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Volumn 77, Issue 1, 1999, Pages 58-63

Targeted disruption of caspase genes in mice: What they tell us about the functions of individual caspases in apoptosis

Author keywords

Apaf 1; Apoptosis; Caspases; Cytochrome c; Death receptors; Development; Gene knockout mice; Mitochondria; Programmed cell death

Indexed keywords

CASPASE; CYSTEINE PROTEINASE; CYTOCHROME C;

EID: 0033026172     PISSN: 08189641     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1440-1711.1999.00788.x     Document Type: Review
Times cited : (46)

References (46)
  • 1
    • 0015383455 scopus 로고
    • Apoptosis: A basic biological phenomenon with wide-ranging implications in tissue kinetics
    • 1 Kerr JFR, Wyllie AH, Currie AR. Apoptosis: A basic biological phenomenon with wide-ranging implications in tissue kinetics. Br. J. Cancer 1972; 26: 239-57.
    • (1972) Br. J. Cancer , vol.26 , pp. 239-257
    • Kerr, J.F.R.1    Wyllie, A.H.2    Currie, A.R.3
  • 3
    • 0029069295 scopus 로고
    • ICE-like proteases in apoptosis
    • 3 Kumar S. ICE-like proteases in apoptosis. Trends Biochem. Sci. 1995; 20: 198-202.
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 198-202
    • Kumar, S.1
  • 4
    • 0029794385 scopus 로고    scopus 로고
    • The ICE family of cysteine proteases as effectors of cell death
    • 4 Kumar S, Lavin MF. The ICE family of cysteine proteases as effectors of cell death. Cell Death Diff. 1996; 3: 255-67.
    • (1996) Cell Death Diff. , vol.3 , pp. 255-267
    • Kumar, S.1    Lavin, M.F.2
  • 6
    • 2642689658 scopus 로고    scopus 로고
    • Proteases to die for
    • 6 Cryns V, Yuan J. Proteases to die for. Genes Dev. 1998; 12: 1551-70.
    • (1998) Genes Dev. , vol.12 , pp. 1551-1570
    • Cryns, V.1    Yuan, J.2
  • 7
    • 0032544268 scopus 로고    scopus 로고
    • Apoptotic pathways: The roads to ruin
    • 7 Green DR. Apoptotic pathways: The roads to ruin. Cell 1998, 94: 695-8.
    • (1998) Cell , vol.94 , pp. 695-698
    • Green, D.R.1
  • 8
    • 0026507126 scopus 로고
    • A novel heterodimeric cysteine protease is required for interleukin-1β processing in monocytes
    • 8 Thornberry NA, Bull HG, Calaycay JR et al. A novel heterodimeric cysteine protease is required for interleukin-1β processing in monocytes. Nature 1992; 356: 768-74.
    • (1992) Nature , vol.356 , pp. 768-774
    • Thornberry, N.A.1    Bull, H.G.2    Calaycay, J.R.3
  • 9
    • 0032544397 scopus 로고    scopus 로고
    • Prodomain-dependent nuclear localization of the caspase-2 (Nedd2) precursor: A novel function for a caspase prodomain
    • 9 Colussi PA, Harvey NL, Kumar S. Prodomain-dependent nuclear localization of the caspase-2 (Nedd2) precursor: A novel function for a caspase prodomain. J. Biol. Chem. 1998; 273: 24 535-42.
    • (1998) J. Biol. Chem. , vol.273 , pp. 24535-24542
    • Colussi, P.A.1    Harvey, N.L.2    Kumar, S.3
  • 10
    • 0030892234 scopus 로고    scopus 로고
    • Apoptosis by death factor
    • 10 Nagata S. Apoptosis by death factor. Cell 1997; 88: 355-65.
    • (1997) Cell , vol.88 , pp. 355-365
    • Nagata, S.1
  • 11
    • 0032575714 scopus 로고    scopus 로고
    • Death receptors: Signalling and modulation
    • 11 Ashkenazi A, Dixit VM. Death receptors: Signalling and modulation. Science 1998; 281: 1305-8.
