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Volumn 11, Issue 1, 1999, Pages 68-75

Mechanisms of apoptosis avoidance in cancer

Author keywords

[No Author keywords available]

Indexed keywords

OXYGEN;

EID: 0033026714     PISSN: 10408746     EISSN: None     Source Type: Journal    
DOI: 10.1097/00001622-199901000-00014     Document Type: Review
Times cited : (352)

References (57)
  • 1
    • 0030702084 scopus 로고    scopus 로고
    • Caspases: Intracellular signaling by proteolysis
    • 1 Salvesen GS, Dixit VM: Caspases: intracellular signaling by proteolysis. Cell 1997, 91:443-446.
    • (1997) Cell , vol.91 , pp. 443-446
    • Salvesen, G.S.1    Dixit, V.M.2
  • 2
    • 0031044652 scopus 로고    scopus 로고
    • Mammalian cell death proteases: A family of highly conserved aspartate specific cysteine proteases
    • 2 Alnemri ES: Mammalian cell death proteases: a family of highly conserved aspartate specific cysteine proteases. J Cell Biochem 1997, 64:33-42.
    • (1997) J Cell Biochem , vol.64 , pp. 33-42
    • Alnemri, E.S.1
  • 3
    • 0029927422 scopus 로고    scopus 로고
    • The role of proteases during apoptosis
    • 3 Patel T, Gores GJ, Kaufmann SH: The role of proteases during apoptosis. FASEB J 1996, 10:587-597.
    • (1996) FASEB J , vol.10 , pp. 587-597
    • Patel, T.1    Gores, G.J.2    Kaufmann, S.H.3
  • 4
    • 0030050416 scopus 로고    scopus 로고
    • Programmed cell death in invertebrates
    • 4 Hengartner MO: Programmed cell death in invertebrates. Curr Opin Genet Dev 1996, 6:34-38.
    • (1996) Curr Opin Genet Dev , vol.6 , pp. 34-38
    • Hengartner, M.O.1
  • 5
    • 34547667507 scopus 로고    scopus 로고
    • IAP-family proteins: Suppressors of apoptosis
    • in press.
    • 5 Deveraux QL, Reed JC: IAP-family proteins: suppressors of apoptosis. Oncogene 1998, in press.
    • (1998) Oncogene
    • Deveraux, Q.L.1    Reed, J.C.2
  • 6
    • 0030810926 scopus 로고    scopus 로고
    • X-linked IAP is a direct inhibitor of cell death proteases
    • 6 Deveraux Q, Takahashi R, Salvesen GS, Reed JC: X-linked IAP is a direct inhibitor of cell death proteases. Nature 1997, 388:300-304. This article presents the first example of direct inhibition of caspases by an IAP family protein.
    • (1997) Nature , vol.388 , pp. 300-304
    • Deveraux, Q.1    Takahashi, R.2    Salvesen, G.S.3    Reed, J.C.4
  • 7
    • 0030746636 scopus 로고    scopus 로고
    • A novel anti-apoptosis gene, survivin, expressed in cancer and lymphoma
    • 7 Ambrosini G, Adida C, Altieri D: A novel anti-apoptosis gene, survivin, expressed in cancer and lymphoma. Nat Med 1997, 3:917-921. This paper provides the first example of overexpression of an IAP family gene in cancers.
    • (1997) Nat Med , vol.3 , pp. 917-921
    • Ambrosini, G.1    Adida, C.2    Altieri, D.3
  • 8
    • 0030928651 scopus 로고    scopus 로고
    • Inhibition of reaper-induced apoptosis by interaction with inhibitor of apoptosis proteins (IAPs)
    • 8 Vucic D, Kaiser WJ, Harvey AJ, Miller LK: Inhibition of reaper-induced apoptosis by interaction with inhibitor of apoptosis proteins (IAPs). Proc Natl Acad Sci U S A 1997, 94:10183-10188.
