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Volumn 7, Issue 5, 2000, Pages 477-484

Properties of DNA fragmentation activity generated by ATP depletion

Author keywords

ATP; Caspase; DNA fragmentation; Endonuclease; Proteasome; Serine protease

Indexed keywords

ADENOSINE TRIPHOSPHATE; CASPASE INHIBITOR; DNA; DNA FRAGMENT; SERINE PROTEINASE INHIBITOR;

EID: 0034014994     PISSN: 13509047     EISSN: None     Source Type: Journal    
DOI: 10.1038/sj.cdd.4400677     Document Type: Erratum
Times cited : (29)

References (58)
  • 5
    • 0033618445 scopus 로고    scopus 로고
    • +, cell shrinkage, and mitochondrial membrane potential during lymphocyte apoptosis
    • +, cell shrinkage, and mitochondrial membrane potential during lymphocyte apoptosis. J. Biol. Chem. 274: 21953-21962
    • (1999) J. Biol. Chem. , vol.274 , pp. 21953-21962
    • Bortner, C.D.1    Cidlowski, J.A.2
  • 8
    • 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
    • Zou H, Henzel WJ, Liu X, Lutschg A and Wang X (1997) Apaf-1, a human protein homologous to C.elegans CED-4, participates in cytochrome c-dependent activation of caspase-3. Cell 90: 405-413
    • (1997) Cell , vol.90 , pp. 405-413
    • Zou, H.1    Henzel, W.J.2    Liu, X.3    Lutschg, A.4    Wang, X.5
  • 9
    • 0030715323 scopus 로고    scopus 로고
    • Cytochrome c and dATP-dependent formation Apaf-1/Caspase-9 complex initiates an apoptotic protease cascade
    • Li P, Nijhawan D, Buduhardjo I, Srinivasula SM, Ahmad M, Alnemri ES and Wang X (1997) Cytochrome c and dATP-dependent formation Apaf-1/Caspase-9 complex initiates an apoptotic protease cascade. Cell 91: 479-489
    • (1997) Cell , vol.91 , pp. 479-489
    • Li, P.1    Nijhawan, D.2    Buduhardjo, I.3    Srinivasula, S.M.4    Ahmad, M.5    Alnemri, E.S.6    Wang, X.7
  • 10
    • 0032544449 scopus 로고    scopus 로고
    • Apaf-1 (CED-4 homolog) regulates programmed cell death in mammalian development
    • Cecconi F, Alvarez-Bolado G, Meyer BI, Roth KA and Gruss P (1998) Apaf-1 (CED-4 homolog) regulates programmed cell death in mammalian development. Cell 94: 727-737
    • (1998) Cell , vol.94 , pp. 727-737
    • Cecconi, F.1    Alvarez-Bolado, G.2    Meyer, B.I.3    Roth, K.A.4    Gruss, P.5
  • 12
    • 0344348821 scopus 로고    scopus 로고
    • Role of cytochrome c and dATP/ ATP hydrolysis in Apaf-1-mediated caspase-9 activation and apoptosis
    • Hu Y, Benedict MA, Ding L and Núñez G (1999) Role of cytochrome c and dATP/ ATP hydrolysis in Apaf-1-mediated caspase-9 activation and apoptosis. EMBO J. 18: 3586-3595
    • (1999) EMBO J. , vol.18 , pp. 3586-3595
    • Hu, Y.1    Benedict, M.A.2    Ding, L.3    Núñez, G.4
  • 14
    • 0033529634 scopus 로고    scopus 로고
    • Caspase activation involves the formation of the aposome, a large ( ∼ 700 kDa) caspase-activating complex
    • Cain K, Brown DG, Langlais C and Cohen GM (1999) Caspase activation involves the formation of the aposome, a large ( ∼ 700 kDa) caspase-activating complex. J. Biol. Chem. 274: 22686-22692
    • (1999) J. Biol. Chem. , vol.274 , pp. 22686-22692
    • Cain, K.1    Brown, D.G.2    Langlais, C.3    Cohen, G.M.4
  • 15
    • 0033545382 scopus 로고    scopus 로고
