메뉴 건너뛰기




Volumn 9, Issue 3, 2004, Pages 377-384

Increase in the ratio of mitochondrial Bax/Bcl-XL induces Bax activation in human leukemic K562 cell line

Author keywords

Bax activation; Bcl XL translocation; DNA damage; Mitochondria; Ratio of Bax Bcl XL

Indexed keywords

BH3 PROTEIN; CYTOCHROME C; PROTEIN BAX; PROTEIN BCL 2; PROTEIN BCL XL; PROTEIN P53;

EID: 3242763808     PISSN: 13608185     EISSN: None     Source Type: Journal    
DOI: 10.1023/B:APPT.0000025815.78761.5c     Document Type: Article
Times cited : (31)

References (38)
  • 1
    • 0035206383 scopus 로고    scopus 로고
    • Mechanisms of p53-dependent apoptosis
    • Schuler M, Green DR. Mechanisms of p53-dependent apoptosis. Biochem Soc Trans 2001; 29: 684-688.
    • (2001) Biochem Soc Trans , vol.29 , pp. 684-688
    • Schuler, M.1    Green, D.R.2
  • 2
    • 0030581151 scopus 로고    scopus 로고
    • Induction of apoptotic program in cell-free extracts: Requirement for dATP and cytochrome c
    • Lui X, Kim CN, Yang J, Jemmerson R, Wang X. Induction of apoptotic program in cell-free extracts: Requirement for dATP and cytochrome c. Cell 1996; 86: 147-157.
    • (1996) Cell , vol.86 , pp. 147-157
    • Lui, X.1    Kim, C.N.2    Yang, J.3    Jemmerson, R.4    Wang, X.5
  • 3
    • 0031036872 scopus 로고    scopus 로고
    • Prevention of apoptosis by Bcl-2: Release of cytochrome c from mitochondria blocked
    • Yang J, Liu X, Bhalla K, et al. Prevention of apoptosis by Bcl-2: Release of cytochrome c from mitochondria blocked. Science 1997; 275: 1129-1132.
    • (1997) Science , vol.275 , pp. 1129-1132
    • Yang, J.1    Liu, X.2    Bhalla, K.3
  • 4
    • 0034616945 scopus 로고    scopus 로고
    • Smac, a mitochondrial protein that promotes cytochrome c-dependent caspase activation by eliminating IAP inhibition
    • Du C, Fang M, Li Y, Li L, Wang X. Smac, a mitochondrial protein that promotes cytochrome c-dependent caspase activation by eliminating IAP inhibition. Cell 2000; 102: 33-42.
    • (2000) Cell , vol.102 , pp. 33-42
    • Du, C.1    Fang, M.2    Li, Y.3    Li, L.4    Wang, X.5
  • 5
    • 0035833337 scopus 로고    scopus 로고
    • Bax translocation is crucial for the sensitivity of leukaemic cells to etoposide-induced apoptosis
    • Jia L, Patwari Y, Srinivasula SM, et al. Bax translocation is crucial for the sensitivity of leukaemic cells to etoposide-induced apoptosis. Oncogene 2001; 20: 4817-4826.
    • (2001) Oncogene , vol.20 , pp. 4817-4826
    • Jia, L.1    Patwari, Y.2    Srinivasula, S.M.3
  • 6
    • 0035880232 scopus 로고    scopus 로고
    • Apaf-1 protein deficiency confers resistance to cytochrome c-dependent apoptosis in human leukemic cells
    • Jia L, Srinivasula SM, Liu FT, et al. Apaf-1 protein deficiency confers resistance to cytochrome c-dependent apoptosis in human leukemic cells. Blood 2001; 98: 414-421.
    • (2001) Blood , vol.98 , pp. 414-421
    • Jia, L.1    Srinivasula, S.M.2    Liu, F.T.3
  • 7
    • 0037456993 scopus 로고    scopus 로고
    • Role of Smac in human leukaemic cell apoptosis and proliferation
    • Jia L, Patwari Y, Kelsey SM, et al. Role of Smac in human leukaemic cell apoptosis and proliferation. Oncogene 2003; 22: 1589-1599.
    • (2003) Oncogene , vol.22 , pp. 1589-1599
    • Jia, L.1    Patwari, Y.2    Kelsey, S.M.3
  • 8
    • 0030715323 scopus 로고    scopus 로고
    • Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade
    • Li P, Nijhawan D, Budihardjo I, et al. Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade. Cell 1997; 91: 479-489.
    • (1997) Cell , vol.91 , pp. 479-489
    • Li, P.1    Nijhawan, D.2    Budihardjo, I.3
  • 9
    • 0031037897 scopus 로고    scopus 로고
    • The release of cytochrome c from mitochondria: A primary site for Bcl-2 regulation of apoptosis
