메뉴 건너뛰기




Volumn 12, Issue 6, 1998, Pages 806-819

Essential contribution of caspase 3/CPPp32 to apoptosis and its associated nuclear changes

Author keywords

Apoptosis; Caspase; Cell death; CPP32; MEFs

Indexed keywords

CASPASE; ENZYME; UNCLASSIFIED DRUG;

EID: 15644364847     PISSN: 08909369     EISSN: None     Source Type: Journal    
DOI: 10.1101/gad.12.6.806     Document Type: Review
Times cited : (778)

References (57)
  • 1
    • 0031080895 scopus 로고    scopus 로고
    • Cellular environments and apoptosis: Tissue microenvironments control activated T-cell death
    • Akbar, A.N. and M. Salmon. 1997. Cellular environments and apoptosis: Tissue microenvironments control activated T-cell death. Immunol. Today 18: 72-76.
    • (1997) Immunol. Today , vol.18 , pp. 72-76
    • Akbar, A.N.1    Salmon, M.2
  • 4
  • 7
    • 0030985969 scopus 로고    scopus 로고
    • T-cell receptor ligation by peptidc/MHC induces activation of a caspase in immature thymocytes: The molecular basis of negative selection
    • Clayton, L.K., Y. Ghendler, E. Mizoguchi, R.J. Patch, T.D. Ocain, K. Orth, A.K. Bhan, V.M. Dixit, and E.L. Reinherz. 1997. T-cell receptor ligation by peptidc/MHC induces activation of a caspase in immature thymocytes: The molecular basis of negative selection. EMBO J. 16: 2282-2293.
    • (1997) EMBO J. , vol.16 , pp. 2282-2293
    • Clayton, L.K.1    Ghendler, Y.2    Mizoguchi, E.3    Patch, R.J.4    Ocain, T.D.5    Orth, K.6    Bhan, A.K.7    Dixit, V.M.8    Reinherz, E.L.9
  • 8
    • 0026344133 scopus 로고
    • Prevention of apoptosis by a baculovirus gene during infection of insect cells
    • Clem, R.J., M. Fechheimer, and L.K. Miller. 1991. Prevention of apoptosis by a baculovirus gene during infection of insect cells. Science 254: 1388-1390.
    • (1991) Science , vol.254 , pp. 1388-1390
    • Clem, R.J.1    Fechheimer, M.2    Miller, L.K.3
  • 9
    • 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
  • 10
    • 0029832173 scopus 로고    scopus 로고
    • Cleavage of CPP32 by granzyme B represents a critical role for granzyme B in the induction of target cell DNA fragmentation
    • Darmon, A.J., T.J. Ley, D.W. Nicholson, and R.C. Bleackley. 1996. Cleavage of CPP32 by granzyme B represents a critical role for granzyme B in the induction of target cell DNA fragmentation. J. Biol. Chem. 271:21709-21712.
    • (1996) J. Biol. Chem. , vol.271 , pp. 21709-21712
    • Darmon, A.J.1    Ley, T.J.2    Nicholson, D.W.3    Bleackley, R.C.4
  • 11
    • 0030008812 scopus 로고    scopus 로고
    • ICE-LAP6, a novel member of the ICE/Ced-3 gene family, is activated by the cytotoxic T cell protease granzyme B
    • Duan, H., K. Orth, A.M. Chinnaiyan, G.G. Poirier, C.J. Froelich, W.W. He, and V.M. Dixit. 1996. ICE-LAP6, a novel member of the ICE/Ced-3 gene family, is activated by the cytotoxic T cell protease granzyme B. J. Biol. Chem. 271: 16720-16724.
    • (1996) J. Biol. Chem. , vol.271 , pp. 16720-16724
    • Duan, H.1    Orth, K.2    Chinnaiyan, A.M.3    Poirier, G.G.4    Froelich, C.J.5    He, W.W.6    Dixit, V.M.7
  • 12
    • 0026508561 scopus 로고
    • Exposure of phosphatidylserine on the surface of apoptotic lymphocytes triggers specific recognition and removal by macrophages
    • Fadok, V.A., D.R. Voelker, P.A. Campbell, J.J. Cohen, D.L. Bratton, and P.M. Henson. 1992. Exposure of phosphatidylserine on the surface of apoptotic lymphocytes triggers specific recognition and removal by macrophages. J. Immunol. 148: 2207-2216.
