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Volumn 144, Issue 2, 1999, Pages 281-292

Ordering the cytochrome c-initiated caspase cascade: Hierarchical activation of caspases-2,-3,-6,-7,-8, and -10 in a caspase-9-dependent manner

Author keywords

Apaf 1; Apoptosis; Caspases; Cell free; Cytochrome C

Indexed keywords

ADAPTOR PROTEIN; CASPASE; CASPASE 3; CYTOCHROME C; INTERLEUKIN 1BETA CONVERTING ENZYME;

EID: 0033601746     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.144.2.281     Document Type: Article
Times cited : (1723)

References (66)
  • 1
    • 0031045588 scopus 로고    scopus 로고
    • CRADD, a novel human apoptotic adaptor molecule for caspase-2, and FasL/tumor necrosis factor receptor-interacting protein RIP
    • Ahmad, M., S.M. Srinivasula, L. Wang, R.V. Talanian, G. Litwack, T. Fernandes-Alnemri, and E.S. Alnemri. 1997. CRADD, a novel human apoptotic adaptor molecule for caspase-2, and FasL/tumor necrosis factor receptor-interacting protein RIP. Cancer Res. 57:615-619.
    • (1997) Cancer Res. , vol.57 , pp. 615-619
    • Ahmad, M.1    Srinivasula, S.M.2    Wang, L.3    Talanian, R.V.4    Litwack, G.5    Fernandes-Alnemri, T.6    Alnemri, E.S.7
  • 2
    • 0031044652 scopus 로고    scopus 로고
    • Mammalian cell death proteases: A family of highly conserved aspartate specific cysteine proteases
    • Alnemri, E.S. 1997. Mammalian cell death proteases: a family of highly conserved aspartate specific cysteine proteases. J. Cell. Biochem. 64:33-42
    • (1997) J. Cell. Biochem. , vol.64 , pp. 33-42
    • Alnemri, E.S.1
  • 4
    • 0030011398 scopus 로고    scopus 로고
    • Involvement of MACH, a novel MORT1/FADD-interacting protease, in Fas/APO-1 and TNF receptor-induced cell death
    • Boldin, M.P., T.M. Goncharov, Y.V. Goltsev, and D. Wallach. 1996. Involvement of MACH, a novel MORT1/FADD-interacting protease, in Fas/APO-1 and TNF receptor-induced cell death. Cell. 85:803-815.
    • (1996) Cell , vol.85 , pp. 803-815
    • Boldin, M.P.1    Goncharov, T.M.2    Goltsev, Y.V.3    Wallach, D.4
  • 5
    • 0032472329 scopus 로고    scopus 로고
    • Mitochondrial cytochrome c release in apoptosis occurs upstream of DEVD-specific caspase activation and independently of mitochondrial transmembrane depolarization
    • Bossy-Wetzel, E., D.D. Newmeyer, and D.R. Green. 1998. Mitochondrial cytochrome c release in apoptosis occurs upstream of DEVD-specific caspase activation and independently of mitochondrial transmembrane depolarization. EMBO (Eur. Mol. Biol. Organ.) J. 17:37-49.
    • (1998) EMBO (Eur. Mol. Biol. Organ.) J. , vol.17 , pp. 37-49
    • Bossy-Wetzel, E.1    Newmeyer, D.D.2    Green, D.R.3
  • 6
    • 0028788309 scopus 로고
    • Microfilament reorganization during apoptosis: The role of Gas2, a possible substrate for ICE-like proteases
    • Brancolini, C., M. Bendetti, and C. Schneider. 1995. Microfilament reorganization during apoptosis: the role of Gas2, a possible substrate for ICE-like proteases. EMBO (Eur. Mol. Biol. Organ.) J. 14:5179-5190.
    • (1995) EMBO (Eur. Mol. Biol. Organ.) J. , vol.14 , pp. 5179-5190
    • Brancolini, C.1    Bendetti, M.2    Schneider, C.3
  • 7
    • 0027999537 scopus 로고
    • Specific cleavage of the 70-kD protein component of the U1 small nuclear ribonucleoprotein is a characteristic biochemical feature of apoptotic cell death
    • Casciola-Rosen, L.A., D.K. Miller, G.J. Anhalt, and A. Rosen. 1994. Specific cleavage of the 70-kD protein component of the U1 small nuclear ribonucleoprotein is a characteristic biochemical feature of apoptotic cell death. J. Biol. Chem. 269:30757-30760.
    • (1994) J. Biol. Chem. , vol.269 , pp. 30757-30760
    • Casciola-Rosen, L.A.1    Miller, D.K.2    Anhalt, G.J.3    Rosen, A.4
  • 8
    • 0028881847 scopus 로고
    • DNA-dependent protein kinase is one of a subset of autoantigens specifically cleaved early during apoptosis
