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Volumn 258, Issue 1, 2000, Pages 223-235

Doxorubicin treatment activates a Z-VAD-sensitive caspase, which causes ΔΨ(m)) loss, caspase-9 activity, and apoptosis in Jurkat cells

Author keywords

Apoptosis; Caspases; Doxorubicin; Leukemia; Mitochondria

Indexed keywords

CASPASE; CASPASE 2; CASPASE 3; CASPASE 7; CASPASE 8; CASPASE 9; CASPASE INHIBITOR; CASPASE X; CYCLOHEXIMIDE; DOXORUBICIN; LAMIN B; PHOSPHATIDYLSERINE; PROTEIN BCL 2; UNCLASSIFIED DRUG;

EID: 0034631974     PISSN: 00144827     EISSN: None     Source Type: Journal    
DOI: 10.1006/excr.2000.4924     Document Type: Article
Times cited : (123)

References (70)
  • 1
    • 0033006172 scopus 로고    scopus 로고
    • A critical evaluation of the mechanisms of action proposed for the antitumor effects of the anthracycline antibiotics adriamycin and daunorubicin
    • Gewitz D. A. A critical evaluation of the mechanisms of action proposed for the antitumor effects of the anthracycline antibiotics adriamycin and daunorubicin. Biochem. Pharmacol. 57:1999;727-741.
    • (1999) Biochem. Pharmacol. , vol.57 , pp. 727-741
    • Gewitz, D.A.1
  • 2
    • 0025047803 scopus 로고
    • Activation of programmed cell death (apoptosis) by cisplatin, other anticancer drugs, toxins and hyperthermia
    • Barry M. A., Behnke C. A., Eastman A. Activation of programmed cell death (apoptosis) by cisplatin, other anticancer drugs, toxins and hyperthermia. Biochem. Pharmacol. 40:1990;2353-2362.
    • (1990) Biochem. Pharmacol. , vol.40 , pp. 2353-2362
    • Barry, M.A.1    Behnke, C.A.2    Eastman, A.3
  • 3
    • 0027237540 scopus 로고
    • Adriamycin and daunomycin induce programmed cell death (apoptosis) in tumor cells
    • Skladanowski A., Konopa J. Adriamycin and daunomycin induce programmed cell death (apoptosis) in tumor cells. Biochem. Pharmacol. 46:1993;375-382.
    • (1993) Biochem. Pharmacol. , vol.46 , pp. 375-382
    • Skladanowski, A.1    Konopa, J.2
  • 5
    • 0030999750 scopus 로고    scopus 로고
    • Apoptosis and the dilemma of cancer chemotherapy
    • Hannun Y. A. Apoptosis and the dilemma of cancer chemotherapy. Blood. 89:1997;1845-1853.
    • (1997) Blood , vol.89 , pp. 1845-1853
    • Hannun, Y.A.1
  • 6
    • 0029148660 scopus 로고
    • Ceramide synthase mediates daunorubicin-induced apoptosis: An alternative mechanism for generating death signals
    • Bose R., Verheij M., Haimovitz-Friedman A., Scotto K., Fuks Z., Kolesnick R. Ceramide synthase mediates daunorubicin-induced apoptosis: An alternative mechanism for generating death signals. Cell. 82:1995;405-414.
    • (1995) Cell , vol.82 , pp. 405-414
    • Bose, R.1    Verheij, M.2    Haimovitz-Friedman, A.3    Scotto, K.4    Fuks, Z.5    Kolesnick, R.6
  • 8
    • 0031041448 scopus 로고    scopus 로고
    • Cytokine response modifier A (CrmA) inhibits ceramide formation in response to tumour necrosis factor (TNF)-α: CrmA and Bcl-2 target distinct components in the apoptotic pathway
    • Dbaibo G. S., Perry D. K., Gamard C. J., Platt R., Poirier G. G., Obeid L. M., Hannun Y. A. Cytokine response modifier A (CrmA) inhibits ceramide formation in response to tumour necrosis factor (TNF)-α: CrmA and Bcl-2 target distinct components in the apoptotic pathway. J. Exp. Med. 185:1997;481-490.
