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Volumn 2, Issue 1, 1999, Pages 21-29

Activation and role of caspases in chemotherapy-induced apoptosis

Author keywords

[No Author keywords available]

Indexed keywords

ANTINEOPLASTIC AGENT; CAMPTOTHECIN; CASPASE; CISPLATIN; CYTARABINE; CYTOCHROME C; DNA TOPOISOMERASE INHIBITOR; ETOPOSIDE; FAS ANTIGEN; GYRASE INHIBITOR; PACLITAXEL; PROTEIN BAX; PROTEIN BCL 2; PROTEIN BCL X; VINBLASTINE;

EID: 0033082063     PISSN: 13687646     EISSN: None     Source Type: Journal    
DOI: 10.1054/drup.1999.0065     Document Type: Article
Times cited : (20)

References (84)
  • 1
    • 0015383455 scopus 로고
    • Apoptosis: A basic biological phenomenon with wide-ranging implications in tissue kinetics
    • Kerr J. F., Wyllie A. H., Currie A. R. Apoptosis: a basic biological phenomenon with wide-ranging implications in tissue kinetics. Br J Cancer. 26:1972;239-257.
    • (1972) Br J Cancer , vol.26 , pp. 239-257
    • Kerr, J.F.1    Wyllie, A.H.2    Currie, A.R.3
  • 2
    • 0031046848 scopus 로고    scopus 로고
    • Apoptosis and disease - Regulation and clinical relevance of programmed cell death
    • Rudin C. M., Thompson C. B. Apoptosis and disease - Regulation and clinical relevance of programmed cell death. Ann Rev Med. 48:1997;267-281.
    • (1997) Ann Rev Med , vol.48 , pp. 267-281
    • Rudin, C.M.1    Thompson, C.B.2
  • 3
    • 0031464448 scopus 로고    scopus 로고
    • Bcl-2 family proteins - Regulators of apoptosis and chemoresistance in hematologic malignancies
    • Reed J. C. Bcl-2 family proteins - Regulators of apoptosis and chemoresistance in hematologic malignancies. Seminars in Hematology. 34:1997;9-19.
    • (1997) Seminars in Hematology , vol.34 , pp. 9-19
    • Reed, J.C.1
  • 4
    • 0026582702 scopus 로고
    • Caenorhabditis elegans gene ced-9 protects cells from programmed cell death
    • Hengartner M. O., Ellis R. E., Horvitz H. R. Caenorhabditis elegans gene ced-9 protects cells from programmed cell death. Nature. 356:1992;494-496.
    • (1992) Nature , vol.356 , pp. 494-496
    • Hengartner, M.O.1    Ellis, R.E.2    Horvitz, H.R.3
  • 5
    • 0026448963 scopus 로고
    • The Caenorhabditis elegans cell death gene ced-4 encodes a novel protein and is expressed during the period of extensive programmed cell death
    • Yuan J., Horvitz H. R. The Caenorhabditis elegans cell death gene ced-4 encodes a novel protein and is expressed during the period of extensive programmed cell death. Development 1992;116:309-320.
    • (1992) Development , vol.116 , pp. 309-320
    • Yuan, J.1    Horvitz, H.R.2
  • 8
    • 0031918223 scopus 로고    scopus 로고
    • BCL-2 family - Regulators of cell death
    • Chao D. T., Korsmeyer S. J. BCL-2 family - regulators of cell death. Annu Rev Immunol. 16:1998;395-419.
    • (1998) Annu Rev Immunol , vol.16 , pp. 395-419
    • Chao, D.T.1    Korsmeyer, S.J.2
  • 10
    • 0031044652 scopus 로고    scopus 로고
    • Mammalian cell death proteases - A family of highly conserved aspartate specific cysteine proteases
    • Alnemri E. S. Mammalian cell death proteases - a family of highly conserved aspartate specific cysteine proteases. J Cell Biochem. 64:1997;33-42.
    • (1997) J Cell Biochem , vol.64 , pp. 33-42
    • Alnemri, E.S.1
  • 11
    • 2642689658 scopus 로고    scopus 로고
    • Proteases to die for
    • Cryns V., Yuan J. Y. Proteases to die for. Genes Dev. 12:1998;1551-1570.
    • (1998) Genes Dev , vol.12 , pp. 1551-1570
    • Cryns, V.1    Yuan, J.Y.2
  • 14
    • 0031034997 scopus 로고    scopus 로고
    • Interaction of Ced-4 with Ced-3 and Ced-9 - A molecular framework for cell death
    • Chinnaiyan A. M., Orourke K., Lane B. R., Dixit V. M. Interaction of Ced-4 with Ced-3 and Ced-9 - a molecular framework for cell death. Science. 275:1997;1122-1126.
    • (1997) Science , vol.275 , pp. 1122-1126
    • Chinnaiyan, A.M.1    Orourke, K.2    Lane, B.R.3    Dixit, V.M.4
  • 15
    • 0030715323 scopus 로고    scopus 로고
    • Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade
    • Li P., Nijhawan D., Budihardjo I. Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade. Cell. 91:1997;479-489.
