메뉴 건너뛰기




Volumn 286, Issue 2, 2003, Pages 186-198

Expression of Smac/DIABLO in ovarian carcinoma cells induces apoptosis via a caspase-9-mediated pathway

Author keywords

Adenovirus; Caspase; Cisplatin; Ovarian cancer; Smac DIABLO

Indexed keywords

ADENOVIRUS VECTOR; APOPTOSIS INDUCING FACTOR; CASPASE 12; CASPASE 3; CASPASE 8; CASPASE 9; CISPLATIN; CYTOCHROME C; ENZYME; ENZYME ACTIVATOR; ENZYME ACTIVATOR SMAC; ENZYME INHIBITOR; INHIBITOR OF APOPTOSIS PROTEIN; PACLITAXEL; PROTEIN BCL 2; UNCLASSIFIED DRUG;

EID: 0038297558     PISSN: 00144827     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0014-4827(03)00073-9     Document Type: Article
Times cited : (71)

References (42)
  • 1
    • 0032877668 scopus 로고    scopus 로고
    • Dysregulation of apoptosis in cancer
    • Reed J.C. Dysregulation of apoptosis in cancer. J. Clin. Oncol. 17:1999;2941-2953.
    • (1999) J. Clin. Oncol. , vol.17 , pp. 2941-2953
    • Reed, J.C.1
  • 2
    • 0035823503 scopus 로고    scopus 로고
    • Defective cytochrome c-dependent caspase activation in ovarian cancer cell lines due to diminished or absent apoptotic protease activating factor-1 activity
    • Wolf B.B., et al. Defective cytochrome c-dependent caspase activation in ovarian cancer cell lines due to diminished or absent apoptotic protease activating factor-1 activity. J. Biol. Chem. 276:2001;34244-34251.
    • (2001) J. Biol. Chem. , vol.276 , pp. 34244-34251
    • Wolf, B.B.1
  • 3
    • 0035039678 scopus 로고    scopus 로고
    • A structural view of mitochondria-mediated apoptosis
    • Shi Y.G. A structural view of mitochondria-mediated apoptosis. Nature. Struct. Biol. 8:2001;394-401.
    • (2001) Nature. Struct. Biol. , vol.8 , pp. 394-401
    • Shi, Y.G.1
  • 4
    • 0032575750 scopus 로고    scopus 로고
    • Caspases: Enemies within
    • Thornberry N., Lazebnik Y. Caspases enemies within . Science. 281:1998;1312-1316.
    • (1998) Science. , vol.281 , pp. 1312-1316
    • Thornberry, N.1    Lazebnik, Y.2
  • 5
    • 0034610743 scopus 로고    scopus 로고
    • Caspase-12 mediates endoplasmic-reticulum-specific apoptosis and cytotoxicity by amyloid-beta
    • Nakagawa T., et al. Caspase-12 mediates endoplasmic-reticulum-specific apoptosis and cytotoxicity by amyloid-beta. Nature. 403:2000;98-103.
    • (2000) Nature , vol.403 , pp. 98-103
    • Nakagawa, T.1
  • 6
    • 0035823579 scopus 로고    scopus 로고
    • Coupling endoplasmic reticulum stress to the cell death program. Mechanism of caspase activation
    • Rao R.V., et al. Coupling endoplasmic reticulum stress to the cell death program. Mechanism of caspase activation. J. Biol. Chem. 276:2001;33869-33874.
    • (2001) J. Biol. Chem. , vol.276 , pp. 33869-33874
    • Rao, R.V.1
  • 7
    • 0034993758 scopus 로고    scopus 로고
    • Two kinds of BIR-containing protein - Inhibitors of apoptosis, or required for mitosis
    • Silke J., Vaux D. Two kinds of BIR-containing protein - inhibitors of apoptosis, or required for mitosis. J. Cell Sci. 114:2001;1821-1827.
