메뉴 건너뛰기




Volumn 25, Issue 5, 2004, Pages 259-264

Nuclear and mitochondrial conversations in cell death: PARP-1 and AIF signaling

Author keywords

[No Author keywords available]

Indexed keywords

APOPTOSIS INDUCING FACTOR; CASPASE; DNA; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE;

EID: 2142694340     PISSN: 01656147     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tips.2004.03.005     Document Type: Article
Times cited : (420)

References (55)
  • 2
    • 0015383455 scopus 로고
    • Apoptosis: A basic biological phenomenon with wide-ranging implications in tissue kinetics
    • Kerr J.F., et al. Apoptosis: a basic biological phenomenon with wide-ranging implications in tissue kinetics. Br. J. Cancer. 26:1972;239-257
    • (1972) Br. J. Cancer , vol.26 , pp. 239-257
    • Kerr, J.F.1
  • 3
    • 0030842946 scopus 로고    scopus 로고
    • Poly(ADP-ribose) polymerase gene disruption renders mice resistant to cerebral ischemia
    • Eliasson M.J., et al. Poly(ADP-ribose) polymerase gene disruption renders mice resistant to cerebral ischemia. Nat. Med. 3:1997;1089-1095
    • (1997) Nat. Med. , vol.3 , pp. 1089-1095
    • Eliasson, M.J.1
  • 4
    • 0030832874 scopus 로고    scopus 로고
    • Ischemic brain injury is mediated by the activation of poly(ADP-ribose)polymerase
    • Endres M., et al. Ischemic brain injury is mediated by the activation of poly(ADP-ribose)polymerase. J. Cereb. Blood Flow Metab. 17:1997;1143-1151
    • (1997) J. Cereb. Blood Flow Metab. , vol.17 , pp. 1143-1151
    • Endres, M.1
  • 5
    • 0028294246 scopus 로고
    • Nitric oxide activation of poly(ADP-ribose) synthetase in neurotoxicity
    • Zhang J., et al. Nitric oxide activation of poly(ADP-ribose) synthetase in neurotoxicity. Science. 263:1994;687-689
    • (1994) Science , vol.263 , pp. 687-689
    • Zhang, J.1
  • 6
    • 0348109491 scopus 로고    scopus 로고
    • Poly(ADP-ribose) polymerase-1 and apoptosis inducing factor in neurotoxicity
    • (in press).
    • Yu, S.W., et al. Poly(ADP-ribose) polymerase-1 and apoptosis inducing factor in neurotoxicity. Neurobiol. Dis. (in press).
    • Neurobiol. Dis.
    • Yu, S.W.1
  • 7
    • 0035281786 scopus 로고    scopus 로고
    • The world according to PARP
    • Smith S. The world according to PARP. Trends Biochem. Sci. 26:2001;174-179
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 174-179
    • Smith, S.1
  • 8
    • 0034124881 scopus 로고    scopus 로고
    • Roles of poly(ADP-ribosyl)ation and PARP in apoptosis, DNA repair, genomic stability and functions of p53 and E2F-1
    • Smulson M.E., et al. Roles of poly(ADP-ribosyl)ation and PARP in apoptosis, DNA repair, genomic stability and functions of p53 and E2F-1. Adv. Enzyme Regul. 40:2000;183-215
    • (2000) Adv. Enzyme Regul. , vol.40 , pp. 183-215
    • Smulson, M.E.1
  • 9
    • 0034733928 scopus 로고    scopus 로고
    • Poly(ADP-ribose) polymerase-1: What have we learned from the deficient mouse model?
