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Volumn 1773, Issue 10, 2007, Pages 1546-1557

Cystein cathepsin and Hsp90 activities determine the balance between apoptotic and necrotic cell death pathways in caspase-compromised U937 cells

Author keywords

Apoptosis; Caspase independent; Cathepsin; Heat shock protein 90 kDa; Necrosis; Staurosporine

Indexed keywords

BENZYLOXYCARBONYLVALYLALANYLASPARTYL FLUOROMETHYL KETONE; CASPASE; CATHEPSIN; GELDANAMYCIN; HEAT SHOCK PROTEIN 90; HYDROGEN PEROXIDE; STAUROSPORINE;

EID: 34848838563     PISSN: 01674889     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamcr.2007.07.003     Document Type: Article
Times cited : (6)

References (65)
  • 3
    • 1642419553 scopus 로고    scopus 로고
    • Geldanamycin, an inhibitor of the chaperone activity of HSP90, induces MAPK-independent cell cycle arrest
    • Bedin M., Gaben A.M., Saucier C., and Mester J. Geldanamycin, an inhibitor of the chaperone activity of HSP90, induces MAPK-independent cell cycle arrest. Int. J. Cancer 109 (2004) 643-652
    • (2004) Int. J. Cancer , vol.109 , pp. 643-652
    • Bedin, M.1    Gaben, A.M.2    Saucier, C.3    Mester, J.4
  • 5
    • 0344431242 scopus 로고    scopus 로고
    • U937 apoptotic cell death by nitric oxide: Bcl-2 downregulation and caspase activation
    • Brockhaus F., and Brune B. U937 apoptotic cell death by nitric oxide: Bcl-2 downregulation and caspase activation. Exp. Cell Res. 238 (1998) 33-41
    • (1998) Exp. Cell Res. , vol.238 , pp. 33-41
    • Brockhaus, F.1    Brune, B.2
  • 6
    • 0042665423 scopus 로고    scopus 로고
    • Nitric oxide: NO apoptosis or turning it ON?
    • Brune B. Nitric oxide: NO apoptosis or turning it ON?. Cell Death Differ. 10 (2003) 864-869
    • (2003) Cell Death Differ. , vol.10 , pp. 864-869
    • Brune, B.1
  • 7
    • 0030757986 scopus 로고    scopus 로고
    • Photo-oxidative disruption of lysosomal membranes causes apoptosis of cultured human fibroblasts
    • Brunk U.T., Dalen H., Roberg K., and Hellquist H.B. Photo-oxidative disruption of lysosomal membranes causes apoptosis of cultured human fibroblasts. Free Radic. Biol. Med. 23 (1997) 616-626
    • (1997) Free Radic. Biol. Med. , vol.23 , pp. 616-626
    • Brunk, U.T.1    Dalen, H.2    Roberg, K.3    Hellquist, H.B.4
  • 8
    • 0036799548 scopus 로고    scopus 로고
    • Biphasic translocation of Bax to mitochondria
    • Capano M., and Crompton M. Biphasic translocation of Bax to mitochondria. Biochem. J. 367 (2002) 169-178
    • (2002) Biochem. J. , vol.367 , pp. 169-178
    • Capano, M.1    Crompton, M.2
  • 10
    • 0033910983 scopus 로고    scopus 로고
    • Analysis of apoptotic cells by flow and laser scanning cytometry
    • Darzynkiewicz Z., and Bedner E. Analysis of apoptotic cells by flow and laser scanning cytometry. Methods Enzymol. 322 (2000) 18-39
    • (2000) Methods Enzymol. , vol.322 , pp. 18-39
    • Darzynkiewicz, Z.1    Bedner, E.2
  • 11
    • 0031036984 scopus 로고    scopus 로고
    • Cytometry in cell necrobiology: analysis of apoptosis and accidental cell death (necrosis)
    • Darzynkiewicz Z., Juan G., Li X., Gorczyca W., Murakami T., and Traganos F. Cytometry in cell necrobiology: analysis of apoptosis and accidental cell death (necrosis). Cytometry 27 (1997) 1-20
    • (1997) Cytometry , vol.27 , pp. 1-20
    • Darzynkiewicz, Z.1    Juan, G.2    Li, X.3    Gorczyca, W.4    Murakami, T.5    Traganos, F.6
  • 13
    • 8844244753 scopus 로고    scopus 로고
    • Inhibitor of apoptosis proteins: new therapeutic targets in hematological cancer?
