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Volumn 92, Issue 9, 1998, Pages 3042-3049

Phosphorylated forms of activated caspases are present in cytosol from HL-60 cells during etoposide-induced apoptosis

Author keywords

[No Author keywords available]

Indexed keywords

ASPARTYLGLUTAMYLVALINYLASPARTYL 7 AMINO 4 TRIFLUOROMETHYLCOUMARIN; CASPASE; COUMARIN DERIVATIVE; CYSTEINE PROTEINASE; ETOPOSIDE; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE; PHOSPHATASE; PHOSPHOPROTEIN; PHOSPHORUS 32; UNCLASSIFIED DRUG;

EID: 0032211157     PISSN: 00064971     EISSN: None     Source Type: Journal    
DOI: 10.1182/blood.v92.9.3042     Document Type: Article
Times cited : (47)

References (63)
  • 1
    • 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 82:349, 1995
    • (1995) Cell , vol.82 , pp. 349
    • Martin, S.J.1    Green, D.R.2
  • 2
    • 0030892234 scopus 로고    scopus 로고
    • Apoptosis by death factor
    • Nagata S: Apoptosis by death factor. Cell 88:355, 1997
    • (1997) Cell , vol.88 , pp. 355
    • Nagata, S.1
  • 4
    • 0030715323 scopus 로고    scopus 로고
    • Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade
    • Li P, Nijhawan D, Budihardjo I, Sirnivasula SM, Ahmad M, Alnemri ES, Wang X: Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade. Cell 91:479, 1997
    • (1997) Cell , vol.91 , pp. 479
    • Li, P.1    Nijhawan, D.2    Budihardjo, I.3    Sirnivasula, S.M.4    Ahmad, M.5    Alnemri, E.S.6    Wang, X.7
  • 7
    • 0029961420 scopus 로고    scopus 로고
    • Role of protein kinase activity in apoptosis
    • Lavin MF, Watters D, Song Q: Role of protein kinase activity in apoptosis. Experientia 52:979, 1996
    • (1996) Experientia , vol.52 , pp. 979
    • Lavin, M.F.1    Watters, D.2    Song, Q.3
  • 8
    • 0030759279 scopus 로고    scopus 로고
    • Kinase cascades regulating entry into apoptosis
    • Anderson P: Kinase cascades regulating entry into apoptosis. Microbiol Mol Biol Rev 61:33, 1997
    • (1997) Microbiol Mol Biol Rev , vol.61 , pp. 33
    • Anderson, P.1
  • 9
    • 0032053709 scopus 로고    scopus 로고
    • Mechanisms and consequences of activation of protein kinase B/Akt
    • Downward J: Mechanisms and consequences of activation of protein kinase B/Akt. Curr Opin Cell Biol 10:262, 1998
    • (1998) Curr Opin Cell Biol , vol.10 , pp. 262
    • Downward, J.1
  • 16
    • 0028865539 scopus 로고
    • Involvement of stress-activated protein kinase in the cellular response to 1-beta-D-arabinofuranosylcytosine and other DNA-damaging agents
    • Saleem A, Datta R, Yuan ZM, Kharbanda S, Kufe D: Involvement of stress-activated protein kinase in the cellular response to 1-beta-D-arabinofuranosylcytosine and other DNA-damaging agents. Cell Growth Differ 6:1651, 1995
    • (1995) Cell Growth Differ , vol.6 , pp. 1651
    • Saleem, A.1    Datta, R.2    Yuan, Z.M.3    Kharbanda, S.4    Kufe, D.5
  • 17
    • 0031029911 scopus 로고    scopus 로고
    • Interleukin-6 inhibits Fas-induced apoptosis and stress-activated protein kinase activation in multiple myeloma cells
    • Chauhan D, Kharbanda S, Ogata A, Urashima M, Teoh G, Robertson M, Kufe DW, Anderson KC: Interleukin-6 inhibits Fas-induced apoptosis and stress-activated protein kinase activation in multiple myeloma cells. Blood 89:227, 1997
