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Volumn 256, Issue 1, 2000, Pages 12-18

Apoptotic DNA fragmentation

Author keywords

Apoptosis; Caspases; DNase; Programmed cell death

Indexed keywords

CASPASE; DNA FRAGMENT;

EID: 0034630317     PISSN: 00144827     EISSN: None     Source Type: Journal    
DOI: 10.1006/excr.2000.4834     Document Type: Article
Times cited : (766)

References (56)
  • 1
    • 0033593572 scopus 로고    scopus 로고
    • Cell death in development
    • Vaux D. L., Korsmeyer S. J. Cell death in development. Cell. 96:1999;245-254.
    • (1999) Cell , vol.96 , pp. 245-254
    • Vaux, D.L.1    Korsmeyer, S.J.2
  • 2
    • 0030947095 scopus 로고    scopus 로고
    • Programmed cell death in animal development
    • Jacobson M. D., Weil M., Raff M. C. Programmed cell death in animal development. Cell. 88:1997;347-354.
    • (1997) Cell , vol.88 , pp. 347-354
    • Jacobson, M.D.1    Weil, M.2    Raff, M.C.3
  • 4
    • 0018830636 scopus 로고
    • Glucocorticoid-induced thymocyte apoptosis is associated with endogenous endonuclease activation
    • Wyllie A. H. Glucocorticoid-induced thymocyte apoptosis is associated with endogenous endonuclease activation. Nature. 284:1980;555-556.
    • (1980) Nature , vol.284 , pp. 555-556
    • Wyllie, A.H.1
  • 5
    • 0032575714 scopus 로고    scopus 로고
    • Death receptors: Signaling and modulation
    • Ashkenazi A., Dixit V. M. Death receptors: Signaling and modulation. Science. 281:1998;1305-1308.
    • (1998) Science , vol.281 , pp. 1305-1308
    • Ashkenazi, A.1    Dixit, V.M.2
  • 6
    • 0030892234 scopus 로고    scopus 로고
    • Apoptosis by death factor
    • Nagata S. Apoptosis by death factor. Cell. 88:1997;355-365.
    • (1997) Cell , vol.88 , pp. 355-365
    • Nagata, S.1
  • 7
    • 0032511880 scopus 로고    scopus 로고
    • Cell suicide for beginners
    • Raff M. Cell suicide for beginners. Nature. 396:1998;119-122.
    • (1998) Nature , vol.396 , pp. 119-122
    • Raff, M.1
  • 8
    • 0032575752 scopus 로고    scopus 로고
    • Mitochondria and apoptosis
    • Green D. R., Reed J. C. Mitochondria and apoptosis. Science. 281:1998;1309-1312.
    • (1998) Science , vol.281 , pp. 1309-1312
    • Green, D.R.1    Reed, J.C.2
  • 9
    • 0032575750 scopus 로고    scopus 로고
    • Caspases: Enemies within
    • Thornberry N. A., Lazebnik Y. Caspases: Enemies within. Science. 281:1998;1312-1316.
    • (1998) Science , vol.281 , pp. 1312-1316
    • Thornberry, N.A.1    Lazebnik, Y.2
  • 10
    • 0032416062 scopus 로고    scopus 로고
    • Death by a thousand cuts: An ever-increasing list of caspase substrates
    • Stroh C., Schulze-Osthoff K. Death by a thousand cuts: An ever-increasing list of caspase substrates. Cell Death Diff. 5:1998;997-1000.
    • (1998) Cell Death Diff. , vol.5 , pp. 997-1000
    • Stroh, C.1    Schulze-Osthoff, K.2
  • 11
    • 0029042718 scopus 로고
    • Nuclear changes in apoptosis
    • Earnshaw W. C. Nuclear changes in apoptosis. Curr. Biol. 7:1995;337-343.
