메뉴 건너뛰기




Volumn 26, Issue 4, 2005, Pages 713-723

Human colon cancer cells lacking Bax resist curcumin-induced apoptosis and Bax requirement is dispensable with ectopic expression of Smac or downregulation of Bcl-XL

Author keywords

[No Author keywords available]

Indexed keywords

APOPTOSIS INDUCING FACTOR; CASPASE 3; CASPASE 8; CASPASE 9; COMPLEMENTARY DNA; CURCUMIN; CYTOCHROME C; PROTEIN BAX; PROTEIN BCL XL; SECOND MITOCHONDRIAL ACTIVATOR OF CASPASE; ANTINEOPLASTIC AGENT; ANTISENSE OLIGONUCLEOTIDE; BAX PROTEIN, HUMAN; BCL2L1 PROTEIN, HUMAN; CASPASE; COMPLEMENT; FLAVOPROTEIN; GLYCOPROTEIN; MEMBRANE PROTEIN; PDCD8 PROTEIN, HUMAN; PROTEIN BCL 2; PROTEIN BCL X; SC5B 9 PROTEIN COMPLEX; SC5B-9 PROTEIN COMPLEX;

EID: 17844392101     PISSN: 01433334     EISSN: None     Source Type: Journal    
DOI: 10.1093/carcin/bgi025     Document Type: Article
Times cited : (88)

References (51)
  • 2
    • 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., Jemmerson, R. and Wang, X. (1996) Induction of apoptotic program in cell-free extracts: requirement for dATP and cytochrome c. Cell, 86, 147-157.
    • (1996) Cell , vol.86 , pp. 147-157
    • Liu, X.1    Kim, C.N.2    Yang, J.3    Jemmerson, R.4    Wang, X.5
  • 3
    • 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., Srinivasula, S.M., Ahmad, M., Alnemri, E.S. and Wang, X. (1997) Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade. Cell, 91, 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
  • 4
    • 0033596980 scopus 로고    scopus 로고
    • An APAF-1 · cytochrome c multimeric complex is a functional apoptosome that activates procaspase-9
    • Zou, H., Li, Y., Liu, X. and Wang, X. (1999) An APAF-1 · cytochrome c multimeric complex is a functional apoptosome that activates procaspase-9. J. Biol. Chem., 274, 11549-11556.
    • (1999) J. Biol. Chem. , vol.274 , pp. 11549-11556
    • Zou, H.1    Li, Y.2    Liu, X.3    Wang, X.4
  • 5
    • 0032785181 scopus 로고    scopus 로고
    • Serial killers: Ordering caspase activation events in apoptosis
    • Slee, E.A., Adrain, C. and Martin, S.J. (1999) Serial killers: ordering caspase activation events in apoptosis. Cell Death Differ., 6, 1067-1074.
    • (1999) Cell Death Differ. , vol.6 , pp. 1067-1074
    • Slee, E.A.1    Adrain, C.2    Martin, S.J.3
  • 6
    • 0034616945 scopus 로고    scopus 로고
    • Smac, a mitochondrial protein that promotes cytochrome c-dependent caspase activation by eliminating IAP inhibition
    • Du, C., Fang, M., Li, Y., Li, L. and Wang, X. (2000) Smac, a mitochondrial protein that promotes cytochrome c-dependent caspase activation by eliminating IAP inhibition. Cell, 102, 33-42.
    • (2000) Cell , vol.102 , pp. 33-42
    • Du, C.1    Fang, M.2    Li, Y.3    Li, L.4    Wang, X.5
  • 8
    • 0034785591 scopus 로고    scopus 로고
    • A serine protease, HtrA2, is released from the mitochondria and interacts with XIAP, inducing cell death
    • Suzuki, Y., Imai, Y., Nakayama, H., Takahashi, K., Takio, K. and Takahashi, R. (2001) A serine protease, HtrA2, is released from the mitochondria and interacts with XIAP, inducing cell death. Mol. Cell, 8, 613-621.