    • (1997) Cell , vol.91 , pp. 479-489
    • Li, P.1    Nijhawan, D.2    Budihardjo, I.3
  • 16
    • 0032489390 scopus 로고    scopus 로고
    • Caspase-9, Bcl-X-L, and Apaf-1 form a ternary complex
    • Pan G. H., Orourke K., Dixit V. M. Caspase-9, Bcl-X-L, and Apaf-1 form a ternary complex. J Biol Chem. 273:1998;5841-5845.
    • (1998) J Biol Chem , vol.273 , pp. 5841-5845
    • Pan, G.H.1    Orourke, K.2    Dixit, V.M.3
  • 17
    • 0032515874 scopus 로고    scopus 로고
    • Bcl-X-L interacts with Apaf-1 and inhibits Apaf-1-dependent caspase-9 activation
    • Hu Y. M., Benedict M. A., Wu D. Y., Inohara N., Nunez G. Bcl-X-L interacts with Apaf-1 and inhibits Apaf-1-dependent caspase-9 activation. Proc Nat Acad Sci USA. 95:1998;4386-4391.
    • (1998) Proc Nat Acad Sci USA , vol.95 , pp. 4386-4391
    • Hu, Y.M.1    Benedict, M.A.2    Wu, D.Y.3    Inohara, N.4    Nunez, G.5
  • 18
    • 0032080197 scopus 로고    scopus 로고
    • Defects in regulation of apoptosis in caspase-2-deficient mice
    • Bergeron L., Perez G. I., Macdonald G. Defects in regulation of apoptosis in caspase-2-deficient mice. Genes Devel. 12:1998;1304-1314.
    • (1998) Genes Devel , vol.12 , pp. 1304-1314
    • Bergeron, L.1    Perez, G.I.2    Macdonald, G.3
  • 19
    • 0029956641 scopus 로고    scopus 로고
    • Decreased apoptosis in the brain and premature lethality in Cpp32-deficient mice
    • Kuida K., Zheng T. S., Na S. Q. Decreased apoptosis in the brain and premature lethality in Cpp32-deficient mice. Nature. 384:1996;368-372.
    • (1996) Nature , vol.384 , pp. 368-372
    • Kuida, K.1    Zheng, T.S.2    Na, S.Q.3
  • 20
    • 0032143986 scopus 로고    scopus 로고
    • Targeted disruption of the mouse caspase 8 gene ablates cell death induction by the TNF receptors, Fas/Apo1, and Dr3 and is lethal prenatally
    • Varfolomeev E. E., Schuchmann M., Luria V. Targeted disruption of the mouse caspase 8 gene ablates cell death induction by the TNF receptors, Fas/Apo1, and Dr3 and is lethal prenatally. Immunity. 9:1998;267-276.
    • (1998) Immunity , vol.9 , pp. 267-276
    • Varfolomeev, E.E.1    Schuchmann, M.2    Luria, V.3
  • 21
    • 0032493910 scopus 로고    scopus 로고
    • Reduced apoptosis and cytochrome c-mediated caspase activation in mice lacking caspase 9
    • Kuida K., Haydar T. F., Kuan C. Y. Reduced apoptosis and cytochrome c-mediated caspase activation in mice lacking caspase 9. Cell. 94:1998;325-337.
    • (1998) Cell , vol.94 , pp. 325-337
    • Kuida, K.1    Haydar, T.F.2    Kuan, C.Y.3
  • 22
    • 0032493870 scopus 로고    scopus 로고
    • Differential requirement for caspase 9 in apoptotic pathways in vivo
    • Hakem R., Hakem A., Duncan G. S. Differential requirement for caspase 9 in apoptotic pathways in vivo. Cell. 94:1998;339-352.
    • (1998) Cell , vol.94 , pp. 339-352
    • Hakem, R.1    Hakem, A.2    Duncan, G.S.3
  • 23
    • 0028920863 scopus 로고
    • Altered cytokine export and apoptosis in mice deficient in interleukin-1 beta converting enzyme
    • Kuida K., Lippke J. A., Ku G. Altered cytokine export and apoptosis in mice deficient in interleukin-1 beta converting enzyme. Science. 267:1995;2000-2003.
    • (1995) Science , vol.267 , pp. 2000-2003
    • Kuida, K.1    Lippke, J.A.2    Ku, G.3
  • 24
    • 0032548919 scopus 로고    scopus 로고
    • Murine caspase-11, an ICE-interacting protease, is essential for the activation of ICE
    • Wang S. Y., Miura M., Jung Y. K., Zhu H., Li E., Yuan J. Y. Murine caspase-11, an ICE-interacting protease, is essential for the activation of ICE. Cell. 92:1998;501-509.