    • (1995) Curr. Biol. , vol.7 , pp. 337-343
    • Earnshaw, W.C.1
  • 12
    • 0026648674 scopus 로고
    • Identification of programmed cell death in situ via specific labeling of nuclear DNA fragmentation
    • Gavrieli Y., Sherman Y., Ben-Sasson S. A. Identification of programmed cell death in situ via specific labeling of nuclear DNA fragmentation. J. Cell Biol. 119:1992;493-501.
    • (1992) J. Cell Biol. , vol.119 , pp. 493-501
    • Gavrieli, Y.1    Sherman, Y.2    Ben-Sasson, S.A.3
  • 14
    • 0027145632 scopus 로고
    • Molecular cloning and expression of the Fas ligand: A novel member of the tumor necrosis factor family
    • Suda T., Takahashi T., Golstein P., Nagata S. Molecular cloning and expression of the Fas ligand: A novel member of the tumor necrosis factor family. Cell. 75:1993;1169-1178.
    • (1993) Cell , vol.75 , pp. 1169-1178
    • Suda, T.1    Takahashi, T.2    Golstein, P.3    Nagata, S.4
  • 18
    • 0028927607 scopus 로고
    • The Fas death factor
    • Nagata S., Golstein P. The Fas death factor. Science. 267:1995;1449-1456.
    • (1995) Science , vol.267 , pp. 1449-1456
    • Nagata, S.1    Golstein, P.2
  • 19
  • 21
    • 0033534446 scopus 로고    scopus 로고
    • Caspase cleaved BID targets mitochondria and is required for cytochrome c release, while BCL-XL prevents this release but not tumor necrosis factor-R1/Fas death
    • Gross A., Yin X. M., Wang K., Wei M. C., Jockel J., Milliman C., Erdjument B. H., Tempst P., Korsmeyer S. J. Caspase cleaved BID targets mitochondria and is required for cytochrome c release, while BCL-XL prevents this release but not tumor necrosis factor-R1/Fas death. J. Biol. Chem. 274:1999;1156-1163.
    • (1999) J. Biol. Chem. , vol.274 , pp. 1156-1163
    • Gross, A.1    Yin, X.M.2    Wang, K.3    Wei, M.C.4    Jockel, J.5    Milliman, C.6    Erdjument, B.H.7    Tempst, P.8    Korsmeyer, S.J.9
  • 22
    • 0032555697 scopus 로고    scopus 로고
    • Cleavage of BID by caspase 8 mediates the mitochondrial damage in the Fas pathway of apoptosis
    • Li H., Zhu H., Xu C. J., Yuan J. Cleavage of BID by caspase 8 mediates the mitochondrial damage in the Fas pathway of apoptosis. Cell. 94:1998;491-501.
    • (1998) Cell , vol.94 , pp. 491-501
    • Li, H.1    Zhu, H.2    Xu, C.J.3    Yuan, J.4
  • 23
    • 0032555716 scopus 로고    scopus 로고
    • Bid, a Bcl2 interacting protein, mediates cytochrome c release from mitochondria in response to activation of cell surface death receptors
    • Luo X., Budihardjo I., Zou H., Slaughter C., Wang X. Bid, a Bcl2 interacting protein, mediates cytochrome c release from mitochondria in response to activation of cell surface death receptors. Cell. 94:1998;481-490.
    • (1998) Cell , vol.94 , pp. 481-490
    • Luo, X.1    Budihardjo, I.2    Zou, H.3    Slaughter, C.4    Wang, X.5
  • 24
    • 0032736175 scopus 로고    scopus 로고
    • In vivo evidence that caspase-3 is required for Fas-mediated apoptosis of hepatocytes
    • Woo M., Hakem A., Elia A. J., Hakem R., Duncan G. S., Patterson B. J., Mak T. W. In vivo evidence that caspase-3 is required for Fas-mediated apoptosis of hepatocytes. J. Immunol. 163:1999;4909-4916.