    • (1998) Science , vol.281 , pp. 1305-1308
    • Ashkenazi, A.1    Dixit, V.M.2
  • 12
    • 0032563323 scopus 로고    scopus 로고
    • Solution structure of the RAIDD CARD and model for CARD/CARD interaction in caspase-2 and caspase-9 recruitment
    • 12 Chou JJ, Matsuo H, Duan H, Wagner G. Solution structure of the RAIDD CARD and model for CARD/CARD interaction in caspase-2 and caspase-9 recruitment. Cell 1998; 94: 171-80.
    • (1998) Cell , vol.94 , pp. 171-180
    • Chou, J.J.1    Matsuo, H.2    Duan, H.3    Wagner, G.4
  • 13
    • 0032549652 scopus 로고    scopus 로고
    • Dimerisation and autoprocessing of the Nedd2 (caspase-2) precursor requires both the prodomain and the carboxyl terminal regions
    • 13 Butt AJ, Harvey NL, Parasivam G, Kumar S. Dimerisation and autoprocessing of the Nedd2 (caspase-2) precursor requires both the prodomain and the carboxyl terminal regions. J. Biol. Chem. 1998; 273: 6763-8.
    • (1998) J. Biol. Chem. , vol.273 , pp. 6763-6768
    • Butt, A.J.1    Harvey, N.L.2    Parasivam, G.3    Kumar, S.4
  • 14
    • 0032500552 scopus 로고    scopus 로고
    • Conversion of procaspase-3 to an autoactivating caspase by fusion to the caspase-2 prodomain
    • 14 Colussi PA, Harvey NL, Shearwin-Whyatt LM, Kumar S. Conversion of procaspase-3 to an autoactivating caspase by fusion to the caspase-2 prodomain. J. Biol. Chem. 1998; 273: 26 566-70.
    • (1998) J. Biol. Chem. , vol.273 , pp. 26566-26570
    • Colussi, P.A.1    Harvey, N.L.2    Shearwin-Whyatt, L.M.3    Kumar, S.4
  • 15
    • 0029905073 scopus 로고    scopus 로고
    • Molecular ordering of the Fas-apoptotic pathway: The Fas/APO-I protease Mch5 is a CrmA-inhibitable protease that activates multiple Ced-3/ICE-like cysteine proteases
    • 15 Srinivasula SM, Ahmed M, Fernandes-Alnemri T, Liwack G, Alnemri ES. Molecular ordering of the Fas-apoptotic pathway: The Fas/APO-I protease Mch5 is a CrmA-inhibitable protease that activates multiple Ced-3/ICE-like cysteine proteases. Proc. Natl Acad. Sci. USA 1996; 93: 14 486-91.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 14486-14491
    • Srinivasula, S.M.1    Ahmed, M.2    Fernandes-Alnemri, T.3    Liwack, G.4    Alnemri, E.S.5
  • 16
    • 15144345497 scopus 로고    scopus 로고
    • Pro-caspase-3 is a major physiologic target of caspase-8
    • 16 Stennicke HR, Jurgensmeier JM, Shin H et al. Pro-caspase-3 is a major physiologic target of caspase-8. J. Biol. Chem. 1998; 273: 27 084-90.
    • (1998) J. Biol. Chem. , vol.273 , pp. 27084-27090
    • Stennicke, H.R.1    Jurgensmeier, J.M.2    Shin, H.3
  • 17
    • 0030715323 scopus 로고    scopus 로고
    • Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates the apoptotic protease cascade
    • 17 Li P, Nijhawan D, Budihardjo I et al. Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates the apoptotic protease cascade. Cell 1997; 91: 479-89.
    • (1997) Cell , vol.91 , pp. 479-489
    • Li, P.1    Nijhawan, D.2    Budihardjo, I.3
  • 18
    • 0032515874 scopus 로고    scopus 로고
    • Bcl-XL interacts with Apaf-1 and inhibits Apaf-1-dependent caspase-9 activation
    • 18 Hu Y, Benedict MA, Wu D, Inohara N, Nunez G. Bcl-XL interacts with Apaf-1 and inhibits Apaf-1-dependent caspase-9 activation. Proc. Natl Acad. Sci. USA 1998; 95: 4386-91.
    • (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
  • 19
    • 0032489390 scopus 로고    scopus 로고
    • Caspase-9, Bcl-XL, and Apaf-1 form a ternary complex
    • 19 Pan G, O'Rourke K, Dixit VM. Caspase-9, Bcl-XL, and Apaf-1 form a ternary complex. J. Biol. Chem. 1998; 273: 5841-5.