    • (1997) Blood , vol.89 , pp. 227
    • Chauhan, D.1    Kharbanda, S.2    Ogata, A.3    Urashima, M.4    Teoh, G.5    Robertson, M.6    Kufe, D.W.7    Anderson, K.C.8
  • 18
    • 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 53:3976, 1993
    • (1993) Cancer Res , vol.53 , pp. 3976
    • Kaufmann, S.H.1    Desnoyers, S.2    Ottaviano, Y.3    Davidson, N.E.4    Poirier, G.G.5
  • 20
    • 0031911792 scopus 로고    scopus 로고
    • ZIP kinase, a novel serine/threonine kinase which mediates apoptosis
    • Kawai T, Matsumoto M, Takeda K, Sanjo H, Akira S: ZIP kinase, a novel serine/threonine kinase which mediates apoptosis. Mol Cell Biol 18:1642, 1998
    • (1998) Mol Cell Biol , vol.18 , pp. 1642
    • Kawai, T.1    Matsumoto, M.2    Takeda, K.3    Sanjo, H.4    Akira, S.5
  • 21
    • 0028831202 scopus 로고
    • Identification of a novel serine/threonine kinase and a novel 15-kD protein as potential mediators of the γ interferon-induced cell death
    • Deiss LP, Feinstein E, Berissi H, Cohen O, Kimchi A: Identification of a novel serine/threonine kinase and a novel 15-kD protein as potential mediators of the γ interferon-induced cell death. Genes Dev 9:15, 1994
    • (1994) Genes Dev , vol.9 , pp. 15
    • Deiss, L.P.1    Feinstein, E.2    Berissi, H.3    Cohen, O.4    Kimchi, A.5
  • 22
    • 0029054725 scopus 로고
    • RIP: A novel protein containing a death domain that interacts with Fas/APO-I (CD95) in yeast and causes cell death
    • Stanger BZ, Leder P, Lee T-H, Kim E, Seed B: RIP: A novel protein containing a death domain that interacts with Fas/APO-I (CD95) in yeast and causes cell death. Cell 81:513, 1995
    • (1995) Cell , vol.81 , pp. 513
    • Stanger, B.Z.1    Leder, P.2    Lee, T.-H.3    Kim, E.4    Seed, B.5
  • 23
    • 0029949257 scopus 로고    scopus 로고
    • TNF-dependent recruitment of the protein kinase RIP to the TNF receptor-1 signaling complex
    • Hsu HL, Huang JN, Shu HB, Baichwal V, Goeddel DV: TNF-dependent recruitment of the protein kinase RIP to the TNF receptor-1 signaling complex. Immunity 4:387, 1996
    • (1996) Immunity , vol.4 , pp. 387
    • Hsu, H.L.1    Huang, J.N.2    Shu, H.B.3    Baichwal, V.4    Goeddel, D.V.5
  • 24
    • 0031021356 scopus 로고    scopus 로고
    • RAIDD is a new 'death' adaptor molecule
    • Duan H, Dixit VM: RAIDD is a new 'death' adaptor molecule. Nature 385:86, 1997
    • (1997) Nature , vol.385 , pp. 86
    • Duan, H.1    Dixit, V.M.2
  • 26
    • 0032479145 scopus 로고    scopus 로고
    • RIP2 is a novel NF-kappaB-activating and cell death-inducing kinase
    • McCarthy JV, Ni J, Dixit VM: RIP2 is a novel NF-kappaB-activating and cell death-inducing kinase. J Biol Chem 273:16968, 1998
    • (1998) J Biol Chem , vol.273 , pp. 16968
    • McCarthy, J.V.1    Ni, J.2    Dixit, V.M.3
  • 27
  • 30
    • 0032032270 scopus 로고    scopus 로고
    • Bcr-Abl exerts its antiapoptotic effect against diverse apoptotic stimuli through blockage of mitochondrial release of cytochrome C and activation of caspase-3
