Tumor necrosis factor signaling

Wajant, Harald; Pfizenmaier, Klaus; Scheurich, Peter

doi:10.1038/sj.cdd.4401189

Cited by 2,106 publications

(1,998 citation statements)

References 333 publications

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“…TNFα is a major proinflammatory mediator and efficiently induces a cytotoxic effect in most cell lines [19]. In this study, we used TNFα to induce the apoptosis, therefore it was important to assess the cytotoxic effect of low concentrations of TNFα (10, 20, and 40 ng/mL) on the NCI-H292 cell line to choose a suitable concentration for subsequent experiments.…”

Section: Resultsmentioning

confidence: 99%

Silver nanoparticles reduce the apoptosis induced by tumor necrosis factor-α

Fehaid

Taniguchi

2018

Science and Technology of Advanced Materials

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Silver nanoparticles (AgNPs) are widely known to have anti-inflammatory properties, but the exact mechanism underlying this anti-inflammatory effect is not clearly understood. Tumor necrosis factor-α (TNFα) is a major pro-inflammatory cytokine that is expressed in the early stage of cell inflammation and induces apoptosis by several known pathways. Our study aimed to investigate the effect of AgNPs on the response of lung epithelial cells to TNFα and the molecular mechanism of this response. Lung epithelial cell line NCI-H292 cells were exposed to AgNPs (5 µg/mL) and/or TNFα (20 ng/mL) for 24 h, then cellular uptake was analyzed using flow cytometry. Our results showed that AgNPs were taken up by cells in a dose-dependent manner and that the cellular uptake ratio of AgNPs was significantly increased in the presence of TNFα. Apoptosis assays indicated that exposure to AgNPs significantly decreased the apoptotic effect of TNFα. Confocal microscopy was used to localize the tumor necrosis factor receptor 1 (TNFR1) and revealed that TNFR1 localized on the surface of cells exposed to TNFα. In contrast, TNFR1 localized inside cells exposed to both AgNPs and TNFα, with very few receptors scattered on the cell membrane. The results indicated that AgNPs reduced the cell surface TNFR1 expression level. The results suggested that the reduction of surface TNFR1 reduced cellular response to TNFα, resulting in an anti-apoptotic effect.

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Section: Resultsmentioning

confidence: 99%

Silver nanoparticles reduce the apoptosis induced by tumor necrosis factor-α

Fehaid

Taniguchi

2018

Science and Technology of Advanced Materials

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“…These cellular responses to TNF-a is signaled through two different cell surface receptors, p55 TNF-R1 and p75 TNF-R2 (Tartaglia and Goeddel, 1992). TNF-a induces homotypic aggregation of these receptors, resulting in the recruitment of a number of adaptor proteins to the cytoplasmic aminoterminal domains of the clustered receptors and consequent initiation of signal transduction (Smith et al, 1994;Ashkenazi and Dixit, 1998;Wajant et al, 2003).…”

Section: Introductionmentioning

confidence: 99%

Human glutathione S-transferase P1-1 interacts with TRAF2 and regulates TRAF2–ASK1 signals

et al. 2006

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Human glutathione S-transferase P1-1 (GSTP1-1) is an ubiquitously expressed protein that plays an important role in the detoxification and xenobiotics metabolism. It has been shown that GSTP1-1 interacts with c-Jun NH 2 -terminal kinase (JNK) and suppresses its activity. Here, we report a novel function of GSTP1-1 in regulating tumor necrosis factor-a (TNF-a)-triggered signaling. The present experiments showed that GSTP1-1 physically associated with tumor necrosis factor receptor-associated factor 2 (TRAF2) in vivo and in vitro. Overexpression of GSTP1-1 inhibited TRAF2-induced activation of both JNK and p38 but not of nuclear factor-jB (NF-jB). Glutathione S-transferase P1-1 also attenuated TRAF2-enhanced apoptosis signal-regulating kinase 1 (ASK1) autophosphorylation and inhibited TRAF2-ASK1-induced cell apoptosis by suppressing the interaction of TRAF2 and ASK1. Conversely, silencing of GSTP1-1 expression through RNA interference (RNAi) resulted in increase of TNF-a-dependent TRAF2-ASK1 association followed by hyper-activation of ASK1 and JNK. A mutant GSTP1-1 lacking TRAF domain-binding motif exhibited a significant decline of capacity to bind TRAF2 and block TRAF2-ASK1 signaling compared with the wild type of GSTP1-1. Moreover, the glutathione-conjugating activity of GSTP1-1 was not involved in the regulation of TRAF2 signaling. These findings indicate that GSTP1-1 plays an important regulatory role in TNF-a-induced signaling by forming ligand-binding interactions with TRAF2, which provides a new insight for analysing the protective effects of GSTP1-1 in tumor cells.

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“…Tumor necrosis factor alpha (TNFα) mediates a variety of biological functions such as cell proliferation, differentiation and cell death. TNFα-TNFR interactions generate two different signaling cascades: the death signaling pathway (via TRADD/FADD/Caspase-8) and the survival pathway, in which the signal adapter TNFR-associated factor-2 (TRAF2) plays a primary regulatory role [22,23]. Upon stimulation of TNFR1 with TNFα, TRAF2 has been implicated in the activation of transcription factors NF-κB and c-Jun via inhibitor nuclear factor kappa B kinase (IKK) and Jun N-terminal kinase (JNK), respectively.…”

Section: Introductionmentioning

confidence: 99%

Dual treatment with COX-2 inhibitor and sodium arsenite leads to induction of surface Fas Ligand expression and Fas-Ligand-mediated apoptosis in human melanoma cells

Ivanov¹,

Hei²

2006

Experimental Cell Research

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Most human melanomas express Fas receptor on the cell surface, and treatment with exogenous Fas Ligand (FasL) efficiently induces apoptosis of these cells. In contrast, endogenous surface expression of FasL is suppressed in Fas-positive melanomas. We report here the use of a combination of sodium arsenite, an inhibitor of NF-κB activation, and NS398, a cyclooxygenase-2 (COX-2) inhibitor, for restoration of the surface FasL expression. We observed a large increase of Fas-mediated apoptosis in Fas-positive melanomas. This was due to induction of FasL surface expression and increased susceptibility to Fas death signaling after arsenite and NS398 treatment. Furthermore, silencing COX-2 expression by specific RNAi also effectively increased surface FasL expression following arsenite treatment. Upregulation of the surface FasL levels was based on an increase in the efficiency of translocation to the cell surface and stabilization of FasL protein on the cell surface, rather than on acceleration of the FasL gene transcription. Data obtained demonstrate that the combination of arsenite with inhibitors of COX-2 may affect the target cancer cells via induction of FasL-mediated death signaling.

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Tumor necrosis factor signaling

Cited by 2,106 publications

References 333 publications

Silver nanoparticles reduce the apoptosis induced by tumor necrosis factor-α

Silver nanoparticles reduce the apoptosis induced by tumor necrosis factor-α

Human glutathione S-transferase P1-1 interacts with TRAF2 and regulates TRAF2–ASK1 signals

Dual treatment with COX-2 inhibitor and sodium arsenite leads to induction of surface Fas Ligand expression and Fas-Ligand-mediated apoptosis in human melanoma cells

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