    • de Graaf A.O., de Witte T., and Jansen J.H. Inhibitor of apoptosis proteins: new therapeutic targets in hematological cancer?. Leukemia 18 (2004) 1751-1759
    • (2004) Leukemia , vol.18 , pp. 1751-1759
    • de Graaf, A.O.1    de Witte, T.2    Jansen, J.H.3
  • 15
    • 0036839331 scopus 로고    scopus 로고
    • Caspase-independent phosphatidylserine exposure during apoptosis of primary T lymphocytes
    • Ferraro-Peyret C., Quemeneur L., Flacher M., Revillard J.P., and Genestier L. Caspase-independent phosphatidylserine exposure during apoptosis of primary T lymphocytes. J. Immunol. 169 (2002) 4805-4810
    • (2002) J. Immunol. , vol.169 , pp. 4805-4810
    • Ferraro-Peyret, C.1    Quemeneur, L.2    Flacher, M.3    Revillard, J.P.4    Genestier, L.5
  • 16
    • 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. Biochim. Biophys. Acta 1757 (2006) 1371-1387
    • (2006) Biochim. Biophys. Acta , vol.1757 , pp. 1371-1387
    • Festjens, N.1    Vanden Berghe, T.2    Vandenabeele, P.3
  • 17
    • 0037131352 scopus 로고    scopus 로고
    • Cathepsin B mediates tumor necrosis factor-induced arachidonic acid release in tumor cells
    • Foghsgaard L., Lademann U., Wissing D., Poulsen B., and Jaattela M. Cathepsin B mediates tumor necrosis factor-induced arachidonic acid release in tumor cells. J. Biol. Chem. 277 (2002) 39499-39506
    • (2002) J. Biol. Chem. , vol.277 , pp. 39499-39506
    • Foghsgaard, L.1    Lademann, U.2    Wissing, D.3    Poulsen, B.4    Jaattela, M.5
  • 20
    • 0034949086 scopus 로고    scopus 로고
    • Characterization of the necrotic cleavage of poly(ADP-ribose) polymerase (PARP-1): implication of lysosomal proteases
    • Gobeil S., Boucher C.C., Nadeau D., and Poirier G.G. Characterization of the necrotic cleavage of poly(ADP-ribose) polymerase (PARP-1): implication of lysosomal proteases. Cell Death Differ. 8 (2001) 588-594
    • (2001) Cell Death Differ. , vol.8 , pp. 588-594
    • Gobeil, S.1    Boucher, C.C.2    Nadeau, D.3    Poirier, G.G.4
  • 21
    • 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
  • 22
    • 0028323164 scopus 로고
    • A selective procedure for DNA extraction from apoptotic cells applicable for gel electrophoresis and flow cytometry
    • Gong J., Traganos F., and Darzynkiewicz Z. A selective procedure for DNA extraction from apoptotic cells applicable for gel electrophoresis and flow cytometry. Anal. Biochem. 218 (1994) 314-319
    • (1994) Anal. Biochem. , vol.218 , pp. 314-319
    • Gong, J.1    Traganos, F.2    Darzynkiewicz, Z.3
  • 23
    • 0037308679 scopus 로고    scopus 로고
    • Activity and subcellular distribution of cathepsins in primary human monocytes
    • Greiner A., Lautwein A., Overkleeft H.S., Weber E., and Driessen C. Activity and subcellular distribution of cathepsins in primary human monocytes. J. Leukoc. Biol. 73 (2003) 235-242
    • (2003) J. Leukoc. Biol. , vol.73 , pp. 235-242
    • Greiner, A.1    Lautwein, A.2    Overkleeft, H.S.3    Weber, E.4    Driessen, C.5
  • 24
    • 0036304261 scopus 로고    scopus 로고
    • Mode of cell death after acetaminophen overdose in mice: apoptosis or oncotic necrosis?