    • Bcl-2 regulates amplification of caspase activation by cytochrome c
    • Cosulich SC, Savory PJ and Clarke PR (1999) Bcl-2 regulates amplification of caspase activation by cytochrome c. Curr. Biol. 9: 147-150
    • (1999) Curr. Biol. , vol.9 , pp. 147-150
    • Cosulich, S.C.1    Savory, P.J.2    Clarke, P.R.3
  • 16
    • 0030915587 scopus 로고    scopus 로고
    • Intracellular ATP levels determine cell death fate by apoptosis or necrosis
    • Eguchi Y, Shimizu S and Tsujimoto Y (1997) Intracellular ATP levels determine cell death fate by apoptosis or necrosis. Cancer Res. 57: 1835-1840
    • (1997) Cancer Res. , vol.57 , pp. 1835-1840
    • Eguchi, Y.1    Shimizu, S.2    Tsujimoto, Y.3
  • 19
    • 0031054903 scopus 로고    scopus 로고
    • Energy metabolism during apoptosis
    • Garland JM and Halestrap A (1997) Energy metabolism during apoptosis. J. Biol. Chem. 272: 4680-4688
    • (1997) J. Biol. Chem. , vol.272 , pp. 4680-4688
    • Garland, J.M.1    Halestrap, A.2
  • 20
    • 0028049621 scopus 로고
    • Apoptosis is regulated by the rate of glucose transport in an interleukin 3 dependent cell line
    • Kan O, Baldwin SA and Whetton AD (1994) Apoptosis is regulated by the rate of glucose transport in an interleukin 3 dependent cell line. J. Exp. Med. 180:917-923
    • (1994) J. Exp. Med. , vol.180 , pp. 917-923
    • Kan, O.1    Baldwin, S.A.2    Whetton, A.D.3
  • 24
    • 0033011114 scopus 로고    scopus 로고
    • Mice lacking the poly(ADP-ribose) polymerase gene are resistant to pancreatic beta-cell destruction and diabetes development induced by streptozocin
    • Burkart V, Wang Z-Q, Radons J, Heller B, Herceg Z, Stingl L, Wagner EF and Kolb H (1999) Mice lacking the poly(ADP-ribose) polymerase gene are resistant to pancreatic beta-cell destruction and diabetes development induced by streptozocin. Nat. Med. 5: 314-319
    • (1999) Nat. Med. , vol.5 , pp. 314-319
    • Burkart, V.1    Wang, Z.-Q.2    Radons, J.3    Heller, B.4    Herceg, Z.5    Stingl, L.6    Wagner, E.F.7    Kolb, H.8
  • 25
    • 0031888955 scopus 로고    scopus 로고
    • A caspase-activated DNase that degrades DNA during apoptosis, and its inhibitor ICAD
    • Enari M, Sakahira H, Yokoyama H, Okawa K, Iwamatsu A and Nagata S (1998) A caspase-activated DNase that degrades DNA during apoptosis, and its inhibitor ICAD. Nature 391: 43-50
    • (1998) Nature , vol.391 , pp. 43-50
    • Enari, M.1    Sakahira, H.2    Yokoyama, H.3    Okawa, K.4    Iwamatsu, A.5    Nagata, S.6
  • 26
    • 0027971322 scopus 로고
    • Purification of a 24-kD protease from apoptotic tumor cells that activates DNA fragmentation
    • Wright SC, Wei QS, Zhong J, Zheng H, Kinder DH and Larrick JW (1994) Purification of a 24-kD protease from apoptotic tumor cells that activates DNA fragmentation. J. Exp. Med. 180: 2113-2123
    • (1994) J. Exp. Med. , vol.180 , pp. 2113-2123
    • Wright, S.C.1    Wei, Q.S.2    Zhong, J.3    Zheng, H.4    Kinder, D.H.5    Larrick, J.W.6
  • 28
    • 0028964628 scopus 로고
    • Isolation and partial characterization of a protease involved in Fas-induced apoptosis
