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Volumn 184, Issue 4, 1996, Pages 1331-1341

Bcl-2 inhibits the mitochondrial release of an apoptogenic protease

Author keywords

[No Author keywords available]

Indexed keywords

DNA FRAGMENT; INTERLEUKIN 1BETA CONVERTING ENZYME; REGULATOR PROTEIN;

EID: 0029950290     PISSN: 00221007     EISSN: None     Source Type: Journal    
DOI: 10.1084/jem.184.4.1331     Document Type: Article
Times cited : (1046)

References (45)
  • 1
    • 0028903933 scopus 로고
    • Reduction in mitochondrial potential constitutes an early irreversible step of programmed lymphocyte death in vivo
    • Zamzami, N., P. Marchetti, M. Castedo, C. Zanin, J.-L. Vayssière, P.X. Petit, and G. Kroemer. 1995. Reduction in mitochondrial potential constitutes an early irreversible step of programmed lymphocyte death in vivo. J. Exp. Med. 181: 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
  • 5
    • 0029944880 scopus 로고    scopus 로고
    • Sequential acquisition of mitochondrial and plasma membrane alterations during early lymphocyte apoptosis
    • Castedo, M., T. Hirsch, S.A. Susin, N. Zamzami, P. Marchetti, A. Macho, and G. Kroemer. 1996. Sequential acquisition of mitochondrial and plasma membrane alterations during early lymphocyte apoptosis. J. Immunol. 157:512-521.
    • (1996) J. Immunol. , vol.157 , pp. 512-521
    • Castedo, M.1    Hirsch, T.2    Susin, S.A.3    Zamzami, N.4    Marchetti, P.5    Macho, A.6    Kroemer, G.7
  • 7
    • 0030051609 scopus 로고    scopus 로고
    • Interactions of cyclophilin with mitochondrial inner membrane and regulation of the permeability transition pore, a cyclosporin A-sensitive channel
    • Nicolli, A., E. Basso, V. Petronilli, R.M. Wenger, and P. Bernardi. 1996. Interactions of cyclophilin with mitochondrial inner membrane and regulation of the permeability transition pore, a cyclosporin A-sensitive channel. J. Biol. Chem. 271:2185-2192.
    • (1996) J. Biol. Chem. , vol.271 , pp. 2185-2192
    • Nicolli, A.1    Basso, E.2    Petronilli, V.3    Wenger, R.M.4    Bernardi, P.5
  • 9
    • 0028149786 scopus 로고
    • Checkpoints of dueling dimers foil death wishes
    • Oltvai, Z.N., and S.J. Korsmeyer. 1994. Checkpoints of dueling dimers foil death wishes. Cell. 79:189-192.
    • (1994) Cell , vol.79 , pp. 189-192
    • Oltvai, Z.N.1    Korsmeyer, S.J.2
  • 10
    • 0029125701 scopus 로고
    • Protease activation during apoptosis: Death by a thousand cuts?
    • Martin, S.J., and D.R. Green. 1995. Protease activation during apoptosis: death by a thousand cuts? Cell. 82:349-352.
    • (1995) Cell , vol.82 , pp. 349-352
    • Martin, S.J.1    Green, D.R.2
  • 11
    • 0029664296 scopus 로고    scopus 로고
    • ICE family proteases: Mediators of all apoptotic cell death?
    • Henkart, P.A. 1996. ICE family proteases: mediators of all apoptotic cell death? Immunity. 4:195-201.
    • (1996) Immunity , vol.4 , pp. 195-201
    • Henkart, P.A.1
  • 12
    • 0029912189 scopus 로고    scopus 로고
    • Molecular ordering of the cell death pathway - Bcl-2 and Bcl-X(L) function upstream of the CED-3-like apoptotic proteases
    • Chinnaiyan, A.M., K. Orth, K. Orourke, H.J. Duan, G.G. Poirier, and V.M. Dixit. 1996. Molecular ordering of the cell death pathway - Bcl-2 and Bcl-X(L) function upstream of the CED-3-like apoptotic proteases. J. Biol. Chem. 271: 4573-4576.