    • (1999) J. Immunol. , vol.163 , pp. 4909-4916
    • Woo, M.1    Hakem, A.2    Elia, A.J.3    Hakem, R.4    Duncan, G.S.5    Patterson, B.J.6    Mak, T.W.7
  • 25
    • 0028805524 scopus 로고
    • Apoptosis by a cytosolic extract from Fas-activated cells
    • Enari M., Hase A., Nagata S. Apoptosis by a cytosolic extract from Fas-activated cells. EMBO J. 14:1995;5201-5208.
    • (1995) EMBO J. , vol.14 , pp. 5201-5208
    • Enari, M.1    Hase, A.2    Nagata, S.3
  • 28
    • 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., Nagata S. A caspase-activated DNase that degrades DNA during apoptosis and its inhibitor ICAD. Nature. 391:1998;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
  • 29
    • 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., Wang X. DFF, a heterodimeric protein that functions downstream of caspase-3 to trigger DNA fragmentation during apoptosis. Cell. 89:1997;175-184.
    • (1997) Cell , vol.89 , pp. 175-184
    • Liu, X.1    Zou, H.2    Slaughter, C.3    Wang, X.4
  • 32
    • 0032555215 scopus 로고    scopus 로고
    • The 40-kDa subunit of DNA fragmentation factor induces DNA fragmentation and chromatin condensation during apoptosis
    • Liu X., Li P., Widlak P., Zou H., Luo X., Garrard W. T., Wang X. The 40-kDa subunit of DNA fragmentation factor induces DNA fragmentation and chromatin condensation during apoptosis. Proc. Natl. Acad. Sci. USA. 95:1998;8461-8466.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 8461-8466
    • Liu, X.1    Li, P.2    Widlak, P.3    Zou, H.4    Luo, X.5    Garrard, W.T.6    Wang, X.7
  • 33
    • 0034678123 scopus 로고    scopus 로고
    • Specific Chaperone-like Activity of Inhibitor of Caspase-activated DNase for Caspase-activated DNase
    • Sakahira H., Iwamatsu A., Nagata S. Specific Chaperone-like Activity of Inhibitor of Caspase-activated DNase for Caspase-activated DNase. J. Biol. Chem. 2000.
    • (2000) J. Biol. Chem.
    • Sakahira, H.1    Iwamatsu, A.2    Nagata, S.3
  • 35
    • 0032501396 scopus 로고    scopus 로고
    • Inhibition of apoptosis-associated DNA fragmentation activity in nonapoptotic cells: The role of DNA fragmentation factor-45 (DFF45/ICAD)
    • Sabol S. L., Li R., Lee T. Y., Abdul-Khalek R. Inhibition of apoptosis-associated DNA fragmentation activity in nonapoptotic cells: The role of DNA fragmentation factor-45 (DFF45/ICAD). Biochem. Biophys. Res. Commun. 253:1998;151-158.
    • (1998) Biochem. Biophys. Res. Commun. , vol.253 , pp. 151-158
    • Sabol, S.L.1    Li, R.2    Lee, T.Y.3    Abdul-Khalek, R.4
  • 36
    • 0033597882 scopus 로고    scopus 로고
    • Functional interaction of DFF35 and DFF45 with caspase-activated DNA fragmentation nuclease DFF40
    • Gu J., Dong R. P., Zhang C., McLaughlin D. F., Wu M. X., Schlossman S. F. Functional interaction of DFF35 and DFF45 with caspase-activated DNA fragmentation nuclease DFF40. J. Biol. Chem. 274:1999;20759-20762.
    • (1999) J. Biol. Chem. , vol.274 , pp. 20759-20762
    • Gu, J.1    Dong, R.P.2    Zhang, C.3    McLaughlin, D.F.4    Wu, M.X.5    Schlossman, S.F.6
  • 37
    • 0032080022 scopus 로고    scopus 로고
    • CIDE, a novel family of cell death activators with homology to the 45 kDa subunit of the DNA fragmentation factor
    • Inohara N., Koseki T., Chen S., Wu X., Nunez G. CIDE, a novel family of cell death activators with homology to the 45 kDa subunit of the DNA fragmentation factor. EMBO J. 17:1998;2526-2533.