    • (1998) J. Biol. Chem. , vol.273 , pp. 5841-5845
    • Pan, G.1    O'Rourke, K.2    Dixit, V.M.3
  • 21
    • 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
    • 21 Zou H, Henzel WJ, Liu X, Lutschg A, Wang X. Apaf-1, a human protein homologous to C. elegans CED-4, participates in cytochrome c-dependent activation of caspase-3. Cell 1997; 90: 405-13.
    • (1997) Cell , vol.90 , pp. 405-413
    • Zou, H.1    Henzel, W.J.2    Liu, X.3    Lutschg, A.4    Wang, X.5
  • 22
    • 0032555697 scopus 로고    scopus 로고
    • Cleavage of BID by caspase-8 mediates the mitochondrial damage in the Fas pathway of apoptosis
    • 22 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
  • 23
    • 0032555716 scopus 로고    scopus 로고
    • Bcl2 interacting protein, mediates cytochrome c release from mitochondria in response to activation of cell surface death receptors
    • 23 Luo X, Budihardjo I, Zou H, Slaughter C, Wang X. Bcl2 interacting protein, mediates cytochrome c release from mitochondria in response to activation of cell surface death receptors. Cell 1998; 94: 481-90.
    • (1998) Cell , vol.94 , pp. 481-490
    • Luo, X.1    Budihardjo, I.2    Zou, H.3    Slaughter, C.4    Wang, X.5
  • 24
    • 0026517239 scopus 로고
    • Molecular cloning of the interleukin-1β converting enzyme
    • 24 Cerretti DP, Kozlosky CJ, Mosley B et al. Molecular cloning of the interleukin-1β converting enzyme. Science 1992; 256: 97-100.
    • (1992) Science , vol.256 , pp. 97-100
    • Cerretti, D.P.1    Kozlosky, C.J.2    Mosley, B.3
  • 25
    • 0027525104 scopus 로고
    • The C. Elegans cell death gene ced-3 encodes a protein similar to mammalian interleukin-1β-converting enzyme
    • 25 Yuan J, Shaham S, Ledoux S, Ellis H, Horvitz HR. The C. elegans cell death gene ced-3 encodes a protein similar to mammalian interleukin-1β-converting enzyme. Cell 1993; 75: 641-52.
    • (1993) Cell , vol.75 , pp. 641-652
    • Yuan, J.1    Shaham, S.2    Ledoux, S.3    Ellis, H.4    Horvitz, H.R.5
  • 26
    • 0027449187 scopus 로고
    • Induction of apoptosis in fibroblasts by IL-1b-converting enzyme, a mammalian homologue of the C. Elegans cell death gene ced-3
    • 26 Miura M, Zhu H, Rotello R, Hartwieg EA, Yuan J. Induction of apoptosis in fibroblasts by IL-1b-converting enzyme, a mammalian homologue of the C. elegans cell death gene ced-3. Cell 1993; 75: 653-60.
    • (1993) Cell , vol.75 , pp. 653-660
    • Miura, M.1    Zhu, H.2    Rotello, R.3    Hartwieg, E.A.4    Yuan, J.5
  • 27
    • 0028920863 scopus 로고
    • Altered cytokine export and apoptosis in mice deficient in interleukin-1beta converting enzyme
    • 27 Kuida K, Lippke JA, Ku G et al. Altered cytokine export and apoptosis in mice deficient in interleukin-1beta converting enzyme. Science 1995; 267: 2000-3.
    • (1995) Science , vol.267 , pp. 2000-2003
    • Kuida, K.1    Lippke, J.A.2    Ku, G.3
  • 28
    • 0028984948 scopus 로고
    • Mice deficient in IL-1β-converting enzyme are defective in production of mature IL-1β and resistant to endotoxin shock
    • 28 Li P, Allen H, Banerjee S et al. Mice deficient in IL-1β-converting enzyme are defective in production of mature IL-1β and resistant to endotoxin shock. Cell 1995; 80: 401-11.
    • (1995) Cell , vol.80 , pp. 401-411
    • Li, P.1    Allen, H.2    Banerjee, S.3
  • 29
    • 0032548919 scopus 로고    scopus 로고
    • Murine caspase-11, an ICE-interacting protease, is essential for the activation of ICE
    • 29 Wang S, Miura M, Bergeron L, Zhu H, Yuan J. Murine caspase-11, an ICE-interacting protease, is essential for the activation of ICE. Cell 1998; 92: 501-9.
