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Volumn 5 APR, Issue , 2014, Pages

New roles for old enzymes: Killer caspases as the engine of cell behavior changes

Author keywords

Apoptosis; Caspase; Differentiation; Myogenesis; Non apoptotic roles; Proliferation

Indexed keywords

CASPASE; CASPASE 10; CASPASE 11; CASPASE 12; CASPASE 14; CASPASE 15; CASPASE 16; CASPASE 17; CASPASE 18; CASPASE 2; CASPASE 3; CASPASE 5; CASPASE 6; CASPASE 7; CASPASE 8; CASPASE 9; INTERLEUKIN 1BETA CONVERTING ENZYME; UNCLASSIFIED DRUG;

EID: 84901035390     PISSN: None     EISSN: 1664042X     Source Type: Journal    
DOI: 10.3389/fphys.2014.00149     Document Type: Review
Times cited : (72)

References (112)
  • 1
    • 0035956931 scopus 로고    scopus 로고
    • Programmed cell death mediated by ced-3 and ced-4 protects Caenorhabditis elegans from Salmonella typhimurium-mediated killing
    • doi: 10.1073/pnas.041613098
    • Aballay, A., and Ausubel, F. M. (2001). Programmed cell death mediated by ced-3 and ced-4 protects Caenorhabditis elegans from Salmonella typhimurium-mediated killing. Proc. Natl. Acad. Sci. U.S.A. 98, 2735-2739. doi: 10.1073/pnas.041613098
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 2735-2739
    • Aballay, A.1    Ausubel, F.M.2
  • 2
    • 0037654554 scopus 로고    scopus 로고
    • Caspase activity and a specific cytochrome C are required for sperm differentiation in Drosophila
    • doi: 10.1016/S1534-5807(03)00120-5
    • Arama, E., Agapite, J., and Steller, H. (2003). Caspase activity and a specific cytochrome C are required for sperm differentiation in Drosophila. Dev. Cell 4, 687-697. doi: 10.1016/S1534-5807(03)00120-5
    • (2003) Dev. Cell , vol.4 , pp. 687-697
    • Arama, E.1    Agapite, J.2    Steller, H.3
  • 3
    • 35649007879 scopus 로고    scopus 로고
    • A ubiquitin ligase complex regulates caspase activation during sperm differentiation in Drosophila
    • doi: 10.1371/journal.pbio.0050251
    • Arama, E., Bader, M., Rieckhof, G. E., and Steller, H. (2007). A ubiquitin ligase complex regulates caspase activation during sperm differentiation in Drosophila. PLoS Biol. 5:e251. doi: 10.1371/journal.pbio.0050251
    • (2007) PLoS Biol. , vol.5
    • Arama, E.1    Bader, M.2    Rieckhof, G.E.3    Steller, H.4
  • 4
    • 65949097277 scopus 로고    scopus 로고
    • Caspase-8 association with the focal adhesion complex promotes tumor cell migration and metastasis
    • doi: 10.1158/0008-5472.CAN-08-3937
    • Barbero, S., Mielgo, A., Torres, V., and Teitz, T. (2009). Caspase-8 association with the focal adhesion complex promotes tumor cell migration and metastasis. Cancer Res. 69, 3755-3763. doi: 10.1158/0008-5472.CAN-08-3937
    • (2009) Cancer Res. , vol.69 , pp. 3755-3763
    • Barbero, S.1    Mielgo, A.2    Torres, V.3    Teitz, T.4
  • 5
    • 81955167953 scopus 로고    scopus 로고
    • Abnormal prostaglandin E2 production blocks myogenic differentiation in myotonic dystrophy
    • doi: 10.1016/j.nbd.2011.06.014
    • Beaulieu, D., Thebault, P., Pelletier, R., Chapdelaine, P., Tarnopolsky, M., Furling, D., et al. (2012). Abnormal prostaglandin E2 production blocks myogenic differentiation in myotonic dystrophy. Neurobiol. Dis. 45, 122-129. doi: 10.1016/j.nbd.2011.06.014
    • (2012) Neurobiol. Dis. , vol.45 , pp. 122-129
    • Beaulieu, D.1    Thebault, P.2    Pelletier, R.3    Chapdelaine, P.4    Tarnopolsky, M.5    Furling, D.6
  • 6
    • 78049502859 scopus 로고    scopus 로고
    • Apoptosis, stem cells, and tissue regeneration
    • doi: 10.1126/scisignal.3145re8.Apoptosis
    • Bergmann, A., and Steller, H. (2010). Apoptosis, stem cells, and tissue regeneration. Sci. Signal. 3, 1-16. doi: 10.1126/scisignal.3145re8.Apoptosis
    • (2010) Sci. Signal. , vol.3 , pp. 1-16
    • Bergmann, A.1    Steller, H.2
  • 7
    • 1642433091 scopus 로고    scopus 로고
    • Syncytial fusion of human trophoblast depends on caspase 8
    • doi: 10.1038/sj.cdd.4401307
    • Black, S., Kadyrov, M., Kaufmann, P., Ugele, B., Emans, N., and Huppertz, B. (2004). Syncytial fusion of human trophoblast depends on caspase 8. Cell Death Differ. 11, 90-98. doi: 10.1038/sj.cdd.4401307
    • (2004) Cell Death Differ. , vol.11 , pp. 90-98
    • Black, S.1    Kadyrov, M.2    Kaufmann, P.3    Ugele, B.4    Emans, N.5    Huppertz, B.6
  • 8
    • 84881071322 scopus 로고    scopus 로고
    • Paracrine control of tissue regeneration and cell proliferation by Caspase-3
    • doi: 10.1038/cddis.2013.250
    • Boland, K., Flanagan, L., and Prehn, J. (2013). Paracrine control of tissue regeneration and cell proliferation by Caspase-3. Cell Death Dis. 4, e725. doi: 10.1038/cddis.2013.250
    • (2013) Cell Death Dis. , vol.4
    • Boland, K.1    Flanagan, L.2    Prehn, J.3
  • 9
    • 0030579175 scopus 로고    scopus 로고
    • Scatter factor/hepatocyte growth factor (SF/HGF) induces emigration of myogenic cells at interlimb level in vivo
    • doi: 10.1006/dbio.1996.0260
    • Brand-Saberi, B., Müller, T. S., Wilting, J., Christ, B., and Birchmeier, C. (1996). Scatter factor/hepatocyte growth factor (SF/HGF) induces emigration of myogenic cells at interlimb level in vivo. Dev. Biol. 179, 303-308. doi: 10.1006/dbio.1996.0260
    • (1996) Dev. Biol. , vol.179 , pp. 303-308
    • Brand-Saberi, B.1    Müller, T.S.2    Wilting, J.3    Christ, B.4    Birchmeier, C.5
  • 10
    • 79960151477 scopus 로고    scopus 로고
    • Macrophages programmed by apoptotic cells promote angiogenesis via prostaglandin E2
    • doi: 10.1096/fj.10-179473
    • Brecht, K., Weigert, A., Hu, J., Popp, R., Fisslthaler, B., Korff, T., et al. (2011). Macrophages programmed by apoptotic cells promote angiogenesis via prostaglandin E2. FASEB J. 25, 2408-2417. doi: 10.1096/fj.10-179473
    • (2011) FASEB J. , vol.25 , pp. 2408-2417
    • Brecht, K.1    Weigert, A.2    Hu, J.3    Popp, R.4    Fisslthaler, B.5    Korff, T.6
  • 11
    • 0037468853 scopus 로고    scopus 로고
    • Apoptotic pathway and MAPKs differentially regulate chemotropic responses of retinal growth cones
    • doi: 10.1016/S0896-6273(03)00158-2
    • Campbell, D. S., and Holt, C. E. (2003). Apoptotic pathway and MAPKs differentially regulate chemotropic responses of retinal growth cones. Neuron 37, 939-952. doi: 10.1016/S0896-6273(03)00158-2
    • (2003) Neuron , vol.37 , pp. 939-952
    • Campbell, D.S.1    Holt, C.E.2
  • 12
    • 28544444039 scopus 로고    scopus 로고
    • Prostaglandin E2 promotes colon cancer cell growth through a Gs-axin-beta-catenin signaling axis
    • doi: 10.1126/science.1116221
    • Castellone, M. D., Teramoto, H., Williams, B. O., Druey, K. M., and Gutkind, J. S. (2005). Prostaglandin E2 promotes colon cancer cell growth through a Gs-axin-beta-catenin signaling axis. Science 310, 1504-1510. doi: 10.1126/science.1116221
    • (2005) Science , vol.310 , pp. 1504-1510
    • Castellone, M.D.1    Teramoto, H.2    Williams, B.O.3    Druey, K.M.4    Gutkind, J.S.5
