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Volumn 8, Issue 6, 2003, Pages 617-629

Apoptosis modulatory activities of transiently expressed Bcl-2: Roles in cytochrome c release and Bax regulation

Author keywords

Apoptosis; Bax; Bcl 2; Bcl XL; Mitochondria

Indexed keywords

CALPASTATIN; CASPASE INHIBITOR; CYTOCHROME C; PROTEIN BAX; PROTEIN BCL 2; PROTEIN BCL XL; PROTEIN BID;

EID: 0242551447     PISSN: 13608185     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1026187526113     Document Type: Article
Times cited : (56)

References (58)
  • 1
    • 0032575688 scopus 로고    scopus 로고
    • The Bcl-2 protein family: Arbiters of cell survival
    • Adams JM, 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.M.1    Cory, S.2
  • 2
    • 0021679848 scopus 로고
    • Cloning of the chromosomes breakpoint of neoplastic B cells with the t(14;18) chromosome translocation
    • Tsujimoto Y, Finger LR, Yunis J, Nowell PC, Croce CM. Cloning of the chromosomes breakpoint of neoplastic B cells with the t(14;18) chromosome translocation. Science 1984; 226: 1097-1099.
    • (1984) Science , vol.226 , pp. 1097-1099
    • Tsujimoto, Y.1    Finger, L.R.2    Yunis, J.3    Nowell, P.C.4    Croce, C.M.5
  • 3
    • 0021934042 scopus 로고
    • Cloning of the chromosomal breakpoint of t(14;18) human lymphomas: Clustering around JH on chromosome 14 and near a transcriptional unit on 18
    • Bakhshi A, Jensen JP, Goldman P, et al. Cloning of the chromosomal breakpoint of t(14;18) human lymphomas: Clustering around JH on chromosome 14 and near a transcriptional unit on 18. Cell 1985; 41: 899-906.
    • (1985) Cell , vol.41 , pp. 899-906
    • Bakhshi, A.1    Jensen, J.P.2    Goldman, P.3
  • 4
    • 0022971142 scopus 로고
    • Cloning and structural analysis of cDNAs from bcl-2 and the hybrid bcl-2/immunoglobulin transcript resulting from the t(14;18) translocation
    • Cleary ML, Smith SD, Sklar J. Cloning and structural analysis of cDNAs from bcl-2 and the hybrid bcl-2/immunoglobulin transcript resulting from the t(14;18) translocation. Cell 1986; 47: 19-28.
    • (1986) Cell , vol.47 , pp. 19-28
    • Cleary, M.L.1    Smith, S.D.2    Sklar, J.3
  • 5
    • 0028670378 scopus 로고
    • Analysis of the role of bcl-2 in apoptosis
    • Hawkins CJ, Vaux DL. Analysis of the role of bcl-2 in apoptosis. Immunol Rev 1994; 142: 127-139.
    • (1994) Immunol Rev , vol.142 , pp. 127-139
    • Hawkins, C.J.1    Vaux, D.L.2
  • 7
    • 0028958030 scopus 로고
    • Bcl-2: Prevention of apoptosis as a mechanism of drug resistance
    • Reed JC. Bcl-2: Prevention of apoptosis as a mechanism of drug resistance. Hematol Oncol Clin North Am 1995; 9: 451-473.
    • (1995) Hematol Oncol Clin North Am , vol.9 , pp. 451-473
    • Reed, J.C.1
  • 8
    • 0030046508 scopus 로고    scopus 로고
    • Life, death, and the pursuit of apoptosis
    • White E. Life, death, and the pursuit of apoptosis. Genes & Devel 1996; 10: 1-15.
    • (1996) Genes & Devel , vol.10 , pp. 1-15
    • White, E.1
  • 9
    • 0029899181 scopus 로고    scopus 로고
    • Molecular thanatopsis: A discourse on the Bcl-2 family and cell death
    • Yang E, Korsmeyer SJ. Molecular thanatopsis: A discourse on the Bcl-2 family and cell death. Blood 1996; 88: 386-401.