    • (1998) Cell , vol.92 , pp. 501-509
    • Wang, S.Y.1    Miura, M.2    Jung, Y.K.3    Zhu, H.4    Li, E.5    Yuan, J.Y.6
  • 25
    • 0032580361 scopus 로고    scopus 로고
    • Subcellular and submitochondrial mode of action of bcl-2-like oncoproteins
    • Zamzami N., Brenner C., Marzo I., Susin S. A., Kroemer G. Subcellular and submitochondrial mode of action of bcl-2-like oncoproteins. Oncogene. 16:1998;2265-2282.
    • (1998) Oncogene , vol.16 , pp. 2265-2282
    • Zamzami, N.1    Brenner, C.2    Marzo, I.3    Susin, S.A.4    Kroemer, G.5
  • 26
    • 0032544449 scopus 로고    scopus 로고
    • Apaf-1 (Ced-4 homolog) regulates programmed cell death in mammalian development
    • Cecconi F., Alvarezbolado G., Meyer B. I., Roth K. A., Gruss P. Apaf-1 (Ced-4 homolog) regulates programmed cell death in mammalian development. Cell. 94:1998;727-737.
    • (1998) Cell , vol.94 , pp. 727-737
    • Cecconi, F.1    Alvarezbolado, G.2    Meyer, B.I.3    Roth, K.A.4    Gruss, P.5
  • 27
    • 0032544564 scopus 로고    scopus 로고
    • Apaf1 is required for mitochondrial pathways of apoptosis and brain development
    • Yoshida H., Kong Y. Y., Yoshida R. Apaf1 is required for mitochondrial pathways of apoptosis and brain development. Cell. 94:1998;739-750.
    • (1998) Cell , vol.94 , pp. 739-750
    • Yoshida, H.1    Kong, Y.Y.2    Yoshida, R.3
  • 28
    • 0030849093 scopus 로고    scopus 로고
    • A combinatorial approach defines specificities of members of the caspase family and granzyme B - Functional relationships established for key mediators of apoptosis
    • Thornberry N. A., Ranon T. A., Pieterson E. P. A combinatorial approach defines specificities of members of the caspase family and granzyme B - functional relationships established for key mediators of apoptosis. J Biol Chem. 272:1997;17907-17911.
    • (1997) J Biol Chem , vol.272 , pp. 17907-17911
    • Thornberry, N.A.1    Ranon, T.A.2    Pieterson, E.P.3
  • 29
    • 0030916417 scopus 로고    scopus 로고
    • DFF, a heterodimeric protein that functions downstream of caspase-3 to trigger DNA fragmentation during apoptosis
    • Liu X. S., Zou H., Slaughter C., Wang X. D. DFF, a heterodimeric protein that functions downstream of caspase-3 to trigger DNA fragmentation during apoptosis. Cell. 89:1997;175-184.
    • (1997) Cell , vol.89 , pp. 175-184
    • Liu, X.S.1    Zou, H.2    Slaughter, C.3    Wang, X.D.4
  • 30
    • 0031888955 scopus 로고    scopus 로고
    • Caspase-activated DNAse that degrades DNA during apoptosis, and its inhibitor ICAD
    • Enari M., Sakahira H., Yokoyama H., Okawa K., Iwamatsu A., Nagata S. A. Caspase-activated DNAse that degrades DNA during apoptosis, and its inhibitor ICAD. Nature. 391:1998;43-50.
    • (1998) Nature , vol.391 , pp. 43-50
    • Enari, M.1    Sakahira, H.2    Yokoyama, H.3    Okawa, K.4    Iwamatsu, A.5    Nagata, S.A.6
  • 32
    • 0027971322 scopus 로고
    • Purification of a 24-kD protease from apoptotic tumor cells that activates DNA fragmentation
    • Wright S. C., Wei Q. S., Zhong J., Zheng H., Kinder D. H., Larrick J. W. Purification of a 24-kD protease from apoptotic tumor cells that activates DNA fragmentation. J Exp Med. 180:1994;2113-2123.
    • (1994) J Exp Med , vol.180 , pp. 2113-2123
    • Wright, S.C.1    Wei, Q.S.2    Zhong, J.3    Zheng, H.4    Kinder, D.H.5    Larrick, J.W.6
  • 33
    • 0032528175 scopus 로고    scopus 로고
    • Distinct steps in DNA fragmentation pathway during camptothecin-induced apoptosis involved caspase-, benzyloxycarbonyl- and N-tosyl-L-phenylalanylchloromethyl ketone-sensitive activities
    • Sane A. T., Bertrand R. Distinct steps in DNA fragmentation pathway during camptothecin-induced apoptosis involved caspase-, benzyloxycarbonyl- and N-tosyl-L-phenylalanylchloromethyl ketone-sensitive activities. Cancer Res. 58:1998;3066-3072.
    • (1998) Cancer Res , vol.58 , pp. 3066-3072
    • Sane, A.T.1    Bertrand, R.2
  • 34
    • 0032525332 scopus 로고    scopus 로고
    • 2+-dependent endonuclease (AN34) from etoposide-treated human leukemia HL-60 cells undergoing apoptosis
    • 2+-dependent endonuclease (AN34) from etoposide-treated human leukemia HL-60 cells undergoing apoptosis. Cancer Res. 58:1998;2576-2582.