    • Shall S., de Murcia G. Poly(ADP-ribose) polymerase-1: what have we learned from the deficient mouse model? Mutat. Res. 460:2000;1-15
    • (2000) Mutat. Res. , vol.460 , pp. 1-15
    • Shall, S.1    De Murcia, G.2
  • 10
    • 0038449141 scopus 로고    scopus 로고
    • PARP-1, a determinant of cell survival in response to DNA damage
    • Bouchard V.J., et al. PARP-1, a determinant of cell survival in response to DNA damage. Exp. Hematol. 31:2003;446-454
    • (2003) Exp. Hematol. , vol.31 , pp. 446-454
    • Bouchard, V.J.1
  • 11
    • 0036499892 scopus 로고    scopus 로고
    • Poly(ADP-ribose) polymerase: Killer or conspirator? the 'suicide hypothesis' revisited
    • Chiarugi A. Poly(ADP-ribose) polymerase: killer or conspirator? The 'suicide hypothesis' revisited. Trends Pharmacol. Sci. 23:2002;122-129
    • (2002) Trends Pharmacol. Sci. , vol.23 , pp. 122-129
    • Chiarugi, A.1
  • 12
    • 0038641860 scopus 로고    scopus 로고
    • A proteomic approach to the identification of heterogeneous nuclear ribonucleoproteins as a new family of poly(ADP-ribose)-binding proteins
    • Gagne J.P., et al. A proteomic approach to the identification of heterogeneous nuclear ribonucleoproteins as a new family of poly(ADP-ribose)- binding proteins. Biochem. J. 371:2003;331-340
    • (2003) Biochem. J. , vol.371 , pp. 331-340
    • Gagne, J.P.1
  • 13
    • 0036733355 scopus 로고    scopus 로고
    • The therapeutic potential of poly(ADP-Ribose) polymerase inhibitors
    • Virag L., Szabo C. The therapeutic potential of poly(ADP-Ribose) polymerase inhibitors. Pharmacol. Rev. 54:2002;375-429
    • (2002) Pharmacol. Rev. , vol.54 , pp. 375-429
    • Virag, L.1    Szabo, C.2
  • 15
    • 0028865245 scopus 로고
    • Post-translational modification of poly(ADP-ribose) polymerase induced by DNA strand breaks
    • Lindahl T., et al. Post-translational modification of poly(ADP-ribose) polymerase induced by DNA strand breaks. Trends Biochem. Sci. 20:1995;405-411
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 405-411
    • Lindahl, T.1
  • 16
    • 0037016765 scopus 로고    scopus 로고
    • Transcriptional repression by binding of poly(ADP-ribose) polymerase to promoter sequences
    • Soldatenkov V.A., et al. Transcriptional repression by binding of poly(ADP-ribose) polymerase to promoter sequences. J. Biol. Chem. 277:2002;665-670
    • (2002) J. Biol. Chem. , vol.277 , pp. 665-670
    • Soldatenkov, V.A.1
  • 17
    • 0037462597 scopus 로고    scopus 로고
    • Chromatin loosening by poly(ADP)-ribose polymerase (PARP) at Drosophila puff loci
    • Tulin A., Spradling A. Chromatin loosening by poly(ADP)-ribose polymerase (PARP) at Drosophila puff loci. Science. 299:2003;560-562
    • (2003) Science , vol.299 , pp. 560-562
    • Tulin, A.1    Spradling, A.2
  • 18
    • 0035202873 scopus 로고    scopus 로고
    • Regulation of microglial expression of integrins by poly(ADP-ribose) polymerase-1
    • Ullrich O., et al. Regulation of microglial expression of integrins by poly(ADP-ribose) polymerase-1. Nat. Cell Biol. 3:2001;1035-1042
    • (2001) Nat. Cell Biol. , vol.3 , pp. 1035-1042
    • Ullrich, O.1
  • 19
    • 0037178870 scopus 로고    scopus 로고
    • Centromere proteins Cenpa, Cenpb, and Bub3 interact with poly(ADP-ribose) polymerase-1 protein and are poly(ADP-ribosyl)ated