    • (2001) Mol. Cell , vol.8 , pp. 613-621
    • Suzuki, Y.1    Imai, Y.2    Nakayama, H.3    Takahashi, K.4    Takio, K.5    Takahashi, R.6
  • 13
    • 0035811496 scopus 로고    scopus 로고
    • Endonuclease G is an apoptotic DNase when released from mitochondria
    • Li, L.Y., Luo, X. and Wang, X. (2001) Endonuclease G is an apoptotic DNase when released from mitochondria. Nature, 412, 95-99.
    • (2001) Nature , vol.412 , pp. 95-99
    • Li, L.Y.1    Luo, X.2    Wang, X.3
  • 14
    • 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, C.J. and Yuan, J. (1998) Cleavage of BID by caspase 8 mediates the mitochondrial damage in the Fas pathway of apoptosis. Cell, 94, 491-501.
    • (1998) Cell , vol.94 , pp. 491-501
    • Li, H.1    Zhu, H.2    Xu, C.J.3    Yuan, J.4
  • 15
    • 0034523818 scopus 로고    scopus 로고
    • Pro-apoptotic cascade activates BID, which oligomerizes BAK or BAX into pores that result in the release of cytochrome c
    • Korsmeyer, S.J., Wei, M.C., Saito, M., Weiler, S., Oh, K.J. and Schlesinger, P.H. (2000) Pro-apoptotic cascade activates BID, which oligomerizes BAK or BAX into pores that result in the release of cytochrome c. Cell Death Differ., 7, 1166-1173.
    • (2000) Cell Death Differ. , vol.7 , pp. 1166-1173
    • Korsmeyer, S.J.1    Wei, M.C.2    Saito, M.3    Weiler, S.4    Oh, K.J.5    Schlesinger, P.H.6
  • 16
    • 0031918223 scopus 로고    scopus 로고
    • BCL-2 family: Regulators of cell death
    • Chao, D.T. and Korsmeyer, S.J. (1998) BCL-2 family: regulators of cell death. Annu. Rev. Immunol., 16, 395-419.
    • (1998) Annu. Rev. Immunol. , vol.16 , pp. 395-419
    • Chao, D.T.1    Korsmeyer, S.J.2
  • 17
    • 0035844867 scopus 로고    scopus 로고
    • Bax and Bak coalesce into novel mitochondria-associated clusters during apoptosis
    • Nechushtan, A., Smith, C.L., Lamensdorf, I., Yoon, S.H. and Youle, R.J. (2001) Bax and Bak coalesce into novel mitochondria-associated clusters during apoptosis. J. Cell Biol., 153, 1265-1276.
    • (2001) J. Cell Biol. , vol.153 , pp. 1265-1276
    • Nechushtan, A.1    Smith, C.L.2    Lamensdorf, I.3    Yoon, S.H.4    Youle, R.J.5
  • 18
    • 0037096737 scopus 로고    scopus 로고
    • Critical requirement of BAX for manifestation of apoptosis induced by multiple stimuli in human epithelial cancer cells
    • Theodorakis, P., Lomonosova, E. and Chinnadurai, G. (2002) Critical requirement of BAX for manifestation of apoptosis induced by multiple stimuli in human epithelial cancer cells. Cancer Res., 62, 3373-3376.
    • (2002) Cancer Res. , vol.62 , pp. 3373-3376
    • Theodorakis, P.1    Lomonosova, E.2    Chinnadurai, G.3
  • 19
    • 0033535347 scopus 로고    scopus 로고
    • Cell damage-induced conformational changes of the pro-apoptotic protein Bak in vivo precede the onset of apoptosis
    • Griffiths, G.J., Dubrez, L., Morgan, C.P., Jones, N.A., Whitehouse, J., Corfe, B.M., Dive, C. and Hickman, J.A. (1999) Cell damage-induced conformational changes of the pro-apoptotic protein Bak in vivo precede the onset of apoptosis. J. Cell Biol., 144, 903-914.