    • (1998) Cancer Res , vol.58 , pp. 2576-2582
    • Yoshida, A.1    Pourquier, P.2    Pommier, Y.3
  • 35
    • 0028979439 scopus 로고
    • Bcl-X(L) is expressed in neuroblastoma cells and modulates chemotherapy-induced apoptosis
    • Dole M. G., Jasty R., Cooper M. J., Thompson C. B., Nunez G., Castle V. P. Bcl-X(L) is expressed in neuroblastoma cells and modulates chemotherapy-induced apoptosis. Cancer Res. 55:1995;2576-2582.
    • (1995) Cancer Res , vol.55 , pp. 2576-2582
    • Dole, M.G.1    Jasty, R.2    Cooper, M.J.3    Thompson, C.B.4    Nunez, G.5    Castle, V.P.6
  • 36
    • 0029658187 scopus 로고    scopus 로고
    • Bcl-X(L) overexpression inhibits taxol-induced YAMA protease activity and apoptosis
    • Ibrado A. M., Huang Y., Fang G. F., Bhalla K. Bcl-X(L) overexpression inhibits taxol-induced YAMA protease activity and apoptosis. Cell Growth Diff. 7:1996;1087-1094.
    • (1996) Cell Growth Diff , vol.7 , pp. 1087-1094
    • Ibrado, A.M.1    Huang, Y.2    Fang, G.F.3    Bhalla, K.4
  • 37
    • 0030795866 scopus 로고    scopus 로고
    • Bcl-2 and Bcl-XL can differentially block chemotherapy-induced cell death
    • Simonian P. L., Grillot D. A. M., Nunez G. Bcl-2 and Bcl-XL can differentially block chemotherapy-induced cell death. Blood. 90:1997;1208-1216.
    • (1997) Blood , vol.90 , pp. 1208-1216
    • Simonian, P.L.1    Grillot, D.A.M.2    Nunez, G.3
  • 38
    • 0031843863 scopus 로고    scopus 로고
    • Bcl-xL modulates apoptosis induced by anticancer drugs and delays DEVDase and DNA fragmentation-promoting activities
    • Schmitt E., Cimoli G., Steyaert A., Bertrand R. Bcl-xL modulates apoptosis induced by anticancer drugs and delays DEVDase and DNA fragmentation-promoting activities. Exp Cell Res. 240:1998;107-121.
    • (1998) Exp Cell Res , vol.240 , pp. 107-121
    • Schmitt, E.1    Cimoli, G.2    Steyaert, A.3    Bertrand, R.4
  • 39
    • 0031870835 scopus 로고    scopus 로고
    • Bax-alpha promotes apoptosis induced by cancer chemotherapy and accelerates the activation of caspase 3-like cysteine proteases in p53 double mutant B lymphoma Namalwa cells
    • Schmitt E., Steyaert A., Cimoli G., Bertrand R. Bax-alpha promotes apoptosis induced by cancer chemotherapy and accelerates the activation of caspase 3-like cysteine proteases in p53 double mutant B lymphoma Namalwa cells. Cell Death Diff. 5:1998;506-516.
    • (1998) Cell Death Diff , vol.5 , pp. 506-516
    • Schmitt, E.1    Steyaert, A.2    Cimoli, G.3    Bertrand, R.4
  • 40
    • 0032504575 scopus 로고    scopus 로고
    • Mitochondria as regulators of apoptosis - Doubt no more
    • Susin S. A., Zamzami N., Kroemer G. Mitochondria as regulators of apoptosis - doubt no more. Biochim Biophys Acta. 1366:1998;151-165.
    • (1998) Biochim Biophys Acta , vol.1366 , pp. 151-165
    • Susin, S.A.1    Zamzami, N.2    Kroemer, G.3
  • 41
    • 0031974274 scopus 로고    scopus 로고
    • Mitochondria in chemotherapy-induced apoptosis - A prospective novel target of cancer therapy
    • Decaudin D., Marzo I., Brenner C., Kroemer G. Mitochondria in chemotherapy-induced apoptosis - a prospective novel target of cancer therapy. Int J Oncol. 12:1998;141-152.
    • (1998) Int J Oncol , vol.12 , pp. 141-152
    • Decaudin, D.1    Marzo, I.2    Brenner, C.3    Kroemer, G.4
  • 43
    • 0030581151 scopus 로고    scopus 로고
    • Induction of apoptotic program in cell-free extracts:requirement for dATP and cytochrome c
    • Liu X., Kim C. N., Yang J., Wang X. Induction of apoptotic program in cell-free extracts:requirement for dATP and cytochrome c. Cell. 86:1996;147-157.
    • (1996) Cell , vol.86 , pp. 147-157
    • Liu, X.1    Kim, C.N.2    Yang, J.3    Wang, X.4
  • 45
    • 0032502855 scopus 로고    scopus 로고
    • Activation of caspases triggered by cytochrome c in vitro
    • Pan G. H., Humke E. W., Dixit V. M. Activation of caspases triggered by cytochrome c in vitro. FEBS Letters. 426:1998;151-154.
