메뉴 건너뛰기




Volumn 101, Issue 5, 2003, Pages 1987-1995

Tumor necrosis factor α induces a caspase-independent death pathway in human neutrophils

Author keywords

[No Author keywords available]

Indexed keywords

BENZYLOXYCARBONYLVALYLALANYLASPARTYL FLUOROMETHYL KETONE; CASPASE; CASPASE 3; CASPASE 8; CASPASE INHIBITOR; CYTOKINE; FAS ANTIGEN; PHOSPHATIDYLSERINE; PROTEIN BAX; REACTIVE OXYGEN METABOLITE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE; SCAVENGER; TUMOR NECROSIS FACTOR ALPHA;

EID: 0037370784     PISSN: 00064971     EISSN: None     Source Type: Journal    
DOI: 10.1182/blood-2002-02-0522     Document Type: Article
Times cited : (125)

References (73)
  • 1
    • 0027333425 scopus 로고
    • Tumor necrosis factor, other cytokines and disease
    • Tracey KJ, Cerami A. Tumor necrosis factor, other cytokines and disease. Annu Rev Cell Biol. 1993;9:317-343.
    • (1993) Annu Rev Cell Biol , vol.9 , pp. 317-343
    • Tracey, K.J.1    Cerami, A.2
  • 4
    • 0027196141 scopus 로고
    • Tumor necrosis factor-alpha blockade prevents neutrophil CD18 receptor upregulation and attenuates acute lung injury in porcine sepsis without inhibition of neutrophil oxygen radical generation
    • Windsor AC, Walsh CJ, Mullen PG, et al. Tumor necrosis factor-alpha blockade prevents neutrophil CD18 receptor upregulation and attenuates acute lung injury in porcine sepsis without inhibition of neutrophil oxygen radical generation. J Clin Invest. 1993;91:1459-1468.
    • (1993) J Clin Invest , vol.91 , pp. 1459-1468
    • Windsor, A.C.1    Walsh, C.J.2    Mullen, P.G.3
  • 5
    • 0345609037 scopus 로고    scopus 로고
    • Characterization of tumor necrosis factor-deficient mice
    • Marino MW, Dunn A, Grail D, et al. Characterization of tumor necrosis factor-deficient mice. Proc Natl Acad Sci U S A. 1997;94:8093-8098.
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 8093-8098
    • Marino, M.W.1    Dunn, A.2    Grail, D.3
  • 6
    • 0031916192 scopus 로고    scopus 로고
    • TNF is a potent anti-inflammatory cytokine in autolmmune-mediated demyelination
    • Liu J, Marino MW, Wong G, et al. TNF is a potent anti-inflammatory cytokine in autolmmune-mediated demyelination. Nat Med. 1998;4:78-83.
    • (1998) Nat Med , vol.4 , pp. 78-83
    • Liu, J.1    Marino, M.W.2    Wong, G.3
  • 7
    • 0024536234 scopus 로고
    • Macrophage phagocytosis of aging neutrophils in inflammation. Programmed cell death in the neutrophil leads to its recognition by macrophages
    • Savill JS, Wyllie AH, Henson JE, Walport MJ, Henson PM, Haslett C. Macrophage phagocytosis of aging neutrophils in inflammation. Programmed cell death in the neutrophil leads to its recognition by macrophages. J Clin Invest. 1989;83:865-875.
    • (1989) J Clin Invest , vol.83 , pp. 865-875
    • Savill, J.S.1    Wyllie, A.H.2    Henson, J.E.3    Walport, M.J.4    Henson, P.M.5    Haslett, C.6
  • 8
    • 0034641931 scopus 로고    scopus 로고
    • Corpse clearance defines the meaning of cell death
    • Savill J, Fadok V. Corpse clearance defines the meaning of cell death. Nature. 2000;407:784-788.
    • (2000) Nature , vol.407 , pp. 784-788
    • Savill, J.1    Fadok, V.2
  • 10
    • 0029681635 scopus 로고    scopus 로고
    • Bacterial ingestion, tumor necrosis factor-alpha, and heat induce programmed cell death in activated neutrophils
    • Watson RW, Redmond HP, Wang JH, Bouchier-Hayes D. Bacterial ingestion, tumor necrosis factor-alpha, and heat induce programmed cell death in activated neutrophils. Shock. 1996;5:47-51.