    • (1998) Cell , vol.92 , pp. 501-509
    • Wang, S.1    Miura, M.2    Bergeron, L.3    Zhu, H.4    Yuan, J.5
  • 30
    • 0029808205 scopus 로고    scopus 로고
    • Identification and characterization of Ich-3, a member of the interleukin-1beta converting enzyme (ICE)/Ced-3 family and an upstream regulator of ICE
    • 30 Wang S, Miura M, Jung Y et al. Identification and characterization of Ich-3, a member of the interleukin-1beta converting enzyme (ICE)/Ced-3 family and an upstream regulator of ICE. J. Biol. Chem. 1996; 271: 20 580-7.
    • (1996) J. Biol. Chem. , vol.271 , pp. 20580-20587
    • Wang, S.1    Miura, M.2    Jung, Y.3
  • 31
    • 0000610642 scopus 로고    scopus 로고
    • Cell death
    • Riddle DL, Blumanthal T, Meyer BJ, Priess JR (eds) Plainview NY: Cold Spring Harbor Laboratory Press
    • 31 Hengartner MO. Cell death. In: Riddle DL, Blumanthal T, Meyer BJ, Priess JR (eds) C. elegans II. Plainview NY: Cold Spring Harbor Laboratory Press, 1997; 383-415.
    • (1997) C. Elegans , vol.2 , pp. 383-415
    • Hengartner, M.O.1
  • 32
    • 0031034997 scopus 로고    scopus 로고
    • Interaction of CED-4 with CED-3 and CED-9: A molecular framework for cell death
    • 32 Chinnaiyan AM, O'Rourke K, Lane BR, Dixit VM. Interaction of CED-4 with CED-3 and CED-9: A molecular framework for cell death. Science 1997; 275: 1122-6.
    • (1997) Science , vol.275 , pp. 1122-1126
    • Chinnaiyan, A.M.1    O'Rourke, K.2    Lane, B.R.3    Dixit, V.M.4
  • 33
    • 0031037897 scopus 로고    scopus 로고
    • The release of cytochrome c from mitochondria: A primary site for Bcl-2 regulation of apoptosis
    • 33 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: 1132-6.
    • (1997) Science , vol.275 , pp. 1132-1136
    • Kluck, R.M.1    Bossy-Wetzel, E.2    Green, D.R.3    Newmeyer, D.D.4
  • 34
    • 0029956641 scopus 로고    scopus 로고
    • Decreased apoptosis in the brain and premature lethality in CPP32-deficient mice
    • 34 Kuida K, Zheng TS, Na S et al. Decreased apoptosis in the brain and premature lethality in CPP32-deficient mice. Nature 1996; 384: 368-72.
    • (1996) Nature , vol.384 , pp. 368-372
    • Kuida, K.1    Zheng, T.S.2    Na, S.3
  • 35
    • 15644364847 scopus 로고    scopus 로고
    • Essential contribution of caspase 3/CPP32 to apoptosis and its associated nuclear changes
    • 35 Woo M, Hakem R, Soengas MS et al. Essential contribution of caspase 3/CPP32 to apoptosis and its associated nuclear changes. Genes Dev. 1998; 12: 806-19.
    • (1998) Genes Dev. , vol.12 , pp. 806-819
    • Woo, M.1    Hakem, R.2    Soengas, M.S.3
  • 36
    • 0032493910 scopus 로고    scopus 로고
    • Reduced apoptosis and cytochrome c-mediated caspase activation in mice lacking caspase 9
    • 36 Kuida K, Haydar TF, Kuan CY et al. Reduced apoptosis and cytochrome c-mediated caspase activation in mice lacking caspase 9. Cell 1998; 94: 325-37.
    • (1998) Cell , vol.94 , pp. 325-337
    • Kuida, K.1    Haydar, T.F.2    Kuan, C.Y.3
  • 37
    • 0032493870 scopus 로고    scopus 로고
    • Differential requirement for caspase-9 in apoptotic pathways in vivo
    • 37 Hakem R, Hakem A, Duncan GS et al. Differential requirement for caspase-9 in apoptotic pathways in vivo. Cell 1998; 94: 339-52.