    • (1998) FEBS Letters , vol.426 , pp. 151-154
    • Pan, G.H.1    Humke, E.W.2    Dixit, V.M.3
  • 46
    • 0031037897 scopus 로고    scopus 로고
    • The release of cytochrome c from mitochondria - A primary site for Bcl-2 regulation of apoptosis
    • Kluck R. M., Bossywetzel E., Green D. R., Newmeyer D. D. The release of cytochrome c from mitochondria - a primary site for Bcl-2 regulation of apoptosis. Science. 275:1997;1132-1136.
    • (1997) Science , vol.275 , pp. 1132-1136
    • Kluck, R.M.1    Bossywetzel, E.2    Green, D.R.3    Newmeyer, D.D.4
  • 47
    • 0031036872 scopus 로고    scopus 로고
    • Prevention of apoptosis by Bcl-2 - Release of cytochrome c from mitochondria blocked
    • Yang J., Liu X. S., Bhalla K. Prevention of apoptosis by Bcl-2 - release of cytochrome c from mitochondria blocked. Science. 275:1997;1129-1132.
    • (1997) Science , vol.275 , pp. 1129-1132
    • Yang, J.1    Liu, X.S.2    Bhalla, K.3
  • 48
    • 0030610962 scopus 로고    scopus 로고
    • Bcl-X(L) as an inhibitor of cytosolic cytochrome c accumulation in DNA damage-induced apoptosis
    • Kharbanda S., Pandey P., Schofield L. Bcl-X(L) as an inhibitor of cytosolic cytochrome c accumulation in DNA damage-induced apoptosis. Proc Nat Acad Sci (USA). 94:1997;6939-6942.
    • (1997) Proc Nat Acad Sci (USA) , vol.94 , pp. 6939-6942
    • Kharbanda, S.1    Pandey, P.2    Schofield, L.3
  • 49
    • 0032576692 scopus 로고    scopus 로고
    • Bcl-2 prolongs cell survival after Bax-induced release of cytochrome c
    • Rosse T., Olivier R., Monney L. Bcl-2 prolongs cell survival after Bax-induced release of cytochrome c. Nature. 391:1998;496-499.
    • (1998) Nature , vol.391 , pp. 496-499
    • Rosse, T.1    Olivier, R.2    Monney, L.3
  • 50
    • 0029906828 scopus 로고    scopus 로고
    • Bax-induced cell death may not require interleukin 1-beta-converting enzyme-like proteases
    • Xiang J. L., Chao D. T., Korsmeyer S. J. Bax-induced cell death may not require interleukin 1-beta-converting enzyme-like proteases. Proc Nat Acad Sci (USA). 93:1996;14559-14563.
    • (1996) Proc Nat Acad Sci (USA) , vol.93 , pp. 14559-14563
    • Xiang, J.L.1    Chao, D.T.2    Korsmeyer, S.J.3
  • 52
    • 0032472329 scopus 로고    scopus 로고
    • Mitochondrial cytochrome C release in apoptosis occurs upstream of DEVD-specific caspase activation and independently of mitochondrial transmembrane depolarization
    • Bossywetzel E., Newmeyer D. D., Green D. R. Mitochondrial cytochrome C release in apoptosis occurs upstream of DEVD-specific caspase activation and independently of mitochondrial transmembrane depolarization. EMBO J. 17:1998;37-49.
    • (1998) EMBO J , vol.17 , pp. 37-49
    • Bossywetzel, E.1    Newmeyer, D.D.2    Green, D.R.3
  • 53
    • 0032496401 scopus 로고    scopus 로고
    • Caspases disrupt mitochondrial membrane barrier function
    • Marzo I., Susin S. A., Petit P. X. Caspases disrupt mitochondrial membrane barrier function. FEBS Letters. 427:1998;198-202.
    • (1998) FEBS Letters , vol.427 , pp. 198-202
    • Marzo, I.1    Susin, S.A.2    Petit, P.X.3
  • 54
    • 0031020227 scopus 로고    scopus 로고
    • Interaction and regulation of subcellular localization of Ced-4 by Ced-9
    • Wu D. Y., Wallen H. D., Nunez G. Interaction and regulation of subcellular localization of Ced-4 by Ced-9. Science. 275:1997;1126-1129.
    • (1997) Science , vol.275 , pp. 1126-1129
    • Wu, D.Y.1    Wallen, H.D.2    Nunez, G.3
  • 56
    • 0032575714 scopus 로고    scopus 로고
    • Death receptors - Signaling and modulation
    • Ashkenazi A., Dixit V. M. Death receptors - signaling and modulation. Science. 281:1998;1305-1308.