    • (1996) Shock , vol.5 , pp. 47-51
    • Watson, R.W.1    Redmond, H.P.2    Wang, J.H.3    Bouchier-Hayes, D.4
  • 11
    • 0030767702 scopus 로고    scopus 로고
    • Regulation of neutrophil apoptosis by tumor necrosis factor-alpha: Requirement for TNFR55 and TNFR75 for induction of apoptosis in vitro
    • Murray J, Barbara JA, Dunkley SA, et al. Regulation of neutrophil apoptosis by tumor necrosis factor-alpha: requirement for TNFR55 and TNFR75 for induction of apoptosis in vitro, Blood. 1997;90:2772-2783.
    • (1997) Blood , vol.90 , pp. 2772-2783
    • Murray, J.1    Barbara, J.A.2    Dunkley, S.A.3
  • 12
    • 0031910119 scopus 로고    scopus 로고
    • Interleukin-8 delays spontaneous and tumor necrosis factor-alpha-mediated apoptosis of human neutrophils
    • Kettritz R, Gaido ML, Hailer H, Luft FC, Jennette CJ, Falk RJ. Interleukin-8 delays spontaneous and tumor necrosis factor-alpha-mediated apoptosis of human neutrophils. Kidney Int. 1998;53:84-91.
    • (1998) Kidney Int , vol.53 , pp. 84-91
    • Kettritz, R.1    Gaido, M.L.2    Hailer, H.3    Luft, F.C.4    Jennette, C.J.5    Falk, R.J.6
  • 13
    • 0033556157 scopus 로고    scopus 로고
    • Caspases mediate tumor necrosis factor-alpha-induced neutrophil apoptosis and downregulation of reactive oxygen production
    • Yamashita K, Takahashi A, Kobayashi S, et al. Caspases mediate tumor necrosis factor-alpha-induced neutrophil apoptosis and downregulation of reactive oxygen production. Blood. 1999;93:674-685.
    • (1999) Blood , vol.93 , pp. 674-685
    • Yamashita, K.1    Takahashi, A.2    Kobayashi, S.3
  • 14
    • 0033121315 scopus 로고    scopus 로고
    • Bcl-XL-and Bax-α-mediated regulation of apoptosis of human neutrophils via caspase-3
    • Weinmann P, Gaehtgens P, Walzog B. Bcl-XL-and Bax-α-mediated regulation of apoptosis of human neutrophils via caspase-3. Blood. 1999;99:3106-3115.
    • (1999) Blood , vol.99 , pp. 3106-3115
    • Weinmann, P.1    Gaehtgens, P.2    Walzog, B.3
  • 15
    • 0026795415 scopus 로고
    • Modulation of granulocyte survival and programmed cell death by cytokines and bacterial products
    • Colotta F, Re F, Polentarutti N, Sozzani S, Mantovani A. Modulation of granulocyte survival and programmed cell death by cytokines and bacterial products. Blood. 1992;80:2012-2020.
    • (1992) Blood , vol.80 , pp. 2012-2020
    • Colotta, F.1    Re, F.2    Polentarutti, N.3    Sozzani, S.4    Mantovani, A.5
  • 16
    • 0030736624 scopus 로고    scopus 로고
    • Interleukin-10 counterregulates proinflammatory cytokine-induced inhibition of neutrophil apoptosis during severe sepsis
    • Keel M, Ungethum U, Steckholzer U, et al. Interleukin-10 counterregulates proinflammatory cytokine-induced inhibition of neutrophil apoptosis during severe sepsis. Blood. 1997;90:3356-3363.
    • (1997) Blood , vol.90 , pp. 3356-3363
    • Keel, M.1    Ungethum, U.2    Steckholzer, U.3
  • 17
    • 0035106745 scopus 로고    scopus 로고
    • Divergent effects of tumor necrosis factor-alpha on apoptosis of human neutrophils
    • van den Berg JM, Weyer S, Weening JJ, Roos D, Kuijpers TW. Divergent effects of tumor necrosis factor-alpha on apoptosis of human neutrophils. J Leukoc Biol. 2001;69:467-473.
