3.4.22.61 (aspartyl)2-rhodamine 110 + H2O - Pichia kudriavzevii ? - ? 411098 3.4.22.61 (aspartyl)2-rhodamine 110 + H2O - Candida albicans ? - ? 411098 3.4.22.61 (aspartyl)2-rhodamine 110 + H2O - Candida parapsilosis ? - ? 411098 3.4.22.61 (aspartyl)2-rhodamine 110 + H2O - Pichia kudriavzevii Glasgow ? - ? 411098 3.4.22.61 (aspartyl)2-rhodamine 110 + H2O - Candida parapsilosis AAHB 4479 ? - ? 411098 3.4.22.61 (aspartyl)2-rhodamine 110 + H2O - Candida albicans GDH 2346 ? - ? 411098 3.4.22.61 Ac-IEPD-7-amido-4-methylcoumarin + H2O 37°C Homo sapiens Ac-IEPD + 7-amino-4-methylcoumarin - ? 381308 3.4.22.61 Ac-IEPD-AMC + H2O 37°C Homo sapiens Ac-IEPD + AMC - ? 381309 3.4.22.61 Ac-IETD-4-methylcoumarin 7-amide + H2O an artificial caspase-8 substrate Homo sapiens Ac-IETD + 7-amino-4-methylcoumarin - ? 418422 3.4.22.61 Ac-IETD-7-amido-4-methylcoumarin + H2O - Mus musculus Ac-IETD + 7-amino-4-methylcoumarin - ? 404165 3.4.22.61 Ac-IETD-7-amido-4-methylcoumarin + H2O - Mus musculus BALB/c Ac-IETD + 7-amino-4-methylcoumarin - ? 404165 3.4.22.61 Ac-Leu-Glu-Thr-Asp-7-amido-4-trifluoromethylcoumarin + H2O - Sus scrofa Ac-Leu-Glu-Thr-Asp + 7-amino-4-trifluoromethylcoumarin - ? 449490 3.4.22.61 acetyl-DEVD-4-nitroanilide + H2O - Homo sapiens acetyl-DEVD + 4-nitroaniline - ? 361978 3.4.22.61 acetyl-DEVD-7-amido-4-methylcoumarin + H2O - Homo sapiens acetyl-DEVD + 7-amino-4-methylcoumarin - ? 361962 3.4.22.61 acetyl-DEVD-p-nitroanilide + H2O 49% of the activity with acetyl-IETD-p-nitroanilide Cricetulus griseus acetyl-DEVD + p-nitroaniline - ? 391142 3.4.22.61 acetyl-IETD-4-nitroanilide + H2O - Homo sapiens acetyl-IETD + 4-nitroaniline - ? 361979 3.4.22.61 acetyl-IETD-7-amido-4-fluoromethylcoumarin + H2O - Homo sapiens acetyl-IETD + 7-amino-4-fluoromethylcoumarin - ? 404199 3.4.22.61 acetyl-IETD-p-nitroanilide + H2O - Cricetulus griseus acetyl-IETD + p-nitroaniline - ? 391152 3.4.22.61 acetyl-Ile-Glu(OMe)-Thr-Asp(OMe)-7-amido-4-trifluoromethylcoumarin + H2O - Mus musculus acetyl-Ile-Glu(OMe)-Thr-Asp(OMe) + 7-amino-4-trifluoromethylcoumarin - ? 404200 3.4.22.61 acetyl-Ile-Glu(OMe)-Thr-Asp(OMe)-7-amido-4-trifluoromethylcoumarin + H2O - Homo sapiens acetyl-Ile-Glu(OMe)-Thr-Asp(OMe) + 7-amino-4-trifluoromethylcoumarin - ? 404200 3.4.22.61 acetyl-Ile-Glu-Thr-Asp-7-amino-4-fluoromethylcoumarin + H2O 37°C, pH 7.4 Homo sapiens Ac-IETD + 7-amino-4-fluoromethylcoumarin - ? 381329 3.4.22.61 acetyl-LEHD-p-nitroanilide + H2O 142% of the activity with acetyl-IETD-p-nitroanilide Cricetulus griseus acetyl-LEHD + p-nitroaniline - ? 391158 3.4.22.61 acetyl-VDVAD-p-nitroanilide + H2O 36% of the activity with acetyl-IETD-p-nitroanilide Cricetulus griseus acetyl-VDVAD + p-nitroaniline - ? 391165 3.4.22.61 acetyl-VEID-p-nitroanilide + H2O 76% of the activity with acetyl-IETD-p-nitroanilide Cricetulus griseus acetyl-VEID + p-nitroaniline - ? 391168 3.4.22.61 acetyl-WEHD-p-nitroanilide + H2O 64% of the activity with acetyl-IETD-p-nitroanilide Cricetulus griseus acetyl-WEHD + p-nitroaniline - ? 391169 3.4.22.61 alpha-fodrin + H2O - Homo sapiens ? - ? 410714 3.4.22.61 Atg3 protein + H2O - Homo sapiens ? - ? 430898 3.4.22.61 BAP31 + H2O cleavage results in a proapoptotic p20 fragment Homo sapiens ? - ? 381519 3.4.22.61 basic transcription factor 3 + H2O - Mus musculus ? - ? 391403 3.4.22.61 Bcl-2 + H2O - Cricetulus griseus ? - ? 381520 3.4.22.61 Bcl-2 protein Bid + H2O cleavage results in a proapoptotic p15 tBid fragment Homo sapiens ? - ? 381521 3.4.22.61 benzyloxycarbonyl-IETD-7-amido-4-trifluoromethylcoumarin + H2O - Mus musculus benzyloxycarbonyl-IETD + 7-amino-4-trifluoromethylcoumarin - ? 411715 3.4.22.61 beta-catenin + H2O - Mus musculus ? - ? 361977 3.4.22.61 BH3-only protein Bid + H2O - Homo sapiens ? - ? 448480 3.4.22.61 BID + H2O - Homo sapiens ? - ? 361973 3.4.22.61 BID + H2O a 15000 Da C-terminal frament and a 14000 Da N-terminal fragment are generated by caspase-8 cleavage at T58-/-D59 Homo sapiens ? - ? 361973 3.4.22.61 BID + H2O a 15000 Da C-terminal frament and a 14000 Da N-terminal fragment are generated by caspase-8 cleavage at T58-/-D59. While full-length BID is localized in cytosol, truncated BID translocates to mitochondria and thus transduces apoptotic signals from cytoplasmic membrane to mitochondria. BID is a mediator of mitochondrial damage induced by Casp8 Homo sapiens ? - ? 361973 3.4.22.61 BID + H2O the cleavage sequences for caspase-8 are IEAD/S and LQTD/G Mus musculus ? - ? 361973 3.4.22.61 Bid + H2O Bid is a caspase-8 substrate and that its cleavage can be crucial for CD95-induced apoptosis. Caspase-8-mediated cleavage of Bid into a pro-apoptotically active, truncated form provides the link between death receptor stimulation and mitochondrial apoptotic events Homo sapiens tBid + ? - ? 417899 3.4.22.61 Bid + H2O i.e. BH3 interacting domain death agonist Homo sapiens tBid + ? - ? 