Caspases - An update

Comparative Biochemistry and Physiology - B Biochemistry and Molecular Biology

Volumn 151, Issue 1, 2008, Pages 10-27

  Chowdhury, Indrajit ^a   Tharakan, Binu ^b   Bhat, Ganapathy K ^a  

^a MOREHOUSE SCHOOL OF MEDICINE   (United States)

^b TEXAS A M COLLEGE OF MEDICINE   (United States)

Author keywords

Apoptosis; Apoptosome; Caspase; Inflammasome; Programmed cell death

Indexed keywords

APOPTOSOME; CALCIUM ION; CALPAIN; CASPASE; CASPASE 5; FLICE INHIBITORY PROTEIN; GRANZYME B; INHIBITOR OF APOPTOSIS PROTEIN; INTERLEUKIN 1BETA CONVERTING ENZYME; PROCASPASE 9; PROTEINASE;

APOPTOSIS; CELL DEATH; CELL DIFFERENTIATION; CELL PROLIFERATION; CYTOKINE RELEASE; ENZYME ACTIVATION; ENZYME SPECIFICITY; ENZYME STRUCTURE; ENZYME SUBSTRATE; IMMUNE FUNCTION TEST; IMMUNITY; INFLAMMATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEGRADATION; REVIEW; SIGNAL TRANSDUCTION;

MAMMALIA;

EID: 47949120317     PISSN: 10964959     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cbpb.2008.05.010     Document Type: Review

References (263)

1. Aballay A., and Ausubel F.M. Programmed cell death mediated by ced-3 and ced-4 protects Caenorhabditis elegans from Salmonella typhimurium mediated killing. Proc. Natl. Acad. Sci. USA 98 (2001) 2735-2739
2. Acehan D., Jiang X., Morgan D.G., Heuser J.E., Wang X., and Akey C.W. Three-dimensional structure of the apoptosome. Implications for assembly, procaspase-9 binding, and activation. Mol Cell 9 (2002) 423-432
3. Ahmad M., Srinivasula S.M., Wang L., Litwack G., Fernandes-Alnemri T., and Alnemri E.S. Spodoptera frugiperda caspase-1, a novel insect death protease that cleaves the nuclear immunophilin FKBP46, is the target of the baculovirus antiapoptotic protein p35. J. Biol. Chem. 272 (1997) 1421-1424
4. Alnemri E.S., Livingston D.J., Nicholson D.W., Salvesen G., Thornberry N.A., Wong W.W., and Yuan J. Human ICE/CED-3 protease nomenclature [letter]. Cell. 87 (1996) 171
5. Aravind L., Dixit V.M., and Koonin E.V. The domains of death: evolution of the apoptosis machinery. Trends Biochem. Sci. 24 (1999) 47-53
6. Aravind L., and Koonin E.V. Classification of the caspase-hemoglobinase fold: detection of new families and implications for the origin of the eukaryotic separins. Proteins: Struct. Funct. Genet. 46 (2002) 355-367
7. Ashkenazi A., and Dixit V.M. Death receptors: signaling and modulation. Science 281 (1998) 1305-1308
8. Baliga B.C., Read S.H., and Kumar S. The biochemical mechanism of caspase-2 activation. Cell Death Differ. 11 (2004) 1234-1241
9. Barrett A.J., and Rawlings N.D. Evolutionary lines of cysteine peptidases. Biol. Chem. 382 (2001) 727-733
10. Barry M., Heibein J.A., Pinkoski M.J., Lee S.F., Moyer R.W., Green D.R., and Bleackley R.C. Granzyme B short-circuits the need for caspase 8 activity during granule mediated cytotoxic T-lymphocyte killing by directly cleaving Bid. Mol. Cell Biol. 20 (2000) 3781-3794
11. Bayascas J.R., Yuste V.J., Benito E., Garcia-Fernandez J., and Comella J.X. Isolation of AmphiCASP-3/7, an ancestral caspase from amphioxus (Branchiostoma floridae). Evolutionary considerations for vertebrate caspases. Cell Death Differ. 9 (2002) 1078-1089
12. Becker J.W., Rotonda J., Soisson S.M., Aspiotis R., Bayly C., Francoeur S., Gallant M., Garcia-Calvo M., Giroux A., Grimm E., Han Y., McKay D., Nicholson D.W., Peterson E., Renaud J., Roy S., Thornberry N., and Zamboni R. Reducing the peptidyl features of caspase-3 inhibitors: a structural analysis. J. Med. Chem. 47 (2004) 2466-2474
13. Beisner D.R., Chen I.L., Kolla R.V., Hoffmann A., and Hedrick S.M. Cutting edge: innate immunity conferred by B cells is regulated by caspase-8. J. Immunol. 175 (2005) 3469-3473
14. Birnbaum M.J., Clem R.J., and Miller L.K. An apoptosis-inhibiting gene from a nuclear polyhedrosis virus encoding a polypeptide with Cys/His sequence motifs. J. Virol. 68 (1994) 2521-2528
15. Black R.A., Kronheim S.R., and Sleath P.R. Activation of interleukin-1β by a co-induced protease. FEBS Lett. 247 (1989) 386-390
16. Black S., Kadyrov M., Kaufmann P., Ugele B., Emans N., and Huppertz B. Syncytial fusion of human trophoblast depends on caspase 8. Cell Death Differ. 11 (2004) 90-98
17. Blanchard H., Donepudi M., Tschopp M., Kodandapani L., Wu J.C., and Grütter M.G. Caspase-8 specificity probed at sub site S (4): crystal structure of the caspase-8-Z-DEVD-cho complex. J. Mol. Biol. 302 (2000) 9-16
18. Blanchard H., Kodandapani L., Mittl P.R., Marco S.D., Krebs J.F., Wu J.C., Tomaselli K.J., and Grütter M.G. The three-dimensional structure of caspase-8: an initiator enzyme in apoptosis. Structure 7 (1999) 1125-1133
19. Blomgren K., Zhu C.L., Wang X.Y., Karlsson J.O., Leverin A.L., Bahr B.A., Mallard C., and Hagberg H. Synergistic activation of caspase-3 by m-calpain after neonatal hypoxia-ischemia. J. Biol. Chem. 276 (2001) 10191-10198
20. Boatright K.M., Renatus M., Scott F.L., Sperandio S., Shin H., Pedersen I.M., Ricci J.E., Edris W.A., Sutherlin D.P., Green D.R., and Salvesen G.S. A unified model for apical caspase activation. Mol. Cell. 11 (2003) 529-541
21. Boldin M.P., Goncharov T.M., Goltsev Y.V., and Wallach D. Involvement of MACH, a novel Mort1/FADD-interacting protease, in Fas/APO1- and TNF receptor-induced cell death. Cell 85 (1996) 803-815
22. Boyce M., Degterev A., and Yuan J. Caspases: an ancient cellular sword of Damocles. Cell Death Differ. 11 (2004) 29-37
23. Bozhkov P.V., Filonova L.H., Suarez M.F., Helmersson A., Smertenko A.P., Zhivotovsky B., and von Arnold S. VEIDase is a principal caspase-like activity involved in plant programmed cell death and essential for embryonic pattern formation. Cell Death Differ. 11 (2004) 175-182
24. Butt A.J., Harvey N.L., Parasivam G., and Kumar S. Dimerization and autoprocessing of the Nedd2(caspase-2) precursor requires both the prodomain and the carboxyl-terminal regions. J. Biol. Chem. 273 (1998) 6763-6768
25. Cerretti D.P., Kozlosky C.J., Mosley B., Nelson N., Van Ness K., Greenstreet T.A., March C.J., Kronheim S.R., Druck T., and Cannizzaro L.A. Molecular cloning of the interleukin-1 beta converting enzyme. Science 256 (1992) 97-100
26. Chai J., Wu Q., Shiozaki E., Srinivasula S.M., Alnemri E.S., and Shi Y. Crystal structure of a procaspase-7 zymogen: mechanisms of activation and substrate binding. Cell 107 (2001) 399-407
27. Chai J., Shiozaki E., Srinivasula M., Wu Q., Datta P., Alnemri E.S., and Shi Y. Structural basis of caspase-7 inhibition by XIAP. Cell 104 (2001) 769-780
