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Volumn 160, Issue 11, 1998, Pages 5605-5615

Potassium leakage during the apoptotic degradation phase

Author keywords

[No Author keywords available]

Indexed keywords

BENZOFURAN DERIVATIVE; FAS ANTIGEN; GLUCOCORTICOID; PHOSPHATIDYLSERINE; POTASSIUM ION; PROTEIN BCL 2;

EID: 0032103970     PISSN: 00221767     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (169)

References (62)
  • 1
    • 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.
    • (1995) Science , vol.267 , pp. 1456
    • Thompson, C.B.1
  • 3
    • 0030916669 scopus 로고    scopus 로고
    • The proto-oncogene Bcl-2 and its role in regulating apoptosis
    • Kroemer, G. 1997. The proto-oncogene Bcl-2 and its role in regulating apoptosis. Nat Med. 3:614.
    • (1997) Nat Med. , vol.3 , pp. 614
    • Kroemer, G.1
  • 4
    • 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.
    • (1997) Nature , vol.387 , pp. 773
    • Reed, J.C.1
  • 5
    • 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.
    • (1996) Cell , vol.86 , pp. 147
    • Liu, X.1    Kim, C.N.2    Yang, J.3    Jemmerson, R.4    Wang, X.5
  • 6
    • 0031019739 scopus 로고    scopus 로고
    • Interaction between the C. elegans cell-death regulators CED-9 and CED-4
    • Spector, M. S., S. Desnoyers, D. J. Hoeppner, and M. O. Hengartner. 1997. Interaction between the C. elegans cell-death regulators CED-9 and CED-4. Nature 385:653.
    • (1997) Nature , vol.385 , pp. 653
    • Spector, M.S.1    Desnoyers, S.2    Hoeppner, D.J.3    Hengartner, M.O.4
  • 7
    • 0031034997 scopus 로고    scopus 로고
    • Interaction of CED-4 with CED-3 and CED-9: A molecular frame for cell death
    • Chinnaiyan, A. M., K. O'Rourke, B. R. Lane, and V. M. Dixit. 1997. Interaction of CED-4 with CED-3 and CED-9: a molecular frame for cell death. Science 275:1122.
    • (1997) Science , vol.275 , pp. 1122
    • Chinnaiyan, A.M.1    O'Rourke, K.2    Lane, B.R.3    Dixit, V.M.4
  • 8
    • 0031020227 scopus 로고    scopus 로고
    • Interaction and regulation of subcellular localization of CED-4 by CED-9
    • Wu, D., H. D. Wallen, and G. Nuñez. 1997. Interaction and regulation of subcellular localization of CED-4 by CED-9. Science 275:1126.
    • (1997) Science , vol.275 , pp. 1126
    • Wu, D.1    Wallen, H.D.2    Nuñez, G.3
  • 14
    • 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. 1997. The release of cytochrome c from mitochondria: a primary site for Bcl-2 regulation of apoptosis. Science 275:1132.
    • (1997) Science , vol.275 , pp. 1132
    • Kluck, R.M.1    Bossy-Wetzel, E.2    Green, D.R.3    Newmeyer, D.D.4
  • 15
    • 0029982148 scopus 로고    scopus 로고
    • The cytotoxicity of tumor necrosis factor depends on induction of the mitochondrial permeability transition
    • Pastorino, J. G., G. Simbula, K. Yamamoto, P. A. J. Glascott, R. J. Rothman, and J. L. Farber. 1996. The cytotoxicity of tumor necrosis factor depends on induction of the mitochondrial permeability transition. J. Biol. Chem. 271:29792.
    • (1996) J. Biol. Chem. , vol.271 , pp. 29792
    • Pastorino, J.G.1    Simbula, G.2    Yamamoto, K.3    Glascott, P.A.J.4    Rothman, R.J.5    Farber, J.L.6
  • 16
    • 0030592172 scopus 로고    scopus 로고
    • The permeability transition pore: Control points of a cyclosporin A-sensitive mitochondrial channel involved in cell death
    • Bernardi, P. 1996. The permeability transition pore: control points of a cyclosporin A-sensitive mitochondrial channel involved in cell death. Biochim. Biophys. Acta 1275:5.
    • (1996) Biochim. Biophys. Acta , vol.1275 , pp. 5