    • (1997) J. Exp. Med. , vol.185 , pp. 481-490
    • Dbaibo, G.S.1    Perry, D.K.2    Gamard, C.J.3    Platt, R.4    Poirier, G.G.5    Obeid, L.M.6    Hannun, Y.A.7
  • 9
    • 0031817917 scopus 로고    scopus 로고
    • Caspases are the main executioniers of Fas-mediated apoptosis, irrespective of the ceramide-signaling pathway
    • Gamen S., Anel A., Piñeiro A., Naval J. Caspases are the main executioniers of Fas-mediated apoptosis, irrespective of the ceramide-signaling pathway. Cell Death Differ. 5:1998;241-249.
    • (1998) Cell Death Differ. , vol.5 , pp. 241-249
    • Gamen, S.1    Anel, A.2    Piñeiro, A.3    Naval, J.4
  • 11
    • 0029935682 scopus 로고    scopus 로고
    • Involvement of the CD95 (APO-1/Fas) receptor/ligand system in drug-induced apoptosis of leukemia cells
    • Friesen C., Herr I., Krammer P. H., Debatin K. M. Involvement of the CD95 (APO-1/Fas) receptor/ligand system in drug-induced apoptosis of leukemia cells. Nature Med. 2:1996;574-577.
    • (1996) Nature Med. , vol.2 , pp. 574-577
    • Friesen, C.1    Herr, I.2    Krammer, P.H.3    Debatin, K.M.4
  • 12
    • 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
  • 13
    • 0030781018 scopus 로고    scopus 로고
    • Doxorubicin-induced apoptosis in human T-cell leukemia is mediated by caspase-3 activation in a Fas-independent way
    • Gamen S., Anel A., Lasierra P., Alava M. A., Martinez-Lorenzo M. J., Piñeiro A., Naval J. Doxorubicin-induced apoptosis in human T-cell leukemia is mediated by caspase-3 activation in a Fas-independent way. FEBS Lett. 417:1997;360-364.
    • (1997) FEBS Lett. , vol.417 , pp. 360-364
    • Gamen, S.1    Anel, A.2    Lasierra, P.3    Alava, M.A.4    Martinez-Lorenzo, M.J.5    Piñeiro, A.6    Naval, J.7
  • 14
    • 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., Basi G. S., Tung J. S., Earnshaw W. C., Leibson P. J., Kaufmann S. H. 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    Basi, G.S.4    Tung, J.S.5    Earnshaw, W.C.6    Leibson, P.J.7    Kaufmann, S.H.8
  • 15
    • 0030744833 scopus 로고    scopus 로고
    • Drug-induced apoptosis is associated with enhanced Fas (Apo-1/CD95) ligand expression but occurs independently of Fas signaling in human T-acute lymphatic leukemia cells
    • Villunger A., Egle A., Kos M., Hartmann B. L., Geley S., Kofler R., Greil R. Drug-induced apoptosis is associated with enhanced Fas (Apo-1/CD95) ligand expression but occurs independently of Fas 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    Hartmann, B.L.4    Geley, S.5    Kofler, R.6    Greil, R.7
  • 17
    • 0001616299 scopus 로고    scopus 로고
    • P53-mediated upregulation of CD95 is not involved in genotoxic drug-induced apoptosis of human breast tumor cells
    • Ruiz-Ruiz M. C., López-Rivas A. p53-mediated upregulation of CD95 is not involved in genotoxic drug-induced apoptosis of human breast tumor cells. Cell Death Differ. 6:1999;271-280.
    • (1999) Cell Death Differ. , vol.6 , pp. 271-280
    • Ruiz-Ruiz, M.C.1    López-Rivas, A.2
  • 18
    • 0033135406 scopus 로고    scopus 로고
    • Anticancer drugs induce caspase-8/FLICE activation and apoptosis in the absence of CD95 receptor/ligand interaction
    • Wesselborg S., Engels I. H., Rossman E., Los M., Schulze-Osthoff K. Anticancer drugs induce caspase-8/FLICE activation and apoptosis in the absence of CD95 receptor/ligand interaction. Blood. 93:1999;3053-3063.
    • (1999) Blood , vol.93 , pp. 3053-3063
    • Wesselborg, S.1    Engels, I.H.2    Rossman, E.3    Los, M.4    Schulze-Osthoff, K.5
  • 20
    • 0030694424 scopus 로고    scopus 로고
    • Inhibition of caspase proteases by CrmA enhances the resistance of human leukemic cells to multiple chemotherapeutic agents
    • Antoku K., Liu Z., Johnson D. E. Inhibition of caspase proteases by CrmA enhances the resistance of human leukemic cells to multiple chemotherapeutic agents. Leukemia. 11:1997;1665-1672.