    • (1998) EMBO J. , vol.17 , pp. 2526-2533
    • Inohara, N.1    Koseki, T.2    Chen, S.3    Wu, X.4    Nunez, G.5
  • 38
    • 0033598940 scopus 로고    scopus 로고
    • Solution structure of the CIDE-N domain of CIDE-B and a model for CIDE-N/CIDE-N interaction in the DNA fragmentation pathway of apoptosis
    • Lugovskoy A., Zhou P., Chou J., McCarty J., Li P., Wagner G. Solution structure of the CIDE-N domain of CIDE-B and a model for CIDE-N/CIDE-N interaction in the DNA fragmentation pathway of apoptosis. Cell. 99:1999;747-755.
    • (1999) Cell , vol.99 , pp. 747-755
    • Lugovskoy, A.1    Zhou, P.2    Chou, J.3    McCarty, J.4    Li, P.5    Wagner, G.6
  • 39
    • 0033056950 scopus 로고    scopus 로고
    • Functional differences of two forms of the inhibitor of caspase-activated DNase, ICAD-L and ICAD-S
    • Sakahira H., Enari M., Nagata S. Functional differences of two forms of the inhibitor of caspase-activated DNase, ICAD-L and ICAD-S. J. Biol. Chem. 274:1999;15740-15744.
    • (1999) J. Biol. Chem. , vol.274 , pp. 15740-15744
    • Sakahira, H.1    Enari, M.2    Nagata, S.3
  • 40
    • 0033527063 scopus 로고    scopus 로고
    • Involvement of caspase 3-activated DNase in internucleosomal DNA cleavage induced by diverse apoptotic stimuli
    • McIlroy D., Sakahira H., Talanian R. V., Nagata S. Involvement of caspase 3-activated DNase in internucleosomal DNA cleavage induced by diverse apoptotic stimuli. Oncogene. 18:1999;4401-4408.
    • (1999) Oncogene , vol.18 , pp. 4401-4408
    • McIlroy, D.1    Sakahira, H.2    Talanian, R.V.3    Nagata, S.4
  • 41
    • 0032724653 scopus 로고    scopus 로고
    • Caspase-3 is the primary activator of apoptotic DNA fragmentation via DNA fragmentation factor-45/inhibitor of caspase-activated DNase inactivation
    • Wolf B. B., Schuler M., Echeverri F., Green D. R. Caspase-3 is the primary activator of apoptotic DNA fragmentation via DNA fragmentation factor-45/inhibitor of caspase-activated DNase inactivation. J. Biol. Chem. 274:1999;30651-30656.
    • (1999) J. Biol. Chem. , vol.274 , pp. 30651-30656
    • Wolf, B.B.1    Schuler, M.2    Echeverri, F.3    Green, D.R.4
  • 42
    • 0031889132 scopus 로고    scopus 로고
    • Cleavage of CAD inhibitor in CAD activation and DNA degradation during apoptosis
    • Sakahira H., Enari M., Nagata S. Cleavage of CAD inhibitor in CAD activation and DNA degradation during apoptosis. Nature. 391:1998;96-99.
    • (1998) Nature , vol.391 , pp. 96-99
    • Sakahira, H.1    Enari, M.2    Nagata, S.3
  • 43
    • 0033554615 scopus 로고    scopus 로고
    • Multiple domains of DFF45 bind synergistically to DFF40: Roles of caspase cleavage and sequestration of activator domain of DFF40
    • McCarty J. S., Toh S. Y., Li P. Multiple domains of DFF45 bind synergistically to DFF40: Roles of caspase cleavage and sequestration of activator domain of DFF40. Biochem. Biophys. Res. Commun. 264:1999;181-185.
    • (1999) Biochem. Biophys. Res. Commun. , vol.264 , pp. 181-185
    • McCarty, J.S.1    Toh, S.Y.2    Li, P.3
  • 44
    • 0029992278 scopus 로고    scopus 로고
    • Molecular chaperones in cellular protein folding
    • Hartl F. U. Molecular chaperones in cellular protein folding. Nature. 381:1996;571-579.
