메뉴 건너뛰기




Volumn 26, Issue 2, 2011, Pages 143-152

A novel agonistic anti-human death receptor 5 monoclonal antibody with tumoricidal activity induces caspase- and mitochondrial-dependent apoptosis in human leukemia jurkat cells

Author keywords

apoptosis; death receptor 5; Jurkat cells; monoclonal antibody; TRAIL

Indexed keywords

CASPASE; DEATH RECEPTOR 5; IMMUNOGLOBULIN G1; MONOCLONAL ANTIBODY;

EID: 79955903076     PISSN: 10849785     EISSN: None     Source Type: Journal    
DOI: 10.1089/cbr.2010.0827     Document Type: Article
Times cited : (9)

References (36)
  • 1
    • 13344285339 scopus 로고
    • Identification and characterization of a new member of the TNF family that induces apoptosis
    • Wiley SR, Schooley K, Smolak PJ, et al. Identification and characterization of a new member of the TNF family that induces apoptosis. Immunity 1995;3:673.
    • (1995) Immunity , vol.3 , pp. 673
    • Wiley, S.R.1    Schooley, K.2    Smolak, P.J.3
  • 2
    • 0030996297 scopus 로고    scopus 로고
    • The receptor for the cytotoxic ligand trail
    • Pan G, O Rourke K, Chinnaiyan AM, et al. The receptor for the cytotoxic ligand TRAIL. Science 1997;276:111.
    • (1997) Science , vol.276 , pp. 111
    • Pan, G.1    O Rourke, K.2    Chinnaiyan, A.M.3
  • 3
    • 0037273848 scopus 로고    scopus 로고
    • Apo2L/TRAIL and its death and decoy receptors
    • LeBlanc HN, Ashkenazi A. Apo2L/TRAIL and its death and decoy receptors. Cell Death Differ 2003;10:66.
    • (2003) Cell Death Differ. , vol.10 , pp. 66
    • LeBlanc, H.N.1    Ashkenazi, A.2
  • 4
    • 17544367410 scopus 로고    scopus 로고
    • Induction of apoptosis by Apo-2 ligand a new member of the tumor necrosis factor cytokine family
    • Pitti RM, Marster SA, Ruppert S, et al. Induction of apoptosis by Apo-2 ligand, a new member of the tumor necrosis factor cytokine family. J Biol Chem 1996;271:12687.
    • (1996) J. Biol. Chem. , vol.271 , pp. 12687
    • Pitti, R.M.1    Marster, S.A.2    Ruppert, S.3
  • 5
    • 0030792712 scopus 로고    scopus 로고
    • Control of TRAILinduced apoptosis by a family of signaling and decoy receptors
    • Sheridan JP, Marsters SA, Pitti RM, et al. Control of TRAILinduced apoptosis by a family of signaling and decoy receptors. Science 1997;277:818.
    • (1997) Science , vol.277 , pp. 818
    • Sheridan, J.P.1    Marsters, S.A.2    Pitti, R.M.3
  • 6
    • 50349092260 scopus 로고    scopus 로고
    • A phase 1 study of mapatumumab fully human monoclonal antibody to TRAIL-R1 in patients with advanced solid malignancies
    • Hotte SJ, Hirte HW, Chen EX, et al. A phase 1 study of mapatumumab (fully human monoclonal antibody to TRAIL-R1) in patients with advanced solid malignancies. Clin Cancer Res 2008;14:3450.
    • (2008) Clin. Cancer Res. , vol.14 , pp. 3450
    • Hotte, S.J.1    Hirte, H.W.2    Chen, E.X.3
  • 7
    • 40949138762 scopus 로고    scopus 로고
    • Structural and functional analysis of the interaction between the agonistic monoclonal antibody apomab and the proapoptotic receptor DR5
    • Adams C, Totpal K, Lawrence D, et al. Structural and functional analysis of the interaction between the agonistic monoclonal antibody Apomab and the proapoptotic receptor DR5. Cell Death Differ 2008;15:751.
    • (2008) Cell Death Differ. , vol.15 , pp. 751
    • Adams, C.1    Totpal, K.2    Lawrence, D.3
  • 8
    • 49049086338 scopus 로고    scopus 로고
    • Ligand-based targeting of apoptosis in cancer: The potential of recombinant human apoptosis ligand 2/Tumor necrosis factor-related apoptosis-inducing ligand rhApo2L/TRAIL