  • 13
    • 0346849710 scopus 로고    scopus 로고
    • Satellite cells attract monocytes and use macrophages as a support to escape apoptosis and enhance muscle growth
    • doi: 10.1083/jcb.200212046
    • Chazaud, B., Sonnet, C., Lafuste, P., Bassez, G., Rimaniol, A. C., Poron, F., et al. (2003). Satellite cells attract monocytes and use macrophages as a support to escape apoptosis and enhance muscle growth. J. Cell Biol. 163, 1133-1143. doi: 10.1083/jcb.200212046
    • (2003) J. Cell Biol. , vol.163 , pp. 1133-1143
    • Chazaud, B.1    Sonnet, C.2    Lafuste, P.3    Bassez, G.4    Rimaniol, A.C.5    Poron, F.6
  • 14
    • 68349122622 scopus 로고    scopus 로고
    • Apoptotic cells provide an unexpected source of Wnt3 signaling to drive hydra head regeneration
    • doi: 10.1016/j.devcel.2009.07.014
    • Chera, S., Ghila, L., Dobretz, K., Wenger, Y., Bauer, C., Buzgariu, W., et al. (2009). Apoptotic cells provide an unexpected source of Wnt3 signaling to drive hydra head regeneration. Dev. Cell 17, 279-289. doi: 10.1016/j.devcel.2009.07.014
    • (2009) Dev. Cell , vol.17 , pp. 279-289
    • Chera, S.1    Ghila, L.2    Dobretz, K.3    Wenger, Y.4    Bauer, C.5    Buzgariu, W.6
  • 15
    • 18544383460 scopus 로고    scopus 로고
    • Pleiotropic defects in lymphocyte activation caused by caspase-8 mutations lead to human immunodeficiency
    • doi: 10.1038/nature01063
    • Chun, H. J., Zheng, L., Ahmad, M., Wang, J., Speirs, C. K., Siegel, R. M., et al. (2002). Pleiotropic defects in lymphocyte activation caused by caspase-8 mutations lead to human immunodeficiency. Nature 419, 395-399. doi: 10.1038/nature01063
    • (2002) Nature , vol.419 , pp. 395-399
    • Chun, H.J.1    Zheng, L.2    Ahmad, M.3    Wang, J.4    Speirs, C.K.5    Siegel, R.M.6
  • 16
    • 0033539017 scopus 로고    scopus 로고
    • Identification of caspases and apoptosis in the simple metazoan Hydra
    • doi: 10.1016/S0960-9822(99)80423-0
    • Cikala, M., Wilm, B., Hobmayer, E., Böttger, A., and David, C. N. (1999). Identification of caspases and apoptosis in the simple metazoan Hydra. Curr. Biol. 9, 959-962. doi: 10.1016/S0960-9822(99)80423-0
    • (1999) Curr. Biol. , vol.9 , pp. 959-962
    • Cikala, M.1    Wilm, B.2    Hobmayer, E.3    Böttger, A.4    David, C.N.5
  • 17
    • 0030931876 scopus 로고    scopus 로고
    • Caspases: the executioners of apoptosis
    • Cohen, G. M. (1997). Caspases: the executioners of apoptosis. Biochem. J. 326, 1-16.
    • (1997) Biochem. J. , vol.326 , pp. 1-16
    • Cohen, G.M.1
  • 18
    • 0037103295 scopus 로고    scopus 로고
    • Platelet formation is the consequence of caspase activation within megakaryocytes
    • doi: 10.1182/blood-2002-03-0686
    • De Botton, S., Sabri, S., Daugas, E., Zermati, Y., Guidotti, J. E., Hermine, O., et al. (2002). Platelet formation is the consequence of caspase activation within megakaryocytes. Blood 100, 1310-1317. doi: 10.1182/blood-2002-03-0686
    • (2002) Blood , vol.100 , pp. 1310-1317
    • De Botton, S.1    Sabri, S.2    Daugas, E.3    Zermati, Y.4    Guidotti, J.E.5    Hermine, O.6
  • 19
    • 46649096691 scopus 로고    scopus 로고
    • Identification of novel mammalian caspases reveals an important role of gene loss in shaping the human caspase repertoire
    • doi: 10.1093/molbev/msn012
    • Eckhart, L., Ballaun, C., Hermann, M., Vandeberg, J. L., Sipos, W., Uthman, A., et al. (2008). Identification of novel mammalian caspases reveals an important role of gene loss in shaping the human caspase repertoire. Mol. Biol. Evol. 25, 831-841. doi: 10.1093/molbev/msn012
    • (2008) Mol. Biol. Evol. , vol.25 , pp. 831-841
    • Eckhart, L.1    Ballaun, C.2    Hermann, M.3    Vandeberg, J.L.4    Sipos, W.5    Uthman, A.6
  • 20
    • 27444439113 scopus 로고    scopus 로고
    • Identification and characterization of a novel mammalian caspase with proapoptotic activity
    • doi: 10.1074/jbc.C500282200
    • Eckhart, L., Ballaun, C., Uthman, A., Kittel, C., Stichenwirth, M., Buchberger, M., et al. (2005). Identification and characterization of a novel mammalian caspase with proapoptotic activity. J. Biol. Chem. 280, 35077-35080. doi: 10.1074/jbc.C500282200
    • (2005) J. Biol. Chem. , vol.280 , pp. 35077-35080
    • Eckhart, L.1    Ballaun, C.2    Uthman, A.3    Kittel, C.4    Stichenwirth, M.5    Buchberger, M.6
  • 21
    • 0034523695 scopus 로고    scopus 로고
    • Terminal differentiation of human keratinocytes and stratum corneum formation is associated with caspase-14 activation
    • doi: 10.1046/j.1523-1747.2000.00205.x
    • Eckhart, L., Declercq, W., Ban, J., Rendl, M., Lengauer, B., Mayer, C., et al. (2000). Terminal differentiation of human keratinocytes and stratum corneum formation is associated with caspase-14 activation. J. Invest. Dermatol. 115, 1148-1151. doi: 10.1046/j.1523-1747.2000.00205.x
    • (2000) J. Invest. Dermatol. , vol.115 , pp. 1148-1151
    • Eckhart, L.1    Declercq, W.2    Ban, J.3    Rendl, M.4    Lengauer, B.5    Mayer, C.6
  • 22
    • 52949102178 scopus 로고    scopus 로고
    • Apoptosis-induced compensatory proliferation. The Cell is dead. Long live the Cell!
    • doi: 10.1016/j.tcb.2008.08.001
    • Fan, Y., and Bergmann, A. (2008). Apoptosis-induced compensatory proliferation. The Cell is dead. Long live the Cell! Trends Cell Biol. 18, 467-473. doi: 10.1016/j.tcb.2008.08.001
    • (2008) Trends Cell Biol. , vol.18 , pp. 467-473
    • Fan, Y.1    Bergmann, A.2
  • 23
    • 84875584603 scopus 로고    scopus 로고
    • Caspase-2 at a glance
    • doi: 10.1242/jcs.115105.95
    • Fava, L. L., Bock, F. J., Geley, S., and Villunger, A. (2012). Caspase-2 at a glance. J. Cell Sci. 125, 5911-5915. doi: 10.1242/jcs.115105.95
    • (2012) J. Cell Sci. , vol.125 , pp. 5911-5915
    • Fava, L.L.1    Bock, F.J.2    Geley, S.3    Villunger, A.4
  • 24
    • 26444537963 scopus 로고    scopus 로고
    • Neural stem cell differentiation is dependent upon endogenous caspase 3 activity
    • doi: 10.1096/fj.04-2981fje
    • Fernando, P., Brunette, S., and Megeney, L. A. (2005). Neural stem cell differentiation is dependent upon endogenous caspase 3 activity. FASEB J. 19, 1671-1673. doi: 10.1096/fj.04-2981fje
    • (2005) FASEB J. , vol.19 , pp. 1671-1673
    • Fernando, P.1    Brunette, S.2    Megeney, L.A.3
  • 25
    • 0037143626 scopus 로고    scopus 로고
    • Caspase 3 activity is required for skeletal muscle differentiation
    • doi: 10.1073/pnas.162172899
    • Fernando, P., and Kelly, J. (2002). Caspase 3 activity is required for skeletal muscle differentiation. Proc. Natl. Acad. Sci. U.S.A. 99, 11025-11030. doi: 10.1073/pnas.162172899
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 11025-11030
    • Fernando, P.1    Kelly, J.2
  • 26
    • 33845975986 scopus 로고    scopus 로고
    • Is caspase-dependent apoptosis only cell differentiation taken to the extreme?