    • (1997) Leukemia , vol.11 , pp. 1665-1672
    • Antoku, K.1    Liu, Z.2    Johnson, D.E.3
  • 21
    • 0033582526 scopus 로고    scopus 로고
    • Distinct caspase cascades are initiated in receptor-mediated and chemical-induced apoptosis
    • Sun X. M., MacFarlane M., Zhuang J., Wolf B. B., Green D. R., Cohen G. M. Distinct caspase cascades are initiated in receptor-mediated and chemical-induced apoptosis. J. Biol. Chem. 274:1999;5053-5060.
    • (1999) J. Biol. Chem. , vol.274 , pp. 5053-5060
    • Sun, X.M.1    MacFarlane, M.2    Zhuang, J.3    Wolf, B.B.4    Green, D.R.5    Cohen, G.M.6
  • 22
    • 0030943468 scopus 로고    scopus 로고
    • Fas stimulation induces RB dephosphorylation and proteolysis that is blocked by inhibitors of the ICE protease family
    • Dou Q. P., An B., Antoku K., Johnson D. E. Fas stimulation induces RB dephosphorylation and proteolysis that is blocked by inhibitors of the ICE protease family. J. Cell. Biochem. 64:1997;586-594.
    • (1997) J. Cell. Biochem. , vol.64 , pp. 586-594
    • Dou, Q.P.1    An, B.2    Antoku, K.3    Johnson, D.E.4
  • 24
    • 0030018840 scopus 로고    scopus 로고
    • Role of oxidative damage and ICE-like proteases in Fas-based cytotoxicity exerted by effector T cells
    • Anel A., Gamen S., Alava M. A., Schmitt-Verhulst A. M., Piñeiro A., Naval J. Role of oxidative damage and ICE-like proteases in Fas-based cytotoxicity exerted by effector T cells. Int. Immunol. 8:1996;1173-1183.
    • (1996) Int. Immunol. , vol.8 , pp. 1173-1183
    • Anel, A.1    Gamen, S.2    Alava, M.A.3    Schmitt-Verhulst, A.M.4    Piñeiro, A.5    Naval, J.6
  • 25
    • 0028800947 scopus 로고
    • Early redistribution of plasma membrane phosphatydilserine is a general feature of apoptosis regardless of the initiating stimulus: Inhibition by overexpression of Bcl-2 and Abl
    • Martin S. J., Reutelingsperger C. P. M., McGahon A. J., Rader J. A., van Schie R. C. A. A., LaFace D. M., Green D. R. Early redistribution of plasma membrane phosphatydilserine is a general feature of apoptosis regardless of the initiating stimulus: Inhibition by overexpression of Bcl-2 and Abl. J. Exp. Med. 182:1995;1545-1556.
    • (1995) J. Exp. Med. , vol.182 , pp. 1545-1556
    • Martin, S.J.1    Reutelingsperger, C.P.M.2    McGahon, A.J.3    Rader, J.A.4    Van Schie, R.C.A.A.5    Laface, D.M.6    Green, D.R.7
  • 26
    • 0029036412 scopus 로고
    • Alterations in mitochondrial structure and function are early events of dexamethsone-induced thymocyte apoptosis
    • Petit P. X., Lecoeur H., Zorn E., Dauguet C., Mignotte B., Gougeon M. L. Alterations in mitochondrial structure and function are early events of dexamethsone-induced thymocyte apoptosis. J. Cell Biol. 130:1995;157-167.
    • (1995) J. Cell Biol. , vol.130 , pp. 157-167
    • Petit, P.X.1    Lecoeur, H.2    Zorn, E.3    Dauguet, C.4    Mignotte, B.5    Gougeon, M.L.6
  • 38
    • 0028903933 scopus 로고
    • Reduction in mitochondrial potential constitutes an early irreversible step of programmed lymphocyte death in vivo
    • Zamzami N., Marchetti P., Castedo M., Zanin C., Vayssière J. L., Petit P. X., Kroemer G. Reduction in mitochondrial potential constitutes an early irreversible step of programmed lymphocyte death in vivo. J. Exp. Med. 181:1995;1661-1672.