    • Gujral J.S., Knight T.R., Farhood A., Bajt M.L., and Jaeschke H. Mode of cell death after acetaminophen overdose in mice: apoptosis or oncotic necrosis?. Toxicol. Sci. 67 (2002) 322-328
    • (2002) Toxicol. Sci. , vol.67 , pp. 322-328
    • Gujral, J.S.1    Knight, T.R.2    Farhood, A.3    Bajt, M.L.4    Jaeschke, H.5
  • 25
    • 12244277466 scopus 로고    scopus 로고
    • Caspase-dependent initiation of apoptosis and necrosis by the Fas receptor in lymphoid cells: onset of necrosis is associated with delayed ceramide increase
    • Hetz C.A., Hunn M., Rojas P., Torres V., Leyton L., and Quest A.F. Caspase-dependent initiation of apoptosis and necrosis by the Fas receptor in lymphoid cells: onset of necrosis is associated with delayed ceramide increase. J. Cell Sci. 115 (2002) 4671-4683
    • (2002) J. Cell Sci. , vol.115 , pp. 4671-4683
    • Hetz, C.A.1    Hunn, M.2    Rojas, P.3    Torres, V.4    Leyton, L.5    Quest, A.F.6
  • 28
    • 0038731167 scopus 로고    scopus 로고
    • Caspase-independent cell death in T lymphocytes
    • Jaattela M., and Tschopp J. Caspase-independent cell death in T lymphocytes. Nat. Immunol. 4 (2003) 416-423
    • (2003) Nat. Immunol. , vol.4 , pp. 416-423
    • Jaattela, M.1    Tschopp, J.2
  • 29
    • 28944447430 scopus 로고    scopus 로고
    • PIDD mediates NF-kappaB activation in response to DNA damage
    • Janssens S., Tinel A., Lippens S., and Tschopp J. PIDD mediates NF-kappaB activation in response to DNA damage. Cell 123 (2005) 1079-1092
    • (2005) Cell , vol.123 , pp. 1079-1092
    • Janssens, S.1    Tinel, A.2    Lippens, S.3    Tschopp, J.4
  • 30
    • 0036668520 scopus 로고    scopus 로고
    • Proteomic analysis of human lysosomes: application to monocytic and breast cancer cells
    • Journet A., Chapel A., Kieffer S., Roux F., and Garin J. Proteomic analysis of human lysosomes: application to monocytic and breast cancer cells. Proteomics 2 (2002) 1026-1040
    • (2002) Proteomics , vol.2 , pp. 1026-1040
    • Journet, A.1    Chapel, A.2    Kieffer, S.3    Roux, F.4    Garin, J.5
  • 31
    • 0036715377 scopus 로고    scopus 로고
    • Tipping the balance between necrosis and apoptosis in human and murine cells treated with interferon and dsRNA
    • Kalai M., Van Loo G., Vanden Berghe T., Meeus A., Burm W., Saelens X., and Vandenabeele P. Tipping the balance between necrosis and apoptosis in human and murine cells treated with interferon and dsRNA. Cell Death Differ. 9 (2002) 981-994
    • (2002) Cell Death Differ. , vol.9 , pp. 981-994
    • Kalai, M.1    Van Loo, G.2    Vanden Berghe, T.3    Meeus, A.4    Burm, W.5    Saelens, X.6    Vandenabeele, P.7
  • 32
    • 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., Mol. Cell Biol. 2 (2001) 589-598
    • (2001) Nat. Rev., Mol. Cell Biol. , vol.2 , pp. 589-598
    • Leist, M.1    Jaattela, M.2
  • 33
    • 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
  • 34
    • 0035811496 scopus 로고    scopus 로고
    • Endonuclease G is an apoptotic DNase when released from mitochondria
    • Li L.Y., Luo X., and Wang X. Endonuclease G is an apoptotic DNase when released from mitochondria. Nature 412 (2001) 95-99