417899 3.4.22.61 Bid + H2O caspase-8 cleaves Bid at Asp60 leading to the release of a truncated form containing the C-terminal part of the protein, 15 kDa. Cleavage of Bid by caspase-8 removes the N-terminal portion of the protein which, when still linked to the C-terminal p15 portion inhibits the pro-apoptotic function of the latter Homo sapiens tBid + ? - ? 417899 3.4.22.61 Bid peptide + H2O - Homo sapiens ? - ? 402515 3.4.22.61 Bid peptide + H2O a specific caspase-8 substrate Homo sapiens ? - ? 402515 3.4.22.61 Bid peptide + H2O CTX III, from crude venom of Naja naja atra, inhibits proliferation of human leukemia K562 cells by G2/M phase arresting and apoptosis which is associated with the activation of caspase-8 and cytochrome c release as well as the p38 and c-Jun N-terminal protein kinase phosphorylation signaling pathway in vitro and in vivo, caspase-8-dependent Bid-Bax pathway, overview Homo sapiens ? - ? 402515 3.4.22.61 Bid peptide + H2O upon cleavage by caspase-8, Bid peptide activates Bax peptide Homo sapiens ? - ? 402515 3.4.22.61 Bid peptide + H2O - Mus musculus truncated Bid peptide + ? - ? 410764 3.4.22.61 Bid peptide + H2O - Homo sapiens truncated Bid peptide + ? - ? 410764 3.4.22.61 Bid protein + H2O - Homo sapiens ? - ? 391506 3.4.22.61 Bid protein + H2O i.e. BH3 interacting domain death agonist protein Homo sapiens cleaved Bid protein - ? 402516 3.4.22.61 Ca2+/calmodulin-dependent protein kinase-like kinase + H2O cleavage generates a 43 kDa C-terminal fragment and a small N-terminal fragment with proapoptotic activity Homo sapiens ? - ? 381608 3.4.22.61 carbonic anhydrase XIV + H2O cleaved at Asp53 Homo sapiens ? - ? 418534 3.4.22.61 carboxypeptidase E + H2O - Mus musculus ? - ? 391578 3.4.22.61 caspase-3 + H2O - Homo sapiens ? - ? 410769 3.4.22.61 cellular FLIP long form + H2O - Mus musculus ? - ? 381636 3.4.22.61 cellular inhibitor of apoptosis 1 + H2O i.e. cIAP-1, TRAIL-induced degradation of cIAP-1 requires caspase 8 activity, and it is, at least in part, due to direct cleavage of cIAP-1 by caspase 8 Homo sapiens ? - ? 417920 3.4.22.61 cellular inhibitor of apoptosis 1 + H2O i.e. cIAP-1, degradation. No activity with cIAP-2. In vitro substrate is recombinant human cIAP-1 Homo sapiens ? - ? 417920 3.4.22.61 CYLD + H2O key substrate processed by caspase 8 to block necrosis, CYLD is a key requirement for necrosis Homo sapiens CYLDp25 + ? - ? 417930 3.4.22.61 CYLD + H2O key substrate processed by caspase 8 to block necrosis, CYLD is a key requirement for necrosis of L929 fibrosarcoma cells Mus musculus CYLDp25 + ? - ? 417930 3.4.22.61 CYLD + H2O caspase 8 directly cleaves CYLD after Asp 215, an Asp215 CYLD substitution mutant cannot be cleaved by caspase 8 Mus musculus CYLDp25 + ? - ? 417930 3.4.22.61 CYLD + H2O caspase 8 directly cleaves CYLD after Asp 215, an Asp215 CYLD substitution mutant cannot be cleaved by caspase 8 Homo sapiens CYLDp25 + ? - ? 417930 3.4.22.61 DEVD-rhodamine + H2O - Mus musculus rhodamine + DEVD - ? 381789 3.4.22.61 Dopey family membrane 1 + H2O - Mus musculus ? - ? 391876 3.4.22.61 evolutionarily related interleukin-1beta converting enzyme + H2O ERICE i.e. evolutionarily related interleukin-1beta converting enzyme, cleavage at LEED289-/-, processing leads to the generation of two subunits Homo sapiens ? - ? 361972 3.4.22.61 FLICE + H2O 37°C Rattus norvegicus ? - ? 381870 3.4.22.61 FLICE2 + H2O - Homo sapiens ? - ? 361971 3.4.22.61 FLIPL + H2O the cleavage sequence for caspase-8 is LEVD/G Mus musculus ? - ? 418625 3.4.22.61 FLIPL protein + H2O - Homo sapiens ? - ? 417950 3.4.22.61 FLIPL protein + H2O processing of free FLIPL by caspase-8, FLIPL cleavage increases the recruitment of caspase-8 Mus musculus ? - ? 417950 3.4.22.61 FLIPL protein + H2O processing of free FLIPL by caspase-8, FLIPL cleavage increases the recruitment of caspase-8 Homo sapiens ? - ? 417950 3.4.22.61 FLIPL protein + H2O processing of free FLIPL by caspase-8 Mus musculus ? - ? 417950 3.4.22.61 FLIPL protein + H2O processing of free FLIPL by caspase-8 Homo sapiens ? - ? 417950 3.4.22.61 fluorescein isothiocyanate + H2O 37°C, pH 7.4 Mus musculus ? - ? 381872 3.4.22.61 glutaredoxin-1 + H2O murine or human protein substrate, the putative cleavage site of caspase-8, amino acids 43-46 EFVD and 56-59 AIQD, which has predicted affiffinity toward glutamic and aspartic acid residues Homo sapiens ? cleavage produces a 8 kDA fragment ? 405290 3.4.22.61 Golgi associated PDZ and coiled-coil motif containing trancription variant 1 + H2O - Mus musculus ? - ? 392155 3.4.22.61 HDAC-7 + H2O the cleavage sequence for caspase-8 is LETD/G Mus musculus ? - ? 418707 3.4.22.61 HER-2 + H2O - Homo sapiens ? - ? 382018 3.4.22.61 HER-2 + H2O 37°C, HER-2 double mutant MT34, carrying the mutation D1125A/D837A Homo sapiens ? - ? 382018 3.4.22.61 HER-2 + H2O 37°C, HER-2 double mutant MT35, carrying the mutation D1125A/D1087A, completely resistant to proteolysis Homo sapiens ? - ? 382018 3.4.22.61 HER-2 + H2O 37°C, HER-2 double mutant MT36, carrying the mutation D1125A/D1115A Homo sapiens ? - ? 382018 3.4.22.61 HER-2 + H2O 37°C, HER-2 mutant MT1, carrying the mutation D1012A Homo sapiens ? - ? 