메뉴 건너뛰기




Volumn 35, Issue 6, 2003, Pages 559-567

Mitochondria-assisted cell suicide: A license to kill

Author keywords

Apoptosis; Bcl 2; Mitochondria; Ventricular myocytes

Indexed keywords

CYTOCHROME C; DIAZOXIDE; NICORANDIL; PROTEIN; PROTEIN BAD; PROTEIN BAK; PROTEIN BAX; PROTEIN BCL 2; PROTEIN BCL W; PROTEIN BCL X; PROTEIN BID; PROTEIN BNIP3; PROTEIN MCL 1; PROTEIN NIX; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE; UNCLASSIFIED DRUG;

EID: 0037604666     PISSN: 00222828     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-2828(03)00118-4     Document Type: Review
Times cited : (72)

References (90)
  • 1
    • 0027479796 scopus 로고
    • Apoptosis (the 1992 Frank Rose Memorial Lecture)
    • Wyllie A.H. Apoptosis (the 1992 Frank Rose Memorial Lecture). Br J Cancer. 67:(2):1993;205-208.
    • (1993) Br J Cancer , vol.67 , Issue.2 , pp. 205-208
    • Wyllie, A.H.1
  • 2
    • 0028780735 scopus 로고
    • Apoptosis. Death gets a brake [news; Comment]
    • Wyllie A.H. Apoptosis. Death gets a brake [news; comment]. Nature. 369:(6478):1994;272-273.
    • (1994) Nature , vol.369 , Issue.6478 , pp. 272-273
    • Wyllie, A.H.1
  • 3
    • 0025932984 scopus 로고
    • Apoptosis: Mechanisms and roles in pathology
    • Arends M.J., Wyllie A.H. Apoptosis: mechanisms and roles in pathology. Int Rev Exp Pathol. 32:1991;223-254.
    • (1991) Int Rev Exp Pathol , vol.32 , pp. 223-254
    • Arends, M.J.1    Wyllie, A.H.2
  • 4
    • 0028939862 scopus 로고
    • The genetic regulation of apoptosis
    • Wyllie A.H. The genetic regulation of apoptosis. Curr Opin Genet Dev. 5:(1):1995;97-104.
    • (1995) Curr Opin Genet Dev , vol.5 , Issue.1 , pp. 97-104
    • Wyllie, A.H.1
  • 5
    • 0026670335 scopus 로고
    • Apoptosis and the regulation of cell numbers in normal and neoplastic tissues: An overview
    • Wyllie A.H. Apoptosis and the regulation of cell numbers in normal and neoplastic tissues: an overview. Cancer Metast Rev. 11:(2):1992;95-103.
    • (1992) Cancer Metast Rev , vol.11 , Issue.2 , pp. 95-103
    • Wyllie, A.H.1
  • 6
    • 0028943734 scopus 로고
    • Apoptosis in the pathogenesis and treatment of disease
    • Thompson C.B. Apoptosis in the pathogenesis and treatment of disease. Science. 267:(5203):1995;1456-1462.
    • (1995) Science , vol.267 , Issue.5203 , pp. 1456-1462
    • Thompson, C.B.1
  • 7
    • 0028283855 scopus 로고
    • Cell death in cancer and development. AACR special conference in cancer research
    • Eastman A., Grant S., Lock R., Tritton T., Van Houten N., Yuan J. Cell death in cancer and development. AACR special conference in cancer research. Cancer Res. 54:(10):1994;2812-2818.
    • (1994) Cancer Res , vol.54 , Issue.10 , pp. 2812-2818
    • Eastman, A.1    Grant, S.2    Lock, R.3    Tritton, T.4    Van Houten, N.5    Yuan, J.6
  • 8
    • 0028890119 scopus 로고
    • Apoptosis and cancer: The failure of controls on cell death and cell survival
    • Martin S.J., Green D.R. Apoptosis and cancer: the failure of controls on cell death and cell survival. Crit Rev Oncol Hematol. 18:(2):1995;137-153.
    • (1995) Crit Rev Oncol Hematol , vol.18 , Issue.2 , pp. 137-153
    • Martin, S.J.1    Green, D.R.2
  • 9
    • 0027935409 scopus 로고
    • Hypoxia induces apoptosis with enhanced expression of Fas antigen messenger RNA in cultured neonatal rat cardiomyocytes
    • Tanaka M., Ito H., Adachi S., Akimoto H., Nishikawa T., Kasajima T., et al. Hypoxia induces apoptosis with enhanced expression of Fas antigen messenger RNA in cultured neonatal rat cardiomyocytes. Circ Res. 75:(3):1994;426-433.
    • (1994) Circ Res , vol.75 , Issue.3 , pp. 426-433
    • Tanaka, M.1    Ito, H.2    Adachi, S.3    Akimoto, H.4    Nishikawa, T.5    Kasajima, T.6
  • 10
    • 0033959317 scopus 로고    scopus 로고
    • Caspase activation and mitochondrial cytochrome C release during hypoxia-mediated apoptosis of adult ventricular myocytes
    • Moissac D., Gurevich R.M., Zheng H., Singal P.K., Kirshenbaum L.A. Caspase activation and mitochondrial cytochrome C release during hypoxia-mediated apoptosis of adult ventricular myocytes. J Mol Cell Cardiol. 32:(1):2000;53-63.
    • (2000) J Mol Cell Cardiol , vol.32 , Issue.1 , pp. 53-63
    • Moissac, D.1    Gurevich, R.M.2    Zheng, H.3    Singal, P.K.4    Kirshenbaum, L.A.5
  • 11
    • 0032728077 scopus 로고    scopus 로고
    • Bishopric NH. Hypoxia-activated apoptosis of cardiac myocytes requires reoxygenation or a pH shift and is independent of p53
    • Webster K.A., Discher D.J., Kaiser S., Hernandez O., Sato B. Bishopric NH. Hypoxia-activated apoptosis of cardiac myocytes requires reoxygenation or a pH shift and is independent of p53. J Clin Invest. 104:(3):1999;239-252.