    • (2001) J. Cell Sci. , vol.114 , pp. 1821-1827
    • Silke, J.1    Vaux, D.2
  • 8
    • 0034525374 scopus 로고    scopus 로고
    • The role of the Bcl-2 family in the regulation of outer mitochondrial membrane permeability
    • Harris M.H., Thompson C.B. The role of the Bcl-2 family in the regulation of outer mitochondrial membrane permeability. Cell Death Differ. 7:2000;1182-1191.
    • (2000) Cell Death Differ. , vol.7 , pp. 1182-1191
    • Harris, M.H.1    Thompson, C.B.2
  • 9
    • 0033519705 scopus 로고    scopus 로고
    • Bcl-2 family proteins regulate the release of apoptogenic cytochrome c by the mitochondrial channel VDAC
    • Shimizu S., et al. Bcl-2 family proteins regulate the release of apoptogenic cytochrome c by the mitochondrial channel VDAC. Nature. 399:1999;483-487.
    • (1999) Nature , vol.399 , pp. 483-487
    • Shimizu, S.1
  • 10
    • 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., et al. 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
  • 11
    • 0034616945 scopus 로고    scopus 로고
    • Smac, a mitochondrial protein that promotes cytochrome c-dependent caspase activation by eliminating IAP inhibition
    • Du C., et al. Smac, a mitochondrial protein that promotes cytochrome c-dependent caspase activation by eliminating IAP inhibition. Cell. 102:2000;33-42.
    • (2000) Cell , vol.102 , pp. 33-42
    • Du, C.1
  • 12
    • 0034616942 scopus 로고    scopus 로고
    • Identification of DIABLO, a mammalian protein that promotes apoptosis by binding to and antagonizing IAP proteins
    • Verhagen A., et al. Identification of DIABLO, a mammalian protein that promotes apoptosis by binding to and antagonizing IAP proteins. Cell. 102:2000;43-53.
    • (2000) Cell , vol.102 , pp. 43-53
    • Verhagen, A.1
  • 13
    • 0034700495 scopus 로고    scopus 로고
    • Structural basis for binding of Smac/DIABLO to the XIAP BIR3 domain
    • Liu Z.H., et al. Structural basis for binding of Smac/DIABLO to the XIAP BIR3 domain. Nature. 408:2000;1004-1008.
    • (2000) Nature , vol.408 , pp. 1004-1008
    • Liu, Z.H.1
  • 14
    • 0034710649 scopus 로고    scopus 로고
    • Structural and biochemical basis of apoptotic activation by Smac/DIABLO
    • Chai J., et al. Structural and biochemical basis of apoptotic activation by Smac/DIABLO. Nature. 406:2000;855-862.
    • (2000) Nature , vol.406 , pp. 855-862
    • Chai, J.1
  • 15
    • 0035795418 scopus 로고    scopus 로고
    • The inhibitor of apoptosis protein-binding domain of Smac is not essential for its proapoptotic activity
    • Roberts D.L., et al. The inhibitor of apoptosis protein-binding domain of Smac is not essential for its proapoptotic activity. J. Cell Biol. 153:2001;221-228.
    • (2001) J. Cell Biol. , vol.153 , pp. 221-228
    • Roberts, D.L.1
  • 16
    • 0035816553 scopus 로고    scopus 로고
    • Apaf-1/cytochrome c-independent and Smac-dependent induction of apoptosis in multiple myeloma (MM) cells
    • Chauhan D., et al. Apaf-1/cytochrome c-independent and Smac-dependent induction of apoptosis in multiple myeloma (MM) cells. J. Biol. Chem. 276:2001;24453-24456.
    • (2001) J. Biol. Chem. , vol.276 , pp. 24453-24456
    • Chauhan, D.1
  • 17
    • 0036141029 scopus 로고    scopus 로고
    • TRAIL-induced apoptosis requires Bax-dependent mitochondrial release of Smac/DIABLO
    • Deng Y., et al. TRAIL-induced apoptosis requires Bax-dependent mitochondrial release of Smac/DIABLO. Genes Dev. 16:2002;33-45.
