메뉴 건너뛰기




Volumn 315, Issue 1, 2009, Pages 26-38

Necrotic cell death: From reversible mitochondrial uncoupling to irreversible lysosomal permeabilization

Author keywords

Dictyostelium; Lysosomes; Mitochondria; Necrotic cell death

Indexed keywords

ACRIDINE; CATHEPSIN B; CYCLIC AMP; DEXTRAN; DIFFERENTIATION INDUCING FACTOR;

EID: 56949085541     PISSN: 00144827     EISSN: 10902422     Source Type: Journal    
DOI: 10.1016/j.yexcr.2008.09.028     Document Type: Article
Times cited : (26)

References (67)
  • 2
    • 0035433420 scopus 로고    scopus 로고
    • Four deaths and a funeral: from caspases to alternative mechanisms
    • Leist M., and Jaattela M. Four deaths and a funeral: from caspases to alternative mechanisms. Nat. Rev. 2 (2001) 589-598
    • (2001) Nat. Rev. , vol.2 , pp. 589-598
    • Leist, M.1    Jaattela, M.2
  • 3
    • 0141884305 scopus 로고    scopus 로고
    • Diversity in the mechanisms of neuronal cell death
    • Yuan J., Lipinski M., and Degterev A. Diversity in the mechanisms of neuronal cell death. Neuron 40 (2003) 401-413
    • (2003) Neuron , vol.40 , pp. 401-413
    • Yuan, J.1    Lipinski, M.2    Degterev, A.3
  • 4
    • 29944438881 scopus 로고    scopus 로고
    • Necrotic death as a cell fate
    • Zong W.X., and Thompson C.B. Necrotic death as a cell fate. Genes Dev. 20 (2006) 1-15
    • (2006) Genes Dev. , vol.20 , pp. 1-15
    • Zong, W.X.1    Thompson, C.B.2
  • 5
    • 33749178260 scopus 로고    scopus 로고
    • Necrosis, a well-orchestrated form of cell demise: signalling cascades, important mediators and concomitant immune response
    • Festjens N., Vanden Berghe T., and Vandenabeele P. Necrosis, a well-orchestrated form of cell demise: signalling cascades, important mediators and concomitant immune response. Biochimi. Biophys. Acta 1757 (2006) 1371-1387
    • (2006) Biochimi. Biophys. Acta , vol.1757 , pp. 1371-1387
    • Festjens, N.1    Vanden Berghe, T.2    Vandenabeele, P.3
  • 6
    • 33846018602 scopus 로고    scopus 로고
    • Cell death by necrosis: towards a molecular definition
    • Golstein P., and Kroemer G. Cell death by necrosis: towards a molecular definition. Trends Biochem. Sci. 32 (2007) 37-43
    • (2007) Trends Biochem. Sci. , vol.32 , pp. 37-43
    • Golstein, P.1    Kroemer, G.2
  • 8
    • 0043238675 scopus 로고    scopus 로고
    • The biochemistry of neuronal necrosis: rogue biology?