    • Saxena A., et al. Centromere proteins Cenpa, Cenpb, and Bub3 interact with poly(ADP-ribose) polymerase-1 protein and are poly(ADP-ribosyl)ated. J. Biol. Chem. 277:2002;26921-26926
    • (2002) J. Biol. Chem. , vol.277 , pp. 26921-26926
    • Saxena, A.1
  • 20
    • 0032127666 scopus 로고    scopus 로고
    • Role of poly(ADP-ribose) synthetase in inflammation and ischaemia- reperfusion
    • Szabo C., Dawson V.L. Role of poly(ADP-ribose) synthetase in inflammation and ischaemia- reperfusion. Trends Pharmacol. Sci. 19:1998;287-298
    • (1998) Trends Pharmacol. Sci. , vol.19 , pp. 287-298
    • Szabo, C.1    Dawson, V.L.2
  • 21
    • 0037713529 scopus 로고    scopus 로고
    • Apoptosis inducing factor and PARP-mediated injury in the MPTP mouse model of Parkinson's disease
    • Wang H., et al. Apoptosis inducing factor and PARP-mediated injury in the MPTP mouse model of Parkinson's disease. Ann. New York Acad Sci. 991:2003;132-139
    • (2003) Ann. New York Acad Sci , vol.991 , pp. 132-139
    • Wang, H.1
  • 22
    • 0035929591 scopus 로고    scopus 로고
    • TANK2, a new TRF1-associated poly(ADP-ribose) polymerase, causes rapid induction of cell death upon overexpression
    • Kaminker P.G., et al. TANK2, a new TRF1-associated poly(ADP-ribose) polymerase, causes rapid induction of cell death upon overexpression. J. Biol. Chem. 276:2001;35891-35899
    • (2001) J. Biol. Chem. , vol.276 , pp. 35891-35899
    • Kaminker, P.G.1
  • 23
    • 0032193692 scopus 로고    scopus 로고
    • Poly(ADP-ribose) synthetase activation mediates mitochondrial injury during oxidant-induced cell death
    • Virag L., et al. Poly(ADP-ribose) synthetase activation mediates mitochondrial injury during oxidant-induced cell death. J. Immunol. 161:1998;3753-3759
    • (1998) J. Immunol. , vol.161 , pp. 3753-3759
    • Virag, L.1
  • 24
    • 0038043242 scopus 로고    scopus 로고
    • Intra-mitochondrial poly(ADP-ribosylation) contributes to NAD+ depletion and cell death induced by oxidative stress
    • Du L., et al. Intra-mitochondrial poly(ADP-ribosylation) contributes to NAD+ depletion and cell death induced by oxidative stress. J. Biol. Chem. 278:2003;18426-18433
    • (2003) J. Biol. Chem. , vol.278 , pp. 18426-18433
    • Du, L.1
  • 25
    • 0037067317 scopus 로고    scopus 로고
    • Mediation of poly(ADP-ribose) polymerase-1-dependent cell death by apoptosis-inducing factor
    • Yu, S.W., et al. (2002) Mediation of poly(ADP-ribose) polymerase-1-dependent cell death by apoptosis-inducing factor. Science 297, 259-263.
    • (2002) Science , vol.297 , pp. 259-263
    • Yu, S.W.1
  • 26
    • 0033830186 scopus 로고    scopus 로고
    • Poly(ADP-ribose) polymerase-1 in the nervous system
    • Ha H.C., Snyder S.H. Poly(ADP-ribose) polymerase-1 in the nervous system. Neurobiol. Dis. 7:2000;225-239
    • (2000) Neurobiol. Dis. , vol.7 , pp. 225-239
    • Ha, H.C.1    Snyder, S.H.2
  • 27
    • 0022634961 scopus 로고
    • Metabolic consequences of DNA damage: DNA damage induces alterations in glucose metabolism by activation of poly(ADP-ribose) polymerase
    • Berger S.J., et al. Metabolic consequences of DNA damage: DNA damage induces alterations in glucose metabolism by activation of poly(ADP-ribose) polymerase. Biochem. Biophys. Res. Commun. 134:1986;227-232
    • (1986) Biochem. Biophys. Res. Commun. , vol.134 , pp. 227-232
    • Berger, S.J.1
  • 28
    • 0020980976 scopus 로고
    • Poly(ADP-ribose) polymerase mediates the suicide response to massive DNA damage: Studies in normal and DNA-repair defective cells