    • (2002) Genes Dev. , vol.16 , pp. 33-45
    • Deng, Y.1
  • 18
    • 0037134495 scopus 로고    scopus 로고
    • Caspase-2 induces apoptosis by releasing proapoptotic proteins from mitochondria
    • Guo Y., et al. Caspase-2 induces apoptosis by releasing proapoptotic proteins from mitochondria. J. Biol. Chem. 277:2002;13430-13437.
    • (2002) J. Biol. Chem. , vol.277 , pp. 13430-13437
    • Guo, Y.1
  • 19
    • 0037192790 scopus 로고    scopus 로고
    • Bcl-2 and Bcl-xL inhibit CD95-mediated apoptosis by preventing mitochondrial release of Smac/DIABLO and subsequent inactivation of XIAP
    • Sun X.-M., et al. Bcl-2 and Bcl-xL inhibit CD95-mediated apoptosis by preventing mitochondrial release of Smac/DIABLO and subsequent inactivation of XIAP. J. Biol. Chem. 277:2002;11345-11351.
    • (2002) J. Biol. Chem. , vol.277 , pp. 11345-11351
    • Sun, X.-M.1
  • 20
    • 18544386724 scopus 로고    scopus 로고
    • Identification of Oml/HtrA2 as a mitochondrial apoptotic serine protease that disrupts inhibitor of apoptosis protein-caspase interaction
    • Hegde R., et al. Identification of Oml/HtrA2 as a mitochondrial apoptotic serine protease that disrupts inhibitor of apoptosis protein-caspase interaction. J. Biol. Chem. 277:2002;432-438.
    • (2002) J. Biol. Chem. , vol.277 , pp. 432-438
    • Hegde, R.1
  • 21
    • 0037016707 scopus 로고    scopus 로고
    • The serine protease Omi/HtrA2 regulates apoptosis by binding XIAP through a Reaper-like motif
    • Martins L.M., et al. The serine protease Omi/HtrA2 regulates apoptosis by binding XIAP through a Reaper-like motif. J. Biol. Chem. 277:2002;439-444.
    • (2002) J. Biol. Chem. , vol.277 , pp. 439-444
    • Martins, L.M.1
  • 22
    • 0037016686 scopus 로고    scopus 로고
    • HtrA2 promotes cell death through its serine protease activity and its ability to antagonize inhibitor of apoptosis proteins
    • Verhagen A.M., et al. HtrA2 promotes cell death through its serine protease activity and its ability to antagonize inhibitor of apoptosis proteins. J. Biol. Chem. 277:2002;445-454.
    • (2002) J. Biol. Chem. , vol.277 , pp. 445-454
    • Verhagen, A.M.1
  • 23
    • 0035803568 scopus 로고    scopus 로고
    • Apoptosis-associated release of Smac/DIABLO from mitochondria requires active caspases and is blocked by Bcl-2
    • Adrain C., et al. Apoptosis-associated release of Smac/DIABLO from mitochondria requires active caspases and is blocked by Bcl-2. EMBO J. 20:2001;6627-6636.
    • (2001) EMBO J. , vol.20 , pp. 6627-6636
    • Adrain, C.1
  • 24
    • 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., et al. 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. 99:2002;3419-3426.
    • (2002) Blood , vol.99 , pp. 3419-3426
    • Guo, F.1
  • 25
    • 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., et al. Smac agonists sensitize for Apo2L/TRAIL- or anticancer drug-induced apoptosis and induce regression of malignant glioma in vivo. Nature Med. 8:2002;808-815.
    • (2002) Nature Med. , vol.8 , pp. 808-815
    • Fulda, S.1
  • 26
    • 0035072535 scopus 로고    scopus 로고
    • Pro-caspase-3 overexpression sensitises ovarian cancer cells to proteasome inhibitors
    • Tenev T., et al. Pro-caspase-3 overexpression sensitises ovarian cancer cells to proteasome inhibitors. Cell Death Differ. 8:2001;256-264.