    • Syntichaki P., and Tavernarakis N. The biochemistry of neuronal necrosis: rogue biology?. Nat. Rev. Neurosci. 4 (2003) 672-684
    • (2003) Nat. Rev. Neurosci. , vol.4 , pp. 672-684
    • Syntichaki, P.1    Tavernarakis, N.2
  • 9
    • 33646081999 scopus 로고    scopus 로고
    • Lysosomal biogenesis and function is critical for necrotic cell death in Caenorhabditis elegans
    • Artal-Sanz M., Samara C., Syntichaki P., and Tavernarakis N. Lysosomal biogenesis and function is critical for necrotic cell death in Caenorhabditis elegans. J. Cell Biol. 173 (2006) 231-239
    • (2006) J. Cell Biol. , vol.173 , pp. 231-239
    • Artal-Sanz, M.1    Samara, C.2    Syntichaki, P.3    Tavernarakis, N.4
  • 10
    • 6344287496 scopus 로고    scopus 로고
    • Cyclophilin-D promotes the mitochondrial permeability transition but has opposite effects on apoptosis and necrosis
    • Li Y., Johnson N., Capano M., Edwards M., and Crompton M. Cyclophilin-D promotes the mitochondrial permeability transition but has opposite effects on apoptosis and necrosis. Biochem. J. 383 (2004) 101-109
    • (2004) Biochem. J. , vol.383 , pp. 101-109
    • Li, Y.1    Johnson, N.2    Capano, M.3    Edwards, M.4    Crompton, M.5
  • 12
  • 15
    • 19944417921 scopus 로고    scopus 로고
    • Inhibition of hydrogen peroxide-induced necrotic cell death with 3-amino-2-indolylmaleimide derivatives
    • Dodo K., Katoh M., Shimizu T., Takahashi M., and Sodeoka M. Inhibition of hydrogen peroxide-induced necrotic cell death with 3-amino-2-indolylmaleimide derivatives. Bioorg. Med. Chem. Lett. 15 (2005) 3114-3118
    • (2005) Bioorg. Med. Chem. Lett. , vol.15 , pp. 3114-3118
    • Dodo, K.1    Katoh, M.2    Shimizu, T.3    Takahashi, M.4    Sodeoka, M.5
  • 17
    • 0023063763 scopus 로고
    • Cell differentiation in monolayers and the investigation of slime mold morphogens
    • Kay R.R. Cell differentiation in monolayers and the investigation of slime mold morphogens. Methods Cell Biol. 28 (1987) 433-448
    • (1987) Methods Cell Biol. , vol.28 , pp. 433-448
    • Kay, R.R.1
  • 20
    • 39449105425 scopus 로고    scopus 로고
    • The IP3 receptor is required to signal autophagic cell death
    • Lam D., Kosta A., Luciani M.F., and Golstein P. The IP3 receptor is required to signal autophagic cell death. Mol. Biol. Cell. 19 (2008) 691-700
    • (2008) Mol. Biol. Cell. , vol.19 , pp. 691-700
    • Lam, D.1    Kosta, A.2    Luciani, M.F.3    Golstein, P.4
  • 21
    • 1842577042 scopus 로고    scopus 로고
    • Dictyostelium macroautophagy mutants vary in the severity of their developmental defects
    • Otto G.P., Wu M.Y., Kazgan N., Anderson O.R., and Kessin R.H. Dictyostelium macroautophagy mutants vary in the severity of their developmental defects. J. Biol. Chem. 279 (2004) 15621-15629
    • (2004) J. Biol. Chem. , vol.279 , pp. 15621-15629
    • Otto, G.P.1    Wu, M.Y.2    Kazgan, N.3    Anderson, O.R.4    Kessin, R.H.5
  • 26
    • 0033539141 scopus 로고    scopus 로고
    • Interdigital cell death can occur through a necrotic and caspase-independent pathway
    • Chautan C., Chazal G., Cecconi F., Gruss P., and Golstein P. Interdigital cell death can occur through a necrotic and caspase-independent pathway. Curr. Biol. 9 (1999) 967-970
    • (1999) Curr. Biol. , vol.9 , pp. 967-970
    • Chautan, C.1    Chazal, G.2    Cecconi, F.3    Gruss, P.4    Golstein, P.5
  • 27
