메뉴 건너뛰기




Volumn 160, Issue 2, 2003, Pages 235-243

Spatio-temporal activation of caspase revealed by indicator that is insensitive to environmental effects

Author keywords

Apoptosis; Caspase 3; Caspase 9; FRET; Nuclear activation of caspase 3

Indexed keywords

CASPASE; CASPASE 3; CASPASE 9; CHLORIDE ION; PROTON; YELLOW FLUORESCENT PROTEIN;

EID: 0037455553     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.200207111     Document Type: Article
Times cited : (270)

References (34)
  • 1
    • 0036289544 scopus 로고    scopus 로고
    • Down-regulation of Mcl-1 by inhibition of the PI3-K/Akt pathway is required for cell shrinkage-dependent cell death
    • Araki, T., M. Hayashi, N. Watanabe, H. Kanuka, J. Yoshino, M. Miura, and T. Saruta. 2002. Down-regulation of Mcl-1 by inhibition of the PI3-K/Akt pathway is required for cell shrinkage-dependent cell death. Biochem. Biophys. Res. Commun. 290:1275-1281.
    • (2002) Biochem. Biophys. Res. Commun. , vol.290 , pp. 1275-1281
    • Araki, T.1    Hayashi, M.2    Watanabe, N.3    Kanuka, H.4    Yoshino, J.5    Miura, M.6    Saruta, T.7
  • 2
    • 0032544449 scopus 로고    scopus 로고
    • Apaf1 (CED-4 homolog) regulates programmed cell death in mammalian development
    • Cecconi, F., G. Alvarez-Bolado, B.I. Meyer, K.A. Roth, and P. Gruss. 1998. Apaf1 (CED-4 homolog) regulates programmed cell death in mammalian development. Cell 94:727-737.
    • (1998) Cell , vol.94 , pp. 727-737
    • Cecconi, F.1    Alvarez-Bolado, G.2    Meyer, B.I.3    Roth, K.A.4    Gruss, P.5
  • 3
    • 0032080004 scopus 로고    scopus 로고
    • Different subcellular distribution of caspase-3 and caspase-7 following Fas-induced apoptosis in mouse liver
    • Chandler, J.M., G.M. Cohen, and M. MacFarlane. 1998. Different subcellular distribution of caspase-3 and caspase-7 following Fas-induced apoptosis in mouse liver. J. Biol. Chem. 273:10815-10818.
    • (1998) J. Biol. Chem. , vol.273 , pp. 10815-10818
    • Chandler, J.M.1    Cohen, G.M.2    MacFarlane, M.3
  • 4
    • 2642689658 scopus 로고    scopus 로고
    • Proteases to die for
    • Cryns, V., and J. Yuan. 1998. Proteases to die for. Genes Dev. 12:1551-1570.
    • (1998) Genes Dev. , vol.12 , pp. 1551-1570
    • Cryns, V.1    Yuan, J.2
  • 6
    • 0034722379 scopus 로고    scopus 로고
    • Caspases disrupt the nuclear-cytoplasmic barrier
    • Faleiro, L., and Y. Lazebnik. 2000. Caspases disrupt the nuclear-cytoplasmic barrier. J. Cell Biol. 151:951-959.
    • (2000) J. Cell Biol. , vol.151 , pp. 951-959
    • Faleiro, L.1    Lazebnik, Y.2
  • 8
    • 0034052719 scopus 로고    scopus 로고
    • Mechanism and cellular applications of a green fluorescent protein-based halide sensor
    • Jayaraman, S., P. Haggie, R.M. Wachter, S.J. Remington, and A.S. Verkman. 2000. Mechanism and cellular applications of a green fluorescent protein-based halide sensor. J. Biol. Chem. 275:6047-6050.
    • (2000) J. Biol. Chem. , vol.275 , pp. 6047-6050
    • Jayaraman, S.1    Haggie, P.2    Wachter, R.M.3    Remington, S.J.4    Verkman, A.S.5
  • 12
    • 0033724998 scopus 로고    scopus 로고
    • A genetically encoded ratiometric indicator for chloride: Capturing chloride transients in cultured hippocampal neurons
    • Kuner, T., and G.J. Augustine. 2000. A genetically encoded ratiometric indicator for chloride: capturing chloride transients in cultured hippocampal neurons. Neuron. 27:447-459.
    • (2000) Neuron , vol.27 , pp. 447-459
    • Kuner, T.1    Augustine, G.J.2
  • 14
    • 0032499784 scopus 로고    scopus 로고
    • Measurement of cytosolic, mitochondrial, and Golgi pH in single living cells with green fluorescent proteins
    • Llopis, J., J.M. McCaffery, A. Miyawaki, M.G. Farquhar, and R.Y. Tsien. 1998. Measurement of cytosolic, mitochondrial, and Golgi pH in single living cells with green fluorescent proteins. Proc. Natl. Acad. Sci. USA. 95:6803-6808.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 6803-6808
    • Llopis, J.1    McCaffery, J.M.2    Miyawaki, A.3    Farquhar, M.G.4    Tsien, R.Y.5
  • 15