    • Bernardi, P.1
  • 17
    • 0024603904 scopus 로고
    • Calcium-activated DNA fragmentation kills immature thymocytes
    • McConkey, D. J., P. Hartzell, P. Nicotera, and S. Orrenius. 1989. Calcium-activated DNA fragmentation kills immature thymocytes. FASEB J. 3:1843.
    • (1989) FASEB J , vol.3 , pp. 1843
    • McConkey, D.J.1    Hartzell, P.2    Nicotera, P.3    Orrenius, S.4
  • 18
    • 0029831619 scopus 로고    scopus 로고
    • Calcium-dependent, interleukin 1 beta-converting enzyme inhibitor-insensitive degradation of lamin B-1 and DNA fragmentation in isolated thymocyte nuclei
    • McConkey, D. J. 1996. Calcium-dependent, interleukin 1 beta-converting enzyme inhibitor-insensitive degradation of lamin B-1 and DNA fragmentation in isolated thymocyte nuclei. J. Biol. Chem. 271:22398.
    • (1996) J. Biol. Chem. , vol.271 , pp. 22398
    • McConkey, D.J.1
  • 20
    • 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.
    • (1995) J. Exp. Med. , vol.181 , pp. 1661
    • Zamzami, N.1    Marchetti, P.2    Castedo, M.3    Zanin, C.4    Vayssière, J.-L.5    Petit, P.X.6    Kroemer, G.7
  • 23
    • 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.
    • (1996) J. Immunol. , vol.157 , pp. 512
    • Castedo, M.1    Hirsch, T.2    Susin, S.A.3    Zamzami, N.4    Marchetti, P.5    Macho, A.6    Kroemer, G.7
  • 26
    • 0030943967 scopus 로고    scopus 로고
    • Relationships between the mitochondrial permeability transition and oxidative stress during ara-C toxicity
    • Backway, K. L., E. A. McCulloch, S. Chow, and D. W. Hedley. 1997. Relationships between the mitochondrial permeability transition and oxidative stress during ara-C toxicity. Cancer Res. 57:2446.
    • (1997) Cancer Res. , vol.57 , pp. 2446
    • Backway, K.L.1    McCulloch, E.A.2    Chow, S.3    Hedley, D.W.4
  • 28
    • 0029036412 scopus 로고
    • Alterations of mitochondrial structure and function are early events of dexamethasone-induced thymocyte apoptosis
    • Petit, P. X., H. LeCoeur, E. Zorn, C. Dauguet, B. Mignotte, and M. L. Gougeon. 1995. Alterations of mitochondrial structure and function are early events of dexamethasone-induced thymocyte apoptosis. J. Cell. Biol. 130:157.
    • (1995) J. Cell. Biol. , vol.130 , pp. 157
    • Petit, P.X.1    LeCoeur, H.2    Zorn, E.3    Dauguet, C.4    Mignotte, B.5    Gougeon, M.L.6
  • 29
    • 0029884711 scopus 로고    scopus 로고
    • Bcl-2 blocks loss of mitochondrial membrane potential while ICE inhibitors act at a different step during inhibition of death induced by respiratory chain inhibitors
    • Shimizu, S., Y. Eguchi, W. Kamiike, S. Waguri, Y. Uchiyama, H. Matsuda, and Y. Tsujimoto. 1996. Bcl-2 blocks loss of mitochondrial membrane potential while ICE inhibitors act at a different step during inhibition of death induced by respiratory chain inhibitors. Oncogene 13:21.
    • (1996) Oncogene , vol.13 , pp. 21
    • Shimizu, S.1    Eguchi, Y.2    Kamiike, W.3    Waguri, S.4    Uchiyama, Y.5    Matsuda, H.6    Tsujimoto, Y.7
  • 30
    • 0029906828 scopus 로고    scopus 로고
    • Bax-induced cell death may not require interleukin 1β-converting enzyrne-like proteases
    • Xiang, J., D. T. Chao, and S. J. Korsmeyer. 1996. Bax-induced cell death may not require interleukin 1β-converting enzyrne-like proteases. Proc. Natl. Acad. Sci. USA 93:14559.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 14559
    • Xiang, J.1    Chao, D.T.2    Korsmeyer, S.J.3
  • 31
    • 0030994024 scopus 로고    scopus 로고
    • Bcl-XL can inhibit apoptosis in cells that have undergone Fas-induced protease activation