    • (2001) J Leukoc Biol , vol.69 , pp. 467-473
    • Van den Berg, J.M.1    Weyer, S.2    Weening, J.J.3    Roos, D.4    Kuijpers, T.W.5
  • 18
    • 0034320568 scopus 로고    scopus 로고
    • Mechanisms of apoptosis
    • Reed JC. Mechanisms of apoptosis. Am J Pathol. 2000;157:1415-1430.
    • (2000) Am J Pathol , vol.157 , pp. 1415-1430
    • Reed, J.C.1
  • 19
    • 0034641918 scopus 로고    scopus 로고
    • The biochemistry of apoptosis
    • Hengartner MO. The biochemistry of apoptosis. Nature. 2000;407:770-776.
    • (2000) Nature , vol.407 , pp. 770-776
    • Hengartner, M.O.1
  • 20
    • 0028883850 scopus 로고
    • Cytotoxicity-dependent APO-1 (Fas/CD95)-associated proteins form a death-inducing signaling complex (DISC) with the receptor
    • Kischkel FC, Hellbardt S, Behrmann I, et al. Cytotoxicity-dependent APO-1 (Fas/CD95)-associated proteins form a death-inducing signaling complex (DISC) with the receptor. EMBO J. 1995;14:5579-5588.
    • (1995) EMBO J , vol.14 , pp. 5579-5588
    • Kischkel, F.C.1    Hellbardt, S.2    Behrmann, I.3
  • 21
    • 0032575714 scopus 로고    scopus 로고
    • Death receptors: Signaling and modulation
    • Ashkenazi A, Dixit VM. Death receptors: signaling and modulation. Science. 1998;281:1305-1308.
    • (1998) Science , vol.281 , pp. 1305-1308
    • Ashkenazi, A.1    Dixit, V.M.2
  • 23
    • 0032535016 scopus 로고    scopus 로고
    • Involvement of caspases in neutrophil apoptosis: Regulation by reactive oxygen species
    • Fadeel B, Ahlin A, Ftenter JI, Orrenius S, Hampton MB. Involvement of caspases in neutrophil apoptosis: regulation by reactive oxygen species. Blood. 1998;92:4808-4818.
    • (1998) Blood , vol.92 , pp. 4808-4818
    • Fadeel, B.1    Ahlin, A.2    Ftenter, J.I.3    Orrenius, S.4    Hampton, M.B.5
  • 24
    • 0037079734 scopus 로고    scopus 로고
    • Granulocyte colony-stimulating factor inhibits the mitochondria-dependent activation of caspase-3 in neutrophils
    • Maianski NA, Mul FPJ, van Buul JD, Roos D, Kuijpers TW. Granulocyte colony-stimulating factor inhibits the mitochondria-dependent activation of caspase-3 in neutrophils. Blood. 2002;99:672-679.
    • (2002) Blood , vol.99 , pp. 672-679
    • Maianski, N.A.1    Mul, F.P.J.2    Van Buul, J.D.3    Roos, D.4    Kuijpers, T.W.5
  • 25
    • 0022928014 scopus 로고
    • Purification and cryopreservation of phagocytes from human blood
    • Roos D, de Boer M. Purification and cryopreservation of phagocytes from human blood. Methods Enzymol. 1986;132:225-243.
    • (1986) Methods Enzymol , vol.132 , pp. 225-243
    • Roos, D.1    De Boer, M.2
  • 26
    • 0022928008 scopus 로고
    • Preparation and cryopreservation of cytoplasts from human phagocytes
    • Roos D, Voetman AA. Preparation and cryopreservation of cytoplasts from human phagocytes. Methods Enzymol. 1986;132:250-257.
    • (1986) Methods Enzymol , vol.132 , pp. 250-257
    • Roos, D.1    Voetman, A.A.2
  • 27
    • 15844412409 scopus 로고    scopus 로고
    • FLICE, a novel FADD-homologous ICE/CED-3-like protease, is recruited to the CD95 (Fas/APO-1) death-inducing signaling complex
    • Muzio M, Chinnaiyan AM, Kischkel FC, et al. FLICE, a novel FADD-homologous ICE/CED-3-like protease, is recruited to the CD95 (Fas/APO-1) death-inducing signaling complex. Cell. 1996;85:817-827.