    • (1992) J. Immunol. , vol.148 , pp. 2207-2216
    • Fadok, V.A.1    Voelker, D.R.2    Campbell, P.A.3    Cohen, J.J.4    Bratton, D.L.5    Henson, P.M.6
  • 13
    • 0030973417 scopus 로고    scopus 로고
    • Multiple species of CPP32 and Mch2 are the major active caspases present in apoptotic cells
    • Faleiro, L., R. Kobayashi, H. Fearnhead, and Y. Lazebnik. 1997. Multiple species of CPP32 and Mch2 are the major active caspases present in apoptotic cells. EMBO J. 16: 2271-2281.
    • (1997) EMBO J. , vol.16 , pp. 2271-2281
    • Faleiro, L.1    Kobayashi, R.2    Fearnhead, H.3    Lazebnik, Y.4
  • 14
    • 0027973061 scopus 로고
    • CPP32, a novel human apoptotic protein with homology to Caenorhabditis elegans cell death protein Ced-3 and mammalian interleukin-1 β- Converting enzyme
    • Fernandes-Alnemri, T., G. Litwack, and E.S. Alnemri. 1994. CPP32, a novel human apoptotic protein with homology to Caenorhabditis elegans cell death protein Ced-3 and mammalian interleukin-1 β-converting enzyme. J. Biol. Chem. 269: 30761-30764.
    • (1994) J. Biol. Chem. , vol.269 , pp. 30761-30764
    • Fernandes-Alnemri, T.1    Litwack, G.2    Alnemri, E.S.3
  • 16
  • 17
    • 0028789425 scopus 로고
    • The killer and the executioner: How apoptosis controls malignancy
    • Green, D.R. and S.J. Martin. 1995. The killer and the executioner: How apoptosis controls malignancy. Curr. Opin. Immunol. 7: 694-703.
    • (1995) Curr. Opin. Immunol. , vol.7 , pp. 694-703
    • Green, D.R.1    Martin, S.J.2
  • 19
    • 0027447188 scopus 로고
    • Elimination of self-reactive B lymphocytes proceeds in two stages: Arrested development and cell death
    • Hartley, S.B., M.P. Cooke, D.A. Fulcher, A.W. Harris, S. Cory, A. Basten, and C.C. Goodnow. 1993. Elimination of self-reactive B lymphocytes proceeds in two stages: Arrested development and cell death. Cell 72: 325-335.
    • (1993) Cell , vol.72 , pp. 325-335
    • Hartley, S.B.1    Cooke, M.P.2    Fulcher, D.A.3    Harris, A.W.4    Cory, S.5    Basten, A.6    Goodnow, C.C.7
  • 20
    • 0030050416 scopus 로고    scopus 로고
    • Programmed cell death in invertebrates
    • Hengartner, M.O. 1996. Programmed cell death in invertebrates. Curr. Opin. Genet. Dev. 6: 34-38.
    • (1996) Curr. Opin. Genet. Dev. , vol.6 , pp. 34-38
    • Hengartner, M.O.1
  • 21
    • 0028147070 scopus 로고
    • Programmed cell death in Caenorhabditis elegans
    • Hengartner, M.O. and H.R. Horvitz. 1994a. Programmed cell death in Caenorhabditis elegans. Curr. Opin. Genet. Dev. 4: 581-586.
    • (1994) Curr. Opin. Genet. Dev. , vol.4 , pp. 581-586
    • Hengartner, M.O.1    Horvitz, H.R.2
  • 22
    • 0028288277 scopus 로고
    • C. elegans cell survival gene ced-9 encodes a functional homolog of the mammalian proto-oncogene bcl-2
    • _. 1994b. C. elegans cell survival gene ced-9 encodes a functional homolog of the mammalian proto-oncogene bcl-2. Cell 76: 665-676.
