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Human Caspase 8 Protein expressed in Escherichia coli (E. coli) - ABIN2487286
Appukuttan, Kasseckert, Micoogullari, Flacke, Kumar, Woste, Abdallah, Pott, Reusch, Ladilov: Type 10 adenylyl cyclase mediates mitochondrial Bax translocation and apoptosis of adult rat cardiomyocytes under simulated ischaemia/reperfusion. in Cardiovascular research 2012
Show all 6 Pubmed References
Human Caspase 8 Protein expressed in Escherichia coli (E. coli) - ABIN2688834
Nicholson, Ali, Thornberry, Vaillancourt, Ding, Gallant, Gareau, Griffin, Labelle, Lazebnik: Identification and inhibition of the ICE/CED-3 protease necessary for mammalian apoptosis. in Nature 1995
Show all 3 Pubmed References
Furthermore, while activities to process procaspase-8 and procaspase-9 appeared in SAMDC (show AMD1 Proteins)-overexpressed apoptotic embryos, the activity to process procaspase-8 did not appear in p53 (show TP53 Proteins)-overexpressed apoptotic embryos.
tail regression at metamorphosis implicates an apoptotic pathway inducible by T(3) hormone in an organ autonomous manner and involving the cell death executioners BH3 interacting domain death agonist (show BID Proteins) and Caspases-2 and -8
These data demonstrate that caspase-8 functions in synovial antigen-presenting cells to regulate the response to inflammatory stimuli by controlling RIPK3 (show RIPK3 Proteins) action, and this delicate balance maintains homeostasis within the joint.
Results illustrate the temporal and spatial activation of caspase-8 and -3 in microglia/macrophages occurring upon ischemic stroke and suggest that the expression of these caspases could be used in neuropathological diagnostic work.
inhibition of TAK1 (show NR2C2 Proteins) triggered two caspase 8 activation pathways through the induction of RIP1 (show RALBP1 Proteins)-FADD (show FADD Proteins)-caspase 8 complex as well as FLIP cleavage/degradation.
this study identifies a crucial role for caspase-8 in the development of allergic airway inflammation
Prolonged treatment of human PMNs or mice bone marrow derived neutrophils (BMDN) with nitric oxide led to enhanced reactive oxygen species generation, caspase-8/caspase-3 (show CASP3 Proteins) cleavage, reduced mitochondrial membrane potential and finally cellular apoptosis.
caspase-8-dependent apoptosis was linked to hepatocellular carcinoma development.
Statistically significant increases in the expression of Fas (show FAS Proteins) and caspase-8 were observed, along with other molecules involved in the extrinsic apoptotic pathway such as Dapk1 (show DAPK1 Proteins), Traf3 (show TRAF3 Proteins), Tnsf12, Tnfrsf1A (show TNFRSF1A Proteins) and Ripk1 (show RIPK1 Proteins).
Results suggest that caspase-8 could regulate receptor-interacting protein 3 (RIP3 (show RIPK3 Proteins))-mediated necroptosis.
we show that caspase-8 activity promotes cell-intrinsic cytokine expression, independent of its role in cell death in response to Yersinia infection
Data indicate that NLRC4 (show NLRC4 Proteins) activation in Intestinal epithelial cells (IECs) leads to cell expulsion and IL-18 (show IL18 Proteins) release, and implicate Caspase-8 in NLRC4 (show NLRC4 Proteins) inflammasome responses in vivo by generation of doubly deficient in Caspase-1 (show CASP1 Proteins) and Caspase-8.
Caspase-3 (show CASP3 Proteins) and -8 and annexin V (show ANXA5 Proteins) may serve as diagnostic markers in Ovarian cancer , also explained that the decrement in control of the S phase in the cell cycle may considered one of the significant factors in the development of ovarian tumors
High CASP8 expression is associated with Colorectal Cancer.
Sleep duration is associated with plasma caspase-8. Caspase-8 independently predicts diabetes mellitus years before disease onset and modifies the effect of sleep duration on incident diabetes mellitus.
Caspase-8 and Caspase-3 (show CASP3 Proteins) expressions in tumor tissues are novel candidate prognostic markers for colorectal cancer patients
Reactive oxygen species-induced cleavage of NHLRC2 by caspase-8 leads to apoptotic cell death in the HCT116 human colon cancer cells.
this study is the first report on reduced expression of CASP8 in breast cancer versus adjacent normal tissues.