    • (1999) J. Cell Biol. , vol.144 , pp. 903-914
    • Griffiths, G.J.1    Dubrez, L.2    Morgan, C.P.3    Jones, N.A.4    Whitehouse, J.5    Corfe, B.M.6    Dive, C.7    Hickman, J.A.8
  • 20
    • 0037379739 scopus 로고    scopus 로고
    • Involvement of proapoptotic molecules Bax and Bak in tumor necrosis factor-related apoptosis-inducing ligand (TRAIL)-induced mitochondrial disruption and apoptosis: Differential regulation of cytochrome c and Smac/DIABLO release
    • Kandasamy, K., Srinivasula, S.M., Alnemri, E.S., Thompson, C.B., Korsmeyer, S.J., Bryant, J.L. and Srivastava, R.K. (2003) Involvement of proapoptotic molecules Bax and Bak in tumor necrosis factor-related apoptosis-inducing ligand (TRAIL)-induced mitochondrial disruption and apoptosis: differential regulation of cytochrome c and Smac/DIABLO release. Cancer Res., 63, 1712-1721.
    • (2003) Cancer Res. , vol.63 , pp. 1712-1721
    • Kandasamy, K.1    Srinivasula, S.M.2    Alnemri, E.S.3    Thompson, C.B.4    Korsmeyer, S.J.5    Bryant, J.L.6    Srivastava, R.K.7
  • 21
    • 0032562796 scopus 로고    scopus 로고
    • Bax in murine thymus is a soluble monomeric protein that displays differential detergent-induced conformations
    • Hsu, Y.T. and Youle, R.J. (1998) Bax in murine thymus is a soluble monomeric protein that displays differential detergent-induced conformations. J. Biol. Chem., 273, 10777-10783.
    • (1998) J. Biol. Chem. , vol.273 , pp. 10777-10783
    • Hsu, Y.T.1    Youle, R.J.2
  • 22
    • 0035890335 scopus 로고    scopus 로고
    • Damage-induced Bax N-terminal change, translocation to mitochondria and formation of Bax dimers/complexes occur regardless of cell fate
    • Makin, G.W., Corfe, B.M., Griffiths, G.J., Thistlethwaite, A., Hickman, J.A. and Dive, C. (2001) Damage-induced Bax N-terminal change, translocation to mitochondria and formation of Bax dimers/complexes occur regardless of cell fate. EMBO J., 20, 6306-6315.
    • (2001) EMBO J. , vol.20 , pp. 6306-6315
    • Makin, G.W.1    Corfe, B.M.2    Griffiths, G.J.3    Thistlethwaite, A.4    Hickman, J.A.5    Dive, C.6
  • 23
    • 0033713002 scopus 로고    scopus 로고
    • Structure of Bax: Coregulation of dimer formation and intracellular localization
    • Suzuki, M., Youle, R.J. and Tjandra, N. (2000) Structure of Bax: coregulation of dimer formation and intracellular localization. Cell, 103, 645-654.
    • (2000) Cell , vol.103 , pp. 645-654
    • Suzuki, M.1    Youle, R.J.2    Tjandra, N.3
  • 24
    • 0037380884 scopus 로고    scopus 로고
    • Bax plays a pivotal role in thapsigargin-induced apoptosis of human colon cancer HCT116 cells by controlling Smac/Diablo and Omi/HtrA2 release from mitochondria
    • Yamaguchi, H., Bhalla, K. and Wang, H.G. (2003) Bax plays a pivotal role in thapsigargin-induced apoptosis of human colon cancer HCT116 cells by controlling Smac/Diablo and Omi/HtrA2 release from mitochondria. Cancer Res., 63, 1483-1489.
    • (2003) Cancer Res. , vol.63 , pp. 1483-1489
    • Yamaguchi, H.1    Bhalla, K.2    Wang, H.G.3
  • 25
    • 0031018674 scopus 로고    scopus 로고
    • Somatic frameshift mutations in the BAX gene in colon cancers of the microsatellite mutator phenotype
    • Rampino, N., Yamamoto, H., Ionov, Y., Li, Y., Sawai, H., Reed, J.C. and Perucho, M. (1997) Somatic frameshift mutations in the BAX gene in colon cancers of the microsatellite mutator phenotype. Science, 275, 967-969.