    • (1996) Blood , vol.88 , pp. 386-401
    • Yang, E.1    Korsmeyer, S.J.2
  • 10
    • 0027427492 scopus 로고
    • Bcl-2-deficient mice demonstrate fulminant lymphoid apoptosis, polycystic kidneys, and hypopigmented hair
    • Veis DJ, Sorenson CM, Shutter JR, Korsmeyer SJ. Bcl-2-deficient mice demonstrate fulminant lymphoid apoptosis, polycystic kidneys, and hypopigmented hair. Cell 1993; 75: 229-240.
    • (1993) Cell , vol.75 , pp. 229-240
    • Veis, D.J.1    Sorenson, C.M.2    Shutter, J.R.3    Korsmeyer, S.J.4
  • 11
    • 0028175759 scopus 로고
    • Targeted disruption of Bcl-2ab in mice: Occurrence of gray hair, polycystic kidney disease, and lymphocytopenia
    • Nakayama K, Nakayama K-I, Negishi I, Kuida K, Sawa H, Loh DY. Targeted disruption of Bcl-2ab in mice: Occurrence of gray hair, polycystic kidney disease, and lymphocytopenia. Proc Natl Acad Sci USA 1994; 91: 3700-3704.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 3700-3704
    • Nakayama, K.1    Nakayama, K.-I.2    Negishi, I.3    Kuida, K.4    Sawa, H.5    Loh, D.Y.6
  • 12
    • 0027282044 scopus 로고
    • bcl-X, a Bcl-2 related gene that functions as a dominant regulator of apoptotic cell death
    • Boise LH, Gonzalez-Garcia M, Postema CE, et al. bcl-X, a Bcl-2 related gene that functions as a dominant regulator of apoptotic cell death. Cell 1993; 74: 597-608.
    • (1993) Cell , vol.74 , pp. 597-608
    • Boise, L.H.1    Gonzalez-Garcia, M.2    Postema, C.E.3
  • 14
    • 0028922885 scopus 로고
    • Massive cell death of immature hematopoietic cells and neurons in Bcl-X-deficient mice
    • Motoyama N, Wang F, Roth KA, et al. Massive cell death of immature hematopoietic cells and neurons in Bcl-X-deficient mice. Science 1995; 267: 1506-1510.
    • (1995) Science , vol.267 , pp. 1506-1510
    • Motoyama, N.1    Wang, F.2    Roth, K.A.3
  • 15
    • 0027166048 scopus 로고
    • Bcl-2 heterodimerizes in vivo with a conserved homolog, Bax, that accelerates programmed cell death
    • Oltvai ZN, Milliman CL, Korsmeyer SJ. Bcl-2 heterodimerizes in vivo with a conserved homolog, Bax, that accelerates programmed cell death. Cell 1993; 74: 609-619.
    • (1993) Cell , vol.74 , pp. 609-619
    • Oltvai, Z.N.1    Milliman, C.L.2    Korsmeyer, S.J.3
  • 17
    • 0030975776 scopus 로고    scopus 로고
    • An early and massive wave of germinal cell apoptosis is required for the development of functional spermatogenesis
    • Rodriguez I, Ody C, Araki K, Garcia I, Vassalli P. An early and massive wave of germinal cell apoptosis is required for the development of functional spermatogenesis. EMBO J 1997; 16: 2262-2270.
    • (1997) EMBO J , vol.16 , pp. 2262-2270
    • Rodriguez, I.1    Ody, C.2    Araki, K.3    Garcia, I.4    Vassalli, P.5
  • 18
    • 0030898680 scopus 로고    scopus 로고
    • bax deficiency prevents the increased cell death of immature neurons in bcl-x-deficient mice
    • Shindler KS, Latham CB, Roth KA. bax deficiency prevents the increased cell death of immature neurons in bcl-x-deficient mice. J Neurosci 1997; 17: 3112-3119.