    • Ashkenazi A, Holland P, Eckhardt SG. Ligand-based targeting of apoptosis in cancer: The potential of recombinant human apoptosis ligand 2/Tumor necrosis factor-related apoptosis-inducing ligand (rhApo2L/TRAIL).J Clin Oncol 2008;26:3621.
    • (2008) J. Clin. Oncol. , vol.26 , pp. 3621
    • Ashkenazi, A.1    Holland, P.2    Eckhardt, S.G.3
  • 9
    • 0034725664 scopus 로고    scopus 로고
    • Temperaturesensitive differential affinity of TRAIL for its receptors DR5 is the highest affinity receptor
    • Truneh A, Sharma S, Silverman C, et al. Temperaturesensitive differential affinity of TRAIL for its receptors. DR5 is the highest affinity receptor. J Biol Chem 2000;275:23319.
    • (2000) J. Biol. Chem. , vol.275 , pp. 23319
    • Truneh, A.1    Sharma, S.2    Silverman, C.3
  • 10
    • 0038574326 scopus 로고    scopus 로고
    • Analysis of trail receptor expression using a novel anti-trail death receptor 5 monoclonal antibody
    • Yuan-Fang Ma, Dong-Liang D, You-Hai Chen. Analysis of TRAIL receptor expression using a novel anti-TRAIL death receptor 5 monoclonal antibody. Chin Med J 2003;116:947.
    • (2003) Chin. Med. J. , vol.116 , pp. 947
    • Yuan-Fang, M.A.1    Dong-Liang, D.2    You-Hai, C.3
  • 11
    • 0034022160 scopus 로고    scopus 로고
    • Apoptosis induced in normal human hepatocytes by tumor necrosis factor-related apoptosis-inducing ligand
    • Jo M, Kim TH, Seol DW, et al. Apoptosis induced in normal human hepatocytes by tumor necrosis factor-related apoptosis- inducing ligand. Nat Med 2000;6:564.
    • (2000) Nat. Med. , vol.6 , pp. 564
    • Jo, M.1    Kim, T.H.2    Seol, D.W.3
  • 12
    • 0035050960 scopus 로고    scopus 로고
    • Differential hepatocyte toxicity of recombinant Apo2L/TRAIL versions
    • Lawrence D, Shahrokh Z, Marsters S, et al. Differential hepatocyte toxicity of recombinant Apo2L/TRAIL versions. Nat Med 2001;7:383.
    • (2001) Nat. Med. , vol.7 , pp. 383
    • Lawrence, D.1    Shahrokh, Z.2    Marsters, S.3
  • 13
    • 17944376030 scopus 로고    scopus 로고
    • Tumoricidal activity of a novel anti-human DR5 monoclonal antibidy without hepatocytotoxicity
    • Ichikawa K, Liu W, Zhao L, et al. Tumoricidal activity of a novel anti-human DR5 monoclonal antibidy without hepatocytotoxicity. Nat Med 2001;7:954.
    • (2001) Nat. Med. , vol.7 , pp. 954
    • Ichikawa, K.1    Liu, W.2    Zhao, L.3
  • 14
    • 45749098451 scopus 로고    scopus 로고
    • To kill a tumor cell: The porential of proapoptotic receptor agonists
    • Ashkenazi A, Herbst RS. To kill a tumor cell: The porential of proapoptotic receptor agonists. J Clin Invest 2008;118: 1979.
    • (2008) J. Clin. Invest. , vol.118 , pp. 1979
    • Ashkenazi, A.1    Herbst, R.S.2
  • 15
    • 33750090076 scopus 로고    scopus 로고
    • Preparation and Characterization of a novel agonistic anti-human death receptor 5 monoclonal antibody with apoptosis activity
    • In Chinese
    • Guang-chao Liu, Yuan-fang Ma, Shu-lian Li, et al. Preparation and Characterization of a novel agonistic anti-human death receptor 5 monoclonal antibody with apoptosis activity. Chin J Microbiol Immunology (In Chinese) 2006:26:632.
    • (2006) Chin. J. Microbiol. Immunology. , vol.26 , pp. 632
    • Liu, G.-C.1    Ma, Y.-F.2    Li, S.-L.3
  • 16
    • 79952117056 scopus 로고    scopus 로고
    • Leukemic cell apoptosis induced by anti-human DR5 monoclonal antibody mDRA-6
    • In Chinese
    • Shu-lian Li,Yuan-fang Ma, Guang-chao Liu, et al. Leukemic cell apoptosis induced by anti-human DR5 monoclonal antibody mDRA-6. Xi Bao Yu Fen Zi Mian Yi Xue Za Zhi (In Chinese) 2007;23:754.
    • (2007) Xi Bao Yu Fen Zi Mian Yi Xue Za Zhi , vol.23 , pp. 754
    • Li, S.-L.1    Ma, Y.-F.2    Liu, G.-C.3
  • 17
    • 36048941011 scopus 로고    scopus 로고
