Receptor System of Tumor Necrosis Factor: Cell Surface Fas Antigen Appears to Mediate Only the Cytolytic Activity of TNF

2015 ◽  
pp. 58-65
Author(s):  
Shin Yonehara ◽  
Ai Ishii ◽  
Minako Yonehara
Keyword(s):  
Tumor Necrosis Factor ◽  
Cell Surface ◽  
Tumor Necrosis ◽  
Cytolytic Activity ◽  
Receptor System ◽  
Fas Antigen ◽  
Necrosis Factor

scholarly journals Size-Dependent Effect of Silver Nanoparticles on the Tumor Necrosis Factor α-Induced DNA Damage Response

2019 ◽  
Vol 20 (5) ◽  
pp. 1038 ◽  
Author(s):  
Alaa Fehaid ◽  
Akiyoshi Taniguchi
Keyword(s):  
Dna Damage ◽  
Silver Nanoparticles ◽  
Tumor Necrosis Factor ◽  
Cell Surface ◽  
Dna Damage Response ◽  
Tumor Necrosis ◽  
Tumor Necrosis Factor Α ◽  
Damage Response ◽  
Factor Α ◽  
Necrosis Factor

Silver nanoparticles (AgNPs) are widely used in many consumer products due to their anti-inflammatory properties. Therefore, the effect of exposure to AgNPs should be investigated in diseased states in addition to healthy ones. Tumor necrosis factor-α (TNFα) is a major cytokine that is highly expressed in many diseased conditions, such as inflammatory diseases, sepsis, and cancer. We investigated the effects of two different sizes of AgNPs on the TNFα-induced DNA damage response. Cells were exposed to 10 and 200 nm AgNPs separately and the results showed that the 200 nm AgNPs had a lower cytotoxic effect with a higher percent of cellular uptake compared to the 10 nm AgNPs. Moreover, analysis of reactive oxygen species (ROS) generation and DNA damage indicated that TNFα-induced ROS-mediated DNA damage was reduced by 200 nm AgNPs, but not by 10 nm AgNPs. Tumor necrosis factor receptor 1 (TNFR1) was localized on the cell surface after TNFα exposure with or without 10 nm AgNPs. In contrast, the expression of TNFR1 on the cell surface was reduced by the 200 nm AgNPs. These results suggested that exposure of cells to 200 nm AgNPs reduces the TNFα-induced DNA damage response via reducing the surface expression of TNFR1, thus reducing the signal transduction of TNFα.

Expression of genes coding for the tumor necrosis factor and lymphotoxin ligand-receptor system in non-Hodgkin's lymphomas

2000 ◽  
Vol 49 (9) ◽  
pp. 469-475 ◽  
Author(s):  
Krzysztof Warzocha ◽  
Patricia Ribeiro ◽  
Nathalie Renard ◽  
Jacques Bienvenu ◽  
Carloe Charlot ◽  
...  
Keyword(s):  
Tumor Necrosis Factor ◽  
Tumor Necrosis ◽  
Receptor System ◽  
Expression Of Genes ◽  
Hodgkin's Lymphomas ◽  
Necrosis Factor

scholarly journals Modulation of endothelial cell hemostatic properties by tumor necrosis factor.

1986 ◽  
Vol 163 (3) ◽  
pp. 740-745 ◽  
Author(s):  
P P Nawroth ◽  
D M Stern
Keyword(s):  
Endothelial Cells ◽  
Endothelial Cell ◽  
Tumor Necrosis Factor ◽  
Cell Surface ◽  
Protein C ◽  
Tumor Necrosis ◽  
Protein S ◽  
Active Role ◽  
Procoagulant Activity ◽  
Necrosis Factor

Tumor necrosis factor/cachectin (TNF) is a mediator of the septic state, which involves diffuse abnormalities of coagulation throughout the vasculature. Since previous studies have shown that endothelial cells can play an active role in coagulation, we wished to determine whether TNF could modulate endothelial cell hemostatic properties. Incubation of purified recombinant TNF with cultured endothelial cells resulted in a time- and dose-dependent acquisition of tissue factor procoagulant activity. Concomitant with enhanced procoagulant activity, TNF also suppressed endothelial cell cofactor activity for the anticoagulant protein C pathway; both thrombin-mediated protein C activation and formation of functional activated protein C-protein S complex on the cell surface were considerably attenuated. Comparable concentrations of TNF (half-maximal affect at approximately 50 pM) and incubation times (half-maximal affect by 4 h after addition to cultures) were required for each of these changes in endothelial cell coagulant properties. This unidirectional shift in cell surface hemostatic properties favoring promotion of clot formation indicates that, in addition to leukocyte procoagulants, endothelium can potentially be instrumental in the pathogenesis of the thrombotic state associated with inflammatory and malignant disorders.

scholarly journals Poliovirus Protein 3A Inhibits Tumor Necrosis Factor (TNF)-Induced Apoptosis by Eliminating the TNF Receptor from the Cell Surface

2001 ◽  
Vol 75 (21) ◽  
pp. 10409-10420 ◽  
Author(s):  
Nickolay Neznanov ◽  
Anna Kondratova ◽  
Konstantin M. Chumakov ◽  
Brigitte Angres ◽  
Bakhyt Zhumabayeva ◽  
...  
Keyword(s):  
Tumor Necrosis Factor ◽  
Cell Surface ◽  
Protein Trafficking ◽  
Tumor Necrosis ◽  
Viral Infections ◽  
Brefeldin A ◽  
Tnf Receptor ◽  
Apoptotic Pathways ◽  
Induced Apoptosis ◽  
Necrosis Factor

ABSTRACT Viral infections often trigger host defensive reactions by activating intrinsic (intracellular) and extrinsic (receptor-mediated) apoptotic pathways. Poliovirus is known to encode an antiapoptotic function(s) suppressing the intrinsic pathway. Here, the effect of poliovirus nonstructural proteins on cell sensitivity to tumor necrosis factor (TNF)-induced (i.e., receptor-mediated) apoptosis was studied. This sensitivity is dramatically enhanced by the viral proteinase 2A, due, most likely, to inhibition of cellular translation. On the other hand, cells expressing poliovirus noncapsid proteins 3A and 2B exhibit strong TNF resistance. Expression of 3A neutralizes the proapoptotic activity of 2A and results in a specific suppression of TNF signaling, including the lack of activation of NF-κB, due to elimination of the TNF receptor from the cell surface. In agreement with this, poliovirus infection results in a dramatic decrease in TNF receptor abundance on the surfaces of infected cells as early as 4 h postinfection. Poliovirus proteins that confer resistance to TNF interfere with endoplasmic reticulum-Golgi protein trafficking, and their effect on TNF signaling can be imitated by brefeldin A, suggesting that the mechanism of poliovirus-mediated resistance to TNF is a result of aberrant TNF receptor trafficking.

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