28. Chakraborty C., Nandi S.S., Sinha S., and Gera V.K. Zebrafish caspase-3: molecular cloning, characterization, crystallization and phylogenetic analysis. Protein Pept Lett. 13 (2006) 633-640
29. Chang D.W., Xing Z., Capacio V.L., Peter M.E., and Yang X. Interdimer processing mechanism of procaspase-8 activation. EMBO J. 22 (2003) 4132-4142
30. Chang D.W., Xing Z., Pan Y., Algeciras-Schimnich A., Barnhart B.C., Yaish-Ohad S., Peter M.E., and Yang X. c-FLIP(L) is a dual function regulator for caspase-8 activation and CD95-mediated apoptosis. EMBO J. 21 (2002) 3704-3714
31. Chen J.M., Rawlings N.D., Stevens R.A., and Barrett A.J. Identification of the active site of legumain links it to caspases, clostripain and gingipains in a new clan of cysteine endopeptidases. FEBS Lett. 441 (1998) 361-365
32. Cheng E.H., Levine B., Boise L.H., Thompson C.B., and Hardwick J.M. Bax-independent inhibition of apoptosis by Bcl-XL. Nature. 379 (1996) 554-556
33. Cheng J., Park T.S., Chio L.C., Fischl A.S., and Ye X.S. Induction of apoptosis by sphingoid long-chain bases in Aspergillus nidulans. Mol. Cell. Biol. 23 (2003) 163-177
34. Chéreau D., Kodandapani L., Tomaselli K.J., Spada A.P., and Wu J.C. Structural and functional analysis of caspase active sites. Biochemistry. 42 (2003) 4151-4160
35. Chinnaiyan A.M. The apoptosome: heart and soul of the cell death machine. Neoplasia 1 (1999) 5-15
36. Chowdhury I., Tharakan B., and Bhat G.K. Current concepts in apoptosis: the physiological suicide program revisited. Cell Mol. Biol. Lett. 11 (2006) 506-525
37. Chun H.J., Zheng L., Ahmad M., Wang J., Speirs C.K., Siegel R.M., Dale J.K., Puck J., Davis J., Hall C.G., Skoda-Smith S., Atkinson T.P., Straus S.E., and Lenardo M.J. Pleiotropic defects in lymphocyte activation caused by caspase-8 mutations lead to human immunodeficiency. Nature 419 (2002) 395-399
38. Cikala M., Wilm B., Hobmayer E., Bottger A., and David C.N. Identification of caspases and apoptosis in the simple metazoan Hydra. Curr. Biol. 9 (1999) 959-962
39. Coffeen W.C., and Wolpert T.J. Purification and characterization of serine proteases that exhibit caspase-like activity and are associated with programmed cell death in Avena sativa. Plant Cell 16 (2004) 857-873
40. Cohen G.M. Caspases: the executioners of apoptosis. Biochem. J. 326 (1997) 1-16
41. Colussi P.A., Harvey N.L., and Kumar S. Prodomain-dependent nuclear localization of the caspase-2(Nedd2) precursor. J. Biol. Chem. 273 (1998) 24535-24542
42. Costantini P., Bruey J.M., Castedo M., Métivier D., Loeffler M., Susin S.A., Ravagnan L., Zamzami N., Garrido C., and Kroemer G. Pre-processed caspase-9 contained in mitochondria participates in apoptosis. Cell Death Differ. 9 (2002) 82-88
43. Creagh E.M., and Martin S.J. Caspases: cellular demolition experts. Biochem. Soc. Trans. 29 (2001) 696-702
44. Dahm R. Lens fibre cell differentiation - a link with apoptosis?. Ophthalmic Res. 31 (1999) 163-183
45. Darmon A.J., Nicholson D.W., and Bleackley R.C. Activation of the apoptotic protease CPP32 by cytotoxic T-cell derived granzyme B. Nature 377 (1995) 446-448
46. De Botton S., Sabri S., Daugas E., Zermati Y., Guidotti J.E., Hermine O., Kroemer G., Vainchenker W., and Debili N. Platelet formation is the consequence of caspase activation within megakaryocytes. Blood 100 (2002) 1310-1317
47. Degterev A., Boyce M., and Yuan J. A decade of caspases. Oncogene 22 (2003) 8543-8567
48. Denault J.B., and Salvesen G.S. Caspases: keys in the ignition of cell death. Chem. Rev. 102 (2002) 4489-4500
49. Deveraux Q.L., Takahashi R., Salvesen G.S., and Reed J.C. X-linked IAP is a direct inhibitor of cell-death proteases. Nature 388 (1997) 300-304
50. Deveraux Q.L., Roy N., Stennicke H.R., Van Arsdale T., Zhou Q., Srinivasula S.M., Alnemri E.S., Salvesen G.S., and Reed J.C. IAPs block apoptotic events induced by caspase-8 and Cytochrome C by direct inhibition of distinct caspases. EMBO J. 17 (1998) 2215-2223
51. Deveraux Q.L., and Reed J.C. IAP family proteins: suppressors of apoptosis. Genes Dev. 13 (1999) 239-252
52. Dietrich R.A., Richberg M.H., Schmidt R., Dean C., and Dangl J.L. A novel zinc finger protein is encoded by the Arabidopsis LSD1 gene and functions as a negative regulator of plant cell death. Cell 88 (1997) 685-694
53. Dorstyn L., Read S.H., Quinn L.M., Richardson H., and Kumar S. DECAY, a novel Drosophila caspase related to mammalian caspase-3 and caspase-7. J. Biol. Chem. 274 (1999) 30778-30783
54. Dorstyn L., Read S., Cakouros D., Huh J.R., Hay B.A., and Kumar S. The role of Cytochrome C in caspase activation in Drosophila melanogaster cells. J. Cell Biol. 156 (2002) 1089-1098
55. dos Santos N.M., do Vale A., Reis M.I., and Silva M.T. Fish and apoptosis: molecules and pathways. Curr. Pharm. Des. 14 (2008) 148-169
56. Droin N., Bichat F., Rebe C., Wotawa A., Sordet O., Hammann A., Bertrand R., and Solary E. Involvement of caspase-2 long isoform in Fas-mediated cell death of human leukemic cells. Blood 97 (2001) 1835-1844
57. Earnshaw W.C., Martins L.M., and Kaufmann S.H. Mammalian caspases: structure, activation, substrates, and functions during apoptosis. Annu. Rev. Biochem. 68 (1999) 383-424
58. Eberstadt M., Huang B., Chen Z., Meadows R.P., Ng S.C., Zheng L., Lenardo M.J., and Fesik S.W. NMR structure and mutagenesis of the FADD (Mort1) death-effector domain. Nature 392 (1998) 941-945
59. Eckhart L., Ballaun C., Uthman A., Kittel C., Stichenwirth M., Buchberger M., Fischer H., Sipos W., and Tschachler E. Identification and characterization of a novel mammalian caspase with proapoptotic activity. J. Biol. Chem. 280 (2005) 35077-35080
60. Eichinger A., Beisel H.G., Jacob U., Huber R., Medrano F.J., Banbula A., Potempa J., Travis J., and Bode W. Crystal structure of gingipain R: an Arg-specific bacterial cysteine proteinase with a caspase-like fold. EMBO J. 18 (1999) 5453-5462
61. Eimon P.M., Kratz E., Varfolomeev E., Hymowitz S.G., Stern H., Zha J., and Ashkenazi A. Delineation of the cell-extrinsic apoptosis pathway in the zebrafish. Cell Death Differ. 13 (2006) 1619-1630
62. Ellis H.M., and Horvitz H.R. Genetic control of programmed cell death in the nematode C. elegans. Cell 44 (1986) 817-829
63. Enari M., Sakahira H., Yokoyama H., Okawa K., Iwamatsu A., and Nagata S. A caspase-activated DNase that degrades DNA during apoptosis, and its inhibitor ICAD. Nature 391 (1998) 43-50
64. Fan T.J., Xia L., and Han Y.R. Mitochondrion and apoptosis. Acta Biochim. Biophys. Sin (Shanghai) 33 (2001) 7-12