    • (1996) Cell , vol.85 , pp. 817-827
    • Muzio, M.1    Chinnaiyan, A.M.2    Kischkel, F.C.3
  • 28
    • 0032536771 scopus 로고    scopus 로고
    • Two CD95 (APO-1 /Fas) signaling pathways
    • Scaffidi, C, Fulda S, Srinivasan A, et al. Two CD95 (APO-1 /Fas) signaling pathways. EM BO J. 1998;17:1675-1687.
    • (1998) EMBO J , vol.17 , pp. 1675-1687
    • Scaffidi, C.1    Fulda, S.2    Srinivasan, A.3
  • 29
    • 0032189802 scopus 로고    scopus 로고
    • Mcl-1 expression in human neutrophils: Regulation by cytokines and correlation with cell survival
    • Moulding DA, Quayle JA, Hart CA, Edwards SW. Mcl-1 expression in human neutrophils: regulation by cytokines and correlation with cell survival. Blood. 1998;92:2495-2502.
    • (1998) Blood , vol.92 , pp. 2495-2502
    • Moulding, D.A.1    Quayle, J.A.2    Hart, C.A.3    Edwards, S.W.4
  • 30
    • 0035213274 scopus 로고    scopus 로고
    • BCL-2 family expression in human neutrophils during delayed and accelerated apoptosis
    • Moulding DA, Akgul C, Derouet M, White MR, Edwards SW. BCL-2 family expression in human neutrophils during delayed and accelerated apoptosis. J Leukoc Biol. 2001;70:783-792.
    • (2001) J Leukoc Biol , vol.70 , pp. 783-792
    • Moulding, D.A.1    Akgul, C.2    Derouet, M.3    White, M.R.4    Edwards, S.W.5
  • 31
    • 0035876931 scopus 로고    scopus 로고
    • Cooperative regulation of Mcl-1 by Janus kinase/stat and phosphatidylinositol 3-kinase contribute to granulocyte-macrophage colony-stimulating factor-delayed apoptosis in human neutrophils
    • Epling-Burnette PK, Zhong B, Bai F, et al. Cooperative regulation of Mcl-1 by Janus kinase/stat and phosphatidylinositol 3-kinase contribute to granulocyte-macrophage colony-stimulating factor-delayed apoptosis in human neutrophils. J Immunol. 2001;166:7486-7495.
    • (2001) J Immunol , vol.166 , pp. 7486-7495
    • Epling-Burnette, P.K.1    Zhong, B.2    Bai, F.3
  • 32
    • 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. 1980;284:555-556.
    • (1980) Nature , vol.284 , pp. 555-556
    • Wyllie, A.H.1
  • 33
    • 0028927607 scopus 로고
    • The Fas death factor
    • Nagata S, Golstein P. The Fas death factor. Science. 1995;267:1449-1456.
    • (1995) Science , vol.267 , pp. 1449-1456
    • Nagata, S.1    Golstein, P.2
  • 34
    • 0031035427 scopus 로고    scopus 로고
    • Involvement of reactive oxygen intermediates in spontaneous and CD95 (Fas/APO-1)-mediated apoptosis of neutrophils
    • Kasahara Y, Iwai K, Yachie A, et al. Involvement of reactive oxygen intermediates in spontaneous and CD95 (Fas/APO-1)-mediated apoptosis of neutrophils. Blood. 1997;89:1748-1753.
    • (1997) Blood , vol.89 , pp. 1748-1753
    • Kasahara, Y.1    Iwai, K.2    Yachie, A.3
  • 36
    • 0032487582 scopus 로고    scopus 로고
    • Regulated targeting of BAX to mitochondria
    • Goping IS, Gross A, Lavoie JN, et al. Regulated targeting of BAX to mitochondria. J Cell Biol. 1998;143:207-215.