    • Kluck RM, Bossy-Wetzel E, Green DR, Newmeyer DD. The release of cytochrome c from mitochondria: A primary site for Bcl-2 regulation of apoptosis. Science 1997; 275: 1132-1136.
    • (1997) Science , vol.275 , pp. 1132-1136
    • Kluck, R.M.1    Bossy-Wetzel, E.2    Green, D.R.3    Newmeyer, D.D.4
  • 10
    • 0034717014 scopus 로고    scopus 로고
    • Death signal-induced localization of p53 protein to mitochondria. A potential role in apoptotic signaling
    • Marchenko ND, Zaika A, Moll UM. Death signal-induced localization of p53 protein to mitochondria. A potential role in apoptotic signaling. J Biol Chem 2000; 275: 16202-16212.
    • (2000) J Biol Chem , vol.275 , pp. 16202-16212
    • Marchenko, N.D.1    Zaika, A.2    Moll, U.M.3
  • 11
    • 0036830438 scopus 로고    scopus 로고
    • Bcl-XL protects BimEL-induced Bax conformational change and cytochrome C release independent of interacting with Bax or BimEL
    • Yamaguchi H, Wang HG. Bcl-XL protects BimEL-induced Bax conformational change and cytochrome C release independent of interacting with Bax or BimEL. J Biol Chem 2002; 277: 41604-41612.
    • (2002) J Biol Chem , vol.277 , pp. 41604-41612
    • Yamaguchi, H.1    Wang, H.G.2
  • 12
    • 0033120383 scopus 로고    scopus 로고
    • Subcellular distribution and redistribution of Bcl-2 family proteins in human leukemia cells undergoing apoptosis
    • Jia L, Macey MG, Yin Y, Newland AC, Kelsey SM. Subcellular distribution and redistribution of Bcl-2 family proteins in human leukemia cells undergoing apoptosis. Blood 1999; 93: 2353-2359.
    • (1999) Blood , vol.93 , pp. 2353-2359
    • Jia, L.1    Macey, M.G.2    Yin, Y.3    Newland, A.C.4    Kelsey, S.M.5
  • 13
    • 0035823558 scopus 로고    scopus 로고
    • A role for mitochondrial Bak in apoptotic response to anticancer drugs
    • Wang GQ, Gastman BR, Wieckowski E, et al. A role for mitochondrial Bak in apoptotic response to anticancer drugs. J Biol Chem 2001; 276: 34307-34017.
    • (2001) J Biol Chem , vol.276 , pp. 34307-134017
    • Wang, G.Q.1    Gastman, B.R.2    Wieckowski, E.3
  • 14
    • 0037513376 scopus 로고    scopus 로고
    • p53 triggers apoptosis in oncogene-expressing fibroblasts by the induction of Noxa and mitochondrial Bax translocation
    • Schuler M, Maurer U, Goldstein JC, et al. p53 triggers apoptosis in oncogene-expressing fibroblasts by the induction of Noxa and mitochondrial Bax translocation. Cell Death Differ 2003; 10: 451-460.
    • (2003) Cell Death Differ , vol.10 , pp. 451-460
    • Schuler, M.1    Maurer, U.2    Goldstein, J.C.3
  • 15
    • 0034640281 scopus 로고    scopus 로고
    • Noxa, a BH3-only member of the Bcl-2 family and candidate mediator of p53-induced apoptosis
    • Oda E, Ohki R, Murasawa H, et al. Noxa, a BH3-only member of the Bcl-2 family and candidate mediator of p53-induced apoptosis. Science 2000; 288: 1053-1058.
    • (2000) Science , vol.288 , pp. 1053-1058
    • Oda, E.1    Ohki, R.2    Murasawa, H.3
  • 16
  • 18
    • 0035265686 scopus 로고    scopus 로고
    • PUMA, a novel proapoptotic gene, is induced by p53
    • Nakano K, Vousden KH. PUMA, a novel proapoptotic gene, is induced by p53. Mol Cell 2001; 7: 683-694.
    • (2001) Mol Cell , vol.7 , pp. 683-694
    • Nakano, K.1    Vousden, K.H.2
  • 19
    • 0035949470 scopus 로고    scopus 로고
    • Expression of bbc3, a pro-apoptotic BH3-only gene, is regulated by diverse cell death and survival signals
    • Han J, Flemington C, Houghton AB, et al. Expression of bbc3, a pro-apoptotic BH3-only gene, is regulated by diverse cell death and survival signals. Proc Natl Acad Sci USA 2001; 98: 11318-11323.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 11318-11323
    • Han, J.1    Flemington, C.2    Houghton, A.B.3
  • 20
    • 0031007644 scopus 로고    scopus 로고
    • Nonionic detergents induce dimerization among members of the Bcl-2 family
