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Open AccessJournal ArticleDOI

Hepatocytes Sensitized to Tumor Necrosis Factor-α Cytotoxicity Undergo Apoptosis through Caspase-dependent and Caspase-independent Pathways

TLDR
ActD-induced hepatocyte sensitization to TNF-α cytotoxicity occurs through a FADD-dependent, caspase-independent pathway of apoptosis, suggesting that NF-κB inactivation and inhibition of RNA synthesis sensitize RALA255-10G hepatocytes to TNP toxicity through distinct cell death pathways that diverge below the level of FADD.
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This article is published in Journal of Biological Chemistry.The article was published on 2000-01-07 and is currently open access. It has received 109 citations till now. The article focuses on the topics: FADD & Death domain.

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Journal ArticleDOI

Cathepsin B contributes to TNF-α–mediated hepatocyte apoptosis by promoting mitochondrial release of cytochrome c

TL;DR: Caspase-mediated release of cat B from lysosomes enhances mitochondrial release of cytochrome c and subsequent caspase activation in TNF-alpha-treated hepatocytes.
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β-Amyloid Stimulation of Microglia and Monocytes Results in TNFα-Dependent Expression of Inducible Nitric Oxide Synthase and Neuronal Apoptosis

TL;DR: A functional linkage between β-amyloid-dependent activation of microglia and several characteristic markers of neuronal death occurring in Alzheimer's disease brains is demonstrated.
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Hepatocyte Death: A Clear and Present Danger

TL;DR: The hepatocyte is especially vulnerable to injury due to its central role in xenobiotic metabolism including drugs and alcohol, participation in lipid and fatty acid metabolism, its unique role in the enterohepatic circulation of bile acids, and the widespread prevalence of hepatotropic viruses.
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Molecular mechanisms underlying chemical liver injury.

TL;DR: Research aimed at elucidating the molecular mechanism of the pathogenesis of chemical-induced liver diseases is fundamental for preventing or devising new modalities of treatment for liver injury by chemicals.
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NF-κB inhibition sensitizes hepatocytes to TNF-induced apoptosis through a sustained activation of JNK and c-Jun☆

TL;DR: Sustained JNK activation that occurs in the absence of NF‐κB initiates apoptosis through a c‐Jun–dependent induction of the mitochondrial death pathway through down‐regulation of JNK and c‐ Jun/AP‐1.
References
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Journal ArticleDOI

Mitochondria and apoptosis

TL;DR: A variety of key events in apoptosis focus on mitochondria, including the release of caspase activators (such as cytochrome c), changes in electron transport, loss of mitochondrial transmembrane potential, altered cellular oxidation-reduction, and participation of pro- and antiapoptotic Bcl-2 family proteins.
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Prevention of Apoptosis by Bcl-2: Release of Cytochrome c from Mitochondria Blocked

TL;DR: One possible role of Bcl-2 in prevention of apoptosis is to block cytochrome c release from mitochondria, which is normally located in the mitochondrial intermembrane space.
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Caspases: the executioners of apoptosis

TL;DR: The importance of caspase prodomains in the regulation of apoptosis is further highlighted by the recognition of adapter molecules, such as RAIDD [receptor-interacting protein (RIP)-associated ICH-1/CED-3-homologous protein with a death domain]/CRADD (caspase and RIP adapter with death domain), which binds to the prodomain of cspase-2 and recruits it to the signalling complex.
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Rapid colorimetric assay for cell growth and survival. Modifications to the tetrazolium dye procedure giving improved sensitivity and reliability.

TL;DR: The reliability and sensitivity of the test have been increased to the point where it can in many cases replace the [3H]thymidine uptake assay to measure cell proliferation or survival in growth factor or cytotoxicity assays.
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A caspase-activated DNase that degrades DNA during apoptosis, and its inhibitor ICAD

TL;DR: A caspase-activated deoxyribonuclease (CAD) and its inhibitor (ICAD) have now been identified in the cytoplasmic fraction of mouse lymphoma cells and seems to function as a chaperone for CAD during its synthesis, remaining complexed with CAD to inhibit its DNase activity.
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