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Volumn 1813, Issue 2, 2011, Pages 315-321

Evidence for a second messenger function of dUTP during Bax mediated apoptosis of yeast and mammalian cells

Author keywords

Anti apoptosis; Anti apoptotic; Anti death; Apoptosis; C2C12 cells; Cell death; Cell survival; DUTP; Yeast

Indexed keywords

CADMIUM; CERAMIDE; COMPLEMENTARY DNA; DEOXYURIDINE PHOSPHATE; DEOXYURIDINE TRIPHOSPHATE PYROPHOSPHATASE; HYDROGEN PEROXIDE; PROTEIN BAX; REACTIVE OXYGEN METABOLITE;

EID: 78650956818     PISSN: 01674889     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamcr.2010.11.021     Document Type: Article
Times cited : (25)

References (58)
  • 3
    • 77955965172 scopus 로고    scopus 로고
    • Cellular stress responses: cell survival and cell death
    • Fulda S., Gorman A.M., Hori O., Samali A. Cellular stress responses: cell survival and cell death. Int. J. Cell. Biol. 2010, 2010:214074.
    • (2010) Int. J. Cell. Biol. , vol.2010 , pp. 214074
    • Fulda, S.1    Gorman, A.M.2    Hori, O.3    Samali, A.4
  • 4
    • 73349091842 scopus 로고    scopus 로고
    • The role of mitochondria in apoptosis
    • Wang C., Youle R.J. The role of mitochondria in apoptosis. Annu. Rev. Genet. 2009, 43:95-118.
    • (2009) Annu. Rev. Genet. , vol.43 , pp. 95-118
    • Wang, C.1    Youle, R.J.2
  • 5
    • 41149152733 scopus 로고    scopus 로고
    • How do BCL-2 proteins induce mitochondrial outer membrane permeabilization?
    • Chipuk J.E., Green D.R. How do BCL-2 proteins induce mitochondrial outer membrane permeabilization?. Trends Cell Biol. 2008, 18:157-164.
    • (2008) Trends Cell Biol. , vol.18 , pp. 157-164
    • Chipuk, J.E.1    Green, D.R.2
  • 7
    • 77949890661 scopus 로고    scopus 로고
    • Heat shock proteins; an overview
    • Tutar L., Tutar Y. Heat shock proteins; an overview. Curr. Pharm. Biotechnol. 2010, 11:216-222.
    • (2010) Curr. Pharm. Biotechnol. , vol.11 , pp. 216-222
    • Tutar, L.1    Tutar, Y.2
  • 10
    • 47149103242 scopus 로고    scopus 로고
    • Pre-conditioning and postconditioning to limit ischemia-reperfusion-induced myocardial injury: what could be the next footstep?
    • Balakumar P., Rohilla A., Singh M. Pre-conditioning and postconditioning to limit ischemia-reperfusion-induced myocardial injury: what could be the next footstep?. Pharmacol. Res. 2008, 57:403-412.
    • (2008) Pharmacol. Res. , vol.57 , pp. 403-412
    • Balakumar, P.1    Rohilla, A.2    Singh, M.3
  • 11
    • 58149296552 scopus 로고    scopus 로고
    • Tumor resistance to apoptosis
    • Fulda S. Tumor resistance to apoptosis. Int. J. Cancer 2009, 124:511-515.
    • (2009) Int. J. Cancer , vol.124 , pp. 511-515
    • Fulda, S.1
  • 12
    • 77955933845 scopus 로고    scopus 로고
    • Evasion of apoptosis as a cellular stress response in cancer
    • Fulda S. Evasion of apoptosis as a cellular stress response in cancer. Int. J. Cell. Biol. 2010, 2010:370835.
    • (2010) Int. J. Cell. Biol. , vol.2010 , pp. 370835
    • Fulda, S.1
  • 13
    • 33846847943 scopus 로고    scopus 로고
    • Decoding NMDA receptor signaling: identification of genomic programs specifying neuronal survival and death
    • Zhang S.J., Steijaert M.N., Lau D., Schutz G., Delucinge-Vivier C., Descombes P., Bading H. Decoding NMDA receptor signaling: identification of genomic programs specifying neuronal survival and death. Neuron 2007, 53:549-562.