    • (1998) J Cell Biol , vol.143 , pp. 207-215
    • Goping, I.S.1    Gross, A.2    Lavoie, J.N.3
  • 37
    • 0033406781 scopus 로고    scopus 로고
    • Withdrawal of IL-7 induces Bax translocation from cytosol to mitochondria through a rise in intracellular pH
    • Khaled AR, Kim K, Hofmeister R, Muegge K, Durum SK. Withdrawal of IL-7 induces Bax translocation from cytosol to mitochondria through a rise in intracellular pH. Proc Natl Acad Sci U S A. 1999;96:14476-14481.
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 14476-14481
    • Khaled, A.R.1    Kim, K.2    Hofmeister, R.3    Muegge, K.4    Durum, S.K.5
  • 38
    • 0034059440 scopus 로고    scopus 로고
    • Bcl-2 inhibits Bax translocation from cytosol to mitochondria during drug-induced apoptosis of human tumor cells
    • Murphy KM, Ranganathan V, Farnsworth ML, Kavallaris M, Lock RB. Bcl-2 inhibits Bax translocation from cytosol to mitochondria during drug-induced apoptosis of human tumor cells. Cell Death Differ. 2000;7:102-111.
    • (2000) Cell Death Differ , vol.7 , pp. 102-111
    • Murphy, K.M.1    Ranganathan, V.2    Farnsworth, M.L.3    Kavallaris, M.4    Lock, R.B.5
  • 39
    • 0020513579 scopus 로고
    • Functional activity of enucleated human polymorphonuclear leukocytes
    • Roos D, Voetman AA, Meerhof LJ. Functional activity of enucleated human polymorphonuclear leukocytes. J Cell Biol. 1983;97:368-377.
    • (1983) J Cell Biol , vol.97 , pp. 368-377
    • Roos, D.1    Voetman, A.A.2    Meerhof, L.J.3
  • 40
    • 0032908810 scopus 로고    scopus 로고
    • Cytokine-specific activation of distinct mitogen-activated protein kinase subtype cascades in human neutrophils stimulated by granulocyte colony-stimulating factor, granulocyte-macrophage colony-stimulating factor, and tumor necrosis factor-alpha
    • Suzuki K, Hino M, Hato F,Tatsumi N, Kitagawa S. Cytokine-specific activation of distinct mitogen-activated protein kinase subtype cascades in human neutrophils stimulated by granulocyte colony-stimulating factor, granulocyte-macrophage colony-stimulating factor, and tumor necrosis factor-alpha. Blood. 1999;93:341-349.
    • (1999) Blood , vol.93 , pp. 341-349
    • Suzuki, K.1    Hino, M.2    Hato, F.3    Tatsumi, N.4    Kitagawa, S.5
  • 41
    • 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 AC, Vanhaesebroeck B, Beyaert R, Jacob WA, Fiers W. 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. 1992;267:5317-5323.
    • (1992) J Biol Chem , vol.267 , pp. 5317-5323
    • Schulze-Osthoff, K.1    Bakker, A.C.2    Vanhaesebroeck, B.3    Beyaert, R.4    Jacob, W.A.5    Fiers, W.6
  • 42
    • 0029090167 scopus 로고
    • Direct evidence for tumor necrosis factor-induced mitochondrial reactive oxygen intermediates and their involvement in cytotoxicity
    • Goossens V, Grooten J, De Vos K, Fiers W. Direct evidence for tumor necrosis factor-induced mitochondrial reactive oxygen intermediates and their involvement in cytotoxicity. Proc Natl Acad Sci U S A. 1995;92:8115-8119.
    • (1995) Proc Natl Acad Sci U S A , vol.92 , pp. 8115-8119
    • Goossens, V.1    Grooten, J.2    De Vos, K.3    Fiers, W.4
  • 43
    • 0034725109 scopus 로고    scopus 로고
    • Selective involvement of superoxide anion, but not downstream compounds hydrogen peroxide and peroxynitrite, in tumor necrosis factor-alpha-induced apoptosis of rat mesangial cells
    • Moreno-Manzano V, Ishikawa Y, Lucio-Cazana J, Kitamura M. Selective involvement of superoxide anion, but not downstream compounds hydrogen peroxide and peroxynitrite, in tumor necrosis factor-alpha-induced apoptosis of rat mesangial cells. J Biol Chem. 2000;275:12684-12691.
