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Volumn 6, Issue 8, 1996, Pages 997-1005

Bcl-2 regulates activation of apoptotic proteases in a cell-free system

Author keywords

[No Author keywords available]

Indexed keywords

ANIMALIA; METAZOA; NEMATODA; XENOPUS LAEVIS;

EID: 0030220462     PISSN: 09609822     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0960-9822(02)00644-9     Document Type: Article
Times cited : (50)

References (50)
  • 1
    • 0026504147 scopus 로고
    • Social controls on cell survival and cell death
    • Raff MC: Social controls on cell survival and cell death. Nature 1992, 356:397-400.
    • (1992) Nature , vol.356 , pp. 397-400
    • Raff, M.C.1
  • 2
    • 0026698173 scopus 로고
    • Apoptosis induced by anti-cancer drugs
    • Hickman JA: Apoptosis induced by anti-cancer drugs. Cancer Metastasis Rev 1992, 11:121-139.
    • (1992) Cancer Metastasis Rev , vol.11 , pp. 121-139
    • Hickman, J.A.1
  • 3
    • 0028782774 scopus 로고
    • Death from inside out: An overview
    • Wyllie AH: Death from inside out: an overview. Philos Trans R Soc Lond [Biol] 1994, 345:237-241.
    • (1994) Philos Trans R Soc Lond [Biol] , vol.345 , pp. 237-241
    • Wyllie, A.H.1
  • 4
    • 0027945731 scopus 로고
    • The Bcl-2 family of proteins: Regulators of cell death and survival
    • Nuñez G, Clarke MF: The Bcl-2 family of proteins: regulators of cell death and survival. Trends Cell Biol 1994, 4:399-403.
    • (1994) Trends Cell Biol , vol.4 , pp. 399-403
    • Nuñez, G.1    Clarke, M.F.2
  • 5
    • 0028040019 scopus 로고
    • Bcl-2 and the regulation of programmed cell death
    • Reed JC: Bcl-2 and the regulation of programmed cell death. J Cell Biol 1994, 124:1-6.
    • (1994) J Cell Biol , vol.124 , pp. 1-6
    • Reed, J.C.1
  • 6
    • 0026582702 scopus 로고
    • Caenorhabditis elegans gene ced-9 protects cells from programmed cell death
    • Hengartner MO, Ellis RE, Horvitz HR: Caenorhabditis elegans gene ced-9 protects cells from programmed cell death. Nature 1992, 356:494-499.
    • (1992) Nature , vol.356 , pp. 494-499
    • Hengartner, M.O.1    Ellis, R.E.2    Horvitz, H.R.3
  • 7
    • 0028288277 scopus 로고
    • C. elegans cell survival gene ced-9 encodes a functional homolog of the mammalian proto-oncogene bcl-2
    • Hengartner MO, Horvitz HR: C. elegans cell survival gene ced-9 encodes a functional homolog of the mammalian proto-oncogene bcl-2.Cell 1994, 76:665-676.
    • (1994) Cell , vol.76 , pp. 665-676
    • Hengartner, M.O.1    Horvitz, H.R.2
  • 8
    • 0027050145 scopus 로고
    • Prevention of programmed cell death in Caenorhabditis elegans by human bcl-2
    • Vaux DL, Weissman IL, Kim SK: Prevention of programmed cell death in Caenorhabditis elegans by human bcl-2. Science 1992, 258:1955-1957.
    • (1992) Science , vol.258 , pp. 1955-1957
    • Vaux, D.L.1    Weissman, I.L.2    Kim, S.K.3
  • 9
    • 0028149786 scopus 로고
    • Checkpoints of duelling dimers foil death wishes
    • Oltvai ZN, Korsmeyer SJ: Checkpoints of duelling dimers foil death wishes. Cell 1994, 79:189-192.
    • (1994) Cell , vol.79 , pp. 189-192
    • Oltvai, Z.N.1    Korsmeyer, S.J.2
  • 10
    • 0028147070 scopus 로고
    • Programmed cell death in Caenorhabditis elegans
    • Hengartner MO, Horvitz HR: Programmed cell death in Caenorhabditis elegans. Curr Opin Genet Dev 1994, 4:581-586.