    • Boise, L. H., and C. B. Thompson. 1997. Bcl-XL can inhibit apoptosis in cells that have undergone Fas-induced protease activation. Proc. Natl. Acad. Sci. USA 94:3759.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 3759
    • Boise, L.H.1    Thompson, C.B.2
  • 34
    • 0027483920 scopus 로고
    • Induction of apoptosis in cerebellar granule neurons by low potassium: Inhibition of death by insulin-like growth factor I and cAMP
    • D'mello, S. R., C. Galli, T. Ciotti, and P. Calissano. 1993. Induction of apoptosis in cerebellar granule neurons by low potassium: inhibition of death by insulin-like growth factor I and cAMP. Proc. Natl. Acad. Sci. USA 90:10989.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 10989
    • D'mello, S.R.1    Galli, C.2    Ciotti, T.3    Calissano, P.4
  • 35
    • 0028013217 scopus 로고
    • Cytolysis mediated by ionophores and pore-forming agents: Role of intracellular calcium in apoptosis
    • Duke, R. C., R. Z. Witter, P. B. Nash, J. D.-E. Young, and D. M. Ojcius. 1994. Cytolysis mediated by ionophores and pore-forming agents: role of intracellular calcium in apoptosis. FASEB J. 8:237.
    • (1994) FASEB J , vol.8 , pp. 237
    • Duke, R.C.1    Witter, R.Z.2    Nash, P.B.3    Young, J.D.-E.4    Ojcius, D.M.5
  • 36
    • 0028924891 scopus 로고
    • Apoptosis in cerebellar granule cells is blocked by high KCI, forskolin, and IGF-1 through distinct mechanisms of action: The involvement of intracellular calcium and RNA synthesis
    • Galli, C., O. Meucci, A. Scorziello, T. M. Werge, P. Calissano, and G. Schettini. 1995. Apoptosis in cerebellar granule cells is blocked by high KCI, forskolin, and IGF-1 through distinct mechanisms of action: the involvement of intracellular calcium and RNA synthesis. J. Neurosci. 15:1172.
    • (1995) J. Neurosci. , vol.15 , pp. 1172
    • Galli, C.1    Meucci, O.2    Scorziello, A.3    Werge, T.M.4    Calissano, P.5    Schettini, G.6
  • 39
    • 0000756177 scopus 로고    scopus 로고
    • Detection of apoptosis and apoptosis associated alterations
    • Ch. 14.2. R. Lefkovitz, ed. Academic Press, San Diego
    • Kroemer, G., B. Lisardo, P. Zamzami, S. Hortelano, and C.-A. Martinez. 1997. Detection of apoptosis and apoptosis associated alterations. In The Immunology Methods Manual, Ch. 14.2. R. Lefkovitz, ed. Academic Press, San Diego, pp. 1111-1125.
    • (1997) The Immunology Methods Manual , pp. 1111-1125
    • Kroemer, G.1    Lisardo, B.2    Zamzami, P.3    Hortelano, S.4    Martinez, C.-A.5
  • 40
    • 0024853570 scopus 로고
    • Fluorescent indicators for cytosolic sodium
    • Minta, A., and R. Y. Tsien. 1989. Fluorescent indicators for cytosolic sodium. J. Biol. Chem. 264:19449.
    • (1989) J. Biol. Chem. , vol.264 , pp. 19449
    • Minta, A.1    Tsien, R.Y.2
  • 41
    • 0026534296 scopus 로고
    • Regulation of intracellular potassium in mesangial cells: A fluorescence analysis using the dye, PBFI
    • Kasner, S. E., and M. B. Ganz. 1992. Regulation of intracellular potassium in mesangial cells: a fluorescence analysis using the dye, PBFI. Am. J. Physiol. 262:F462.
    • (1992) Am. J. Physiol. , vol.262
    • Kasner, S.E.1    Ganz, M.B.2
  • 43
    • 0025726216 scopus 로고
    • A rapid simple method for measuring thymocyte apoptosis by propidium iodide staining and flow cytometry
    • Nicoletti, I., G. Migliorati, M. C. Pagliacci, and C. Riccardi. 1991. A rapid simple method for measuring thymocyte apoptosis by propidium iodide staining and flow cytometry. J. Immunol. Methods 139:271.
    • (1991) J. Immunol. Methods , vol.139 , pp. 271
    • Nicoletti, I.1    Migliorati, G.2    Pagliacci, M.C.3    Riccardi, C.4