    • (1996) J. Biol. Chem. , vol.271 , pp. 4573-4576
    • Chinnaiyan, A.M.1    Orth, K.2    Orourke, K.3    Duan, H.J.4    Poirier, G.G.5    Dixit, V.M.6
  • 13
    • 0027437541 scopus 로고
    • Nuclear events of apoptosis in vitro in cell-free mitotic extracts: A model system for analysis of the active phase of apoptosis
    • Lazebnik, Y.A., S. Cole, C.A. Cooke, W.G. Nelson, and W.C. Earnshaw. 1993. Nuclear events of apoptosis in vitro in cell-free mitotic extracts: a model system for analysis of the active phase of apoptosis. J. Cell. Biol. 123:7-22.
    • (1993) J. Cell. Biol. , vol.123 , pp. 7-22
    • Lazebnik, Y.A.1    Cole, S.2    Cooke, C.A.3    Nelson, W.G.4    Earnshaw, W.C.5
  • 15
    • 0028019746 scopus 로고
    • Cell-free apoptosis in xenopus egg extracts: Inhibition by Bcl-2 and requirement for an organelle fraction enriched in mitochondria
    • Newmeyer, D.D., D.M. Farschon, and J.C. Reed. 1994. Cell-free apoptosis in xenopus egg extracts: inhibition by Bcl-2 and requirement for an organelle fraction enriched in mitochondria. Cell. 79:353-364.
    • (1994) Cell , vol.79 , pp. 353-364
    • Newmeyer, D.D.1    Farschon, D.M.2    Reed, J.C.3
  • 17
    • 0028805524 scopus 로고
    • Apoptosis by a cytosolic extract from Fas-activated cells
    • Enari, M., A. Hase, and S. Nagata. 1995. Apoptosis by a cytosolic extract from Fas-activated cells. EMBO (Eur. Mol. Biol. Organ.) J. 14:5201-5208.
    • (1995) EMBO (Eur. Mol. Biol. Organ.) J. , vol.14 , pp. 5201-5208
    • Enari, M.1    Hase, A.2    Nagata, S.3
  • 19
    • 0020182282 scopus 로고
    • Mitochondrial modifications associated with the cytoplasmic male sterility in fava beans
    • Boutry, M., and M. Briquet. 1982. Mitochondrial modifications associated with the cytoplasmic male sterility in fava beans. Eur. J. Biochem. 127:129-135.
    • (1982) Eur. J. Biochem. , vol.127 , pp. 129-135
    • Boutry, M.1    Briquet, M.2
  • 21
    • 0020479616 scopus 로고
    • Demonstration of an ATP-dependent, vanadate-sensitive endoprotease in the matrix of rat liver mitochondria
    • Desautels, M., and A.L. Goldberg. 1982. Demonstration of an ATP-dependent, vanadate-sensitive endoprotease in the matrix of rat liver mitochondria. J. Biol. Chem. 257:11673-11679.
    • (1982) J. Biol. Chem. , vol.257 , pp. 11673-11679
    • Desautels, M.1    Goldberg, A.L.2
  • 22
    • 0027752461 scopus 로고
    • A mitochondrial protease with two catalytic subunits of nonoverlapping specificities
    • Nunnari, J., T.D. Fox, and P. Walter. 1993. A mitochondrial protease with two catalytic subunits of nonoverlapping specificities. Science (Wash. DC). 262:1997-2004.
    • (1993) Science (Wash. DC) , vol.262 , pp. 1997-2004
    • Nunnari, J.1    Fox, T.D.2    Walter, P.3
  • 23
    • 0025666621 scopus 로고
    • Mitotic chromatin condensation in vitro using somatic cell extracts and nuclei with variable levels of endogenous topoisomerase II
    • Wood, E.R., and W.C. Earnshaw. 1990. Mitotic chromatin condensation in vitro using somatic cell extracts and nuclei with variable levels of endogenous topoisomerase II. J. Cell Biol. 111:2839-2850.