    • (2001) Cell Death Differ. , vol.8 , pp. 256-264
    • Tenev, T.1
  • 27
    • 0035017144 scopus 로고    scopus 로고
    • Herpes simplex virus thymidine kinase/ganciclovir-induced cell death is enhanced by co-expression of caspase-3 in ovarian carcinoma cells
    • McNeish I.A., et al. Herpes simplex virus thymidine kinase/ganciclovir-induced cell death is enhanced by co-expression of caspase-3 in ovarian carcinoma cells. Cancer Gene Ther. 8:2001;308-319.
    • (2001) Cancer Gene Ther. , vol.8 , pp. 308-319
    • McNeish, I.A.1
  • 28
    • 0027211019 scopus 로고
    • Analysis of the tissue-specific promoter of the MUC1 gene
    • Kovarik A., et al. Analysis of the tissue-specific promoter of the MUC1 gene. J. Biol. Chem. 268:1993;9917-9926.
    • (1993) J. Biol. Chem. , vol.268 , pp. 9917-9926
    • Kovarik, A.1
  • 29
    • 0032478271 scopus 로고    scopus 로고
    • A simplified system for generating recombinant adenoviruses
    • He T.-C., et al. A simplified system for generating recombinant adenoviruses. Proc. Natl. Acad. Sci. USA. 95:1998;2509-2514.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 2509-2514
    • He, T.-C.1
  • 30
    • 0021061819 scopus 로고
    • Rapid colorimetric assay for cellular growth and survival: Application to proliferation and cytotoxicity assays
    • Mosmann T. Rapid colorimetric assay for cellular growth and survival application to proliferation and cytotoxicity assays . J. Immunol. Methods. 65:1983;55-63.
    • (1983) J. Immunol. Methods , vol.65 , pp. 55-63
    • Mosmann, T.1
  • 31
    • 0034759102 scopus 로고    scopus 로고
    • Multiple kinetics of mitochondrial cytochrome c release in drug-induced apoptosis
    • Luetjens C.M., et al. Multiple kinetics of mitochondrial cytochrome c release in drug-induced apoptosis. Mol. Pharmacol. 60:2001;1008-1019.
    • (2001) Mol. Pharmacol. , vol.60 , pp. 1008-1019
    • Luetjens, C.M.1
  • 32
    • 0034664030 scopus 로고    scopus 로고
    • Negative regulation of cytochrome c-mediated oligomerization of Apaf-1 and activation of procaspase-9 by heat shock protein 90
    • Pandey P., et al. Negative regulation of cytochrome c-mediated oligomerization of Apaf-1 and activation of procaspase-9 by heat shock protein 90. EMBO J. 19:2000;4310-4322.
    • (2000) EMBO J. , vol.19 , pp. 4310-4322
    • Pandey, P.1
  • 33
    • 0035266318 scopus 로고    scopus 로고
    • XIAP regulates Akt activity and caspase-3-dependent cleavage during cisplatin-induced apoptosis in human ovarian epithelial cancer cells
    • Asselin E., et al. XIAP regulates Akt activity and caspase-3-dependent cleavage during cisplatin-induced apoptosis in human ovarian epithelial cancer cells. Cancer Res. 61:2001;1862-1868.
    • (2001) Cancer Res. , vol.61 , pp. 1862-1868
    • Asselin, E.1
  • 34
    • 0033978815 scopus 로고    scopus 로고
    • E1A-mediated paclitaxel sensitization in HER-2/neu-overexpressing ovarian cancer SKOV3.ip1 through apoptosis involving the caspase-3 pathway
    • Ueno N.T., et al. E1A-mediated paclitaxel sensitization in HER-2/neu-overexpressing ovarian cancer SKOV3.ip1 through apoptosis involving the caspase-3 pathway. Clin. Cancer Res. 6:2000;250-259.