    • (2007) Neuron , vol.53 , pp. 549-562
    • Zhang, S.J.1    Steijaert, M.N.2    Lau, D.3    Schutz, G.4    Delucinge-Vivier, C.5    Descombes, P.6    Bading, H.7
  • 15
    • 45049085330 scopus 로고    scopus 로고
    • The pleiotropic effects of heterologous Bax expression in yeast
    • Khoury C.M., Greenwood M.T. The pleiotropic effects of heterologous Bax expression in yeast. Biochim. Biophys. Acta 2008, 1783:1449-1465.
    • (2008) Biochim. Biophys. Acta , vol.1783 , pp. 1449-1465
    • Khoury, C.M.1    Greenwood, M.T.2
  • 18
    • 77950854718 scopus 로고    scopus 로고
    • Expressing and functional analysis of mammalian apoptotic regulators in yeast
    • Greenwood M.T., Ludovico P. Expressing and functional analysis of mammalian apoptotic regulators in yeast. Cell Death Differ. 2010, 17:737-745.
    • (2010) Cell Death Differ. , vol.17 , pp. 737-745
    • Greenwood, M.T.1    Ludovico, P.2
  • 20
    • 77952741735 scopus 로고    scopus 로고
    • Modelling neurodegeneration in Saccharomyces cerevisiae: why cook with baker's yeast?
    • Khurana V., Lindquist S. Modelling neurodegeneration in Saccharomyces cerevisiae: why cook with baker's yeast?. Nat. Rev. Neurosci. 2010, 11:436-449.
    • (2010) Nat. Rev. Neurosci. , vol.11 , pp. 436-449
    • Khurana, V.1    Lindquist, S.2
  • 22
    • 33745883535 scopus 로고    scopus 로고
    • Identification of mouse sphingomyelin synthase 1 as a suppressor of Bax-mediated cell death in yeast
    • Yang Z., Khoury C., Jean-Baptiste G., Greenwood M.T. Identification of mouse sphingomyelin synthase 1 as a suppressor of Bax-mediated cell death in yeast. FEMS Yeast Res. 2006, 6:751-762.
    • (2006) FEMS Yeast Res. , vol.6 , pp. 751-762
    • Yang, Z.1    Khoury, C.2    Jean-Baptiste, G.3    Greenwood, M.T.4
  • 24
    • 0030964838 scopus 로고    scopus 로고
    • Defective viral vectors as agents for gene transfer in the nervous system
    • Kaplitt M.G., Makimura H. Defective viral vectors as agents for gene transfer in the nervous system. J. Neurosci. Methods 1997, 71:125-132.
    • (1997) J. Neurosci. Methods , vol.71 , pp. 125-132
    • Kaplitt, M.G.1    Makimura, H.2
  • 26
    • 46949102023 scopus 로고    scopus 로고
    • Transmembrane protein 85 from both human (TMEM85) and yeast (YGL231c) inhibit hydrogen peroxide mediated cell death in yeast
    • Ring G., Khoury C.M., Solar A.J., Yang Z., Mandato C.A., Greenwood M.T. Transmembrane protein 85 from both human (TMEM85) and yeast (YGL231c) inhibit hydrogen peroxide mediated cell death in yeast. FEBS Lett. 2008, 582:2637-2642.
    • (2008) FEBS Lett. , vol.582 , pp. 2637-2642
    • Ring, G.1    Khoury, C.M.2    Solar, A.J.3    Yang, Z.4    Mandato, C.A.5    Greenwood, M.T.6
  • 28
    • 0030791450 scopus 로고    scopus 로고
    • The human dUTPase gene encodes both nuclear and mitochondrial isoforms. Differential expression of the isoforms and characterization of a cDNA encoding the mitochondrial species
    • Ladner R.D., Caradonna S.J. The human dUTPase gene encodes both nuclear and mitochondrial isoforms. Differential expression of the isoforms and characterization of a cDNA encoding the mitochondrial species. J. Biol. Chem. 1997, 272:19072-19080.
