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CASP1 — CASP8

Protein-Protein interactions - manually collected from original source literature:

Studies that report less than 10 interactions are marked with *

• IRef Biogrid Interaction: CASP8 — CASP1 (direct interaction, enzymatic study) Srinivasula et al., Proc Natl Acad Sci U S A 1996

Text-mined interactions from Literome

Zhuang et al., Exp Cell Res 1999 : Caspase-8 mediates caspase-3 activation and cytochrome c release during singlet oxygen induced apoptosis of HL-60 cells
Raoul et al., J Cell Biol 1999 : Motoneurons resistant to Fas activation expressed high levels of FLICE-inhibitory protein (FLIP) , an endogenous inhibitor of caspase-8 activation
Okamoto et al., Rheumatology (Oxford) 2000 (Arthritis, Rheumatoid) : Caspase-8-specific inhibitor suppressed the activation of caspase-3 after Fas ligation on RA synoviocytes
de Bilbao et al., Neuroscience 2000 (Facial Nerve Injuries) : Similar results were obtained in interleukin-1 beta converting enzyme-deficient and wild-type mice, indicating that the interleukin-1 beta converting enzyme may not be required for caspase 3 activation
Hernandez et al., Surgery 2001 (Colonic Neoplasms) : Western blots were performed to assess intracellular expression of Flice-like inhibitory protein (FLIP) , a caspase inhibitor
Thomas et al., Surgery 2002 (Pancreatic Neoplasms) : FLICE-like inhibitory protein (FLIP) , an inhibitor of caspase-8 , ( also known as FLICE ) is regulated by the transcription factor nuclear factor-kappaB (NF-kappaB) and can contribute to TRAIL resistance
Xu et al., Anticancer Res 2003 (Pancreatic Neoplasms) : Caspase-8 and -3 activities were increased by TRAIL treatment and apoptosis was largely blocked by caspase-8 and -3 inhibitors
Fujii et al., Infect Immun 2003 : Caspase-8 is known to activate Bid, and a specific inhibitor of caspase-8 prevented the mitochondrial damage
Yang et al., Nephron. Experimental nephrology 2004 (Necrosis) : Here we evaluate three caspase inhibitors : B-D-FMK ( pan caspase inhibitor ), Z-DEVDFMK ( predominantly Caspase-3 inhibitor ) and Z-VAD-FMK ( predominantly Caspase-1 and -3 inhibitor ) to ameliorate apoptosis induced by cisplatin in rat proximal tubular ( RPT ) cells
Messerli et al., Neoplasia (New York, N.Y.) 2004 (Glioma) : The specificity of this probe for caspase-1 is supported by various lines of evidence : 1 ) activation by purified caspase-1, but not another caspase in vitro ; 2 ) activation of the probe by infection of cells with a herpes simplex virus amplicon vector ( HGC-ICE-lacZ ) expressing a catalytically active caspase-1-lacZ fusion protein; 3 ) inhibition of HGC-ICE-lacZ vector induced activation of the probe by coincubation with the caspase-1 inhibitor YVAD-cmk, but not with a caspase-3 inhibitor ; and 4 ) activation of the probe following standard methods of inducing apoptosis with staurosporine, ganciclovir, or ionizing radiation in culture
Perchellet et al., Anticancer Drugs 2004 : Caspase-2 and -8 may both act upstream of mitochondria to promote Cyt c release, but caspase-2 is already maximally activated 6 h after 4 microM DAU or TT13 treatments, whereas DAU- or TT-induced caspase-8 and -9 activities peak at 9 h. Pre-treatments with 15 microM of the caspase-2 inhibitor benzyloxycarbonyl ( z ) -Val-Asp-Val-Ala-Asp ( VDVAD ) -fluoromethyl ketone ( fmk ) totally block DAU- and TT13 induced caspase-2, -8 and -9 activities, whereas pre-treatments with 15 microM of the caspase-8 inhibitor z-Ile-Glu-Thr-Asp ( IETD ) -fmk prevent DAU and TT13 from inducing caspase-8 activities without affecting their caspase-2- and -9-inducing activities, suggesting that the induction of apical caspase-2 activity by these drugs may be a critical upstream event required for the activation of other downstream caspases, including caspase-9 and the mitochondrial amplification loop through caspase-8
Maitra et al., Crit Care Med 2005 (Sepsis) : Caspase-8 activates caspase-3 , which in turn degrades fibronectin and focal adhesion kinase and leads to disruption of hepatic architecture and integrity
Guo et al., Cell Death Differ 2006 : Caspase-1 activation of caspase-6 in human apoptotic neurons
Miyao et al., Otol Neurotol 2006 (Cholesteatoma, Middle Ear) : Caspase-8 , which is activated by the induction of tumor necrosis factor-alpha, leads to activation of caspase-3 , which activates apoptotic nucleases
Wu et al., Cell Mol Life Sci 2006 : Caspase-8 played important roles in the activation of caspase-3 and induction of apoptosis, whereas the role of the caspase-9 was limited
Yamaguchi et al., Biochim Biophys Acta 2006 (Carcinoma, Hepatocellular...) : We demonstrated that Adv-Casp8 increased expression of active forms of caspase-8 in MOI dependent manner
Faragher et al., Mol Biol Cell 2007 (Breast Neoplasms) : Caspase-8 activates cytoplasmic caspase-7 , which is likely to be the primary caspase responsible for cleavage of CENP-C and INCENP, a key chromosomal passenger protein
Pesakhov et al., Nutr Cancer 2010 (Leukemia, Myeloid, Acute) : Caspase-8 inhibition abrogated Bid cleavage and strongly reduced caspase-9 activation, suggesting that the cross-talk mechanism mediated by caspase-8 dependent Bid cleavage can contribute to the activation of the intrinsic apoptotic pathway by curcumin + carnosic acid
Fang et al., J Immunol 2011 (Disease Resistance...) : Caspase-1 activation was partially impaired in NLRP3 ( -/- ) macrophages, whereas knockdown and knockout of AIM2 resulted in a clear decrease in caspase-1 activation in response to S. pneumoniae
Moujalled et al., Cell Death Differ 2012 : In mouse embryonic fibroblasts, neither caspase-8 nor cellular FLICE-inhibitory protein (FLIP) is necessary for TNF to activate NF-?B, but caspase-8 is required for TNF to cause cell death, and induction of FLIP by NF-?B is required to prevent it
LaRock et al., Cell Host Microbe 2012 : Caspase-1 activation antagonizes Yersinia survival in vivo, and consequently YopM inhibition of caspase-1 is required for Yersinia pathogenesis
Wang et al., Cell 1998 (Shock, Septic) : Murine caspase-11 , an ICE interacting protease, is essential for the activation of ICE ... Furthermore, we found that pro-caspase-11 physically interacts with pro-ICE in cells, and the expression of casp-11 is essential for activation of ICE ... Our data suggest that caspase-11 is a component of ICE complex and is required for the activation of ICE
Sata et al., J Biol Chem 1998 : Here, we show that endothelial cell apoptosis by OxLDL and LPC-C16 : 0 was dose dependent and correlated with down-regulation of FLICE-inhibitory protein (FLIP) , an intracellular caspase inhibitor
Yamashita et al., Blood 1999 : Caspase-8 activated caspase-3 and T18 in neutrophil cytoplasmic extracts