    • doi: 10.1096/fj.06-5912hyp
    • Fernando, P., and Megeney, L. A. (2007). Is caspase-dependent apoptosis only cell differentiation taken to the extreme? FASEB J. 21, 8-17. doi: 10.1096/fj.06-5912hyp
    • (2007) FASEB J. , vol.21 , pp. 8-17
    • Fernando, P.1    Megeney, L.A.2
  • 27
    • 84859975588 scopus 로고    scopus 로고
    • Caspase levels and execution efficiencies determine the apoptotic potential of the cell
    • doi: 10.1083/jcb.201107133
    • Florentin, A., and Arama, E. (2012). Caspase levels and execution efficiencies determine the apoptotic potential of the cell. J. Cell Biol. 196, 513-527. doi: 10.1083/jcb.201107133
    • (2012) J. Cell Biol. , vol.196 , pp. 513-527
    • Florentin, A.1    Arama, E.2
  • 28
    • 60749104683 scopus 로고    scopus 로고
    • The inflammasome: a caspase-1-activation platform that regulates immune responses and disease pathogenesis
    • doi: 10.1038/ni.1703
    • Franchi, L., Eigenbrod, T., Muñoz-Planillo, R., and Nuñez, G. (2009). The inflammasome: a caspase-1-activation platform that regulates immune responses and disease pathogenesis. Nat. Immunol. 10, 241-247. doi: 10.1038/ni.1703
    • (2009) Nat. Immunol. , vol.10 , pp. 241-247
    • Franchi, L.1    Eigenbrod, T.2    Muñoz-Planillo, R.3    Nuñez, G.4
  • 29
    • 0035901969 scopus 로고    scopus 로고
    • Exploitation of a non-apoptotic caspase to regulate the abundance of the cdkI p27(KIP1) in transformed lymphoid cells
    • doi: 10.1038/sj.onc.1204367
    • Frost, V., Al-Mehairi, S., and Sinclair, A. J. (2001). Exploitation of a non-apoptotic caspase to regulate the abundance of the cdkI p27(KIP1) in transformed lymphoid cells. Oncogene 20, 2737-2748. doi: 10.1038/sj.onc.1204367
    • (2001) Oncogene , vol.20 , pp. 2737-2748
    • Frost, V.1    Al-Mehairi, S.2    Sinclair, A.J.3
  • 30
    • 81055125652 scopus 로고    scopus 로고
    • Programmed cell death in animal development and disease
    • doi: 10.1016/j.cell.2011.10.033
    • Fuchs, Y., and Steller, H. (2011). Programmed cell death in animal development and disease. Cell 147, 742-758. doi: 10.1016/j.cell.2011.10.033
    • (2011) Cell , vol.147 , pp. 742-758
    • Fuchs, Y.1    Steller, H.2
  • 31
    • 44349111132 scopus 로고    scopus 로고
    • Caspase activity mediates the differentiation of embryonic stem cells
    • doi: 10.1016/j.stem.2008.04.001
    • Fujita, J., Crane, A. M., Souza, M. K., Dejosez, M., Kyba, M., Flavell, R. A., et al. (2008). Caspase activity mediates the differentiation of embryonic stem cells. Cell Stem Cell 2, 595-601. doi: 10.1016/j.stem.2008.04.001
    • (2008) Cell Stem Cell , vol.2 , pp. 595-601
    • Fujita, J.1    Crane, A.M.2    Souza, M.K.3    Dejosez, M.4    Kyba, M.5    Flavell, R.A.6
  • 32
    • 84891764979 scopus 로고    scopus 로고
    • Dual role of the caspase enzymes in satellite cells from aged and young subjects
    • doi: 10.1038/cddis.2013.472
    • Fulle, S., Sancilio, S., Mancinelli, R., Gatta, V., and Di Pietro, R. (2013). Dual role of the caspase enzymes in satellite cells from aged and young subjects. Cell Death Dis. 4, e955. doi: 10.1038/cddis.2013.472
    • (2013) Cell Death Dis. , vol.4
    • Fulle, S.1    Sancilio, S.2    Mancinelli, R.3    Gatta, V.4    Di Pietro, R.5
  • 33
    • 37849026760 scopus 로고    scopus 로고
    • Basal caspase activity promotes migration and invasiveness in glioblastoma cells
    • doi: 10.1158/1541-7786.MCR-07-0343
    • Gdynia, G., Grund, K., Eckert, A., Böck, B. C., Funke, B., Macher-Goeppinger, S., et al. (2007). Basal caspase activity promotes migration and invasiveness in glioblastoma cells. Mol. Cancer Res. 5, 1232-1240. doi: 10.1158/1541-7786.MCR-07-0343
    • (2007) Mol. Cancer Res. , vol.5 , pp. 1232-1240
    • Gdynia, G.1    Grund, K.2    Eckert, A.3    Böck, B.C.4    Funke, B.5    Macher-Goeppinger, S.6
  • 34
    • 62149148156 scopus 로고    scopus 로고
    • Genetic interaction of PGE2 and Wnt signaling regulates developmental specification of stem cells and regeneration
    • doi: 10.1016/j.cell.2009.01.015.
    • Goessling, W., North, T. E., Loewer, S., Lord, A. M., Lee, S., Stoick-Cooper, C. L., et al. (2009). Genetic interaction of PGE2 and Wnt signaling regulates developmental specification of stem cells and regeneration Cell 136, 1136-1147. doi: 10.1016/j.cell.2009.01.015
    • (2009) Cell , vol.136 , pp. 1136-1147
    • Goessling, W.1    North, T.E.2    Loewer, S.3    Lord, A.M.4    Lee, S.5    Stoick-Cooper, C.L.6
  • 35
    • 0034642306 scopus 로고    scopus 로고
    • Caveolin-3 deficiency causes muscle degeneration in mice
    • doi: 10.1093/hmg/9.20.3047
    • Hagiwara, Y., Sasaoka, T., Araishi, K., Imamura, M., Yorifuji, H., Nonaka, I., et al. (2000). Caveolin-3 deficiency causes muscle degeneration in mice. Hum. Mol. Genet. 9, 3047-3054. doi: 10.1093/hmg/9.20.3047
    • (2000) Hum. Mol. Genet. , vol.9 , pp. 3047-3054
    • Hagiwara, Y.1    Sasaoka, T.2    Araishi, K.3    Imamura, M.4    Yorifuji, H.5    Nonaka, I.6
  • 36
    • 0032493870 scopus 로고    scopus 로고
    • Differential requirement for caspase 9 in apoptotic pathways in vivo
    • doi: 10.1016/S0092-8674(00)81477-4
    • Hakem, R., Hakem, A., Duncan, G. S., Henderson, J. T., Woo, M., Soengas, M. S., et al. (1998). Differential requirement for caspase 9 in apoptotic pathways in vivo. Cell 94, 339-352. doi: 10.1016/S0092-8674(00)81477-4
    • (1998) Cell , vol.94 , pp. 339-352
    • Hakem, R.1    Hakem, A.2    Duncan, G.S.3    Henderson, J.T.4    Woo, M.5    Soengas, M.S.6
  • 37
    • 79953321047 scopus 로고    scopus 로고
    • Contribution of caspase(s) to the cell cycle regulation at mitotic phase
    • doi: 10.1371/journal.pone.0018449
    • Hashimoto, T., Kikkawa, U., and Kamada, S. (2011). Contribution of caspase(s) to the cell cycle regulation at mitotic phase. PLoS ONE 6:e18449. doi: 10.1371/journal.pone.0018449
    • (2011) PLoS ONE , vol.6
    • Hashimoto, T.1    Kikkawa, U.2    Kamada, S.3
  • 38
    • 33646264300 scopus 로고    scopus 로고
    • Caspase-8 promotes cell motility and calpain activity under nonapoptotic conditions
    • doi: 10.1158/0008-5472.CAN-05-4183
    • Helfer, B., Boswell, B. C., Finlay, D., Cipres, A., Vuori, K., Bong Kang, T., et al. (2006). Caspase-8 promotes cell motility and calpain activity under nonapoptotic conditions. Cancer Res. 66, 4273-4278. doi: 10.1158/0008-5472.CAN-05-4183
    • (2006) Cancer Res. , vol.66 , pp. 4273-4278
    • Helfer, B.1    Boswell, B.C.2    Finlay, D.3    Cipres, A.4    Vuori, K.5    Bong Kang, T.6
  • 39
    • 84877775057 scopus 로고    scopus 로고
    • Phosphatidylserine receptor BAI1 and apoptotic cells as new promoters of myoblast fusion
    • doi: 10.1038/nature12135
    • Hochreiter-Hufford, A. E., Lee, C. S., Kinchen, J. M., Sokolowski, J. D., Arandjelovic, S., Call, J. A., et al. (2013). Phosphatidylserine receptor BAI1 and apoptotic cells as new promoters of myoblast fusion. Nature 497, 263-267. doi: 10.1038/nature12135
    • (2013) Nature , vol.497 , pp. 263-267
    • Hochreiter-Hufford, A.E.1    Lee, C.S.2    Kinchen, J.M.3    Sokolowski, J.D.4    Arandjelovic, S.5    Call, J.A.6
  • 40
    • 19344368275 scopus 로고    scopus 로고
    • Multiple apoptotic caspase cascades are required in nonapoptotic roles for Drosophila spermatid individualization
    • doi: 10.1371/journal.pbio.0020015
    • Huh, J. R., Vernooy, S. Y., Yu, H., Yan, N., Shi, Y., Guo, M., et al. (2004). Multiple apoptotic caspase cascades are required in nonapoptotic roles for Drosophila spermatid individualization. PLoS Biol. 2:E15. doi: 10.1371/journal.pbio.0020015
    • (2004) PLoS Biol. , vol.2
    • Huh, J.R.1    Vernooy, S.Y.2    Yu, H.3    Yan, N.4    Shi, Y.5    Guo, M.6
  • 41
    • 84862113237 scopus 로고    scopus 로고
    • Apoptotic and non-apoptotic roles of caspases in neuronal physiology and pathophysiology
    • doi: 10.1038/nrn3228
    • Hyman, B. T., and Yuan, J. (2012). Apoptotic and non-apoptotic roles of caspases in neuronal physiology and pathophysiology. Nat. Rev. Neurosci. 13, 395-406. doi: 10.1038/nrn3228
    • (2012) Nat. Rev. Neurosci. , vol.13 , pp. 395-406
    • Hyman, B.T.1    Yuan, J.2
  • 42
    • 65649142191 scopus 로고    scopus 로고
    • The death domain of FADD is essential for embryogenesis, lymphocyte development, and proliferation
    • doi: 10.1074/jbc.M900249200
    • Imtiyaz, H. Z., Zhou, X., Zhang, H., Chen, D., Hu, T., and Zhang, J. (2009). The death domain of FADD is essential for embryogenesis, lymphocyte development, and proliferation. J. Biol. Chem. 284, 9917-9926. doi: 10.1074/jbc.M900249200
    • (2009) J. Biol. Chem. , vol.284 , pp. 9917-9926
    • Imtiyaz, H.Z.1    Zhou, X.2    Zhang, H.3    Chen, D.4    Hu, T.5    Zhang, J.6
  • 43
    • 67549118622 scopus 로고    scopus 로고
    • Ordering of caspases in cells undergoing apoptosis by the intrinsic pathway
    • doi: 10.1038/cdd.2009.29
    • Inoue, S., Browne, G., Melino, G., and Cohen, G. M. (2009). Ordering of caspases in cells undergoing apoptosis by the intrinsic pathway. Cell Death Differ. 16, 1053-1061. doi: 10.1038/cdd.2009.29
    • (2009) Cell Death Differ. , vol.16 , pp. 1053-1061
    • Inoue, S.1    Browne, G.2    Melino, G.3    Cohen, G.M.4
  • 44
    • 0031894491 scopus 로고    scopus 로고
    • A role for caspases in lens fiber differentiation
    • Ishizaki, Y., Jacobson, M. D., and Raff, M. C. (1998). A role for caspases in lens fiber differentiation. J. Cell Biol. 140, 153-158.
