메뉴 건너뛰기




Volumn 95, Issue 6, 2000, Pages 2015-2023

Tumor-induced apoptosis of T lymphocytes: Elucidation of intracellular apoptotic events

Author keywords

[No Author keywords available]

Indexed keywords

CASPASE 3; CASPASE 8; INTERLEUKIN 1BETA CONVERTING ENZYME; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE;

EID: 0034653462     PISSN: 00064971     EISSN: None     Source Type: Journal    
DOI: 10.1182/blood.v95.6.2015     Document Type: Article
Times cited : (94)

References (73)
  • 1
    • 0029808372 scopus 로고    scopus 로고
    • The Fas counterattack: Fas-mediated T cell killing by colon cancer cells expressing Fas ligand
    • O'Connell J, O'Sullivan GC, Collins JK, Shanahan F. The Fas counterattack: Fas-mediated T cell killing by colon cancer cells expressing Fas ligand. J Exp Med. 1996;184:1075.
    • (1996) J Exp Med , vol.184 , pp. 1075
    • O'Connell, J.1    O'Sullivan, G.C.2    Collins, J.K.3    Shanahan, F.4
  • 3
    • 16144363507 scopus 로고    scopus 로고
    • Lymphocyte apoptosis induced by CD95 (APO-1/Fas) ligand-expressing tumor cells: A mechanism of immune evasion?
    • Strand S, Hofmann WJ, Hug H, et al. Lymphocyte apoptosis induced by CD95 (APO-1/Fas) ligand-expressing tumor cells: a mechanism of immune evasion? Nat Med. 1997;2:1361.
    • (1997) Nat Med , vol.2 , pp. 1361
    • Strand, S.1    Hofmann, W.J.2    Hug, H.3
  • 4
    • 10544232277 scopus 로고    scopus 로고
    • Melanoma cell expression of Fas (Apo-1/CD95) ligand: Implications for tumor immune escape
    • Hahne M, Rimoldi D, Schroter M, et al. Melanoma cell expression of Fas (Apo-1/CD95) ligand: implications for tumor immune escape. Science. 1996; 274:1363.
    • (1996) Science , vol.274 , pp. 1363
    • Hahne, M.1    Rimoldi, D.2    Schroter, M.3
  • 5
    • 0030895084 scopus 로고    scopus 로고
    • Fas ligand expression by astrocytoma in vivo: Maintaining immune privilege in the brain?
    • Saas P, Walker PR, Hahne M, et al. Fas ligand expression by astrocytoma in vivo: maintaining immune privilege in the brain? J Clin Invest. 1997;99:1173.
    • (1997) J Clin Invest , vol.99 , pp. 1173
    • Saas, P.1    Walker, P.R.2    Hahne, M.3
  • 6
    • 0031570098 scopus 로고    scopus 로고
    • Role of Fas ligand (CD95L) in immune escape: The tumor cell strikes back
    • Walker PR, Saas P, Dietrich PY. Role of Fas ligand (CD95L) in immune escape: the tumor cell strikes back. J Immunol. 1997;158:4521.
    • (1997) J Immunol , vol.158 , pp. 4521
    • Walker, P.R.1    Saas, P.2    Dietrich, P.Y.3
  • 8
    • 0032102258 scopus 로고    scopus 로고
    • Lymphocyte apoptosis induced by Fas ligand-expressing ovarian carcinoma cells: Implications for altered expression of TcR in tumor-associated lymphocytes
    • Rabinowich H, Reichert TE, Kashii Y, Gastman BR, Bell MC, Whiteside TL. Lymphocyte apoptosis induced by Fas ligand-expressing ovarian carcinoma cells: implications for altered expression of TcR in tumor-associated lymphocytes. J Clin Invest. 1998;101:2579.
    • (1998) J Clin Invest , vol.101 , pp. 2579
    • Rabinowich, H.1    Reichert, T.E.2    Kashii, Y.3    Gastman, B.R.4    Bell, M.C.5    Whiteside, T.L.6
  • 9
    • 0032523931 scopus 로고    scopus 로고
    • Up-regulation of Fas (APO-1/CD95) ligand and down-regulation of Fas expression in human esophageal cancer
    • Gratas C, Tohma Y, Barnas C, Taniere P, Hainaut P, Ohgaki H. Up-regulation of Fas (APO-1/CD95) ligand and down-regulation of Fas expression in human esophageal cancer. Cancer Res. 1998; 58:2057.