    • 0034801529 scopus 로고    scopus 로고
    • Application of the fluorescence resonance energy transfer method for studying the dynamics of caspase-3 activation during UV-induced apoptosis in living HeLa cells
    • Luo, K.Q., V.C. Yu, Y. Pu, and D.C. Chang. 2001. Application of the fluorescence resonance energy transfer method for studying the dynamics of caspase-3 activation during UV-induced apoptosis in living HeLa cells. Biochem. Biophys. Res. Commun. 283:1054-1060.
    • (2001) Biochem. Biophys. Res. Commun. , vol.283 , pp. 1054-1060
    • Luo, K.Q.1    Yu, V.C.2    Pu, Y.3    Chang, D.C.4
  • 16
    • 0034662989 scopus 로고    scopus 로고
    • Normotonic cell shrinkage because of disordered volume regulation is an early prerequisite to apoptosis
    • Maeno, E., Y. Ishizaki, T. Kanaseki, A. Hazama, and Y. Okada. 2000. Normotonic cell shrinkage because of disordered volume regulation is an early prerequisite to apoptosis. Proc. Natl. Acad. Sci. USA. 97:9487-9492.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 9487-9492
    • Maeno, E.1    Ishizaki, Y.2    Kanaseki, T.3    Hazama, A.4    Okada, Y.5
  • 17
    • 0032559799 scopus 로고    scopus 로고
    • The caspase-3 precursor has a cytosolic and mitochondrial distribution: Implications for apoptotic signaling
    • Mancini, M., D.W. Nicholson, S. Roy, N.A. Thornberry, E.P. Peterson, R.L. Casciola, and A. Rosen. 1998. The caspase-3 precursor has a cytosolic and mitochondrial distribution: implications for apoptotic signaling. J. Cell Biol. 140:1485-1495.
    • (1998) J. Cell Biol. , vol.140 , pp. 1485-1495
    • Mancini, M.1    Nicholson, D.W.2    Roy, S.3    Thornberry, N.A.4    Peterson, E.P.5    Casciola, R.L.6    Rosen, A.7
  • 18
    • 0033776271 scopus 로고    scopus 로고
    • Changes in intramitochondrial and cytosolic pH: Early events that modulate caspase activation during apoptosis
    • Matsuyama, S., J. Llopis, Q.L. Deveraux, R.Y. Tsien, and J.C. Reed. 2000. Changes in intramitochondrial and cytosolic pH: early events that modulate caspase activation during apoptosis. Nat. Cell Biol. 2:318-325.
    • (2000) Nat. Cell Biol. , vol.2 , pp. 318-325
    • Matsuyama, S.1    Llopis, J.2    Deveraux, Q.L.3    Tsien, R.Y.4    Reed, J.C.5
  • 20
    • 0037192850 scopus 로고    scopus 로고
    • Nicotine preconditioning antagonizes activity-dependent caspase proteolysis of a glutamate receptor
    • Meyer, E.L., L.C. Gahring, and S.W. Rogers. 2002. Nicotine preconditioning antagonizes activity-dependent caspase proteolysis of a glutamate receptor. J. Biol. Chem. 277:10869-10875.
    • (2002) J. Biol. Chem. , vol.277 , pp. 10869-10875
    • Meyer, E.L.1    Gahring, L.C.2    Rogers, S.W.3
  • 21
    • 0036138908 scopus 로고    scopus 로고
    • A variant of yellow fluorescent protein with fast and efficient maturation for cell-biological applications
    • Nagai, T., K. Ibata, E.S. Park, M. Kubota, K. Mikoshiba, and A. Miyawaki. 2002. A variant of yellow fluorescent protein with fast and efficient maturation for cell-biological applications. Nat. Biotechnol. 20:87-90.
    • (2002) Nat. Biotechnol. , vol.20 , pp. 87-90
    • Nagai, T.1    Ibata, K.2    Park, E.S.3    Kubota, M.4    Mikoshiba, K.5    Miyawaki, A.6
  • 22
    • 0035798645 scopus 로고    scopus 로고
    • Identification of a caspase-9 substrate and detection of its cleavage in programmed cell death during mouse development
    • Nakanishi, K., M. Maruyama, T. Shibara, and N. Morishima. 2001. Identification of a caspase-9 substrate and detection of its cleavage in programmed cell death during mouse development. J. Biol. Chem. 276:41237-41244.
    • (2001) J. Biol. Chem. , vol.276 , pp. 41237-41244
    • Nakanishi, K.1    Maruyama, M.2    Shibara, T.3    Morishima, N.4
  • 23
    • 0028917643 scopus 로고
    • Intracellular alkalinization suppresses lovastatin-induced apoptosis in HL-60 cells through the inactivation of a pH-dependent endonuclease
    • Perez, S.D., E.D. Collado, and F. Mollinedo. 1995. Intracellular alkalinization suppresses lovastatin-induced apoptosis in HL-60 cells through the inactivation of a pH-dependent endonuclease. J. Biol. Chem. 270:6235-6242.