    • (1998) J. Cell Biol. , vol.140 , pp. 153-158
    • Ishizaki, Y.1    Jacobson, M.D.2    Raff, M.C.3
  • 45
    • 84866235333 scopus 로고    scopus 로고
    • "Dead Cells Talking": the silent form of cell death is not so quiet
    • doi: 10.1155/2012/453838
    • Jäger, R., and Fearnhead, H. O. (2012). "Dead Cells Talking": the silent form of cell death is not so quiet. Biochem. Res. Int. 2012:453838. doi: 10.1155/2012/453838
    • (2012) Biochem. Res. Int. , vol.2012 , pp. 453838
    • Jäger, R.1    Fearnhead, H.O.2
  • 46
    • 79952301185 scopus 로고    scopus 로고
    • The enigmatic roles of caspases in tumor development
    • doi: 10.3390/cancers2041952
    • Jäger, R., and Zwacka, R. M. (2010). The enigmatic roles of caspases in tumor development. Cancers (Basel) 2, 1952-1979. doi: 10.3390/cancers2041952
    • (2010) Cancers (Basel) , vol.2 , pp. 1952-1979
    • Jäger, R.1    Zwacka, R.M.2
  • 47
    • 44349188910 scopus 로고    scopus 로고
    • Hematopoietic stem cell responsiveness to exogenous signals is limited by caspase-3
    • doi: 10.1016/j.stem.2008.03.012
    • Janzen, V., Fleming, H. E., Riedt, T., Karlsson, G., Riese, M. J., Lo Celso, C., et al. (2008). Hematopoietic stem cell responsiveness to exogenous signals is limited by caspase-3. Cell Stem Cell 2, 584-594. doi: 10.1016/j.stem.2008.03.012
    • (2008) Cell Stem Cell , vol.2 , pp. 584-594
    • Janzen, V.1    Fleming, H.E.2    Riedt, T.3    Karlsson, G.4    Riese, M.J.5    Lo Celso, C.6
  • 48
    • 50249184065 scopus 로고    scopus 로고
    • Caspase cleavage is not for everyone
    • doi: 10.1016/j.cell.2008.08.019
    • Johnson, C. E., and Kornbluth, S. (2008). Caspase cleavage is not for everyone. Cell 134, 720-721. doi: 10.1016/j.cell.2008.08.019
    • (2008) Cell , vol.134 , pp. 720-721
    • Johnson, C.E.1    Kornbluth, S.2
  • 49
    • 4344560197 scopus 로고    scopus 로고
    • Caspase-8 serves both apoptotic and nonapoptotic roles
    • Kang, T., and Ben-Moshe, T. (2004). Caspase-8 serves both apoptotic and nonapoptotic roles. J. Immunol. 173, 2976-2984.
    • (2004) J. Immunol. , vol.173 , pp. 2976-2984
    • Kang, T.1    Ben-Moshe, T.2
  • 50
    • 77954927345 scopus 로고    scopus 로고
    • Gradients of a ubiquitin E3 ligase inhibitor and a caspase inhibitor determine differentiation or death in spermatids
    • doi: 10.1016/j.devcel.2010.06.009
    • Kaplan, Y., Gibbs-Bar, L., Kalifa, Y., Feinstein-Rotkopf, Y., and Arama, E. (2010). Gradients of a ubiquitin E3 ligase inhibitor and a caspase inhibitor determine differentiation or death in spermatids. Dev. Cell 19, 160-173. doi: 10.1016/j.devcel.2010.06.009
    • (2010) Dev. Cell , vol.19 , pp. 160-173
    • Kaplan, Y.1    Gibbs-Bar, L.2    Kalifa, Y.3    Feinstein-Rotkopf, Y.4    Arama, E.5
  • 51
    • 80455176839 scopus 로고    scopus 로고
    • Non-canonical inflammasome activation targets caspase-11
    • doi: 10.1038/nature10558
    • Kayagaki, N., Warming, S., Lamkanfi, M., Vande Walle, L., Louie, S., Dong, J., et al. (2011). Non-canonical inflammasome activation targets caspase-11. Nature 479, 117-121. doi: 10.1038/nature10558
    • (2011) Nature , vol.479 , pp. 117-121
    • Kayagaki, N.1    Warming, S.2    Lamkanfi, M.3    Vande Walle, L.4    Louie, S.5    Dong, J.6
  • 52
    • 0033386808 scopus 로고    scopus 로고
    • Caspase activation is required for T cell proliferation
    • doi: 10.1084/jem.190.12.1891
    • Kennedy, N. J., Kataoka, T., Tschopp, J., and Budd, R. C. (1999). Caspase activation is required for T cell proliferation. J. Exp. Med. 190, 1891-1896. doi: 10.1084/jem.190.12.1891
    • (1999) J. Exp. Med. , vol.190 , pp. 1891-1896
    • Kennedy, N.J.1    Kataoka, T.2    Tschopp, J.3    Budd, R.C.4
  • 53
    • 76249099065 scopus 로고    scopus 로고
    • Role of CX3CL1/fractalkine in osteoclast differentiation and bone resorption
    • doi: 10.4049/jimmunol.0803627
    • Koizumi, K., Saitoh, Y., Minami, T., Takeno, N., Tsuneyama, K., Miyahara, T., et al. (2009). Role of CX3CL1/fractalkine in osteoclast differentiation and bone resorption. J. Immunol. 183, 7825-7831. doi: 10.4049/jimmunol.0803627
    • (2009) J. Immunol. , vol.183 , pp. 7825-7831
    • Koizumi, K.1    Saitoh, Y.2    Minami, T.3    Takeno, N.4    Tsuneyama, K.5    Miyahara, T.6
  • 54
    • 0032493910 scopus 로고    scopus 로고
    • Reduced apoptosis and cytochrome c-mediated caspase activation in mice lacking caspase 9
    • doi: 10.1016/S0092-8674(00)81476-2
    • Kuida, K., Haydar, T. F., Kuan, C. Y., Gu, Y., Taya, C., Karasuyama, H., et al. (1998). Reduced apoptosis and cytochrome c-mediated caspase activation in mice lacking caspase 9. Cell 94, 325-337. doi: 10.1016/S0092-8674(00)81476-2
    • (1998) Cell , vol.94 , pp. 325-337
    • Kuida, K.1    Haydar, T.F.2    Kuan, C.Y.3    Gu, Y.4    Taya, C.5    Karasuyama, H.6
  • 55
    • 0029956641 scopus 로고    scopus 로고
    • Decreased apoptosis in the brain and premature lethality in CPP32-deficient mice
    • Kuida, K., Zheng, T. S., Na, S., Kuan, C., Yang, D., Karasuyama, H., et al. (1996). Decreased apoptosis in the brain and premature lethality in CPP32-deficient mice. Nature 384, 368-372.