    • (1998) Cancer Res , vol.58 , pp. 2057
    • Gratas, C.1    Tohma, Y.2    Barnas, C.3    Taniere, P.4    Hainaut, P.5    Ohgaki, H.6
  • 10
    • 0030610033 scopus 로고    scopus 로고
    • Fas ligand expression in glioblastoma cell lines and primary astrocytic brain tumors
    • Gratas C, Tohma Y, Van Meir EG, et al. Fas ligand expression in glioblastoma cell lines and primary astrocytic brain tumors. Brain Pathol. 1997;7:863.
    • (1997) Brain Pathol , vol.7 , pp. 863
    • Gratas, C.1    Tohma, Y.2    Van Meir, E.G.3
  • 11
    • 0032927310 scopus 로고    scopus 로고
    • Mechanisms of apoptosis in T cells from patients with renal cell carcinoma
    • Uzzo RG, Rayman P, Kolenko V, et al. Mechanisms of apoptosis in T cells from patients with renal cell carcinoma. Clin Cancer Res. 1999;5: 1219.
    • (1999) Clin Cancer Res , vol.5 , pp. 1219
    • Uzzo, R.G.1    Rayman, P.2    Kolenko, V.3
  • 12
    • 0031846804 scopus 로고    scopus 로고
    • Human immune cells in the tumor microenvironment: Mechanisms responsible for signaling and functional defects
    • Reichert TE, Rabinowich H, Johnson JT, Whiteside TL. Human immune cells in the tumor microenvironment: mechanisms responsible for signaling and functional defects. J Immmunother. 1998; 21:295.
    • (1998) J Immmunother , vol.21 , pp. 295
    • Reichert, T.E.1    Rabinowich, H.2    Johnson, J.T.3    Whiteside, T.L.4
  • 15
    • 0028909197 scopus 로고
    • Fas ligand mediates activation-induced cell death in human T lymphocytes
    • Alderson MR, Tough TW, Davis-Smith T, et al. Fas ligand mediates activation-induced cell death in human T lymphocytes. J Exp Med. 1995; 181:71.
    • (1995) J Exp Med , vol.181 , pp. 71
    • Alderson, M.R.1    Tough, T.W.2    Davis-Smith, T.3
  • 17
    • 0031202422 scopus 로고    scopus 로고
    • ZAP-70 tyrosine kinase is required for the up-regulation of Fas ligand in activation-induced T cell apoptosis
    • Eischen CM, Williams BL, Zhang W, et al. ZAP-70 tyrosine kinase is required for the up-regulation of Fas ligand in activation-induced T cell apoptosis. J Immunol. 1997;159:1135.
    • (1997) J Immunol , vol.159 , pp. 1135
    • Eischen, C.M.1    Williams, B.L.2    Zhang, W.3
  • 18
    • 0030731919 scopus 로고    scopus 로고
    • Interleukin-1 beta converting enzyme-like protease involvement in Fas-induced and activation-induced peripheral blood T cell apoptosis in HIV infection. TNF-related apoptosis-inducing ligand can mediate activation-induced T cell death in HIV infection
    • Katsikis PD, Garcia-Ojeda ME, Totres-Roca JF, et al. Interleukin-1 beta converting enzyme-like protease involvement in Fas-induced and activation-induced peripheral blood T cell apoptosis in HIV infection. TNF-related apoptosis-inducing ligand can mediate activation-induced T cell death in HIV infection. J Exp Med. 1997;186: 1365.
    • (1997) J Exp Med , vol.186 , pp. 1365
    • Katsikis, P.D.1    Garcia-Ojeda, M.E.2    Totres-Roca, J.F.3
  • 19
    • 0031719383 scopus 로고    scopus 로고
    • Involvement of APO2 ligand/TRAIL in activation-induced death of Jurkat and human peripheral blood T cells
    • Martinez-Lorenzo MJ, Alava MA, Gamen S, et al. Involvement of APO2 ligand/TRAIL in activation-induced death of Jurkat and human peripheral blood T cells. Eur J Immunol. 1998;28:2714.