The polymorphisms of CASP8, rs7608692, and haplotype AGAACAG correlated with neutropenia toxicity. The haplotype GGGGAAA was associated with thrombocytopenia toxicity. We conclude that the polymorphisms of CASP8 contribute to the prognosis of advanced lung adenocarcinoma and influence the quality of life and survival.
These results indicated that cMyc (show MYC Proteins) and Fas (show FAS Proteins) regulated the sensitivity of A549 cells to irradiation by regulating caspase8-mediated Bid (show BID Proteins) activation and the subsequent association with the mitochondrial pathway of apoptosis.
The caspase-8/Bid (show BID Proteins)/cytochrome c (show CYCS Proteins) axis links signals from death receptors to mitochondrial reactive oxygen species production.
miR (show MLXIP Proteins)-21 was elevated in osteosarcoma, and overexpression of miR (show MLXIP Proteins)-21 suppressed apoptosis via targeting caspase 8.
S. aureus-induced apoptosis in bovine mammary epithelial cells apoptosis was mitigated by caspase-3 (show CASP3 Proteins) and caspase-8 inhibitors, suggesting that apoptosis is initiated via caspase-8 activation.
Endothelial cell apoptosis by H. somnus-activated platelets required activation of both caspase-8 and caspase-9 (show CASP9 Proteins).
Nitric oxide-dependent increase in caspase-8 mRNA levels is associated with phosphorylation of STAT-1 (show STAT1 Proteins) at Ser (show SIGLEC1 Proteins)-727 and STAT1 (show STAT1 Proteins) binding to the caspase-8 promoter in cultured lung endothelial cells.
Data show that cysteine significantly reduced the expression of pro-inflammatory cytokines, including TNF-alpha (show TNF Proteins), IL-6 (show IL6 Proteins), IL-12p40, IL-1beta (show IL1B Proteins), and resulted in increased expression of the apoptosis initiator caspase-8 and bcl2L1 (show BCL2L1 Proteins).
Induction of apoptosis through targeted activation of caspase (show CASP3 Proteins) by tamoxifen (ATTAC(TM)) further expands the repertoire of genetic tools for conditional interrogation of cellular functions.
Targeted gene knockdown of TNFRSF1B (show TNFRSF1B Proteins) in zebrafish embryos results in the induction of a caspase-8, caspase-2 (show CASP2 Proteins) and P53 (show TP53 Proteins)-dependent apoptotic program in endothelial cells that bypasses caspase-3 (show CASP3 Proteins).
These results show that zebrafish casp8 has a structure and function similar to mammalian CASP8 orthologs and the role of caspase-8 in the apoptotic signal pathway has been conserved over at least 450 million years of vertebrate evolution.
This gene encodes a member of the cysteine-aspartic acid protease (caspase) family. Sequential activation of caspases plays a central role in the execution-phase of cell apoptosis. Caspases exist as inactive proenzymes composed of a prodomain, a large protease subunit, and a small protease subunit. Activation of caspases requires proteolytic processing at conserved internal aspartic residues to generate a heterodimeric enzyme consisting of the large and small subunits. This protein is involved in the programmed cell death induced by Fas and various apoptotic stimuli. The N-terminal FADD-like death effector domain of this protein suggests that it may interact with Fas-interacting protein FADD. This protein was detected in the insoluble fraction of the affected brain region from Huntington disease patients but not in those from normal controls, which implicated the role in neurodegenerative diseases. Many alternatively spliced transcript variants encoding different isoforms have been described, although not all variants have had their full-length sequences determined.
, xcaspase 8
, death related ced-3/Nedd2-like protein
, caspase 8, apoptosis-related cysteine peptidase
, caspase 8
, DEATH effector domain caspase
, Fas-linked ICE-like protease
, FADD-homologous ICE/CED-3-like protease
, FADD-like ICE
, ICE-like apoptotic protease 5
, MACH-alpha-1/2/3 protein
, MACH-beta-1/2/3/4 protein
, MORT1-associated ced-3 homolog
, apoptotic cysteine protease
, apoptotic protease Mch-5
, caspase 8, apoptosis-related cysteine protease
, cysteine protease