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 10183-10188
    • Vucic, D.1    Kaiser, W.J.2    Harvey, A.J.3    Miller, L.K.4
  • 9
    • 0031815071 scopus 로고    scopus 로고
    • Inhibitor of apoptosis proteins physically interact with and block apoptosis induced by drosophila proteins HID and GRIM
    • 9 Vucic D, Kaiser WJ, Miller LK: Inhibitor of apoptosis proteins physically interact with and block apoptosis induced by drosophila proteins HID and GRIM. Mol Cell Biol 1998, 18:3300-3309.
    • (1998) Mol Cell Biol , vol.18 , pp. 3300-3309
    • Vucic, D.1    Kaiser, W.J.2    Miller, L.K.3
  • 10
    • 0032508669 scopus 로고    scopus 로고
    • Apoptosis induced by drosophila reaper and grim in a human system
    • 10 McCarthy JV, Dixit VM: Apoptosis induced by drosophila reaper and grim in a human system. J Biol Chem 1998, 273:24009-24015.
    • (1998) J Biol Chem , vol.273 , pp. 24009-24015
    • McCarthy, J.V.1    Dixit, V.M.2
  • 11
    • 0028040019 scopus 로고
    • Bcl-2 and the regulation of programmed cell death
    • 11 Reed JC: Bcl-2 and the regulation of programmed cell death. J Cell Biol 1994, 124:1-6.
    • (1994) J Cell Biol , vol.124 , pp. 1-6
    • Reed, J.C.1
  • 12
    • 0032580361 scopus 로고    scopus 로고
    • Subcellular and submitochondrial mode of action of Bcl-2-like proteins
    • 12 Zamzami N, Brenner C, Marzo I, Susin SA, Kroemer G: Subcellular and submitochondrial mode of action of Bcl-2-like proteins. Oncogene 1998, 16:2265-2282.
    • (1998) Oncogene , vol.16 , pp. 2265-2282
    • Zamzami, N.1    Brenner, C.2    Marzo, I.3    Susin, S.A.4    Kroemer, G.5
  • 13
    • 0031436251 scopus 로고    scopus 로고
    • Heterodimerization-independent functions of cell death regulatory proteins Bax and Bcl-2 in yeast and mammalian cells
    • 13 Zha H, Reed JC: Heterodimerization-independent functions of cell death regulatory proteins Bax and Bcl-2 in yeast and mammalian cells. J Biol Chem 1997, 272:31482-31488.
    • (1997) J Biol Chem , vol.272 , pp. 31482-31488
    • Zha, H.1    Reed, J.C.2
  • 14
    • 0032502776 scopus 로고    scopus 로고
    • Mtd, a novel Bcl-2 family member activates apoptosis in the absence of heterodimerization with Bcl-2 and Bcl-XL
    • 14 Inohara N, Ekhterae D, Garcia I, Carrio R, Merino J, Merry A, et al.: Mtd, a novel Bcl-2 family member activates apoptosis in the absence of heterodimerization with Bcl-2 and Bcl-XL. J Biol Chem 1998, 273:8705-8710.
    • (1998) J Biol Chem , vol.273 , pp. 8705-8710
    • Inohara, N.1    Ekhterae, D.2    Garcia, I.3    Carrio, R.4    Merino, J.5    Merry, A.6
  • 15
    • 0030669561 scopus 로고    scopus 로고
    • Bak can accelerate chemotherapy-induced cell death independently of itsheterodimerization with Bcl-XL and Bcl-2
    • 15 Simonian PL, Grillot DA, Nunez G: Bak can accelerate chemotherapy-induced cell death independently of itsheterodimerization with Bcl-XL and Bcl-2. Oncogene 1997, 15:1871-1875.
    • (1997) Oncogene , vol.15 , pp. 1871-1875
    • Simonian, P.L.1    Grillot, D.A.2    Nunez, G.3
  • 16
    • 0032146987 scopus 로고    scopus 로고
    • Bcl-2-family proteins-the role of the BH3 domain in apoptosis
    • 16 Kelekar A, Thompson CB: Bcl-2-family proteins-the role of the BH3 domain in apoptosis. Trends Cell Biol 1998, 8:324-330.