    • (1998) Eur J Immunol , vol.28 , pp. 2714
    • Martinez-Lorenzo, M.J.1    Alava, M.A.2    Gamen, S.3
  • 20
    • 0032014073 scopus 로고    scopus 로고
    • DNA damaging agents induce expression of Fas ligand and subsequent apoptosis in T lymphocytes via the activation of NF-kappa B and AP-1
    • Kasibhatla S, Brunner T, Genestier L, Echeverri F, Mahboubi A, Green DR. DNA damaging agents induce expression of Fas ligand and subsequent apoptosis in T lymphocytes via the activation of NF-kappa B and AP-1. Mol Cell. 1998;1:543.
    • (1998) Mol Cell , vol.1 , pp. 543
    • Kasibhatla, S.1    Brunner, T.2    Genestier, L.3    Echeverri, F.4    Mahboubi, A.5    Green, D.R.6
  • 21
    • 0031253977 scopus 로고    scopus 로고
    • Killer/DR5 is a DNA damage-inducible p53-regulated death receptor gene
    • Wu GS, Burns TF, McDonald ER, et al. Killer/DR5 is a DNA damage-inducible p53-regulated death receptor gene. Nat Genet. 1997;17:141.
    • (1997) Nat Genet , vol.17 , pp. 141
    • Wu, G.S.1    Burns, T.F.2    McDonald, E.R.3
  • 22
    • 0032192236 scopus 로고    scopus 로고
    • Induction of apoptosis by Smad3 and down-regulation of Smard3 expression in response to TGF-beta in human normal lung epithelial cells
    • Yanagisawa K, Osada H, Masuda A, et al. induction of apoptosis by Smad3 and down-regulation of Smard3 expression in response to TGF-beta in human normal lung epithelial cells. Oncogene. 1998;17:1743.
    • (1998) Oncogene , vol.17 , pp. 1743
    • Yanagisawa, K.1    Osada, H.2    Masuda, A.3
  • 23
    • 0032536519 scopus 로고    scopus 로고
    • Caspases are activated in a branched proteases cascade and control distinct downstream processes in Fas-induced apoptosis
    • Hirata H, Takahashi A, Kobayashi S, et al. Caspases are activated in a branched proteases cascade and control distinct downstream processes in Fas-induced apoptosis. J Exp Med. 1998;187:587.
    • (1998) J Exp Med , vol.187 , pp. 587
    • Hirata, H.1    Takahashi, A.2    Kobayashi, S.3
  • 24
    • 0030701895 scopus 로고    scopus 로고
    • Comparison of caspase activation and sub-cellular localization in HL-60 and K562 cells undergoing etoposide-induced apoptosis
    • Martins LM, Mesner PW, Kottke TJ, et al. Comparison of caspase activation and sub-cellular localization in HL-60 and K562 cells undergoing etoposide-induced apoptosis. Blood. 1997;90: 4283.
    • (1997) Blood , vol.90 , pp. 4283
    • Martins, L.M.1    Mesner, P.W.2    Kottke, T.J.3
  • 25
    • 0030702084 scopus 로고    scopus 로고
    • Caspases: Intracellular signaling by proteolysis
    • Salvesen GS, Dixit VM. Caspases: intracellular signaling by proteolysis. Cell. 1997;91:443.
    • (1997) Cell , vol.91 , pp. 443
    • Salvesen, G.S.1    Dixit, V.M.2
  • 26
    • 0032489390 scopus 로고    scopus 로고
    • Caspase-9, Bcl-XL, and Apaf-1 form a ternary complex
    • Pan GH, O'Rourke K, Dixit VM. Caspase-9, Bcl-XL, and Apaf-1 form a ternary complex. J Biol Chem. 1998;273:5841.
    • (1998) J Biol Chem , vol.273 , pp. 5841
    • Pan, G.H.1    O'Rourke, K.2    Dixit, V.M.3
  • 27
    • 0031027297 scopus 로고    scopus 로고
    • Activation of a CrmA-insensitive, p35-sensitive pathway in ionizing radiation-induced apoptosis
    • Datta R, Kojima H, Banach D, et al. Activation of a CrmA-insensitive, p35-sensitive pathway in ionizing radiation-induced apoptosis. J Biol Chem. 1997;272:1965.