    • (1999) J Clin Invest , vol.104 , Issue.3 , pp. 239-252
    • Webster, K.A.1    Discher, D.J.2    Kaiser, S.3    Hernandez, O.4    Sato, B.5
  • 12
    • 0029885316 scopus 로고    scopus 로고
    • Preconditioning rabbit cardiomyocytes: Role of pH, vacuolar proton ATPase, and apoptosis
    • Gottlieb R.A., Gruol D.L., Zhu J.Y., Engler R.L. Preconditioning rabbit cardiomyocytes: role of pH, vacuolar proton ATPase, and apoptosis. J Clin Invest. 97:(10):1996;2391-2398.
    • (1996) J Clin Invest , vol.97 , Issue.10 , pp. 2391-2398
    • Gottlieb, R.A.1    Gruol, D.L.2    Zhu, J.Y.3    Engler, R.L.4
  • 13
    • 0030031983 scopus 로고    scopus 로고
    • Sonnenblick EH, Krajewski S, et al. Apoptotic and necrotic myocyte cell deaths are independent contributing variables of infarct size in rats
    • Kajstura J., Cheng W., Reiss K., Clark W.A.R. Sonnenblick EH, Krajewski S, et al. Apoptotic and necrotic myocyte cell deaths are independent contributing variables of infarct size in rats. Lab Invest. 74:(1):1996;86-107.
    • (1996) Lab Invest , vol.74 , Issue.1 , pp. 86-107
    • Kajstura, J.1    Cheng, W.2    Reiss, K.3    Clark, W.A.R.4
  • 15
    • 0028088576 scopus 로고
    • End-stage cardiac failure in humans is coupled with the induction of proliferating cell nuclear antigen and nuclear mitotic division in ventricular myocytes
    • Quaini F., Cigola E., Lagrasta C., Saccani G., Quaini E., Rossi C., et al. End-stage cardiac failure in humans is coupled with the induction of proliferating cell nuclear antigen and nuclear mitotic division in ventricular myocytes. Circ Res. 75:1994;1050-1063.
    • (1994) Circ Res , vol.75 , pp. 1050-1063
    • Quaini, F.1    Cigola, E.2    Lagrasta, C.3    Saccani, G.4    Quaini, E.5    Rossi, C.6
  • 16
    • 0029022554 scopus 로고
    • Apoptosis in human atherosclerosis and restenosis
    • Isner J.M., Kearney M., Bortman S., Passeri J. Apoptosis in human atherosclerosis and restenosis. Circulation. 91:(11):1995;2703-2711.
    • (1995) Circulation , vol.91 , Issue.11 , pp. 2703-2711
    • Isner, J.M.1    Kearney, M.2    Bortman, S.3    Passeri, J.4
  • 17
    • 0028334555 scopus 로고
    • Normal and abnormal consequences of apoptosis in the human heart. From postnatal morphogenesis to paroxysmal arrhythmias
    • James T.N. Normal and abnormal consequences of apoptosis in the human heart. From postnatal morphogenesis to paroxysmal arrhythmias. Circulation. 90:(1):1994;556-573.
    • (1994) Circulation , vol.90 , Issue.1 , pp. 556-573
    • James, T.N.1
  • 18
    • 0028147070 scopus 로고
    • Programmed cell death in Caenorhabditis elegans
    • Hengartner M.O., Horvitz H.R. Programmed cell death in Caenorhabditis elegans. Curr Opin Genet Dev. 4:(4):1994;581-586.
    • (1994) Curr Opin Genet Dev , vol.4 , Issue.4 , pp. 581-586
    • Hengartner, M.O.1    Horvitz, H.R.2
  • 19
    • 0028288277 scopus 로고
    • C. elegans cell survival gene ced-9 encodes a functional homolog of the mammalian proto-oncogene bcl-2
    • Hengartner M.O., Horvitz H.R. C. elegans cell survival gene ced-9 encodes a functional homolog of the mammalian proto-oncogene bcl-2. Cell. 76:(4):1994;665-676.
    • (1994) Cell , vol.76 , Issue.4 , pp. 665-676
    • Hengartner, M.O.1    Horvitz, H.R.2
  • 20
    • 0028281026 scopus 로고
    • Bcl-2 protein localizes to the chromosomes of mitotic nuclei and is correlated with the cell cycle in cultured epithelial cell lines
    • Lu Q.L., Hanby A.M., Nasser Hajibagheri M.A., Gschmeissner S.E., Lu P.J., Taylor Papadimitriou J., et al. Bcl-2 protein localizes to the chromosomes of mitotic nuclei and is correlated with the cell cycle in cultured epithelial cell lines. J Cell Sci. 107:(Pt 2):1994;363-371.
    • (1994) J Cell Sci , vol.107 , Issue.PART 2 , pp. 363-371
    • Lu, Q.L.1    Hanby, A.M.2    Nasser Hajibagheri, M.A.3    Gschmeissner, S.E.4    Lu, P.J.5    Taylor Papadimitriou, J.6
  • 21
    • 0028972616 scopus 로고
    • Regulation of apoptosis by bcl-2 family proteins and its role in cancer and chemoresistance
    • Reed J.C. Regulation of apoptosis by bcl-2 family proteins and its role in cancer and chemoresistance. Curr Opin Oncol. 7:(6):1995;541-546.