65. Fan T.J., Han L.H., Cong R.S., and Liang J. Caspase family proteases and apoptosis. Acta Biochim. Biophys. Sin (Shanghai). 37 (2005) 719-727
66. Fernando P., Brunette S., and Megeney L.A. Neural stem cell differentiation is dependent upon endogenous caspase 3 activity. FASEB J. 19 (2005) 1671-1673
67. Fernando P., Kelly J.F., Balazsi K., Slack R.S., and Megeney L.A. Caspase-3 activity is required for skeletal muscle differentiation. Proc. Natl. Acad. Sci. USA 99 (2002) 11025-11030
68. Ferri K.F., and Kroemer G. Organelle-specific initiation of cell death pathways. Nat. Cell Biol. 3 (2001) E255-263
69. Fesik S.W. Insights into programmed cell death through structural biology. Cell 103 (2000) 273-282
70. Finkel E. The mitochondrion: Is it central to apoptosis?. Science 292 (2001) 624-626
71. Fischer U., Jänicke R.U., and Schulze-Osthoff K. Many cuts to ruin: a comprehensive update of caspase substrates. Cell Death Differ. 10 (2003) 76-100
72. Fraser A.G., and Evan G.I. Identification of a Drosophila melanogaster ICE/CED-3-related protease, drICE. EMBO J. 16 (1997) 2805-2813
73. Fraser A.G., McCarthy N.J., and Evan G.I. drICE is an essential caspase required for apoptotic activity in Drosophila cells. EMBO J. 16 (1997) 6192-6199
74. Frost V., Al-Mehairi S., and Sinclair A.J. Exploitation of a non-apoptotic caspase to regulate the abundance of the cdkI p27 (KIP1) in transformed lymphoid cells. Oncogene 20 (2001) 2737-2748
75. Frost V., Delikat S., Al-Mehairi S., and Sinclair A.J. Regulation of p27KIP1 in Epstein-Barr virus immortalized lymphoblastoid cell lines involves non-apoptotic caspase cleavage. J. Gen. Virol. 82 (2001) 3057-3066
76. Fuentes-Prior P., and Salvesen G.S. The protein structures that shape caspase activity, specificity, activation and inhibition. Biochem. J. 384 (2004) 201-232
77. Georgel P., Naitza S., Kappler C., Ferrandon D., Zachary D., Swimmer C., Kopczynski C., Duyk G., Reichhart J.M., and Hoffmann J.A. Drosophila immune deficiency (IMD) is a death domain protein that activates antibacterial defense and can promote apoptosis. Dev Cell. 1 (2001) 503-514
78. Golks A., Brenner D., Fritsch C., Krammer P.H., and Lavrik I.N. C-FLIPR: a new regulator of death receptor-induced apoptosis. J. Biol. Chem. 280 (2005) 14507-14513
79. González I.J., Desponds C., Schaff C., Mottram J.C., and Fasel N. Leishmania major metacaspase can replace yeast metacaspase in programmed cell death and has arginine-specific cysteine peptidase activity. Int. J. Parasitol. 37 (2007) 161-172
80. Gross A., McDonnell J.M., and Korsmeyer S.J. BCL-2 family members and the mitochondria in apoptosis. Genes Dev. 13 (1999) 1899-1911
81. Grütter M.G. Caspases: key players in programmed cell death. Curr. Opin. Struct. Biol. 10 (2000) 649-655
82. Guo Y., Srinivasula S.M., Druilhe A., Fernandes-Alnemri T., and Alnemri E.S. Caspase-2 induces apoptosis by releasing proapoptotic proteins from mitochondria. J. Biol. Chem. 277 (2002) 13430-13437
83. Gurcel L., Abrami L., Girardin S., Tschopp J., and van der Goot F.G. Caspase-1 activation of lipid metabolic pathways in response to bacterial pore-forming toxins promotes cell survival. Cell 126 (2006) 1135-1145
84. Hara-Nishimura I., Hatsugai N., Nakaune S., Kuroyanagi M., and Nishimura M. Vacuolar processing enzyme: an executor of plant cell death. Curr. Opin. Plant Biol. 8 (2005) 404-408
85. Hatsugai N., Kuroyanagi M., Nishimura M., and Hara-Nishimura I. A cellular suicide strategy of plants: vacuole-mediated cell death. Apoptosis 11 (2006) 905-911
86. Hawkins C.J., Wang S.L., and Hay B.A. A cloning method to identify caspases and their regulators in yeast: identification of Drosophila IAP1 as an inhibitor of the Drosophila caspase DCP-1. Proc. Natl. Acad. Sci. USA. 96 (1999) 2885-2890
87. Hawkins C.J., Yoo S.J., Peterson E.P., Wang S.L., Vernooy S.Y., and Hay B.A. The Drosophila caspase DRONC cleaves following glutamate or aspartate and is regulated by DIAP1, HID and GRIM. J. Biol. Chem. 275 (2000) 27084-27093
88. Heibein J.A., Goping I.S., Barry M., Pinkoski M.J., Shore G.C., Green D.R., and Bleackley R.C. Granzyme B-mediated Cytochrome C release is regulated by the Bcl-2 family members bid and Bax. J. Exp. Med. 192 (2000) 1391-1402
89. Hengartner M.O. Programmed cell death in the nematode C. elegans [review]. Recent Prog.Horm. Res. 54 (1999) 213-222
90. Hofmann K. The modular nature of apoptotic signaling proteins. Cell Mol. Life Sci. 55 (1999) 1113-1128
91. Hu Y., Ding L., Spencer D.M., and Nunez G. WD-40 repeat region regulates Apaf-1 self-association and procaspase-9 activation. J. Biol. Chem. 273 (1998) 33489-33494
92. Huang Y., Park Y.C., Rich R.L., Segal D., Myszka D.G., and Wu H. Structural basis of caspase inhibition by XIAP: differential roles of the linker versus the BIR domain. Cell 104 (2001) 781-790
93. Inohara N., Koseki T., Hu Y., Chen S., and Núñez G. CLARP, a death effector domain-containing protein interacts with caspase-8 and regulates apoptosis. Proc. Natl. Acad. Sci. USA. 94 (1997) 10717-10722
94. Inohara N., and Nunez G. Gene with homology to mammalian apoptosis regulators identified in zebrafish. Cell Death Differ. 7 (2000) 509-510
95. Irmler M., Thome M., Hahne M., Schneider P., Hofmann K., Steiner V., Bodmer J.L., Schröter M., Burns K., Mattmann C., Rimoldi D., French L.E., and Tschopp J. Inhibition of death receptor signals by cellular FLIP. Nature 388 (1997) 190-195
96. Jiang X., and Wang X. Cytochrome c promotes caspase-9 activation by inducing nucleotide binding to Apaf-1. J. Biol. Chem. 275 (2000) 31199-31203
97. Johnson A.L., and Bridgham J.T. Caspase-mediated apoptosis in the vertebrate ovary. Reproduction 124 (2002) 19-27
98. Johnson C.R., and Jarvis W.D. Caspase-9 regulation: an update. Apoptosis 9 (2004) 423-427
99. Kang T.B., Ben-Moshe T., Varfolomeev E.E., Pewzner-Jung Y., Yogev N., Jurewicz A., Waisman A., Brenner O., Haffner R., Gustafsson E., Ramakrishnan P., Lapidot T., and Wallach D. Caspase-8 serves both apoptotic and nonapoptotic roles. J. Immunol. 173 (2004) 2976-2984
100. Kaufman R.J. Stress signaling from the lumen of the endoplasmic reticulam: coordination of gene transcriptional and translational controls. Gene Dev. 13 (1999) 1211-1233
101. Kischkel F.C., Hellbardt S., Behrmann I., Germer M., Pawlita M., Krammer P.H., and Peter M.E. Cytotoxicity-dependent APO-1 (Fas/CD95)-associated proteins form a death-inducing signaling complex (DISC) with the receptor. EMBO J. 14 (1995) 5579-5588