    • (1997) J Biol Chem , vol.272 , pp. 1965
    • Datta, R.1    Kojima, H.2    Banach, D.3
  • 28
    • 0000194079 scopus 로고    scopus 로고
    • Differential inhibitory effects of CrmA, p35, IAP and three mammalian IAP homologues on apoptosis in NIH3T3 cells following various death stimuli
    • Dorstyn L, Kumar S. Differential inhibitory effects of CrmA, p35, IAP and three mammalian IAP homologues on apoptosis in NIH3T3 cells following various death stimuli. Cell Death Differ. 1997;4: 570.
    • (1997) Cell Death Differ , vol.4 , pp. 570
    • Dorstyn, L.1    Kumar, S.2
  • 29
    • 15644364847 scopus 로고    scopus 로고
    • Essential contribution of caspase 3/CPP32 to apoptosis and its associated nuclear changes
    • Woo M, Hakem R, Soengas MS, et al. Essential contribution of caspase 3/CPP32 to apoptosis and its associated nuclear changes. Genes Dev. 1998;12:806.
    • (1998) Genes Dev , vol.12 , pp. 806
    • Woo, M.1    Hakem, R.2    Soengas, M.S.3
  • 30
    • 0030973417 scopus 로고    scopus 로고
    • Multiple species of CPP32 and Mch2 are the major active caspases present in apoptotic cells
    • Faleiro L, Kobayashi R, Fearnhead H, Lazebnik Y. Multiple species of CPP32 and Mch2 are the major active caspases present in apoptotic cells. EMBO J. 1997;16:2271.
    • (1997) EMBO J , vol.16 , pp. 2271
    • Faleiro, L.1    Kobayashi, R.2    Fearnhead, H.3    Lazebnik, Y.4
  • 31
    • 0024448596 scopus 로고
    • Biology, cytogenetics, and sensitivity to immunological effector cells of new head and neck squamous cell carcinoma lines
    • Heo DS, Snyderman C, Gollin SM, et al. Biology, cytogenetics, and sensitivity to immunological effector cells of new head and neck squamous cell carcinoma lines. Cancer Res. 1989;49:5167.
    • (1989) Cancer Res , vol.49 , pp. 5167
    • Heo, D.S.1    Snyderman, C.2    Gollin, S.M.3
  • 32
    • 0030943468 scopus 로고    scopus 로고
    • Fas stimulation induces RB dephosphorylation and proteolysis that is blocked by inhibitors of the ICE protease family
    • Dou QP, An B, Antoku K, Johnson DE. Fas stimulation induces RB dephosphorylation and proteolysis that is blocked by inhibitors of the ICE protease family. J Cell Biochem. 1997;64:586.
    • (1997) J Cell Biochem , vol.64 , pp. 586
    • Dou, Q.P.1    An, B.2    Antoku, K.3    Johnson, D.E.4
  • 33
    • 0031036984 scopus 로고    scopus 로고
    • Cytometry in cell necrobiology: Analysis of apoptosis and accidental cell death (necrosis)
    • Darzynkiewicz Z, Juan G, Li X, Gorczyca W, Murakami T, Traganos F. Cytometry in cell necrobiology: analysis of apoptosis and accidental cell death (necrosis). Cytometry. 1997;27:1.
    • (1997) Cytometry , vol.27 , pp. 1
    • Darzynkiewicz, Z.1    Juan, G.2    Li, X.3    Gorczyca, W.4    Murakami, T.5    Traganos, F.6
  • 34
    • 0027161821 scopus 로고
    • DIOC6 staining reveals organelle structure and dynamics in living yeast cells
    • Koning AJ, Lum PY, Williams JM, Wright R. DIOC6 staining reveals organelle structure and dynamics in living yeast cells. Cell Motil Cytoskeleton. 1993;25:111.
    • (1993) Cell Motil Cytoskeleton , vol.25 , pp. 111
    • Koning, A.J.1    Lum, P.Y.2    Williams, J.M.3    Wright, R.4
  • 35
    • 0030785790 scopus 로고    scopus 로고
    • The central executioner of apoptosis: Multiple connections between protease activation and mitochondria in Fas/Apo-1/CD95- and ceramide-induced apoptosis
    • Susin SA, Zamzami N, Castedo M, et al. The central executioner of apoptosis: multiple connections between protease activation and mitochondria in Fas/Apo-1/CD95- and ceramide-induced apoptosis. J Exp Med. 1997;186:25.