    • Casciola-Rosen, L.A., G.J. Anhalt, and A. Rosen. 1995. DNA-dependent protein kinase is one of a subset of autoantigens specifically cleaved early during apoptosis. J. Exp. Med. 182:1625-1634.
    • (1995) J. Exp. Med. , vol.182 , pp. 1625-1634
    • Casciola-Rosen, L.A.1    Anhalt, G.J.2    Rosen, A.3
  • 9
    • 0029789073 scopus 로고    scopus 로고
    • Proteolysis of a subset of nuclear autoantigens during CD95 (Fas/APO-1 )-mediated T cell apoptosis
    • Casiano, C.A., S.J. Martin, D.R. Green, and E.M. Tan. 1996. Proteolysis of a subset of nuclear autoantigens during CD95 (Fas/APO-1 )-mediated T cell apoptosis. J. Exp. Med. 184:765-770.
    • (1996) J. Exp. Med. , vol.184 , pp. 765-770
    • Casiano, C.A.1    Martin, S.J.2    Green, D.R.3    Tan, E.M.4
  • 10
    • 0032544449 scopus 로고    scopus 로고
    • Apaf1 (CED-4 homolog) regulates programmed cell death in mammalian development
    • Cecconi, F., G. Alvarez-Bolado, B.I. Meyer, K.A. Roth, and P. Gruss. 1998. Apaf1 (CED-4 homolog) regulates programmed cell death in mammalian development. Cell. 94:727-737.
    • (1998) Cell , vol.94 , pp. 727-737
    • Cecconi, F.1    Alvarez-Bolado, G.2    Meyer, B.I.3    Roth, K.A.4    Gruss, P.5
  • 11
    • 0030134624 scopus 로고    scopus 로고
    • The cell-death machine
    • Chinnaiyan, A.M., and V.M. Dixit. 1996. The cell-death machine. Curr. Biol. 6:555-562.
    • (1996) Curr. Biol. , vol.6 , pp. 555-562
    • Chinnaiyan, A.M.1    Dixit, M.2
  • 12
    • 0029099845 scopus 로고
    • Activation of the apoptotic protease CPP32 by cytotoxic T-cell-derived granzyme B
    • Darmon, A.J., D.W. Nicholson, and R.C. Bleackley. 1995. Activation of the apoptotic protease CPP32 by cytotoxic T-cell-derived granzyme B. Nature. 377:446-448.
    • (1995) Nature , vol.377 , pp. 446-448
    • Darmon, A.J.1    Nicholson, D.W.2    Bleackley, R.C.3
  • 14
    • 0031021356 scopus 로고    scopus 로고
    • RAIDD is a new "death" adaptor molecule
    • Duan, H., and V.M. Dixit. 1997. RAIDD is a new "death" adaptor molecule. Nature. 385:86-89.
    • (1997) Nature , vol.385 , pp. 86-89
    • Duan, H.1    Dixit, V.M.2
  • 15
    • 0030044324 scopus 로고    scopus 로고
    • ICE-LAP3, a novel mammalian homologue of the Caenorhabditis elegans cell death protein Ced-3 is activated during Fas- and tumor necrosis factor-induced apoptosis
    • Duan, H., A.M. Chinnaiyan, P.L. Hudson, J.P. Wing, W.-W. He, and V.M. Dixit. 1996. ICE-LAP3, a novel mammalian homologue of the Caenorhabditis elegans cell death protein Ced-3 is activated during Fas- and tumor necrosis factor-induced apoptosis. J. Biol. Chem. 271:1621-1625.
    • (1996) J. Biol. Chem. , vol.271 , pp. 1621-1625
    • Duan, H.1    Chinnaiyan, A.M.2    Hudson, P.L.3    Wing, J.P.4    He, W.-W.5    Dixit, V.M.6
  • 21
    • 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
  • 22
    • 0030058584 scopus 로고    scopus 로고
    • Dynamic changes of NuMA during the cell cycle and possible appearance of a truncated form of NuMA during apoptosis
    • Hsu, H.-L., and N.-H. Yeh. 1996. Dynamic changes of NuMA during the cell cycle and possible appearance of a truncated form of NuMA during apoptosis. J. Cell Sci. 109:277-288.
    • (1996) J. Cell Sci. , vol.109 , pp. 277-288
    • Hsu, H.-L.1    Yeh, N.-H.2
  • 23
    • 0032515874 scopus 로고    scopus 로고
    • Bcl-XL interacts with Apaf-1 and inhibits Apaf-1-dependent caspase-9 activation
    • Hu, Y., M.A. Benedict, D. Wu, N. Inohara, and G. Nunez. 1998. Bcl-XL interacts with Apaf-1 and inhibits Apaf-1-dependent caspase-9 activation. Proc. Natl. Acad. Sci. USA. 95:4386-4391.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 4386-4391
    • Hu, Y.1    Benedict, M.A.2    Wu, D.3    Inohara, N.4    Nunez, G.5
  • 24
    • 0028406305 scopus 로고
    • Apoptosis. Breaking the ICE