102. Kischkel F.C., Lawrence D.A., Tinel A., LeBlanc H., Virmani A., Schow P., Gazdar A., Blenis J., Arnott D., and Ashkenazi A. Death receptor recruitment of endogenous caspase-10 and apoptosis initiation in the absence of caspase-8. J Biol Chem 276 (2001) 46639-46646
103. Koonin E.V., and Aravind L. Origin and evolution of eukaryotic apoptosis: the bacterial connection. Cell Death Differ. 9 (2002) 394-404
104. Korsmeyer S.J., Wei M.C., Saito M., Weiler S., Oh K.J., and Schlesinger P.H. Pro-apoptotic cascade activates BID, which oligomerizes BAK or BAX into pores that result in the release of Cytochrome C. Cell Death Differ. 7 (2000) 1166-1173
105. Kosec G., Alvarez V.E., Agüero F., Sánchez D., Dolinar M., Turk B., Turk V., and Cazzulo J.J. Metacaspases of Trypanosoma cruzi: possible candidates for programmed cell death mediators. Mol. Biochem. Parasitol. 145 (2006) 18-28
106. Kostura M.J., Tocci M.J., Limjuco G., Chin J., Cameron P., Hillman A.G., Chartrain N.A., and Schmidt J.A. Identification of a monocyte specific pre-interleukin1β convertase activity. Proc. Natl. Acad. Sci. USA 86 (1989) 5227-5231
107. Krammer P.H. The CD95(APO-1/Fas)/CD95L system [review]. Toxicol. Lett. 102-103 (1998) 131-137
108. Kratz E., Eimon P.M., Mukhyala K., Stern H., Zha J., Strasser A., Hart R., and Ashkenazi A. Functional characterization of the Bcl-2 gene family in the zebrafish. Cell Death Differ. 13 (2006) 1631-1640
109. Krueger A., Schmitz I., Baumann S., Krammer P.H., and Kirchhoff S. Cellular flice-inhibitory protein splice variants inhibit different steps of caspase-8 activation at the cd95 death-inducing complex. J. Biol. Chem.. 276 (2001) 20633-20640
110. Kuida K., Lippke J.A., Ku G., Harding M.W., Livingston D.J., Su M.S., and Flavell R.A. Altered cytokine export and apoptosis in mice deficient in interleukin-1β converting enzyme. Science 267 (1995) 2000-2003
111. Kuida K., Zheng T.S., Na S., Kuan C., Yang D., Karasuyama H., Rakic P., and Flavell R.A. Decreased apoptosis in the brain and premature lethality in CPP32-deficient mice. Nature 384 (1996) 368-372
112. Kumar S. Caspase function in programmed cell death. Cell Death Differ. 14 (2007) 32-43
113. Kumar S., and Vaux D.L. Apoptosis. A cinderella caspase takes center stage. Science 297 (2002) 1290-1291
114. Kuranaga E., and Miura M. Non-apoptotic functions of caspases: caspases as regulatory molecules for immunity and cell-fate determination. Trends Cell Biol. 17 (2007) 135-144
115. Kuwana T., Mackey M.R., Perkins G., Ellisman M.H., Latterich M., Schneiter R., Green D.R., and Newmeyer D.D. Bid, bax, and lipids cooperate to form supramolecular openings in the outer mitochondrial membrane. Cell 111 (2002) 331-342
116. Laing K.J., Holland J., Bonilla S., Cunningham C., and Secombes C.J. Cloning and sequencing of caspase 6 in rainbow trout, Oncorhynchus mykiss, and analysis of its expression under conditions known to induce apoptosis. Dev. Comp. Immunol. 25 (2001) 303-312
117. Lakhani S.A., Masud A., Kuida K., Porter Jr. G.A., Booth C.J., Mehal W.Z., Inayat I., and Flavell R.A. Caspases 3 and 7: key mediators of mitochondrial events of apoptosis. Science 311 (2006) 847-851
118. Lamkanfi M., Declercq W., Kalai M., Saelens X., and Vandenabeele P. Alice in caspase land. A phylogenetic analysis of caspases from worm to man. Cell Death Differ. 9 (2002) 358-361
119. Lamkanfi M., D'hondt K., Vande Walle L., van Gurp M., Denecker G., Demeulemeester J., Kalai M., Declercq W., Saelens X., and Vandenabeele P. A novel caspase-2 complex containing TRAF2 and RIP1. J. Biol. Chem. 280 (2005) 6923-6932
120. Lamkanfi M., Declercq W., Vanden Berghe T., and Vandenabeele P. Caspases leave the beaten track: caspase-mediated activation of NF-kappa B. J. Cell Biol. 173 (2006) 165-171
121. Lamkanfi M., Festjens N., Declercq W., Vanden Berghe T., and Vandenabeele P. Caspases in cell survival, proliferation and differentiation. Cell Death Differ. 14 (2007) 44-55
122. Lassus P., Opitz-Araya X., and Lazebnik Y. Requirement for caspase-2 in stress induced apoptosis before mitochondrial permeabilization. Science 297 (2002) 1352-1354
123. Launay S., Hermine O., Fontenay M., Kroemer G., Solary E., and Garrido C. Vital functions for lethal caspases. Oncogene 24 (2005) 5137-5148
124. Lavrik I., Golks A., and Krammer P.H. Caspases: pharmacological manipulation of cell death. J. Clin. Invest. 115 (2005) 2665-2672
125. Lavrik I., Krueger A., Schmitz I., Baumann S., Weyd H., Krammer P.H., and Kirchhoff S. The active caspase-8 heterotetramer is formed at the CD95 DISC. Cell Death Differ. 10 (2003) 144-145
126. Le Chat L., Sinden R.E., and Dessens J.T. The role of metacaspase 1 in Plasmodium berghei development and apoptosis. Mol. Biochem. Parasitol. 15 (2007) 41-47
127. Li H., Zhu H., Xu C.J., and Yuan J. Clevage of BID by caspase 8 mediates the mitochondrial damage in the Fas pathway of apoptosis. Cell 94 (1998) 491-501
128. Li P., Allen H., Banerjee S., Franklin S., Herzog L., Johnston C., McDowell J., Paskind M., Rodman L., and Salfeld J. Mice deficiency in IL-1β converting enzyme are defective in production of mature IL-1β and resistant to endotoxic shock. Cell 80 (1995) 401-411
129. Li P., Nijhawan D., Budihardjo I., Srinivasula S.M., Ahmad M., Alnemri E.S., and Wang X. Cytochrome C and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade. Cell 91 (1997) 479-489
130. Liu X.S., Zou H., Slaughter C., and Wang X. DFF, a heterodimeric protein that functions downstream of caspase-3 to trigger DNA fragmentation during apoptosis. Cell 89 (1997) 175-184
131. Long S., Wilson M., Bengtén E., Clem L.W., Miller N.W., and Chinchar V.G. Identification and characterization of a FasL-like protein and cDNAs encoding the channel catfish death-inducing signaling complex. Immunogenetics. 56 (2004) 518-530
132. Lopez-Castejon G., Pilar Sepulcre M., Mulero I., Pelegrin P., Meseguer J., and Mulero V. Molecular and functional characterization of gilthead seabream Sparus aurata caspase-1: the first identification of an inflammatory caspase in fish. Mol. Immunol. 45 (2008) 49-57
133. Lü C.X., Fan T.J., Hu G.B., and Cong R.S. Apoptosis-inducing factor and apoptosis. Acta Biochim. Biophys. Sin. 35 (2003) 881-885
134. Luo X., Budihardjo I., Zou H., Slaughter C., and Wang X. Bid, a Bcl2 interacting protein, mediates Cytochrome C release from mitochondria in response to activation of cell surface death receptors. Cell 94 (1998) 481-490