    • Schlegel J, Peters I and Orrenius S (1995) Isolation and partial characterization of a protease involved in Fas-induced apoptosis. FEBS Lett. 364: 139-142
    • (1995) FEBS Lett. , vol.364 , pp. 139-142
    • Schlegel, J.1    Peters, I.2    Orrenius, S.3
  • 29
    • 0029890322 scopus 로고    scopus 로고
    • Role of serine and ICE-like proteases in induction of apoptosis by etoposide in human leukemia HL-60 cells
    • Yoshida A, Takauji R, Inuzuka M, Ueda T and Nakamura T (1996) Role of serine and ICE-like proteases in induction of apoptosis by etoposide in human leukemia HL-60 cells. Leukemia 10: 821-824
    • (1996) Leukemia , vol.10 , pp. 821-824
    • Yoshida, A.1    Takauji, R.2    Inuzuka, M.3    Ueda, T.4    Nakamura, T.5
  • 30
    • 0030218978 scopus 로고    scopus 로고
    • DNA fragmentation induced by protease activation in p53-null human leukemia HL60 cells undergoing apoptosis following treatment with the topoisomerase I inhibitor camptothecin: Cell-free system studies
    • Shimizu T and Pommier Y (1996) DNA fragmentation induced by protease activation in p53-null human leukemia HL60 cells undergoing apoptosis following treatment with the topoisomerase I inhibitor camptothecin: cell-free system studies. Exp. Cell Res. 226, 292-301
    • (1996) Exp. Cell Res. , vol.226 , pp. 292-301
    • Shimizu, T.1    Pommier, Y.2
  • 31
    • 0030886788 scopus 로고    scopus 로고
    • Camptothecin-induced apoptosis in p53-null human leukemia HL60 cells and their isolated nuclei: Effects of the protease inhibitors Z-VAD-fmk and dichloroisocoumarin suggest an involvement of both caspases and serine proteases
    • Shimizu T and Pommier Y (1997) Camptothecin-induced apoptosis in p53-null human leukemia HL60 cells and their isolated nuclei: effects of the protease inhibitors Z-VAD-fmk and dichloroisocoumarin suggest an involvement of both caspases and serine proteases. Leukemia 11: 1238-1244
    • (1997) Leukemia , vol.11 , pp. 1238-1244
    • Shimizu, T.1    Pommier, Y.2
  • 32
    • 0029807603 scopus 로고    scopus 로고
    • Selective induction of apoptosis in Hep 3B cells by topoisomerase I inhibitors: Evidence for a protease-dependent pathway that does not activate cysteine protease P32
    • Adjei PN, Kaufmann SH, Leung WY, Mao F and Gores GJ (1996) Selective induction of apoptosis in Hep 3B cells by topoisomerase I inhibitors: Evidence for a protease-dependent pathway that does not activate cysteine protease P32. J. Clin. Invest. 98: 2588-2596
    • (1996) J. Clin. Invest. , vol.98 , pp. 2588-2596
    • Adjei, P.N.1    Kaufmann, S.H.2    Leung, W.Y.3    Mao, F.4    Gores, G.J.5
  • 33
    • 0031034160 scopus 로고    scopus 로고
    • Activation of the cell death program by inhibition of proteasome function
    • Drexler HCA (1997) Activation of the cell death program by inhibition of proteasome function. Proc. Natl. Acad. Sci. USA 94: 855-860
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 855-860
    • Drexler, H.C.A.1
  • 34
    • 0031889132 scopus 로고    scopus 로고
    • Cleavage of CAD inhibitor in CAD activation and DNA degradation during apoptosis
    • Sakahira H, Enari M and Nagata S (1998) Cleavage of CAD inhibitor in CAD activation and DNA degradation during apoptosis. Nature 391: 96-99