    • (1997) J Exp Med , vol.186 , pp. 25
    • Susin, S.A.1    Zamzami, N.2    Castedo, M.3
  • 36
    • 0030586675 scopus 로고    scopus 로고
    • Physical and functional association of fcμ receptor on human NK cells with the ζ and Fc∈RI-γ chains and with src-family protein tyrosine kinases
    • Rabinowich H, Manciulea M, Metes M, et al. Physical and functional association of Fcμ receptor on human NK cells with the ζ and Fc∈RI-γ chains and with src-family protein tyrosine kinases. J Immunol. 1996;157:1485.
    • (1996) J Immunol , vol.157 , pp. 1485
    • Rabinowich, H.1    Manciulea, M.2    Metes, M.3
  • 37
    • 0030931876 scopus 로고    scopus 로고
    • Caspases: The executioners of apoptosis
    • Cohen GM. Caspases: the executioners of apoptosis. Biochem J. 1997;326:1.
    • (1997) Biochem J , vol.326 , pp. 1
    • Cohen, G.M.1
  • 39
    • 0029068871 scopus 로고
    • Identification and inhibition of the ICE/CED-3 protease necessary for mammalian apoptosis
    • Nicholson DW, Ali A, Thornberry NA, et al. Identification and inhibition of the ICE/CED-3 protease necessary for mammalian apoptosis. Nature. 1995;376:37.
    • (1995) Nature , vol.376 , pp. 37
    • Nicholson, D.W.1    Ali, A.2    Thornberry, N.A.3
  • 41
    • 0001582524 scopus 로고    scopus 로고
    • Structural characteristics of fluorophores that form intramolecular H-type dimers in a protease substrate
    • Packard BZ, Komoriya A, Toptygin DD, Brand L. Structural characteristics of fluorophores that form intramolecular H-type dimers in a protease substrate. J Phys Chem. 1997;101:5070.
    • (1997) J Phys Chem , vol.101 , pp. 5070
    • Packard, B.Z.1    Komoriya, A.2    Toptygin, D.D.3    Brand, L.4
  • 42
    • 0031673049 scopus 로고    scopus 로고
    • Intramolecular resonance dipole-dipole interactions in a profluorescent protease substrate
    • Packard BZ, Toptygin DD, Komoriya A, Brand L. Intramolecular resonance dipole-dipole interactions in a profluorescent protease substrate. J Phys Chem. 1998;102:752.
    • (1998) J Phys Chem , vol.102 , pp. 752
    • Packard, B.Z.1    Toptygin, D.D.2    Komoriya, A.3    Brand, L.4
  • 43
    • 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.
    • (1996) Cell , vol.85 , pp. 817
    • Muzio, M.1    Chinnaiyan, A.M.2    Kischkel, F.C.3
  • 44
    • 0031018914 scopus 로고    scopus 로고
    • FLICE induced apoptosis in a cell-free system: Cleavage of caspase zymogens
    • Muzio M, Salvesen GS, Dixit VM. FLICE induced apoptosis in a cell-free system: cleavage of caspase zymogens. J Biol Chem. 1997;272:2952.
    • (1997) J Biol Chem , vol.272 , pp. 2952
    • Muzio, M.1    Salvesen, G.S.2    Dixit, V.M.3
  • 45
    • 0031782909 scopus 로고    scopus 로고
    • TRAIL: A molecule with multiple receptors and control mechanisms
    • Griffith TS, Lynch DH. TRAIL: a molecule with multiple receptors and control mechanisms. Curr Opin Immunol. 1998;10:559.
    • (1998) Curr Opin Immunol , vol.10 , pp. 559
    • Griffith, T.S.1    Lynch, D.H.2
  • 46
    • 0344053451 scopus 로고    scopus 로고
    • In vitro activation of CPP32 and Mch3 by Mch4, a novel human apoptotic cysteine protease containing two FADD-like domains
    • Fernandes-Alnemri T, Armstrong RC, Krebs J, et al. In vitro activation of CPP32 and Mch3 by Mch4, a novel human apoptotic cysteine protease containing two FADD-like domains. Proc Natl Acad Sci U S A. 1996;93:7464.
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 7464
    • Fernandes-Alnemri, T.1    Armstrong, R.C.2    Krebs, J.3
  • 47
    • 0031465443 scopus 로고    scopus 로고
    • Conversion of Bcl-2 to a Bax-like death effector by caspases
    • Cheng EH-Y, Kirsh DG, Clem RJ, et al. Conversion of Bcl-2 to a Bax-like death effector by caspases. Science. 1997;278:1966.