135. Madeo F., Herker E., Maldener C., Wissing S., Lachelt S., Herlan M., Fehr M., Lauber K., Sigrist S.J., Wesselborg S., and Frohlich K.U. A caspase-related protease regulates apoptosis in yeast. Mol. Cell 9 (2002) 911-917
136. Mancini M., Machamer C.E., Roy S., Nicholson D.W., Thornberry N.A., Casciola-Rosen L.A., and Rosen A. Caspase-2 is localized at the Golgi complex and cleaves golgin-160 during apoptosis. J Cell Biol 149 (2000) 603-612
137. Mandic A., Hansson J., Linder S., and Shoshan M.C. Cisplatin induces ER stress and nucleus-independent apoptotic signaling. J. Biol. Chem. 278 (2003) 9100-9106
138. Mariathasan S., Newton K., Monack D.M., Vucic D., French D.M., Lee W.P., Roose-Girma M., Erickson S., and Dixit V.M. Differential activation of the inflammasome by caspase-1 adaptors ASC and Ipaf. Nature 430 (2004) 237-241
139. Mariathasan S., Weiss D.S., Newton K., McBride J., O'Rourke K., Roose-Girma M., Lee W.P., Weinrauch Y., Monack D.M., and Dixit V.M. Cryopyrin activates the inflammasome in response to toxins and ATP. Nature 440 (2006) 228-232
140. Martin D.A., Siegel R.M., Zheng L., and Lenardo M.J. Membrane oligomerization and cleavage activates the caspase-8 (FLICE/MACHalpha1) death signal. J. Biol. Chem. 273 (1998) 4345-4349
141. Martinon F., Hofmann K., and Tschopp J. The pyrin domain: a possible member of the death domain-fold family implicated in apoptosis and inflammation. Curr. Biol. 11 (2001) R118-R120
142. Martinon F., and Tschopp J. Inflammatory caspases: linking an intracellular innate immune system to autoinflammatory diseases. Cell 117 (2004) 561-574
143. Martinon F., Pétrilli V., Mayor A., Tardivel A., and Tschopp J. Gout-associated uric acid crystals activate the NALP3 inflammasome. Nature 440 (2006) 237-241
144. Masumoto J., Zhou W., Chen F.F., Su F., Kuwada J.Y., Hidaka E., Katsuyama T., Sagara J., Taniguchi S., Ngo-Hazelett P., Postlethwait J.H., Núñez G., and Inohara N. Caspy, a zebrafish caspase, activated by ASC oligomerization is required for pharyngeal arch development. J. Biol. Chem. 278 (2003) 4268-4276
145. Meier P., Silke J., Leevers S.J., and Evan G.I. The Drosophila caspase DRONC is regulated by DIAP1. EMBO J. 19 (2000) 598-611
146. Micheau O., Thome M., Schneider P., Holler N., Tschopp J., Nicholson D.W., Brand C., and Grutter M.G. The long form of FLIP is an activator of caspase-8 at the Fas death-inducing signaling complex. J Biol Chem 277 (2002) 45162-45171
147. Milan M., Campuzano S., and García-Bellido A. Developmental parameters of cell death in the wing disc of Drosophila. Proc. Natl. Acad Sci USA 94 (1997) 5691-5696
148. Milhas D., Cuvillier O., Therville N., Clave P., Thomsen M., Levade T., Benoist H., and Ségui B. Caspase-10 triggers Bid cleavage and caspase cascade activation in FasL-induced apoptosis. J. Biol. Chem. 280 (2005) 19836-19842
149. Miller L.K. An exegesis of IAPs: salvation and surprises from BIR motifs. Trends Cell Biol. 9 (1999) 323-328
150. Mittl P.R., Di Marco S., Krebs J.F., Bai X., Karanewsky D.S., Priestle J.P., Tomaselli K.J., and Grütter M.G. Structure of recombinant human CPP32 in complex with the tetrapeptide acetyl-Asp-Val-Ala-Asp fluoromethyl ketone. J. Biol. Chem. 272 (1997) 6539-6547
151. Miura M., Chen X.D., Allen M.R., Bi Y., Gronthos S., Seo B.M., Lakhani S., Flavell R.A., Feng X.H., Robey P.G., Young M., and Shi S. A crucial role of caspase-3 in osteogenic differentiation of bone marrow stromal stem cells. J. Clin. Invest. 114 (2004) 1704-1713
152. Muzio M., Chinnaiyan A.M., Kischkel F.C., O'Rourke K., Shevchenko A., Ni J., Scaffidi C., Bretz J.D., Zhang M., Gentz R., Mann M., Krammer P.H., Peter M.E., and Dixit V.M. FLICE, a novel FADD-homologous ICE/CED-3-like protease, is recruited to the CD95 (Fas/APO-1) death-inducing signaling complex. Cell 85 (1996) 817-827
153. Muzio M., Stockwell B.R., Stennicke H.R., Salvesen G.S., and Dixit V.M. An induced proximity model for caspase-8 activation. J. Biol. Chem. 273 (1998) 2926-2930
154. Nadiri A., Wolinski M.K., and Saleh M. The inflammatory caspases: key players in the host response to pathogenic invasion and sepsis. J. Immunol. 177 (2006) 4239-4245
155. Nakagawa T., and Yuan J.Y. Cross-talk between two cysteine protease families: activation of caspase-12 by calpain in apoptosis. J. Cell Biol. 150 (2000) 887-894
156. Nakagawa T., Zhu H., Morishima N., Li E., Xu J., Yankner B.A., and Yuan J. Caspase-12 mediates endoplasmic reticulum specific apoptosis and cytotoxicity by amyloid-beta. Nature 403 (2000) 98-103
157. Nakajima K., Takahashi A., and Yaoita Y. Structure, expression and function of the Xenopus laevis caspase family. J. Biol. Chem. 275 (2000) 10484-10491
158. Nhan T.Q., Liles W.C., and Schwartz S.M. Physiological functions of caspases beyond cell death. Am. J. Pathol. 169 (2006) 729-737
159. Nicholson D.W. Caspase structure, proteolytic substrates, and function during apoptotic cell death. Cell Death Differ. 6 (1999) 1028-1042
160. Nicholson D.W., Ali A., Thornberry N.A., Vaillancourt J.P., Ding C.K., Gallant M., Gareau Y., Griffin P.R., Labelle M., and Lazebnik Y.A. Identification and inhibition of the ICE/CED-3 protease necessary for mammalian apoptosis. Nature 376 6535 (1995) 37-43
161. Nicholson D.W., and Thornberry N.A. Caspases: killer proteases. Trends Biochem. Sci. 22 (1997) 299-306
162. O'Reilly L.A., Ekert P., Harvey N., Marsden V., Cullen L., Vaux D.L., Hacker G., Magnusson C., Pakusch M., Cecconi F., Kuida K., Strasser A., Huang D.C., and Kumar S. Caspase-2 is not required for thymocyte or neuronal apoptosis even though cleavage of caspase-2 is mediated by Apaf-1 and caspase-9. Cell Death Diff 9 (2002) 832-841
163. Ogura Y., Sutterwala F.S., and Flavell R.A. The inflammasome: first line of the immune response to cell stress. Cell 126 (2006) 656-662
164. Okuyama R., Nguyen B.C., Talora C., Ogawa E., Tommasi di Vignano A., Lioumi M., Chiorino G., Tagami H., Woo M., and Dotto G.P. High commitment of embryonic keratinocytes to terminal differentiation through a Notch1-caspase 3 regulatory mechanism. Dev. Cell. 6 (2004) 551-662
165. Paroni G., Henderson C., Schneider C., and Brancolini C. Caspase-2 can trigger Cytochrome C release and apoptosis from the nucleus. J. Biol. Chem. 277 (2002) 15147-15161
166. Peter M.E., and Krammer P.H. The CD95 (APO-1/Fas) DISC and beyond. Cell Death Differ. 10 (2003) 26-35