    • (2001) Nature , vol.412 , pp. 95-99
    • Li, L.Y.1    Luo, X.2    Wang, X.3
  • 35
    • 0034712259 scopus 로고    scopus 로고
    • Cleavage of Poly(ADP-ribose) polymerase measured in situ in individual cells: relationship to DNA fragmentation and cell cycle position during apoptosis
    • Li X., and Darzynkiewicz Z. Cleavage of Poly(ADP-ribose) polymerase measured in situ in individual cells: relationship to DNA fragmentation and cell cycle position during apoptosis. Exp. Cell Res. 255 (2000) 125-132
    • (2000) Exp. Cell Res. , vol.255 , pp. 125-132
    • Li, X.1    Darzynkiewicz, Z.2
  • 36
    • 9944245491 scopus 로고    scopus 로고
    • Cathepsin B-independent abrogation of cell death by CA-074-OMe upstream of lysosomal breakdown
    • Mihalik R., Imre G., Petak I., Szende B., and Kopper L. Cathepsin B-independent abrogation of cell death by CA-074-OMe upstream of lysosomal breakdown. Cell Death Differ. 11 (2004) 1357-1360
    • (2004) Cell Death Differ. , vol.11 , pp. 1357-1360
    • Mihalik, R.1    Imre, G.2    Petak, I.3    Szende, B.4    Kopper, L.5
  • 37
    • 0141794528 scopus 로고    scopus 로고
    • B cell receptor-mediated nuclear fragmentation proceeds in WEHI 231 cells in the absence of detectable DEVDase and FRase activity
    • Mlinaric-Rascan I., and Turk B. B cell receptor-mediated nuclear fragmentation proceeds in WEHI 231 cells in the absence of detectable DEVDase and FRase activity. FEBS Lett. 553 (2003) 51-55
    • (2003) FEBS Lett. , vol.553 , pp. 51-55
    • Mlinaric-Rascan, I.1    Turk, B.2
  • 38
    • 2342465589 scopus 로고    scopus 로고
    • Regulation of the apoptosis-necrosis switch
    • Nicotera P., and Melino G. Regulation of the apoptosis-necrosis switch. Oncogene 23 (2004) 2757-2765
    • (2004) Oncogene , vol.23 , pp. 2757-2765
    • Nicotera, P.1    Melino, G.2
  • 43
    • 0034705684 scopus 로고    scopus 로고
    • Changes in mitochondrial membrane potential during staurosporine-induced apoptosis in Jurkat cells
    • Scarlett J.L., Sheard P.W., Hughes G., Ledgerwood E.C., Ku H.H., and Murphy M.P. Changes in mitochondrial membrane potential during staurosporine-induced apoptosis in Jurkat cells. FEBS Lett. 475 (2000) 267-272
    • (2000) FEBS Lett. , vol.475 , pp. 267-272
    • Scarlett, J.L.1    Sheard, P.W.2    Hughes, G.3    Ledgerwood, E.C.4    Ku, H.H.5    Murphy, M.P.6
  • 45
    • 2242449760 scopus 로고    scopus 로고
    • The kinetics of translocation of Smac/DIABLO from the mitochondria to the cytosol in HeLa cells
    • Springs S.L., Diavolitsis V.M., Goodhouse J., and McLendon G.L. The kinetics of translocation of Smac/DIABLO from the mitochondria to the cytosol in HeLa cells. J. Biol. Chem. 277 (2002) 45715-45718
    • (2002) J. Biol. Chem. , vol.277 , pp. 45715-45718
    • Springs, S.L.1    Diavolitsis, V.M.2    Goodhouse, J.3    McLendon, G.L.4
  • 46
    • 0031005361 scopus 로고    scopus 로고
    • Crystal structure of an Hsp90-geldanamycin complex: targeting of a protein chaperone by an antitumor agent
    • Stebbins C.E., Russo A.A., Schneider C., Rosen N., Hartl F.U., and Pavletich N.P. Crystal structure of an Hsp90-geldanamycin complex: targeting of a protein chaperone by an antitumor agent. Cell 89 (1997) 239-250