    • (1997) J. Biol. Chem. , vol.272 , pp. 19072-19080
    • Ladner, R.D.1    Caradonna, S.J.2
  • 29
    • 61849128423 scopus 로고    scopus 로고
    • Keeping uracil out of DNA: physiological role, structure and catalytic mechanism of dUTPases
    • Vertessy B.G., Toth J. Keeping uracil out of DNA: physiological role, structure and catalytic mechanism of dUTPases. Acc. Chem. Res. 2009, 42:97-106.
    • (2009) Acc. Chem. Res. , vol.42 , pp. 97-106
    • Vertessy, B.G.1    Toth, J.2
  • 30
    • 29144487060 scopus 로고    scopus 로고
    • AP endonuclease deficiency results in extreme sensitivity to thymidine deprivation
    • Dornfeld K., Johnson M. AP endonuclease deficiency results in extreme sensitivity to thymidine deprivation. Nucleic Acids Res. 2005, 33:6644-6653.
    • (2005) Nucleic Acids Res. , vol.33 , pp. 6644-6653
    • Dornfeld, K.1    Johnson, M.2
  • 31
    • 0036731991 scopus 로고    scopus 로고
    • DUTPase and uracil-DNA glycosylase are central modulators of antifolate toxicity in Saccharomyces cerevisiae
    • Tinkelenberg B.A., Hansbury M.J., Ladner R.D. dUTPase and uracil-DNA glycosylase are central modulators of antifolate toxicity in Saccharomyces cerevisiae. Cancer Res. 2002, 62:4909-4915.
    • (2002) Cancer Res. , vol.62 , pp. 4909-4915
    • Tinkelenberg, B.A.1    Hansbury, M.J.2    Ladner, R.D.3
  • 34
    • 31644442238 scopus 로고    scopus 로고
    • Linking uracil base excision repair and 5-fluorouracil toxicity in yeast
    • Seiple L., Jaruga P., Dizdaroglu M., Stivers J.T. Linking uracil base excision repair and 5-fluorouracil toxicity in yeast. Nucleic Acids Res. 2006, 34:140-151.
    • (2006) Nucleic Acids Res. , vol.34 , pp. 140-151
    • Seiple, L.1    Jaruga, P.2    Dizdaroglu, M.3    Stivers, J.T.4
  • 35
    • 33746539166 scopus 로고    scopus 로고
    • DNA precursor pools and genomic stability
    • Mathews C.K. DNA precursor pools and genomic stability. FASEB J. 2006, 20:1300-1314.
    • (2006) FASEB J. , vol.20 , pp. 1300-1314
    • Mathews, C.K.1
  • 36
    • 50949083311 scopus 로고    scopus 로고
    • Chronological aging-induced apoptosis in yeast
    • Fabrizio P., Longo V.D. Chronological aging-induced apoptosis in yeast. Biochim. Biophys. Acta 2008, 1783:1280-1285.
    • (2008) Biochim. Biophys. Acta , vol.1783 , pp. 1280-1285
    • Fabrizio, P.1    Longo, V.D.2
  • 38
    • 44149107268 scopus 로고    scopus 로고
    • Cadmium induces a heterogeneous and caspase-dependent apoptotic response in Saccharomyces cerevisiae
    • Nargund A.M., Avery S.V., Houghton J.E. Cadmium induces a heterogeneous and caspase-dependent apoptotic response in Saccharomyces cerevisiae. Apoptosis 2008, 13:811-821.
    • (2008) Apoptosis , vol.13 , pp. 811-821
    • Nargund, A.M.1    Avery, S.V.2    Houghton, J.E.3
  • 39
    • 23444440791 scopus 로고    scopus 로고
    • Role of Smac/DIABLO in hydrogen peroxide-induced apoptosis in C2C12 myogenic cells
    • Jiang B., Xiao W., Shi Y., Liu M., Xiao X. Role of Smac/DIABLO in hydrogen peroxide-induced apoptosis in C2C12 myogenic cells. Free Radic. Biol. Med. 2005, 39:658-667.
    • (2005) Free Radic. Biol. Med. , vol.39 , pp. 658-667
    • Jiang, B.1    Xiao, W.2    Shi, Y.3    Liu, M.4    Xiao, X.5
  • 40
    • 0346996448 scopus 로고    scopus 로고
    • Heat shock protein 90 suppresses tumor necrosis factor alpha induced apoptosis by preventing the cleavage of Bid in NIH3T3 fibroblasts
    • Zhao C., Wang E. Heat shock protein 90 suppresses tumor necrosis factor alpha induced apoptosis by preventing the cleavage of Bid in NIH3T3 fibroblasts. Cell. Signal. 2004, 16:313-321.