    • Berger N.A., et al. Poly(ADP-ribose) polymerase mediates the suicide response to massive DNA damage: studies in normal and DNA-repair defective cells. Princess Takamatsu Symp. 13:1983;219-226
    • (1983) Princess Takamatsu Symp. , vol.13 , pp. 219-226
    • Berger, N.A.1
  • 29
    • 0036218940 scopus 로고    scopus 로고
    • Poly(ADP-ribose) polymerase impairs early and long-term experimental stroke recovery
    • Goto S., et al. Poly(ADP-ribose) polymerase impairs early and long-term experimental stroke recovery. Stroke. 33:2002;1101-1106
    • (2002) Stroke , vol.33 , pp. 1101-1106
    • Goto, S.1
  • 30
    • 85047691537 scopus 로고    scopus 로고
    • Inhibition of GAPDH activity by poly(ADP-ribose) polymerase activates three major pathways of hyperglycemic damage in endothelial cells
    • Du X., et al. Inhibition of GAPDH activity by poly(ADP-ribose) polymerase activates three major pathways of hyperglycemic damage in endothelial cells. J. Clin. Invest. 112:2003;1049-1057
    • (2003) J. Clin. Invest. , vol.112 , pp. 1049-1057
    • Du, X.1
  • 31
    • 0033198919 scopus 로고    scopus 로고
    • Poly(ADP-ribosyl)ation reactions in the regulation of nuclear functions
    • D'Amours, D., et al. (1999) Poly(ADP-ribosyl)ation reactions in the regulation of nuclear functions. Biochem. J. 342, 249-268.
    • (1999) Biochem. J. , vol.342 , pp. 249-268
    • D'Amours, D.1
  • 32
    • 0034731455 scopus 로고    scopus 로고
    • Poly(ADP-ribose) binds to specific domains in DNA damage checkpoint proteins
    • Pleschke J.M., et al. Poly(ADP-ribose) binds to specific domains in DNA damage checkpoint proteins. J. Biol. Chem. 275:2000;40974-40980
    • (2000) J. Biol. Chem. , vol.275 , pp. 40974-40980
    • Pleschke, J.M.1
  • 33
    • 0030761351 scopus 로고    scopus 로고
    • ATM-dependent telomere loss in aging human diploid fibroblasts and DNA damage lead to the post-translational activation of p53 protein involving poly(ADP-ribose) polymerase
    • Vaziri H., et al. ATM-dependent telomere loss in aging human diploid fibroblasts and DNA damage lead to the post-translational activation of p53 protein involving poly(ADP-ribose) polymerase. EMBO J. 16:1997;6018-6033
    • (1997) EMBO J. , vol.16 , pp. 6018-6033
    • Vaziri, H.1
  • 34
    • 18544371050 scopus 로고    scopus 로고
    • DNA binding is required for the apoptogenic action of apoptosis inducing factor
    • Ye H., et al. DNA binding is required for the apoptogenic action of apoptosis inducing factor. Nat. Struct. Biol. 9:2002;680-684
    • (2002) Nat. Struct. Biol. , vol.9 , pp. 680-684
    • Ye, H.1
  • 35
    • 0033521741 scopus 로고    scopus 로고
    • Molecular characterization of mitochondrial apoptosis-inducing factor
    • Susin S.A., et al. Molecular characterization of mitochondrial apoptosis-inducing factor. Nature. 397:1999;441-446
    • (1999) Nature , vol.397 , pp. 441-446
    • Susin, S.A.1
  • 36
    • 0042237031 scopus 로고    scopus 로고
    • Mitochondrial release of AIF and EndoG requires caspase activation downstream of Bax/Bak-mediated permeabilization
    • Arnoult D., et al. Mitochondrial release of AIF and EndoG requires caspase activation downstream of Bax/Bak-mediated permeabilization. EMBO J. 22:2003;4385-4399
    • (2003) EMBO J. , vol.22 , pp. 4385-4399
    • Arnoult, D.1
  • 37
    • 17944366977 scopus 로고    scopus 로고
