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Volumn 1780, Issue 5, 2008, Pages 793-799

Degradation of caspase-activated DNase by the ubiquitin-proteasome system

Author keywords

CAD; HeLa; ICAD; NIH3T3; Ubiquitination

Indexed keywords

BENZYLOXYCARBONYLLEUCYLLEUCYLLEUCINAL; CASPASE ACTIVATED DEOXYRIBONUCLEASE; NUCLEASE; PROTEASOME; UBIQUITIN;

EID: 45049088373     PISSN: 03044165     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbagen.2007.12.003     Document Type: Article
Times cited : (4)

References (34)
  • 1
    • 17644393549 scopus 로고    scopus 로고
    • DNA degradation in development and programmed cell death
    • Nagata S. DNA degradation in development and programmed cell death. Annu. Rev. Immunol. 23 (2005) 853-875
    • (2005) Annu. Rev. Immunol. , vol.23 , pp. 853-875
    • Nagata, S.1
  • 2
    • 0036469777 scopus 로고    scopus 로고
    • Apoptotic DNA fragmentation and tissue homeostasis
    • Zhang J., and Xu M. Apoptotic DNA fragmentation and tissue homeostasis. Trends Cell Biol. 12 (2002) 84-89
    • (2002) Trends Cell Biol. , vol.12 , pp. 84-89
    • Zhang, J.1    Xu, M.2
  • 4
    • 0028048788 scopus 로고
    • Multiple forms of nuclear deoxyribonuclease in rat thymocytes
    • Tanuma S., and Shiokawa D. Multiple forms of nuclear deoxyribonuclease in rat thymocytes. Biochem. Biophys. Res. Commun. 203 (1994) 789-797
    • (1994) Biochem. Biophys. Res. Commun. , vol.203 , pp. 789-797
    • Tanuma, S.1    Shiokawa, D.2
  • 5
    • 0030926327 scopus 로고    scopus 로고
    • Androgen ablation leads to an upregulation and intranuclear accumulation of deoxyribonuclease I in rat prostate epithelial cells paralleling their apoptotic elimination
    • Rauch F., Polzar B., Stephan H., Zanotti S., Paddenberg R., and Mannherz H.G. Androgen ablation leads to an upregulation and intranuclear accumulation of deoxyribonuclease I in rat prostate epithelial cells paralleling their apoptotic elimination. J. Cell Biol. 137 (1997) 909-923
    • (1997) J. Cell Biol. , vol.137 , pp. 909-923
    • Rauch, F.1    Polzar, B.2    Stephan, H.3    Zanotti, S.4    Paddenberg, R.5    Mannherz, H.G.6
  • 6
    • 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. 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
  • 7
    • 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
  • 9
    • 0037276548 scopus 로고    scopus 로고
    • Mutually regulated expression of caspase-activated DNase and its inhibitor for apoptotic DNA fragmentation
    • Nagase H., Fukuyama H., Tanaka M., Kawane K., and Nagata S. Mutually regulated expression of caspase-activated DNase and its inhibitor for apoptotic DNA fragmentation. Cell Death Differ. 10 (2003) 142-143
    • (2003) Cell Death Differ. , vol.10 , pp. 142-143
    • Nagase, H.1    Fukuyama, H.2    Tanaka, M.3    Kawane, K.4    Nagata, S.5
  • 11
    • 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., and 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
  • 12
    • 0034677931 scopus 로고    scopus 로고
    • Cleavage preferences of the apoptotic endonuclease DFF40 (caspase-activated DNase or nuclease) on naked DNA and chromatin substrates
    • Widlak P., Li P., Wang X., and Garrard W.T. Cleavage preferences of the apoptotic endonuclease DFF40 (caspase-activated DNase or nuclease) on naked DNA and chromatin substrates. J. Biol. Chem. 275 (2000) 8226-8232