    • Hsu YT, Youle RJ. Nonionic detergents induce dimerization among members of the Bcl-2 family. J Biol Chem 1997; 272: 13829-13834.
    • (1997) J Biol Chem , vol.272 , pp. 13829-13834
    • Hsu, Y.T.1    Youle, R.J.2
  • 21
    • 0036728834 scopus 로고    scopus 로고
    • Distinct BH3 domains either sensitize or activate mitochondrial apoptosis, serving as prototype cancer therapeutics
    • Letai A, Bassik MC, Walensky LD, Sorcinelli MD, Weiler S, Korsmeyer SJ. Distinct BH3 domains either sensitize or activate mitochondrial apoptosis, serving as prototype cancer therapeutics. Cancer Cell 2002; 2: 183-192.
    • (2002) Cancer Cell , vol.2 , pp. 183-192
    • Letai, A.1    Bassik, M.C.2    Walensky, L.D.3    Sorcinelli, M.D.4    Weiler, S.5    Korsmeyer, S.J.6
  • 22
    • 0038304520 scopus 로고    scopus 로고
    • Minimal BH3 peptides promote cell death by antagonizing anti-apoptotic proteins
    • Moreau C, Cartron PF, Hunt A, et al. Minimal BH3 peptides promote cell death by antagonizing anti-apoptotic proteins. J Biol Chem 2003; 278: 19426-19435.
    • (2003) J Biol Chem , vol.278 , pp. 19426-19435
    • Moreau, C.1    Cartron, P.F.2    Hunt, A.3
  • 23
    • 0033535350 scopus 로고    scopus 로고
    • Bid-induced conformational change of Bax is responsible for mitochondrial cytochrome c release during apoptosis
    • Desagher S, Osen-Sand A, Nichols A, et al. Bid-induced conformational change of Bax is responsible for mitochondrial cytochrome c release during apoptosis. J Cell Biol 1999; 144: 891-901.
    • (1999) J Cell Biol , vol.144 , pp. 891-901
    • Desagher, S.1    Osen-Sand, A.2    Nichols, A.3
  • 24
    • 0033694859 scopus 로고    scopus 로고
    • BID-dependent and BID-independent pathways for BAX insertion into mitochondria
    • Ruffolo SC, Breckenridge DG, Nguyen M, et al. BID-dependent and BID-independent pathways for BAX insertion into mitochondria. Cell Death and Differ 2000; 7: 1101-1108.
    • (2000) Cell Death and Differ , vol.7 , pp. 1101-1108
    • Ruffolo, S.C.1    Breckenridge, D.G.2    Nguyen, M.3
  • 25
    • 0034786019 scopus 로고    scopus 로고
    • BCL-2, BCL-X(L) sequester BH3 domain-only molecules preventing BAX- And BAK-mediated mitochondrial apoptosis
    • Cheng EH, Wei MC, Weiler S, et al. BCL-2, BCL-X(L) sequester BH3 domain-only molecules preventing BAX- and BAK-mediated mitochondrial apoptosis. Mol Cell 2001; 8: 705-711.
    • (2001) Mol Cell , vol.8 , pp. 705-711
    • Cheng, E.H.1    Wei, M.C.2    Weiler, S.3
  • 26
    • 0035988396 scopus 로고    scopus 로고
    • Defective Bax activation in Hodgkin B-cell lines confers resistance to staurosporine-induced apoptosis
    • Kashkar H, Kronke M, Jurgensmeier JM. Defective Bax activation in Hodgkin B-cell lines confers resistance to staurosporine-induced apoptosis. Cell Death and Differ 2002; 9: 750-757.
    • (2002) Cell Death and Differ , vol.9 , pp. 750-757
    • Kashkar, H.1    Kronke, M.2    Jurgensmeier, J.M.3
  • 27
    • 0037081329 scopus 로고    scopus 로고
    • Epothilone B analogue (BMS-247550)-mediated cytotoxicity through induction of Bax conformational change in human breast cancer cells
    • Yamaguchi H, Paranawithana SR, Lee MW, Huang Z, Bhalla KN, Wang HG. Epothilone B analogue (BMS-247550)-mediated cytotoxicity through induction of Bax conformational change in human breast cancer cells. Cancer Res 2002; 62: 466-471.
    • (2002) Cancer Res , vol.62 , pp. 466-471
    • Yamaguchi, H.1    Paranawithana, S.R.2    Lee, M.W.3    Huang, Z.4    Bhalla, K.N.5    Wang, H.G.6
  • 28
    • 0036253166 scopus 로고    scopus 로고
    • Liposomal encapsulation diminishes daunorubicin-induced generation of reactive oxygen species, depletion of ATP and necrotic cell death in human leukaemic cells
    • Liu FT, Kelsey SM, Newland AC, Jia L. Liposomal encapsulation diminishes daunorubicin-induced generation of reactive oxygen species, depletion of ATP and necrotic cell death in human leukaemic cells. Br J Haematol 2002; 117: 333-342.