    • (1994) Cell , vol.76 , pp. 665-676
  • 24
  • 25
    • 0030886975 scopus 로고    scopus 로고
    • p53-independent apoptosis induced by paclitaxel through an indirect mechanism
    • Lanni, J.S., S.W. Lowe, E.J. Licitra, J.O. Liu, and T. Jacks. 1997. p53-independent apoptosis induced by paclitaxel through an indirect mechanism. Proc. Natl. Acad. Sci. 94: 9679-9683.
    • (1997) Proc. Natl. Acad. Sci. , vol.94 , pp. 9679-9683
    • Lanni, J.S.1    Lowe, S.W.2    Licitra, E.J.3    Liu, J.O.4    Jacks, T.5
  • 26
    • 0029013273 scopus 로고
    • p53 and its 14 kDa C-terminal domain recognize primary DNA damage in the form of insertion/deletion mismatches
    • Lee, S., B. Elenbaas, A. Levine, and J. Griffith. 1995. p53 and its 14 kDa C-terminal domain recognize primary DNA damage in the form of insertion/deletion mismatches. Cell 81: 1013-1020.
    • (1995) Cell , vol.81 , pp. 1013-1020
    • Lee, S.1    Elenbaas, B.2    Levine, A.3    Griffith, J.4
  • 27
    • 0030927115 scopus 로고    scopus 로고
    • Apoptosis - Role in infection and inflammation
    • Liles, C.W. 1997. Apoptosis - role in infection and inflammation. Curr. Opin. Infect. Dis. 10:165-170.
    • (1997) Curr. Opin. Infect. Dis. , vol.10 , pp. 165-170
    • Liles, C.W.1
  • 28
    • 0030916417 scopus 로고    scopus 로고
    • DFF, a heterodimeric protein that functions downstream of caspase-3 to trigger DNA fragmentation during apoptosis
    • Liu, X., H. Zou, C. Slaughter, and X. Wang. 1997. DFF, a heterodimeric protein that functions downstream of caspase-3 to trigger DNA fragmentation during apoptosis. Cell 89: 175-184.
    • (1997) Cell , vol.89 , pp. 175-184
    • Liu, X.1    Zou, H.2    Slaughter, C.3    Wang, X.4
  • 29
    • 0027451668 scopus 로고
    • p53-dependent apoptosis modulates the cytotoxicity of anticancer agents
    • Lowe, S.W., H.E. Ruley, T. Jacks, and D.E. Housman. 1993 p53-dependent apoptosis modulates the cytotoxicity of anticancer agents. Cell 74: 957-967.
    • (1993) Cell , vol.74 , pp. 957-967
    • Lowe, S.W.1    Ruley, H.E.2    Jacks, T.3    Housman, D.E.4
  • 30
    • 0027319521 scopus 로고
    • p53 is required for radiation-induced apoptosis in mouse thymocytes
    • Lowe, S.W., E.M. Schmitt, S.W. Smith, B.A. Osborne, and T. Jacks. 1993. p53 is required for radiation-induced apoptosis in mouse thymocytes. Nature 362: 847-849.
    • (1993) Nature , vol.362 , pp. 847-849
    • Lowe, S.W.1    Schmitt, E.M.2    Smith, S.W.3    Osborne, B.A.4    Jacks, T.5
  • 32
    • 0030938089 scopus 로고    scopus 로고
    • Bax-deficiency promotes drug resistance and oncogenic transformation by attenuating p53-dependent apoptosis
    • McCurrach, M.E., T.M. Connor, C.M. Knudson, S.J. Korsmeyer, and S.W. Lowe. 1997. Bax-deficiency promotes drug resistance and oncogenic transformation by attenuating p53-dependent apoptosis. Proc. Natl. Acad. Sci. 94: 2345-2349.
    • (1997) Proc. Natl. Acad. Sci. , vol.94 , pp. 2345-2349
    • McCurrach, M.E.1    Connor, T.M.2    Knudson, C.M.3    Korsmeyer, S.J.4    Lowe, S.W.5
  • 34
    • 0030892234 scopus 로고    scopus 로고
    • Apoptosis by death factor
    • Nagata, S. 1997. Apoptosis by death factor. Cell 88: 355-365.