    • (1995) Curr Opin Oncol , vol.7 , Issue.6 , pp. 541-546
    • Reed, J.C.1
  • 22
    • 0020658766 scopus 로고
    • Immunoglobulin gene rearrangement and cell surface antigen expression in acute lymphocytic leukemias of T cell and B cell precursor origins
    • Korsmeyer S.J., Arnold A., Bakhshi A., Ravetch J.V., Siebenlist U., Hieter P.A., et al. Immunoglobulin gene rearrangement and cell surface antigen expression in acute lymphocytic leukemias of T cell and B cell precursor origins. J Clin Invest. 71:(2):1983;301-313.
    • (1983) J Clin Invest , vol.71 , Issue.2 , pp. 301-313
    • Korsmeyer, S.J.1    Arnold, A.2    Bakhshi, A.3    Ravetch, J.V.4    Siebenlist, U.5    Hieter, P.A.6
  • 24
    • 0027346272 scopus 로고
    • Programmed cell death: Bcl-2
    • Korsmeyer S.J. Programmed cell death: Bcl-2. Import Adv Oncol. 1993;19-28.
    • (1993) Import Adv Oncol , pp. 19-28
    • Korsmeyer, S.J.1
  • 25
    • 0030047365 scopus 로고    scopus 로고
    • Functional dissection of the human Bc12 protein: Sequence requirements for inhibition of apoptosis
    • Hunter J.J., Bond B.L., Parslow T.G. Functional dissection of the human Bc12 protein: sequence requirements for inhibition of apoptosis. Mol Cell Biol. 16:(3):1996;877-883.
    • (1996) Mol Cell Biol , vol.16 , Issue.3 , pp. 877-883
    • Hunter, J.J.1    Bond, B.L.2    Parslow, T.G.3
  • 26
    • 0029032660 scopus 로고
    • Structure-function analysis of Bcl-2 protein. Identification of conserved domains important for homodimerization with Bcl-2 and heterodimerization with Bax
    • Hanada M., Aime Sempe C., Sato T., Reed J.C. Structure-function analysis of Bcl-2 protein. Identification of conserved domains important for homodimerization with Bcl-2 and heterodimerization with Bax. J Biol Chem. 270:(20):1995;11962-11969.
    • (1995) J Biol Chem , vol.270 , Issue.20 , pp. 11962-11969
    • Hanada, M.1    Aime Sempe, C.2    Sato, T.3    Reed, J.C.4
  • 27
    • 0028206341 scopus 로고
    • Korsmeyer SJ. BH1 and BH2 domains of Bcl-2 are required for inhibition of apoptosis and heterodimerization with Bax [see comments]
    • Yin X.M., Oltvai Z.N. Korsmeyer SJ. BH1 and BH2 domains of Bcl-2 are required for inhibition of apoptosis and heterodimerization with Bax [see comments]. Nature. 369:(6478):1994;321-323.
    • (1994) Nature , vol.369 , Issue.6478 , pp. 321-323
    • Yin, X.M.1    Oltvai, Z.N.2
  • 28
    • 5244224827 scopus 로고    scopus 로고
    • X-ray and NMR structure of human Bcl-xL, an inhibitor of programmed cell death
    • Muchmore S.W., Sattler M., Liang H., Meadows R.P., Harlan J.E., Yoon H.S., et al. X-ray and NMR structure of human Bcl-xL, an inhibitor of programmed cell death. Nature. 381:(6580):1996;335-341.
    • (1996) Nature , vol.381 , Issue.6580 , pp. 335-341
    • Muchmore, S.W.1    Sattler, M.2    Liang, H.3    Meadows, R.P.4    Harlan, J.E.5    Yoon, H.S.6
  • 29
    • 0028809209 scopus 로고
    • Bad, a heterodimeric partner for Bcl-XL and Bcl-2, displaces Bax and promotes cell death
    • Yang E., Zha J., Jockel J., Boise L.H., Thompson C.B., Korsmeyer S.J. Bad, a heterodimeric partner for Bcl-XL and Bcl-2, displaces Bax and promotes cell death. Cell. 80:(2):1995;285-291.
    • (1995) Cell , vol.80 , Issue.2 , pp. 285-291
    • Yang, E.1    Zha, J.2    Jockel, J.3    Boise, L.H.4    Thompson, C.B.5    Korsmeyer, S.J.6
  • 30
    • 0032575752 scopus 로고    scopus 로고
    • Mitochondria and apoptosis
    • Green D.R., Reed J.C. Mitochondria and apoptosis. Science. 281:(5381):1998;1309-1312.
    • (1998) Science , vol.281 , Issue.5381 , pp. 1309-1312
    • Green, D.R.1    Reed, J.C.2
  • 31
    • 1842332735 scopus 로고    scopus 로고
    • Bcl-x(L) forms an ion channel in synthetic lipid membranes
    • Minn A.J., Velez P., Schendel S.L., Liang H., Muchmore S.W., Fesik S.W., et al. Bcl-x(L) forms an ion channel in synthetic lipid membranes. Nature. 385:(6614):1997;353-357.
    • (1997) Nature , vol.385 , Issue.6614 , pp. 353-357
    • Minn, A.J.1    Velez, P.2    Schendel, S.L.3    Liang, H.4    Muchmore, S.W.5    Fesik, S.W.6
  • 32
    • 0029069295 scopus 로고
    • ICE-like proteases in apoptosis
    • Kumar S. ICE-like proteases in apoptosis. Trend Biochem Sci. 20:(5):1995;198-202.
    • (1995) Trend Biochem Sci , vol.20 , Issue.5 , pp. 198-202
    • Kumar, S.1
  • 33
    • 0028986623 scopus 로고
    • Interleukin-1 beta converting enzyme: A novel cysteine protease required for IL-1 beta production and implicated in programmed cell death
    • Thornberry N.A., Molineaux S.M. Interleukin-1 beta converting enzyme: a novel cysteine protease required for IL-1 beta production and implicated in programmed cell death. Protein Sci. 4:(1):1995;3-12.