    • Jacobson, M.D., and G.I. Evan. 1994. Apoptosis. Breaking the ICE. Curr. Biol. 4:337-340.
    • (1994) Curr. Biol. , vol.4 , pp. 337-340
    • Jacobson, M.D.1    Evan, G.I.2
  • 25
    • 0040298568 scopus 로고    scopus 로고
    • Caspase-3 is required for DNA fragmentation and morphological changes associated with apoptosis
    • Jänicke, R.U., M.L. Sprengart, M.R. Wati, and A.G. Porter. 1998. Caspase-3 is required for DNA fragmentation and morphological changes associated with apoptosis. J. Biol. Chem. 273:9357-9360.
    • (1998) J. Biol. Chem. , vol.273 , pp. 9357-9360
    • Jänicke, R.U.1    Sprengart, M.L.2    Wati, M.R.3    Porter, A.G.4
  • 29
    • 0031037897 scopus 로고    scopus 로고
    • The release of cytochrome c from mitochondria: A primary site for Bcl-2 regulation of apoptosis
    • Kluck, R.M., E. Bossy-Wetzel, D.R. Green, and D.D. Newmeyer. 1997a. The release of cytochrome c from mitochondria: a primary site for Bcl-2 regulation of apoptosis. Science. 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
  • 30
  • 34
    • 0027990778 scopus 로고
    • Induction of apoptosis by the mouse Nedd2 gene, which encodes a protein similar to the product of the Caenorhabditis elegans cell death gene ced-3 and the mammalian IL-1β converting enzyme
    • Kumar, S., M. Kinoshita, M. Noda, N.G. Copeland, and N.A. Jenkins, 1994. Induction of apoptosis by the mouse Nedd2 gene, which encodes a protein similar to the product of the Caenorhabditis elegans cell death gene ced-3 and the mammalian IL-1β converting enzyme. Genes Develop. 8:1613-1626.
    • (1994) Genes Develop. , vol.8 , pp. 1613-1626
    • Kumar, S.1    Kinoshita, M.2    Noda, M.3    Copeland, N.G.4    Jenkins, N.A.5
  • 35
    • 0032568954 scopus 로고    scopus 로고
    • Apoptosis induction by caspase-8 is amplified through the mitochondrial release of cytochrome c
    • Kuwana, T., J.J. Smith, M. Muzio, V. Dixit, D.D. Newmeyer, and S. Kornbluth. 1998. Apoptosis induction by caspase-8 is amplified through the mitochondrial release of cytochrome c. J. Biol. Chem. 273:16589-16594.
    • (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
  • 36
    • 0028102478 scopus 로고
    • Cleavage of poly(ADP-ribose) polymerase by a proteinase with properties like ICE
    • Lazebnik, Y.A., S.H. Kaufmann, S. Desnoyers, G.G. Poirier, and W.C. Earnshaw. 1994. Cleavage of poly(ADP-ribose) polymerase by a proteinase with properties like ICE. Nature. 371:346-347.
    • (1994) Nature , vol.371 , pp. 346-347
    • Lazebnik, Y.A.1    Kaufmann, S.H.2    Desnoyers, S.3    Poirier, G.G.4    Earnshaw, W.C.5
  • 37
    • 0032555697 scopus 로고    scopus 로고
    • Cleavage of BID by caspase 8 mediates the mitochondrial damage in the Fas pathway of apoptosis
    • Li, H., H. Zhu, C.J. Xu, and J. Yuan. 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
  • 38
    • 0030715323 scopus 로고    scopus 로고
    • Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade
    • Li, P., D. Nijhawan, I. Budihardjo, S.M. Srinivasula, M. Ahmad, E.S. Alnemri, and X. Wang. 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
  • 39
    • 0030581151 scopus 로고    scopus 로고
    • Induction of apoptotic program in cell-free extracts: Requirement for dATP and cytochrome c
    • Liu, X., C.N. Kim, J. Yang, R. Jemmerson, and X. Wang. 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
  • 40
    • 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., I. Budihardjo, H. Zou, C. Slaughter, and X. Wang. 1998. Bid, a Bcl2 interacting protein, mediates cytochrome c release from mitochondria in response to activation of cell surface death receptors. Cell. 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
  • 41
    • 0030890790 scopus 로고    scopus 로고
    • Processing/activation of at least four interleukin-1beta converting enzyme-like proteases occurs during the execution phase of apoptosis in human monocytic tumor cells