    • (2000) J. Biol. Chem. , vol.275 , pp. 8226-8232
    • Widlak, P.1    Li, P.2    Wang, X.3    Garrard, W.T.4
  • 13
    • 0034678123 scopus 로고    scopus 로고
    • Specific chaperone-like activity of inhibitor of caspase-activated DNase for caspase-activated DNase
    • Sakahira H., Iwamatsu A., and Nagata S. Specific chaperone-like activity of inhibitor of caspase-activated DNase for caspase-activated DNase. J. Biol. Chem. 275 (2000) 8091-8096
    • (2000) J. Biol. Chem. , vol.275 , pp. 8091-8096
    • Sakahira, H.1    Iwamatsu, A.2    Nagata, S.3
  • 14
    • 0033554636 scopus 로고    scopus 로고
    • Study of DFF45 in its role of chaperone and inhibitor: two independent inhibitory domains of DFF40 nuclease activity
    • McCarty J.S., Toh S.Y., and Li P. Study of DFF45 in its role of chaperone and inhibitor: two independent inhibitory domains of DFF40 nuclease activity. Biochem. Biophys. Res. Commun. 264 (1999) 176-180
    • (1999) Biochem. Biophys. Res. Commun. , vol.264 , pp. 176-180
    • McCarty, J.S.1    Toh, S.Y.2    Li, P.3
  • 15
    • 0032535483 scopus 로고    scopus 로고
    • The ubiquitin-proteasome pathway: on protein death and cell life
    • Ciechanover A. The ubiquitin-proteasome pathway: on protein death and cell life. Embo J. 17 (1998) 7151-7160
    • (1998) Embo J. , vol.17 , pp. 7151-7160
    • Ciechanover, A.1
  • 16
    • 0031822941 scopus 로고    scopus 로고
    • Mycoplasma nucleases able to induce internucleosomal DNA degradation in cultured cells possess many characteristics of eukaryotic apoptotic nucleases
    • Paddenberg R., Weber A., Wulf S., and Mannherz H.G. Mycoplasma nucleases able to induce internucleosomal DNA degradation in cultured cells possess many characteristics of eukaryotic apoptotic nucleases. Cell Death Differ. 5 (1998) 517-528
    • (1998) Cell Death Differ. , vol.5 , pp. 517-528
    • Paddenberg, R.1    Weber, A.2    Wulf, S.3    Mannherz, H.G.4
  • 17
    • 0029818003 scopus 로고    scopus 로고
    • Internucleosomal DNA fragmentation in cultured cells under conditions reported to induce apoptosis may be caused by mycoplasma endonucleases
    • Paddenberg R., Wulf S., Weber A., Heimann P., Beck L.A., and Mannherz H.G. Internucleosomal DNA fragmentation in cultured cells under conditions reported to induce apoptosis may be caused by mycoplasma endonucleases. Eur. J. Cell Biol. 71 (1996) 105-119
    • (1996) Eur. J. Cell Biol. , vol.71 , pp. 105-119
    • Paddenberg, R.1    Wulf, S.2    Weber, A.3    Heimann, P.4    Beck, L.A.5    Mannherz, H.G.6
  • 18
    • 33847322104 scopus 로고    scopus 로고
    • RNAi knockdown of caspase-activated DNase inhibits rotenone-induced DNA fragmentation in HeLa cells
    • Tsuruta T., Oh-Hashi K., Ueno Y., Kitade Y., Kiuchi K., and Hirata Y. RNAi knockdown of caspase-activated DNase inhibits rotenone-induced DNA fragmentation in HeLa cells. Neurochem. Int. 50 (2007) 601-606
    • (2007) Neurochem. Int. , vol.50 , pp. 601-606
    • Tsuruta, T.1    Oh-Hashi, K.2    Ueno, Y.3    Kitade, Y.4    Kiuchi, K.5    Hirata, Y.6
  • 19
    • 0026611735 scopus 로고
    • Thapsigargin, and AIF4- stimulate the accumulation of GRP78 mRNA in a cycloheximide dependent manner, whilst induction by hypoxia is independent of protein synthesis