    • (1997) Cell , vol.88 , pp. 355-365
    • Nagata, S.1
  • 38
    • 0030979773 scopus 로고    scopus 로고
    • Double identity for proteins of the Bcl-2 family
    • Reed, J.C. 1997. Double identity for proteins of the Bcl-2 family. Nature 387: 773-776.
    • (1997) Nature , vol.387 , pp. 773-776
    • Reed, J.C.1
  • 39
    • 0030918572 scopus 로고    scopus 로고
    • Membrane and morphological changes in apoptotic cells regulated by caspase-mediated activation of PAK2
    • Rudel, T. and G.M. Bokoch. 1997. Membrane and morphological changes in apoptotic cells regulated by caspase-mediated activation of PAK2. Science 276: 1571-1574.
    • (1997) Science , vol.276 , pp. 1571-1574
    • Rudel, T.1    Bokoch, G.M.2
  • 40
    • 0030726461 scopus 로고    scopus 로고
    • Selective induction of p53 and chemosensitivity in Rb-deficient cells by E1A mutants unable to bind the retinoblastsoma-related proteins. Proc
    • Samuelson, A.V. and S.W. Lowe. 1997. Selective induction of p53 and chemosensitivity in Rb-deficient cells by E1A mutants unable to bind the retinoblastsoma-related proteins. Proc. Natl. Acad. Sci. 94: 12094-12099.
    • (1997) Natl. Acad. Sci. , vol.94 , pp. 12094-12099
    • Samuelson, A.V.1    Lowe, S.W.2
  • 41
    • 0027979892 scopus 로고
    • Sensitive method for measuring apoptosis and cell surface phenotype in human thymocytes by flow cytometry
    • Schmid, I., C.H. Uittenbogaart , J.V. Giorgi. 1994. Sensitive method for measuring apoptosis and cell surface phenotype in human thymocytes by flow cytometry. Cytometry 1: 12-20.
    • (1994) Cytometry , vol.1 , pp. 12-20
    • Schmid, I.1    Uittenbogaart, C.H.2    Giorgi, J.V.3
  • 42
    • 0030944985 scopus 로고    scopus 로고
    • Oncogenic ras provokes premature cell senescence associated with accumulation of p53 and p16INK4a
    • Serrano, M., A.W. Lin, M.E. McCurrach, D. Beach, and S.W. Lowe. 1997. Oncogenic ras provokes premature cell senescence associated with accumulation of p53 and p16INK4a. Cell 88: 593-602.
    • (1997) Cell , vol.88 , pp. 593-602
    • Serrano, M.1    Lin, A.W.2    McCurrach, M.E.3    Beach, D.4    Lowe, S.W.5
  • 43
    • 0024492086 scopus 로고
    • Antibodies to CD3/T-cell receptor complex induce death by apoptosis in immature T cells in thymic cultures
    • Smith, C.A., G.T. Williams, R. Kingston, E.J. Jenkinson, and J.J. Owen. 1989. Antibodies to CD3/T-cell receptor complex induce death by apoptosis in immature T cells in thymic cultures. Nature 337: 181-184.
    • (1989) Nature , vol.337 , pp. 181-184
    • Smith, C.A.1    Williams, G.T.2    Kingston, R.3    Jenkinson, E.J.4    Owen, J.J.5
  • 44
    • 0028929328 scopus 로고
    • Mechanisms and genes of cellular suicide
    • Steller, H. 1995. Mechanisms and genes of cellular suicide. Science 267: 1445-1449.
    • (1995) Science , vol.267 , pp. 1445-1449
    • Steller, H.1
  • 45
    • 0028271740 scopus 로고
    • Baculovirus p35 prevents developmentally programmed cell death and rescues a ced-9 mutant in the nematode Caenorhabditis elegans
    • Sugimoto, A., P.D. Friesen, and J.H. Rothman. 1994. Baculovirus p35 prevents developmentally programmed cell death and rescues a ced-9 mutant in the nematode Caenorhabditis elegans. EMBO J. 13: 2023-2028.