    • (2000) Clin. Cancer Res. , vol.6 , pp. 250-259
    • Ueno, N.T.1
  • 35
    • 0034667372 scopus 로고    scopus 로고
    • Down-regulation of X-linked inhibitor of apoptosis protein induces apoptosis in chemoresistant human ovarian cancer cells
    • Sasaki H., et al. Down-regulation of X-linked inhibitor of apoptosis protein induces apoptosis in chemoresistant human ovarian cancer cells. Cancer Res. 60:2000;5659-5666.
    • (2000) Cancer Res. , vol.60 , pp. 5659-5666
    • Sasaki, H.1
  • 36
    • 0033049597 scopus 로고    scopus 로고
    • Cleavage of Bcl-2 is an early event in chemotherapy-induced apoptosis of human myeloid leukemia cells
    • Fadeel B., et al. Cleavage of Bcl-2 is an early event in chemotherapy-induced apoptosis of human myeloid leukemia cells. Leukemia. 13:1999;719-728.
    • (1999) Leukemia , vol.13 , pp. 719-728
    • Fadeel, B.1
  • 37
    • 0035476255 scopus 로고    scopus 로고
    • Tumor necrosis factor-related apoptosis-inducing ligand-induced apoptosis of human melanoma is regulated by Smac/DIABLO release from mitochondria
    • Zhang X.D., et al. Tumor necrosis factor-related apoptosis-inducing ligand-induced apoptosis of human melanoma is regulated by Smac/DIABLO release from mitochondria. Cancer Res. 61:2001;7339-7348.
    • (2001) Cancer Res. , vol.61 , pp. 7339-7348
    • Zhang, X.D.1
  • 38
    • 0035525748 scopus 로고    scopus 로고
    • Sphingosine 1-phosphate antagonizes apoptosis of human leukemia cells by inhibiting release of cytochrome c and Smac/DIABLO from mitochondria
    • Cuvillier O., Levade T. Sphingosine 1-phosphate antagonizes apoptosis of human leukemia cells by inhibiting release of cytochrome c and Smac/DIABLO from mitochondria. Blood. 98:2001;2828-2836.
    • (2001) Blood , vol.98 , pp. 2828-2836
    • Cuvillier, O.1    Levade, T.2
  • 39
    • 0035036133 scopus 로고    scopus 로고
    • Caspase-9 processing by caspase-3 via a feedback amplification loop in vivo
    • Fujita E., et al. Caspase-9 processing by caspase-3 via a feedback amplification loop in vivo. Cell Death Differ. 8:2001;335-344.
    • (2001) Cell Death Differ. , vol.8 , pp. 335-344
    • Fujita, E.1
  • 40
    • 0035163836 scopus 로고    scopus 로고
    • Caspase activation by adenovirus E4orf4 protein is cell line specific and is mediated by the death receptor pathway
    • Livne A., et al. Caspase activation by adenovirus E4orf4 protein is cell line specific and is mediated by the death receptor pathway. J. Virol. 75:2001;789-798.
    • (2001) J. Virol. , vol.75 , pp. 789-798
    • Livne, A.1
  • 41
    • 0037077254 scopus 로고    scopus 로고
    • Coupling endoplasmic reticulum stress to the cell death program. An Apaf-1-independent intrinsic pathway
    • Rao R.V., et al. Coupling endoplasmic reticulum stress to the cell death program. An Apaf-1-independent intrinsic pathway. J. Biol. Chem. 277:2002;21836-21842.
    • (2002) J. Biol. Chem. , vol.277 , pp. 21836-21842
    • Rao, R.V.1
  • 42
    • 0033393502 scopus 로고    scopus 로고
    • Cancer gene therapy using a pro-apoptotic gene, caspase-3
    • Yamabe K., et al. Cancer gene therapy using a pro-apoptotic gene, caspase-3. Gene Ther. 6:1999;1952-1959.
    • (1999) Gene Ther. , vol.6 , pp. 1952-1959
    • Yamabe, K.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.