    • (1997) Science , vol.275 , pp. 967-969
    • Rampino, N.1    Yamamoto, H.2    Ionov, Y.3    Li, Y.4    Sawai, H.5    Reed, J.C.6    Perucho, M.7
  • 26
    • 0034602188 scopus 로고    scopus 로고
    • Role of BAX in the apoptotic response to anticancer agents
    • Zhang, L., Yu, J., Park, B.H., Kinzler, K.W. and Vogelstein, B. (2000) Role of BAX in the apoptotic response to anticancer agents. Science, 290, 989-992.
    • (2000) Science , vol.290 , pp. 989-992
    • Zhang, L.1    Yu, J.2    Park, B.H.3    Kinzler, K.W.4    Vogelstein, B.5
  • 27
    • 0030589131 scopus 로고    scopus 로고
    • Curcumin, an antioxidant and anti-tumor promoter, induces apoptosis in human leukemia cells
    • Kuo, M.L., Huang, T.S. and Lin, J.K. (1996) Curcumin, an antioxidant and anti-tumor promoter, induces apoptosis in human leukemia cells. Biochim. Biophys. Acta, 1317, 95-100.
    • (1996) Biochim. Biophys. Acta , vol.1317 , pp. 95-100
    • Kuo, M.L.1    Huang, T.S.2    Lin, J.K.3
  • 28
    • 0033563646 scopus 로고    scopus 로고
    • A novel apoptosis-like pathway, independent of mitochondria and caspases, induced by curcumin in human lymphoblastoid T (Jurkat) cells
    • Piwocka, K., Zablocki, K., Wieckowski, M.R., Skierski, J., Feiga, I., Szopa, J., Drela, N., Wojtczak, L. and Sikora, E. (1999) A novel apoptosis-like pathway, independent of mitochondria and caspases, induced by curcumin in human lymphoblastoid T (Jurkat) cells. Exp. Cell Res., 249, 299-307.
    • (1999) Exp. Cell Res. , vol.249 , pp. 299-307
    • Piwocka, K.1    Zablocki, K.2    Wieckowski, M.R.3    Skierski, J.4    Feiga, I.5    Szopa, J.6    Drela, N.7    Wojtczak, L.8    Sikora, E.9
  • 29
    • 0032763091 scopus 로고    scopus 로고
    • Curcumin inhibits cell proliferation by interfering with the cell cycle and inducing apoptosis in colon carcinoma cells
    • Chen, H., Zhang, Z.S., Zhang, Y.L. and Zhou, D.Y. (1999) Curcumin inhibits cell proliferation by interfering with the cell cycle and inducing apoptosis in colon carcinoma cells. Anticancer Res., 19, 3675-3680.
    • (1999) Anticancer Res. , vol.19 , pp. 3675-3680
    • Chen, H.1    Zhang, Z.S.2    Zhang, Y.L.3    Zhou, D.Y.4
  • 30
    • 0037434845 scopus 로고    scopus 로고
    • Human colon cancer cells differ in their sensitivity to curcumin-induced apoptosis and heat shock protects them by inhibiting the release of apoptosis-inducing factor and caspases
    • Rashmi, R., Santhosh Kumar, T.R. and Karunagaran, D. (2003) Human colon cancer cells differ in their sensitivity to curcumin-induced apoptosis and heat shock protects them by inhibiting the release of apoptosis-inducing factor and caspases. FEBS Lett., 538, 19-24.
    • (2003) FEBS Lett. , vol.538 , pp. 19-24
    • Rashmi, R.1    Santhosh Kumar, T.R.2    Karunagaran, D.3
  • 31
    • 1242307957 scopus 로고    scopus 로고
    • Ectopic expression of Hsp70 confers resistance and silencing its expression sensitizes human colon cancer cells to curcumin-induced apoptosis
    • Rashmi, R., Kumar, S. and Karunagaran, D. (2004) Ectopic expression of Hsp70 confers resistance and silencing its expression sensitizes human colon cancer cells to curcumin-induced apoptosis. Carcinogenesis, 25, 179-187.