    • Adriamycin enhances anti-human DR5 monoclonal antibody mDRA-6 induced HL-60 cells apoptosis
    • In Chinese
    • Shu-lian Li, Yuan-fang Ma, Guang-chao Liu, et al. Adriamycin enhances anti-human DR5 monoclonal antibody (mDRA-6) induced HL-60 cells apoptosis. Zhonghua Xue Ye Xue Za Zhi (In Chinese) 2006;27:461.
    • (2006) Zhonghua Xue Ye Xue Za Zhi , vol.27 , pp. 461
    • Li, S.-L.1    Ma, Y.-F.2    Liu, G.-C.3
  • 18
    • 35648992556 scopus 로고    scopus 로고
    • A novel homospermidine conjugate inhibits growth and induces apoptosis in human hepatoma cells
    • Song-qiang Xie, Ying-liang Wu, Peng-fei Cheng, et al. A novel homospermidine conjugate inhibits growth and induces apoptosis in human hepatoma cells. Acta Pharmacol Sin 2007;28:1827.
    • (2007) Acta. Pharmacol. Sin. , vol.28 , pp. 1827
    • Xie, S.-Q.1    Wu, Y.-L.2    Cheng, P.-F.3
  • 19
    • 65349125624 scopus 로고    scopus 로고
    • Effect of anti-human DR5 monoclonal antibody on the apoptosis of human hepatocyte HL7702 cell lines
    • In Chinese
    • Jun Zhang, Yuan-fang Ma, Guang-chao Liu, et al. Effect of anti-human DR5 monoclonal antibody on the apoptosis of human hepatocyte HL7702 cell lines. Xi Bao Yu Fen Zi Mian Yi Xue Za Zhi (In Chinese) 2006;22:641.
    • (2006) Xi Bao Yu Fen Zi Mian Yi Xue Za Zhi , vol.22 , pp. 641
    • Zhang, J.1    Ma, Y.-F.2    Liu, G.-C.3
  • 20
    • 70349528993 scopus 로고    scopus 로고
    • Synergistic lethal effect of mDRA-6 and nimesulide on human hepatocellular cancer cell line SMMC-7721
    • In Chinese
    • Ying-jie Liu, Yuan-fang Ma, Jun Zhang, et al. Synergistic lethal effect of mDRA-6 and nimesulide on human hepatocellular cancer cell line SMMC-7721. AI Zheng (In Chinese) 2008;27:374.
    • (2008) AI Zheng , vol.27 , pp. 374
    • Liu, Y.-J.1    Ma, Y.-F.2    Zhang, J.3
  • 21
    • 29644444314 scopus 로고    scopus 로고
    • A novel antihuman DR5 monoclonal antibody with tumoricidal activity induces caspase-dependent and caspase-independendent cell death
    • Ya-bin Guo, Cai-feng Chen, Yong Zheng, et al. A novel antihuman DR5 monoclonal antibody with tumoricidal activity induces caspase-dependent and caspase-independendent cell death. J Biol Chem 2005;280:41940.
    • (2005) J. Biol. Chem. , vol.280 , pp. 41940
    • Guo, Y.-B.1    Chen, C.-F.2    Zheng, Y.3
  • 22
    • 0034949763 scopus 로고    scopus 로고
    • Different roles of spermine in glucocorticoid and Fas-induced apoptosis
    • Hegardt C, Andersson G, Oredsson SM. Different roles of spermine in glucocorticoid and Fas-induced apoptosis. Exp Cell Res 2001;266:333.
    • (2001) Exp. Cell Res. , vol.266 , pp. 333
    • Hegardt, C.1    Andersson, G.2    Oredsson, S.M.3
  • 23
    • 0032575714 scopus 로고    scopus 로고
    • Death receptors: Signaling and modulation
    • Ashkenazi A, Dixit VM. Death receptors: Signaling and modulation. Science 1998;281:1305.
    • (1998) Science , vol.281 , pp. 1305
    • Ashkenazi, A.1    Dixit, V.M.2
  • 24
    • 0033790715 scopus 로고    scopus 로고
    • TRAIL receptor-2 signals apoptosis through FADD and caspase-8
    • Bodmer JL, Holler N, Reynard S, et al. TRAIL receptor-2 signals apoptosis through FADD and caspase-8. Nat Cell Biol 2000;2:241.
    • (2000) Nat. Cell Biol. , vol.2 , pp. 241
    • Bodmer, J.L.1    Holler, N.2    Reynard, S.3
  • 25
    • 0033662433 scopus 로고    scopus 로고
    • Apo2L/ TRAIL-dependent recruitment of endogenous FADD and caspase-8 to death receptors 4 and 5
    • Kischkel FC, Lawrence DA, Chuntharapai A, et al. Apo2L/ TRAIL-dependent recruitment of endogenous FADD and caspase-8 to death receptors 4 and 5. Immunity 2000;12:611.