382018 3.4.22.61 HER-2 + H2O 37°C, HER-2 mutant MT2, carrying the mutation D1019A Homo sapiens ? - ? 382018 3.4.22.61 HER-2 + H2O 37°C, HER-2 mutant MT3, carrying the mutation D1125A, partially resistant to proteolysis Homo sapiens ? - ? 382018 3.4.22.61 HER-2 + H2O 37°C, wild-type HER-2 Homo sapiens ? - ? 382018 3.4.22.61 IEPD-7-amido-4-methylcoumarin + H2O - Homo sapiens IEPD + 7-amino-4-methylcoumarin - ? 431965 3.4.22.61 IETD-4-nitroanilide + H2O - Homo sapiens IETD + 4-nitroaniline - ? 361981 3.4.22.61 IETD-4-nitroanilide + H2O - Mus musculus IETD + 4-nitroaniline - ? 361981 3.4.22.61 IETD-4-nitroanilide + H2O - Rattus norvegicus IETD + 4-nitroaniline - ? 361981 3.4.22.61 IETD-7-amido-4-trifluoromethylcoumarin + H2O - Homo sapiens IETD + 7-amino-4-trifluoromethylcoumarin - ? 361963 3.4.22.61 IETD-7-amido-4-trifluoromethylcoumarin + H2O a specific caspase-8 substrate Mus musculus IETD + 7-amino-4-trifluoromethylcoumarin - ? 361963 3.4.22.61 Ile-Glu-Thr-Asp-4-nitroanilide + H2O - Homo sapiens Ile-Glu-Thr-Asp + 4-nitroaniline - ? 405478 3.4.22.61 interleukin-21 + H2O - Homo sapiens ? the CASP8-cleaved form of IL21R does not induce phosphorylation at Tyr705 of STAT3 ? 417980 3.4.22.61 interleukin-21 + H2O cleaved at Asp344 Homo sapiens ? - ? 417980 3.4.22.61 kinase anchor protein 1 + H2O - Mus musculus ? - ? 392311 3.4.22.61 LAP3 + H2O - Homo sapiens ? - ? 361968 3.4.22.61 LAP6 + H2O - Homo sapiens ? - ? 361970 3.4.22.61 LETD-4-nitroanilide + H2O - Mus musculus LETD + 4-nitroaniline - ? 412373 3.4.22.61 additional information Mch2 and ICH1 are effectively cleaved only in the presence of native extract Homo sapiens ? - ? 89 3.4.22.61 additional information the preferred cleavage sequence is LETD-/- Homo sapiens ? - ? 89 3.4.22.61 additional information the catalytic triad in caspase-8 comprises C260, H317 and the backbone carbonyl oxygen atom of R258, which points towards the Nepsilon atom of H317 Homo sapiens ? - ? 89 3.4.22.61 additional information the enzyme is indispensable for Fas-mediated apoptotic signaling Mus musculus ? - ? 89 3.4.22.61 additional information caspase-8L acts as an inhibitor of caspase-8 by interfering with the binding of caspase-8 to FADD, i.e. Fas-associated protein with death domain, and is involved in the regulation of Fas-mediated apoptosis Homo sapiens ? - ? 89 3.4.22.61 additional information caspase-8 is an initiator enzyme in the Fas-mediated pathway of which the downstream executioner caspase-3 is a physiological target Homo sapiens ? - ? 89 3.4.22.61 additional information initiator enzyme in apoptosis Homo sapiens ? - ? 89 3.4.22.61 additional information the enzyme acts as apoptosis initiator. Animals deficient in caspase-8 are embryonically lethal at approximately E12.5. Abnormal heart development and vascular hyperemia, EF resistant to Fas, TNF-alpha, and DR3 but exhibit normal sensitivity to UV, etoposide, low serum and staurosporine, death receptor signaling to JNK and NF-kappaB intact Homo sapiens ? - ? 89 3.4.22.61 additional information FLICE binds to the death effector domain of FADD and upon overexpression induces apoptosis that is blocked by the ICE family inhibitors, CrmA and v-VAD-fmk Homo sapiens ? - ? 89 3.4.22.61 additional information FLICE is the first in a cascade of ICE-like proteases activated by CD95. Active FLICE is released into the cytosol, where it can activate a cascade of ICE-like proteases Mus musculus ? - ? 89 3.4.22.61 additional information FLICE is the first in a cascade of ICE-like proteases activated by CD95. Active FLICE is released into the cytosol, where it can activate a cascade of ICE-like proteases Homo sapiens ? - ? 89 3.4.22.61 additional information the enzyme is responsible for activating a protease cascade after Fas-receptor ligation, leading to cell death. Mch5 is the most upstream protease that receives the activation signal from the Fas-receptor to initiate the apoptotic protease cascade that leads to activation of ICE-like proteases (TX, ICE, and ICE-relIII), Ced-3-like proteases (CPP32, Mch2, Mch3, Mch4 and Mch6) and the ICH-1 protease Homo sapiens ? - ? 89 3.4.22.61 additional information preferential recruitment of procaspase-8L by the BAP31 complex at the endoplasmic reticulum suggests an additional pathway for regulating initiator caspase-8 during apoptosis Homo sapiens ? - ? 89 3.4.22.61 additional information caspase-8 has a postnatal role in immune activation of native lymphocytes Homo sapiens ? - ? 89 3.4.22.61 additional information caspase-8 occupies an essential and apical position in the fas signaling pathway and suggests that caspase-8 may participate broadly in multiple apoptotic pathways Homo sapiens ? - ? 89 3.4.22.61 additional information MACH is the most upstream enzymatic component in the Fas/APO-1- and p55-R-induced cell death signaling cascade Homo sapiens ? - ? 