    • (1995) Protein Sci , vol.4 , Issue.1 , pp. 3-12
    • Thornberry, N.A.1    Molineaux, S.M.2
  • 35
    • 0033529534 scopus 로고    scopus 로고
    • Differential modulation of apoptosis sensitivity in CD95 type I and type II cells
    • Scaffidi C., Schmitz I., Zha J., Korsmeyer S.J., Krammer P.H., Peter M.E. Differential modulation of apoptosis sensitivity in CD95 type I and type II cells. J Biol Chem. 274:(32):1999;22532-22538.
    • (1999) J Biol Chem , vol.274 , Issue.32 , pp. 22532-22538
    • Scaffidi, C.1    Schmitz, I.2    Zha, J.3    Korsmeyer, S.J.4    Krammer, P.H.5    Peter, M.E.6
  • 36
    • 0032568954 scopus 로고    scopus 로고
    • Apoptosis induction by caspase-8 is amplified through the mitochondrial release of cytochrome c
    • Kuwana T., Smith J.J., Muzio M., Dixit V., Newmeyer D.D., Kornbluth S. Apoptosis induction by caspase-8 is amplified through the mitochondrial release of cytochrome c. J Biol Chem. 273:(26):1998;16589-16594.
    • (1998) J Biol Chem , vol.273 , Issue.26 , pp. 16589-16594
    • Kuwana, T.1    Smith, J.J.2    Muzio, M.3    Dixit, V.4    Newmeyer, D.D.5    Kornbluth, S.6
  • 37
    • 0033601746 scopus 로고    scopus 로고
    • Ordering the cytochrome c-initiated caspase cascade: Hierarchical activation of caspases-2, -3, -6, -7, -8, and -10 in a caspase-9-dependent manner
    • Slee E.A., Harte M.T., Kluck R.M., Wolf B.B., Casiano C.A., Newmeyer D.D., et al. Ordering the cytochrome c-initiated caspase cascade: hierarchical activation of caspases-2, -3, -6, -7, -8, and -10 in a caspase-9-dependent manner. J Cell Biol. 144:(2):1999;281-292.
    • (1999) J Cell Biol , vol.144 , Issue.2 , pp. 281-292
    • Slee, E.A.1    Harte, M.T.2    Kluck, R.M.3    Wolf, B.B.4    Casiano, C.A.5    Newmeyer, D.D.6
  • 38
    • 0032575750 scopus 로고    scopus 로고
    • Caspases: Enemies within
    • Thornberry N.A., Lazebnik Y. Caspases: enemies within. Science. 281:(5381):1998;1312-1316.
    • (1998) Science , vol.281 , Issue.5381 , pp. 1312-1316
    • Thornberry, N.A.1    Lazebnik, Y.2
  • 39
    • 0028956550 scopus 로고
    • Regulators of cell death
    • Korsmeyer S.J. Regulators of cell death. Trend Genet. 11:(3):1995;101-105.
    • (1995) Trend Genet , vol.11 , Issue.3 , pp. 101-105
    • Korsmeyer, S.J.1
  • 40
    • 0037251768 scopus 로고    scopus 로고
    • Role of mitochondria in apoptosis
    • Gulbins E., Dreschers S., Bock J. Role of mitochondria in apoptosis. Exp Physiol. 88:(Pt 1):2003;85-90.
    • (2003) Exp Physiol , vol.88 , Issue.PART 1 , pp. 85-90
    • Gulbins, E.1    Dreschers, S.2    Bock, J.3
  • 41
    • 0037593851 scopus 로고    scopus 로고
    • Mitochondrially-localized active caspase-9 and caspase-3 result mostly from translocation from the cytosol and partly from caspase-mediated activation in the organelle - Lack of evidence for Apaf-1-mediated procaspase-9 activation in the mitochondria
    • (in press)
    • Chandra D., Tang D.G. Mitochondrially-localized active caspase-9 and caspase-3 result mostly from translocation from the cytosol and partly from caspase-mediated activation in the organelle - lack of evidence for Apaf-1-mediated procaspase-9 activation in the mitochondria. J Biol Chem. 2003;. (in press).
    • (2003) J Biol Chem
    • Chandra, D.1    Tang, D.G.2
  • 43
    • 0031036872 scopus 로고    scopus 로고
    • Prevention of apoptosis by Bcl-2: Release of cytochrome c from mitochondria blocked
    • Yang J., Liu X., Bhalla K., Kim C.N., Ibrado A.M., Cai J., et al. Prevention of apoptosis by Bcl-2: release of cytochrome c from mitochondria blocked. Science. 275:(5303):1997;1129-1132.
    • (1997) Science , vol.275 , Issue.5303 , pp. 1129-1132
    • Yang, J.1    Liu, X.2    Bhalla, K.3    Kim, C.N.4    Ibrado, A.M.5    Cai, J.6
  • 44
    • 0037184910 scopus 로고    scopus 로고
    • Apocytochrome c blocks caspase-9 activation and Bax-induced apoptosis
    • Martin A.G., Fearnhead H.O. Apocytochrome c blocks caspase-9 activation and Bax-induced apoptosis. J Biol Chem. 277:(52):2002;50834-50841.
    • (2002) J Biol Chem , vol.277 , Issue.52 , pp. 50834-50841
    • Martin, A.G.1    Fearnhead, H.O.2
  • 46
    • 0036544535 scopus 로고    scopus 로고
    • The anti-apoptotic activity of XIAP is retained upon mutation of both the caspase 3- and caspase 9-interacting sites
    • Silke J., Hawkins C.J., Ekert P.G., Chew J., Day C.L., Pakusch M., et al. The anti-apoptotic activity of XIAP is retained upon mutation of both the caspase 3- and caspase 9-interacting sites. J Cell Biol. 157:(1):2002;115-124.