    • (1996) Nature , vol.384 , pp. 368-372
    • Kuida, K.1    Zheng, T.S.2    Na, S.3    Kuan, C.4    Yang, D.5    Karasuyama, H.6
  • 56
    • 33746363831 scopus 로고    scopus 로고
    • Identification of E2/E3 ubiquitinating enzymes and caspase activity regulating Drosophila sensory neuron dendrite pruning
    • doi: 10.1016/j.neuron.2006.07.014
    • Kuo, C. T., Zhu, S., Younger, S., Jan, L. Y., and Jan, Y. N. (2006). Identification of E2/E3 ubiquitinating enzymes and caspase activity regulating Drosophila sensory neuron dendrite pruning. Neuron 51, 283-290. doi: 10.1016/j.neuron.2006.07.014
    • (2006) Neuron , vol.51 , pp. 283-290
    • Kuo, C.T.1    Zhu, S.2    Younger, S.3    Jan, L.Y.4    Jan, Y.N.5
  • 57
    • 84855883172 scopus 로고    scopus 로고
    • Beyond apoptosis: caspase regulatory mechanisms and functions in vivo
    • doi: 10.1111/j.1365-2443.2011.01579.x
    • Kuranaga, E. (2012). Beyond apoptosis: caspase regulatory mechanisms and functions in vivo. Genes Cells 17, 83-97. doi: 10.1111/j.1365-2443.2011.01579.x
    • (2012) Genes Cells , vol.17 , pp. 83-97
    • Kuranaga, E.1
  • 58
    • 33847367323 scopus 로고    scopus 로고
    • Nonapoptotic functions of caspases: caspases as regulatory molecules for immunity and cell-fate determination
    • doi: 10.1016/j.tcb.2007.01.001
    • Kuranaga, E., and Miura, M. (2007). Nonapoptotic functions of caspases: caspases as regulatory molecules for immunity and cell-fate determination. Trends Cell Biol. 17, 135-144. doi: 10.1016/j.tcb.2007.01.001
    • (2007) Trends Cell Biol. , vol.17 , pp. 135-144
    • Kuranaga, E.1    Miura, M.2
  • 60
    • 77956863358 scopus 로고    scopus 로고
    • Parole terms for a killer: directing caspase3/CAD induced DNA strand breaks to coordinate changes in gene expression
    • doi: 10.4161/cc.9.15.12335
    • Larsen, B. D., and Megeney, L. A. (2010). Parole terms for a killer: directing caspase3/CAD induced DNA strand breaks to coordinate changes in gene expression. Cell Cycle 9, 2940-2945. doi: 10.4161/cc.9.15.12335
    • (2010) Cell Cycle , vol.9 , pp. 2940-2945
    • Larsen, B.D.1    Megeney, L.A.2
  • 61
    • 77749298000 scopus 로고    scopus 로고
    • Caspase 3/caspase-activated DNase promotes cell differentiation by inducing DNA strand breaks
    • doi: 10.1073/pnas.0913089107
    • Larsen, B. D., Rampalli, S., Burns, L. E., Brunette, S., Dilworth, F. J., and Megeney, L. A. (2010). Caspase 3/caspase-activated DNase promotes cell differentiation by inducing DNA strand breaks. Proc. Natl. Acad. Sci. U.S.A. 107, 4230-4235. doi: 10.1073/pnas.0913089107
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 4230-4235
    • Larsen, B.D.1    Rampalli, S.2    Burns, L.E.3    Brunette, S.4    Dilworth, F.J.5    Megeney, L.A.6
  • 62
    • 0038820117 scopus 로고    scopus 로고
    • Apoptotic cells induce migration of phagocytes via caspase-3-mediated release of a lipid attraction signal
    • doi: 10.1016/S0092-8674(03)00422-7
    • Lauber, K., Bohn, E., Kröber, S., and Xiao, Y. (2003). Apoptotic cells induce migration of phagocytes via caspase-3-mediated release of a lipid attraction signal. Cell 113, 717-730. doi: 10.1016/S0092-8674(03)00422-7
    • (2003) Cell , vol.113 , pp. 717-730
    • Lauber, K.1    Bohn, E.2    Kröber, S.3    Xiao, Y.4
  • 63
    • 0034305744 scopus 로고    scopus 로고
    • The Drosophila caspase Dredd is required to resist gram-negative bacterial infection
    • doi: 10.1093/embo-reports/kvd073
    • Leulier, F., Rodriguez, A., Khush, R. S., Abrams, J. M., and Lemaitre, B. (2000). The Drosophila caspase Dredd is required to resist gram-negative bacterial infection. EMBO Rep. 1, 353-358. doi: 10.1093/embo-reports/kvd073
    • (2000) EMBO Rep. , vol.1 , pp. 353-358
    • Leulier, F.1    Rodriguez, A.2    Khush, R.S.3    Abrams, J.M.4    Lemaitre, B.5
  • 64
    • 77957360239 scopus 로고    scopus 로고
    • Apoptotic caspases regulate induction of iPSCs from human fibroblasts
    • doi: 10.1016/j.stem.2010.09.003
    • Li, F., He, Z., Shen, J., Huang, Q., Li, W., Liu, X., et al. (2010b). Apoptotic caspases regulate induction of iPSCs from human fibroblasts. Cell Stem Cell 7, 508-520. doi: 10.1016/j.stem.2010.09.003
    • (2010) Cell Stem Cell , vol.7 , pp. 508-520
    • Li, F.1    He, Z.2    Shen, J.3    Huang, Q.4    Li, W.5    Liu, X.6
  • 65
    • 77949847250 scopus 로고    scopus 로고
    • Apoptotic cells activate the "phoenix rising" pathway to promote wound healing and tissue regeneration
    • doi: 10.1126/scisignal.2000634
    • Li, F., Huang, Q., Chen, J., Peng, Y., Roop, D. R., and Bedford, J. S. (2010a). Apoptotic cells activate the "phoenix rising" pathway to promote wound healing and tissue regeneration. Sci. Signal. 3, 13. doi: 10.1126/scisignal.2000634
    • (2010) Sci. Signal. , vol.3 , pp. 13
    • Li, F.1    Huang, Q.2    Chen, J.3    Peng, Y.4    Roop, D.R.5    Bedford, J.S.6
  • 66
    • 33847338043 scopus 로고    scopus 로고
    • Caspase-11 regulates cell migration by promoting Aip1-Cofilin-mediated actin depolymerization
    • doi: 10.1038/ncb1541
    • Li, J., Brieher, W. M., Scimone, M. L., Kang, S. J., Zhu, H., Yin, H., et al. (2007). Caspase-11 regulates cell migration by promoting Aip1-Cofilin-mediated actin depolymerization. Nat. Cell Biol. 9, 276-286. doi: 10.1038/ncb1541
    • (2007) Nat. Cell Biol. , vol.9 , pp. 276-286
    • Li, J.1    Brieher, W.M.2    Scimone, M.L.3    Kang, S.J.4    Zhu, H.5    Yin, H.6
  • 67
    • 0028984948 scopus 로고
    • Mice deficient in IL-1 beta-converting enzyme are defective in production of mature IL-1 beta and resistant to endotoxic shock
    • Li, P., Allen, H., Banerjee, S., Frankli, S., Herzog, L., Johnston, C., et al. (1995). Mice deficient in IL-1 beta-converting enzyme are defective in production of mature IL-1 beta and resistant to endotoxic shock. Cell 80, 401-411.