    • (1998) Nature , vol.391 , pp. 96-99
    • Sakahira, H.1    Enari, M.2    Nagata, S.3
  • 35
    • 0033539067 scopus 로고    scopus 로고
    • Acinus is a caspase-3-activated protein required for apoptotic chromatin condensation
    • Sahara S, Aoto M, Eguchi Y, Imamoto N, Yoneda Y and Tsujimoto Y (1999) Acinus is a caspase-3-activated protein required for apoptotic chromatin condensation. Nature 401: 168-173
    • (1999) Nature , vol.401 , pp. 168-173
    • Sahara, S.1    Aoto, M.2    Eguchi, Y.3    Imamoto, N.4    Yoneda, Y.5    Tsujimoto, Y.6
  • 37
    • 0030900980 scopus 로고    scopus 로고
    • Intracellular adenosine triphosphate (ATP) concentration: A switch in the decision between apoptosis and necrosis
    • Leist M, Single B, Castoldi AF, Kühnle S and Nicotera P (1997) Intracellular adenosine triphosphate (ATP) concentration: a switch in the decision between apoptosis and necrosis. J. Exp. Med. 185: 1481-1486
    • (1997) J. Exp. Med. , vol.185 , pp. 1481-1486
    • Leist, M.1    Single, B.2    Castoldi, A.F.3    Kühnle, S.4    Nicotera, P.5
  • 38
    • 0033563776 scopus 로고    scopus 로고
    • Inhibition of mitochondrial ATP generation by nitric oxide switches apoptosis to necrosis
    • Leist M, Single B, Naumann H, Fava E, Simon B, Kühnle S and Nicotera P (1999) Inhibition of mitochondrial ATP generation by nitric oxide switches apoptosis to necrosis. Exp. Cell Res. 249: 396-403
    • (1999) Exp. Cell Res. , vol.249 , pp. 396-403
    • Leist, M.1    Single, B.2    Naumann, H.3    Fava, E.4    Simon, B.5    Kühnle, S.6    Nicotera, P.7
  • 40
    • 0030021349 scopus 로고    scopus 로고
    • Biochemical pathways of apoptosis: Nicotinamide adenine dinucleotide-deficient cells are resistant to tumor necrosis factor or ultraviolet light activation of the 24-kD apoptotic protease and DNA fragmentation
    • Wright SC, Wei QS, Kinder DH and Larrick JW (1996) Biochemical pathways of apoptosis: Nicotinamide adenine dinucleotide-deficient cells are resistant to tumor necrosis factor or ultraviolet light activation of the 24-kD apoptotic protease and DNA fragmentation. J. Exp. Med. 183: 463-471
    • (1996) J. Exp. Med. , vol.183 , pp. 463-471
    • Wright, S.C.1    Wei, Q.S.2    Kinder, D.H.3    Larrick, J.W.4
  • 41
    • 0030817142 scopus 로고    scopus 로고
    • Calmodulin-dependent protein kinase II mediates signal transduction in apoptosis
    • Wright SC, Schellenberger U, Ji L, Wang H and Larrick JW (1997) Calmodulin-dependent protein kinase II mediates signal transduction in apoptosis. FASEB J. 11: 843-849
    • (1997) FASEB J. , vol.11 , pp. 843-849
    • Wright, S.C.1    Schellenberger, U.2    Ji, L.3    Wang, H.4    Larrick, J.W.5
  • 42
    • 0030777366 scopus 로고    scopus 로고
    • Activation of CPP32-like proteases is not sufficient to trigger apoptosis: Inhibition of apoptosis by agents that suppress activation of AP24, but not CPP32-like activity
    • Wright SC, Schellenberger U, Wang H, Kinder DH, Talhouk JW and Larrick JW (1997) Activation of CPP32-like proteases is not sufficient to trigger apoptosis: inhibition of apoptosis by agents that suppress activation of AP24, but not CPP32-like activity. J. Exp. Med. 186: 1107-1117