    • (1997) Science , vol.278 , pp. 1966
    • Eh-Y, C.1    Kirsh, D.G.2    Clem, R.J.3
  • 48
    • 0030698810 scopus 로고    scopus 로고
    • The apoptosis-necrosis paradox: Apoptogenic proteases activated after mitochondrial permeability transition determine the mode of cell death
    • Hirsch T, Marchetti P, Susin SA, et al. The apoptosis-necrosis paradox: apoptogenic proteases activated after mitochondrial permeability transition determine the mode of cell death. Oncogene. 1997;15:1573.
    • (1997) Oncogene , vol.15 , pp. 1573
    • Hirsch, T.1    Marchetti, P.2    Susin, S.A.3
  • 49
    • 0030897988 scopus 로고    scopus 로고
    • Substrate and inhibitor specificity of interleukin-1 beta-converting enzyme and related caspases
    • Margolin N, Raybuck SA, Wilson KP, et al. Substrate and inhibitor specificity of interleukin-1 beta-converting enzyme and related caspases. J Biol Chem. 1997;272:7223.
    • (1997) J Biol Chem , vol.272 , pp. 7223
    • Margolin, N.1    Raybuck, S.A.2    Wilson, Kp.3
  • 51
    • 0027378767 scopus 로고
    • Loss of T-cell receptor zeta chain and p56lck in T-cells infiltrating human renal cell carcinoma
    • Finke JH, Zea AH, Stanley J, et al. Loss of T-cell receptor zeta chain and p56lck in T-cells infiltrating human renal cell carcinoma. Cancer Res. 1993;53:5613.
    • (1993) Cancer Res , vol.53 , pp. 5613
    • Finke, J.H.1    Zea, A.H.2    Stanley, J.3
  • 52
    • 0030035046 scopus 로고    scopus 로고
    • Alteration in expression and function of signal transducing protains in tumor-associated T and NK cells in patients with ovarian carcinoma
    • Lai P, Rabinowich H, Crowley-Nowick PA, Bell MC, Mantovani G, Whiteside TL. Alteration in expression and function of signal transducing protains in tumor-associated T and NK cells in patients with ovarian carcinoma. Clin Cancer Res. 1996;2:161.
    • (1996) Clin Cancer Res , vol.2 , pp. 161
    • Lai, P.1    Rabinowich, H.2    Crowley-Nowick, P.A.3    Bell, M.C.4    Mantovani, G.5    Whiteside, T.L.6
  • 53
    • 0032473496 scopus 로고    scopus 로고
    • Alpha-viruses induce apoptosis in Bcl-2-overexpressing cells: Evidence for a caspase-mediated, proteolytic inactivalion of Bcl-2
    • Grandgirard D, Studer E, Monney L, et al. Alpha-viruses induce apoptosis in Bcl-2-overexpressing cells: evidence for a caspase-mediated, proteolytic inactivalion of Bcl-2, EMBO J. 1998;17:1268.
    • (1998) EMBO J , vol.17 , pp. 1268
    • Grandgirard, D.1    Studer, E.2    Monney, L.3
  • 54
    • 0033564834 scopus 로고    scopus 로고
    • Primary chemically induced tumors induce profound immunosuppression concomitant with apoptosis and alterations in signal transduction in T cells and NK cells
    • Horiguchi S, Petersson M, Nakazawa T, et al. Primary chemically induced tumors induce profound immunosuppression concomitant with apoptosis and alterations in signal transduction in T cells and NK cells. Cancer Res. 1999;59:2950.
    • (1999) Cancer Res , vol.59 , pp. 2950
    • Horiguchi, S.1    Petersson, M.2    Nakazawa, T.3
  • 55
    • 0032103027 scopus 로고    scopus 로고
    • The Fas counterattack in vivo: Apoptotic depletion of tumor-infiltrating lymphocytes associated with Fas ligand expression by human esophageal carcinoma
    • Bennett MW, O'Connell J, O'Sullivan GC, et al. The Fas counterattack in vivo: apoptotic depletion of tumor-infiltrating lymphocytes associated with Fas ligand expression by human esophageal carcinoma. J Immunol. 1998;160:5669.