    • (1994) EMBO J. , vol.13 , pp. 2023-2028
    • Sugimoto, A.1    Friesen, P.D.2    Rothman, J.H.3
  • 47
    • 0028990125 scopus 로고
    • Yama/CPP32 beta, 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/CPP32 beta, 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
  • 48
    • 0028943734 scopus 로고
    • Apoptosis in the pathogenesis and treatment of disease
    • Thompson, C.B. 1995. Apoptosis in the pathogenesis and treatment of disease. Science 267: 1456-1462.
    • (1995) Science , vol.267 , pp. 1456-1462
    • Thompson, C.B.1
  • 49
    • 0028674139 scopus 로고
    • Interleukin-1 beta converting enzyme
    • Thornberry, N.A. 1994. Interleukin-1 beta converting enzyme. Methods Enzymol. 244: 615-631.
    • (1994) Methods Enzymol. , vol.244 , pp. 615-631
    • Thornberry, N.A.1
  • 51
    • 0028959195 scopus 로고
    • In vivo regulation of rat neutrophil apoptosis occurring spontaneously or induced with TNF-alpha or cycloheximide
    • Tsuchida, H., Y. Takeda, H. Takei, H. Shinzawa, T. Takahashi, and F. Sendo. 1995. In vivo regulation of rat neutrophil apoptosis occurring spontaneously or induced with TNF-alpha or cycloheximide. J. Immunol 154: 2403-2412.
    • (1995) J. Immunol , vol.154 , pp. 2403-2412
    • Tsuchida, H.1    Takeda, Y.2    Takei, H.3    Shinzawa, H.4    Takahashi, T.5    Sendo, F.6
  • 52
    • 0029965136 scopus 로고    scopus 로고
    • The molecular biology of apoptosis
    • Vaux, D.L. and A. Strasser. 1996. The molecular biology of apoptosis. Proc. Natl. Acad. Sci. 93: 2239-2244.
    • (1996) Proc. Natl. Acad. Sci. , vol.93 , pp. 2239-2244
    • Vaux, D.L.1    Strasser, A.2
  • 53
    • 0027146334 scopus 로고
    • Death-defying acts: A meeting review on apoptosis
    • White, E. 1993. Death-defying acts: A meeting review on apoptosis. Genes & Dev. 7: 2277-2284.
    • (1993) Genes & Dev. , vol.7 , pp. 2277-2284
    • White, E.1
  • 54
    • 0029880987 scopus 로고    scopus 로고
    • The Caenorhabditis elegans cell-death protein CED-3 is a cysteine protease with substrate specificities similar to those of the human CPP32 protease
    • Xue, D., S. Shaham, and H.R. Horvitz. 1996. The Caenorhabditis elegans cell-death protein CED-3 is a cysteine protease with substrate specificities similar to those of the human CPP32 protease. Genes &. Dev. 10: 1073-1083.
    • (1996) Genes &. Dev. , vol.10 , pp. 1073-1083
    • Xue, D.1    Shaham, S.2    Horvitz, H.R.3
  • 55
    • 0031024011 scopus 로고    scopus 로고
    • A cysteine protease inhibitor prevents activation-induced T-cell apoptosis and death of peripheral blood cells from human immunodeficiency virus-infected individuals by inhibiting upregulation of Fas ligand
    • Yang, Y., Z.H. Liu, C.F. Ware, and J.D. Ashwell. 1997. A cysteine protease inhibitor prevents activation-induced T-cell apoptosis and death of peripheral blood cells from human immunodeficiency virus-infected individuals by inhibiting upregulation of Fas ligand. Blood 89: 550-557.
    • (1997) Blood , vol.89 , pp. 550-557
    • Yang, Y.1    Liu, Z.H.2    Ware, C.F.3    Ashwell, J.D.4
  • 56
    • 0027525104 scopus 로고
    • The C. elegans cell death gene ced-3 encodes a protein similar to mammalian interleukin-1 β-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-1 β-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
  • 57
    • 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
    • Zhou, 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
    • Zhou, H.1    Henzel, W.J.2    Liu, X.3    Lutschg, A.4    Wang, X.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.