167. Pinkoski M.J., Waterhouse N.J., Heibein J.A., Wolf B.B., Kuwana T., Goldstein J.C., Newmeyer D.D., Bleackley R.C., and Green D.R. Granzyme B mediated apoptosis proceeds predominantly through a Bcl-2 inhibitable mitochondrial pathway. J. Biol. Chem. 276 (2001) 12060-12067
168. Porter A.G., and Janicke R.U. Emerging roles of caspase-3 in apoptosis. Cell Death Differ. 6 (1999) 99-104
169. Rano T.A., Timkey T., Peterson E.P., Rotonda J., Nicholson D.W., Becker J.W., Chapman K.T., and Thornberry N.A. A combinatorial approach for determining protease specificities: application to interleukin-1beta converting enzyme (ICE). Chem. Biol. 4 (1997) 149-155
170. Rao R.V., Hermel E., Castro-Obregon S., del Rio G., Ellerby L.M., Ellerby H.M., and Bredesen D.E. Coupling endoplasmic reticulum stress to the cell death program. J. Biol. Chem. 276 (2001) 33869-33874
171. Rao R.V., Castro-Obregon S., Frankowski H., Schuler M., Stoka V., del Rio G., Bredesen D.E., and Ellerby H.M. Coupling endoplasmic reticulum stress to the cell death program. An Apaf-1 independent intrinsic pathway. J. Biol. Chem. 14 (2002) 21836-21842
172. Read S.H., Baliga B.C., Ekert P.G., Vaux D.L., and Kumar S. A novel apaf-1-independent putative caspase-2 activation complex. J. Cell Biol. 159 (2002) 739-745
173. Rébé C., Cathelin S., Launay S., Filomenko R., Prévotat L., L'Ollivier C., Gyan E., Micheau O., Grant S., Dubart-Kupperschmitt A., Fontenay M., and Solary E. Caspase-8 prevents sustained activation of NF-(kappa)B in monocytes undergoing macrophagic differentiation. Blood 109 (2007) 1442-1450
174. Reis M.I., do Vale A., Pinto C., Nascimento D.S., Costa-Ramos C., Silva D.S., Silva M.T., and dos Santos N.M. First molecular cloning and characterisation of caspase-9 gene in fish and its involvement in a gram negative septicaemia. Mol. Immunol. 44 (2007) 1754-1764
175. Renatus M., Stennicke H.R., Scott F.L., Liddington R.C., and Salvesen G.S. Dimer formation drives the activation of the cell death protease caspase 9. Proc. Natl. Acad. Sci. U SA. 98 (2001) 14250-14255
176. Renatus M., Zhou Q., Stennicke H.R., Snipas S.J., Turk D., Bankston L.A., Liddington R.C., and Salvesen G.S. Crystal structure of the apoptotic suppressor CrmA in its cleaved form. Structure 8 (2000) 789-797
177. Richie D.L., Miley M.D., Bhabhra R., Robson G.D., Rhodes J.C., and Askew D.S. The Aspergillus fumigatus metacaspases CasA and CasB facilitate growth under conditions of endoplasmic reticulum stress. Mol. Microbiol. 63 (2007) 591-604
178. Riedl S.J., Renatus M., Schwarzenbacher R., Zhou Q., Sun C., Fesik S.W., Liddington R.C., and Salvesen G.S. Structural basis for the inhibition of caspase-3 by XIAP. Cell. 104 (2001) 791-800
179. Robertson A.J., Croce J., Carbonneau S., Voronina E., Miranda E., McClay D.R., and Coffman J.A. The genomic underpinnings of apoptosis in Strongylocentrotus purpuratus. Dev. Biol. 300 (2006) 321-334
180. Rohn T.T., Cusack S.M., Kessinger S.R., and Oxford J.T. Caspase activation independent of cell death is required for proper cell dispersal and correct morphology in PC12 cells. Exp. Cell Res. 295 (2004) 215-225
181. Rothe M., Pan M.G., Henzel W.J., Ayres T.M., and Goeddel D.V. The TNFR2-TRAF signaling complex contains two novel proteins related to baculoviral inhibitor of apoptosis proteins. Cell. 83 (1995) 1243-1252
182. Rotonda J., Nicholson D.W., Fazil K.M., Gallant M., Gareau Y., Labelle M., Peterson E.P., Rasper D.M., Ruel R., Vaillancourt J.P., Thornberry N.A., and Becker J.W. The three-dimensional structure of apopain/CPP32, a key mediator of apoptosis. Nat. Struct. Biol. 3 (1996) 619-625
183. Roy N., Mahadevan M.S., McLean M., Shutler G., Yaraghi Z., Farahani R., Baird S., Besner-Johnston A., Lefebvre C., and Kang X. The gene for neuronal apoptosis inhibitory protein is partially deleted in individuals with spinal muscular atrophy. Cell 80 (1995) 167-178
184. Roy N., Deveraux Q.L., Takahashi R., Salvesen G.S., and Reed J.C. The c-IAP-1 and c-IAP-2 proteins are direct inhibitors of specific caspases. EMBO J. 16 (1997) 6914-6925
185. Ruggles S.W., Fletterick R.J., and Craik C.S. Characterization of structural determinants of granzyme B reveals potent mediators of extended substrate specificity. J. Biol. Chem. 279 (2004) 30751-30759
186. Sakamaki K., Tsukumo S., and Yonehara S. Molecular cloning and characterization of mouse caspase-8. Eur. J. Biochem. 253 (1998) 399-405
187. Sakamaki K., Nozaki M., Kominami K., and Satou Y. The evolutionary conservation of the core components necessary for the extrinsic apoptotic signaling pathway, in Medaka fish. BMC Genomics. 8 (2007) 141-156
188. Sakata S., Yan Y.L., Satou Y., Momoi A., Ngo-Hazelett P., Nozaki M., Furutani-Seiki M., Postlethwait J.H., Yonehara S., and Sakamaki K. Conserved function of caspase-8 in apoptosis during bony fish evolution. Gene 396 (2007) 134-148
189. Salmena L., Lemmers B., Hakem A., Matysiak-Zablocki E., Murakami K., Au P.Y., Berry D.M., Tamblyn L., Shehabeldin A., Migon E., Wakeham A., Bouchard D., Yeh W.C., McGlade J.C., Ohashi P.S., and Hakem R. Essential role for caspase 8 in T-cell homeostasis and T-cell-mediated immunity. Genes Dev. 17 (2003) 883-895
190. Salmena L., and Hakem R. Caspase-8 deficiency in T cells leads to a lethal lymphoinfiltrative immune disorder. J. Exp. Med. 202 (2005) 727-732
191. Salvesen G.S. Caspases and apoptosis. Essays Biochem. 38 (2002) 9-19
192. Salvesen G.S., and Duckett C.S. IAP proteins: blocking the road to death's door. Nat. Rev. Mol. Cell Biol. 3 (2002) 401-410
193. Sattar R., Ali S.A., and Abbasi A. Molecular mechanism of apoptosis: Prediction of three-dimensional structure of caspase-6 and its interactions by homology modeling. Biochem Biophys. Res. Commun. 308 (2003) 497-504
194. Scaffidi C., Medema J.P., Krammer P.H., and Peter M.E. FLICE is predominantly expressed as two functionally active isoforms, caspase-8/a and caspase-8/b. J. Biol. Chem. 272 (1997) 26953-26958
195. Scaffidi C., Fulda S., Srinivasan A., Friesen C., Li F., Tomaselli K.J., Debatin K.M., Krammer P.H., and Peter M.E. Two CD95 (APO-1/Fas) signaling pathways. EMBO J. 17 (1998) 1675-1687
196. Scaffidi C., Kischkel F.C., Krammer P.H., and Peter M.E. Analysis of the CD95 (APO-1/Fas) death-inducing signaling complex (DISC) by high resolution two-dimensional gel electrophoresis. Methods Enzymol. 322 (1999) 363-373
197. Scaffidi C., Krammer P.H., and Peter M.E. Isolation and analysis of components of CD95 (APO-1/Fas) death-inducing signaling complex. Methods 17 (1999) 287-291