    • (1997) J. Exp. Med. , vol.186 , pp. 1107-1117
    • Wright, S.C.1    Schellenberger, U.2    Wang, H.3    Kinder, D.H.4    Talhouk, J.W.5    Larrick, J.W.6
  • 43
    • 0028258577 scopus 로고
    • Cytotoxic lymphocytes require granzyme B for the rapid induction of DNA fragmentation and apoptosis in allogeneic target cells
    • Heusel JW, Wesselschmidt RL, Shresta S, Russell JH and Ley TJ (1994) Cytotoxic lymphocytes require granzyme B for the rapid induction of DNA fragmentation and apoptosis in allogeneic target cells. Cell 76: 977-987
    • (1994) Cell , vol.76 , pp. 977-987
    • Heusel, J.W.1    Wesselschmidt, R.L.2    Shresta, S.3    Russell, J.H.4    Ley, T.J.5
  • 44
    • 0029099845 scopus 로고
    • Activation of the apoptotic protease CPP32 by cytotoxic T-cell-derived granzyme B
    • Darmon AJ, Nicholson DW and Bleackley RC (1995) Activation of the apoptotic protease CPP32 by cytotoxic T-cell-derived granzyme B. Nature 377: 446-448
    • (1995) Nature , vol.377 , pp. 446-448
    • Darmon, A.J.1    Nicholson, D.W.2    Bleackley, R.C.3
  • 46
    • 9344261615 scopus 로고    scopus 로고
    • The cytotoxic cell protease granzyme B initiates apoptosis in a cell free system by proteolytic processing and activation of the ICE/CED-3 family protease, CPP32, via a novel two-step mechanism
    • Martin SJ, Amarante-Mendes GP, Shi L, ChuangT-H, Casiano CA, O'Brien GA, Fitzgerald P, Tan EM, Bokoch GM, Greenberg AH and Green DR (1996) The cytotoxic cell protease granzyme B initiates apoptosis in a cell free system by proteolytic processing and activation of the ICE/CED-3 family protease, CPP32, via a novel two-step mechanism. EMBO J. 15: 2407-2416
    • (1996) EMBO J. , vol.15 , pp. 2407-2416
    • Martin, S.J.1    Amarante-Mendes, G.P.2    Shi, L.3    Casiano, C.A.4    O'Brien, G.A.5    Fitzgerald, P.6    Tan, E.M.7    Bokoch, G.M.8    Greenberg, A.H.9    Green, D.R.10
  • 47
    • 0033081183 scopus 로고    scopus 로고
    • The proteasome regulates caspase-dependent and caspase-independent protease cascades during apoptosis of MO7e hematopoetic progenitor cells
    • Wu L-W, Reid S, Ritchie A, Broxmeyer HE and Donner DB (1999) The proteasome regulates caspase-dependent and caspase-independent protease cascades during apoptosis of MO7e hematopoetic progenitor cells. Blood Cells Mol. Dis. 25: 20-29
    • (1999) Blood Cells Mol. Dis. , vol.25 , pp. 20-29
    • Wu, L.-W.1    Reid, S.2    Ritchie, A.3    Broxmeyer, H.E.4    Donner, D.B.5
  • 48
    • 0032514713 scopus 로고    scopus 로고
    • Resistance to DNA fragmentation and chromatin condensation in mice lacking the DNA fragmentation factor 45
    • Zhang J, Liu X, Scherer DC, van Kaer Lv, Wang X and Xu M (1998) Resistance to DNA fragmentation and chromatin condensation in mice lacking the DNA fragmentation factor 45. Proc. Natl. Acad. Sci. USA 95: 12480-12485
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 12480-12485
    • Zhang, J.1    Liu, X.2    Scherer, D.C.3    Van Kaer, L.4    Wang, X.5    Xu, M.6
  • 49
    • 0030916417 scopus 로고    scopus 로고
    • DFF, a heterodimeric protein that functions downstream of caspase-3 to trigger DNA fragmentation during apoptosis