    • (1990) J. Cell Biol. , vol.111 , pp. 2839-2850
    • Wood, E.R.1    Earnshaw, W.C.2
  • 24
    • 0027989510 scopus 로고
    • Chromatin condensation during apoptosis is accompanied by degradation of lamin A+B, without enhanced activation of cdc-2 kinase
    • Oberhammer, F.A., K. Hochegger, and G. Froschl. 1994. Chromatin condensation during apoptosis is accompanied by degradation of lamin A+B, without enhanced activation of cdc-2 kinase. J. Cell Biol. 126:827-837.
    • (1994) J. Cell Biol. , vol.126 , pp. 827-837
    • Oberhammer, F.A.1    Hochegger, K.2    Froschl, G.3
  • 27
    • 0030060075 scopus 로고    scopus 로고
    • Requirement of an ICE-like protease for induction of apoptosis and ceramide generation by REAPER
    • Pronk, G.J., K. Ramer, P. Amiri, and L.T. Williams. 1996. Requirement of an ICE-like protease for induction of apoptosis and ceramide generation by REAPER. Science (Wash. DC). 271:808-810.
    • (1996) Science (Wash. DC) , vol.271 , pp. 808-810
    • Pronk, G.J.1    Ramer, K.2    Amiri, P.3    Williams, L.T.4
  • 28
    • 0029670683 scopus 로고    scopus 로고
    • A cleavage-site-directed inhibitor of interleukin 1 beta-converting enzyme-like proteases inhibits apoptosis in primary cultures of rat hepatocytes
    • Cain, K., S.H. Inayathussain, C. Couet, and G.M. Cohen. 1996. A cleavage-site-directed inhibitor of interleukin 1 beta-converting enzyme-like proteases inhibits apoptosis in primary cultures of rat hepatocytes. Biochem. J. 314:27-32.
    • (1996) Biochem. J. , vol.314 , pp. 27-32
    • Cain, K.1    Inayathussain, S.H.2    Couet, C.3    Cohen, G.M.4
  • 29
    • 0028816881 scopus 로고
    • Endonuclease G from mammalian nuclei is identical to the major endonuclease of mitochondria
    • Gerschenson, G., K.L. Houmiel, and R.L. Low. 1995. Endonuclease G from mammalian nuclei is identical to the major endonuclease of mitochondria. Nucleic Acids Res. 23:88-97.
    • (1995) Nucleic Acids Res. , vol.23 , pp. 88-97
    • Gerschenson, G.1    Houmiel, K.L.2    Low, R.L.3
  • 31
    • 0028040019 scopus 로고
    • Bcl-2 and the regulation of programmed cell death
    • Reed, J.C. 1995. Bcl-2 and the regulation of programmed cell death. J. Cell Biol. 124:1-6.
    • (1995) J. Cell Biol. , vol.124 , pp. 1-6
    • Reed, J.C.1
  • 32
    • 0028915454 scopus 로고
    • Regulation of lymphocyte survival by the Bcl-2 gene family
    • Cory, S. 1995. Regulation of lymphocyte survival by the Bcl-2 gene family. Annu. Rev. Immunol. 13:513-543.
    • (1995) Annu. Rev. Immunol. , vol.13 , pp. 513-543
    • Cory, S.1
  • 33
    • 0027362667 scopus 로고
    • Investigation of the subcellular distribution of the bcl-2 oncoprotein: Residence in the nuclear envelope, endoplasmic reticulum, and outer mitochondrial membranes
    • Krajewski, S., S. Tanaka, S. Takayama, M.J. Schibler, W. Fenton, and J.C. Reed. 1993. Investigation of the subcellular distribution of the bcl-2 oncoprotein: residence in the nuclear envelope, endoplasmic reticulum, and outer mitochondrial membranes. Cancer Res. 53:4701-4714.