    • (1995) Cell , vol.80 , pp. 401-411
    • Li, P.1    Allen, H.2    Banerjee, S.3    Frankli, S.4    Herzog, L.5    Johnston, C.6
  • 68
    • 77953271477 scopus 로고    scopus 로고
    • Caspase-3 activation via mitochondria is required for long-term depression and AMPA receptor internalization
    • doi: 10.1016/j.cell.2010.03.053
    • Li, Z., Jo, J., Jia, J. M., Lo, S. C., Whitcomb, D. J., Jiao, S., et al. (2010c). Caspase-3 activation via mitochondria is required for long-term depression and AMPA receptor internalization. Cell 141, 859-871. doi: 10.1016/j.cell.2010.03.053
    • (2010) Cell , vol.141 , pp. 859-871
    • Li, Z.1    Jo, J.2    Jia, J.M.3    Lo, S.C.4    Whitcomb, D.J.5    Jiao, S.6
  • 69
    • 33947426526 scopus 로고    scopus 로고
    • The CASBAH: a searchable database of caspase substrates
    • doi: 10.1038/sj.cdd.4402103
    • Lüthi, A. U., and Martin, S. J. (2007). The CASBAH: a searchable database of caspase substrates. Cell Death Differ. 14, 641-650. doi: 10.1038/sj.cdd.4402103
    • (2007) Cell Death Differ. , vol.14 , pp. 641-650
    • Lüthi, A.U.1    Martin, S.J.2
  • 70
    • 78649635776 scopus 로고    scopus 로고
    • Molecular cell death platforms and assemblies
    • doi: 10.1016/j.ceb.2010.08.004
    • Mace, P. D., and Riedl, S. J. (2010). Molecular cell death platforms and assemblies. Curr. Opin. Cell Biol. 22, 828-836. doi: 10.1016/j.ceb.2010.08.004
    • (2010) Curr. Opin. Cell Biol. , vol.22 , pp. 828-836
    • Mace, P.D.1    Riedl, S.J.2
  • 71
    • 77449084943 scopus 로고    scopus 로고
    • Assembling the building blocks: structure and function of inhibitor of apoptosis proteins
    • doi: 10.1038/cdd.2009.45
    • Mace, P. D., Shirley, S., and Day, C. L. (2010). Assembling the building blocks: structure and function of inhibitor of apoptosis proteins. Cell Death Differ. 17, 46-53. doi: 10.1038/cdd.2009.45
    • (2010) Cell Death Differ. , vol.17 , pp. 46-53
    • Mace, P.D.1    Shirley, S.2    Day, C.L.3
  • 72
    • 50049090026 scopus 로고    scopus 로고
    • Ceramidases: regulators of cellular responses mediated by ceramide, sphingosine, and sphingosine-1-phosphate
    • doi: 10.1016/j.bbalip.2008.06.002
    • Mao, C., and Obeid, L. M. (2008). Ceramidases: regulators of cellular responses mediated by ceramide, sphingosine, and sphingosine-1-phosphate. Biochim. Biophys. Acta 1781, 424-434. doi: 10.1016/j.bbalip.2008.06.002
    • (2008) Biochim. Biophys. Acta , vol.1781 , pp. 424-434
    • Mao, C.1    Obeid, L.M.2
  • 73
    • 84879292885 scopus 로고    scopus 로고
    • Caspase-7 participates in differentiation of cells forming dental hard tissues
    • doi: 10.1111/dgd.12066
    • Matalova, E., Lesot, H., Svandova, E., Vanden Berghe, T., Sharpe, P. T., Healy, C., et al. (2013). Caspase-7 participates in differentiation of cells forming dental hard tissues. Dev. Growth Differ. 55, 615-621. doi: 10.1111/dgd.12066
    • (2013) Dev. Growth Differ. , vol.55 , pp. 615-621
    • Matalova, E.1    Lesot, H.2    Svandova, E.3    Vanden Berghe, T.4    Sharpe, P.T.5    Healy, C.6
  • 74
    • 33745684527 scopus 로고    scopus 로고
    • Metastasis: a question of life or death
    • doi: 10.1038/nrc1886
    • Mehlen, P., and Puisieux, A. (2006). Metastasis: a question of life or death. Nat. Rev. Cancer 6, 449-458. doi: 10.1038/nrc1886
    • (2006) Nat. Rev. Cancer , vol.6 , pp. 449-458
    • Mehlen, P.1    Puisieux, A.2
  • 75
    • 84865655542 scopus 로고    scopus 로고
    • Apoptotic and nonapoptotic caspase functions in animal development
    • doi: 10.1101/cshperspect.a008664
    • Miura, M. (2012). Apoptotic and nonapoptotic caspase functions in animal development. Cold Spring Harb. Perspect. Biol. 4, 1-16. doi: 10.1101/cshperspect.a008664
    • (2012) Cold Spring Harb. Perspect. Biol. , vol.4 , pp. 1-16
    • Miura, M.1
  • 76
    • 0346220291 scopus 로고    scopus 로고
    • Activation of caspases is required for osteoblastic differentiation
    • doi: 10.1074/jbc.M307055200
    • Mogi, M., and Togari, A. (2003). Activation of caspases is required for osteoblastic differentiation. J. Biol. Chem. 278, 47477-47482. doi: 10.1074/jbc.M307055200
    • (2003) J. Biol. Chem. , vol.278 , pp. 47477-47482
    • Mogi, M.1    Togari, A.2
  • 77
    • 0030219748 scopus 로고    scopus 로고
    • Defining the regulatory networks for muscle development
    • doi: 10.1016/S0959-437X(96)80066-9
    • Molkentin, J. D., and Olson, E. N. (1996). Defining the regulatory networks for muscle development. Curr. Opin. Genet. Dev. 6, 445-453. doi: 10.1016/S0959-437X(96)80066-9
    • (1996) Curr. Opin. Genet. Dev. , vol.6 , pp. 445-453
    • Molkentin, J.D.1    Olson, E.N.2
  • 78
    • 79951833653 scopus 로고    scopus 로고
    • Mitogenic signaling from apoptotic cells in Drosophila
    • doi: 10.1111/j.1440-169X.2010.01225.x
    • Morata, G., Shlevkov, E., and Pérez-Garijo, A. (2011). Mitogenic signaling from apoptotic cells in Drosophila. Dev. Growth Differ. 53, 168-176. doi: 10.1111/j.1440-169X.2010.01225.x
    • (2011) Dev. Growth Differ. , vol.53 , pp. 168-176
    • Morata, G.1    Shlevkov, E.2    Pérez-Garijo, A.3
  • 79
    • 65949115922 scopus 로고    scopus 로고
    • Modulation of caspase activity regulates skeletal muscle regeneration and function in response to vasopressin and tumor necrosis factor
    • doi: 10.1371/journal.pone.0005570
    • Moresi, V., Garcia-Alvarez, G., Pristerà, A., Rizzuto, E., Albertini, M. C., Rocchi, M., et al. (2009). Modulation of caspase activity regulates skeletal muscle regeneration and function in response to vasopressin and tumor necrosis factor. PLoS ONE 4:e5570. doi: 10.1371/journal.pone.0005570
    • (2009) PLoS ONE , vol.4
    • Moresi, V.1    Garcia-Alvarez, G.2    Pristerà, A.3    Rizzuto, E.4    Albertini, M.C.5    Rocchi, M.6
  • 80
    • 49249107691 scopus 로고    scopus 로고
    • Tumor necrosis factor-alpha inhibition of skeletal muscle regeneration is mediated by a caspase-dependent stem cell response
    • doi: 10.1634/stemcells.2007-0493
    • Moresi, V., Pristerà, A., Scicchitano, B. M., Molinaro, M., Teodori, L., Sassoon, D., et al. (2008). Tumor necrosis factor-alpha inhibition of skeletal muscle regeneration is mediated by a caspase-dependent stem cell response. Stem Cells 26, 997-1008. doi: 10.1634/stemcells.2007-0493
    • (2008) Stem Cells , vol.26 , pp. 997-1008
    • Moresi, V.1    Pristerà, A.2    Scicchitano, B.M.3    Molinaro, M.4    Teodori, L.5    Sassoon, D.6
  • 81
    • 59549096678 scopus 로고    scopus 로고
    • A non-apoptotic role for caspase-9 in muscle differentiation
    • doi: 10.1242/jcs.024547
    • Murray, T. V., McMahon, J. M., Howley, B. H., Stanley, A., Ritter, T., Mohr, A., et al. (2008). A non-apoptotic role for caspase-9 in muscle differentiation. J. Cell Sci. 121, 3786-3793. doi: 10.1242/jcs.024547
    • (2008) J. Cell Sci. , vol.121 , pp. 3786-3793
    • Murray, T.V.1    McMahon, J.M.2    Howley, B.H.3    Stanley, A.4    Ritter, T.5    Mohr, A.6
  • 82
    • 11144356373 scopus 로고    scopus 로고
    • High commitment of embryonic keratinocytes to terminal differentiation through a Notch1-caspase 3 regulatory mechanism
    • doi: 10.1016/S1534-5807(04)00098-X
    • Okuyama, R., Nguyen, B. C., Talora, C., Ogawa, E., Tommasi di Vignano, A., Lioumi, M., et al. (2004). High commitment of embryonic keratinocytes to terminal differentiation through a Notch1-caspase 3 regulatory mechanism. Dev. Cell 6, 551-562. doi: 10.1016/S1534-5807(04)00098-X
    • (2004) Dev. Cell , vol.6 , pp. 551-562
    • Okuyama, R.1    Nguyen, B.C.2    Talora, C.3    Ogawa, E.4    Tommasi di Vignano, A.5    Lioumi, M.6
  • 83
    • 33645847531 scopus 로고    scopus 로고
    • Bergmann glia utilize active caspase-3 for differentiation
    • doi: 10.1016/j.brainres.2006.01.041
    • Oomman, S., Strahlendorf, H., Dertien, J., and Strahlendorf, J. (2006). Bergmann glia utilize active caspase-3 for differentiation. Brain Res. 1078, 19-34. doi: 10.1016/j.brainres.2006.01.041
