.3    Nakajima, T.4    Nakashima, Y.5    Mori, S.6    Hoshino, T.7    Kishi, K.8
  • 73
    • 0032900335 scopus 로고    scopus 로고
    • Ordering of ceramide formation, caspase activation, and mitochondrial changes during CD95- and DNA damage-induced apoptosis
    • Tepper AD, de Vries E, van Blitterswijk WJ, and Borst J. Ordering of ceramide formation, caspase activation, and mitochondrial changes during CD95- and DNA damage-induced apoptosis. J Clin Invest 103: 971-978, 1999.
    • (1999) J Clin Invest , vol.103 , pp. 971-978
    • Tepper, A.D.1    De Vries, E.2    Van Blitterswijk, W.J.3    Borst, J.4
  • 74
    • 0027093953 scopus 로고
    • Endonuclease-induced DNA damage and cell death in oxidant injury to renal tubular epithelial cells
    • Ueda N and Shah SV. Endonuclease-induced DNA damage and cell death in oxidant injury to renal tubular epithelial cells. J Clin Invest 90: 2593-2597, 1992.
    • (1992) J Clin Invest , vol.90 , pp. 2593-2597
    • Ueda, N.1    Shah, S.V.2
  • 75
    • 0029126059 scopus 로고
    • Activation of a 15 kDa endonuclease in hypoxia/reoxygenation injury without morphologic features of apoptosis
    • Ueda N, Walker PD, Hsu S-M, and Shah SV. Activation of a 15 kDa endonuclease in hypoxia/reoxygenation injury without morphologic features of apoptosis. Proc Natl Acad Sci USA 92: 7202-7206, 1995.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 7202-7206
    • Ueda, N.1    Walker, P.D.2    Hsu, S.-M.3    Shah, S.V.4
  • 76
    • 0031848460 scopus 로고    scopus 로고
    • Role of enhanced ceramide generation in DNA damage and cell death in chemical hypoxic injury to LLC-PK 1 cells
    • Ueda N, Kaushal GP, Hong X, and Shah SV. Role of enhanced ceramide generation in DNA damage and cell death in chemical hypoxic injury to LLC-PK1 cells. Kidney Int 54: 399-406, 1998.
    • (1998) Kidney Int , vol.54 , pp. 399-406
    • Ueda, N.1    Kaushal, G.P.2    Hong, X.3    Shah, S.V.4
  • 78
    • 0023854331 scopus 로고
    • Evidence suggesting a role for hydroxyl radical in gentamicin-induced acute renal failure in rats
    • Walker PD and Shah SV. Evidence suggesting a role for hydroxyl radical in gentamicin-induced acute renal failure in rats. J Clin Invest 81: 334-341, 1988.
    • (1988) J Clin Invest , vol.81 , pp. 334-341
    • Walker, P.D.1    Shah, S.V.2
  • 79
    • 14444274100 scopus 로고    scopus 로고
    • Porcine spleen deoxyribonuclease II. Covalent structure, cDNA sequence, molecular cloning, and gene expression
    • Wang CC, Lu SC, Chen HL, and Liao TH. Porcine spleen deoxyribonuclease II. Covalent structure, cDNA sequence, molecular cloning, and gene expression. J Biol Chem 273: 17192-17198, 1998.
    • (1998) J Biol Chem , vol.273 , pp. 17192-17198
    • Wang, C.C.1    Lu, S.C.2    Chen, H.L.3    Liao, T.H.4
  • 80
    • 0033864457 scopus 로고    scopus 로고
    • Involvement of caspase 3- and 8-like proteases in ceramide-induced apoptosis of cardiomyocytes
    • Wang J, Zhen L, Klug MG, Wood D, Wu X, and Mizrahi J. Involvement of caspase 3- and 8-like proteases in ceramide-induced apoptosis of cardiomyocytes. J Card Fail 6: 243-249, 2000.
    • (2000) J Card Fail , vol.6 , pp. 243-249
    • Wang, J.1    Zhen, L.2    Klug, M.G.3    Wood, D.4    Wu, X.5    Mizrahi, J.6
  • 81
    • 0031938419 scopus 로고    scopus 로고
    • Apoptosis. An endonuclease at last
    • Wyllie A. Apoptosis. An endonuclease at last. Nature 391: 20-21, 1998.
    • (1998) Nature , vol.391 , pp. 20-21
    • Wyllie, A.1
  • 82
    • 0018830636 scopus 로고
    • Glucocorticoid-induced thymocyte apoptosis is associated with endogenous endonuclease activation
    • Wyllie AH. Glucocorticoid-induced thymocyte apoptosis is associated with endogenous endonuclease activation. Nature 284: 555-556, 1980.
    • (1980) Nature , vol.284 , pp. 555-556
    • Wyllie, A.H.1
  • 83
    • 0028924697 scopus 로고
    • Renal cortical mitochondria are the source of oxygen free radicals enhanced by gentamicin
    • Yang CL, Du XH, and Han YX. Renal cortical mitochondria are the source of oxygen free radicals enhanced by gentamicin. Ren Fail 17: 21-26, 1995.