    • (1993) Cancer Res. , vol.53 , pp. 4701-4714
    • Krajewski, S.1    Tanaka, S.2    Takayama, S.3    Schibler, M.J.4    Fenton, W.5    Reed, J.C.6
  • 34
    • 0028793279 scopus 로고
    • Localization of the Bcl-2 protein to the outer mitochondrial membrane by electron microscopy
    • Riparbelli, M.G., G. Callaini, S.A. Tripodi, M. Cintorino, P. Tosi, and R. Dallai. 1995. Localization of the Bcl-2 protein to the outer mitochondrial membrane by electron microscopy. Exp. Cell Res. 221:363-369.
    • (1995) Exp. Cell Res. , vol.221 , pp. 363-369
    • Riparbelli, M.G.1    Callaini, G.2    Tripodi, S.A.3    Cintorino, M.4    Tosi, P.5    Dallai, R.6
  • 35
    • 0029978182 scopus 로고    scopus 로고
    • Sequential activation of ICE-like and CPP32-like proteases during Fas-mediated apoptosis
    • Enari, M., R.V. Talanian, W.W. Wong, and S. Nagata. 1996. Sequential activation of ICE-like and CPP32-like proteases during Fas-mediated apoptosis. Nature (Lond.). 380: 723-726.
    • (1996) Nature (Lond.) , vol.380 , pp. 723-726
    • Enari, M.1    Talanian, R.V.2    Wong, W.W.3    Nagata, S.4
  • 36
    • 0028922462 scopus 로고
    • Mice lacking ADPRT and poly(ADP-ribosyl)ation develop normally but are susceptible to skin disease
    • Wang, Z.-Q., B. Auer, L. Stingl, H. Berghammer, D. Haidacher, M. Schweiger, and E.F. Wagner. 1995. Mice lacking ADPRT and poly(ADP-ribosyl)ation develop normally but are susceptible to skin disease. Genes Dev. 9:509-520.
    • (1995) Genes Dev. , vol.9 , pp. 509-520
    • Wang, Z.-Q.1    Auer, B.2    Stingl, L.3    Berghammer, H.4    Haidacher, D.5    Schweiger, M.6    Wagner, E.F.7
  • 37
    • 0027255417 scopus 로고
    • Specific proteolytic cleavage of poly(ADP)ribose polymerase: An early marker of chemotherapy induced apoptosis
    • Kaufman, S.H., S. Desnoyers, Y. Ottaviano, N.E. Davidson. and G.G. Poirer. 1993. Specific proteolytic cleavage of poly(ADP)ribose polymerase: an early marker of chemotherapy induced apoptosis. Cancer Res. 53:3976-3980.
    • (1993) Cancer Res. , vol.53 , pp. 3976-3980
    • Kaufman, S.H.1    Desnoyers, S.2    Ottaviano, Y.3    Davidson, N.E.4    Poirer, G.G.5
  • 38
    • 0025204548 scopus 로고
    • Bcl-2 is an inner mitochondrial membrane protein that blocks programmed cell death
    • Hockenbery, D., G. Nuñez, C. Milliman, R.D. Schreiber, and S.J. Korsmeyer. 1990. Bcl-2 is an inner mitochondrial membrane protein that blocks programmed cell death. Nature (Lond.). 348:334-338.
    • (1990) Nature (Lond.) , vol.348 , pp. 334-338
    • Hockenbery, D.1    Nuñez, G.2    Milliman, C.3    Schreiber, R.D.4    Korsmeyer, S.J.5
  • 39
    • 0029915241 scopus 로고    scopus 로고
    • Involvement of peripheral benzodiazepine receptors in the protection of hematopoietic cells against oxygen radical species
    • Carayon, P., M. Portier, D. Dussossoy, A. Bord, G. Petitpretre, X. Canat, G. Le Fur, and P. Casellas. 1996. Involvement of peripheral benzodiazepine receptors in the protection of hematopoietic cells against oxygen radical species. Blood. 87: 3170-3178.