    • Heat-shock protein 70 antagonizes apoptosis-inducing factor
    • Ravagnan L., et al. Heat-shock protein 70 antagonizes apoptosis-inducing factor. Nat. Cell Biol. 3:2001;839-843
    • (2001) Nat. Cell Biol. , vol.3 , pp. 839-843
    • Ravagnan, L.1
  • 38
    • 0242426634 scopus 로고    scopus 로고
    • HSP72 inhibits apoptosis-inducing factor release in ATP depleted renal epithelial cells
    • Ruchalski K., et al. HSP72 inhibits apoptosis-inducing factor release in ATP depleted renal epithelial cells. Am. J. Physiol. Cell Physiol. 285:2003;1483-1493
    • (2003) Am. J. Physiol. Cell Physiol. , vol.285 , pp. 1483-1493
    • Ruchalski, K.1
  • 39
    • 0035844170 scopus 로고    scopus 로고
    • NADH oxidase activity of mitochondrial apoptosis-inducing factor
    • Miramar M.D., et al. NADH oxidase activity of mitochondrial apoptosis-inducing factor. J. Biol. Chem. 276:2001;16391-16398
    • (2001) J. Biol. Chem. , vol.276 , pp. 16391-16398
    • Miramar, M.D.1
  • 40
    • 0036263870 scopus 로고    scopus 로고
    • The crystal structure of the mouse apoptosis-inducing factor AIF
    • Mate M.J., et al. The crystal structure of the mouse apoptosis-inducing factor AIF. Nat. Struct. Biol. 9:2002;442-446
    • (2002) Nat. Struct. Biol. , vol.9 , pp. 442-446
    • Mate, M.J.1
  • 41
    • 0035078404 scopus 로고    scopus 로고
    • Dominant cell death induction by extramitochondrially targeted apoptosis-inducing factor
    • Loeffler M., et al. Dominant cell death induction by extramitochondrially targeted apoptosis-inducing factor. FASEB J. 15:2001;758-767
    • (2001) FASEB J. , vol.15 , pp. 758-767
    • Loeffler, M.1
  • 42
    • 0037159784 scopus 로고    scopus 로고
    • Mechanisms of AIF-mediated apoptotic DNA degradation in Caenorhabditis elegans
    • Wang X., et al. Mechanisms of AIF-mediated apoptotic DNA degradation in Caenorhabditis elegans. Science. 298:2002;1587-1592
    • (2002) Science , vol.298 , pp. 1587-1592
    • Wang, X.1
  • 43
    • 0037925454 scopus 로고    scopus 로고
    • CRN-1, a Caenorhabditis elegans FEN-1 homologue, cooperates with CPS-6/EndoG to promote apoptotic DNA degradation
    • Parrish J.Z., et al. CRN-1, a Caenorhabditis elegans FEN-1 homologue, cooperates with CPS-6/EndoG to promote apoptotic DNA degradation. EMBO J. 22:2003;3451-3460
    • (2003) EMBO J. , vol.22 , pp. 3451-3460
    • Parrish, J.Z.1
  • 44
    • 0037131519 scopus 로고    scopus 로고
    • Dueling activities of AIF in cell death versus survival: DNA binding and redox activity
    • Lipton S.A., Bossy-Wetzel E. Dueling activities of AIF in cell death versus survival: DNA binding and redox activity. Cell. 111:2002;147-150
    • (2002) Cell , vol.111 , pp. 147-150
    • Lipton, S.A.1    Bossy-Wetzel, E.2
  • 45
    • 0037179691 scopus 로고    scopus 로고
    • The harlequin mouse mutation downregulates apoptosis-inducing factor
    • Klein J.A., et al. The harlequin mouse mutation downregulates apoptosis-inducing factor. Nature. 419:2002;367-374
    • (2002) Nature , vol.419 , pp. 367-374
    • Klein, J.A.1
  • 46
    • 0035967169 scopus 로고    scopus 로고
    • Essential role of the mitochondrial apoptosis-inducing factor in programmed cell death
    • Joza N., et al. Essential role of the mitochondrial apoptosis-inducing factor in programmed cell death. Nature. 410:2001;549-554
    • (2001) Nature , vol.410 , pp. 549-554
    • Joza, N.1
  • 47
