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Volumn 121, Issue 21, 2008, Pages 3515-3523

An intracellular wave of cytochrome c propagates and precedes Bax redistribution during apoptosis

Author keywords

Apoptosis; Bax; Caspase 3; Cytochrome c; Recombinant probes; Single cell imaging

Indexed keywords

CASPASE 3; CASPASE 7; CYTOCHROME C; PROTEIN BAX; CALCIUM;

EID: 59149097259     PISSN: 00219533     EISSN: None     Source Type: Journal    
DOI: 10.1242/jcs.029587     Document Type: Article
Times cited : (38)

References (36)
  • 1
    • 21844464054 scopus 로고    scopus 로고
    • Bax forms multispanning monomers that oligomerize to permeabilize membranes during apoptosis
    • Annis, M. G., Soucie, E. L., Dlugosz, P. J., Cruz-Aguado, J. A., Penn, L. Z., Leber, B. and Andrews, D. W. (2005). Bax forms multispanning monomers that oligomerize to permeabilize membranes during apoptosis. EMBO J. 24, 2096-2103.
    • (2005) EMBO J , vol.24 , pp. 2096-2103
    • Annis, M.G.1    Soucie, E.L.2    Dlugosz, P.J.3    Cruz-Aguado, J.A.4    Penn, L.Z.5    Leber, B.6    Andrews, D.W.7
  • 3
    • 0344825875 scopus 로고    scopus 로고
    • Cytochrome c binds to inositol (1,4,5) trisphosphate receptors, amplifying calcium-dependent apoptosis
    • Boehning, D., Patterson, R. L., Sedaghat, L., Glebova, N. O., Kurosaki, T. and Snyder, S. H. (2003). Cytochrome c binds to inositol (1,4,5) trisphosphate receptors, amplifying calcium-dependent apoptosis. Nat. Cell Biol. 5, 1051-1061.
    • (2003) Nat. Cell Biol , vol.5 , pp. 1051-1061
    • Boehning, D.1    Patterson, R.L.2    Sedaghat, L.3    Glebova, N.O.4    Kurosaki, T.5    Snyder, S.H.6
  • 5
  • 7
    • 34548305233 scopus 로고    scopus 로고
    • Control of bax homodimerization by its carboxy-terminal
    • Er, E., Lalier, L., Cartron, P., Oliver, L. and Vallette, F. M. (2007). Control of bax homodimerization by its carboxy-terminal. J. Biol. Chem. 282, 24938-24947.
    • (2007) J. Biol. Chem , vol.282 , pp. 24938-24947
    • Er, E.1    Lalier, L.2    Cartron, P.3    Oliver, L.4    Vallette, F.M.5
  • 8
    • 22544450163 scopus 로고    scopus 로고
    • Agaric acid induces mitochondrial permeability transition through its interaction with the adenine nucleotide translocase. its dependence on membrane fluidity
    • García, N., Zazueta, C., Pavón, N. and Chávez, E. (2005). Agaric acid induces mitochondrial permeability transition through its interaction with the adenine nucleotide translocase. its dependence on membrane fluidity. Mitochondrion 5, 272-281.
    • (2005) Mitochondrion , vol.5 , pp. 272-281
    • García, N.1    Zazueta, C.2    Pavón, N.3    Chávez, E.4
  • 9
    • 0033781027 scopus 로고    scopus 로고
    • The coordinate release of cytochrome c during apoptosis is rapid, complete and kinetically invariant
    • Goldstein, J. C., Waterhouse, N. J., Juin, P., Evan, G. I. and Green, D. R. (2000). The coordinate release of cytochrome c during apoptosis is rapid, complete and kinetically invariant. Nat. Cell Biol. 2, 156-162.
    • (2000) Nat. Cell Biol , vol.2 , pp. 156-162
    • Goldstein, J.C.1    Waterhouse, N.J.2    Juin, P.3    Evan, G.I.4    Green, D.R.5
  • 11
    • 0032528118 scopus 로고    scopus 로고
    • Enforced dimerization of bax results in its translocation, mitochondrial dysfunction and apoptosis
    • Gross, A., Jockel, J., Wei, M. C. and Korsmeyer, S. J. (1998). Enforced dimerization of bax results in its translocation, mitochondrial dysfunction and apoptosis. EMBO J. 17, 3878-3885.
    • (1998) EMBO J , vol.17 , pp. 3878-3885
    • Gross, A.1    Jockel, J.2    Wei, M.C.3    Korsmeyer, S.J.4
  • 15
    • 0035988396 scopus 로고    scopus 로고
    • Defective bax activation in hodgkin b-cell lines confers resistance to staurosporine-induced apoptosis
    • Kashkar, H., Krönke, M. and Jürgensmeier, J. M. (2002). Defective bax activation in hodgkin b-cell lines confers resistance to staurosporine-induced apoptosis. Cell Death Differ. 9, 750-757.