  • 44
    • 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.
    • (1990) J. Cell Biol. , vol.111 , pp. 2839
    • Wood, E.R.1    Earnshaw, W.C.2
  • 46
    • 0030785790 scopus 로고    scopus 로고
    • The central executioner of apoptosis: Multiple links between protease activation and mitochondria in Fas/Apo-1/CD95 and ceramide-induced apoptosis
    • Susin, S. A., N. Zamzami, M. Castedo, E. Daugas, H.-G. Wang, S. Geley, F. Fassy, J. Reed, and G. Kroemer. 1997. The central executioner of apoptosis: multiple links between protease activation and mitochondria in Fas/Apo-1/CD95 and ceramide-induced apoptosis. J. Exp. Med. 186:25.
    • (1997) J. Exp. Med. , vol.186 , pp. 25
    • Susin, S.A.1    Zamzami, N.2    Castedo, M.3    Daugas, E.4    Wang, H.-G.5    Geley, S.6    Fassy, F.7    Reed, J.8    Kroemer, G.9
  • 49
    • 0029116916 scopus 로고
    • The mitochondrial permeability transition
    • Zoratti, M., and I. Szabò. 1995. The mitochondrial permeability transition. Biochem. Biophys. Acta 1241:139.
    • (1995) Biochem. Biophys. Acta , vol.1241 , pp. 139
    • Zoratti, M.1    Szabò, I.2
  • 50
    • 0031032294 scopus 로고    scopus 로고
    • Bcl-2 and Bcl-XL antagonize the mitochondrial dysfunction preceding nuclear apoptosis induced by chemotherapeutic agents
    • Decaudin, D., S. Geley, T. Hirsch, M. Castedo, P. Marchetti, A. Macho, R. Kofler, and G. Kroemer. 1997. Bcl-2 and Bcl-XL antagonize the mitochondrial dysfunction preceding nuclear apoptosis induced by chemotherapeutic agents. Cancer Res. 57:62.
    • (1997) Cancer Res. , vol.57 , pp. 62
    • Decaudin, D.1    Geley, S.2    Hirsch, T.3    Castedo, M.4    Marchetti, P.5    Macho, A.6    Kofler, R.7    Kroemer, G.8
  • 53
    • 0030698810 scopus 로고    scopus 로고
    • The apoptosis-necrosis paradox: Apoptogenic proteases activated after mitochondrial permeability transition determine the mode of cell death
    • Hirsch, T., P. Marchetti, S. A. Susin, B. Dallaporta, N. Zamzami, I. Marzo, M. Geuskens, and G. Kroemer. 1997. The apoptosis-necrosis paradox: apoptogenic proteases activated after mitochondrial permeability transition determine the mode of cell death. Oncogene 15:1573.
    • (1997) Oncogene , vol.15 , pp. 1573
    • Hirsch, T.1    Marchetti, P.2    Susin, S.A.3    Dallaporta, B.4    Zamzami, N.5    Marzo, I.6    Geuskens, M.7    Kroemer, G.8
  • 54
    • 0028156903 scopus 로고
    • Separate metabolic pathways leading to DNA fragmentation and apoptotic chromatin condensation
    • Sun, D. Y., S. Jiang, L. M. Zheng, D. M. Ojcius, and J. D. E. Young. 1994. Separate metabolic pathways leading to DNA fragmentation and apoptotic chromatin condensation. J. Exp. Med. 179:559.
    • (1994) J. Exp. Med. , vol.179 , pp. 559
    • Sun, D.Y.1    Jiang, S.2    Zheng, L.M.3    Ojcius, D.M.4    Young, J.D.E.5
  • 58
    • 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.
    • (1997) Cell , vol.89 , pp. 175
    • Liu, X.1    Zou, H.2    Slaughter, C.3    Wang, X.4
  • 60
    • 0000707605 scopus 로고    scopus 로고
    • Cell shrinkage and apoptosis: A role for potassium and sodium ion efflux
    • McCarthy, J. V., and T. G. Cotter. 1997. Cell shrinkage and apoptosis: a role for potassium and sodium ion efflux. Cell Death Differ. 4:756.
    • (1997) Cell Death Differ. , vol.4 , pp. 756
    • McCarthy, J.V.1    Cotter, T.G.2
  • 62
    • 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.
    • (1997) Cell , vol.90 , pp. 405
    • Zhou, H.1    Henzel, W.J.2    Liu, X.3    Lutschg, A.4    Wang, X.5


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