89 3.4.22.61 additional information CD95 and TNFR-1 death receptors initiate apoptosis by recruiting FLICE/MACH, which represents the apical triggering member of the protease death cascade and a target for the cell death inhibitor CrmA Homo sapiens ? - ? 89 3.4.22.61 additional information the initiator caspase-8 activates other downstream caspases that are incapable of autocatalytic processing and activation Homo sapiens ? - ? 89 3.4.22.61 additional information caspase 8 may not only play a role in initiating proapoptotic cascades through activation of downstream caspases but also by amplifying the amount of activated CD95 receptors Rattus norvegicus ? - ? 89 3.4.22.61 additional information caspase-8 inhibits androgen receptor transcriptional activity by disrupting androgen receptor amino-terminal and carboxy-terminal interaction and inhibiting androgen induced androgen receptor nuclear localization Homo sapiens ? - ? 89 3.4.22.61 additional information caspase-8 is dispensable for B-cell development, but its loss in B cells results in attenuated antibody production upon in vivo viral infection. Important role for caspase-8 in maintaining B-cell survival following stimulation of the Toll-like receptor (TLR)2, -3, and -4. In response to TLR4 stimulation, caspase-8 is recruited to a complex containing IKKalphabeta, and its loss results in delayed NFkappaB nuclear translocation and impaired NFkappaB transcriptional activity. Caspase-8 is required forTLRsignaling and in the regulation of NFkappaB function Mus musculus ? - ? 89 3.4.22.61 additional information caspase-8 is possibly involved in the apoptotic cell death in batch and fed-batch cultures of CHO cells Cricetulus griseus ? - ? 89 3.4.22.61 additional information caspase-8 participates in regulation of the cellular response to infection and injury. It does so by affecting various cellular functions, including cell death, cell proliferation, and induction of inflammation Mus musculus ? - ? 89 3.4.22.61 additional information CD95L initiates a rapid caspase 8-dependent endosomal acidification, which triggers ceramide-dependent ROS formation as an upstream event of trafficking of intracellularly stored CD95 to the plasma membrane. A rapid caspase 8 activation in response to CD95L signals to intracellularly stored CD95, which becomes activated and targeted to the plasma membrane Rattus norvegicus ? - ? 89 3.4.22.61 additional information endothelial cell apoptosis induced by bacteria-activated platelets requires caspase-8 and -9 and generation of reactive oxygen species Bos taurus ? - ? 89 3.4.22.61 additional information role of caspase-8 in the apoptotic signal pathway Danio rerio ? - ? 89 3.4.22.61 additional information TLR2- and caspase-8-mediated microglial apoptosis constitutes an autoregulatory mechanism that limits group B Streptococcus-induced overactivation of the innate immune system in the central nervous system Mus musculus ? - ? 89 3.4.22.61 additional information activation of caspase-8 by glycogen synthase kinase-3 inhibitors can overcome the striking resistance to tumor necrosis factor-related apoptosis-inducing ligand, TRAIL, diplayed by hepatocellular carcinoma cells in contrast to normal heptocytes, overview Homo sapiens ? - ? 89 3.4.22.61 additional information apoptosis in ischemic hearts occurs through the receptor-mediated extrinsic caspase-8 apoptotic pathway as opposed to the mitochondrial caspase-3 pathway, overview Mus musculus ? - ? 89 3.4.22.61 additional information apoptotic cell deathin LM3 cells is characterized by the activation of caspase-8, -9 and -3, by an increment in the expression levels of the proapoptotic protein Bax and by the release of cytochrome c to cytosol Mus musculus ? - ? 89 3.4.22.61 additional information caspase 8 activation induced by C5a leads to cell death if protein synthesis of antiapoptotic proteins are blocked Homo sapiens ? - ? 89 3.4.22.61 additional information caspase 8 is an initiator caspase that plays an important role in the Fas-Fas ligand pathway Homo sapiens ? - ? 89 3.4.22.61 additional information caspase family proteases are key proteins in apoptotic signaling pathways, which are activated in both the death receptor-mediated and the mitochondria-mediated apoptosis pathways Homo sapiens ? - ? 89 3.4.22.61 additional information caspase-3 is an initiator caspase. Increased caspase-8 activation is involved in initiation of apoptosis, inhibition of caspase-8 impairs Leptospira interrogans-induced caspase-3 and -6 activation, as well as PARP and lamin A/C cleavage and apoptosis, overview. Leptospira interrogans-induced apoptosis in macrophages is mediated by caspase-3 and -6 activation through a FADD-caspase-8-dependent pathway, independently of mitochondrial cytochrome c-caspase-9-dependent signaling, regulation, overview Homo sapiens ? - ? 