    • (1998) Science , vol.281 , pp. 1305-1308
    • Ashkenazi, A.1    Dixit, V.M.2
  • 57
    • 0032563275 scopus 로고    scopus 로고
    • Identification and functional characterization of Dr6, a novel death domain-containing TNF receptor
    • Pan G. H., Bauer J. H., Haridas V. Identification and functional characterization of Dr6, a novel death domain-containing TNF receptor. FEBS Letters. 431:1998;351-356.
    • (1998) FEBS Letters , vol.431 , pp. 351-356
    • Pan, G.H.1    Bauer, J.H.2    Haridas, V.3
  • 59
    • 15144345497 scopus 로고    scopus 로고
    • Pro-caspase-3 is a major physiologic target of caspase-8
    • Stennicke H. R., Jurgensmeier J. M., Shin H. Pro-caspase-3 is a major physiologic target of caspase-8. J Biol Chem. 273:1998;27084-27090.
    • (1998) J Biol Chem , vol.273 , pp. 27084-27090
    • Stennicke, H.R.1    Jurgensmeier, J.M.2    Shin, H.3
  • 60
    • 0029609086 scopus 로고
    • Bcl-2 and Fas/Apo-1 regulate distinct pathways to lymphocyte apoptosis
    • Strasser A., Harris A. W., Huang D. C. S., Krammer P. H., Cory S. Bcl-2 and Fas/Apo-1 regulate distinct pathways to lymphocyte apoptosis. EMBO J. 14:1995;6136-6147.
    • (1995) EMBO J , vol.14 , pp. 6136-6147
    • Strasser, A.1    Harris, A.W.2    Huang, D.C.S.3    Krammer, P.H.4    Cory, S.5
  • 61
    • 0032548502 scopus 로고    scopus 로고
    • Bcl-X(L) functions downstream of caspase-8 to inhibit Fas- and tumor necrosis factor receptor 1-induced apoptosis of MCF-7 breast carcinoma cells
    • Srinivasan A., Li F., Wong A. Bcl-X(L) functions downstream of caspase-8 to inhibit Fas- and tumor necrosis factor receptor 1-induced apoptosis of MCF-7 breast carcinoma cells. J Biol Chem. 273:1998;4523-4529.
    • (1998) J Biol Chem , vol.273 , pp. 4523-4529
    • Srinivasan, A.1    Li, F.2    Wong, A.3
  • 62
    • 0030994024 scopus 로고    scopus 로고
    • Bcl-X(L) can inhibit apoptosis in cells that have undergone Fas-induced protease activation
    • Boise L. H., Thompson C. B. Bcl-X(L) can inhibit apoptosis in cells that have undergone Fas-induced protease activation. Proc Nat Acad Sci (USA). 94:1997;3759-3764.
    • (1997) Proc Nat Acad Sci (USA) , vol.94 , pp. 3759-3764
    • Boise, L.H.1    Thompson, C.B.2
  • 63
    • 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 S. A., Zamzami N., Castedo M. The central executioner of apoptosis - multiple connections between protease activation and mitochondria in Fas/Apo-1/CD95- and ceramide-induced apoptosis. J Exp Med. 186:1997;25-37.
    • (1997) J Exp Med , vol.186 , pp. 25-37
    • Susin, S.A.1    Zamzami, N.2    Castedo, M.3
  • 64
    • 0032568954 scopus 로고    scopus 로고
    • Apoptosis induction by caspase-8 is amplified through the mitochondrial release of cytochrome c
    • Kuwana T., Smith J. J., Muzio M., Dixit V. M., Newmeyer D. D., Kornbluth S. Apoptosis induction by caspase-8 is amplified through the mitochondrial release of cytochrome c. J Biol Chem. 273:1998;16589-16594.
    • (1998) J Biol Chem , vol.273 , pp. 16589-16594
    • Kuwana, T.1    Smith, J.J.2    Muzio, M.3    Dixit, V.M.4    Newmeyer, D.D.5    Kornbluth, S.6
  • 65
    • 0032536771 scopus 로고    scopus 로고
    • Two CD95 (Apo-1/Fas) signaling pathways
    • Scaffidi C., Fulda S., Srinivasan A. Two CD95 (Apo-1/Fas) signaling pathways. EMBO J. 17:1998;1675-1687.
    • (1998) EMBO J , vol.17 , pp. 1675-1687
    • Scaffidi, C.1    Fulda, S.2    Srinivasan, A.3
  • 66
    • 0032555697 scopus 로고    scopus 로고
    • Cleavage of BID by caspase 8 mediates the mitochondrial damage in the Fas pathway of apoptosis
    • Li H. L., Zhu H., Xu C. J., Yuan J. Y. Cleavage of BID by caspase 8 mediates the mitochondrial damage in the Fas pathway of apoptosis. Cell. 94:1998;491-501.
    • (1998) Cell , vol.94 , pp. 491-501
    • Li, H.L.1    Zhu, H.2    Xu, C.J.3    Yuan, J.Y.4
  • 67
    • 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. D. Bid, a Bcl2 interacting protein, mediates cytochrome c release from mitochondria in response to activation of cell surface death receptors. Cell. 94:1998;481-490.