    • 0035399637 scopus 로고    scopus 로고
    • Programmed cell death of developing mammalian neurons after genetic deletion of caspases
    • Oppenheim R.W., Flavell R.A., Vinsant S., Prevette D., Kuan C.Y., and Rakic P. Programmed cell death of developing mammalian neurons after genetic deletion of caspases. J. Neurosci. 21 (2001) 4752-4760
    • (2001) J. Neurosci. , vol.21 , pp. 4752-4760
    • Oppenheim, R.W.1    Flavell, R.A.2    Vinsant, S.3    Prevette, D.4    Kuan, C.Y.5    Rakic, P.6
  • 28
    • 33846630384 scopus 로고    scopus 로고
    • BIM regulates apoptosis during mammary ductal morphogenesis, and its absence reveals alternative cell death mechanisms
    • Mailleux A.A., Overholtzer M., Schmelzle T., Bouillet P., Strasser A., and Brugge J.S. BIM regulates apoptosis during mammary ductal morphogenesis, and its absence reveals alternative cell death mechanisms. Dev. Cell 12 (2007) 221-234
    • (2007) Dev. Cell , vol.12 , pp. 221-234
    • Mailleux, A.A.1    Overholtzer, M.2    Schmelzle, T.3    Bouillet, P.4    Strasser, A.5    Brugge, J.S.6
  • 30
    • 33750143079 scopus 로고    scopus 로고
    • The secret lives of Dictyostelium
    • Kessin R.H. The secret lives of Dictyostelium. Methods Mol. Biol. 346 (2006) 3-14
    • (2006) Methods Mol. Biol. , vol.346 , pp. 3-14
    • Kessin, R.H.1
  • 31
    • 33750118142 scopus 로고    scopus 로고
    • The genome of Dictyostelium discoideum
    • Kuspa A., and Loomis W.F. The genome of Dictyostelium discoideum. Methods Mol. Biol. 346 (2006) 15-30
    • (2006) Methods Mol. Biol. , vol.346 , pp. 15-30
    • Kuspa, A.1    Loomis, W.F.2
  • 33
    • 34948882797 scopus 로고    scopus 로고
    • Autophagic or necrotic cell death in the absence of caspase and bcl-2 family members
    • Lam D., Levraud J.P., Luciani M.F., and Golstein P. Autophagic or necrotic cell death in the absence of caspase and bcl-2 family members. Biochem. Biophys. Res. Commun. 363 (2007) 536-541
    • (2007) Biochem. Biophys. Res. Commun. , vol.363 , pp. 536-541
    • Lam, D.1    Levraud, J.P.2    Luciani, M.F.3    Golstein, P.4
  • 34
    • 0023073916 scopus 로고
    • Cultivation and synchronous morphogenesis of Dictyostelium under controlled experimental conditions
    • Spudich J.A. (Ed), Harcourt Brace Jovanovich, New York
    • Sussman M. Cultivation and synchronous morphogenesis of Dictyostelium under controlled experimental conditions. In: Spudich J.A. (Ed). Methods in Cell Biology (1987), Harcourt Brace Jovanovich, New York 9-29
    • (1987) Methods in Cell Biology , pp. 9-29
    • Sussman, M.1
  • 36
    • 0034641135 scopus 로고    scopus 로고
    • Tumor necrosis factor induces hyperphosphorylation of kinesin light chain and inhibits kinesin-mediated transport of mitochondria
    • De Vos K., Severin F., Van Herreweghe F., Vancompernolle K., Goossens V., Hyman A., and Grooten J. Tumor necrosis factor induces hyperphosphorylation of kinesin light chain and inhibits kinesin-mediated transport of mitochondria. J. Cell Biol. 149 (2000) 1207-1214
    • (2000) J. Cell Biol. , vol.149 , pp. 1207-1214
    • De Vos, K.1    Severin, F.2    Van Herreweghe, F.3    Vancompernolle, K.4    Goossens, V.5    Hyman, A.6    Grooten, J.7
  • 37
    • 0027723051 scopus 로고
    • Microtubule-dependent control of cell shape and pseudopodial activity is inhibited by the antibody to kinesin motor domain