    • Amarante-Mendes GP, Naekyung-Kim C, Liu L, Huang Y, Perkins CL, Green DR, Bhalla K: Bcr-Abl exerts its antiapoptotic effect against diverse apoptotic stimuli through blockage of mitochondrial release of cytochrome C and activation of caspase-3. Blood 91:1700, 1998
    • (1998) Blood , vol.91 , pp. 1700
    • Amarante-Mendes, G.P.1    Naekyung-Kim, C.2    Liu, L.3    Huang, Y.4    Perkins, C.L.5    Green, D.R.6    Bhalla, K.7
  • 34
    • 0030913673 scopus 로고    scopus 로고
    • Matrix adhesion and ras transformation both activate a phosphoinositide 3-OH kinase and protein kinase B/Akt cellular survival pathway
    • Khwaja A, Rodriguez-Viciana P, Wennstrom S, Warne PH, Downward J: Matrix adhesion and ras transformation both activate a phosphoinositide 3-OH kinase and protein kinase B/Akt cellular survival pathway. EMBO J 16:2783, 1997
    • (1997) EMBO J , vol.16 , pp. 2783
    • Khwaja, A.1    Rodriguez-Viciana, P.2    Wennstrom, S.3    Warne, P.H.4    Downward, J.5
  • 35
    • 0030916669 scopus 로고    scopus 로고
    • The proto-oncogene Bcl-2 and its role in regulating apoptosis
    • Kroemer G: The proto-oncogene Bcl-2 and its role in regulating apoptosis. Nat Med 3:614, 1997
    • (1997) Nat Med , vol.3 , pp. 614
    • Kroemer, G.1
  • 36
    • 0030048476 scopus 로고    scopus 로고
    • Phosphorylation of Bcl-2 protein and association with p21Ras in Ras-induced apoptosis
    • Chen CY, Faller DV: Phosphorylation of Bcl-2 protein and association with p21Ras in Ras-induced apoptosis. J Biol Chem 271:2376, 1996
    • (1996) J Biol Chem , vol.271 , pp. 2376
    • Chen, C.Y.1    Faller, D.V.2
  • 37
    • 0030959304 scopus 로고    scopus 로고
    • Bcl-2 Phosphorylation required for anti-apoptosis function
    • Takahiko I, Xingming D, Carr B, May WS: Bcl-2 Phosphorylation required for anti-apoptosis function. J Biol Chem 272:11671, 1997
    • (1997) J Biol Chem , vol.272 , pp. 11671
    • Takahiko, I.1    Xingming, D.2    Carr, B.3    May, W.S.4
  • 39
    • 0030615086 scopus 로고    scopus 로고
    • Bcl-xL overexpression inhibits progression of molecular events leading to paclitaxel-induced apoptosis of human acute myeloid leukemia HL-60 cells
    • Ibrado AM, Liu L, Bhalla K: Bcl-xL overexpression inhibits progression of molecular events leading to paclitaxel-induced apoptosis of human acute myeloid leukemia HL-60 cells. Cancer Res 57:1109, 1997
    • (1997) Cancer Res , vol.57 , pp. 1109
    • Ibrado, A.M.1    Liu, L.2    Bhalla, K.3
  • 40
    • 0030702123 scopus 로고    scopus 로고
    • Akt Phosphorylation of BAD couples survival signals to the cell-intrinsic death machinery
    • Datta SR, Dudek H, Tao X, Masters S, Fu H, Gotoh Y, Greenberg ME: Akt Phosphorylation of BAD couples survival signals to the cell-intrinsic death machinery. Cell 91:231, 1997
    • (1997) Cell , vol.91 , pp. 231
    • Datta, S.R.1    Dudek, H.2    Tao, X.3    Masters, S.4    Fu, H.5    Gotoh, Y.6    Greenberg, M.E.7
  • 41
    • 1842333237 scopus 로고    scopus 로고
    • Interleukin-3-induced phosphorylation of BAD through the protein kinase Akt
    • del Peso L, Gonzalez-Garcia M, Page C, Herrera R, Nunez G: Interleukin-3-induced phosphorylation of BAD through the protein kinase Akt. Science 278:687, 1997
    • (1997) Science , vol.278 , pp. 687
    • Del Peso, L.1    Gonzalez-Garcia, M.2    Page, C.3    Herrera, R.4    Nunez, G.5