    • (1995) J. Biol. Chem. , vol.270 , pp. 6235-6242
    • Perez, S.D.1    Collado, E.D.2    Mollinedo, F.3
  • 24
    • 0030465544 scopus 로고    scopus 로고
    • Lamin proteolysis facilitates nuclear events during apoptosis
    • Rao, L., D. Perez, and E. White. 1996. Lamin proteolysis facilitates nuclear events during apoptosis. J. Cell Biol. 135:1441-1455.
    • (1996) J. Cell Biol. , vol.135 , pp. 1441-1455
    • Rao, L.1    Perez, D.2    White, E.3
  • 25
    • 0037025346 scopus 로고    scopus 로고
    • Single-cell fluorescence resonance energy transfer analysis demonstrates that caspase activation during apoptosis is a rapid process. Role of caspase-3
    • Rehm, M., H. Dussmann, R.U. Janicke, J.M. Tavare, D. Kogel, and J.H. Prehn. 2002. Single-cell fluorescence resonance energy transfer analysis demonstrates that caspase activation during apoptosis is a rapid process. Role of caspase-3. J. Biol. Chem. 277:24506-24514.
    • (2002) J. Biol. Chem. , vol.277 , pp. 24506-24514
    • Rehm, M.1    Dussmann, H.2    Janicke, R.U.3    Tavare, J.M.4    Kogel, D.5    Prehn, J.H.6
  • 26
    • 0037090614 scopus 로고    scopus 로고
    • Caspase-6 gene disruption reveals a requirement for lamin A cleavage in apoptotic chromatin condensation
    • Ruchaud, S., N. Korfali, P. Villa, T.J. Kottke, C. Dingwall, S.H. Kaufmann, and W.C. Earnshaw. 1997. Caspase-6 gene disruption reveals a requirement for lamin A cleavage in apoptotic chromatin condensation. EMBO J. 21:1967-1977.
    • (1997) EMBO J , vol.21 , pp. 1967-1977
    • Ruchaud, S.1    Korfali, N.2    Villa, P.3    Kottke, T.J.4    Dingwall, C.5    Kaufmann, S.H.6    Earnshaw, W.C.7
  • 27
    • 0036205587 scopus 로고    scopus 로고
    • Mechanisms of caspase activation and inhibition during apoptosis
    • Shi, Y. 2002. Mechanisms of caspase activation and inhibition during apoptosis. Mol. Cell. 9:459-470.
    • (2002) Mol. Cell. , vol.9 , pp. 459-470
    • Shi, Y.1
  • 28
  • 29
    • 0034280126 scopus 로고    scopus 로고
    • Rapid caspase-3 activation during apoptosis revealed using fluorescence-resonance energy transfer
    • Tyas, L., V.A. Brophy, A. Pope, A.J. Rivett, and J.M. Tavare. 2000. Rapid caspase-3 activation during apoptosis revealed using fluorescence-resonance energy transfer. EMBO Rep. 1:266-270.
    • (2000) EMBO Rep. , vol.1 , pp. 266-270
    • Tyas, L.1    Brophy, V.A.2    Pope, A.3    Rivett, A.J.4    Tavare, J.M.5
  • 30
    • 0032864715 scopus 로고    scopus 로고
    • Neuronal intracellular pH directly mediates nitric oxide-induced programmed cell death
    • Vincent, A.M., M. TenBroeke, and K. Maiese. 1999. Neuronal intracellular pH directly mediates nitric oxide-induced programmed cell death. J. Neurobiol. 40:171-184.
    • (1999) J. Neurobiol. , vol.40 , pp. 171-184
    • Vincent, A.M.1    TenBroeke, M.2    Maiese, K.3
  • 31
    • 0031127789 scopus 로고    scopus 로고
    • Is programmed cell death required for neural tube closure?
    • Weil, M., M.D. Jacobson, and M.C. Raff. 1997. Is programmed cell death required for neural tube closure? Curr. Biol. 7:281-284.
    • (1997) Curr. Biol. , vol.7 , pp. 281-284
    • Weil, M.1    Jacobson, M.D.2    Raff, M.C.3
  • 33
    • 0032799633 scopus 로고    scopus 로고
    • Caspases: Their intracellular localization and translocation during apoptosis
    • Zhivotovsky, B., A. Samali, A. Gahm, and S. Orrenius. 1999. Caspases: their intracellular localization and translocation during apoptosis. Cell Death Differ. 6:644-651.
    • (1999) Cell Death Differ , vol.6 , pp. 644-651
    • Zhivotovsky, B.1    Samali, A.2    Gahm, A.3    Orrenius, S.4
  • 34
    • 0029876835 scopus 로고    scopus 로고
    • Requirement for BMP signaling in interdigital apoptosis and scale formation
    • Zou, H., and L. Niswander. 1996. Requirement for BMP signaling in interdigital apoptosis and scale formation. Science. 272:738-741.
    • (1996) Science , vol.272 , pp. 738-741
    • Zou, H.1    Niswander, L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.