    • (2002) Cell Death Differ , vol.9 , pp. 750-757
    • Kashkar, H.1    Krönke, M.2    Jürgensmeier, J.M.3
  • 16
    • 1342303541 scopus 로고    scopus 로고
    • Laser microirradiation of mitochondria: Is there an amplified mitochondrial death signal in neural cells?
    • Khodjakov, A., Rieder, C., Mannella, C. A.and Kinnally, K. W. (2004). Laser microirradiation of mitochondria: is there an amplified mitochondrial death signal in neural cells? Mitochondrion 3, 217-227.
    • (2004) Mitochondrion , vol.3 , pp. 217-227
    • Khodjakov, A.1    Rieder, C.2    Mannella, C.A.3    Kinnally, K.W.4
  • 17
    • 0031037897 scopus 로고    scopus 로고
    • The release of cytochrome c from mitochondria: A primary site for bcl-2 regulation of apoptosis
    • Kluck, R. M., Bossy-Wetzel, E., Green, D. R. and Newmeyer, D. D. (1997). The release of cytochrome c from mitochondria: a primary site for bcl-2 regulation of apoptosis. Science 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
  • 18
    • 33845977959 scopus 로고    scopus 로고
    • Mitochondrial membrane permeabilization in cell death
    • Kroemer, G., Galluzzi, L. and Brenner, C. (2007). Mitochondrial membrane permeabilization in cell death. Physiol Rev. 87, 99-163.
    • (2007) Physiol Rev , vol.87 , pp. 99-163
    • Kroemer, G.1    Galluzzi, L.2    Brenner, C.3
  • 20
    • 0037085380 scopus 로고    scopus 로고
    • Rapid kinetics of tbid-induced cytochrome c and smac/diablo release and mitochondrial depolarization
    • Madesh, M., Antonsson, B., Srinivasula, S. M., Alnemri, E. S. and Hajnóczky, G. (2002). Rapid kinetics of tbid-induced cytochrome c and smac/diablo release and mitochondrial depolarization. J. Biol. Chem. 277, 5651-5659.
    • (2002) J. Biol. Chem , vol.277 , pp. 5651-5659
    • Madesh, M.1    Antonsson, B.2    Srinivasula, S.M.3    Alnemri, E.S.4    Hajnóczky, G.5
  • 21
    • 0030610646 scopus 로고    scopus 로고
    • Fluorescent indicators for ca2+ based on green fluorescent proteins and calmodulin
    • Miyawaki, A., Llopis, J., Heim, R., McCaffery, J. M., Adams, J. A., Ikura, M. and Tsien, R. Y. (1997). Fluorescent indicators for ca2+ based on green fluorescent proteins and calmodulin. Nature 388, 882-887.
    • (1997) Nature , vol.388 , pp. 882-887
    • Miyawaki, A.1    Llopis, J.2    Heim, R.3    McCaffery, J.M.4    Adams, J.A.5    Ikura, M.6    Tsien, R.Y.7
  • 22
    • 0033522391 scopus 로고    scopus 로고
    • Conformation of the bax c-terminus regulates subcellular location and cell death
    • Nechushtan, A., Smith, C. L., Hsu, Y. T. and Youle, R. J. (1999). Conformation of the bax c-terminus regulates subcellular location and cell death. EMBO J. 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
  • 23
    • 0035844867 scopus 로고    scopus 로고
    • Bax and bak coalesce into novel mitochondria-associated clusters during apoptosis
    • Nechushtan, A., Smith, C. L., Lamensdorf, I., Yoon, S. H. and Youle, R. J. (2001). Bax and bak coalesce into novel mitochondria-associated clusters during apoptosis. J. Cell Biol. 153, 1265-1276.
    • (2001) J. Cell Biol , vol.153 , pp. 1265-1276
    • Nechushtan, A.1    Smith, C.L.2    Lamensdorf, I.3    Yoon, S.H.4    Youle, R.J.5
  • 24
    • 0027166048 scopus 로고
    • Bcl-2 heterodimerizes in vivo with a conserved homolog, bax, that accelerates programmed cell death
    • Oltvai, Z. N., Milliman, C. L. and Korsmeyer, S. J. (1993). Bcl-2 heterodimerizes in vivo with a conserved homolog, bax, that accelerates programmed cell death. Cell 74, 609-619.
    • (1993) Cell , vol.74 , pp. 609-619
    • Oltvai, Z.N.1    Milliman, C.L.2    Korsmeyer, S.J.3
  • 25
    • 0035421320 scopus 로고    scopus 로고
    • Propagation of the apoptotic signal by mitochondrial waves
    • Pacher, P. and Hajnoczky, G. (2001). Propagation of the apoptotic signal by mitochondrial waves. EMBO J. 20, 4107-4121.
    • (2001) EMBO J , vol.20 , pp. 4107-4121
    • Pacher, P.1    Hajnoczky, G.2
  • 27