    • (1998) Trends Cell Biol , vol.8 , pp. 324-330
    • Kelekar, A.1    Thompson, C.B.2
  • 17
    • 0031038137 scopus 로고    scopus 로고
    • Bax suppresses tumorigenesis and stimulates apoptosis in vivo
    • 17 Yin C, Knudson CM, Korsmeyer SJ, Van Dyke T: Bax suppresses tumorigenesis and stimulates apoptosis in vivo. Nature 1997, 385:637-640. This article provides direct evidence that the pro-apoptotic protein Bax functions as a tumor supressor.
    • (1997) Nature , vol.385 , pp. 637-640
    • Yin, C.1    Knudson, C.M.2    Korsmeyer, S.J.3    Van Dyke, T.4
  • 18
    • 0030584079 scopus 로고    scopus 로고
    • Apoptosis meets signal transduction: Elimination of a BAD influence
    • 18 Gajewski TF, Thompson CB: Apoptosis meets signal transduction: elimination of a BAD influence. Cell 1996, 87:589-592.
    • (1996) Cell , vol.87 , pp. 589-592
    • Gajewski, T.F.1    Thompson, C.B.2
  • 19
    • 0030884103 scopus 로고    scopus 로고
    • PKB/Akt: Connecting phosphoinositide 3-kinase to cell survival and beyond
    • 19 Marte BM, Downward J: PKB/Akt: connecting phosphoinositide 3-kinase to cell survival and beyond. Trends Biochem Sci 1997, 22:355-358.
    • (1997) Trends Biochem Sci , vol.22 , pp. 355-358
    • Marte, B.M.1    Downward, J.2
  • 20
    • 0028972616 scopus 로고
    • Regulation of apoptosis by Bcl-2 family proteins and its role in cancer and chemoresistance
    • 20 Reed JC: Regulation of apoptosis by Bcl-2 family proteins and its role in cancer and chemoresistance. Curr Opin Oncol 1995, 7:541-546.
    • (1995) Curr Opin Oncol , vol.7 , pp. 541-546
    • Reed, J.C.1
  • 21
    • 0030888664 scopus 로고    scopus 로고
    • BCL-2 antisense therapy in patients with non-Hodgkin lymphoma
    • 21 Webb A, Cunningham D, Cotter F, Clarke PA, di Stefano F, Ross P, et al.: BCL-2 antisense therapy in patients with non-Hodgkin lymphoma. Lancet 1997, 349:1137-1141. This is the first clinical trial of antisense therapy targeted against an anti-apoptosis gene, Bcl-2.
    • (1997) Lancet , vol.349 , pp. 1137-1141
    • Webb, A.1    Cunningham, D.2    Cotter, F.3    Clarke, P.A.4    Di Stefano, F.5    Ross, P.6
  • 22
    • 0028883179 scopus 로고
    • Tumor suppressor p53 is a direct transcriptional activator of human BAX gene
    • 22 Miyashita T, Reed JC: Tumor suppressor p53 is a direct transcriptional activator of human BAX gene. Cell 1995, 80:293-299. This paper demonstrated the direct connection of p53 to a pro-apoptotic gene, BAX.
    • (1995) Cell , vol.80 , pp. 293-299
    • Miyashita, T.1    Reed, J.C.2
  • 23
    • 0027944228 scopus 로고
    • Induction of BAX by genotoxic stress in human cells correlates with normal p53 status and apoptosis
    • 23 Zhan Q, Fan S, Bae I, Guillouf C, Liebermann DA, O'Connor PM, Fornace AJ Jr: Induction of BAX by genotoxic stress in human cells correlates with normal p53 status and apoptosis. Oncogene 1994, 9:3743-3751.
    • (1994) Oncogene , vol.9 , pp. 3743-3751
    • Zhan, Q.1    Fan, S.2    Bae, I.3    Guillouf, C.4    Liebermann, D.A.5    O'Connor, P.M.6    Fornace A.J., Jr.7
  • 24
    • 8944230657 scopus 로고    scopus 로고
    • Overexpression of the death-promoting gene bax-a which is downregulated in breast cancer restores sensitivity to different apoptotic stimuli and reduces tumor growth in SCID mice
    • 24 Bargou RC, Wagener C, Bommert K, Mapara MY, Daniel PT, Arnold W, et al.: Overexpression of the death-promoting gene bax-a which is downregulated in breast cancer restores sensitivity to different apoptotic stimuli and reduces tumor growth in SCID mice. J Clin Invest 1996, 97:2651-2659.