    • (2000) J Biol Chem , vol.275 , pp. 12684-12691
    • Moreno-Manzano, V.1    Ishikawa, Y.2    Lucio-Cazana, J.3    Kitamura, M.4
  • 44
    • 0033579422 scopus 로고    scopus 로고
    • Resistance to the cytotoxic effects of tumor necrosis factor alpha can be overcome by inhibition of a FADD/caspase-dependent signaling pathway
    • Khwaja A, Tatton L. Resistance to the cytotoxic effects of tumor necrosis factor alpha can be overcome by inhibition of a FADD/caspase-dependent signaling pathway. J Biol Chem. 1999;274:36817-36823.
    • (1999) J Biol Chem , vol.274 , pp. 36817-36823
    • Khwaja, A.1    Tatton, L.2
  • 45
    • 0034177682 scopus 로고    scopus 로고
    • Endogenous oxygen radicals modulate protein tyrosine phosphorylation and JNK-1 activation in lectin-stimulated thymocytes
    • Pani G, Colavitti R, Borrello S, Galeotti T. Endogenous oxygen radicals modulate protein tyrosine phosphorylation and JNK-1 activation in lectin-stimulated thymocytes. Biochem J. 2000;347:173-181.
    • (2000) Biochem J , vol.347 , pp. 173-181
    • Pani, G.1    Colavitti, R.2    Borrello, S.3    Galeotti, T.4
  • 46
    • 0035852636 scopus 로고    scopus 로고
    • Mitochondria in eosinophils: Functional role in apoptosis but not respiration
    • Peachman KK, Lyles DS, Bass DA. Mitochondria in eosinophils: functional role in apoptosis but not respiration. Proc Natl Acad Sci U S A. 2001;98:1717-1722.
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 1717-1722
    • Peachman, K.K.1    Lyles, D.S.2    Bass, D.A.3
  • 47
    • 0019969614 scopus 로고
    • Energy metabolism of human neutrophils during phagocytosis
    • Borregaard N, Herlin T. Energy metabolism of human neutrophils during phagocytosis, J Clin Invest. 1982;70:550-557.
    • (1982) J Clin Invest , vol.70 , pp. 550-557
    • Borregaard, N.1    Herlin, T.2
  • 49
    • 0030809576 scopus 로고    scopus 로고
    • Reactive oxygen species, mitochondria, apoptosis and aging
    • Papa S, Skulachev VP. Reactive oxygen species, mitochondria, apoptosis and aging. Mol Cell Biochem. 1997;174:305-319.
    • (1997) Mol Cell Biochem , vol.174 , pp. 305-319
    • Papa, S.1    Skulachev, V.P.2
  • 50
    • 0032053707 scopus 로고    scopus 로고
    • Oxygen radicals and signaling
    • Finkel T. Oxygen radicals and signaling. Curr Opin Cell Biol. 1998;10:248-253.
    • (1998) Curr Opin Cell Biol , vol.10 , pp. 248-253
    • Finkel, T.1
  • 51
    • 0032504657 scopus 로고    scopus 로고
    • Role of mitochondria in oxidative stress and ageing
    • Lenaz G. Role of mitochondria in oxidative stress and ageing. Biochim Biophys Acta. 1998;1366:53-67.
    • (1998) Biochim Biophys Acta , vol.1366 , pp. 53-67
    • Lenaz, G.1
  • 52
    • 0033964762 scopus 로고    scopus 로고
    • Mitochondrial role in life and death of the cell
    • Lee HC, Wei YH. Mitochondrial role in life and death of the cell. J Biomed Sci. 2000;7:2-15.
    • (2000) J Biomed Sci , vol.7 , pp. 2-15
    • Lee, H.C.1    Wei, Y.H.2
  • 53
    • 0029071509 scopus 로고
    • Oxidants in mitochondria: From physiology to diseases
    • Richter C, Gogvadze V, Laffranchi R, et al. Oxidants in mitochondria: from physiology to diseases. Biochim Biophys Acta. 1995;1271:67-74.