    • (1997) J Neurosci , vol.17 , pp. 3112-3119
    • Shindler, K.S.1    Latham, C.B.2    Roth, K.A.3
  • 20
    • 0031007644 scopus 로고    scopus 로고
    • Nonionic detergents induce dimerization among members of the Bcl-2 family
    • Hsu Y-T, Youle RJ. Nonionic detergents induce dimerization among members of the Bcl-2 family. J Biol Chem 1997; 272: 13829-13834.
    • (1997) J Biol Chem , vol.272 , pp. 13829-13834
    • Hsu, Y.-T.1    Youle, R.J.2
  • 21
    • 0032562796 scopus 로고    scopus 로고
    • Bax in murine thymus is a soluble monomeric protein that displays differential detergent-induced conformations
    • Hsu Y-T, Youle RY. Bax in murine thymus is a soluble monomeric protein that displays differential detergent-induced conformations. J Biol Chem 1998; 273: 10777-10783.
    • (1998) J Biol Chem , vol.273 , pp. 10777-10783
    • Hsu, Y.-T.1    Youle, R.Y.2
  • 23
    • 0032528118 scopus 로고    scopus 로고
    • Enforced dimerization of Bax results in its translocation, mitochondrial dysfunction and apoptosis
    • Gross A, Jockel J, Wei MC, Korsmeyer SJ. Enforced dimerization of Bax results in its translocation, mitochondrial dysfunction and apoptosis. EMBO J 1998; 17: 3878-3885.
    • (1998) EMBO J , vol.17 , pp. 3878-3885
    • Gross, A.1    Jockel, J.2    Wei, M.C.3    Korsmeyer, S.J.4
  • 24
    • 0033522391 scopus 로고    scopus 로고
    • Conformation of the Bax C-terminus regulates subcellular location and cell death
    • Nechushtan A, Smith CL, Hsu Y-T, Youle RJ. Conformation of the Bax C-terminus regulates subcellular location and cell death. EMBO J 1999; 18: 2330-2341.
    • (1999) EMBO J , vol.18 , pp. 2330-2341
    • Nechushtan, A.1    Smith, C.L.2    Hsu, Y.-T.3    Youle, R.J.4
  • 26
    • 0035853811 scopus 로고    scopus 로고
    • Bax is present as a high molecular weight oligomer-complex in the mitochondrial membrane of apoptotic cells
    • Antonsson B, Montessuit S, Sanchez B, Martinou JC. Bax is present as a high molecular weight oligomer-complex in the mitochondrial membrane of apoptotic cells. J Biol Chem 2001; 276: 11615-11623.
    • (2001) J Biol Chem , vol.276 , pp. 11615-11623
    • Antonsson, B.1    Montessuit, S.2    Sanchez, B.3    Martinou, J.C.4
  • 28
    • 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, et al. 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
  • 31
    • 0034059440 scopus 로고    scopus 로고
    • Bcl-2 inhibits bax translocation from cytosol to mitochondria during drug-induced apoptosis of human tumor cells
    • Murphy KM, Ranganathan V, Farnsworth ML, Kavallaris M, Lock RB. Bcl-2 inhibits bax translocation from cytosol to mitochondria during drug-induced apoptosis of human tumor cells. Cell Death Differ 2000; 7: 102-111.
    • (2000) Cell Death Differ , vol.7 , pp. 102-111
    • Murphy, K.M.1    Ranganathan, V.2    Farnsworth, M.L.3    Kavallaris, M.4    Lock, R.B.5
  • 32
    • 0031036872 scopus 로고    scopus 로고
    • Prevention of apoptosis by Bcl-2: Release of cytochrome c from mitochondria blocked
    • Yang J, Liu X, Bhalla K, et al. Prevention of apoptosis by Bcl-2: Release of cytochrome c from mitochondria blocked. Science 1997; 275: 1129-1132.