    • (1998) J Immunol , vol.160 , pp. 5669
    • Bennett, M.W.1    O'Connell, J.2    O'Sullivan, G.C.3
  • 56
    • 0031756099 scopus 로고    scopus 로고
    • Tumor expression of Fas ligand (CD95L) and the consequences
    • Walker PR, Saas P, Dietrich PY. Tumor expression of Fas ligand (CD95L) and the consequences. Curr Opin Immunol. 1998;10:564.
    • (1998) Curr Opin Immunol , vol.10 , pp. 564
    • Walker, P.R.1    Saas, P.2    Dietrich, P.Y.3
  • 57
    • 0031007840 scopus 로고    scopus 로고
    • Differential involvement of caspases in apoptosis of myeloid leukemic cells induced by chemotherapy versus growth factor withdrawal
    • Barge RM, Willemze R, Vandenabeele P, Fiers W, Beyaert R. Differential involvement of caspases in apoptosis of myeloid leukemic cells induced by chemotherapy versus growth factor withdrawal. FEBS Lett. 1997;409:207.
    • (1997) FEBS Lett , vol.409 , pp. 207
    • Barge, R.M.1    Willemze, R.2    Vandenabeele, P.3    Fiers, W.4    Beyaert, R.5
  • 58
    • 0031919884 scopus 로고    scopus 로고
    • IL-3 withdrawal activates a Crma-insensitive poly(ADP-ribose) polymerase cleavage enzyme in factor-dependent myeloid progenitor cells
    • Antoku K, Liu Z, Johnson DE. IL-3 withdrawal activates a CrmA-insensitive poly(ADP-ribose) polymerase cleavage enzyme in factor-dependent myeloid progenitor cells. Leukemia. 1998;12:682.
    • (1998) Leukemia , vol.12 , pp. 682
    • Antoku, K.1    Liu, Z.2    Johnson, D.E.3
  • 59
    • 0030977847 scopus 로고    scopus 로고
    • Target protease specificity of the viral serpin Crma: Analysis of five caspases
    • Zhou Q, Snipas S, Orth K, Muzio M, Dixit VM, Salvesen GS. Target protease specificity of the viral serpin Crma: analysis of five caspases. J Biol Chem. 1997;272:7797.
    • (1997) J Biol Chem , vol.272 , pp. 7797
    • Zhou, Q.1    Snipas, S.2    Orth, K.3    Muzio, M.4    Dixit, V.M.5    Salvesen, G.S.6
  • 60
    • 8544225061 scopus 로고    scopus 로고
    • Affinity labeling displays the stepwise activation of ICE-related proteases by Fas, staurosporine, and Crma-sensitive caspase-8
    • Takahashi A, Hirata H, Yonehara S, et al. Affinity labeling displays the stepwise activation of ICE-related proteases by Fas, staurosporine, and CrmA-sensitive caspase-8. Oncogene. 1997;14: 2741.
    • (1997) Oncogene , vol.14 , pp. 2741
    • Takahashi, A.1    Hirata, H.2    Yonehara, S.3
  • 61
    • 0030979773 scopus 로고    scopus 로고
    • Double identity for proteins of the Bcl-2 family
    • Reed JC. Double identity for proteins of the Bcl-2 family. Nature. 1997;387:773.
    • (1997) Nature , vol.387 , pp. 773
    • Reed, J.C.1
  • 62
    • 0031037897 scopus 로고    scopus 로고
    • The release of cytochrome c from mitochondria: A primary site for Bcl-2 regulation of apoptosis
    • Kluck RM, Bossywetzel E, Green DR, Newmeyer DD. The release of cytochrome c from mitochondria: a primary site for Bcl-2 regulation of apoptosis. Science. 1997;275:1132.
    • (1997) Science , vol.275 , pp. 1132
    • Kluck, R.M.1    Bossywetzel, E.2    Green, D.R.3    Newmeyer, D.D.4
  • 64
    • 0342978014 scopus 로고    scopus 로고
    • Cell-specific induction of apoptosis by microinjection of cytochrome c: Bcl-X(L) has activity independent of cytochrome c release
    • Li F, Srinivasan A, Wang Y, Armstrong RC, Tomaselli KJ, Fritz LC. Cell-specific induction of apoptosis by microinjection of cytochrome c: Bcl-X(L) has activity independent of cytochrome c release. J Biol Chem. 1997;272:30.299.