    • (2002) J Cell Biol , vol.157 , Issue.1 , pp. 115-124
    • Silke, J.1    Hawkins, C.J.2    Ekert, P.G.3    Chew, J.4    Day, C.L.5    Pakusch, M.6
  • 48
    • 0036263973 scopus 로고    scopus 로고
    • Structural insights into the pro-apoptotic function of mitochondrial serine protease HtrA2/Omi
    • Li W., Srinivasula S.M., Chai J., Li P., Wu J.W., Zhang Z., et al. Structural insights into the pro-apoptotic function of mitochondrial serine protease HtrA2/Omi. Nat Struct Biol. 9:(6):2002;436-441.
    • (2002) Nat Struct Biol , vol.9 , Issue.6 , pp. 436-441
    • Li, W.1    Srinivasula, S.M.2    Chai, J.3    Li, P.4    Wu, J.W.5    Zhang, Z.6
  • 49
    • 0037562009 scopus 로고    scopus 로고
    • Characterization of a novel and specific inhibitor for the pro-apoptotic protease Omi/HtrA2
    • Cilenti L., Lee Y., Hess S., Srinivasula S., Park K.M., Junqueira D., et al. Characterization of a novel and specific inhibitor for the pro-apoptotic protease Omi/HtrA2. J Biol Chem. 278:(13):2003;11489-11494.
    • (2003) J Biol Chem , vol.278 , Issue.13 , pp. 11489-11494
    • Cilenti, L.1    Lee, Y.2    Hess, S.3    Srinivasula, S.4    Park, K.M.5    Junqueira, D.6
  • 50
    • 0033579810 scopus 로고    scopus 로고
    • Mitochondrial release of caspase-2 and -9 during the apoptotic process
    • Susin S.A., Lorenzo H.K., Zamzami N., Marzo I., Brenner C., Larochette N., et al. Mitochondrial release of caspase-2 and -9 during the apoptotic process. J Exp M. 189:(2):1999;381-394.
    • (1999) J Exp M , vol.189 , Issue.2 , pp. 381-394
    • Susin, S.A.1    Lorenzo, H.K.2    Zamzami, N.3    Marzo, I.4    Brenner, C.5    Larochette, N.6
  • 52
    • 0033010612 scopus 로고    scopus 로고
    • Apoptosis inducing factor (AIF): A phylogenetically old, caspase-independent effector of cell death
    • Lorenzo H.K., Susin S.A., Penninger J., Kroemer G. Apoptosis inducing factor (AIF): a phylogenetically old, caspase-independent effector of cell death. Cell Death Differ. 6:(6):1999;516-524.
    • (1999) Cell Death Differ , vol.6 , Issue.6 , pp. 516-524
    • Lorenzo, H.K.1    Susin, S.A.2    Penninger, J.3    Kroemer, G.4
  • 53
    • 12244268624 scopus 로고    scopus 로고
    • Apoptosis-inducing factor (AIF): Key to the conserved caspase-independent pathways of cell death?
    • Cande C., Cecconi F., Dessen P., Kroemer G. Apoptosis-inducing factor (AIF): key to the conserved caspase-independent pathways of cell death? J Cell Sci. 115:(Pt 24):2002;4727-4734.
    • (2002) J Cell Sci , vol.115 , Issue.PART 24 , pp. 4727-4734
    • Cande, C.1    Cecconi, F.2    Dessen, P.3    Kroemer, G.4
  • 54
    • 0037440692 scopus 로고    scopus 로고
    • 2+-induced mitochondrial permeability transition causes complete release of rat liver endonuclease G activity from its exclusive location within the mitochondrial intermembrane space. Identification of a novel endo-exonuclease activity residing within the mitochondrial matrix
    • 2+-induced mitochondrial permeability transition causes complete release of rat liver endonuclease G activity from its exclusive location within the mitochondrial intermembrane space. Identification of a novel endo-exonuclease activity residing within the mitochondrial matrix. Nucleic Acids Res. 31:(4):2003;1364-1373.
    • (2003) Nucleic Acids Res , vol.31 , Issue.4 , pp. 1364-1373
    • Davies, A.M.1    Hershman, S.2    Stabley, G.J.3    Hoek, J.B.4    Peterson, J.5    Cahill, A.6
  • 55
    • 0028816881 scopus 로고
    • Endonuclease G from mammalian nuclei is identical to the major endonuclease of mitochondria
    • Gerschenson M., Houmiel K.L., Low R.L. Endonuclease G from mammalian nuclei is identical to the major endonuclease of mitochondria. Nucleic Acids Res. 23:(1):1995;88-97.
    • (1995) Nucleic Acids Res , vol.23 , Issue.1 , pp. 88-97
    • Gerschenson, M.1    Houmiel, K.L.2    Low, R.L.3
  • 56
    • 0032422488 scopus 로고    scopus 로고
    • Bax interacts with the permeability transition pore to induce permeability transition and cytochrome c release in isolated mitochondria
    • Narita M., Shimizu S., Ito T., Chittenden T., Lutz R.J., Matsuda H., et al. Bax interacts with the permeability transition pore to induce permeability transition and cytochrome c release in isolated mitochondria. Proc Natl Acad Sci USA. 95:(25):1998;14681-14686.