    • (1997) Science , vol.275 , pp. 1129-1132
    • Yang, J.1    Liu, X.2    Bhalla, K.3
  • 33
    • 0031037897 scopus 로고    scopus 로고
    • The release of cytochrome c from mitochondria: A primary site for Bcl-2 regulation of apoptosis
    • Kluck RM, Bossy-Wetzel E, Green DR, Newmeyer DD. The release of cytochrome c from mitochondria: A primary site for Bcl-2 regulation of apoptosis. Science 1997; 275: 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
  • 34
    • 0030610962 scopus 로고    scopus 로고
    • L as an inhibitor of cytosolic cytochrome c accumulation in DNA damage-induced apoptosis
    • L as an inhibitor of cytosolic cytochrome c accumulation in DNA damage-induced apoptosis. Proc Natl Acad Sci USA 1997; 94: 6939-6942.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 6939-6942
    • Kharbanda, S.1    Pandey, P.2    Schofield, L.3
  • 35
    • 0030843575 scopus 로고    scopus 로고
    • L inhibits Ara-C-induced mitochondrial loss of cytochrome c and other perturbations that activate the molecular cascade of apoptosis
    • L inhibits Ara-C-induced mitochondrial loss of cytochrome c and other perturbations that activate the molecular cascade of apoptosis. Cancer Res 1997; 57: 3115-3120.
    • (1997) Cancer Res , vol.57 , pp. 3115-3120
    • Kim, C.N.1    Wang, X.2    Ibrado, A.M.3    Liu, L.4    Fang, G.5    Bhalla, K.6
  • 36
    • 0032504253 scopus 로고    scopus 로고
    • A potent cell death activity associated with transient high level expression of Bcl-2
    • Uhlmann EJ, Subramanian T, Vater CA, Lutz R, Chinnadurai G. A potent cell death activity associated with transient high level expression of Bcl-2. J Biol Chem 1998; 273: 17926-17932.
    • (1998) J Biol Chem , vol.273 , pp. 17926-17932
    • Uhlmann, E.J.1    Subramanian, T.2    Vater, C.A.3    Lutz, R.4    Chinnadurai, G.5
  • 37
    • 0033566823 scopus 로고    scopus 로고
    • Expression level of Bcl-2 determines anti- or proapoptotic functions
    • Shinoura N, Yoshida Y, Nishimura M, et al. Expression level of Bcl-2 determines anti- or proapoptotic functions. Cancer Res 1999; 59: 4119-4128.
    • (1999) Cancer Res , vol.59 , pp. 4119-4128
    • Shinoura, N.1    Yoshida, Y.2    Nishimura, M.3
  • 38
    • 0035941360 scopus 로고    scopus 로고
    • Transient expression of wild-type or mitochondrially targeted Bcl-2 induces apoptosis, whereas transient expression of endoplasmic reticulum-targeted Bcl-2 is protective against Bax-induced cell death
    • Wang NS, Unkila MT, Reineks EZ, Distelhorst CW. Transient expression of wild-type or mitochondrially targeted Bcl-2 induces apoptosis, whereas transient expression of endoplasmic reticulum-targeted Bcl-2 is protective against Bax-induced cell death. J Biol Chem 2001; 276: 44117-44128.
    • (2001) J Biol Chem , vol.276 , pp. 44117-44128
    • Wang, N.S.1    Unkila, M.T.2    Reineks, E.Z.3    Distelhorst, C.W.4
  • 39
    • 0032571294 scopus 로고    scopus 로고
    • The overexpression of Bax produces cell death upon induction of the mitochondrial permeability transition
    • Pastorino JG, Chen S-T, Tafani M, Snyder JW, Farber JL. The overexpression of Bax produces cell death upon induction of the mitochondrial permeability transition. J Biol Chem 1998; 273: 7770-7775.