    • (1997) J Biol Chem , vol.272 , Issue.30 , pp. 299
    • Li, F.1    Srinivasan, A.2    Wang, Y.3    Armstrong, R.C.4    Tomaselli, K.J.5    Fritz, L.C.6
  • 65
    • 0032515874 scopus 로고    scopus 로고
    • Bcl-XL interacts with Apaf-1 and inhibits Apaf-1-dependent caspase-9 activation
    • Hu Y, Benedict MA, Wu D, Inohara N, Nunez G. Bcl-XL interacts with Apaf-1 and inhibits Apaf-1-dependent caspase-9 activation. Proc Natl Acad Sci U S A. 1998;95:4386.
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 4386
    • Hu, Y.1    Benedict, M.A.2    Wu, D.3    Inohara, N.4    Nunez, G.5
  • 66
    • 0032576692 scopus 로고    scopus 로고
    • Bcl-2 prolongs cell survival after Bax-induced release of cytochrome c
    • Rosse T, Olivier R, Monney L, et al. Bcl-2 prolongs cell survival after Bax-induced release of cytochrome c. Nature. 1998;391:496.
    • (1998) Nature , vol.391 , pp. 496
    • Rosse, T.1    Olivier, R.2    Monney, L.3
  • 67
    • 0032488664 scopus 로고    scopus 로고
    • Bcl-xL acts downstream of caspase-8 activation by the CD95 death-inducing signaling complex
    • Medema JP, Scaffidi C, Krammer PH, Peter ME. Bcl-xL acts downstream of caspase-8 activation by the CD95 death-inducing signaling complex. J Biol Chem. 1998;273:3388.
    • (1998) J Biol Chem , vol.273 , pp. 3388
    • Medema, J.P.1    Scaffidi, C.2    Krammer, P.H.3    Peter, M.E.4
  • 68
    • 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. EMBO J. 1998; 17:1675.
    • (1998) EMBO J , vol.17 , pp. 1675
    • Scaffidi, C.1    Fulda, S.2    Srinivasan, A.3
  • 69
    • 0029609086 scopus 로고
    • Bcl-2 and Fas/APO-1 regulate distinct pathways to lymphocyte apoptosis
    • Strasser A, Harris AW, Huang DC, Krammer PH. Cory S. Bcl-2 and Fas/APO-1 regulate distinct pathways to lymphocyte apoptosis. EMBO J. 1995;14:6136.
    • (1995) EMBO J , vol.14 , pp. 6136
    • Strasser, A.1    Harris, A.W.2    Huang, D.C.3    Krammer, P.H.4    Cory, S.5
  • 71
    • 0032555697 scopus 로고    scopus 로고
    • Cleavage of BID by caspase 8 mediates the mitochondrial damage in the Fas pathway of apoptosis
    • Li H, Zhu H, Xu CJ, Yuan J. Cleavage of BID by caspase 8 mediates the mitochondrial damage in the Fas pathway of apoptosis. Cell. 1998;94:491.
    • (1998) Cell , vol.94 , pp. 491
    • Li, H.1    Zhu, H.2    Xu, C.J.3    Yuan, J.4
  • 72
    • 0032555716 scopus 로고    scopus 로고
    • Bid, a Bcl2 interacting protein, mediates cytochrome c release from mitochondria in response to activation of cell surface death receptors
    • Luo X, Budihardjo I, Zou H, Slaughter C, Wang X. Bid, a Bcl2 interacting protein, mediates cytochrome c release from mitochondria in response to activation of cell surface death receptors. Cell. 1998;94:481.
    • (1998) Cell , vol.94 , pp. 481
    • Luo, X.1    Budihardjo, I.2    Zou, H.3    Slaughter, C.4    Wang, X.5
  • 73
    • 0033534446 scopus 로고    scopus 로고
    • Caspase cleaved BID targets mitochondria and is required for cytochrome c release, while BCL-XL prevents this release but not tumor necrosis factor-R1/Fas death
    • Gross A, Yin XM, Wang K, et al. Caspase cleaved BID targets mitochondria and is required for cytochrome c release, while BCL-XL prevents this release but not tumor necrosis factor-R1/Fas death. J Biol Chem. 1999;274:1156.
    • (1999) J Biol Chem , vol.274 , pp. 1156
    • Gross, A.1    Yin, X.M.2    Wang, K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.