    • (1994) Curr Opin Genet Dev , vol.4 , pp. 581-586
    • Hengartner, M.O.1    Horvitz, H.R.2
  • 11
    • 0025255636 scopus 로고
    • The Caenorhabditis elegans genes ced-3 and ced-4 act autonomously to cause programmed cell death
    • Yuan J, Horvitz HR: The Caenorhabditis elegans genes ced-3 and ced-4 act autonomously to cause programmed cell death. Dev Biol 1990, 138:33-41.
    • (1990) Dev Biol , vol.138 , pp. 33-41
    • Yuan, J.1    Horvitz, H.R.2
  • 12
    • 0027525104 scopus 로고
    • The C. elegans cell death gene ced-3 encodes a protein similar to mammalian interleukin-1 beta-converting enzyme
    • Yuan J, Shaham S, Ledoux S, Ellis HM, Horvitz HR: The C. elegans cell death gene ced-3 encodes a protein similar to mammalian interleukin-1 beta-converting enzyme. Cell 1993, 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
  • 14
    • 0026507126 scopus 로고
    • A novel heterodimeric cysteine protease is required for interleukin-1β processing in monocytes
    • Thornberry NA, Bull HG, Calaycay JR, Chapman KT, Howard AD, Kostura MJ, et al.: A novel heterodimeric cysteine protease is required for interleukin-1β processing in monocytes. Nature 1992, 356:768-774.
    • (1992) Nature , vol.356 , pp. 768-774
    • Thornberry, N.A.1    Bull, H.G.2    Calaycay, J.R.3    Chapman, K.T.4    Howard, A.D.5    Kostura, M.J.6
  • 15
    • 0027449187 scopus 로고
    • Induction of apoptosis in fibroblasts by IL-1β-converting enzyme, a mammalian homolog of the C. elegans cell death gene ced-3
    • Miura M, Zhu H, Rotello R, Hartwieg EA, Yuan J: Induction of apoptosis in fibroblasts by IL-1β-converting enzyme, a mammalian homolog of the C. elegans cell death gene ced-3. Cell 1993, 75:653-660.
    • (1993) Cell , vol.75 , pp. 653-660
    • Miura, M.1    Zhu, H.2    Rotello, R.3    Hartwieg, E.A.4    Yuan, J.5
  • 16
    • 0028920863 scopus 로고
    • Altered cytokine export and apoptosis in mice deficient in interleukin-1 beta converting enzyme
    • Kuida K, Lippke JA, Ku G, Harding MW, Livingston DJ, Su MS, Flavell RA: Altered cytokine export and apoptosis in mice deficient in interleukin-1 beta converting enzyme. Science 1995, 267:2000-2003.
    • (1995) Science , vol.267 , pp. 2000-2003
    • Kuida, K.1    Lippke, J.A.2    Ku, G.3    Harding, M.W.4    Livingston, D.J.5    Su, M.S.6    Flavell, R.A.7
  • 17
    • 0028984948 scopus 로고
    • Mice deficient in IL-1 beta-converting enzyme are defective in production of mature IL-1 beta and resistant to endotoxic shock
    • Li P, Allen H, Banerjee S, Franklin S, Herzog L, Johnston C, et al.: Mice deficient in IL-1 beta-converting enzyme are defective in production of mature IL-1 beta and resistant to endotoxic shock. Cell 1995, 80:401-411.
    • (1995) Cell , vol.80 , pp. 401-411
    • Li, P.1    Allen, H.2    Banerjee, S.3    Franklin, S.4    Herzog, L.5    Johnston, C.6
  • 18
    • 0029069295 scopus 로고
    • ICE-like proteases in apoptosis
    • 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
  • 19
    • 0029125701 scopus 로고
    • Protease activation during apoptosis: Death by a thousand cuts?
    • Martin SJ, Green DR: Protease activation during apoptosis: death by a thousand cuts? Cell 1995, 82:349-352.
    • (1995) Cell , vol.82 , pp. 349-352
    • Martin, S.J.1    Green, D.R.2
  • 20
    • 0027255417 scopus 로고
    • Specific proteolytic cleavage of poly(ADP-ribose) polymerase: An early marker of chemotherapy-induced apoptosis
    • Kaufmann SH, Desnoyers S, Ottaviano Y, Davidson NE, Poirier GG: Specific proteolytic cleavage of poly(ADP-ribose) polymerase: an early marker of chemotherapy-induced apoptosis. Cancer Res 1993, 53:3976-3985.
