scholarly journals Down-regulation of microRNA-155 promotes selenium deficiency-induced apoptosis by tumor necrosis factor receptor superfamily member 1B in the broiler spleen

Oncotarget ◽  
2017 ◽  
Vol 8 (35) ◽  
pp. 58513-58525 ◽  
Author(s):  
Ci Liu ◽  
Zhepeng Sun ◽  
Zhe Xu ◽  
Tianqi Liu ◽  
Tingru Pan ◽  
...  
Keyword(s):  
Tumor Necrosis Factor ◽  
Tumor Necrosis ◽  
Tumor Necrosis Factor Receptor ◽  
Selenium Deficiency ◽  
Down Regulation ◽  
Induced Apoptosis ◽  
Necrosis Factor

scholarly journals Tumor necrosis factor induces rapid down-regulation of TXNIP in human T cells

2019 ◽  
Vol 9 (1) ◽  
Author(s):  
Trine B. Levring ◽  
Martin Kongsbak-Wismann ◽  
Anna K. O. Rode ◽  
Fatima A. H. Al-Jaberi ◽  
Daniel V. Lopez ◽  
...  
Keyword(s):  
T Cells ◽  
Tumor Necrosis Factor ◽  
Glucose Uptake ◽  
Tumor Necrosis ◽  
Gradient Centrifugation ◽  
Tumor Necrosis Factor Receptor ◽  
Down Regulation ◽  
Interacting Protein ◽  
Human T Cells ◽  
Necrosis Factor

Abstract In addition to antigen-driven signals, T cells need co-stimulatory signals for robust activation. Several receptors, including members of the tumor necrosis factor receptor superfamily (TNFRSF), can deliver co-stimulatory signals to T cells. Thioredoxin interacting protein (TXNIP) is an important inhibitor of glucose uptake and cell proliferation, but it is unknown how TXNIP is regulated in T cells. The aim of this study was to determine expression levels and regulation of TXNIP in human T cells. We found that naïve T cells express high levels of TXNIP and that treatment of blood samples with TNF results in rapid down-regulation of TXNIP in the T cells. TNF-induced TXNIP down-regulation correlated with increased glucose uptake. Furthermore, we found that density gradient centrifugation (DGC) induced down-regulation of TXNIP. We demonstrate that DGC induced TNF production that paralleled the TXNIP down-regulation. Treatment of blood with toll-like receptor (TLR) ligands induced TNF production and TXNIP down-regulation, suggesting that damage-associated molecular patterns (DAMPs), such as endogenous TLR ligands, released during DGC play a role in DGC-induced TXNIP down-regulation. Finally, we demonstrate that TNF-induced TXNIP down-regulation is dependent on caspase activity and is caused by caspase-mediated cleavage of TXNIP.

Thioridazine Enhances TRAIL Cytotoxicity in Human Myeloid Leukemic Cells By up-Regulating DR5 and Modulating PI3K-AKT-NF-Kb Pathway

Blood ◽  
2015 ◽  
Vol 126 (23) ◽  
pp. 4938-4938
Author(s):  
Yi Wang ◽  
Yangyi Bao ◽  
Leiming Xia ◽  
Liu Liu ◽  
Kunyuan Guo ◽  
...  
Keyword(s):  
Cancer Research ◽  
Tumor Necrosis Factor ◽  
Tumor Necrosis ◽  
Leukemic Cells ◽  
Leukemia Cells ◽  
Down Regulation ◽  
Trail Receptors ◽  
Trail Resistance ◽  
Induced Apoptosis ◽  
Necrosis Factor

Abstract Tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) can induce apoptosis in cancer cells but not in most normal cells, and is identified to be effective in various cancers, include myeloid leukemic cells[1]. Although some leukemia cell lines, K562 and KG-1, are sensitive to TRAIL, many showed certain degrees of resistance to TRAIL-mediated apoptosis[2,3], and the mechanism remains largely unknown, which forced us to find out ways to solve the problem. In this study, we investigated whether thioridazine, a phenothiazine derivative, could overcome the TRAIL resistance in K562 and KG-1 cells. Recently, we showed that Compared to treatment with thioridazine or TRAIL alone, co-treatment with thioridazine and TRAIL-induced apoptosis in K562 and KG-1 cells synergistically. This combination led to activation of caspase-8 and Bid, the cytosolic cumulation of cytochrome c from mitochondria as well as caspase-3 activated downstream. Treatment with thioridazine induced down-regulation of PI3K-AKT-NF-κB pathway. meanwhile, thioridazine dropped the level of NF-κB-dependent Bcl-xL, leading caspase activated and Bid cleaved. the expression of TRAIL-receptors in both K562 and KG-1 cells underwentthe treatment of thioridazine investigated that thioridazine significantly up-regulated DR5 by up to 51.22%, but not other TRAIL-receptors such as DR4, decoy receptor 1, and DcR2. Therefore, our results indicate that the combination of TRAIL with thioridazine overturn TRAIL resistance through Up-regulating the expression of DR5 and down-regulation of AKT protein, and combination treatment with thioridazine and TRAIL may be a novel therapeutic strategy in leukemia. Reference: Srivastava R K. TRAIL/Apo-2L: mechanisms and clinical applications in cancer.[J]. Neoplasia, 2001, 3(6):535-546. Nimmanapalli R, Porosnicu M, Nguyen D, et al. Cotreatment with STI-571 enhances tumor necrosis factor alpha-related apoptosis-inducing ligand (TRAIL or apo-2L)-induced apoptosis of Bcr-Abl-positive human acute leukemia cells.[J]. Clinical Cancer Research An Official Journal of the American Association for Cancer Research, 2001, 7(2):350-357. Yang T, Lan J, Huang Q, et al. Embelin sensitizes acute myeloid leukemia cells to TRAIL through XIAP inhibition and NF-κB inactivation.[J]. Cell Biochemistry & Biophysics, 2015, 71(1):291-297. Disclosures No relevant conflicts of interest to declare.