89 3.4.22.61 additional information caspase-3 is an initiator caspase. Increased caspase-8 activation is involved in initiation of apoptosis, inhibition of caspase-8 impairs Leptospira interrogans-induced caspase-3 and -6 activation, as well as PARP and lamin A/C cleavage and apoptosis, overview. Leptospira interrogans-induced apoptosis in macrophages is mediated by caspase-3 and -6 activation through a FADD–caspase-8-dependent pathway, independently of mitochondrial cytochrome c–caspase-9-dependent signaling, regulation, overview Mus musculus ? - ? 89 3.4.22.61 additional information caspase-8 acts in apoptosis via the death receptor pathway Mus musculus ? - ? 89 3.4.22.61 additional information caspase-8 expression is reduced in B-cell chronic lymphocytic leukemia Homo sapiens ? - ? 89 3.4.22.61 additional information caspase-8 is a executioner or downstream caspase. Apoptosis induced by PBOX-21/STI571 results in activation of caspase-8, cleavage of PARP and Bcl-2, upregulation of the pro-apoptotic protein Bim and a downregulation of Bcr-Abl, important role for caspase-8 in the apoptotic pathway, overview Mus musculus ? - ? 89 3.4.22.61 additional information caspase-8 is a pro-apoptotic caspase, whose expression is increased in the orbito-frontal cortex 14 days after spared nerve injury of the sciatic nerve, prevented by ozone, regulation, overview Mus musculus ? - ? 89 3.4.22.61 additional information caspase-8 is activated by the death receptor pathway leading to apoptosis. Human herpesvirus HHV-6A-induced apoptosis is associated with activation of caspase-8, caspase-9, and caspase-3, suggesting the involvement of death receptor and mitochondrial signaling pathways, overview. HHV-6 differentially influences the functions of naive T cells and different subsets of memory CD4+ and CD8+ T cells, which in part may be due to differential susceptibility to HHV-6A-induced apoptosis, overview Homo sapiens ? - ? 89 3.4.22.61 additional information caspase-8 is activated downstream of the death receptor signaling or via death receptor-independent pathway Homo sapiens ? - ? 89 3.4.22.61 additional information caspase-8 is an initiator caspase. Procaspase-8 activation is essentially involved in apoptosis induced by selected nutritional free fatty acids, mechanisms, overview Homo sapiens ? - ? 89 3.4.22.61 additional information caspase-8 is involved in apoptosis in multiple myeloma and is the main initiator caspase in the tumor necrosis factor-related apoptosis-inducing pathway overview. c-FLIPL, is the main endogenous regulator of caspase-8 activation, increases with bortezomib treatment but the combination of Apo2L/TRAIL and bortezomib led to a decrease of both FLIP isoforms, regulation, overview Homo sapiens ? - ? 89 3.4.22.61 additional information caspase-8 is involved in apoptosis, but does not require caspase recruitment domain, ARC, which prevents Bax translocation to the mitochondrium and thereby blocks the activation of the mitochondrial apoptotic death pathway in a t-Bid and caspase-8-independent manner, overview Rattus norvegicus ? - ? 89 3.4.22.61 additional information caspase-8 is involved in apoptosis, ischemia upregulates cytoplasmic adaptor protein Fas-associated Fas and Fas-associated death domain, FADD, expression, and increases caspase-8 and -3 activities in ovariectomy female mouse cortex, which are significantly attenuated by estradiol Mus musculus ? - ? 89 3.4.22.61 additional information caspase-8, an initiator caspase, is not involved in MDA-MB-231 apoptotic cell death, overview. Caspase-8 is activated when procaspase-8 is cleaved subsequently from the recruitment of Fas associated protein with death domain, FADD, to the death-effector domain site of procaspase-8 during the oligomerization of death receptor and its ligand Homo sapiens ? - ? 89 3.4.22.61 additional information caspases 3, 8 and 9 are essential to rhein-induced apoptosis, inhibitors of caspases 3, 8 and 9 are efficiently blocked by rhein-induced apoptosis in TNF-alpha-treated human aortic smooth muscle cells, overview Homo sapiens ? - ? 89 3.4.22.61 additional information caspases are a family of aspartate-specific cysteine proteases responsible for the biochemical and morphological changes that occur during the execution phase of apoptosis, model of the intrinsic pathway: caspase-9, the apical caspase, directly processes and activates the effector caspases, caspase-3 and -7, and then active caspase-3, but not caspase-7, processes caspase-2 and -6, and subsequently the activated caspase-6 processes caspase-8 and -10. Caspase-9 but not -8 is required for etoposide-induced processing of caspase-2 and -6. Caspase processing pathways and regulation, overview Homo sapiens ? - ? 89 3.4.22.61 additional information extrinsic and intrinsic apoptosis induced by equol in human breast cancer MDA-MB cells does not involve caspase-8 activation of receptor-mediated apoptosis, overview Homo sapiens ? - ? 89 3.4.22.61 additional information Fas ligand, a type II transmembrane protein expressed on the surface of cells, induces apoptotic cell death by binding to its receptor Fas, resulting in recruitment of the Fas-associated death domain protein and caspase 8 zymogens to the receptor and the formation of the death-inducing signalling complex, after which the caspases cascade can be activated. Defects in the Fas/FasL apoptotic signalling pathway provide a survival advantage to cancer cells and may be implicated in tumorigenesis Homo sapiens ? - ? 