    • (1996) Blood , vol.87 , pp. 3170-3178
    • Carayon, P.1    Portier, M.2    Dussossoy, D.3    Bord, A.4    Petitpretre, G.5    Canat, X.6    Le Fur, G.7    Casellas, P.8
  • 40
    • 0027225445 scopus 로고
    • Structure-function analysis of the Bcl-2 oncoprotein. Addition of a heterologous transmembrane domain to portions of the Bcl-2β protein restores function as a regulator of cell survival
    • Tanaka, S., K. Saito, and J.C. Reed. 1993. Structure-function analysis of the Bcl-2 oncoprotein. Addition of a heterologous transmembrane domain to portions of the Bcl-2β protein restores function as a regulator of cell survival. J. Biol. Chem. 268:10920-10926.
    • (1993) J. Biol. Chem. , vol.268 , pp. 10920-10926
    • Tanaka, S.1    Saito, K.2    Reed, J.C.3
  • 41
    • 0028289951 scopus 로고
    • Role of membrane anchor domain of Bcl-2 in suppression of apoptosis caused by E1B-defective adenovirus
    • Nguyen, M., P.E. Branton, P.A. Walton, Z.N. Oltvai, S.J. Korsmeyer, and G.C. Shore. 1994. Role of membrane anchor domain of Bcl-2 in suppression of apoptosis caused by E1B-defective adenovirus. J. Biol. Chem. 269:16521-16524.
    • (1994) J. Biol. Chem. , vol.269 , pp. 16521-16524
    • Nguyen, M.1    Branton, P.E.2    Walton, P.A.3    Oltvai, Z.N.4    Korsmeyer, S.J.5    Shore, G.C.6
  • 42
    • 0029032660 scopus 로고
    • Structure-function analysis of Bcl-2 protein identification of conserved domains important for homodimerization with Bcl-2 and heterodimerization with Bax
    • Hanada, M., C. Aimesempe, T. Sato, and J.C. Reed. 1995. Structure-function analysis of Bcl-2 protein identification of conserved domains important for homodimerization with Bcl-2 and heterodimerization with Bax. J. Biol. Chem. 270: 11962-11969.
    • (1995) J. Biol. Chem. , vol.270 , pp. 11962-11969
    • Hanada, M.1    Aimesempe, C.2    Sato, T.3    Reed, J.C.4
  • 43
    • 0030052107 scopus 로고    scopus 로고
    • Role of mitochondria and C-terminal membrane anchor of Bcl-2 in Bax induced growth arrest and mortality in Sacharomyces cerevisiae
    • Greenhalf, W., C. Stephan, and B. Chaudhuri. 1996. Role of mitochondria and C-terminal membrane anchor of Bcl-2 in Bax induced growth arrest and mortality in Sacharomyces cerevisiae. FEBS Lett. 380:169-175.
    • (1996) FEBS Lett. , vol.380 , pp. 169-175
    • Greenhalf, W.1    Stephan, C.2    Chaudhuri, B.3
  • 44
    • 0028268215 scopus 로고
    • Programmed cell death and Bcl-2 protection in the absence of a nucleus
    • Jacobson, M.D., J.F. Burne, and M.C. Raff. 1994. Programmed cell death and Bcl-2 protection in the absence of a nucleus. EMBO (Eur. Mol. Biol. Organ.) J. 13:1899-1910.
    • (1994) EMBO (Eur. Mol. Biol. Organ.) J. , vol.13 , pp. 1899-1910
    • Jacobson, M.D.1    Burne, J.F.2    Raff, M.C.3
  • 45
    • 0028939139 scopus 로고
    • Programmed cell death and Bcl-2 protection in very low oxygen
    • Jacobson, M.D., and M.C. Raff. 1995. Programmed cell death and Bcl-2 protection in very low oxygen. Nature (Lond.). 374:814-816.
    • (1995) Nature (Lond.) , vol.374 , pp. 814-816
    • Jacobson, M.D.1    Raff, M.C.2


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