    • (1993) Cancer Res , vol.53 , pp. 3976-3985
    • Kaufmann, S.H.1    Desnoyers, S.2    Ottaviano, Y.3    Davidson, N.E.4    Poirier, G.G.5
  • 21
    • 0028102478 scopus 로고
    • Cleavage of poly(ADP-ribose) polymerase by a proteinase with properties like ICE
    • Lazebnik YA, Kaufmann SH, Desnoyers S, Poirier GG, Earnshaw WC: Cleavage of poly(ADP-ribose) polymerase by a proteinase with properties like ICE. Nature 1994, 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
  • 22
  • 23
    • 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, Quan LT, O'Rourke K, Desnoyers S, Zeng Z, Beidler DR, et al.: Yama/CPP32 beta, a mammalian homolog of CED-3, is a CrmA-inhibitable protease that cleaves the death substrate poly(ADP-ribose) polymerase. Cell 1995, 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
  • 24
    • 0027973061 scopus 로고
    • CPP32, a novel human apoptotic protein with homology to Caenorhabditis elegans cell death protein Ced-3 and mammalian interleukin-1ß-converting enzyme
    • Fernandes-Alnemri T, Litwack G, Alnemri ES: CPP32, a novel human apoptotic protein with homology to Caenorhabditis elegans cell death protein Ced-3 and mammalian interleukin-1ß-converting enzyme. J Biol Chem 1994, 269:30761-30764.
    • (1994) J Biol Chem , vol.269 , pp. 30761-30764
    • Fernandes-Alnemri, T.1    Litwack, G.2    Alnemri, E.S.3
  • 25
    • 0029025549 scopus 로고
    • Mch2, a new member of the apoptotic Ced-3/ Ice cysteine protease gene family
    • Fernandes-Alnemri T, Litwack G, Alnemri ES: Mch2, a new member of the apoptotic Ced-3/ Ice cysteine protease gene family. Cancer Res 1995, 55:2737-2742.
    • (1995) Cancer Res , vol.55 , pp. 2737-2742
    • Fernandes-Alnemri, T.1    Litwack, G.2    Alnemri, E.S.3
  • 27
    • 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 tumour necrosis factor-induced apoptosis
    • Duan H, Chinnaiyan AM, Hudson PL, Wing JP, He W, Dixit VM: ICE-LAP3, a novel mammalian homologue of the Caenorhabditis elegans cell death protein Ced-3 is activated during Fas- and tumour necrosis factor-induced apoptosis. J Biol Chem 1996, 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.5    Dixit, V.M.6
  • 28
    • 0029056059 scopus 로고
    • Inhibition of the Caenorhabditis elegans cell-death protease CED-3 by a CED-3 cleavage site in baculovirus p35 protein
    • Xue D, Horvitz HR: Inhibition of the Caenorhabditis elegans cell-death protease CED-3 by a CED-3 cleavage site in baculovirus p35 protein. Nature 1995, 377:248-251.
    • (1995) Nature , vol.377 , pp. 248-251
    • Xue, D.1    Horvitz, H.R.2
  • 29
    • 0030027151 scopus 로고    scopus 로고
    • Bcl-2 and adenovirus E1B 19 kDa protein prevent E1A-induced processing of CPP32 and cleavage of poly(ADP-ribose) polymerase
    • Boulakia CA, Chen G, Ng FWH, Teodoro JG, Branton PE, Nicholson DW, et al.: Bcl-2 and adenovirus E1B 19 kDa protein prevent E1A-induced processing of CPP32 and cleavage of poly(ADP-ribose) polymerase. Oncogene 1996, 12:529-535.
    • (1996) Oncogene , vol.12 , pp. 529-535
    • Boulakia, C.A.1    Chen, G.2    Ng, F.W.H.3    Teodoro, J.G.4    Branton, P.E.5    Nicholson, D.W.6
  • 31
    • 0028019746 scopus 로고
    • Cell-free apoptosis in Xenopus egg extracts: Inhibition by Bcl-2 and requirement for an organelle fraction enriched in mitochondria
    • Newmeyer DD, Farschon DM, Reed JC: Cell-free apoptosis in Xenopus egg extracts: inhibition by Bcl-2 and requirement for an organelle fraction enriched in mitochondria. Cell 1994, 79:353-364.