198. Scaffidi C., Schmitz I., Krammer P.H., and Peter M.E. The role of c-FLIP in modulation of CD95-induced apoptosis. J. Biol. Chem. 274 (1999) 1541-1548
199. Scaffidi C., Schmitz I., Zha J., Korsmeyer S.J., Krammer P.H., and Peter M.E. Differential modulation of apoptosis sensitivity in CD95 type I and type II cells. J. Biol. Chem. 274 (1999) 22532-22538
200. Schecter I., and Berger M. On the size of the active site in proteases. Biochem. Biophys. Res. Commun. 27 (1967) 157-162
201. Schweizer A., Briand C., and Grutter M.G. Crystal structure of caspase-2, apical initiator of the intrinsic apoptotic pathway. J. Biol. Chem. 278 (2003) 42441-42447
202. Shaham S. Identification of multiple Caenorhabditis elegans caspases and their potential roles in proteolytic cascades. J. Biol. Chem. 273 (1998) 35109-35117
203. Shearwin-Whyatt L.M., Harvey N.L., and Kumar S. Subcellular localization and CARD-dependent oligomerization of the death adaptor RAIDD. Cell Death Diff. 7 (2000) 155-165
204. Shi Y. Apoptosome: the cellular engine for the activation of caspase-9. Structure (Camb) 10 (2002) 285-288
205. Shi Y. Mechanisms of caspase activation and inhibition during apoptosis. Mol. Cell. 9 (2002) 459-470
206. Shin S., Lee Y., Kim W., Ko H., Choi H., and Kim K. Caspase-2 primes cancer cells for TRAIL-mediated apoptosis by processing procaspase-8. EMBO J. 24 (2005) 3532-3542
207. Song Z., McCall K., and Steller H. DCP-1, a Drosophila cell death protease essential for development. Science 275 (1997) 536-540
208. Song Z., Guan B., Bergman A., Nicholson D.W., Thornberry N.A., Peterson E.P., and Steller H. Biochemical and genetic interactions between Drosophila caspases and the proapoptotic genes rpr, hid, and grim. Mol. Cell Biol. 20 (2000) 2907-2914
209. Sordet O., Rébé C., Plenchette S., Zermati Y., Hermine O., Vainchenker W., Garrido C., Solary E., and Dubrez-Daloz L. Specific involvement of caspases in the differentiation of monocytes into macrophages. Blood 100 (2002) 4446-4453
210. Sprick M.R., Rieser E., Stahl H., Grosse-Wilde A., Weigand M.A., and Walczak H. Caspase-10 is recruited to and activated at the native TRAIL and CD95 death inducing signaling complexes in a FADD-dependent manner but can not functionally substitute caspase-8. EMBO J. 21 (2002) 4520-4530
211. Stennicke H.R., Renatus M., Meldal M., and Salvesen G.S. Internally quenched fluorescent peptide substrates disclose the subsite preferences of human caspases 1, 3, 6, 7 and 8. Biochem. J. 350 (2000) 563-568
212. Stennicke H.R., Ryan C.A., and Salvesen G.S. Reprieval from execution: The molecular basis of caspase inhibition. Trends Biochem. Sci. 27 (2002) 94-101
213. Su H., Bidère N., Zheng L., Cubre A., Sakai K., Dale J., Salmena L., Hakem R., Straus S., and Lenardo M. Requirement for caspase-8 in NF-kappaB activation by antigen receptor. Science 307 (2005) 1465-1468
214. Sutterwala F.S., Ogura Y., Szczepanik M., Lara-Tejero M., Lichtenberger G.S., Grant E.P., Bertin J., Coyle A.J., Galán J.E., Askenase P.W., and Flavell R.A. Critical role for NALP3/CIAS1/Cryopyrin in innate and adaptive immunity through its regulation of caspase-1. Immunity 24 (2006) 317-327
215. Sutton V.R., Davis J.E., Cancilla M., Johnstone R.W., Ruefli A.A., Sedelies K., Browne K.A., and Trapani J.A. Initiation of apoptosis by granzyme B requires direct cleavage of bid, but not direct granzyme B-mediated caspase activation. J. Exp. Med. 192 (2000) 1403-1414
216. Sutton V.R., Wowk M.E., Cancilla M., and Trapani J.A. Caspase activation by granzyme B is indirect, and caspase auto processing requires the release of proapoptotic mitochondrial factors. Immunity. 18 (2003) 319-329
217. Szallies A., Kubata B.K., and Duszenko M. A metacaspase of Trypanosoma brucei causes loss of respiration competence and clonal death in the yeast Saccharomyces cerevisiae. FEBS Lett. 517 (2002) 144-150
218. Takle H., McLeod A., and Andersen O. Cloning and characterization of the executioner caspases 3, 6, 7 and Hsp70 in hyperthermic Atlantic salmon (Salmo salar) embryos. Comp. Biochem. Physiol. B Biochem. Mol. Biol. 144 (2006) 188-198
219. Takle H., and Andersen O. Caspases and apoptosis in fish. J. Fish Biol. 71 (2007) 326-349
220. Tartaglia L.A., Ayres T.M., Wong G.H., and Goeddel D.V. A novel domain within the 55 kDa TNF receptor signals cell death. Cell 74 (1993) 845-853
221. Tewari M., Quan L.T., O'Rourke K., Desnoyers S., Zeng Z., Beidler D.R., Poirier G.G., Salvesen G.S., and Dixit V.M. Yama/CPP32β, a mammalian homolog of CED-3, is a CrmA-inhibitable protease that cleaves the death substrate poly(ADP-ribose) polymerase. Cell 81 (1995) 801-809
222. Thome M., and Tschopp J. Regulation of lymphocyte proliferation and death by FLIP. Nat. Rev. Immunol. 1 (2001) 50-58
223. Thome M., Schneider P., Hofmann K., Fickenscher H., Meinl E., Neipel F., Mattmann C., Burns K., Bodmer J.L., Schröter M., Scaffidi C., Krammer P.H., Peter M.E., and Tschopp J. Viral FLICE-inhibitory proteins (FLIPs) prevent apoptosis induced by death receptors. Nature. 386 (1997) 517-521
224. Thornberry N.A., Bull H.G., Calaycay J.R., Chapman K.T., Howard A.D., Kostura M.J., Miller D.K., Molineaux S.M., Weidner J.R., and Aunins J. A novel heterodimeric cysteine protease is required for interleukin-1 beta processing in monocytes. Nature 356 (1992) 768-774
225. Thornberry N.A., Rano T.A., Peterson E.P., Rasper D.M., Timkey T., Garcia-Calvo M., Houtzager V.M., Nordstrom P.A., Roy S., Vaillancourt J.P., Chapman K.T., and Nicolson D.W. A combinatorial approach defines specificities of member of the caspase family and granzyme B. Functional relationships established for the key mediators of apoptosis. J. Biol. Chem. 272 (1997) 17907-17911
226. Thornberry N.A., and Lazebnik Y. Caspases: enemies within. Science 281 (1998) 1312-1316
227. Timmer J.C., and Salvesen G.S. Caspase substrates. Cell Death Differ. 14 (2007) 66-72
228. Tinel A., and Tschopp J. The PIDDosome, a protein complex implicated in activation of caspase-2 in response to genotoxic stress. Science 304 (2004) 843-846
229. Tschopp J., Irmler M., and Thome M. Inhibition of Fas death signals by FLIPs. Curr. Opin. Immunol. 10 (1998) 552-558
230. Tu S., McStay G.P., Boucher L.M., Mak T., Beere H.M., and Green D.R. In situ trapping of activated initiator caspases reveals a role for caspase-2 in heat shock-induced apoptosis. Nat. Cell Biol. 8 (2006) 72-77
231. Uren A.G., Coulson E.J., and Vaux D.L. Conservation of baculovirus inhibitor of apoptosis repeat proteins (BIRPs) in viruses, nematodes, vertebrates and yeasts. Trends Biochem. Sci. 23 (1998) 159-162