    • (2002) Br J Haematol , vol.117 , pp. 333-342
    • Liu, F.T.1    Kelsey, S.M.2    Newland, A.C.3    Jia, L.4
  • 29
    • 0141757205 scopus 로고    scopus 로고
    • Bax conformational change is a crucial step for PUMA-mediated apoptosis in human leukemia
    • Liu FT, Newland AC, Jia L. Bax conformational change is a crucial step for PUMA-mediated apoptosis in human leukemia. Biochem Biophys Res Commun 2003; 310: 956-962.
    • (2003) Biochem Biophys Res Commun , vol.310 , pp. 956-962
    • Liu, F.T.1    Newland, A.C.2    Jia, L.3
  • 30
    • 0030963602 scopus 로고    scopus 로고
    • Cytosol-to-membrane redistribution of Bax and Bcl-X(L) during apoptosis
    • Hsu YT, Wolter KG, Youle RJ. Cytosol-to-membrane redistribution of Bax and Bcl-X(L) during apoptosis. Proc Natl Acad Sci USA 1997; 94: 3668-3672.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 3668-3672
    • Hsu, Y.T.1    Wolter, K.G.2    Youle, R.J.3
  • 31
    • 0034811651 scopus 로고    scopus 로고
    • Trail-induced apoptosis in Type I leukemic cells is not enhanced by overexpression of bax
    • Jia L, Patwari Y, Kelsey SM, Newland AC. Trail-induced apoptosis in Type I leukemic cells is not enhanced by overexpression of bax. Biochem Biopbys Res Commun 2001; 283: 1037-1045.
    • (2001) Biochem Biopbys Res Commun , vol.283 , pp. 1037-1045
    • Jia, L.1    Patwari, Y.2    Kelsey, S.M.3    Newland, A.C.4
  • 32
    • 0036467477 scopus 로고    scopus 로고
    • Apoptosis and tumourigenesis
    • Hickman JA. Apoptosis and tumourigenesis. Curr Opin Genet Dev 2002; 12: 67-72.
    • (2002) Curr Opin Genet Dev , vol.12 , pp. 67-72
    • Hickman, J.A.1
  • 33
    • 0034641918 scopus 로고    scopus 로고
    • The biochemistry of apoptosis
    • Hengartner MO. The biochemistry of apoptosis. Nature 2000; 407: 770-776.
    • (2000) Nature , vol.407 , pp. 770-776
    • Hengartner, M.O.1
  • 34
  • 35
    • 0035936023 scopus 로고    scopus 로고
    • The protein kinase PKB/Akt regulates cell survival and apoptosis by inhibiting Bax conformational change
    • Yamaguchi H, Wang HG. The protein kinase PKB/Akt regulates cell survival and apoptosis by inhibiting Bax conformational change. Oncogene 2001; 20: 7779-7786.
    • (2001) Oncogene , vol.20 , pp. 7779-7786
    • Yamaguchi, H.1    Wang, H.G.2
  • 36
    • 0242410719 scopus 로고    scopus 로고
    • A p53-and drug-induced apoptotic responses mediated by BH3-only proteins Puma and Noxa
    • Villunger A, Michalak EM, Coultas L, et al. A p53-and drug-induced apoptotic responses mediated by BH3-only proteins Puma and Noxa. Science 2003; 302: 1036-1038.
    • (2003) Science , vol.302 , pp. 1036-1038
    • Villunger, A.1    Michalak, E.M.2    Coultas, L.3
  • 37
    • 0035890335 scopus 로고    scopus 로고
    • Damage-induced Bax N-terminal change, translocation to mitochondria and formation of Bax dimers/complexes occur regardless of cell fate
    • Makin GW, Corfe BM, Griffiths GJ, Thistlethwaite A, Hickman JA, Dive C. Damage-induced Bax N-terminal change, translocation to mitochondria and formation of Bax dimers/complexes occur regardless of cell fate. EMBO J 2001; 20: 6306-6315.
    • (2001) EMBO J , vol.20 , pp. 6306-6315
    • Makin, G.W.1    Corfe, B.M.2    Griffiths, G.J.3    Thistlethwaite, A.4    Hickman, J.A.5    Dive, C.6
  • 38
    • 0033522391 scopus 로고    scopus 로고
    • Conformation of the Bax C-terminus regulates subcellular location and cell death
    • Nechushtan A, Smith CL, Hsu YT, Youle RJ. Conformation of the Bax C-terminus regulates subcellular location and cell death. EMBO J 1999; 18: 2330-2341.
    • (1999) EMBO J , vol.18 , pp. 2330-2341
    • Nechushtan, A.1    Smith, C.L.2    Hsu, Y.T.3    Youle, R.J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.