    • (1994) Cell , vol.79 , pp. 353-364
    • Newmeyer, D.D.1    Farschon, D.M.2    Reed, J.C.3
  • 33
    • 0005145017 scopus 로고
    • Preparation of Xenopus egg extracts and their utilization in cell cycle studies
    • Edited by Pagano M. Heidelberg: Springer-Verlag
    • Clarke PR: Preparation of Xenopus egg extracts and their utilization in cell cycle studies. In Cell Cycle: Materials and Methods. Edited by Pagano M. Heidelberg: Springer-Verlag; 1995:103-116.
    • (1995) Cell Cycle: Materials and Methods , pp. 103-116
    • Clarke, P.R.1
  • 34
    • 0028805524 scopus 로고
    • Apoptosis by a cytosolic extract from Fas-activated cells
    • Enari M, Hase A, Nagata S: Apoptosis by a cytosolic extract from Fas-activated cells. EMBO J 1995, 14:5201-5208.
    • (1995) EMBO J , vol.14 , pp. 5201-5208
    • Enari, M.1    Hase, A.2    Nagata, S.3
  • 36
    • 0027287582 scopus 로고
    • Isolation of cDNAs encoding the catalytic domain of poly(ADP-ribose) polymerase from Xenopus laevis and cherry salmon using heterologous oligonucleotide consensus sequences
    • Ozawa Y, Uchida K, Uchida M, Ami Y, Kushida S, Okada N, Miwa M: Isolation of cDNAs encoding the catalytic domain of poly(ADP-ribose) polymerase from Xenopus laevis and cherry salmon using heterologous oligonucleotide consensus sequences. Biochem Biophys Res Commun 1993, 193:119-125.
    • (1993) Biochem Biophys Res Commun , vol.193 , pp. 119-125
    • Ozawa, Y.1    Uchida, K.2    Uchida, M.3    Ami, Y.4    Kushida, S.5    Okada, N.6    Miwa, M.7
  • 38
    • 0028817947 scopus 로고
    • Inhibition of ICE family proteases by baculovirus anti-apoptotic protein p35
    • Bump NJ, Hackett M, Hugunin M, Seshagari S, Brady K, Chen P, et al.: Inhibition of ICE family proteases by baculovirus anti-apoptotic protein p35. Science 1995, 269:1885-1888.
    • (1995) Science , vol.269 , pp. 1885-1888
    • Bump, N.J.1    Hackett, M.2    Hugunin, M.3    Seshagari, S.4    Brady, K.5    Chen, P.6
  • 39
    • 0029099845 scopus 로고
    • Activation of the apoptotic protease CPP32 by cytotoxic T-cell-derived granzyme B
    • Darmon AJ, Nicholson DW, Bleackley RC: Activation of the apoptotic protease CPP32 by cytotoxic T-cell-derived granzyme B. Nature 1995, 377:446-448.
    • (1995) Nature , vol.377 , pp. 446-448
    • Darmon, A.J.1    Nicholson, D.W.2    Bleackley, R.C.3
  • 40
    • 0028790829 scopus 로고
    • Bcl-2 blocks glucocorticoid- but not Fas- or activation-induced apoptosis in a T cell hybridoma
    • Memon SA, Moreno MB, Petrak D, Zacharchuk CM: Bcl-2 blocks glucocorticoid- but not Fas- or activation-induced apoptosis in a T cell hybridoma. J Immunol 1995, 155:4644-4652.
    • (1995) J Immunol , vol.155 , pp. 4644-4652
    • Memon, S.A.1    Moreno, M.B.2    Petrak, D.3    Zacharchuk, C.M.4
  • 41
    • 0028917923 scopus 로고
    • Bcl-2 blocks degranulation but not Fas-based cell-mediated cytotoxicity
    • Chiu VK, Walsh CM, Liu CC, Reed JC, Clark WR: Bcl-2 blocks degranulation but not Fas-based cell-mediated cytotoxicity. J Immunol 1995, 154:2023-2032.