  • 42
    • 0030584079 scopus 로고    scopus 로고
    • Apoptosis meets signal transduction: Elimination of a BAD influence
    • Gajewski TF, Thompson CB: Apoptosis meets signal transduction: Elimination of a BAD influence. Cell 87:619, 1996
    • (1996) Cell , vol.87 , pp. 619
    • Gajewski, T.F.1    Thompson, C.B.2
  • 43
    • 0030584088 scopus 로고    scopus 로고
    • Serine phosphorylation of death agonist BAD in response to survival factor results in binding to 14-3-3, not Bel-XL
    • Zha J, Harada H, Yang E, Jockel J, Korsmeyer SJ: Serine phosphorylation of death agonist BAD in response to survival factor results in binding to 14-3-3, not Bel-XL. Cell 87:619, 1996
    • (1996) Cell , vol.87 , pp. 619
    • Zha, J.1    Harada, H.2    Yang, E.3    Jockel, J.4    Korsmeyer, S.J.5
  • 44
    • 0029066512 scopus 로고
    • FAP-1: A protein tyrosine phosphatase that associates with FAS
    • Sato T, Irie S, Kitada S, Reed JC: FAP-1: A protein tyrosine phosphatase that associates with FAS. Science 268:411, 1995
    • (1995) Science , vol.268 , pp. 411
    • Sato, T.1    Irie, S.2    Kitada, S.3    Reed, J.C.4
  • 45
    • 0029052647 scopus 로고
    • Induction of a retinoblastoma phosphatase activity by anticancer drugs accompanies p53-independent G1 arrest and apoptosis
    • Dou QP, An B, Will PL: Induction of a retinoblastoma phosphatase activity by anticancer drugs accompanies p53-independent G1 arrest and apoptosis. Proc Natl Acad Sc USA 92:9019, 1995
    • (1995) Proc Natl Acad Sc USA , vol.92 , pp. 9019
    • Dou, Q.P.1    An, B.2    Will, P.L.3
  • 46
    • 0029897419 scopus 로고    scopus 로고
    • The involvement of protein phosphatases in the activation of ICE/CED-3 protease, intracellular acidification, DNA digestion, and apoptosis
    • Morana SJ, Wolf CM, Li JF, Reynolds JE, Brown MK, Eastman A: The involvement of protein phosphatases in the activation of ICE/CED-3 protease, intracellular acidification, DNA digestion, and apoptosis. J Biol Chem 271:18263, 1996
    • (1996) J Biol Chem , vol.271 , pp. 18263
    • Morana, S.J.1    Wolf, C.M.2    Li, J.F.3    Reynolds, J.E.4    Brown, M.K.5    Eastman, A.6
  • 47
    • 0031561725 scopus 로고    scopus 로고
    • The temporal relationship between protein phosphatase, ICE/CED-3 proteases, intracellular acidification, and DNA fragmentation in apoptosis
    • Wolf CM, Reynolds JE, Morana SJ, Eastman A: The temporal relationship between protein phosphatase, ICE/CED-3 proteases, intracellular acidification, and DNA fragmentation in apoptosis. Exp Cell Res 230:22, 1997
    • (1997) Exp Cell Res , vol.230 , pp. 22
    • Wolf, C.M.1    Reynolds, J.E.2    Morana, S.J.3    Eastman, A.4
  • 49
    • 0030973417 scopus 로고    scopus 로고
    • Multiple species of CPP32 and Mch2 are the major active caspases present in apoptotic cells
    • Faleiro L, Kobayashi R, Fearnhead H, Lazebnik Y: Multiple species of CPP32 and Mch2 are the major active caspases present in apoptotic cells. EMBO J 16:2271, 1997
    • (1997) EMBO J , vol.16 , pp. 2271
    • Faleiro, L.1    Kobayashi, R.2    Fearnhead, H.3    Lazebnik, Y.4
  • 50
    • 0027437541 scopus 로고
    • Nuclear events of apoptosis in vitro in cell-free mitotic extracts: A model system for analysis of the active phase of apoptosis