    • (1998) Proc Natl Acad Sci USA , vol.95 , Issue.25 , pp. 14681-14686
    • Narita, M.1    Shimizu, S.2    Ito, T.3    Chittenden, T.4    Lutz, R.J.5    Matsuda, H.6
  • 58
  • 59
    • 0032422488 scopus 로고    scopus 로고
    • Bax interacts with the permeability transition pore to induce permeability transition and cytochrome c release in isolated mitochondria
    • Narita M., Shimizu S., Ito T., Chittenden T., Lutz R.J., Matsuda H., et al. Bax interacts with the permeability transition pore to induce permeability transition and cytochrome c release in isolated mitochondria. Proc Natl Acad Sci USA. 95:(25):1998;14681-14686.
    • (1998) Proc Natl Acad Sci USA , vol.95 , Issue.25 , pp. 14681-14686
    • Narita, M.1    Shimizu, S.2    Ito, T.3    Chittenden, T.4    Lutz, R.J.5    Matsuda, H.6
  • 60
    • 0034650523 scopus 로고    scopus 로고
    • Bax oligomerization is required for channel-forming activity in liposomes and to trigger cytochrome c release from mitochondria
    • Antonsson B., Montessuit S., Lauper S., Eskes R., Martinou J.C. Bax oligomerization is required for channel-forming activity in liposomes and to trigger cytochrome c release from mitochondria. Biochem J. 345:(Pt 2):2000;271-278.
    • (2000) Biochem J , vol.345 , Issue.PART 2 , pp. 271-278
    • Antonsson, B.1    Montessuit, S.2    Lauper, S.3    Eskes, R.4    Martinou, J.C.5
  • 62
    • 0033981577 scopus 로고    scopus 로고
    • Bid induces the oligomerization and insertion of Bax into the outer mitochondrial membrane
    • Eskes R., Desagher S., Antonsson B., Martinou J.C. Bid induces the oligomerization and insertion of Bax into the outer mitochondrial membrane. Mol Cell Biol. 20:(3):2000;929-935.
    • (2000) Mol Cell Biol , vol.20 , Issue.3 , pp. 929-935
    • Eskes, R.1    Desagher, S.2    Antonsson, B.3    Martinou, J.C.4
  • 63
    • 0032528118 scopus 로고    scopus 로고
    • Enforced dimerization of BAX results in its translocation, mitochondrial dysfunction and apoptosis
    • Gross A., Jockel J., Wei M.C., Korsmeyer S.J. Enforced dimerization of BAX results in its translocation, mitochondrial dysfunction and apoptosis. EMBO J. 17:(14):1998;3878-3885.
    • (1998) EMBO J , vol.17 , Issue.14 , pp. 3878-3885
    • Gross, A.1    Jockel, J.2    Wei, M.C.3    Korsmeyer, S.J.4
  • 64
    • 0034681110 scopus 로고    scopus 로고
    • Proapoptotic BH3-only Bcl-2 family members induce cytochrome c release, but not mitochondrial membrane potential loss, and do not directly modulate voltage-dependent anion channel activity
    • Shimizu S., Tsujimoto Y. Proapoptotic BH3-only Bcl-2 family members induce cytochrome c release, but not mitochondrial membrane potential loss, and do not directly modulate voltage-dependent anion channel activity. Proc Natl Acad Sci USA. 97:(2):2000;577-582.
    • (2000) Proc Natl Acad Sci USA , vol.97 , Issue.2 , pp. 577-582
    • Shimizu, S.1    Tsujimoto, Y.2
  • 65
    • 0033519705 scopus 로고    scopus 로고
    • Bcl-2 family proteins regulate the release of apoptogenic cytochrome c by the mitochondrial channel VDAC [see comments]
    • Shimizu S., Narita M., Tsujimoto Y. Bcl-2 family proteins regulate the release of apoptogenic cytochrome c by the mitochondrial channel VDAC [see comments]. Nature. 399:(6735):1999;483-487.
    • (1999) Nature , vol.399 , Issue.6735 , pp. 483-487
    • Shimizu, S.1    Narita, M.2    Tsujimoto, Y.3
  • 66
    • 0031772126 scopus 로고    scopus 로고
    • The mitochondrial permeability transition is required for tumor necrosis factor alpha-mediated apoptosis and cytochrome c release
    • Bradham C.A., Qian T., Streetz K., Trautwein C., Brenner D.A., Lemasters J.J. The mitochondrial permeability transition is required for tumor necrosis factor alpha-mediated apoptosis and cytochrome c release. Mol Cell Biol. 18:(11):1998;6353-6364.
    • (1998) Mol Cell Biol , vol.18 , Issue.11 , pp. 6353-6364
    • Bradham, C.A.1    Qian, T.2    Streetz, K.3    Trautwein, C.4    Brenner, D.A.5    Lemasters, J.J.6
  • 67
    • 0033635733 scopus 로고    scopus 로고
    • BH3-only proteins-essential initiators of apoptotic cell death
    • Huang D.C., Strasser A. BH3-only proteins-essential initiators of apoptotic cell death. Cell. 103:(6):2000;839-842.
    • (2000) Cell , vol.103 , Issue.6 , pp. 839-842
    • Huang, D.C.1    Strasser, A.2
  • 68
    • 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:(4):1998;491-501.
    • (1998) Cell , vol.94 , Issue.4 , pp. 491-501
    • Li, H.1    Zhu, H.2    Xu, C.J.3    Yuan, J.4
  • 69
    • 0037047326 scopus 로고    scopus 로고
    • Calpain and mitochondria in ischemia/reperfusion injury
    • Chen M., Won D.J., Krajewski S., Gottlieb R.A. Calpain and mitochondria in ischemia/reperfusion injury. J Biol Chem. 277:(32):2002;29181-29186.