    • MacFarlane, M., K. Cain, X.M. Sun, E.S. Alnemri, and G.M. Cohen. 1997. Processing/activation of at least four interleukin-1beta converting enzyme-like proteases occurs during the execution phase of apoptosis in human monocytic tumor cells. J. Cell Biol. 137:469-479.
    • (1997) J. Cell Biol. , vol.137 , pp. 469-479
    • MacFarlane, M.1    Cain, K.2    Sun, X.M.3    Alnemri, E.S.4    Cohen, G.M.5
  • 42
    • 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
  • 48
    • 0032502855 scopus 로고    scopus 로고
    • Activation of caspases triggered by cytochrome c in vitro
    • Pan, G., E.W. Humke, and V.M. Dixit. 1998a. Activation of caspases triggered by cytochrome c in vitro. FEBS Lett. 426:151-154.
    • (1998) FEBS Lett. , vol.426 , pp. 151-154
    • Pan, G.1    Humke, E.W.2    Dixit, V.M.3
  • 49
    • 0032489390 scopus 로고    scopus 로고
    • Caspase-9, Bcl-XL, and Apaf-1 form a ternary complex
    • Pan, G., K. O'Rourke, and V.M. Dixit. 1998b. Caspase-9, Bcl-XL, and Apaf-1 form a ternary complex. J. Biol. Chem. 273:5841-5845.
    • (1998) J. Biol. Chem. , vol.273 , pp. 5841-5845
    • Pan, G.1    O'Rourke, K.2    Dixit, V.M.3
  • 50
    • 0030782177 scopus 로고    scopus 로고
    • Cytochrome c: Can't live with it - Can't live without it
    • Reed, J.C. 1997. Cytochrome c: can't live with it - can't live without it. Cell. 91: 559-562.
    • (1997) Cell , vol.91 , pp. 559-562
    • Reed, J.C.1
  • 51
    • 0030702084 scopus 로고    scopus 로고
    • Caspases: Intracellular signalling by proteolysis
    • Salvesen, G.S., and V.M. Dixit. 1997. Caspases: intracellular signalling by proteolysis. Cell. 91:443-446.
    • (1997) Cell , vol.91 , pp. 443-446
    • Salvesen, G.S.1    Dixit, V.M.2
  • 56
    • 0028990125 scopus 로고
    • YAMA/CPP32β, a mammalian homolog of Ced-3, is a CrmA-inhibitable protease that cleaves the death substrate poly(ADP-ribose) polymerase
    • Tewari, M., L.T. Quan, K. O'Rourke, S. Desnoyers, Z. Zeng, D.R. Beidler, G.G. Poirier, G.S. Salvesen, and V.M. Dixit. 1995. YAMA/CPP32β, 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
  • 60
    • 0028168593 scopus 로고
    • Ich-1, an Ice/ced-3-related gene, encodes both positive and negative regulators of programmed cell death
    • Wang, L., M. Miura, L. Bergeron, H. Zhu, and J. Yuan. 1994. Ich-1, an Ice/ced-3-related gene, encodes both positive and negative regulators of programmed cell death. Cell. 78:739-750.
    • (1994) Cell , vol.78 , pp. 739-750
    • Wang, L.1    Miura, M.2    Bergeron, L.3    Zhu, H.4    Yuan, J.5
  • 63
    • 0031615875 scopus 로고    scopus 로고
    • Autoproteolytic activation of pro-caspases by oligomerization
    • Yang, X., H.Y. Chang, and D. Baltimore. 1998. Autoproteolytic activation of pro-caspases by oligomerization. Mol. Cell. 1:319-325.
    • (1998) Mol. Cell , vol.1 , pp. 319-325
    • Yang, X.1    Chang, H.Y.2    Baltimore, D.3
  • 65
    • 0027525104 scopus 로고
    • The C. elegans cell death gene ced-3 encodes a protein similar to mammalian interleukin-1β-converting enzyme
    • Yuan, J., S. Shaham, S. Ledoux, H.M. Ellis, and H.R. Horvitz. 1993. The C. elegans cell death gene ced-3 encodes a protein similar to mammalian interleukin-1β-converting enzyme. Cell. 75:641-652.
    • (1993) Cell , vol.75 , pp. 641-652
    • Yuan, J.1    Shaham, S.2    Ledoux, S.3    Ellis, H.M.4    Horvitz, H.R.5
  • 66
    • 0030745646 scopus 로고    scopus 로고
    • Apaf-1 a human protein homologous to C. elegans CED-4 participates in cytochrome c-dependent activation of caspase-3
    • Zou, H., W.J. Henzel, X. Liu, A. Lutschg, and X. Wang. 1997. Apaf-1 a human protein homologous to C. elegans CED-4 participates in cytochrome c-dependent activation of caspase-3. Cell. 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


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