scholarly journals Apparently Normal Tumor Necrosis Factor Receptor 1 Signaling in the Absence of the Silencer of Death Domains

2003 ◽  
Vol 23 (18) ◽  
pp. 6609-6617 ◽  
Author(s):  
Robert Endres ◽  
Georg Häcker ◽  
Inge Brosch ◽  
Klaus Pfeffer
Keyword(s):  
Tumor Necrosis Factor ◽  
Tumor Necrosis ◽  
Tumor Necrosis Factor Receptor ◽  
Death Receptor ◽  
High Dose ◽  
Wild Type ◽  
Induced Apoptosis ◽  
Necrosis Factor

ABSTRACT The silencer of death domains (SODD) has been proposed to prevent constitutive signaling of tumor necrosis factor receptor 1 (TNFR1) in the absence of ligand. Besides TNFR1, death receptor 3 (DR3), Hsp70/Hsc70, and Bcl-2 have been characterized as binding partners of SODD. In order to investigate the in vivo role of SODD, we generated mice congenitally deficient in expression of the sodd gene. No spontaneous inflammatory infiltrations were observed in any organ of these mice. Consistent with this finding, in the absence of SODD no alteration in the activation patterns of nuclear factor κB (NF-κB), stress kinases, or ERK1 or -2 was observed after stimulation with tumor necrosis factor (TNF). Activation of NF-κB by DR3 was also unchanged. The extents of DR3- and TNF-induced apoptosis were comparable in gene-deficient and wild-type cells. Protection of cells against heat shock as mediated by the Hsp70 system and against staurosporine-induced apoptosis was independent of SODD. Furthermore, resistance to high-dose lipopolysaccharide (LPS) injections, LPS-d-GalN injections, and infection with listeriae was similar in wild-type and gene-deficient mice. In conclusion, our data do not support the concept of a unique, nonredundant role of SODD for the functions of TNFR1, Hsp70, and DR3.

scholarly journals I-FLICE, a Novel Inhibitor of Tumor Necrosis Factor Receptor-1- and CD-95-induced Apoptosis

1997 ◽  
Vol 272 (28) ◽  
pp. 17255-17257 ◽  
Author(s):  
Shimin Hu ◽  
Claudius Vincenz ◽  
Jian Ni ◽  
Reiner Gentz ◽  
Vishva M. Dixit
Keyword(s):  
Tumor Necrosis Factor ◽  
Tumor Necrosis ◽  
Tumor Necrosis Factor Receptor ◽  
Induced Apoptosis ◽  
Necrosis Factor

scholarly journals Antisense Oligonucleotide Inhibition of Tumor Necrosis Factor Receptor 1 Protects the Liver from Radiation-Induced Apoptosis

2006 ◽  
Vol 12 (9) ◽  
pp. 2849-2855 ◽  
Author(s):  
Xiao W. Huang ◽  
Jiong Yang ◽  
Aleksandar F. Dragovic ◽  
Hong Zhang ◽  
Theodore S. Lawrence ◽  
...  
Keyword(s):  
Tumor Necrosis Factor ◽  
Antisense Oligonucleotide ◽  
Tumor Necrosis ◽  
Tumor Necrosis Factor Receptor ◽  
Radiation Induced ◽  
Induced Apoptosis ◽  
Necrosis Factor

scholarly journals Phosphorylation of Tumor Necrosis Factor Receptor 1 (p55) Protects Macrophages from Silica-induced Apoptosis

2003 ◽  
Vol 279 (3) ◽  
pp. 2020-2029 ◽  
Author(s):  
Federica Gambelli ◽  
Peter Di ◽  
Xiaomei Niu ◽  
Mitchell Friedman ◽  
Timothy Hammond ◽  
...  
Keyword(s):  
Tumor Necrosis Factor ◽  
Tumor Necrosis ◽  
Tumor Necrosis Factor Receptor ◽  
Induced Apoptosis ◽  
Necrosis Factor

scholarly journals TRAF1 Is a Substrate of Caspases Activated during Tumor Necrosis Factor Receptor-α-induced Apoptosis

2000 ◽  
Vol 276 (11) ◽  
pp. 8087-8093 ◽  
Author(s):  
Eugen Leo ◽  
Quinn L. Deveraux ◽  
Christian Buchholtz ◽  
Kate Welsh ◽  
Shu-ichi Matsuzawa ◽  
...  
Keyword(s):  
Tumor Necrosis Factor ◽  
Tumor Necrosis ◽  
Tumor Necrosis Factor Receptor ◽  
Induced Apoptosis ◽  
Necrosis Factor
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