89 3.4.22.61 additional information Fas-associated death domain-like IL-1beta-converting enzyme inhibitory protein, c-FLIP, can suppress Fas-mediated apoptosis by inhibition of caspase-8 activation. Caspase-8 is active via the death receptor-dependent pathway, or extrinsic pathway, complex formation and mechanism, overview Homo sapiens ? - ? 89 3.4.22.61 additional information harmol activates caspase-8 to 334% and induces apoptosis by caspase-8 activation independently on Fas/Fas ligand interaction in human lung carcinoma H-596 cells, but not in H-596, H-226, and A-549 cells Homo sapiens ? - ? 89 3.4.22.61 additional information homocysteine-mediated EPC toxicity is due to apoptosis involving caspase-8, cytochrome c release, and caspase-3 activation, overview Homo sapiens ? - ? 89 3.4.22.61 additional information initial activation of caspase-8 causes degradation of glutaredoxin-1, resulting in S-glutathionylation of Fas at cysteine 294, which subsequently enhances binding of FasL, aggregation of Fas, accumulation of Fas in lipid rafts, DISC assembly, and further activation of caspases, causing a propagation of apoptotic cell death. activation of caspases is required for degradation of glutaredoxin-1 and S-glutathionylation of Fas, engagement of Fas causes a rapid activation of caspase-8. Overexpression of Grx1 prevents increases in S-glutathionylation of Fas and attenuates caspase activation and apoptosis in response to receptor ligation. Cleaved caspase-8 and -3 demonstrate an association between active caspases and Grx1 in cells after ligation of Fas, whereas in control cells, these associations are not observed, regulation, overview Homo sapiens ? - ? 89 3.4.22.61 additional information interferon regulatory factor 5, IRF-5, promotes apoptosis upon signaling through tumor necrosis factor-related apoptosis-inducing ligand, TRAIL, death receptors, DR. IRF-5 is involved in DR signaling upstream of caspase-8 and induces caspase-8 activation, mechanisms, overview Homo sapiens ? - ? 89 3.4.22.61 additional information involvement of lipid raft aggregates containing recruited Fas/CD95 death receptor, Fas-associated death domain-containing protein, FADD, and procaspase-8 in the induction of apoptosis in human T-cell leukemia Jurkat cells by the antitumor drug edelfosine. Specific inhibition of caspase-8 prevents the apoptotic response triggered by edelfosine Homo sapiens ? - ? 89 3.4.22.61 additional information LRRK2-induced neuronal death is caspase-8-dependent. Fas death domain, FADD, recruits caspase-8 to LRRK2. FADD transduces death signals by binding to ligand-activated Fas via its DD and recruiting and activating caspase-8 via its death-effector domain, DED. The Parkinson disease protein leucine-rich repeat kinase 2 transduces death signals via Fas-associated protein with death domain and caspase-8 in a cellular model of neurodegeneration. In primary neuronal culture LRRK2-mediated neurodegeneration is prevented by the functional inhibition of FADD or depletion of caspase-8, two key elements of the extrinsic cell death pathway, overview Homo sapiens ? - ? 89 3.4.22.61 additional information methotrexate-induced apoptosis does not involve activation of caspase-8, but of caspase-9, overview. Caspase-8 is recruited to an apoptosis-inducing signaling complex when apoptotic receptors are oligomerized after binding of specific ligands. Active caspase-8 can either act directly on downstream executioner caspases, or indirectly on mitochondria Homo sapiens ? - ? 89 3.4.22.61 additional information mRNA and protein level of caspase-8 is closely related to cell apoptosis by a death ligand/receptor-dependent apoptosis pathway, increased by L-carnitine treatment, overview Mus musculus ? - ? 89 3.4.22.61 additional information netrin-1 siRNA-induced H-358 cell death is mediated by caspase-3 and -9 activities, but not by caspase-8 activity Homo sapiens ? - ? 89 3.4.22.61 additional information radiation-induced sensitization of hepatocytes to TNF-alpha-mediated apoptosis additionally requires changes upstream of caspase-8 activation, regulation of caspase-8 and apoptosis in hepatocytes, overview Rattus norvegicus ? - ? 89 3.4.22.61 additional information stem-cell-like glioma cells are resistant to tumour necrosis factor -related apoptosis-inducing ligand, TRAIL/Apo2L and exhibit down-regulation of caspase-8 by promoter methylation Homo sapiens ? - ? 89 3.4.22.61 additional information The cysteine protease caspase-8 plays an essential role in apoptosis induced by death receptors, caspase-8 mediates mitochondrial release of pro-apoptotic proteins in a manner independent of its proteolytic activity in apoptosis induced by the protein synthesis inhibitor acetoxycycloheximide in human leukemia Jurkat cells. Bid is cleaved not by caspase-8 but by other caspases in Ac-CHX-treated cells and is not involved in mitochondrial release of proapoptotic proteins Homo sapiens ? - ? 