    • (1998) J Biol Chem , vol.273 , pp. 7770-7775
    • Pastorino, J.G.1    Chen, S.-T.2    Tafani, M.3    Snyder, J.W.4    Farber, J.L.5
  • 40
    • 9844226204 scopus 로고    scopus 로고
    • L on Bax-induced caspase activation and apoptosis
    • L on Bax-induced caspase activation and apoptosis. Oncogene 1997; 15: 1763-1772.
    • (1997) Oncogene , vol.15 , pp. 1763-1772
    • Kitanaka, C.1    Namiki, T.2    Noguchi, K.3
  • 41
    • 0022546957 scopus 로고
    • Analysis of the structure, transcripts, and protein products of bcl-2, the gene involved in human follicular lymphoma
    • Tsujimoto Y, Croce CM. Analysis of the structure, transcripts, and protein products of bcl-2, the gene involved in human follicular lymphoma. Proc Natl Acad Sci USA 1986; 83: 5214-5218.
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 5214-5218
    • Tsujimoto, Y.1    Croce, C.M.2
  • 42
    • 0023779204 scopus 로고
    • Alternative promoters and exons, somatic mutation and deregulation of the Bcl-2-Ig fusion gene in lymphoma
    • Seto M, Jaeger U, Hockett RD, et al. Alternative promoters and exons, somatic mutation and deregulation of the Bcl-2-Ig fusion gene in lymphoma. EMBO J 1988; 7: 123-131.
    • (1988) EMBO J , vol.7 , pp. 123-131
    • Seto, M.1    Jaeger, U.2    Hockett, R.D.3
  • 43
    • 0032484687 scopus 로고    scopus 로고
    • Bax and Bak proteins require caspase activity to trigger apoptosis in sympathetic neurons
    • Martinou I, Missotten M, Fernandez PA, Sadoul R, Martinou JC. Bax and Bak proteins require caspase activity to trigger apoptosis in sympathetic neurons. Neuroreport 1998; 9: 15-19.
    • (1998) Neuroreport , vol.9 , pp. 15-19
    • Martinou, I.1    Missotten, M.2    Fernandez, P.A.3    Sadoul, R.4    Martinou, J.C.5
  • 45
    • 0032555716 scopus 로고    scopus 로고
    • Bid, a Bcl-2 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. Bid, a Bcl-2 interacting protein, mediates cytochrome c release from mitochondria in response to activation of cell surface death receptors. Cell 1998; 94: 481-490.
    • (1998) Cell , vol.94 , pp. 481-490
    • Luo, X.1    Budihardjo, I.2    Zou, H.3    Slaughter, C.4    Wang, X.5
  • 47
    • 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 CJ, Yuan J. Cleavage of BID by caspase 8 mediates the mitochondrial damage in the Fas pathway of apoptosis. Cell 1998; 94: 491-501.
    • (1998) Cell , vol.94 , pp. 491-501
    • Li, H.1    Zhu, H.2    Xu, C.J.3    Yuan, J.4
  • 48
    • 0033534446 scopus 로고    scopus 로고
    • L prevents this release but not tumor necrosis factor-R1/Fas death
    • L prevents this release but not tumor necrosis factor-R1/Fas death. J Biol Chem 1999; 274: 1156-1163.
    • (1999) J Biol Chem , vol.274 , pp. 1156-1163
    • Gross, A.1    Yin, X.M.2    Wang, K.3
  • 49
    • 0033535350 scopus 로고    scopus 로고
    • Bid-induced conformational change of Bax is responsible for mitochondrial cytochrome c release during apoptosis
    • Desagher S, Osen-Sand A, Nichols A, et al. Bid-induced conformational change of Bax is responsible for mitochondrial cytochrome c release during apoptosis. J Cell Biol 1999; 144: 891-901.
    • (1999) J Cell Biol , vol.144 , pp. 891-901
    • Desagher, S.1    Osen-Sand, A.2    Nichols, A.3
  • 50
    • 0033981577 scopus 로고    scopus 로고
    • Bid induces the oligomerization and insertion of Bax into the outer mitochondrial membrane
    • Eskes R, Desagher S, Antonsson B, Martinou JC. Bid induces the oligomerization and insertion of Bax into the outer mitochondrial membrane. Mol Cell Biol 2000; 20: 929-935.