    • (1995) Biochim Biophys Acta , vol.1271 , pp. 67-74
    • Richter, C.1    Gogvadze, V.2    Laffranchi, R.3
  • 54
    • 0023655449 scopus 로고
    • Protein damage and degradation by oxygen radicals. IV. Degradation of denatured protein
    • Davies KJ, Lin SW, Pacifici RE. Protein damage and degradation by oxygen radicals. IV. Degradation of denatured protein. J Biol Chem. 1987;262:9914-9920.
    • (1987) J Biol Chem , vol.262 , pp. 9914-9920
    • Davies, K.J.1    Lin, S.W.2    Pacifici, R.E.3
  • 55
    • 0021951263 scopus 로고
    • Endogenous free radical generation may influence proteolysis in mitochondria
    • Dean RT, Pollak JK. Endogenous free radical generation may influence proteolysis in mitochondria. Biochem Biophys Res Commun. 1985;126:1082-1089.
    • (1985) Biochem Biophys Res Commun , vol.126 , pp. 1082-1089
    • Dean, R.T.1    Pollak, J.K.2
  • 56
    • 0032482169 scopus 로고    scopus 로고
    • Inhibition of caspases increases the sensitivity of L929 cells to necrosis mediated by tumor necrosis factor
    • Vercammen D, Beyaert R, Denecker G, et al. Inhibition of caspases increases the sensitivity of L929 cells to necrosis mediated by tumor necrosis factor. J Exp Med. 1998;187:1477-1485.
    • (1998) J Exp Med , vol.187 , pp. 1477-1485
    • Vercammen, D.1    Beyaert, R.2    Denecker, G.3
  • 57
    • 18244387009 scopus 로고    scopus 로고
    • Preprocessed caspase-9 contained in mitochondria participates in apoptosis
    • Costantini P, Bruey JM, Castedo M, et al. Preprocessed caspase-9 contained in mitochondria participates in apoptosis. Cell Death Differ. 2002;9:82-88.
    • (2002) Cell Death Differ , vol.9 , pp. 82-88
    • Costantini, P.1    Bruey, J.M.2    Castedo, M.3
  • 58
    • 0034637510 scopus 로고    scopus 로고
    • Sensitization to death receptor cytotoxicity by inhibition of fas-associated death domain protein (FADD)/caspase signaling. Requirement of cell cycle progression
    • Luschen S, Ussat S, Scherer G, Kabelitz D, Adam-Klages S. Sensitization to death receptor cytotoxicity by inhibition of fas-associated death domain protein (FADD)/caspase signaling. Requirement of cell cycle progression. J Biol Chem. 2000;275:24670-24678.
    • (2000) J Biol Chem , vol.275 , pp. 24670-24678
    • Luschen, S.1    Ussat, S.2    Scherer, G.3    Kabelitz, D.4    Adam-Klages, S.5
  • 60
    • 0034599085 scopus 로고    scopus 로고
    • Toward antiapoptosis as a new treatment modality
    • HaunstetterA, Izumo S. Toward antiapoptosis as a new treatment modality. Circ Res. 2000;86:371-376.
    • (2000) Circ Res , vol.86 , pp. 371-376
    • Haunstetter, A.1    Izumo, S.2
  • 61
    • 0034641932 scopus 로고    scopus 로고
    • From bench to clinic with apoptosis-based therapeutic agents
    • Nicholson DW. From bench to clinic with apoptosis-based therapeutic agents. Nature. 2000;407:810-816.
    • (2000) Nature , vol.407 , pp. 810-816
    • Nicholson, D.W.1
  • 62
    • 0033005752 scopus 로고    scopus 로고
    • A caspase inhibitor fully protects rats against lethal normothermic liver ischemia by inhibition of liver apoptosis
    • Cursio R, Gugenheim J, Ricci JE, et aI.A caspase inhibitor fully protects rats against lethal normothermic liver ischemia by inhibition of liver apoptosis. FASEB J. 1999;13:253-261.
    • (1999) FASEB J , vol.13 , pp. 253-261
    • Cursio, R.1    Gugenheim, J.2    Ricci, J.E.3
  • 63
    • 0032743421 scopus 로고    scopus 로고
    • Inhibition of apoptosis induced by ischemia-reperfusion prevents inflammation
    • Daemen MA, van 't Veer C, Denecker G, et al. Inhibition of apoptosis induced by ischemia-reperfusion prevents inflammation. J Clin Invest. 1999;104:541-549.