89 3.4.22.61 additional information caspases contain a reactive cysteine critical for enzymatic activity. Increased S-glutathionylation of Fas, caspase-8 activity, and cell death in cells lacking Grx1 Homo sapiens ? - ? 89 3.4.22.61 additional information Arg-Gly-Asp-Ser directly and specifically binds pro-caspase-8 Homo sapiens ? - ? 89 3.4.22.61 additional information caspase-4 activation requires the action of upstream initiator components such as caspase-8 Homo sapiens ? - ? 89 3.4.22.61 additional information FADD-like interleukin-1beta-converting enzyme-inhibitory protein is an antagonist of caspases-8 Homo sapiens ? - ? 89 3.4.22.61 additional information caspase-8 is involved in activation of acid sphingomyelinase induced by TNF, but caspase-8 does not display firm association neither with caspase-7 nor with A-SMase, overview. Direct binding of caspase-8 to TNF-R1 on internalized receptosomes Homo sapiens ? - ? 89 3.4.22.61 additional information caspase-8 performs self-cleavage to give the processed active dimer. Within the caspase-8/FLIPL heterodimer, caspase-8 prefers to process FLIPL over itself Mus musculus ? - ? 89 3.4.22.61 additional information caspase-8 performs self-cleavage to give the processed active dimer. Within the caspase-8/FLIPL heterodimer, caspase-8 prefers to process FLIPL over itself Homo sapiens ? - ? 89 3.4.22.61 additional information generation of an NCtagged sTMP library and screening for CASP8 substrates, CASP8-cleavable sTMPs in the sTMP library, overview. Determination of cleavage sites by amino acid sequencing, consensus-type sequences are X-E/Q-X-D;-G/S, with X being any amino acid Homo sapiens ? - ? 89 3.4.22.61 additional information pro-caspase-6, linker, is a poor substrate fpr caspase-8 Mus musculus ? - ? 89 3.4.22.61 additional information the substrate cleft is closed in the monomeric zymogen, whereas the cleft is accessible for substrate binding in both dimers, binding structure, overview Mus musculus ? - ? 89 3.4.22.61 additional information the substrate cleft is closed in the monomeric zymogen, whereas the cleft is accessible for substrate binding in both dimers, binding structure, overview Homo sapiens ? - ? 89 3.4.22.61 additional information caspase-8 very weakly cleaves nuclear export signal-DEVDR Homo sapiens ? - ? 89 3.4.22.61 additional information apoptotic cell deathin LM3 cells is characterized by the activation of caspase-8, -9 and -3, by an increment in the expression levels of the proapoptotic protein Bax and by the release of cytochrome c to cytosol Mus musculus BALB/c ? - ? 89 3.4.22.61 additional information the enzyme is indispensable for Fas-mediated apoptotic signaling Mus musculus 129/SvJ ? - ? 89 3.4.22.61 additional information apoptosis in ischemic hearts occurs through the receptor-mediated extrinsic caspase-8 apoptotic pathway as opposed to the mitochondrial caspase-3 pathway, overview Mus musculus C57BL6 ? - ? 89 3.4.22.61 N-acetyl-IETD-4-nitroanilide + H2O - Mytilus galloprovincialis N-acetyl-IETD + 4-nitroaniline - ? 432173 3.4.22.61 N-acetyl-IETD-4-nitroanilide + H2O - Mytilus coruscus N-acetyl-IETD + 4-nitroaniline - ? 432173 3.4.22.61 N-acetyl-IETD-4-nitroanilide + H2O - Mytilus galloprovincialis N-acetyl-IETD + 4-nitroaniline + H2O - ? 433978 3.4.22.61 N-acetyl-IETD-4-nitroanilide + H2O - Mytilus coruscus N-acetyl-IETD + 4-nitroaniline + H2O - ? 433978 3.4.22.61 N-acetyl-IETD-4-trifluoromethylcoumarin 7-amide + H2O - Mus musculus N-acetyl-IETD + 7-amino-4-trifluoromethylcoumarin - ? 418871 3.4.22.61 N-acetyl-IETD-4-trifluoromethylcoumarin 7-amide + H2O - Homo sapiens N-acetyl-IETD + 7-amino-4-trifluoromethylcoumarin - ? 418871 3.4.22.61 nuclear export signal-LQTDG + H2O - Homo sapiens ? - ? 432257 3.4.22.61 p21-activated kinase 2 + H2O separates the N-terminal regulatory domain from the C-terminal catalytic domain Homo sapiens ? - ? 382518 3.4.22.61 p28Bap31 + H2O - Homo sapiens additional information the p20 cleavage product derives from the NH2 terminus of p28 ? 361974 3.4.22.61 parkin + H2O cleavage at Asp126-Ser127 Homo sapiens ? - ? 361975 3.4.22.61 parkin + H2O cleavage at Asp126-Ser127. Caspase-1 and caspase-8 dependent parkin cleavage in sporadic Parkinson‘s disease may play an important role in the degenerative process by initiating a vicious circle that leads to the accumulation of toxic parkin substrates, e.g. alpha-synuclein Homo sapiens ? - ? 361975 3.4.22.61 pro-caspase-3 + H2O - Homo sapiens caspase-3 + ? - ? 361960 3.4.22.61 pro-caspase-3 + H2O caspase-3 is activated through caspase-8 during H2O2-induced apoptosis in HeLa cells Homo sapiens caspase-3 + ? - ? 361960 3.4.22.61 procaspase-10 + H2O the cleavage sequence in procaspase-10, catalytically inactive C285A mutant, for caspase-8 is IEAD/A Mus musculus caspase-3 + ? - ? 