    • Price B.D., Mannheim-Rodman L.A., Calderwood S.K., and Brefeldin A. Thapsigargin, and AIF4- stimulate the accumulation of GRP78 mRNA in a cycloheximide dependent manner, whilst induction by hypoxia is independent of protein synthesis. J. Cell Physiol. 152 (1992) 545-552
    • (1992) J. Cell Physiol. , vol.152 , pp. 545-552
    • Price, B.D.1    Mannheim-Rodman, L.A.2    Calderwood, S.K.3    Brefeldin, A.4
  • 21
    • 0027276494 scopus 로고
    • The protein kinase inhibitor staurosporine induces morphological changes typical of apoptosis in MOLT-4 cells without concomitant DNA fragmentation
    • Falcieri E., Martelli A.M., Bareggi R., Cataldi A., and Cocco L. The protein kinase inhibitor staurosporine induces morphological changes typical of apoptosis in MOLT-4 cells without concomitant DNA fragmentation. Biochem. Biophys. Res. Commun. 193 (1993) 19-25
    • (1993) Biochem. Biophys. Res. Commun. , vol.193 , pp. 19-25
    • Falcieri, E.1    Martelli, A.M.2    Bareggi, R.3    Cataldi, A.4    Cocco, L.5
  • 22
    • 84975751684 scopus 로고
    • Complex I inhibitors induce dose-dependent apoptosis in PC12 cells: relevance to Parkinson's disease
    • Hartley A., Stone J.M., Heron C., Cooper J.M., and Schapira A.H. Complex I inhibitors induce dose-dependent apoptosis in PC12 cells: relevance to Parkinson's disease. J. Neurochem. 63 (1994) 1987-1990
    • (1994) J. Neurochem. , vol.63 , pp. 1987-1990
    • Hartley, A.1    Stone, J.M.2    Heron, C.3    Cooper, J.M.4    Schapira, A.H.5
  • 23
    • 0035900197 scopus 로고    scopus 로고
    • Caspase-3 activation induced by inhibition of mitochondrial complex I is facilitated by glycogen synthase kinase-3beta and attenuated by lithium
    • King T.D., Bijur G.N., and Jope R.S. Caspase-3 activation induced by inhibition of mitochondrial complex I is facilitated by glycogen synthase kinase-3beta and attenuated by lithium. Brain Res. 919 (2001) 106-114
    • (2001) Brain Res. , vol.919 , pp. 106-114
    • King, T.D.1    Bijur, G.N.2    Jope, R.S.3
  • 24
    • 0031712374 scopus 로고    scopus 로고
    • Activation of JNK pathway and induction of apoptosis by manganese in PC12 cells
    • Hirata Y., Adachi K., and Kiuchi K. Activation of JNK pathway and induction of apoptosis by manganese in PC12 cells. J. Neurochem. 71 (1998) 1607-1615
    • (1998) J. Neurochem. , vol.71 , pp. 1607-1615
    • Hirata, Y.1    Adachi, K.2    Kiuchi, K.3
  • 25
    • 0035859853 scopus 로고    scopus 로고
    • Mitochondria play no roles in Mn(II)-induced apoptosis in HeLa cells
    • Oubrahim H., Stadtman E.R., and Chock P.B. Mitochondria play no roles in Mn(II)-induced apoptosis in HeLa cells. Proc. Natl. Acad. Sci. U. S. A. 98 (2001) 9505-9510
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 9505-9510
    • Oubrahim, H.1    Stadtman, E.R.2    Chock, P.B.3
  • 27
    • 0034643336 scopus 로고    scopus 로고
    • Rapid degradation of a large fraction of newly synthesized proteins by proteasomes
    • Schubert U., Anton L.C., Gibbs J., Norbury C.C., Yewdell J.W., and Bennink J.R. Rapid degradation of a large fraction of newly synthesized proteins by proteasomes. Nature 404 (2000) 770-774
    • (2000) Nature , vol.404 , pp. 770-774
    • Schubert, U.1    Anton, L.C.2    Gibbs, J.3    Norbury, C.C.4    Yewdell, J.W.5    Bennink, J.R.6