    • (2004) Cell. Signal. , vol.16 , pp. 313-321
    • Zhao, C.1    Wang, E.2
  • 41
    • 68949210567 scopus 로고    scopus 로고
    • Anti-apoptotic genes in the survival of monocytic cells during infection
    • Busca A., Saxena M., Kryworuchko M., Kumar A. Anti-apoptotic genes in the survival of monocytic cells during infection. Curr. Genomics 2009, 10:306-317.
    • (2009) Curr. Genomics , vol.10 , pp. 306-317
    • Busca, A.1    Saxena, M.2    Kryworuchko, M.3    Kumar, A.4
  • 43
    • 0023786047 scopus 로고
    • Bcl-2 gene promotes haemopoietic cell survival and cooperates with c-myc to immortalize pre-B cells
    • Vaux D.L., Cory S., Adams J.M. Bcl-2 gene promotes haemopoietic cell survival and cooperates with c-myc to immortalize pre-B cells. Nature 1988, 335:440-442.
    • (1988) Nature , vol.335 , pp. 440-442
    • Vaux, D.L.1    Cory, S.2    Adams, J.M.3
  • 44
    • 76049083966 scopus 로고    scopus 로고
    • Reactive oxygen species, cellular redox systems, and apoptosis
    • Circu M.L., Aw T.Y. Reactive oxygen species, cellular redox systems, and apoptosis. Free Radic. Biol. Med. 2010, 48:749-762.
    • (2010) Free Radic. Biol. Med. , vol.48 , pp. 749-762
    • Circu, M.L.1    Aw, T.Y.2
  • 45
    • 78049509565 scopus 로고    scopus 로고
    • Tales and mysteries of the enigmatic sphingomyelin synthase family
    • C.D.P. Chalfant, Maurizio (Eds.)
    • Holthuis J.C.M., Luberto C. Tales and mysteries of the enigmatic sphingomyelin synthase family. Advances in Experimental Medicine and Biology 2010, vol. 668. C.D.P. Chalfant, Maurizio (Eds.).
    • (2010) Advances in Experimental Medicine and Biology , vol.668
    • Holthuis, J.C.M.1    Luberto, C.2
  • 46
    • 45549097700 scopus 로고    scopus 로고
    • Uracil within DNA: an actor of antiviral immunity
    • Sire J., Querat G., Esnault C., Priet S. Uracil within DNA: an actor of antiviral immunity. Retrovirology 2008, 5:45.
    • (2008) Retrovirology , vol.5 , pp. 45
    • Sire, J.1    Querat, G.2    Esnault, C.3    Priet, S.4
  • 47
    • 0027426749 scopus 로고
    • DUTP pyrophosphatase is an essential enzyme in Saccharomyces cerevisiae
    • Gadsden M.H., McIntosh E.M., Game J.C., Wilson P.J., Haynes R.H. dUTP pyrophosphatase is an essential enzyme in Saccharomyces cerevisiae. EMBO J. 1993, 12:4425-4431.
    • (1993) EMBO J. , vol.12 , pp. 4425-4431
    • Gadsden, M.H.1    McIntosh, E.M.2    Game, J.C.3    Wilson, P.J.4    Haynes, R.H.5
  • 48
    • 33645924354 scopus 로고    scopus 로고
    • DUTPase activity is critical to maintain genetic stability in Saccharomyces cerevisiae
    • Guillet M., Van Der Kemp P.A., Boiteux S. dUTPase activity is critical to maintain genetic stability in Saccharomyces cerevisiae. Nucleic Acids Res. 2006, 34:2056-2066.
    • (2006) Nucleic Acids Res. , vol.34 , pp. 2056-2066
    • Guillet, M.1    Van Der Kemp, P.A.2    Boiteux, S.3
  • 49
    • 0026724896 scopus 로고
    • The presence of uracil-DNA glycosylase in insects is dependent upon developmental complexity
    • Dudley B., Hammond A., Deutsch W.A. The presence of uracil-DNA glycosylase in insects is dependent upon developmental complexity. J. Biol. Chem. 1992, 267:11964-11967.