    • (2000) Mol Cell Biol , vol.20 , pp. 929-935
    • Eskes, R.1    Desagher, S.2    Antonsson, B.3    Martinou, J.C.4
  • 51
    • 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 SJ, Wei MC, Saito M, Weiler S, Oh KJ, Schlesinger PH. Pro-apoptotic cascade activates BID, which oligomerizes BAK or BAX into pores that result in the release of cytochrome c. Cell Death Differ 2000; 7: 1166-1673.
    • (2000) Cell Death Differ , vol.7 , pp. 1166-1673
    • Korsmeyer, S.J.1    Wei, M.C.2    Saito, M.3    Weiler, S.4    Oh, K.J.5    Schlesinger, P.H.6
  • 52
    • 0033694859 scopus 로고    scopus 로고
    • BID-dependent and BID-independent pathways for BAX insertion into mitochondria
    • Ruffolo SC, Breckenridge DG, Nguyen M, et al. BID-dependent and BID-independent pathways for BAX insertion into mitochondria. Cell Death Differ 2000; 7: 1101-1108.
    • (2000) Cell Death Differ , vol.7 , pp. 1101-1108
    • Ruffolo, S.C.1    Breckenridge, D.G.2    Nguyen, M.3
  • 53
    • 0034866507 scopus 로고    scopus 로고
    • Bax translocation to mitochondria subsequent to a rapid loss of mitochondrial membrane potential
    • Smaili SS, Hsu Y-T, Sanders KM, Russell JT, Youle RJ. Bax translocation to mitochondria subsequent to a rapid loss of mitochondrial membrane potential. Cell Death Differ 2001; 8: 909-920.
    • (2001) Cell Death Differ , vol.8 , pp. 909-920
    • Smaili, S.S.1    Hsu, Y.-T.2    Sanders, K.M.3    Russell, J.T.4    Youle, R.J.5
  • 54
    • 0030745646 scopus 로고    scopus 로고
    • Apaf-1, a human protein homologous to C. elegansf CED-4, participates in cytochrome c-dependent activation of caspase-3
    • Zou H, Henzel WJ, Liu X, Lutschg A, Wang X. Apaf-1, a human protein homologous to C. elegansf CED-4, participates in cytochrome c-dependent activation of caspase-3. Cell 1997; 90: 405-413.
    • (1997) Cell , vol.90 , pp. 405-413
    • Zou, H.1    Henzel, W.J.2    Liu, X.3    Lutschg, A.4    Wang, X.5
  • 55
    • 1842332735 scopus 로고    scopus 로고
    • L forms an ion channel in synthetic lipid membranes
    • L forms an ion channel in synthetic lipid membranes. Nature 1997; 385: 353-357.
    • (1997) Nature , vol.385 , pp. 353-357
    • Minn, A.J.1    Velez, P.2    Schendel, S.L.3
  • 57
    • 0031465443 scopus 로고    scopus 로고
    • Conversion of Bcl-2 to a Bax-like death effector by caspases
    • Cheng EH, Kirsch DG, Clem RJ, et al. Conversion of Bcl-2 to a Bax-like death effector by caspases. Science 1997; 278: 1966-1968.
    • (1997) Science , vol.278 , pp. 1966-1968
    • Cheng, E.H.1    Kirsch, D.G.2    Clem, R.J.3
  • 58
    • 0033545722 scopus 로고    scopus 로고
    • L, decreases the lifetime of planar phospholipid bilayer membranes at subnanomolar concentrations
    • L, decreases the lifetime of planar phospholipid bilayer membranes at subnanomolar concentrations. Proc Natl Acad Sci USA 1999; 96: 5492-5497.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 5492-5497
    • Basanez, G.1    Nechushtan, A.2    Drozhinin, O.3


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