    • (2002) J Biol Chem , vol.277 , Issue.32 , pp. 29181-29186
    • Chen, M.1    Won, D.J.2    Krajewski, S.3    Gottlieb, R.A.4
  • 70
    • 0034724190 scopus 로고    scopus 로고
    • BH4 domain of antiapoptotic Bcl-2 family members closes voltage-dependent anion channel and inhibits apoptotic mitochondrial changes and cell death
    • Shimizu S., Konishi A., Kodama T., Tsujimoto Y. BH4 domain of antiapoptotic Bcl-2 family members closes voltage-dependent anion channel and inhibits apoptotic mitochondrial changes and cell death. Proc Natl Acad Sci USA. 97:(7):2000;3100-3105.
    • (2000) Proc Natl Acad Sci USA , vol.97 , Issue.7 , pp. 3100-3105
    • Shimizu, S.1    Konishi, A.2    Kodama, T.3    Tsujimoto, Y.4
  • 71
    • 0031436251 scopus 로고    scopus 로고
    • Heterodimerization-independent functions of cell death regulatory proteins bax and bcl-2 in yeast and mammalian cells [in process citation]
    • Zha H., Reed J.C. Heterodimerization-independent functions of cell death regulatory proteins bax and bcl-2 in yeast and mammalian cells [in process citation]. J Biol Chem. 272:(50):1997;31482-31488.
    • (1997) J Biol Chem , vol.272 , Issue.50 , pp. 31482-31488
    • Zha, H.1    Reed, J.C.2
  • 72
    • 0032575688 scopus 로고    scopus 로고
    • The Bcl-2 protein family: Arbiters of cell survival
    • Adams J.M., Cory S. The Bcl-2 protein family: arbiters of cell survival. Science. 281:(5381):1998;1322-1326.
    • (1998) Science , vol.281 , Issue.5381 , pp. 1322-1326
    • Adams, J.M.1    Cory, S.2
  • 73
    • 0025214625 scopus 로고
    • A relative deficit in antioxidant reserve may contribute in cardiac failure
    • Singal P.K., Kirshenbaum L.A. A relative deficit in antioxidant reserve may contribute in cardiac failure. Can J Cardiol. 6:(2):1990;47-49.
    • (1990) Can J Cardiol , vol.6 , Issue.2 , pp. 47-49
    • Singal, P.K.1    Kirshenbaum, L.A.2
  • 74
    • 0030030304 scopus 로고    scopus 로고
    • Antioxidant and oxidative stress changes during heart failure subsequent to myocardial infarction in rats
    • Hill M.F., Singal P.K. Antioxidant and oxidative stress changes during heart failure subsequent to myocardial infarction in rats. Am J Pathol. 148:(1):1996;291-300.
    • (1996) Am J Pathol , vol.148 , Issue.1 , pp. 291-300
    • Hill, M.F.1    Singal, P.K.2
  • 75
    • 0032563825 scopus 로고    scopus 로고
    • Doxorubicin-induced cardiomyopathy
    • Singal P.K., Iliskovic N. Doxorubicin-induced cardiomyopathy. N Engl J M. 339:(13):1998;900-905.
    • (1998) N Engl J M , vol.339 , Issue.13 , pp. 900-905
    • Singal, P.K.1    Iliskovic, N.2
  • 76
    • 0033535974 scopus 로고    scopus 로고
    • Signaling pathways in reactive oxygen species-induced cardiomyocyte apoptosis
    • von Harsdorf R., Li P.F., Dietz R. Signaling pathways in reactive oxygen species-induced cardiomyocyte apoptosis. Circulation. 99:(22):1999;2934-2941.
    • (1999) Circulation , vol.99 , Issue.22 , pp. 2934-2941
    • Von Harsdorf, R.1    Li, P.F.2    Dietz, R.3
  • 77
    • 0035823571 scopus 로고    scopus 로고
    • The apoptotic regulatory protein ARC (apoptosis repressor with caspase recruitment domain) prevents oxidant stress-mediated cell death by preserving mitochondrial function
    • Neuss M., Monticone R., Lundberg M.S., Chesley A.T., Fleck E., Crow M.T. The apoptotic regulatory protein ARC (apoptosis repressor with caspase recruitment domain) prevents oxidant stress-mediated cell death by preserving mitochondrial function. J Biol Chem. 276:(36):2001;33915-33922.
    • (2001) J Biol Chem , vol.276 , Issue.36 , pp. 33915-33922
    • Neuss, M.1    Monticone, R.2    Lundberg, M.S.3    Chesley, A.T.4    Fleck, E.5    Crow, M.T.6
  • 78
    • 0037031297 scopus 로고    scopus 로고
    • TAT protein transduction into isolated perfused hearts: TAT-apoptosis repressor with caspase recruitment domain is cardioprotective
    • Gustafsson A.B., Sayen M.R., Williams S.D., Crow M.T., Gottlieb R.A. TAT protein transduction into isolated perfused hearts: TAT-apoptosis repressor with caspase recruitment domain is cardioprotective. Circulation. 106:(6):2002;735-739.
    • (2002) Circulation , vol.106 , Issue.6 , pp. 735-739
    • Gustafsson, A.B.1    Sayen, M.R.2    Williams, S.D.3    Crow, M.T.4    Gottlieb, R.A.5
  • 79
    • 0037151626 scopus 로고    scopus 로고
    • Antiapoptotic effect of nicorandil mediated by mitochondrial atp-sensitive potassium channels in cultured cardiac myocytes
    • Akao M., Teshima Y., Marban E. Antiapoptotic effect of nicorandil mediated by mitochondrial atp-sensitive potassium channels in cultured cardiac myocytes. J Am Coll Cardiol. 40:(4):2002;803-810.