    • (1996) Nature , vol.381 , pp. 571-579
    • Hartl, F.U.1
  • 45
    • 0033553481 scopus 로고    scopus 로고
    • Activation of the apoptotic endonuclease DFF40 (caspase-activated DNase or nuclease). Oligomerization and direct interaction with histone H1
    • Liu X., Zou H., Widlak P., Garrard W., Wang X. Activation of the apoptotic endonuclease DFF40 (caspase-activated DNase or nuclease). Oligomerization and direct interaction with histone H1. J. Biol. Chem. 274:1999;13836-13840.
    • (1999) J. Biol. Chem. , vol.274 , pp. 13836-13840
    • Liu, X.1    Zou, H.2    Widlak, P.3    Garrard, W.4    Wang, X.5
  • 46
    • 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 D. C., van Kaer L., Wang X., Xu M. Resistance to DNA fragmentation and chromatin condensation in mice lacking the DNA fragmentation factor 45. Proc. Natl. Acad. Sci. USA. 95:1998;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
    • 0027217084 scopus 로고
    • Apoptotic death in epithelial cells: Cleavage of DNA to 300 and/or 50 kb fragments prior to or in the absence of internucleosomal fragmentation
    • Oberhammer F., Wilson J. W., Dive C., Morris I. D., Hickman J. A., Wakeling A. E., Walker P. R., Sikorska M. Apoptotic death in epithelial cells: Cleavage of DNA to 300 and/or 50 kb fragments prior to or in the absence of internucleosomal fragmentation. EMBO J. 12:1993;3679-3684.
    • (1993) EMBO J. , vol.12 , pp. 3679-3684
    • Oberhammer, F.1    Wilson, J.W.2    Dive, C.3    Morris, I.D.4    Hickman, J.A.5    Wakeling, A.E.6    Walker, P.R.7    Sikorska, M.8
  • 50
    • 0029130703 scopus 로고
    • Large-scale fragmentation of mammalian DNA in the course of apoptosis proceeds via excision of chromosomal DNA loops and their oligomers
    • Lagarkova M. A., Iarovaia O. V., Razin S. V. Large-scale fragmentation of mammalian DNA in the course of apoptosis proceeds via excision of chromosomal DNA loops and their oligomers. J. Biol. Chem. 270:1995;20239-20241.
    • (1995) J. Biol. Chem. , vol.270 , pp. 20239-20241
    • Lagarkova, M.A.1    Iarovaia, O.V.2    Razin, S.V.3
  • 52
    • 0033587066 scopus 로고    scopus 로고
    • Apoptotic nuclear morphological change without DNA fragmentation
    • Sakahira H., Enari M., Ohsawa Y., Uchiyama Y., Nagata S. Apoptotic nuclear morphological change without DNA fragmentation. Curr. Biol. 9:1999;543-546.
    • (1999) Curr. Biol. , vol.9 , pp. 543-546
    • Sakahira, H.1    Enari, M.2    Ohsawa, Y.3    Uchiyama, Y.4    Nagata, S.5
  • 53
    • 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., Tsujimoto Y. Acinus is a caspase-3-activated protein required for apoptotic chromatin condensation. Nature. 401:1999;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
  • 54
    • 0033601251 scopus 로고    scopus 로고
    • DNA fragmentation factor 45-deficient cells are more resistant to apoptosis and exhibit different dying morphology than wild-type control cells
    • Zhang J., Wang X., Bove K., Xu M. DNA fragmentation factor 45-deficient cells are more resistant to apoptosis and exhibit different dying morphology than wild-type control cells. J. Biol. Chem. 274:1999;37450-37454.
    • (1999) J. Biol. Chem. , vol.274 , pp. 37450-37454
    • Zhang, J.1    Wang, X.2    Bove, K.3    Xu, M.4


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