  • 28
    • 0035976991 scopus 로고    scopus 로고
    • CAD/DFF40 nuclease is dispensable for high molecular weight DNA cleavage and stage I chromatin condensation in apoptosis
    • Samejima K., Tone S., and Earnshaw W.C. CAD/DFF40 nuclease is dispensable for high molecular weight DNA cleavage and stage I chromatin condensation in apoptosis. J. Biol. Chem. 276 (2001) 45427-45432
    • (2001) J. Biol. Chem. , vol.276 , pp. 45427-45432
    • Samejima, K.1    Tone, S.2    Earnshaw, W.C.3
  • 29
    • 0037077292 scopus 로고    scopus 로고
    • The role of topoisomerase II in the excision of DNA loop domains during apoptosis
    • Solovyan V.T., Bezvenyuk Z.A., Salminen A., Austin C.A., and Courtney M.J. The role of topoisomerase II in the excision of DNA loop domains during apoptosis. J. Biol. Chem. 277 (2002) 21458-21467
    • (2002) J. Biol. Chem. , vol.277 , pp. 21458-21467
    • Solovyan, V.T.1    Bezvenyuk, Z.A.2    Salminen, A.3    Austin, C.A.4    Courtney, M.J.5
  • 30
    • 0036629253 scopus 로고    scopus 로고
    • Protein quality control: U-box-containing E3 ubiquitin ligases join the fold
    • Cyr D.M., Hohfeld J., and Patterson C. Protein quality control: U-box-containing E3 ubiquitin ligases join the fold. Trends Biochem. Sci. 27 (2002) 368-375
    • (2002) Trends Biochem. Sci. , vol.27 , pp. 368-375
    • Cyr, D.M.1    Hohfeld, J.2    Patterson, C.3
  • 31
    • 0037401714 scopus 로고    scopus 로고
    • CHIP: a quality-control E3 ligase collaborating with molecular chaperones
    • Murata S., Chiba T., and Tanaka K. CHIP: a quality-control E3 ligase collaborating with molecular chaperones. Int. J. Biochem. Cell Biol. 35 (2003) 572-578
    • (2003) Int. J. Biochem. Cell Biol. , vol.35 , pp. 572-578
    • Murata, S.1    Chiba, T.2    Tanaka, K.3
  • 32
    • 0041439707 scopus 로고    scopus 로고
    • Heat shock protein 70 binds caspase-activated DNase and enhances its activity in TCR-stimulated T cells
    • Liu Q.L., Kishi H., Ohtsuka K., and Muraguchi A. Heat shock protein 70 binds caspase-activated DNase and enhances its activity in TCR-stimulated T cells. Blood 102 (2003) 1788-1796
    • (2003) Blood , vol.102 , pp. 1788-1796
    • Liu, Q.L.1    Kishi, H.2    Ohtsuka, K.3    Muraguchi, A.4
  • 33
    • 0028276554 scopus 로고
    • Degradation of the tumor suppressor protein p53 by the ubiquitin-mediated proteolytic system requires a novel species of ubiquitin-carrier protein, E2
    • Ciechanover A., Shkedy D., Oren M., and Bercovich B. Degradation of the tumor suppressor protein p53 by the ubiquitin-mediated proteolytic system requires a novel species of ubiquitin-carrier protein, E2. J. Biol. Chem. 269 (1994) 9582-9589
    • (1994) J. Biol. Chem. , vol.269 , pp. 9582-9589
    • Ciechanover, A.1    Shkedy, D.2    Oren, M.3    Bercovich, B.4
  • 34
    • 0027358723 scopus 로고
    • The HPV-16 E6 and E6-AP complex functions as a ubiquitin-protein ligase in the ubiquitination of p53
    • Scheffner M., Huibregtse J.M., Vierstra R.D., and Howley P.M. The HPV-16 E6 and E6-AP complex functions as a ubiquitin-protein ligase in the ubiquitination of p53. Cell 75 (1993) 495-505
    • (1993) Cell , vol.75 , pp. 495-505
    • Scheffner, M.1    Huibregtse, J.M.2    Vierstra, R.D.3    Howley, P.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.