    • (2000) Immunity , vol.12 , pp. 611
    • Kischkel, F.C.1    Lawrence, D.A.2    Chuntharapai, A.3
  • 26
    • 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, et al. 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
  • 27
    • 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, et al. 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
  • 28
    • 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
  • 29
    • 0034058683 scopus 로고    scopus 로고
    • Distinct stages of cytochrome c release from mitochondria: Evidence for a feedback amplification loop linking caspase activation to mitochondrial dysfunction in genotoxic stress induced apoptosis
    • Chen Q, Gong B, Almasan A. Distinct stages of cytochrome c release from mitochondria: Evidence for a feedback amplification loop linking caspase activation to mitochondrial dysfunction in genotoxic stress induced apoptosis. Cell Death Differ 2000;7:227.
    • (2000) Cell Death Differ. , vol.7 , pp. 227
    • Chen, Q.1    Gong, B.2    Almasan, A.3
  • 30
    • 0030026865 scopus 로고    scopus 로고
    • Bax-independent inhibition of apoptosis by Bcl-XL
    • Cheng EH, Levine B, Boise LH, et al. Bax-independent inhibition of apoptosis by Bcl-XL. Nature 1996;379:554.
    • (1996) Nature , vol.379 , pp. 554
    • Cheng, E.H.1    Levine, B.2    Boise, L.H.3
  • 31
    • 0032575688 scopus 로고    scopus 로고
    • The Bcl-2 protein family: Arbiters of cell survival
    • Adams JM, Cory S. The Bcl-2 protein family: Arbiters of cell survival. Science 1998;281:1322.
    • (1998) Science , vol.281 , pp. 1322
    • Adams, J.M.1    Cory, S.2
  • 32
    • 0031036872 scopus 로고    scopus 로고
    • Prevention of apoptosis by Bcl-2: Release of cytochrome c from mitochondria blocked
    • Yang J, Liu X, Bhalla K, et al. Prevention of apoptosis by Bcl-2: Release of cytochrome c from mitochondria blocked. Science 1997;275:1129.
    • (1997) Science , vol.275 , pp. 1129
    • Yang, J.1    Liu, X.2    Bhalla, K.3
  • 33
    • 0031037897 scopus 로고    scopus 로고
    • The release of cytochrome c from mitochondria: A primary site for Bcl-2 regulation of apoptosis
    • Kluck RM, Bossy-Wetzel E, Green DR, et al. 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    Bossy-Wetzel, E.2    Green, D.R.3
  • 34
    • 0029912189 scopus 로고    scopus 로고
    • Molecular ordering of the cell death pathway, Bcl-2 and Bcl-xl function upstream of the CED-3-like apoptotic proteases
    • Chinnaiyan AM, Orth K, O Rourke K, et al. Molecular ordering of the cell death pathway, Bcl-2 and Bcl-xl function upstream of the CED-3-like apoptotic proteases. J Biol Chem 1996;271:4573.
    • (1996) J Biol Chem , vol.271 , pp. 4573
    • Chinnaiyan, A.M.1    Orth, K.2    O Rourke, K.3
  • 35
    • 0033179760 scopus 로고    scopus 로고
    • BCL-2 family members and the mitochondria in apoptosis
    • Gross A, McDonnell JM, Korsmeyer SJ. BCL-2 family members and the mitochondria in apoptosis. Genes Dev 1999;13:1899.
    • (1999) Genes. Dev. , vol.13 , pp. 1899
    • Gross, A.1    McDonnell, J.M.2    Korsmeyer, S.J.3
  • 36
    • 0032535730 scopus 로고    scopus 로고
    • Blood cells with reduced mitochondrial membrane potential and cytosolic cytochrome c can survive and maintain clonogenicity given appropriate signals to suppress apoptosis
    • Chen Q, Takeyama N, Brady G, et al. Blood cells with reduced mitochondrial membrane potential and cytosolic cytochrome c can survive and maintain clonogenicity given appropriate signals to suppress apoptosis. Blood 1998;92: 4545.
    • (1998) Blood , vol.92 , pp. 4545
    • Chen, Q.1    Takeyama, N.2    Brady, G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.