    • 0034698733 scopus 로고    scopus 로고
    • Two distinct pathways leading to nuclear apoptosis
    • Susin S.A., et al. Two distinct pathways leading to nuclear apoptosis. J. Exp. Med. 192:2000;571-580
    • (2000) J. Exp. Med. , vol.192 , pp. 571-580
    • Susin, S.A.1
  • 48
    • 0036323443 scopus 로고    scopus 로고
    • Apoptosis-inducing factor is involved in the regulation of caspase-independent neuronal cell death
    • Cregan S.P., et al. Apoptosis-inducing factor is involved in the regulation of caspase-independent neuronal cell death. J. Cell Biol. 158:2002;507-517
    • (2002) J. Cell Biol. , vol.158 , pp. 507-517
    • Cregan, S.P.1
  • 49
    • 18644377709 scopus 로고    scopus 로고
    • Critical role of photoreceptor apoptosis in functional damage after retinal detachment
    • Hisatomi T., et al. Critical role of photoreceptor apoptosis in functional damage after retinal detachment. Curr. Eye Res. 24:2002;161-172
    • (2002) Curr. Eye Res. , vol.24 , pp. 161-172
    • Hisatomi, T.1
  • 50
    • 20244364788 scopus 로고    scopus 로고
    • Intranuclear localization of apoptosis-inducing factor (AIF) and large scale DNA fragmentation after traumatic brain injury in rats and in neuronal cultures exposed to peroxynitrite
    • Zhang X., et al. Intranuclear localization of apoptosis-inducing factor (AIF) and large scale DNA fragmentation after traumatic brain injury in rats and in neuronal cultures exposed to peroxynitrite. J. Neurochem. 82:2002;181-191
    • (2002) J. Neurochem. , vol.82 , pp. 181-191
    • Zhang, X.1
  • 51
    • 0038493644 scopus 로고    scopus 로고
    • Involvement of apoptosis-inducing factor in neuronal death after hypoxia-ischemia in the neonatal rat brain
    • Zhu C., et al. Involvement of apoptosis-inducing factor in neuronal death after hypoxia-ischemia in the neonatal rat brain. J. Neurochem. 86:2003;306-317
    • (2003) J. Neurochem. , vol.86 , pp. 306-317
    • Zhu, C.1
  • 52
    • 0035890012 scopus 로고    scopus 로고
    • Apoptosis-inducing factor mediates microglial and neuronal apoptosis caused by pneumococcus
    • Braun J.S., et al. Apoptosis-inducing factor mediates microglial and neuronal apoptosis caused by pneumococcus. J. Infect. Dis. 184:2001;1300-1309
    • (2001) J. Infect. Dis. , vol.184 , pp. 1300-1309
    • Braun, J.S.1
  • 53
    • 0041335559 scopus 로고    scopus 로고
    • Minocycline inhibits caspase-independent and -dependent mitochondrial cell death pathways in models of Huntington's disease
    • Wang X., et al. Minocycline inhibits caspase-independent and -dependent mitochondrial cell death pathways in models of Huntington's disease. Proc. Natl. Acad. Sci. U. S. A. 100:2003;10483-10487
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 10483-10487
    • Wang, X.1
  • 54
    • 0035433420 scopus 로고    scopus 로고
    • Four deaths and a funeral: From caspases to alternative mechanisms
    • Leist M., 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
  • 55
    • 0034910509 scopus 로고    scopus 로고
    • Death receptor-induced apoptotic and necrotic cell death: Differential role of caspases and mitochondria
    • Denecker G., et al. Death receptor-induced apoptotic and necrotic cell death: differential role of caspases and mitochondria. Cell Death Differ. 8:2001;829-840
    • (2001) Cell Death Differ. , vol.8 , pp. 829-840
    • Denecker, G.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.