419012 3.4.22.61 procaspase-3 + H2O - Mus musculus caspase-3 + ? - ? 361976 3.4.22.61 procaspase-3 + H2O - Homo sapiens caspase-3 + ? - ? 361976 3.4.22.61 procaspase-3 + H2O pro-caspase-3 is a major physiologic target of caspase-8 Homo sapiens caspase-3 + ? - ? 361976 3.4.22.61 procaspase-3 + H2O activation Mus musculus caspase-3 + ? - ? 361976 3.4.22.61 procaspase-3 + H2O activation Homo sapiens caspase-3 + ? - ? 361976 3.4.22.61 procaspase-3 + H2O activation of effector caspase-3 by the initiator caspase-8 Homo sapiens caspase-3 + ? - ? 361976 3.4.22.61 procaspase-3 + H2O cleavage of caspases 3 and 6 by caspase-8 results in apoptosis Homo sapiens caspase-3 + ? - ? 361976 3.4.22.61 procaspase-3 + H2O in some cells, active caspase-8 is sufficient to activate caspase-3 directly. In other cells, however, caspase-8 indirectly mediates caspase-3 activation by cleaving the proapoptotic Bcl-2 family member Bid, which induces mitochondrial cytochrome c release Mus musculus caspase-3 + ? - ? 361976 3.4.22.61 procaspase-3 + H2O in some cells, active caspase-8 is sufficient to activate caspase-3 directly. In other cells, however, caspase-8 indirectly mediates caspase-3 activation by cleaving the proapoptotic Bcl-2 family member Bid, which induces mitochondrial cytochrome c release Homo sapiens caspase-3 + ? - ? 361976 3.4.22.61 procaspase-3 + H2O procaspase-8 activation in the death-inducing signalling complex, DISC, leads to cleavage of procaspase-3 and engagement of the cellular machinery associated with the type I extrinsic apoptotic pathway Homo sapiens caspase-3 + ? - ? 361976 3.4.22.61 procaspase-3 + H2O the cleavage sequence in procaspase-3, catalytically inactive C285A mutant, for caspase-8 is IETD/S Mus musculus caspase-3 + ? - ? 361976 3.4.22.61 procaspase-3 + H2O - Homo sapiens ? - ? 362371 3.4.22.61 procaspase-3 + H2O results in a p11 and p20 fragment Homo sapiens ? - ? 362371 3.4.22.61 procaspase-3 + H2O caspase-8 induces apoptosis by directly activating caspase-3, which in turn causes the characteristic features of apoptosis, including DNA fragmentation and cell death Homo sapiens ? - ? 362371 3.4.22.61 procaspase-3 + H2O direct activation by caspase-8 in type I cells Rattus norvegicus active caspase-3 + ? - ? 402871 3.4.22.61 procaspase-3 + H2O activation by caspase-8 Rattus norvegicus active caspase-3 + ? - ? 402871 3.4.22.61 procaspase-6 + H2O activation Homo sapiens caspase-6 + ? - ? 402872 3.4.22.61 procaspase-6 + H2O cleavage of caspases 3 and 6 by caspase-8 results in apoptosis Homo sapiens caspase-6 + ? - ? 402872 3.4.22.61 procaspase-7 + H2O the cleavage sequence in procaspase-7, catalytically inactive C285A mutant, for caspase-8 is IQAD/S Mus musculus caspase-3 + ? - ? 419013 3.4.22.61 procaspase-8 + H2O caspase-8 is initially synthesized as a single-chain zymogen, procaspase-8, and activated by autocleavage at proteolytic sites Asp126, Asp216, Asp374, and Asp384 after recruitment to DISCs by N-terminal two tandem DEDs of procaspase-8. The proximity-driven dimerization of procaspase-8 is attributable to initiate autocleavage of procaspase-8 involving intra-dimeric and inter-dimeric attack. Dimerized procaspase-8 which achieves enzymatical competency specifically processes one another, while mature caspase-8 can cleave effector caspases and some other substrates. Dramatical conformation changes of the linker region undergo in order to bring cleavage sites, Asp374 and Asp384, to the vicinity of catalytic residue Cys283 from other protomer during dimerization of procaspase-8. Separation of the large and small subunit after intra-dimeric cleavage in the linker region between the large and small subunit renders the linker region between the large subunit and the prodomain of caspase-8 susceptible for the further inter-dimeric cleavage Homo sapiens caspase-8 + ? the C- and N-terminal end, of linker region are released with cleavage at Asp374 and Asp384 before separation of the large and small subunit ? 393338 3.4.22.61 procaspase-8 + H2O the autocleavage sequences of procaspase-8 monomers are VETD/S and LEMD/L, and of procaspase-8 dimers VETD/S and LEMD/L Mus musculus caspase-8 + ? - ? 393338 3.4.22.61 receptor-indicating protein + H2O separates the N-terminal kinase from the C-terminal death domain Homo sapiens ? - ? 382713 3.4.22.61 receptor-indicating protein + H2O separates the N-terminal kinase from the C-terminal death domain Mus musculus ? - ? 382713 3.4.22.61 RIPK1 + H2O - Homo sapiens ? - ? 418059 3.4.22.61 RIPK1 + H2O Lys63-linked RIPK1 ubiquitylation is required to render RIPK1 susceptible to caspase 8-mediated cleavage, the mechanism by which RIPK1 signalling is suppressed in this context Homo sapiens ? - ? 418059 3.4.22.61 RIPK1 + H2O the cleavage sequence for caspase-8 is LQLD/C Mus musculus ? - ? 418059 3.4.22.61 Tx + H2O - Homo sapiens ? - ? 361969 3.4.22.61 vezatin + H2O cleaved at Asp655 Homo sapiens ? - ? 418120 3.4.22.61 Yama + H2O - Homo sapiens ? - ? 361967