    • Rodionov V.I., Gyoeva F.K., Tanaka E., Bershadsky A.D., Vasiliev J.M., and Gelfand V.I. Microtubule-dependent control of cell shape and pseudopodial activity is inhibited by the antibody to kinesin motor domain. J. Cell Biol. 123 (1993) 1811-1820
    • (1993) J. Cell Biol. , vol.123 , pp. 1811-1820
    • Rodionov, V.I.1    Gyoeva, F.K.2    Tanaka, E.3    Bershadsky, A.D.4    Vasiliev, J.M.5    Gelfand, V.I.6
  • 38
    • 0032568790 scopus 로고    scopus 로고
    • Targeted disruption of mouse conventional kinesin heavy chain, kif5B, results in abnormal perinuclear clustering of mitochondria
    • Tanaka Y., Kanai Y., Okada Y., Nonaka S., Takeda S., Harada A., and Hirokawa N. Targeted disruption of mouse conventional kinesin heavy chain, kif5B, results in abnormal perinuclear clustering of mitochondria. Cell 93 (1998) 1147-1158
    • (1998) Cell , vol.93 , pp. 1147-1158
    • Tanaka, Y.1    Kanai, Y.2    Okada, Y.3    Nonaka, S.4    Takeda, S.5    Harada, A.6    Hirokawa, N.7
  • 40
    • 0035366499 scopus 로고    scopus 로고
    • Apoptosis induced by exposure to a low steady-state concentration of H2O2 is a consequence of lysosomal rupture
    • Antunes F., Cadenas E., and Brunk U.T. Apoptosis induced by exposure to a low steady-state concentration of H2O2 is a consequence of lysosomal rupture. Biochem. J. 356 (2001) 549-555
    • (2001) Biochem. J. , vol.356 , pp. 549-555
    • Antunes, F.1    Cadenas, E.2    Brunk, U.T.3
  • 41
    • 0029017037 scopus 로고
    • Mitochondrial DNA replication but no nuclear DNA replication during development of Dictyostelium
    • Shaulsky G., and Loomis W.F. Mitochondrial DNA replication but no nuclear DNA replication during development of Dictyostelium. Proc. Natl. Acad. Sci. U. S. A. 92 (1995) 5660-5663
    • (1995) Proc. Natl. Acad. Sci. U. S. A. , vol.92 , pp. 5660-5663
    • Shaulsky, G.1    Loomis, W.F.2
  • 43
    • 33747388358 scopus 로고    scopus 로고
    • Lysosomal system pathways: genes to neurodegeneration in Alzheimer's disease
    • Nixon R.A., and Cataldo A.M. Lysosomal system pathways: genes to neurodegeneration in Alzheimer's disease. J. Alzheimers Dis. 9 (2006) 277-289
    • (2006) J. Alzheimers Dis. , vol.9 , pp. 277-289
    • Nixon, R.A.1    Cataldo, A.M.2
  • 44
    • 28544435485 scopus 로고    scopus 로고
    • Lysosomes and autophagy in cell death control
    • Kroemer G., and Jaattela M. Lysosomes and autophagy in cell death control. Nat. Rev. Cancer 5 (2005) 886-897
    • (2005) Nat. Rev. Cancer , vol.5 , pp. 886-897
    • Kroemer, G.1    Jaattela, M.2
  • 45
    • 33846702991 scopus 로고    scopus 로고
    • Autophagy, organelles and ageing
    • Terman A., Gustafsson B., and Brunk U.T. Autophagy, organelles and ageing. J. Pathol. 211 (2007) 134-143
    • (2007) J. Pathol. , vol.211 , pp. 134-143
    • Terman, A.1    Gustafsson, B.2    Brunk, U.T.3
  • 47
    • 0043234207 scopus 로고    scopus 로고
    • Cathepsin D triggers Bax activation, resulting in selective apoptosis-inducing factor (AIF) relocation in T lymphocytes entering the early commitment phase to apoptosis
    • Bidere N., Lorenzo H.K., Carmona S., Laforge M., Harper F., Dumont C., and Senik A. Cathepsin D triggers Bax activation, resulting in selective apoptosis-inducing factor (AIF) relocation in T lymphocytes entering the early commitment phase to apoptosis. J. Biol. Chem. 278 (2003) 31401-31411
    • (2003) J. Biol. Chem. , vol.278 , pp. 31401-31411