    • (1998) Cell , vol.94 , pp. 481-490
    • Luo, X.1    Budihardjo, I.2    Zou, H.3    Slaughter, C.4    Wang, X.D.5
  • 68
    • 0029820016 scopus 로고    scopus 로고
    • Activation of the CPP32 protease in apoptosis induced by 1-beta-D-arabinofuranosylcytosine and other DNA-damaging agents
    • Datta R., Banach D., Kojima H. Activation of the CPP32 protease in apoptosis induced by 1-beta-D-arabinofuranosylcytosine and other DNA-damaging agents. Blood. 88:1996;1936-1943.
    • (1996) Blood , vol.88 , pp. 1936-1943
    • Datta, R.1    Banach, D.2    Kojima, H.3
  • 69
    • 0029853389 scopus 로고    scopus 로고
    • Pivotal role of a DEVD-sensitive step in etoposide-induced and Fas-mediated apoptotic pathways
    • Dubrez L., Savoy I., Hamman A., Solary E. Pivotal role of a DEVD-sensitive step in etoposide-induced and Fas-mediated apoptotic pathways. EMBO J. 15:1996;5504-5512.
    • (1996) EMBO J , vol.15 , pp. 5504-5512
    • Dubrez, L.1    Savoy, I.2    Hamman, A.3    Solary, E.4
  • 70
    • 0030890790 scopus 로고    scopus 로고
    • Processing/Activation of at least four interleukin-1-beta converting enzyme-like proteases occurs during the execution phase of apoptosis in human monocytic tumor cells
    • Macfarlane M., Cain K., Sun X. M., Alnemri E. S., Cohen G. M. Processing/Activation of at least four interleukin-1-beta converting enzyme-like proteases occurs during the execution phase of apoptosis in human monocytic tumor cells. J Cell Biol. 137:1997;469-479.
    • (1997) J Cell Biol , vol.137 , pp. 469-479
    • Macfarlane, M.1    Cain, K.2    Sun, X.M.3    Alnemri, E.S.4    Cohen, G.M.5
  • 71
    • 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. 16:1997;2271-2281.
    • (1997) EMBO J , vol.16 , pp. 2271-2281
    • Faleiro, L.1    Kobayashi, R.2    Fearnhead, H.3    Lazebnik, Y.4
  • 72
    • 15444344933 scopus 로고    scopus 로고
    • Activation of multiple interleukin-1-beta converting enzyme homologues in cytosol and nuclei of HL-60 cells during etoposide-induced apoptosis
    • Martins L. M., Kottke T., Mesner P. W. Activation of multiple interleukin-1-beta converting enzyme homologues in cytosol and nuclei of HL-60 cells during etoposide-induced apoptosis. J Biol Chem. 272:1997;7421-7430.
    • (1997) J Biol Chem , vol.272 , pp. 7421-7430
    • Martins, L.M.1    Kottke, T.2    Mesner, P.W.3
  • 73
    • 0032482441 scopus 로고    scopus 로고
    • Upregulation of casp genes in human tumor cells undergoing etoposide-induced apoptosis
    • Droin N., Dubrez L., Eymin B. Upregulation of casp genes in human tumor cells undergoing etoposide-induced apoptosis. Oncogene. 16:1998;2885-2894.
    • (1998) Oncogene , vol.16 , pp. 2885-2894
    • Droin, N.1    Dubrez, L.2    Eymin, B.3
  • 74
    • 0032189535 scopus 로고    scopus 로고
    • Molecular ordering of apoptosis induced by anticancer drugs in neuroblastoma cells
    • Fulda S., Susin S. A., Kroemer G., Debatin K. M. Molecular ordering of apoptosis induced by anticancer drugs in neuroblastoma cells. Cancer Res. 58:1998;4453-4460.
    • (1998) Cancer Res , vol.58 , pp. 4453-4460
    • Fulda, S.1    Susin, S.A.2    Kroemer, G.3    Debatin, K.M.4
  • 75
    • 0032532653 scopus 로고    scopus 로고
    • Overexpression of Apaf-1 promotes apoptosis of untreated and paclitaxel- or etoposide-treated HL-60 cells
    • Perkins C., Kim C. N., Fang G. F., Bhalla K. N. Overexpression of Apaf-1 promotes apoptosis of untreated and paclitaxel- or etoposide-treated HL-60 cells. Cancer Res. 58:1998;4561-4566.
    • (1998) Cancer Res , vol.58 , pp. 4561-4566
    • Perkins, C.1    Kim, C.N.2    Fang, G.F.3    Bhalla, K.N.4
  • 76
    • 0030752603 scopus 로고    scopus 로고
    • The CD95 (Apo-1/Fas) system mediates drug-induced apoptosis in neuroblastoma cells
    • Fulda S., Sieverts H., Friesen C., Herr I., Debatin K. M. The CD95 (Apo-1/Fas) system mediates drug-induced apoptosis in neuroblastoma cells. Cancer Res. 57:1997;3823-3829.