    • (1995) Ren Fail , vol.17 , pp. 21-26
    • Yang, C.L.1    Du, X.H.2    Han, Y.X.3
  • 84
    • 0035129976 scopus 로고    scopus 로고
    • Bile acid-induced rat hepatocyte apoptosis is inhibited by antioxidants and blockers of the mitochondrial permeability transition
    • Yerushalmi B, Dahl R, Devereaux MW, Gumpricht E, and Sokol RJ. Bile acid-induced rat hepatocyte apoptosis is inhibited by antioxidants and blockers of the mitochondrial permeability transition. Hepatology 33: 616-626, 2001.
    • (2001) Hepatology , vol.33 , pp. 616-626
    • Yerushalmi, B.1    Dahl, R.2    Devereaux, M.W.3    Gumpricht, E.4    Sokol, R.J.5
  • 85
    • 0026779264 scopus 로고
    • Combined mannitol and deferoxamine therapy for myohemoglobinuric renal injury and oxidant tubular stress. Mechanistic and therapeutic implications
    • Zager RA. Combined mannitol and deferoxamine therapy for myohemoglobinuric renal injury and oxidant tubular stress. Mechanistic and therapeutic implications. J Clin Invest 90: 711-719, 1992.
    • (1992) J Clin Invest , vol.90 , pp. 711-719
    • Zager, R.A.1
  • 86
    • 0030070639 scopus 로고    scopus 로고
    • Rhabdomyolysis and myohemoglobinuric acute renal failure
    • Zager RA. Rhabdomyolysis and myohemoglobinuric acute renal failure. Kidney Int 49: 314-326, 1996.
    • (1996) Kidney Int , vol.49 , pp. 314-326
    • Zager, R.A.1
  • 87
    • 0029916477 scopus 로고    scopus 로고
    • Mitochondrial free radical production induces lipid peroxidation during myohemoglobinuria
    • Zager RA. Mitochondrial free radical production induces lipid peroxidation during myohemoglobinuria. Kidney Int 49: 741-751, 1996.
    • (1996) Kidney Int , vol.49 , pp. 741-751
    • Zager, R.A.1
  • 88
    • 0030842898 scopus 로고    scopus 로고
    • Altered ceramide and sphingosine expression during the induction phase of ischemic acute renal failure
    • Zager RA, Iwata M, Conrad DS, Burkhart KM, and Igarashi Y. Altered ceramide and sphingosine expression during the induction phase of ischemic acute renal failure. Kidney Int 52: 60-70, 1997.
    • (1997) Kidney Int , vol.52 , pp. 60-70
    • Zager, R.A.1    Iwata, M.2    Conrad, D.S.3    Burkhart, K.M.4    Igarashi, Y.5
  • 89
    • 0031890997 scopus 로고    scopus 로고
    • Altered sphingomyelinase and ceramide expression in the setting of ischemic and nephrotoxic acute renal failure
    • Zager RA, Conrad S, Lochhead K, Sweeney EA, Igarashi Y, and Burkhart KM. Altered sphingomyelinase and ceramide expression in the setting of ischemic and nephrotoxic acute renal failure. Kidney Int 53: 573-582, 1998.
    • (1998) Kidney Int , vol.53 , pp. 573-582
    • Zager, R.A.1    Conrad, S.2    Lochhead, K.3    Sweeney, E.A.4    Igarashi, Y.5    Burkhart, K.M.6
  • 90
    • 0033601251 scopus 로고    scopus 로고
    • DNA fragmentation factor 45-deficient cells are more resistant to apoptosis and exhibit different dying morphology than wild-type control cells
    • Zhang J, Wang X, Bove KE, and Xu M. DNA fragmentation factor 45-deficient cells are more resistant to apoptosis and exhibit different dying morphology than wild-type control cells. J Biol Chem 274: 37450-37454, 1999.
    • (1999) J Biol Chem , vol.274 , pp. 37450-37454
    • Zhang, J.1    Wang, X.2    Bove, K.E.3    Xu, M.4
  • 91
    • 0033542780 scopus 로고    scopus 로고
    • Caspase-8 mediates caspase-3 activation and cytochrome c release during singlet oxygen-induced apoptosis of HL-60 cells
    • Zhuang S, Lynch MC, and Kochevar IE. Caspase-8 mediates caspase-3 activation and cytochrome c release during singlet oxygen-induced apoptosis of HL-60 cells. Exp Cell Res 250: 203-212, 1999.
    • (1999) Exp Cell Res , vol.250 , pp. 203-212
    • Zhuang, S.1    Lynch, M.C.2    Kochevar, I.E.3
  • 92
    • 0034714334 scopus 로고    scopus 로고
    • p38 mitogen-activated protein kinase mediates bid cleavage, mitochondrial dysfunction, and caspase-3 activation during apoptosis induced by singlet oxygen but not by hydrogen peroxide
    • Zhuang S, Demirs JT, and Kochevar IE. p38 mitogen-activated protein kinase mediates bid cleavage, mitochondrial dysfunction, and caspase-3 activation during apoptosis induced by singlet oxygen but not by hydrogen peroxide. J Biol Chem 275: [25939-25948, 2000.
    • (2000) J Biol Chem , vol.275 , pp. 25939-25948
    • Zhuang, S.1    Demirs, J.T.2    Kochevar, I.E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.