    • (1996) J Clin Invest , vol.97 , pp. 2651-2659
    • Bargou, R.C.1    Wagener, C.2    Bommert, K.3    Mapara, M.Y.4    Daniel, P.T.5    Arnold, W.6
  • 25
    • 0030694255 scopus 로고    scopus 로고
    • Apoptosis-associated signaling pathways are required for chemotherapy-mediated female germ cell destruction
    • 25 Perez GI, Knudson CM, Leykin L, Korsmeyer SJ, Tilly JL: Apoptosis-associated signaling pathways are required for chemotherapy-mediated female germ cell destruction. Nat Med 1997, 3:1228-1232.
    • (1997) Nat Med , vol.3 , pp. 1228-1232
    • Perez, G.I.1    Knudson, C.M.2    Leykin, L.3    Korsmeyer, S.J.4    Tilly, J.L.5
  • 26
    • 0030979773 scopus 로고    scopus 로고
    • Double identity for proteins of the Bcl-2 family
    • 26 Reed JC: Double identity for proteins of the Bcl-2 family. Nature 1997, 387:773-776.
    • (1997) Nature , vol.387 , pp. 773-776
    • Reed, J.C.1
  • 28
    • 0032575752 scopus 로고    scopus 로고
    • Mitochondria and apoptosis
    • 28 Green D, Reed J: Mitochondria and apoptosis. Science 1998, 281:1309-1312.
    • (1998) Science , vol.281 , pp. 1309-1312
    • Green, D.1    Reed, J.2
  • 30
    • 0032576692 scopus 로고    scopus 로고
    • Bcl-2 prolongs cell survival after bax-induced release of cytochrome c
    • 30 Rosse T, Olivier R, Monney L, Rager M, Conus S, Fellay J, et al.: Bcl-2 prolongs cell survival after bax-induced release of cytochrome c. Nature 1998, 391:496-499.
    • (1998) Nature , vol.391 , pp. 496-499
    • Rosse, T.1    Olivier, R.2    Monney, L.3    Rager, M.4    Conus, S.5    Fellay, J.6
  • 32
    • 0032566649 scopus 로고    scopus 로고
    • The pro-apoptotic protein Bax and the adenine nucleotide translocator cooperate in the control of mitochondrial membrane permeability and apoptosis
    • 32 Marzo I, et al.: The pro-apoptotic protein Bax and the adenine nucleotide translocator cooperate in the control of mitochondrial membrane permeability and apoptosis. Science 1998, 281:2027-2031. This article provides the first evidence of a direct interaction of Bcl-2 family proteins with the adenine nucleotide translocator, a component of the permeability transition pore complex.
    • (1998) Science , vol.281 , pp. 2027-2031
    • Marzo, I.1
  • 33
    • 0030916669 scopus 로고    scopus 로고
    • The proto-oncogene Bcl-2 and its role in regulating apoptosis
    • 33 Kroemer G: The proto-oncogene Bcl-2 and its role in regulating apoptosis. Nat Med 1997, 3:614-620.
    • (1997) Nat Med , vol.3 , pp. 614-620
    • Kroemer, G.1
  • 34
    • 0030782177 scopus 로고    scopus 로고
    • Cytochrome C: Can't live with it; can't live without it
    • 34 Reed JC: Cytochrome C: can't live with it; can't live without it. Cell 1997, 91:559-562.
    • (1997) Cell , vol.91 , pp. 559-562
    • Reed, J.C.1
  • 36
    • 0032575750 scopus 로고    scopus 로고
    • Caspases: Enemies within
    • 36 Thornberry N, Lazebnik Y: Caspases: enemies within. Science 1998, 281:1312-1316.
    • (1998) Science , vol.281 , pp. 1312-1316
    • Thornberry, N.1    Lazebnik, Y.2
  • 37
    • 0030745646 scopus 로고    scopus 로고
    • Apaf-1, a human protein homologous to C. elegans CED-4, particpates in cytochrome c-dependent activation of caspase-3
    • 37 Zou H, Henzel WJ, Liu X, Lutschg A, Wang X: Apaf-1, a human protein homologous to C. elegans CED-4, particpates in cytochrome c-dependent activation of caspase-3. Cell 1997, 90:405-413. Demonstrates molecular cloning of first human homologue of CED-4. Provides the missing link between Bcl-2 family proteins and caspases in mammals.