    • (1997) Cell , vol.89 , pp. 239-250
    • Stebbins, C.E.1    Russo, A.A.2    Schneider, C.3    Rosen, N.4    Hartl, F.U.5    Pavletich, N.P.6
  • 48
    • 0037147147 scopus 로고    scopus 로고
    • Regulation of intracellular pH mediates Bax activation in HeLa cells treated with staurosporine or tumor necrosis factor-alpha
    • Tafani M., Cohn J.A., Karpinich N.O., Rothman R.J., Russo M.A., and Farber J.L. Regulation of intracellular pH mediates Bax activation in HeLa cells treated with staurosporine or tumor necrosis factor-alpha. J. Biol. Chem. 277 (2002) 49569-49576
    • (2002) J. Biol. Chem. , vol.277 , pp. 49569-49576
    • Tafani, M.1    Cohn, J.A.2    Karpinich, N.O.3    Rothman, R.J.4    Russo, M.A.5    Farber, J.L.6
  • 49
    • 0035866785 scopus 로고    scopus 로고
    • Induction of the mitochondrial permeability transition mediates the killing of HeLa cells by staurosporine
    • Tafani M., Minchenko D.A., Serroni A., and Farber J.L. Induction of the mitochondrial permeability transition mediates the killing of HeLa cells by staurosporine. Cancer Res. 61 (2001) 2459-2466
    • (2001) Cancer Res. , vol.61 , pp. 2459-2466
    • Tafani, M.1    Minchenko, D.A.2    Serroni, A.3    Farber, J.L.4
  • 52
    • 33846219997 scopus 로고    scopus 로고
    • Autoproteolysis of PIDD marks the bifurcation between pro-death caspase-2 and pro-survival NF-kappaB pathway
    • Tinel A., Janssens S., Lippens S., Cuenin S., Logette E., Jaccard B., Quadroni M., and Tschopp J. Autoproteolysis of PIDD marks the bifurcation between pro-death caspase-2 and pro-survival NF-kappaB pathway. EMBO J. 26 (2007) 197-208
    • (2007) EMBO J. , vol.26 , pp. 197-208
    • Tinel, A.1    Janssens, S.2    Lippens, S.3    Cuenin, S.4    Logette, E.5    Jaccard, B.6    Quadroni, M.7    Tschopp, J.8
  • 53
    • 2442453730 scopus 로고    scopus 로고
    • The PIDDosome, a protein complex implicated in activation of caspase-2 in response to genotoxic stress
    • Tinel A., and Tschopp J. The PIDDosome, a protein complex implicated in activation of caspase-2 in response to genotoxic stress. Science 304 (2004) 843-846
    • (2004) Science , vol.304 , pp. 843-846
    • Tinel, A.1    Tschopp, J.2
  • 54
    • 0028708948 scopus 로고
    • Lysosomal proton pump activity: supravital cell staining with acridine orange differentiates leukocyte subpopulations
    • Traganos F., and Darzynkiewicz Z. Lysosomal proton pump activity: supravital cell staining with acridine orange differentiates leukocyte subpopulations. Methods Cell Biol. 41 (1994) 185-194
    • (1994) Methods Cell Biol. , vol.41 , pp. 185-194
    • Traganos, F.1    Darzynkiewicz, Z.2
  • 55
    • 13644270245 scopus 로고    scopus 로고
    • Proteasome inhibition protects HT22 neuronal cells from oxidative glutamate toxicity
    • van Leyen K., Siddiq A., Ratan R.R., and Lo E.H. Proteasome inhibition protects HT22 neuronal cells from oxidative glutamate toxicity. J. Neurochem. 92 (2005) 824-830
    • (2005) J. Neurochem. , vol.92 , pp. 824-830
    • van Leyen, K.1    Siddiq, A.2    Ratan, R.R.3    Lo, E.H.4