    • (1995) J. Exp. Med. , vol.181 , pp. 1661-1672
    • Zamzami, N.1    Marchetti, P.2    Castedo, M.3    Zanin, C.4    Vayssière, J.L.5    Petit, P.X.6    Kroemer, G.7
  • 39
    • 0030942175 scopus 로고    scopus 로고
    • Phosphatidylserine externalization is a downstream event of interleukin-1β-converting enzyme family protease activation during apoptosis
    • Naito M., Nagashima K., Mashima T., Tsuruo T. Phosphatidylserine externalization is a downstream event of interleukin-1β-converting enzyme family protease activation during apoptosis. Blood. 89:1997;2060-2066.
    • (1997) Blood , vol.89 , pp. 2060-2066
    • Naito, M.1    Nagashima, K.2    Mashima, T.3    Tsuruo, T.4
  • 40
    • 0031566155 scopus 로고    scopus 로고
    • Effect of concentration on the cytotoxic mechanism of doxorubicin-apoptosis and oxidative DNA damage
    • Müller I., Jenner A., Bruchelt G., Niethammer D., Halliwell B. Effect of concentration on the cytotoxic mechanism of doxorubicin-apoptosis and oxidative DNA damage. Biochem. Biophys. Res. Commun. 230:1997;254-257.
    • (1997) Biochem. Biophys. Res. Commun. , vol.230 , pp. 254-257
    • Müller, I.1    Jenner, A.2    Bruchelt, G.3    Niethammer, D.4    Halliwell, B.5
  • 41
    • 0027303695 scopus 로고
    • Cellular pharmacokinetics of doxorubicin in patients with chronic lymphocytic leukemia: Comparison of bolus administration and continuous infusion
    • Muller C., Chatelut E., Gualano V., De Forni M., Huguet F., Attal M., Canal P., Laurent G. Cellular pharmacokinetics of doxorubicin in patients with chronic lymphocytic leukemia: Comparison of bolus administration and continuous infusion. Cancer Chemother. Pharmacol. 32:1993;379-384.
    • (1993) Cancer Chemother. Pharmacol. , vol.32 , pp. 379-384
    • Muller, C.1    Chatelut, E.2    Gualano, V.3    De Forni, M.4    Huguet, F.5    Attal, M.6    Canal, P.7    Laurent, G.8
  • 42
  • 46
    • 0029905073 scopus 로고    scopus 로고
    • Molecular ordering of the Fas-apoptotic pathway: The Fas/APO-1 protease Mch5 is a CrmA-inhibitable protease that activates multiple Ced-3/ICE-like cysteine proteases
    • Srinivasula S. M., Ahmad M., Fernandes-Alnemri T., Litwack G., Alnemri E. S. Molecular ordering of the Fas-apoptotic pathway: The Fas/APO-1 protease Mch5 is a CrmA-inhibitable protease that activates multiple Ced-3/ICE-like cysteine proteases. Proc. Natl. Acad. Sci. USA. 93:1996;14486-14491.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 14486-14491
    • Srinivasula, S.M.1    Ahmad, M.2    Fernandes-Alnemri, T.3    Litwack, G.4    Alnemri, E.S.5
  • 47
    • 0032478614 scopus 로고    scopus 로고
    • Blk, a BH3-containing mouse protein that interacts with Bcl-2 and Bcl-xL, is a potent death agonist
    • Hedge R., Srinivasula S. M., Ahmad M., Fernandes-Alnemri T., Alnemri E. S. Blk, a BH3-containing mouse protein that interacts with Bcl-2 and Bcl-xL, is a potent death agonist. J. Biol. Chem. 273:1998;7783-7786.
    • (1998) J. Biol. Chem. , vol.273 , pp. 7783-7786
    • Hedge, R.1    Srinivasula, S.M.2    Ahmad, M.3    Fernandes-Alnemri, T.4    Alnemri, E.S.5
  • 48
    • 0026576779 scopus 로고
    • Abrogation of adriamycin toxicity in vivo by cycloheximide
    • Thakkar N. S., Potten C. S. Abrogation of adriamycin toxicity in vivo by cycloheximide. Biochem. Pharmacol. 43:1992;1683-1691.
    • (1992) Biochem. Pharmacol. , vol.43 , pp. 1683-1691
    • Thakkar, N.S.1    Potten, C.S.2
  • 50
    • 11944252783 scopus 로고
    • A human temperature-sensitive p53 mutant p53Val-138: Modulation of the cell cycle, viability and expression of p53-responsive genes
    • Yamato K., Yamamoto M., Hirano Y., Tsuchida N. A human temperature-sensitive p53 mutant p53Val-138: Modulation of the cell cycle, viability and expression of p53-responsive genes. Oncogene. 11:1995;1-6.