    • (1997) Cell , vol.90 , pp. 405-413
    • Zou, H.1    Henzel, W.J.2    Liu, X.3    Lutschg, A.4    Wang, X.5
  • 38
    • 0030715323 scopus 로고    scopus 로고
    • Cytochrome c and dATP-dependent formation of Apaf-1/Caspase-9 complex initiates an apoptotic protease cascade
    • 38 Li P, Nijhawan D, Budihardjo I, Srinivasula SM, Ahmad M, Alnemri ES, Wang X: Cytochrome c and dATP-dependent formation of Apaf-1/Caspase-9 complex initiates an apoptotic protease cascade. Cell 1997, 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
  • 39
    • 0032576641 scopus 로고    scopus 로고
    • Apoptosis. Death cycle and Swiss army knives
    • 39 Hengartner MO: Apoptosis. Death cycle and Swiss army knives. Nature 1998, 391:441-442.
    • (1998) Nature , vol.391 , pp. 441-442
    • Hengartner, M.O.1
  • 40
    • 0032575688 scopus 로고    scopus 로고
    • The Bcl-2 protein family: Arbiters of cell survival
    • 40 Adams J, Cory S: The Bcl-2 protein family: arbiters of cell survival. Science 1998, 281:1322-1326.
    • (1998) Science , vol.281 , pp. 1322-1326
    • Adams, J.1    Cory, S.2
  • 41
    • 0029906828 scopus 로고    scopus 로고
    • BAX-induced cell death may not require interleukin 1b-converting enzyme-like proteases
    • 41 Xiang J, Chao DT, Korsmeyer SJ: BAX-induced cell death may not require interleukin 1b-converting enzyme-like proteases. Proc Natl Acad Sci U S A 1996, 93:14559-14563. This article provided some of the first evidence that Bcl-2 family proteins can regulate cell death independently of caspases.
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 14559-14563
    • Xiang, J.1    Chao, D.T.2    Korsmeyer, S.J.3
  • 43
  • 44
    • 0030987071 scopus 로고    scopus 로고
    • Transducing signals of life and death
    • 44 Yuan J: Transducing signals of life and death. Curr Opin Cell Biol 1997, 9:247-251.
    • (1997) Curr Opin Cell Biol , vol.9 , pp. 247-251
    • Yuan, J.1
  • 45
    • 0032536771 scopus 로고    scopus 로고
    • Two CD95 (APO-1/Fas) signaling pathways
    • 45 Scaffidi C, Fulda S, Srinivasan A, Friesen C, Li F, Tomaselli KJ, et al.: Two CD95 (APO-1/Fas) signaling pathways. EMBO J 1998, 17:1675-1687. The authors provide insights into why Bcl-2 blocks death induced by Fas (CD95) in some cells but not others.
    • (1998) EMBO J , vol.17 , pp. 1675-1687
    • Scaffidi, C.1    Fulda, S.2    Srinivasan, A.3    Friesen, C.4    Li, F.5    Tomaselli, K.J.6
  • 46
    • 0032568954 scopus 로고    scopus 로고
    • Apoptosis induction by caspase-8 is amplified through the mitochondrial release of cytochrome c
    • 46 Kuwana T, Smith JJ, Muzio M, Dixit V, Newmeyer DD, Kornbluth S: Apoptosis induction by caspase-8 is amplified through the mitochondrial release of cytochrome c. J Biol Chem 1998, 273:16589-16594. The authors provide insights into why Bcl-2 blocks death induced by Fas (CD95) in some cells but not others.
    • (1998) J Biol Chem , vol.273 , pp. 16589-16594
    • Kuwana, T.1    Smith, J.J.2    Muzio, M.3    Dixit, V.4    Newmeyer, D.D.5    Kornbluth, S.6
  • 47
    • 0032544268 scopus 로고    scopus 로고
    • Apoptotic pathways: The roads to ruin
    • 47 Green D: Apoptotic pathways: the roads to ruin. Cell 1998, 94:695-698.