    • (2004) Carcinogenesis , vol.25 , pp. 179-187
    • Rashmi, R.1    Kumar, S.2    Karunagaran, D.3
  • 33
    • 0028990125 scopus 로고
    • Yama/CPP32 beta, a mammalian homolog of CED-3, is a CrmA-inhibitable protease that cleaves the death substrate poly(ADP-ribose) polymerase
    • Tewari, M., Quan, L.T., O'Rourke, K., Desnoyers, S., Zeng, Z., Beidler, D.R., Poirier, G.G., Salvesen, G.S. and Dixit, V.M. (1995) Yama/CPP32 beta, a mammalian homolog of CED-3, is a CrmA-inhibitable protease that cleaves the death substrate poly(ADP-ribose) polymerase. Cell, 81, 801-809.
    • (1995) Cell , vol.81 , pp. 801-809
    • Tewari, M.1    Quan, L.T.2    O'Rourke, K.3    Desnoyers, S.4    Zeng, Z.5    Beidler, D.R.6    Poirier, G.G.7    Salvesen, G.S.8    Dixit, V.M.9
  • 34
    • 0036195104 scopus 로고    scopus 로고
    • Curcumin (diferuloylmethane) induces apoptosis through activation of caspase-8, BID cleavage and cytochrome c release: Its suppression by ectopic expression of Bcl-2 and Bcl-x1
    • Anto, R.J., Mukhopadhyay, A., Denning, K. and Aggarwal, B.B. (2002) Curcumin (diferuloylmethane) induces apoptosis through activation of caspase-8, BID cleavage and cytochrome c release: its suppression by ectopic expression of Bcl-2 and Bcl-x1. Carcinogenesis, 23, 143-150.
    • (2002) Carcinogenesis , vol.23 , pp. 143-150
    • Anto, R.J.1    Mukhopadhyay, A.2    Denning, K.3    Aggarwal, B.B.4
  • 35
    • 0034718591 scopus 로고    scopus 로고
    • Mutational inactivation of the proapoptotic gene BAX confers selective advantage during tumor clonal evolution
    • Ionov, Y., Yamamoto, H., Krajewski, S., Reed, J.C. and Perucho, M. (2000) Mutational inactivation of the proapoptotic gene BAX confers selective advantage during tumor clonal evolution. Proc. Natl. Acad. Sci. USA, 97, 10872-10877.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 10872-10877
    • Ionov, Y.1    Yamamoto, H.2    Krajewski, S.3    Reed, J.C.4    Perucho, M.5
  • 37
    • 0029903534 scopus 로고    scopus 로고
    • Cancer of the microsatellite mutator phenotype
    • Perucho, M. (1996) Cancer of the microsatellite mutator phenotype. Biol. Chem., 377, 675-684.
    • (1996) Biol. Chem. , vol.377 , pp. 675-684
    • Perucho, M.1
  • 39
    • 4043095823 scopus 로고    scopus 로고
    • Differential apoptotic response to the proteasome inhibitor bortezomib [VELCADE(TM), PS-341] in Bax-deficient and p21-deficient colon cancer cells
    • Yu, J., Tiwari, S., Steiner, P. and Zhang, L. (2003) Differential apoptotic response to the proteasome inhibitor bortezomib [VELCADE(TM), PS-341] in Bax-deficient and p21-deficient colon cancer cells. Cancer Biol. Ther., 2, 694-699.