    • (1999) J Clin Invest , vol.104 , pp. 541-549
    • Daemen, M.A.1    Van 't Veer, C.2    Denecker, G.3
  • 64
    • 0034016833 scopus 로고    scopus 로고
    • Caspase inhibition and limitation of myocardial infarct size: Protection against lethal reperfusion injury
    • Mocanu MM, Baxter GF, Yellen DM. Caspase inhibition and limitation of myocardial infarct size: protection against lethal reperfusion injury. Br J Pharmacol. 2000;130:197-200.
    • (2000) Br J Pharmacol , vol.130 , pp. 197-200
    • Mocanu, M.M.1    Baxter, G.F.2    Yellen, D.M.3
  • 66
    • 0033276621 scopus 로고    scopus 로고
    • Peptidomimetic fluoromethylketone rescues mice from lethal endotoxic shock
    • Grobmyer SR, Armstrong RC, Nicholson SC, et al. Peptidomimetic fluoromethylketone rescues mice from lethal endotoxic shock. Mol Med. 1999;5:585-594.
    • (1999) Mol Med , vol.5 , pp. 585-594
    • Grobmyer, S.R.1    Armstrong, R.C.2    Nicholson, S.C.3
  • 68
    • 17844365555 scopus 로고    scopus 로고
    • Direct cleavage of the human DNA fragmentation factor-45 by granzyme B induces caspase-activated DNase release and DNA fragmentation
    • Sharif-Askari E, Alam A, Rheaume E, et al. Direct cleavage of the human DNA fragmentation factor-45 by granzyme B induces caspase-activated DNase release and DNA fragmentation. EMBO J. 2001;20:3101-3113.
    • (2001) EMBO J , vol.20 , pp. 3101-3113
    • Sharif-Askari, E.1    Alam, A.2    Rheaume, E.3
  • 69
    • 0036417225 scopus 로고    scopus 로고
    • Beta-bungarotoxin is a potent inducer of apoptosis in cultured rat neurons by receptor-mediated internalization
    • Herkert M, Shakhman O, Schweins E, Becker CM. Beta-bungarotoxin is a potent inducer of apoptosis in cultured rat neurons by receptor-mediated internalization. Eur J Neurosci. 2001;14:821-828.
    • (2001) Eur J Neurosci , vol.14 , pp. 821-828
    • Herkert, M.1    Shakhman, O.2    Schweins, E.3    Becker, C.M.4
  • 71
    • 0034941698 scopus 로고    scopus 로고
    • Role of DNA-dependent protein kinase in neuronal survival
    • Chechlacz M, Vemuri MC, Naegele JR. Role of DNA-dependent protein kinase in neuronal survival. J Neurochem. 2001;78:141-154.
    • (2001) J Neurochem , vol.78 , pp. 141-154
    • Chechlacz, M.1    Vemuri, M.C.2    Naegele, J.R.3
  • 72
    • 0035469857 scopus 로고    scopus 로고
    • Growth factor withdrawal from primary human erythroid progenitors induces apoptosis through a pathway involving glycogen synthase kinase-3 and Bax
    • Somervaille TC, Linch DC, Khwaja A. Growth factor withdrawal from primary human erythroid progenitors induces apoptosis through a pathway involving glycogen synthase kinase-3 and Bax. Blood. 2001;98:1374-1381.
    • (2001) Blood , vol.98 , pp. 1374-1381
    • Somervaille, T.C.1    Linch, D.C.2    Khwaja, A.3
  • 73
    • 0034960490 scopus 로고    scopus 로고
    • Caspase-independent cell death and mitochondrial disruptions observed in the Apafl-deficient cells
    • Miyazaki K, Yoshida H, Sasaki M, et al. Caspase-independent cell death and mitochondrial disruptions observed in the Apafl-deficient cells. J Biochem (Tokyo). 2001;129:963-969.
    • (2001) J Biochem (Tokyo) , vol.129 , pp. 963-969
    • Miyazaki, K.1    Yoshida, H.2    Sasaki, M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.