    • Liu X, Zou H, Slaughter C and Wang X (1997) DFF, a heterodimeric protein that functions downstream of caspase-3 to trigger DNA fragmentation during apoptosis. Cell 89:175-184
    • (1997) Cell , vol.89 , pp. 175-184
    • Liu, X.1    Zou, H.2    Slaughter, C.3    Wang, X.4
  • 50
    • 0032525332 scopus 로고    scopus 로고
    • 2+-dependent endonuclease (AN34) from etoposide-treated human leukemia HL-60 cells undergoing apoptosis
    • 2+-dependent endonuclease (AN34) from etoposide-treated human leukemia HL-60 cells undergoing apoptosis. Cancer Res. 58: 2576-2582
    • (1998) Cancer Res. , vol.58 , pp. 2576-2582
    • Yoshida, A.1    Pourquier, P.2    Pommier, Y.3
  • 51
    • 0032535483 scopus 로고    scopus 로고
    • The ubiquitin-proteasome pathway: On protein death and cell life
    • Ciechanover A (1998) The ubiquitin-proteasome pathway: on protein death and cell life. EMBO J. 17: 7151-7160
    • (1998) EMBO J. , vol.17 , pp. 7151-7160
    • Ciechanover, A.1
  • 52
    • 0032488846 scopus 로고    scopus 로고
    • The proteasome: Paradigm of a self-compartmentalizing protease
    • Baumeister W, Walz J, Zühl F and Seemüller E (1998) The proteasome: paradigm of a self-compartmentalizing protease. Cell 92: 367-380
    • (1998) Cell , vol.92 , pp. 367-380
    • Baumeister, W.1    Walz, J.2    Zühl, F.3    Seemüller, E.4
  • 53
    • 0032919345 scopus 로고    scopus 로고
    • The role of the ubiquitin-proteasome pathway in apoptosis
    • Orlowski RZ (1999) The role of the ubiquitin-proteasome pathway in apoptosis. Cell Death Differ. 6: 303-313
    • (1999) Cell Death Differ. , vol.6 , pp. 303-313
    • Orlowski, R.Z.1
  • 54
    • 0031823018 scopus 로고    scopus 로고
    • Inhibition versus induction of apoptosis by proteasome inhibitors depends on concentration
    • Lin K-I, Baraban JM and Ratan RR (1998) Inhibition versus induction of apoptosis by proteasome inhibitors depends on concentration. Cell Death Differ. 5: 577-583
    • (1998) Cell Death Differ. , vol.5 , pp. 577-583
    • Lin, K.-I.1    Baraban, J.M.2    Ratan, R.R.3
  • 57
    • 0032513291 scopus 로고    scopus 로고
    • Defects in the ubiquitin pathway induce caspase-independent apoptosis blocked by Bcl-2
    • Monney L, Otter I, Olivier R, Ozer HL, Haas AL, Omura S and Borner C (1998) Defects in the ubiquitin pathway induce caspase-independent apoptosis blocked by Bcl-2. J. Biol. Chem. 273: 6121-6131
    • (1998) J. Biol. Chem. , vol.273 , pp. 6121-6131
    • Monney, L.1    Otter, I.2    Olivier, R.3    Ozer, H.L.4    Haas, A.L.5    Omura, S.6    Borner, C.7
  • 58
    • 0032080664 scopus 로고    scopus 로고
    • Localization of the apoptosis-inducing activity of lupus anticoagulant in an annexin V-binding antibody subset
    • Nakamura N, Ban T, Yamaji K, Yoneda Y and Wada Y (1998) Localization of the apoptosis-inducing activity of lupus anticoagulant in an annexin V-binding antibody subset. J. Clin. Invest. 101: 1951-1959
    • (1998) J. Clin. Invest. , vol.101 , pp. 1951-1959
    • Nakamura, N.1    Ban, T.2    Yamaji, K.3    Yoneda, Y.4    Wada, Y.5


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