    • (1995) Oncogene , vol.11 , pp. 1-6
    • Yamato, K.1    Yamamoto, M.2    Hirano, Y.3    Tsuchida, N.4
  • 51
    • 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., 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    Bhalla, K.N.3
  • 52
    • 0028156903 scopus 로고
    • Separate metabolic pathways leading to DNA fragmentation and apoptotic chromatin condensation
    • Sun D. Y., Jiang S., Zheng L. M., Ojcius D. M., Young J. D. E. Separate metabolic pathways leading to DNA fragmentation and apoptotic chromatin condensation. J. Exp. Med. 179:1994;559-568.
    • (1994) J. Exp. Med. , vol.179 , pp. 559-568
    • Sun, D.Y.1    Jiang, S.2    Zheng, L.M.3    Ojcius, D.M.4    Young, J.D.E.5
  • 53
    • 0030890790 scopus 로고    scopus 로고
    • Processing/activation of at least four interleukin-1β converting enzyme-like proteases occurs during the execution phase of apoptosis in human momocytic tumor cells
    • McFarlane M., Cain K., Sun X. M., Alnemri E. S., Cohen G. M. Processing/activation of at least four interleukin-1β converting enzyme-like proteases occurs during the execution phase of apoptosis in human momocytic tumor cells. J. Cell Biol. 137:1997;469-479.
    • (1997) J. Cell Biol. , vol.137 , pp. 469-479
    • McFarlane, M.1    Cain, K.2    Sun, X.M.3    Alnemri, E.S.4    Cohen, G.M.5
  • 57
    • 0031037897 scopus 로고    scopus 로고
    • The release of cytochrome c from mitochondria: A primary site for Bcl-2 regulation of apoptosis
    • Kluck R. M., Bossy-Wetzel 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    Bossy-Wetzel, E.2    Green, D.R.3    Newmeyer, D.D.4
  • 61
    • 0030715323 scopus 로고    scopus 로고
    • Cytochrome c and dATP-dependent formation of Apaf-1/Caspase-9 complex initiates apoptotic protease cascade
    • Li P., Nijhawan D., Budihardjo I., Srinivasula S. M., Ahmad M., Alnemri E. S., Wang X. Cytochrome c and dATP-dependent formation of Apaf-1/Caspase-9 complex initiates apoptotic protease cascade. Cell. 91:1997;479-489.
    • (1997) Cell , vol.91 , pp. 479-489
    • Li, P.1    Nijhawan, D.2    Budihardjo, I.3    Srinivasula, S.M.4    Ahmad, M.5    Alnemri, E.S.6    Wang, X.7
  • 65
    • 0033580901 scopus 로고    scopus 로고
    • Caspases induce cytochrome c release from mitochondria by activating cytosolic factors
    • Bossy-Wetzel E., Green D. R. Caspases induce cytochrome c release from mitochondria by activating cytosolic factors. J. Biol. Chem. 274:1999;17484-17490.
    • (1999) J. Biol. Chem. , vol.274 , pp. 17484-17490
    • Bossy-Wetzel, E.1    Green, D.R.2
  • 66
    • 0032502855 scopus 로고    scopus 로고
    • Activation of caspases triggered by cytochrome c in vitro
    • Pan G., Humke E. W., Dixit V. M. Activation of caspases triggered by cytochrome c in vitro. FEBS Lett. 426:1998;151-154.
    • (1998) FEBS Lett. , vol.426 , pp. 151-154
    • Pan, G.1    Humke, E.W.2    Dixit, V.M.3
  • 70
    • 0031033274 scopus 로고    scopus 로고
    • Inhibition of Ced-3/ICE-related proteases does not prevent cell death induced by oncogenes, DNA damage, or the Bcl-2 homologue Bak
    • McCarthy N. J., Whyte M. K. B., Gilbert C. S., Evan G. I. Inhibition of Ced-3/ICE-related proteases does not prevent cell death induced by oncogenes, DNA damage, or the Bcl-2 homologue Bak. J. Cell. Biol. 136:1997;215-227.
    • (1997) J. Cell. Biol. , vol.136 , pp. 215-227
    • McCarthy, N.J.1    Whyte, M.K.B.2    Gilbert, C.S.3    Evan, G.I.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.