    • (2003) Cancer Biol. Ther. , vol.2 , pp. 694-699
    • Yu, J.1    Tiwari, S.2    Steiner, P.3    Zhang, L.4
  • 43
    • 0036565885 scopus 로고    scopus 로고
    • Ectopic overexpression of second mitochondria-derived activator of caspases (Smac/DIABLO) or cotreatment with N-terminus of Smac/ DIABLO peptide potentiates epothilone B derivative-(BMS 247550) and Apo-2L/TRAIL-induced apoptosis
    • Guo, F., Nimmanapalli, R., Paranawithana, S., Wittman, S., Griffin, D., Bali, P., O'Bryan, E., Fumero, C., Wang, H.G. and Bhalla, K. (2002) Ectopic overexpression of second mitochondria-derived activator of caspases (Smac/DIABLO) or cotreatment with N-terminus of Smac/ DIABLO peptide potentiates epothilone B derivative-(BMS 247550) and Apo-2L/TRAIL-induced apoptosis. Blood, 99, 3419-3426.
    • (2002) Blood , vol.99 , pp. 3419-3426
    • Guo, F.1    Nimmanapalli, R.2    Paranawithana, S.3    Wittman, S.4    Griffin, D.5    Bali, P.6    O'Bryan, E.7    Fumero, C.8    Wang, H.G.9    Bhalla, K.10
  • 44
    • 0036341291 scopus 로고    scopus 로고
    • Smac agonists sensitize for Apo2L/TRAIL- Or anticancer drug-induced apoptosis and induce regression of malignant glioma in vivo
    • Fulda, S., Wick, W., Weller, M. and Debatin, K.M. (2002) Smac agonists sensitize for Apo2L/TRAIL- or anticancer drug-induced apoptosis and induce regression of malignant glioma in vivo. Nature Med., 8, 808-815.
    • (2002) Nature Med. , vol.8 , pp. 808-815
    • Fulda, S.1    Wick, W.2    Weller, M.3    Debatin, K.M.4
  • 45
    • 0038297558 scopus 로고    scopus 로고
    • Expression of Smac/DIABLO in ovarian carcinoma cells induces apoptosis via a caspase-9-mediated pathway
    • McNeish, I.A., Bell, S., McKay, T., Tenev, T., Marani, M. and Lemoine, N.R. (2003) Expression of Smac/DIABLO in ovarian carcinoma cells induces apoptosis via a caspase-9-mediated pathway. Exp. Cell Res., 286, 186-198.
    • (2003) Exp. Cell Res. , vol.286 , pp. 186-198
    • McNeish, I.A.1    Bell, S.2    McKay, T.3    Tenev, T.4    Marani, M.5    Lemoine, N.R.6
  • 47
    • 0030667245 scopus 로고    scopus 로고
    • The E1B 19K protein associates with lamins in vivo and its proper localization is required for inhibition of apoptosis
    • Rao, L., Modha, D. and White, E. (1997) The E1B 19K protein associates with lamins in vivo and its proper localization is required for inhibition of apoptosis. Oncogene, 15, 1587-1597.
    • (1997) Oncogene , vol.15 , pp. 1587-1597
    • Rao, L.1    Modha, D.2    White, E.3
  • 50
    • 0042237031 scopus 로고    scopus 로고
    • Mitochondrial release of AIF and EndoG requires caspase activation downstream of Bax/Bak-mediated permeabilization
    • Arnoult, D., Gaume, B., Karbowski, M., Sharpe, J.C., Cecconi, F. and Youle, R.J. (2003) Mitochondrial release of AIF and EndoG requires caspase activation downstream of Bax/Bak-mediated permeabilization. EMBO J., 22, 4385-4399.
    • (2003) EMBO J. , vol.22 , pp. 4385-4399
    • Arnoult, D.1    Gaume, B.2    Karbowski, M.3    Sharpe, J.C.4    Cecconi, F.5    Youle, R.J.6
  • 51
    • 0037818277 scopus 로고    scopus 로고
    • Caspase inhibition prevents the mitochondrial release of apoptosis-inducing factor
    • Arnoult, D., Karbowski, M. and Youle, R.J. (2003) Caspase inhibition prevents the mitochondrial release of apoptosis-inducing factor. Cell Death Differ., 10, 845-849.
    • (2003) Cell Death Differ. , vol.10 , pp. 845-849
    • Arnoult, D.1    Karbowski, M.2    Youle, R.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.