    • (1995) J Immunol , vol.154 , pp. 2023-2032
    • Chiu, V.K.1    Walsh, C.M.2    Liu, C.C.3    Reed, J.C.4    Clark, W.R.5
  • 42
    • 0029609086 scopus 로고
    • Bcl-2 and Fas/APO-1 regulate distinct pathways to lymphocyte apoptosis
    • Strasser A, Harris AW, Huang DCS, Krammer PH, CoryS: Bcl-2 and Fas/APO-1 regulate distinct pathways to lymphocyte apoptosis. EMBO J 1995, 14:6136-6147.
    • (1995) EMBO J , vol.14 , pp. 6136-6147
    • Strasser, A.1    Harris, A.W.2    Huang, D.C.S.3    Krammer, P.H.4    Cory, S.5
  • 43
    • 0029022365 scopus 로고
    • Involvement of an ICE-like protease in Fas-mediated apoptosis
    • Enari M, Hug H, Nagata S: Involvement of an ICE-like protease in Fas-mediated apoptosis. Nature 1995, 375:78-81.
    • (1995) Nature , vol.375 , pp. 78-81
    • Enari, M.1    Hug, H.2    Nagata, S.3
  • 44
    • 0027989510 scopus 로고
    • Chromatin condensation during apoptosis is accompanied by degradation of lamin A+ B, without enhanced activation of cdc2 kinase
    • Oberhammer FA, Hochegger K, Froschl G, Tiefenbacher R, Pavelka M: Chromatin condensation during apoptosis is accompanied by degradation of lamin A+ B, without enhanced activation of cdc2 kinase. J Cell Biol 1994, 126:827-837.
    • (1994) J Cell Biol , vol.126 , pp. 827-837
    • Oberhammer, F.A.1    Hochegger, K.2    Froschl, G.3    Tiefenbacher, R.4    Pavelka, M.5
  • 45
    • 14844356354 scopus 로고
    • Degradation of lamin B1 precedes oligonucleosomal DNA fragmentation in apoptotic thymocytes and isolated thymocyte nuclei
    • Neamati N, Fernandez A, Wright S, Kiefer J, McConkey DJ: Degradation of lamin B1 precedes oligonucleosomal DNA fragmentation in apoptotic thymocytes and isolated thymocyte nuclei. J Immunol 1995, 154:3788-3795.
    • (1995) J Immunol , vol.154 , pp. 3788-3795
    • Neamati, N.1    Fernandez, A.2    Wright, S.3    Kiefer, J.4    McConkey, D.J.5
  • 46
  • 47
    • 0027999537 scopus 로고
    • Specific cleavage of the 70 kDa protein component of the U1 small nuclear ribonucleoprotein is a characteristic biochemical feature of apoptotic cell death
    • Casciola-Rosen LA, Miller DK, Anhalt GJ, Rosen A: Specific cleavage of the 70 kDa protein component of the U1 small nuclear ribonucleoprotein is a characteristic biochemical feature of apoptotic cell death. J Biol Chem 1994, 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
  • 48
    • 13344259987 scopus 로고
    • Proteolytic activation of protein kinase Cδ by an ICE-like protease in apoptotic cells
    • Emoto Y, Manome Y, Meinhardt G, Kisaki H, Kharbanda S, Robertson M, et al.: Proteolytic activation of protein kinase Cδ by an ICE-like protease in apoptotic cells. EMBO J 1995, 14:6148-6156.
    • (1995) EMBO J , vol.14 , pp. 6148-6156
    • Emoto, Y.1    Manome, Y.2    Meinhardt, G.3    Kisaki, H.4    Kharbanda, S.5    Robertson, M.6
  • 50
    • 0025666621 scopus 로고
    • Mitotic chromatin condensation in vitro using somatic cell extracts and nuclei with variable levels of endogenous topoisomerase II
    • Wood ER, Earnshaw WC: Mitotic chromatin condensation in vitro using somatic cell extracts and nuclei with variable levels of endogenous topoisomerase II. J Cell Biol 1990, 111:2839-2850.
    • (1990) J Cell Biol , vol.111 , pp. 2839-2850
    • Wood, E.R.1    Earnshaw, W.C.2


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