    • (1998) Cell , vol.94 , pp. 339-352
    • Hakem, R.1    Hakem, A.2    Duncan, G.S.3
  • 38
    • 0032544564 scopus 로고    scopus 로고
    • Apaf1 is required for mitochondrial pathways of apoptosis and brain development
    • 38 Yoshida H, Kong YY, Yoshida R et al. Apaf1 is required for mitochondrial pathways of apoptosis and brain development. Cell 1998; 94: 739-50.
    • (1998) Cell , vol.94 , pp. 739-750
    • Yoshida, H.1    Kong, Y.Y.2    Yoshida, R.3
  • 39
    • 0032544449 scopus 로고    scopus 로고
    • Apaf1 (CED-4 homolog) regulates programmed cell death in mammalian development
    • 39 Cecconi F, Alvarez-Bolado G, Meyer BI, Roth KA, Gruss P. Apaf1 (CED-4 homolog) regulates programmed cell death in mammalian development. Cell 1998; 94: 727-37.
    • (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
  • 40
    • 0031021356 scopus 로고    scopus 로고
    • RAIDD is a new 'death' adaptor molecule
    • 40 Duan H, Dixit VM. RAIDD is a new 'death' adaptor molecule. Nature 1997; 385: 86-90.
    • (1997) Nature , vol.385 , pp. 86-90
    • Duan, H.1    Dixit, V.M.2
  • 41
    • 0032143986 scopus 로고    scopus 로고
    • Targeted disruption of the mouse Caspase 8 gene ablates cell death induction by the TNF receptors, Fas/Apo1, and DR3 and is lethal prenatally
    • 41 Varfolomeev EE, Schuchmann M, Luria V et al. Targeted disruption of the mouse Caspase 8 gene ablates cell death induction by the TNF receptors, Fas/Apo1, and DR3 and is lethal prenatally. Immunity 1998; 9: 267-76.
    • (1998) Immunity , vol.9 , pp. 267-276
    • Varfolomeev, E.E.1    Schuchmann, M.2    Luria, V.3
  • 42
    • 7144263731 scopus 로고    scopus 로고
    • FADD: Essential for embryo development and signaling from some, but not all, inducers of apoptosis
    • 42 Yeh WC, Pompa JL, McCurrach ME et al. FADD: Essential for embryo development and signaling from some, but not all, inducers of apoptosis. Science 1998; 279: 1954-8.
    • (1998) Science , vol.279 , pp. 1954-1958
    • Yeh, W.C.1    Pompa, J.L.2    McCurrach, M.E.3
  • 43
    • 0032546387 scopus 로고    scopus 로고
    • Fas-mediated apoptosis and activation-induced T-cell proliferation are defective in mice lacking FADD/Mort1
    • 43 Zhang J, Cado D, Chen A, Kabra NH, Winoto A. Fas-mediated apoptosis and activation-induced T-cell proliferation are defective in mice lacking FADD/Mort1. Nature 1998; 392: 296-9.
    • (1998) Nature , vol.392 , pp. 296-299
    • Zhang, J.1    Cado, D.2    Chen, A.3    Kabra, N.H.4    Winoto, A.5
  • 44
    • 0032472916 scopus 로고    scopus 로고
    • A dominant interfering mutant of FADD/MORT1 enhances deletion of autoreactive thymocytes and inhibits proliferation of mature T lymphocytes
    • 44 Newton K, Harris AW, Bath ML, Smith KGC, Strasser A. A dominant interfering mutant of FADD/MORT1 enhances deletion of autoreactive thymocytes and inhibits proliferation of mature T lymphocytes. EMBO J. 1998; 17: 706-18.
    • (1998) EMBO J. , vol.17 , pp. 706-718
    • Newton, K.1    Harris, A.W.2    Bath, M.L.3    Smith, K.G.C.4    Strasser, A.5
  • 45
    • 0032080197 scopus 로고    scopus 로고
    • Defects in regulation of apoptosis in caspase-2-deficient mice
    • 45 Bergeron L, Perez GI, Macdonald G et al. Defects in regulation of apoptosis in caspase-2-deficient mice. Genes Dev. 1998; 12: 1304-14.
    • (1998) Genes Dev. , vol.12 , pp. 1304-1314
    • Bergeron, L.1    Perez, G.I.2    Macdonald, G.3


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