    • (2006) Brain Res. , vol.1078 , pp. 19-34
    • Oomman, S.1    Strahlendorf, H.2    Dertien, J.3    Strahlendorf, J.4
  • 84
    • 28444464769 scopus 로고    scopus 로고
    • Non-lethal active caspase-3 expression in Bergmann glia of postnatal rat cerebellum
    • doi: 10.1016/j.devbrainres.2005.07.010
    • Oomman, S., Strahlendorf, H., Finckbone, V., and Strahlendorf, J. (2005). Non-lethal active caspase-3 expression in Bergmann glia of postnatal rat cerebellum. Brain Res. Dev. Brain Res. 160, 130-145. doi: 10.1016/j.devbrainres.2005.07.010
    • (2005) Brain Res. Dev. Brain Res. , vol.160 , pp. 130-145
    • Oomman, S.1    Strahlendorf, H.2    Finckbone, V.3    Strahlendorf, J.4
  • 85
    • 18344386198 scopus 로고    scopus 로고
    • Inactivating mutations of the caspase-10 gene in gastric cancer
    • doi: 10.1038/sj.onc.1205394
    • Park, W. S., Lee, J. H., Shin, M. S., Park, J. Y., Kim, H. S., Lee, J. H., et al. (2002). Inactivating mutations of the caspase-10 gene in gastric cancer. Oncogene 21, 2919-2925. doi: 10.1038/sj.onc.1205394
    • (2002) Oncogene , vol.21 , pp. 2919-2925
    • Park, W.S.1    Lee, J.H.2    Shin, M.S.3    Park, J.Y.4    Kim, H.S.5    Lee, J.H.6
  • 86
    • 69249100500 scopus 로고    scopus 로고
    • Human caspases: activation, specificity, and regulation
    • doi: 10.1074/jbc.R800084200
    • Pop, C., and Salvesen, G. S. (2009). Human caspases: activation, specificity, and regulation. J. Biol. Chem. 284, 21777-21781. doi: 10.1074/jbc.R800084200
    • (2009) J. Biol. Chem. , vol.284 , pp. 21777-21781
    • Pop, C.1    Salvesen, G.S.2
  • 87
    • 0038024241 scopus 로고    scopus 로고
    • Rocks: multifunctional kinases in cell behaviour
    • doi: 10.1038/nrm1128
    • Riento, K., and Ridley, A. J. (2003). Rocks: multifunctional kinases in cell behaviour. Nat. Rev. Mol. Cell Biol. 4, 446-456. doi: 10.1038/nrm1128
    • (2003) Nat. Rev. Mol. Cell Biol. , vol.4 , pp. 446-456
    • Riento, K.1    Ridley, A.J.2
  • 88
    • 84873411033 scopus 로고    scopus 로고
    • Caspase signalling in the absence of apoptosis drives Jnk-dependent invasion
    • doi: 10.1038/embor.2012.217
    • Rudrapatna, V. A., Bangi, E., and Cagan, R. L. (2013). Caspase signalling in the absence of apoptosis drives Jnk-dependent invasion. EMBO Rep. 14, 172-177. doi: 10.1038/embor.2012.217
    • (2013) EMBO Rep. , vol.14 , pp. 172-177
    • Rudrapatna, V.A.1    Bangi, E.2    Cagan, R.L.3
  • 89
    • 12344320655 scopus 로고    scopus 로고
    • Lysophosphatidylcholine induces keratinocyte differentiation and upregulation of AP-1- and NF-kappaB DNA-binding activity
    • doi: 10.1080/00015550410016930
    • Ryborg, A. K., Johansen, C., Iversen, L., and Kragballe, K. (2004). Lysophosphatidylcholine induces keratinocyte differentiation and upregulation of AP-1- and NF-kappaB DNA-binding activity. Acta Derm. Venereol. 84, 433-438. doi: 10.1080/00015550410016930
    • (2004) Acta Derm. Venereol. , vol.84 , pp. 433-438
    • Ryborg, A.K.1    Johansen, C.2    Iversen, L.3    Kragballe, K.4
  • 90
    • 2342457148 scopus 로고    scopus 로고
    • Differential modulation of endotoxin responsiveness by human caspase-12 polymorphisms
    • doi: 10.1038/nature02502.1
    • Saleh, M., Vaillancourt, J. P., Graham, R. K., and Huyck, M. (2004). Differential modulation of endotoxin responsiveness by human caspase-12 polymorphisms. Nature 429, 75-79. doi: 10.1038/nature02502.1
    • (2004) Nature , vol.429 , pp. 75-79
    • Saleh, M.1    Vaillancourt, J.P.2    Graham, R.K.3    Huyck, M.4
  • 91
    • 0642314384 scopus 로고    scopus 로고
    • Non-apoptotic functions of caspases in cellular proliferation and differentiation
    • doi: 10.1016/S0006-2952(03)00497-0
    • Schwerk, C., and Schulze-Osthoff, K. (2003). Non-apoptotic functions of caspases in cellular proliferation and differentiation. Biochem. Pharmacol. 66, 1453-1458. doi: 10.1016/S0006-2952(03)00497-0
    • (2003) Biochem. Pharmacol. , vol.66 , pp. 1453-1458
    • Schwerk, C.1    Schulze-Osthoff, K.2
  • 92
    • 0034651562 scopus 로고    scopus 로고
    • A new look at the origin, function, and "stem-cell" status of muscle satellite cells
    • doi: 10.1006/dbio.1999.9565
    • Seale, P., and Rudnicki, M. A. (2000). A new look at the origin, function, and "stem-cell" status of muscle satellite cells. Dev. Biol. 218, 115-124. doi: 10.1006/dbio.1999.9565
    • (2000) Dev. Biol. , vol.218 , pp. 115-124
    • Seale, P.1    Rudnicki, M.A.2
  • 93
    • 37549062115 scopus 로고    scopus 로고
    • Caspase-8 interacts with the p85 subunit of phosphatidylinositol 3-kinase to regulate cell adhesion and motility
    • doi: 10.1158/0008-5472.CAN-07-5755
    • Senft, J., Helfer, B., and Frisch, S. M. (2007). Caspase-8 interacts with the p85 subunit of phosphatidylinositol 3-kinase to regulate cell adhesion and motility. Cancer Res. 67, 11505-11509. doi: 10.1158/0008-5472.CAN-07-5755
    • (2007) Cancer Res. , vol.67 , pp. 11505-11509
    • Senft, J.1    Helfer, B.2    Frisch, S.M.3
  • 94
    • 0037114624 scopus 로고    scopus 로고
    • Specific involvement of caspases in the differentiation of monocytes into macrophages
    • doi: 10.1182/blood-2002-06-1778
    • Sordet, O., Rébé, C., Plenchette, S., Zermati, Y., Hermine, O., Vainchenker, W., et al. (2002). Specific involvement of caspases in the differentiation of monocytes into macrophages. Blood 100, 4446-4453. doi: 10.1182/blood-2002-06-1778
    • (2002) Blood , vol.100 , pp. 4446-4453
    • Sordet, O.1    Rébé, C.2    Plenchette, S.3    Zermati, Y.4    Hermine, O.5    Vainchenker, W.6
  • 95
    • 44649139105 scopus 로고    scopus 로고
    • Mutational analysis of caspase 1, 4, and 5 genes in common human cancers
    • doi: 10.1016/j.humpath.2007.10.015
    • Soung, Y. H., Jeong, E. G., Ahn, C. H., Kim, S. S., Song, S. Y., Yoo, N. J., et al. (2008). Mutational analysis of caspase 1, 4, and 5 genes in common human cancers. Hum. Pathol. 39, 895-900. doi: 10.1016/j.humpath.2007.10.015
    • (2008) Hum. Pathol. , vol.39 , pp. 895-900
    • Soung, Y.H.1    Jeong, E.G.2    Ahn, C.H.3    Kim, S.S.4    Song, S.Y.5    Yoo, N.J.6
  • 96
    • 0035253580 scopus 로고    scopus 로고
    • Transgenic mice expressing mutant caveolin-3 show severe myopathy associated with increased nNOS activity
    • doi: 10.1093/hmg/10.3.173
    • Sunada, Y., Ohi, H., Hase, A., Ohi, H., Hosono, T., Arata, S., et al. (2001). Transgenic mice expressing mutant caveolin-3 show severe myopathy associated with increased nNOS activity. Hum. Mol. Genet. 10, 173-178. doi: 10.1093/hmg/10.3.173
    • (2001) Hum. Mol. Genet. , vol.10 , pp. 173-178
    • Sunada, Y.1    Ohi, H.2    Hase, A.3    Ohi, H.4    Hosono, T.5    Arata, S.6
  • 97
    • 84877582384 scopus 로고    scopus 로고
    • Shaping organisms with apoptosis
    • doi: 10.1038/cdd.2013.11
    • Suzanne, M., and Steller, H. (2013). Shaping organisms with apoptosis. Cell Death Differ. 20, 669-675. doi: 10.1038/cdd.2013.11
    • (2013) Cell Death Differ. , vol.20 , pp. 669-675
    • Suzanne, M.1    Steller, H.2
  • 98
    • 77956095537 scopus 로고    scopus 로고
    • Mitochondria and cell death: outer membrane permeabilization and beyond
    • doi: 10.1038/nrm2952
    • Tait, S. W. G., and Green, D. R. (2010). Mitochondria and cell death: outer membrane permeabilization and beyond. Nat. Rev. Mol. Cell Biol. 11, 621-632. doi: 10.1038/nrm2952
    • (2010) Nat. Rev. Mol. Cell Biol. , vol.11 , pp. 621-632
    • Tait, S.W.G.1    Green, D.R.2
  • 99
    • 33645786318 scopus 로고    scopus 로고
    • Roles of caspase-8 and caspase-10 in innate immune responses to double-stranded RNA
    • Takahashi, K., Kawai, T., Kumar, H., Sato, S., Yonehara, S., and Akira, S. J. (2006). Roles of caspase-8 and caspase-10 in innate immune responses to double-stranded RNA. J. Immunol. 176, 4520-4524.