    • Lazebnik YA, Cole S, Cooke CA, Nelson WG, Earnshaw WC: Nuclear events of apoptosis in vitro in cell-free mitotic extracts: A model system for analysis of the active phase of apoptosis. J Cell Biol 123:7, 1993
    • (1993) J Cell Biol , vol.123 , pp. 7
    • Lazebnik, Y.A.1    Cole, S.2    Cooke, C.A.3    Nelson, W.G.4    Earnshaw, W.C.5
  • 51
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM: A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72:248, 1976
    • (1976) Anal Biochem , vol.72 , pp. 248
    • Bradford, M.M.1
  • 53
    • 0030931876 scopus 로고    scopus 로고
    • Caspases: The executioners of apoptosis
    • Cohen GM: Caspases: The executioners of apoptosis. Biochem J 326:1, 1997
    • (1997) Biochem J , vol.326 , pp. 1
    • Cohen, G.M.1
  • 57
    • 0030795091 scopus 로고    scopus 로고
    • Caspase-3-mediated cleavage of protein kinase C theta in induction of apoptosis
    • Datta R, Kojima H, Yoshida K, Kufe D: Caspase-3-mediated cleavage of protein kinase C theta in induction of apoptosis. J Biol Chem 272:20317, 1997
    • (1997) J Biol Chem , vol.272 , pp. 20317
    • Datta, R.1    Kojima, H.2    Yoshida, K.3    Kufe, D.4
  • 58
    • 0032502793 scopus 로고    scopus 로고
    • Lamin B phosphorylation by protein kinase C alpha and proteolysis during apoptosis in human leukemia HL-60 cells
    • Shimizu T, Cao CX, Shao RG, Pommier Y: Lamin B phosphorylation by protein kinase C alpha and proteolysis during apoptosis in human leukemia HL-60 cells. J Biol Chem 273:8669, 1998
    • (1998) J Biol Chem , vol.273 , pp. 8669
    • Shimizu, T.1    Cao, C.X.2    Shao, R.G.3    Pommier, Y.4
  • 59
    • 0031282980 scopus 로고    scopus 로고
    • Activation of PKCalpha downstream from caspases during apoptosis induced by 7-hydroxystaurosporine or the topoisomerase inhibitors, camptothecin and etoposide, in human myeloid leukemia HL-60 cells
    • Shao RG, Cao CX, Pommier Y: Activation of PKCalpha downstream from caspases during apoptosis induced by 7-hydroxystaurosporine or the topoisomerase inhibitors, camptothecin and etoposide, in human myeloid leukemia HL-60 cells. J Biol Chem 272:31321, 1997
    • (1997) J Biol Chem , vol.272 , pp. 31321
    • Shao, R.G.1    Cao, C.X.2    Pommier, Y.3
  • 61
    • 0028990801 scopus 로고
    • Direct demonstration of NFATp dephosphorylation and nuclear localization in activated HT-2 cells using a specific NFATp polyclonal antibody
    • Ruff VA, Leach KL: Direct demonstration of NFATp dephosphorylation and nuclear localization in activated HT-2 cells using a specific NFATp polyclonal antibody. J Biol Chem 270:22602, 1995
    • (1995) J Biol Chem , vol.270 , pp. 22602
    • Ruff, V.A.1    Leach, K.L.2
  • 62
    • 0028234529 scopus 로고
    • Jak-STAT pathways and transcriptional activation in response to IFNs and other extracellular signaling proteins
    • Darnell JEJ, Kerr IM, Stark GR: Jak-STAT pathways and transcriptional activation in response to IFNs and other extracellular signaling proteins. Science 264:1415, 1994
    • (1994) Science , vol.264 , pp. 1415
    • Jej, D.1    Kerr, I.M.2    Stark, G.R.3


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