    • Bidere, N.1    Lorenzo, H.K.2    Carmona, S.3    Laforge, M.4    Harper, F.5    Dumont, C.6    Senik, A.7
  • 51
    • 28844490007 scopus 로고    scopus 로고
    • The lysosome-associated apoptosis-inducing protein containing the pleckstrin homology (PH) and FYVE domains (LAPF), representative of a novel family of PH and FYVE domain-containing proteins, induces caspase-independent apoptosis via the lysosomal-mitochondrial pathway
    • Chen W., Li N., Chen T., Han Y., Li C., Wang Y., He W., Zhang L., Wan T., and Cao X. The lysosome-associated apoptosis-inducing protein containing the pleckstrin homology (PH) and FYVE domains (LAPF), representative of a novel family of PH and FYVE domain-containing proteins, induces caspase-independent apoptosis via the lysosomal-mitochondrial pathway. J. Biol. Chem. 280 (2005) 40985-40995
    • (2005) J. Biol. Chem. , vol.280 , pp. 40985-40995
    • Chen, W.1    Li, N.2    Chen, T.3    Han, Y.4    Li, C.5    Wang, Y.6    He, W.7    Zhang, L.8    Wan, T.9    Cao, X.10
  • 52
    • 0033540289 scopus 로고    scopus 로고
    • Mitochondrial permeability transition and swelling can occur reversibly without inducing cell death in intact human cells
    • Minamikawa T., Williams D.A., Bowser D.N., and Nagley P. Mitochondrial permeability transition and swelling can occur reversibly without inducing cell death in intact human cells. Exp. Cell Res. 246 (1999) 26-37
    • (1999) Exp. Cell Res. , vol.246 , pp. 26-37
    • Minamikawa, T.1    Williams, D.A.2    Bowser, D.N.3    Nagley, P.4
  • 53
    • 33845996199 scopus 로고    scopus 로고
    • Link between mitochondria and NADPH oxidase 1 isozyme for the sustained production of reactive oxygen species and cell death
    • Lee S.B., Bae I.H., Bae Y.S., and Um H.D. Link between mitochondria and NADPH oxidase 1 isozyme for the sustained production of reactive oxygen species and cell death. J. Biol. Chem. 281 (2006) 36228-36235
    • (2006) J. Biol. Chem. , vol.281 , pp. 36228-36235
    • Lee, S.B.1    Bae, I.H.2    Bae, Y.S.3    Um, H.D.4
  • 54
    • 0029090167 scopus 로고
    • Direct evidence for tumor necrosis factor-induced mitochondrial reactive oxygen intermediates and their involvement in cytotoxicity
    • Goossens V., Grooten J., De Vos K., and Fiers W. Direct evidence for tumor necrosis factor-induced mitochondrial reactive oxygen intermediates and their involvement in cytotoxicity. Proc. Natl. Acad. Sci. U.S.A. 92 (1995) 8115-8119
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 8115-8119
    • Goossens, V.1    Grooten, J.2    De Vos, K.3    Fiers, W.4
  • 55
    • 0033576675 scopus 로고    scopus 로고
    • More than one way to die: apoptosis, necrosis and reactive oxygen damage
    • Fiers W., Beyaert R., Declercq W., and Vandenabeele P. More than one way to die: apoptosis, necrosis and reactive oxygen damage. Oncogene 18 (1999) 7719-7730
    • (1999) Oncogene , vol.18 , pp. 7719-7730
    • Fiers, W.1    Beyaert, R.2    Declercq, W.3    Vandenabeele, P.4
  • 56
    • 0036478970 scopus 로고    scopus 로고
    • Mitochondrial reactive oxygen species in cell death signaling
    • Fleury C., Mignotte B., and Vayssiere J.L. Mitochondrial reactive oxygen species in cell death signaling. Biochimie 84 (2002) 131-141
    • (2002) Biochimie , vol.84 , pp. 131-141
    • Fleury, C.1    Mignotte, B.2    Vayssiere, J.L.3
  • 59
    • 0034739734 scopus 로고    scopus 로고