232. Uren A.G., O'Rourke K., Aravind L., Pisabarro M.T., Seshagiri S., Koonin E.V., and Dixit V.M. Identification of paracaspases and metacaspases: two ancient families of caspase-related proteins, one of which plays a central role in MALT lymphoma. Mol. Cell. 6 (2000) 961-967
233. Valencia C.A., Bailey C., and Liu R. Novel zebrafish caspase-3 substrates. Biochem. Biophys. Res. Commun. 361 (2007) 311-316
234. Varfolomeev E.E., Schuchmann M., Luria V., Chiannilkulchai N., Beckmann J.S., Mett I.L., Rebrikov D., Brodianski V.M., Kemper O.C., Kollet O., Lapidot T., Soffer D., Sobe T., Avraham K.B., Goncharov T., Holtmann H., Lonai P., and Wallach D. Targeted disruption of the mouse caspase 8 gene ablates cell death induction by the TNF receptors, Fas/Apo1, and DR3 and is lethal prenatally. Immunity 9 (1998) 267-276
235. Vercammen D., van de Cotte B., De Jaeger G., Eeckhout D., Casteels P., Vandepoele K., Vandenberghe I., Van Beeumen J., Inzé D., and Van Breusegem F. Type II metacaspases Atmc4 and Atmc9 of Arabidopsis thaliana cleave substrates after arginine and lysine. J. Biol. Chem. 279 (2004) 45329-45336
236. Vercammen D., Belenghi B., van de Cotte B., Beunens T., Gavigan J.-A., De Rycke R., Brackenier A., Inzé D., Harris J.L., and Van Breusegem F. Serpin1 of Arabidopsis thaliana is a suicide inhibitor for metacaspase 9. J. Mol. Biol. 364 (2006) 625-636
237. Vercammen D., Declercq W., Vandenabeele P., and Van Breusegem F. Are metacaspases caspases?. J. Cell Biol. 179 (2007) 375-380
238. Wagner K.W., Engels I.H., and Deveraux Q.L. Caspase-2 can function upstream of bid cleavage in the TRAIL apoptosis pathway. J. Biol. Chem. 279 (2004) 35047-35052
239. Walker N.P., Talanian R.V., Brady K.D., Dang L.C., Bump N.J., Ferenz C.R., Franklin S., Ghayur T., Hackett M.C., and Hammill L.D. Crystal structure of the cysteine protease interleukin-1 beta-converting enzyme: a (p20/p10)2 homodimer. Cell 78 (1994) 343-352
240. Wang J., Zheng L., Lobito A., Chan F.K., Dale J., and Sneller M. Inherited human caspase 10 mutations underlie defective lymphocyte and dendritic cell apoptosis in autoimmune lymphoproliferative syndrome type II. Cell 98 (1999) 47-58
241. Wang J., Chun H.J., Wong W., Spencer D.M., and Lenardo M.J. Caspase-10 is an initiator caspase in death receptor signaling. Proc. Natl. Acad. Sci. USA 98 (2001) 13884-13888
242. Wang K.K. Calpain and caspase: can you tell the difference?. Trends Neurosci. 23 (2000) 20-26
243. Wang L., Miura M., Bergeron L., Zhu H., and Yuan J. Ich-1, an Ice/ced-3-related gene, encodes both positive and negative regulators of programmed cell death. Cell 78 (1994) 739-750
244. Wang S., Miura M., Jung Y.K., Zhu H., Li E., and Yuan J. Murine caspase-11, an ICE-interacting protease, is essential for the activation of ICE. Cell 92 (1998) 501-509
245. Wang Z.B., Liu Y.Q., and Cui Y.F. Pathways to caspase activation. Cell Biol. Int. 29 (2005) 489-496
246. Watanabe N., and Lam E. Two Arabidopsis metacaspases AtMCP1b and AtMCP2b are arginine/lysine-specific cysteine proteases and activate apoptosis-like cell death in yeast. J. Biol. Chem. 280 (2005) 14691-14699
247. Weber C.H., and Vincenz C. The death domain superfamily: a tale of two interfaces [review]? Trends Biochem. Sci. 26 (2001) 475-481
248. Wei Y., Fox T., Chambers S.P., Sintchak J., Coll J.T., Golec J.M., Swenson L., Wilson K.P., and Charifson P.S. The structures of caspases-1, -3, -7 and -8 reveal the basis for substrate and inhibitor selectivity. Chem. Biol. 7 (2000) 423-432
249. Weill M., Philips A., Chourrout D., and Fort P. The caspase family in urochordates: distinct evolutionary fates in ascidians and larvaceans. Biol Cell. 97 (2005) 857-866
250. Wiens M., Krasko A., Perovic S., and Muller W.E. Caspase-mediated apoptosis in sponges: cloning and function of the phylogenetic oldest apoptotic proteases from metazoan. Biochem Biophys Acta 1593 (2003) 179-189
251. Wilson K.P., Black J.A., Thomson J.A., Kim E.E., Griffith J.P., Navia M.A., Murcko M.A., Chambers S.P., Aldape R.A., and Raybuck S.A. Structure and mechanism of interleukin-1 beta converting enzyme. Nature. 370 (1994) 270-275
252. Woltering E.J., van der Bent A., and Hoeberichts F.A. Do plant caspases exist?. Plant Physiol. 130 (2002) 1764-1769
253. Xu G., Cirilli M., Huang Y., Rich R.L., Myszka D.G., and Wu H. Covalent inhibition revealed by the crystal structure of the caspase-8/p35 complex. Nature 410 (2001) 494-497
254. Xue D., and Horvitz H.R. Inhibition of the Caenorhabditis elegans cell-death protease CED-3 by a CED-3 cleavage site in baculovirus p35 protein. Nature 377 (1995) 248-251
255. Xue D., Shaham S., and Horvitz H.R. The Caenorhabditis elegans cell-death protein CED-3 is a cysteine protease with substrate specificities similar to those of the human CPP32 protease. Genes Dev. 10 (1996) 1073-1083
256. Yabu T., Kishi S., Okazaki T., and Yamashita M. Characterization of zebrafish caspase-3 and induction of apoptosis through ceramide generation in fish fathead minnow tailbud cells and zebrafish embryo. Biochem. J. 360 (2001) 39-47
257. Yaoita Y., and Nakajima K. Induction of apoptosis and CPP32 expression by thyroid hormone in a myoblastic cell line derived from tadpole tail. J. Biol. Chem. 272 (1997) 5122-5127
258. Yokoyama H., Mukae N., Sakahira H., Okawa K., Iwamatsu A., and Nagata S. A novel activation mechanism of caspase-activated DNase from Drosophila melanogaster. J. Biol. Chem. 275 (2000) 12978-12986
259. Yuan J., Shaham S., Ledoux S., Ellis H.M., and Horvitz H.R. The C. elegans cell death genes ced3 encodes a protein similar to mammalian interleukin-1β-converting enzyme. Cell 75 (1993) 641-652
260. Zermati Y., Garrido C., Amsellem S., Fishelson S., Bouscary D., Valensi F., Varet B., Solary E., and Hermine O. Caspase activation is required for terminal erythroid differentiation. J. Exp. Med. 193 (2001) 247-254
261. Zhivotovsky B., and Orrenius S. Caspase-2 function in response to DNA damage. Biochem Biophys. Res. Commun. 331 (2005) 859-867
262. Zimmermann P., Hirsch-Hoffmann M., Hennig L., and Gruissem W. GENEVESTIGATOR. Arabidopsis microarray database and analysis toolbox. Plant Physiol. 136 (2004) 2621-2632
263. Zou H., Henzel W.J., Liu X., Lutschg A., and Wang X. Apaf-1, a human protein homologous to C. elegans CED-4, participates in Cytochrome C dependent activation of caspase-3. Cell 90 (1997) 405-413