    • (1997) Cancer Res , vol.57 , pp. 3823-3829
    • Fulda, S.1    Sieverts, H.2    Friesen, C.3    Herr, I.4    Debatin, K.M.5
  • 77
    • 0040419494 scopus 로고    scopus 로고
    • Drug-induced apoptosis in hepatoma cells is mediated by the CD95 (Apo-1/Fas) receptor/ligand system and involves activation of wild-type p53
    • Muller M., Strand S., Hug H. Drug-induced apoptosis in hepatoma cells is mediated by the CD95 (Apo-1/Fas) receptor/ligand system and involves activation of wild-type p53. J Clin Invest. 99:1997;403-413.
    • (1997) J Clin Invest , vol.99 , pp. 403-413
    • Muller, M.1    Strand, S.2    Hug, H.3
  • 78
    • 0030670626 scopus 로고    scopus 로고
    • Activation of CD95 (Apo-1/Fas) signaling by ceramide mediates cancer therapy-induced apoptosis
    • Herr I., Wilhelm D., Bohler T., Angel P., Debatin K. M. Activation of CD95 (Apo-1/Fas) signaling by ceramide mediates cancer therapy-induced apoptosis. EMBO J. 16:1997;6200-6208.
    • (1997) EMBO J , vol.16 , pp. 6200-6208
    • Herr, I.1    Wilhelm, D.2    Bohler, T.3    Angel, P.4    Debatin, K.M.5
  • 79
    • 0030806351 scopus 로고    scopus 로고
    • Comparison of apoptosis in wild-type and Fas-resistant cells - Chemotherapy-induced apoptosis is not dependent on Fas/Fas ligand interactions
    • Eischen C. M., Kottke T. J., Martins L. M. Comparison of apoptosis in wild-type and Fas-resistant cells - chemotherapy-induced apoptosis is not dependent on Fas/Fas ligand interactions. Blood. 90:1997;935-943.
    • (1997) Blood , vol.90 , pp. 935-943
    • Eischen, C.M.1    Kottke, T.J.2    Martins, L.M.3
  • 80
    • 0030744833 scopus 로고    scopus 로고
    • Drug-induced apoptosis is associated with enhanced Fas (Apo-1/CD95) ligand expression but occurs independently of Fas (Apo-1/CD95) signaling in human T-acute lymphatic leukemia cells
    • Villunger A., Egle A., Kos M. Drug-induced apoptosis is associated with enhanced Fas (Apo-1/CD95) ligand expression but occurs independently of Fas (Apo-1/CD95) signaling in human T-acute lymphatic leukemia cells. Cancer Res. 57:1997;3331-3334.
    • (1997) Cancer Res , vol.57 , pp. 3331-3334
    • Villunger, A.1    Egle, A.2    Kos, M.3
  • 81
    • 7144263731 scopus 로고    scopus 로고
    • Fadd - Essential for embryo development and signaling from some, but not all, inducers of apoptosis
    • Yeh W. C., Delapomp J. L., McCurrach M. E. Fadd - essential for embryo development and signaling from some, but not all, inducers of apoptosis. Science. 279:1998;1954-1958.
    • (1998) Science , vol.279 , pp. 1954-1958
    • Yeh, W.C.1    Delapomp, J.L.2    McCurrach, M.E.3
  • 82
    • 0029834497 scopus 로고    scopus 로고
    • CrmA expression in T lymphocytes of transgenic mice inhibits CD95 (Fas/Apo-1)-transduced apoptosis, but does not cause lymphadenopathy or autoimmune disease
    • Smith K. G. C., Strasser A., Vaux D. L. CrmA expression in T lymphocytes of transgenic mice inhibits CD95 (Fas/Apo-1)-transduced apoptosis, but does not cause lymphadenopathy or autoimmune disease. EMBO J. 15:1996;5167-5176.
    • (1996) EMBO J , vol.15 , pp. 5167-5176
    • Smith, K.G.C.1    Strasser, A.2    Vaux, D.L.3
  • 83
    • 0031301839 scopus 로고    scopus 로고
    • The CrmA- and TPCK-sensitive pathways that trigger oligonucleosome-sized DNA fragmentation in camptothecin-induced apoptosis - Relation to caspase activation and high molecular weight DNA fragmentation
    • Sané A. T., Schmitt E., Steyaert A., Meyer D., Bertrand R. The CrmA- and TPCK-sensitive pathways that trigger oligonucleosome-sized DNA fragmentation in camptothecin-induced apoptosis - relation to caspase activation and high molecular weight DNA fragmentation. Biochem Cell Biol. 75:1997;359-358.
    • (1997) Biochem Cell Biol , vol.75 , pp. 359-358
    • Sané, A.T.1    Schmitt, E.2    Steyaert, A.3    Meyer, D.4    Bertrand, R.5
  • 84
    • 0028579733 scopus 로고
    • Oncogenes and the strategy of growth factors
    • Baserga R. Oncogenes and the strategy of growth factors. Cell. 79:1994;927-930.
    • (1994) Cell , vol.79 , pp. 927-930
    • Baserga, R.1


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