    • Implication of cysteine proteases calpain, cathepsin and caspase in ischemic neuronal death of primates
    • Yamashima T. Implication of cysteine proteases calpain, cathepsin and caspase in ischemic neuronal death of primates. Prog. Neurobiol. 62 (2000) 273-295
    • (2000) Prog. Neurobiol. , vol.62 , pp. 273-295
    • Yamashima, T.1
  • 60
    • 3342900223 scopus 로고    scopus 로고
    • Ca2+-dependent proteases in ischemic neuronal death: a conserved 'calpain-cathepsin cascade' from nematodes to primates
    • Yamashima T. Ca2+-dependent proteases in ischemic neuronal death: a conserved 'calpain-cathepsin cascade' from nematodes to primates. Cell Calcium 36 (2004) 285-293
    • (2004) Cell Calcium , vol.36 , pp. 285-293
    • Yamashima, T.1
  • 61
    • 0242539781 scopus 로고    scopus 로고
    • Sustained calpain activation associated with lysosomal rupture executes necrosis of the postischemic CA1 neurons in primates
    • Yamashima T., Tonchev A.B., Tsukada T., Saido T.C., Imajoh-Ohmi S., Momoi T., and Kominami E. Sustained calpain activation associated with lysosomal rupture executes necrosis of the postischemic CA1 neurons in primates. Hippocampus 13 (2003) 791-800
    • (2003) Hippocampus , vol.13 , pp. 791-800
    • Yamashima, T.1    Tonchev, A.B.2    Tsukada, T.3    Saido, T.C.4    Imajoh-Ohmi, S.5    Momoi, T.6    Kominami, E.7
  • 62
    • 0037206901 scopus 로고    scopus 로고
    • Specific aspartyl and calpain proteases are required for neurodegeneration in C. elegans
    • Syntichaki P., Xu K., Driscoll M., and Tavernarakis N. Specific aspartyl and calpain proteases are required for neurodegeneration in C. elegans. Nature 419 (2002) 939-944
    • (2002) Nature , vol.419 , pp. 939-944
    • Syntichaki, P.1    Xu, K.2    Driscoll, M.3    Tavernarakis, N.4
  • 63
    • 0141539596 scopus 로고    scopus 로고
    • Calcium-dependent and aspartyl proteases in neurodegeneration and ageing in C. elegans
    • Samara C., and Tavernarakis N. Calcium-dependent and aspartyl proteases in neurodegeneration and ageing in C. elegans. Ageing Res. Rev. 2 (2003) 451-471
    • (2003) Ageing Res. Rev. , vol.2 , pp. 451-471
    • Samara, C.1    Tavernarakis, N.2
  • 64
    • 0030900980 scopus 로고    scopus 로고
    • Intracellular adenosine triphosphate (ATP) concentration: a switch in the decision between apoptosis and necrosis
    • Leist M., Single B., Castoldi A.F., Kuhnle S., and Nicotera P. Intracellular adenosine triphosphate (ATP) concentration: a switch in the decision between apoptosis and necrosis. J. Exp. Med. 185 (1997) 1481-1486
    • (1997) J. Exp. Med. , vol.185 , pp. 1481-1486
    • Leist, M.1    Single, B.2    Castoldi, A.F.3    Kuhnle, S.4    Nicotera, P.5
  • 65
    • 0030915587 scopus 로고    scopus 로고
    • Intracellular ATP levels determine cell death fate by apoptosis or necrosis
    • Eguchi Y., Shimizu S., and Tsujimoto Y. Intracellular ATP levels determine cell death fate by apoptosis or necrosis. Cancer Res. 57 (1997) 1835-1840
    • (1997) Cancer Res. , vol.57 , pp. 1835-1840
    • Eguchi, Y.1    Shimizu, S.2    Tsujimoto, Y.3
  • 66
  • 67
    • 0025950667 scopus 로고
    • Programmed cell death in the immune system
    • Cohen J.J. Programmed cell death in the immune system. Adv. Immunol. 50 (1991) 55-83
    • (1991) Adv. Immunol. , vol.50 , pp. 55-83
    • Cohen, J.J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.