    • (2002) J Am Coll Cardiol , vol.40 , Issue.4 , pp. 803-810
    • Akao, M.1    Teshima, Y.2    Marban, E.3
  • 80
    • 0035901575 scopus 로고    scopus 로고
    • Serpin protein CrmA suppresses hypoxia-mediated apoptosis of ventricular myocytes
    • Gurevich R.M., Regula K.M., Kirshenbaum L.A. Serpin protein CrmA suppresses hypoxia-mediated apoptosis of ventricular myocytes. Circulation. 103:(15):2001;1984-1991.
    • (2001) Circulation , vol.103 , Issue.15 , pp. 1984-1991
    • Gurevich, R.M.1    Regula, K.M.2    Kirshenbaum, L.A.3
  • 81
    • 0033520463 scopus 로고    scopus 로고
    • The mitochondrial apoptotic pathway is activated by serum and glucose deprivation in cardiac myocytes
    • Bialik S., Cryns V.L., Drincic A., Miyata S., Wollowick A.L., Srinivasan A., et al. The mitochondrial apoptotic pathway is activated by serum and glucose deprivation in cardiac myocytes. Circ Res. 85:(5):1999;403-414.
    • (1999) Circ Res , vol.85 , Issue.5 , pp. 403-414
    • Bialik, S.1    Cryns, V.L.2    Drincic, A.3    Miyata, S.4    Wollowick, A.L.5    Srinivasan, A.6
  • 82
    • 0033617296 scopus 로고    scopus 로고
    • Glucose uptake and glycolysis reduce hypoxia-induced apoptosis in cultured neonatal rat cardiac myocytes
    • Malhotra R., Brosius F.C. III. Glucose uptake and glycolysis reduce hypoxia-induced apoptosis in cultured neonatal rat cardiac myocytes. J Biol Chem. 274:(18):1999;12567-12575.
    • (1999) J Biol Chem , vol.274 , Issue.18 , pp. 12567-12575
    • Malhotra, R.1    Brosius F.C. III2
  • 83
    • 0032524656 scopus 로고    scopus 로고
    • Adenovirus E1B-19K/BCL-2 interacting protein BNIP3 contains a BH3 domain and a mitochondrial targeting sequence
    • Yasuda M., Theodorakis P., Subramanian T., Chinnadurai G. Adenovirus E1B-19K/BCL-2 interacting protein BNIP3 contains a BH3 domain and a mitochondrial targeting sequence. J Biol Chem. 273:(20):1998;12415-12421.
    • (1998) J Biol Chem , vol.273 , Issue.20 , pp. 12415-12421
    • Yasuda, M.1    Theodorakis, P.2    Subramanian, T.3    Chinnadurai, G.4
  • 84
    • 0037047647 scopus 로고    scopus 로고
    • Inducible expression of BNIP3 provokes mitochondrial defects and hypoxia-mediated cell death of ventricular myocytes
    • Regula K.M., Ens K., Kirshenbaum L.A. Inducible expression of BNIP3 provokes mitochondrial defects and hypoxia-mediated cell death of ventricular myocytes. Circ Res. 91:(3):2002;226-231.
    • (2002) Circ Res , vol.91 , Issue.3 , pp. 226-231
    • Regula, K.M.1    Ens, K.2    Kirshenbaum, L.A.3
  • 86
    • 0033942613 scopus 로고    scopus 로고
    • BNIP3 and genetic control of necrosis-like cell death through the mitochondrial permeability transition pore
    • Vande V.C., Cizeau J., Dubik D., Alimonti J., Brown T., Israels S., et al. BNIP3 and genetic control of necrosis-like cell death through the mitochondrial permeability transition pore. Mol Cell Biol. 20:(15):2000;5454-5468.
    • (2000) Mol Cell Biol , vol.20 , Issue.15 , pp. 5454-5468
    • Vande, V.C.1    Cizeau, J.2    Dubik, D.3    Alimonti, J.4    Brown, T.5    Israels, S.6
  • 87
    • 0031455410 scopus 로고    scopus 로고
    • The E1B 19K/Bcl-2-binding protein Nip3 is a dimeric mitochondrial protein that activates apoptosis
    • Chen G., Ray R., Dubik D., Shi L., Cizeau J., Bleackley R.C., et al. The E1B 19K/Bcl-2-binding protein Nip3 is a dimeric mitochondrial protein that activates apoptosis. J Exp M. 186:(12):1997;1975-1983.
    • (1997) J Exp M , vol.186 , Issue.12 , pp. 1975-1983
    • Chen, G.1    Ray, R.2    Dubik, D.3    Shi, L.4    Cizeau, J.5    Bleackley, R.C.6
  • 88
    • 0032932923 scopus 로고    scopus 로고
    • Nix and Nip3 form a subfamily of pro-apoptotic mitochondrial proteins
    • Chen G., Cizeau J., Vande V.C., Park J.H., Bozek G., Bolton J., et al. Nix and Nip3 form a subfamily of pro-apoptotic mitochondrial proteins. J Biol Chem. 274:(1):1999;7-10.
    • (1999) J Biol Chem , vol.274 , Issue.1 , pp. 7-10
    • Chen, G.1    Cizeau, J.2    Vande, V.C.3    Park, J.H.4    Bozek, G.5    Bolton, J.6
  • 89
    • 0031040328 scopus 로고    scopus 로고
    • Sphingosine mediates the immediate negative inotropic effects of tumor necrosis factor-alpha in the adult mammalian cardiac myocyte
    • Oral H., Dorn G.W., Mann D.L. Sphingosine mediates the immediate negative inotropic effects of tumor necrosis factor-alpha in the adult mammalian cardiac myocyte. J Biol Chem. 272:(8):1997;4836-4842.
    • (1997) J Biol Chem , vol.272 , Issue.8 , pp. 4836-4842
    • Oral, H.1    Dorn, G.W.2    Mann, D.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.