    • (1998) Cell , vol.94 , pp. 695-698
    • Green, D.1
  • 49
    • 1842367285 scopus 로고    scopus 로고
    • Placing death under control
    • 49 Wallach D: Placing death under control. Nature 1997, 388:123-126.
    • (1997) Nature , vol.388 , pp. 123-126
    • Wallach, D.1
  • 51
    • 0031034563 scopus 로고    scopus 로고
    • Controlling cell death
    • 51 Golstein P: Controlling cell death. Science 1997, 275:1081-1082.
    • (1997) Science , vol.275 , pp. 1081-1082
    • Golstein, P.1
  • 52
    • 10544232277 scopus 로고    scopus 로고
    • Melanoma cell expression of Fas(Apo-1/CD95) ligand: Implications for tumor immune escape
    • 52 Hahne M, Rimoldi D, Schroter M, Romero P, Schreier M, Frenck LE, et al.: Melanoma cell expression of Fas(Apo-1/CD95) ligand: implications for tumor immune escape. Science 1996, 274:1363-1366.
    • (1996) Science , vol.274 , pp. 1363-1366
    • Hahne, M.1    Rimoldi, D.2    Schroter, M.3    Romero, P.4    Schreier, M.5    Frenck, L.E.6
  • 53
    • 0029808372 scopus 로고    scopus 로고
    • The Fas counterattack: Fas-mediated T cell killing by colon cancer cells expressing Fas ligand
    • 53 O'Connell J, O'Sullivan GC, Collins JK, Shanahan F: The Fas counterattack: Fas-mediated T cell killing by colon cancer cells expressing Fas ligand. J Exp Med 1996, 184:1075-1082.
    • (1996) J Exp Med , vol.184 , pp. 1075-1082
    • O'Connell, J.1    O'Sullivan, G.C.2    Collins, J.K.3    Shanahan, F.4
  • 54
    • 0032103027 scopus 로고    scopus 로고
    • The Fas counterattack in vivo: Apoptotic depletion of tumor-infiltrating lymphocytes associated with Fas ligand expression by human esophageal carcinoma
    • 54 Bennett M, O'Connell J, O'Sullivan GC, Brady C, Roche D, Collins JK, Shanahan F: The Fas counterattack in vivo: apoptotic depletion of tumor-infiltrating lymphocytes associated with Fas ligand expression by human esophageal carcinoma. J Immunol 1998, 160:5669-5675.
    • (1998) J Immunol , vol.160 , pp. 5669-5675
    • Bennett, M.1    O'Connell, J.2    O'Sullivan, G.C.3    Brady, C.4    Roche, D.5    Collins, J.K.6    Shanahan, F.7
  • 55
    • 0031253967 scopus 로고    scopus 로고
    • On the TRAIL from p53 to apoptosis?
    • 55 Kastan M: On the TRAIL from p53 to apoptosis? Nat Genet 1997, 17:130-131.
    • (1997) Nat Genet , vol.17 , pp. 130-131
    • Kastan, M.1
  • 56
    • 0032575705 scopus 로고    scopus 로고
    • A matter of life and cell death
    • 56 Evan G, Littlewood T: A matter of life and cell death. Science 1998, 281:1317-1322.
    • (1998) Science , vol.281 , pp. 1317-1322
    • Evan, G.1    Littlewood, T.2
  • 57
    • 0028057613 scopus 로고
    • Disruption of epithelial cell-matrix interactions induces apoptosis
    • 57 Frisch SM, Francis H: Disruption of epithelial cell-matrix interactions induces apoptosis. J Cell Biol 1994, 124:619-626. This article provides the original description of apoptosis induced by detachment of normal cells from the extracellular matrix due to lack of survival signals provided by integrins. The term anoikis (Greek for "without roots" or "homeless") was coined to describe this phenomenon of importance for tumor cell invasion and metastasis and for some anti-angiogenic therapies.
    • (1994) J Cell Biol , vol.124 , pp. 619-626
    • Frisch, S.M.1    Francis, H.2


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