    • (2006) J. Immunol. , vol.176 , pp. 4520-4524
    • Takahashi, K.1    Kawai, T.2    Kumar, H.3    Sato, S.4    Yonehara, S.5    Akira, S.J.6
  • 100
    • 5044232017 scopus 로고    scopus 로고
    • Liver regeneration: from myth to mechanism
    • doi: 10.1038/nrm1489
    • Taub, R. (2004). Liver regeneration: from myth to mechanism. Nat. Rev. Mol. Cell Biol. 5, 836-847. doi: 10.1038/nrm1489
    • (2004) Nat. Rev. Mol. Cell Biol. , vol.5 , pp. 836-847
    • Taub, R.1
  • 101
    • 58149398634 scopus 로고    scopus 로고
    • CX3CL1/fractalkine is released from apoptotic lymphocytes to stimulate macrophage chemotaxis
    • doi: 10.1182/blood-2008-06-162404
    • Truman, L. A., Ford, C. A., Pasikowska, M., Pound, J. D., Wilkinson, S. J., Dumitriu, I. E., et al. (2008). CX3CL1/fractalkine is released from apoptotic lymphocytes to stimulate macrophage chemotaxis. Blood 112, 5026-5036. doi: 10.1182/blood-2008-06-162404
    • (2008) Blood , vol.112 , pp. 5026-5036
    • Truman, L.A.1    Ford, C.A.2    Pasikowska, M.3    Pound, J.D.4    Wilkinson, S.J.5    Dumitriu, I.E.6
  • 102
    • 33845602214 scopus 로고    scopus 로고
    • Apoptosis is required during early stages of tail regeneration in Xenopus laevis
    • doi: 10.1016/j.ydbio.2006.10.048
    • Tseng, A. S., Adams, D. S., Qiu, D., Koustubhan, P., and Levin, M. (2007). Apoptosis is required during early stages of tail regeneration in Xenopus laevis. Dev. Biol. 301, 62-69. doi: 10.1016/j.ydbio.2006.10.048
    • (2007) Dev. Biol. , vol.301 , pp. 62-69
    • Tseng, A.S.1    Adams, D.S.2    Qiu, D.3    Koustubhan, P.4    Levin, M.5
  • 103
    • 17444406677 scopus 로고    scopus 로고
    • Caspase-1 activity is required for neuronal differentiation of PC12 cells: cross-talk between the caspase and calpain systems
    • doi: 10.1016/j.bbamcr.2005.01.001
    • Vaisid, T., Kosower, N. S., and Barnoy, S. (2005). Caspase-1 activity is required for neuronal differentiation of PC12 cells: cross-talk between the caspase and calpain systems. Biochim. Biophys. Acta 1743, 223-230. doi: 10.1016/j.bbamcr.2005.01.001
    • (2005) Biochim. Biophys. Acta , vol.1743 , pp. 223-230
    • Vaisid, T.1    Kosower, N.S.2    Barnoy, S.3
  • 104
    • 5744221183 scopus 로고    scopus 로고
    • Growth and apoptosis during larval forelimb development and adult forelimb regeneration in the newt (Notophthalmus viridescens)
    • doi: 10.1007/s00427-004-0417-1
    • Vlaskalin, T., Wong, C. J., and Tsilfidis, C. (2004). Growth and apoptosis during larval forelimb development and adult forelimb regeneration in the newt (Notophthalmus viridescens). Dev. Genes Evol. 214, 423-431. doi: 10.1007/s00427-004-0417-1
    • (2004) Dev. Genes Evol. , vol.214 , pp. 423-431
    • Vlaskalin, T.1    Wong, C.J.2    Tsilfidis, C.3
  • 105
    • 20444498637 scopus 로고    scopus 로고
    • The canonical intrinsic mitochondrial death pathway has a non-apoptotic role in signaling lens cell differentiation
    • doi: 10.1074/jbc.M414270200
    • Weber, G. F., and Menko, A. S. (2005). The canonical intrinsic mitochondrial death pathway has a non-apoptotic role in signaling lens cell differentiation. J. Biol. Chem. 280, 22135-22145. doi: 10.1074/jbc.M414270200
    • (2005) J. Biol. Chem. , vol.280 , pp. 22135-22145
    • Weber, G.F.1    Menko, A.S.2
  • 106
    • 0033535607 scopus 로고    scopus 로고
    • Caspase activation in the terminal differentiation of human epidermal keratinocytes
    • doi: 10.1016/S0960-9822(99)80162-6
    • Weil, M., Raff, M. C., and Braga, V. M. (1999). Caspase activation in the terminal differentiation of human epidermal keratinocytes. Curr. Biol. 9, 361-364. doi: 10.1016/S0960-9822(99)80162-6
    • (1999) Curr. Biol. , vol.9 , pp. 361-364
    • Weil, M.1    Raff, M.C.2    Braga, V.M.3
  • 107
    • 84857650277 scopus 로고    scopus 로고
    • Fractalkine: a survivor's guide: chemokines as antiapoptotic mediators
    • doi: 10.1161/ATVBAHA.111.237412
    • White, G. E., and Greaves, D. R. (2012). Fractalkine: a survivor's guide: chemokines as antiapoptotic mediators. Arterioscler. Thromb. Vasc. Biol. 32, 589-594. doi: 10.1161/ATVBAHA.111.237412
    • (2012) Arterioscler. Thromb. Vasc. Biol. , vol.32 , pp. 589-594
    • White, G.E.1    Greaves, D.R.2
  • 108
    • 33749000311 scopus 로고    scopus 로고
    • Local caspase activity directs engulfment of dendrites during pruning
    • doi: 10.1038/nn1774
    • Williams, D. W., Kondo, S., Krzyzanowska, A., Hiromi, Y., and Truman, J. W. (2006). Local caspase activity directs engulfment of dendrites during pruning. Nat. Neurosci. 9, 1234-1236. doi: 10.1038/nn1774
    • (2006) Nat. Neurosci. , vol.9 , pp. 1234-1236
    • Williams, D.W.1    Kondo, S.2    Krzyzanowska, A.3    Hiromi, Y.4    Truman, J.W.5
  • 109
    • 0142092617 scopus 로고    scopus 로고
    • Caspase-3 regulates cell cycle in B cells: a consequence of substrate specificity
    • doi: 10.1038/ni976
    • Woo, M., Hakem, R., Furlonger, C., Hakem, A., Duncan, G. S., Sasaki, T., et al. (2003). Caspase-3 regulates cell cycle in B cells: a consequence of substrate specificity. Nat. Immunol. 4, 1016-1022. doi: 10.1038/ni976
    • (2003) Nat. Immunol. , vol.4 , pp. 1016-1022
    • Woo, M.1    Hakem, R.2    Furlonger, C.3    Hakem, A.4    Duncan, G.S.5    Sasaki, T.6
  • 110
    • 0035862331 scopus 로고    scopus 로고
    • Caspase activation is required for terminal erythroid differentiation
    • doi: 10.1084/jem.193.2.247
    • Zermati, Y., Garrido, C., Amsellem, S., Fishelson, S., Bouscary, D., Valensi, F., et al. (2001). Caspase activation is required for terminal erythroid differentiation. J. Exp. Med. 193, 247-254. doi: 10.1084/jem.193.2.247
    • (2001) J. Exp. Med. , vol.193 , pp. 247-254
    • Zermati, Y.1    Garrido, C.2    Amsellem, S.3    Fishelson, S.4    Bouscary, D.5    Valensi, F.6
  • 111
    • 0032546387 scopus 로고    scopus 로고
    • Fas-mediated apoptosis and activation-induced T-cell proliferation are defective in mice lacking FADD/Mort1
    • doi: 10.1038/32681
    • Zhang, J., Cado, D., Chen, A., Kabra, N., and Winoto, A. (1998). Fas-mediated apoptosis and activation-induced T-cell proliferation are defective in mice lacking FADD/Mort1. Nature 392, 296-300. doi: 10.1038/32681
    • (1998) Nature , vol.392 , pp. 296-300
    • Zhang, J.1    Cado, D.2    Chen, A.3    Kabra, N.4    Winoto, A.5
  • 112
    • 0035839640 scopus 로고    scopus 로고
    • FADD-deficient T cells exhibit a disaccord in regulation of the cell cycle machinery
    • doi: 10.1074/jbc.M103838200
    • Zhang, J., Kabra, N. H., Cado, D., Kang, C., and Winoto, A. (2001). FADD-deficient T cells exhibit a disaccord in regulation of the cell cycle machinery. J. Biol. Chem. 276, 29815-29818. doi: 10.1074/jbc.M103838200
    • (2001) J. Biol. Chem. , vol.276 , pp. 29815-29818
    • Zhang, J.1    Kabra, N.H.2    Cado, D.3    Kang, C.4    Winoto, A.5


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