  • 60
    • 33744462507 scopus 로고    scopus 로고
    • Activation of the transient receptor potential M2 channel and poly(ADP-ribose) polymerase is involved in oxidative stress-induced cardiomyocyte death
    • Yang K.T., Chang W.L., Yang P.C., Chien C.L., Lai M.S., Su M.J., and Wu M.L. Activation of the transient receptor potential M2 channel and poly(ADP-ribose) polymerase is involved in oxidative stress-induced cardiomyocyte death. Cell Death Differ. 13 (2006) 1815-1826
    • (2006) Cell Death Differ. , vol.13 , pp. 1815-1826
    • Yang, K.T.1    Chang, W.L.2    Yang, P.C.3    Chien, C.L.4    Lai, M.S.5    Su, M.J.6    Wu, M.L.7
  • 61
    • 33744959426 scopus 로고    scopus 로고
    • PS-341 (bortezomib) induces lysosomal cathepsin B release and a caspase-2-dependent mitochondrial permeabilization and apoptosis in human pancreatic cancer cells
    • Yeung B.H., Huang D.C., and Sinicrope F.A. PS-341 (bortezomib) induces lysosomal cathepsin B release and a caspase-2-dependent mitochondrial permeabilization and apoptosis in human pancreatic cancer cells. J. Biol. Chem. 281 (2006) 11923-11932
    • (2006) J. Biol. Chem. , vol.281 , pp. 11923-11932
    • Yeung, B.H.1    Huang, D.C.2    Sinicrope, F.A.3
  • 62
    • 4444372444 scopus 로고    scopus 로고
    • Staurosporine induces apoptosis of melanoma by both caspase-dependent and -independent apoptotic pathways
    • Zhang X.D., Gillespie S.K., and Hersey P. Staurosporine induces apoptosis of melanoma by both caspase-dependent and -independent apoptotic pathways. Mol. Cancer Ther. 3 (2004) 187-197
    • (2004) Mol. Cancer Ther. , vol.3 , pp. 187-197
    • Zhang, X.D.1    Gillespie, S.K.2    Hersey, P.3
  • 63
    • 14644403687 scopus 로고    scopus 로고
    • Nitric oxide inhibits caspase activation and apoptotic morphology but does not rescue neuronal death
    • Zhou P., Qian L., and Iadecola C. Nitric oxide inhibits caspase activation and apoptotic morphology but does not rescue neuronal death. J. Cereb. Blood Flow Metab. 25 (2005) 348-357
    • (2005) J. Cereb. Blood Flow Metab. , vol.25 , pp. 348-357
    • Zhou, P.1    Qian, L.2    Iadecola, C.3
  • 64
    • 0035876483 scopus 로고    scopus 로고
    • BH3-only proteins that bind pro-survival Bcl-2 family members fail to induce apoptosis in the absence of Bax and Bak
    • Zong W.X., Lindsten T., Ross A.J., MacGregor G.R., and Thompson C.B. BH3-only proteins that bind pro-survival Bcl-2 family members fail to induce apoptosis in the absence of Bax and Bak. Genes Dev. 15 (2001) 1481-1486
    • (2001) Genes Dev. , vol.15 , pp. 1481-1486
    • Zong, W.X.1    Lindsten, T.2    Ross, A.J.3    MacGregor, G.R.4    Thompson, C.B.5
  • 65
    • 0033596980 scopus 로고    scopus 로고
    • An APAF-1.cytochrome c multimeric complex is a functional apoptosome that activates procaspase-9
    • Zou H., Li Y., Liu X., and Wang X. An APAF-1.cytochrome c multimeric complex is a functional apoptosome that activates procaspase-9. J. Biol. Chem. 274 (1999) 11549-11556
    • (1999) J. Biol. Chem. , vol.274 , pp. 11549-11556
    • Zou, H.1    Li, Y.2    Liu, X.3    Wang, X.4


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