    • (1992) J. Biol. Chem. , vol.267 , pp. 11964-11967
    • Dudley, B.1    Hammond, A.2    Deutsch, W.A.3
  • 50
    • 39149103752 scopus 로고    scopus 로고
    • A tyrosine kinase inhibitor, beta-hydroxyisovalerylshikonin, induced apoptosis in human lung cancer DMS114 cells through reduction of dUTP nucleotidohydrolase activity
    • Kajimoto S., Horie M., Manabe H., Masuda Y., Shibayama-Imazu T., Nakajo S., Gong X.F., Obama T., Itabe H., Nakaya K. A tyrosine kinase inhibitor, beta-hydroxyisovalerylshikonin, induced apoptosis in human lung cancer DMS114 cells through reduction of dUTP nucleotidohydrolase activity. Biochim. Biophys. Acta 2008, 1782:41-50.
    • (2008) Biochim. Biophys. Acta , vol.1782 , pp. 41-50
    • Kajimoto, S.1    Horie, M.2    Manabe, H.3    Masuda, Y.4    Shibayama-Imazu, T.5    Nakajo, S.6    Gong, X.F.7    Obama, T.8    Itabe, H.9    Nakaya, K.10
  • 51
    • 53849136625 scopus 로고    scopus 로고
    • Viral subversion of apoptotic enzymes: escape from death row
    • Best S.M. Viral subversion of apoptotic enzymes: escape from death row. Annu. Rev. Microbiol. 2008, 62:171-192.
    • (2008) Annu. Rev. Microbiol. , vol.62 , pp. 171-192
    • Best, S.M.1
  • 53
    • 77952669155 scopus 로고    scopus 로고
    • Regulation of ceramide channels by Bcl-2 family proteins
    • Ganesan V., Colombini M. Regulation of ceramide channels by Bcl-2 family proteins. FEBS Lett. 2010, 584:2128-2134.
    • (2010) FEBS Lett. , vol.584 , pp. 2128-2134
    • Ganesan, V.1    Colombini, M.2
  • 56
    • 0031783829 scopus 로고    scopus 로고
    • H2O2 acts on cellular membranes to generate ceramide signaling and initiate apoptosis in tracheobronchial epithelial cells
    • Goldkorn T., Balaban N., Shannon M., Chea V., Matsukuma K., Gilchrist D., Wang H., Chan C. H2O2 acts on cellular membranes to generate ceramide signaling and initiate apoptosis in tracheobronchial epithelial cells. J. Cell Sci. 1998, 111(Pt 21):3209-3220.
    • (1998) J. Cell Sci. , vol.111 , Issue.PART 21 , pp. 3209-3220
    • Goldkorn, T.1    Balaban, N.2    Shannon, M.3    Chea, V.4    Matsukuma, K.5    Gilchrist, D.6    Wang, H.7    Chan, C.8
  • 57
    • 0030915927 scopus 로고    scopus 로고
    • Modulation of cell death in yeast by the Bcl-2 family of proteins
    • Tao W., Kurschner C., Morgan J.I. Modulation of cell death in yeast by the Bcl-2 family of proteins. J. Biol. Chem. 1997, 272:15547-15552.
    • (1997) J. Biol. Chem. , vol.272 , pp. 15547-15552
    • Tao, W.1    Kurschner, C.2    Morgan, J.I.3
  • 58
    • 3543022743 scopus 로고    scopus 로고
    • Tomato phospholipid hydroperoxide glutathione peroxidase inhibits cell death induced by Bax and oxidative stresses in yeast and plants
    • Chen S., Vaghchhipawala Z., Li W., Asard H., Dickman M.B. Tomato phospholipid hydroperoxide glutathione peroxidase inhibits cell death induced by Bax and oxidative stresses in yeast and plants. Plant Physiol. 2004, 135:1630-1641.
    • (2004) Plant Physiol. , vol.135 , pp. 1630-1641
    • Chen, S.1    Vaghchhipawala, Z.2    Li, W.3    Asard, H.4    Dickman, M.B.5


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