    • 1842613595 scopus 로고    scopus 로고
    • Conformational control of bax localization and apoptotic activity by pro168
    • Schinzel, A., Kaufmann, T., Schuler, M., Martinalbo, J., Grubb, D. and Borner, C. (2004). Conformational control of bax localization and apoptotic activity by pro168. J. Cell Biol. 164, 1021-1032.
    • (2004) J. Cell Biol , vol.164 , pp. 1021-1032
    • Schinzel, A.1    Kaufmann, T.2    Schuler, M.3    Martinalbo, J.4    Grubb, D.5    Borner, C.6
  • 28
    • 34247527336 scopus 로고    scopus 로고
    • Mitochondrial permeabilization relies on bh3 ligands engaging multiple prosurvival bcl-2 relatives, not bak
    • Uren, R. T., Dewson, G., Chen, L., Coyne, S. C., Huang, D. C., Adams, J. M. and Kluck, R. M. (2007). Mitochondrial permeabilization relies on bh3 ligands engaging multiple prosurvival bcl-2 relatives, not bak. J. Cell Biol. 177, 277-287.
    • (2007) J. Cell Biol , vol.177 , pp. 277-287
    • Uren, R.T.1    Dewson, G.2    Chen, L.3    Coyne, S.C.4    Huang, D.C.5    Adams, J.M.6    Kluck, R.M.7
  • 29
    • 4644226744 scopus 로고    scopus 로고
    • Revealing protein dynamics by photobleaching techniques
    • van Drogen, F. and Peter, M. (2004). Revealing protein dynamics by photobleaching techniques. Methods Mol. Biol. 284, 287-306.
    • (2004) Methods Mol. Biol , vol.284 , pp. 287-306
    • van Drogen, F.1    Peter, M.2
  • 30
    • 33646838466 scopus 로고    scopus 로고
    • Real time single cell analysis of bid cleavage and bid translocation during caspase-dependent and neuronal caspase-independent apoptosis
    • Ward, M. W., Rehm, M., Duessmann, H., Kacmar, S., Concannon, C. G. and Prehn, J. H. (2006). Real time single cell analysis of bid cleavage and bid translocation during caspase-dependent and neuronal caspase-independent apoptosis. J. Biol. Chem. 281, 5837-5844.
    • (2006) J. Biol. Chem , vol.281 , pp. 5837-5844
    • Ward, M.W.1    Rehm, M.2    Duessmann, H.3    Kacmar, S.4    Concannon, C.G.5    Prehn, J.H.6
  • 33
    • 33744814124 scopus 로고    scopus 로고
    • The 2.1a crystal structure of copgfp, a representative member of the copepod clade within the green fluorescent protein superfamily
    • Wilmann, P. G., Battad, J., Petersen, J., Wilce, M. C., Dove, S., Devenish, R. J., Prescott, M. and Rossjohn, J. (2006). The 2.1a crystal structure of copgfp, a representative member of the copepod clade within the green fluorescent protein superfamily. J. Mol. Biol. 359, 890-900.
    • (2006) J. Mol. Biol , vol.359 , pp. 890-900
    • Wilmann, P.G.1    Battad, J.2    Petersen, J.3    Wilce, M.C.4    Dove, S.5    Devenish, R.J.6    Prescott, M.7    Rossjohn, J.8
  • 34
    • 0029906828 scopus 로고    scopus 로고
    • Bax-induced cell death may not require interleukin 1 beta-converting enzyme-like proteases
    • Xiang, J., Chao, D. T. and Korsmeyer, S. J. (1996). Bax-induced cell death may not require interleukin 1 beta-converting enzyme-like proteases. Proc. Natl. Acad. Sci. USA 93, 14559-14563.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 14559-14563
    • Xiang, J.1    Chao, D.T.2    Korsmeyer, S.J.3
  • 35
    • 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., Peng, T. I., Jones, D. P. and Wang, X. (1997). Prevention of apoptosis by bcl-2: release of cytochrome c from mitochondria blocked. Science 275, 1129-1132.
    • (1997) Science , vol.275 , pp. 1129-1132
    • Yang, J.1    Liu, X.2    Bhalla, K.3    Kim, C.N.4    Ibrado, A.M.5    Cai, J.6    Peng, T.I.7    Jones, D.P.8    Wang, X.9
  • 36
    • 0034602188 scopus 로고    scopus 로고
    • Role of bax in the apoptotic response to anticancer agents
    • Zhang, L., Yu, J., Park, B. H., Kinzler, K. W. and Vogelstein, B. (2000). Role of bax in the apoptotic response to anticancer agents. Science 290, 989-992.
    • (2000) Science , vol.290 , pp. 989-992
    • Zhang, L.1    Yu, J.2    Park, B.H.3    Kinzler, K.W.4    Vogelstein, B.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.