Lysates of Sarcocystis cruzi Bradyzoites Stimulate Raw 264.7 Macrophages to Produce Tumor Necrosis Factor (Cachectin)

1988 ◽  
Vol 74 (4) ◽  
pp. 660 ◽  
Author(s):  
R. Fayer ◽  
C. Andrews ◽  
J. P. Dubey
Keyword(s):  
Tumor Necrosis Factor ◽  
Tumor Necrosis ◽  
Raw 264.7 ◽  
Raw 264.7 Macrophages ◽  
Produce Tumor Necrosis Factor ◽  
Sarcocystis Cruzi ◽  
Necrosis Factor

scholarly journals The Role of Selected Flavonols in Tumor Necrosis Factor-Related Apoptosis-Inducing Ligand Receptor–1 (TRAIL-R1) Expression on Activated RAW 264.7 Macrophages

Molecules ◽  
2015 ◽  
Vol 20 (1) ◽  
pp. 900-912 ◽  
Author(s):  
Monika Warat ◽  
Tadeusz Sadowski ◽  
Ewelina Szliszka ◽  
Wojciech Król ◽  
Zenon Czuba
Keyword(s):  
Tumor Necrosis Factor ◽  
Tumor Necrosis ◽  
Raw 264.7 ◽  
Raw 264.7 Macrophages ◽  
Necrosis Factor

scholarly journals Release of tumor necrosis factor by human polymorphonuclear leukocytes

Blood ◽  
1990 ◽  
Vol 76 (7) ◽  
pp. 1405-1409 ◽  
Author(s):  
JY Djeu ◽  
D Serbousek ◽  
DK Blanchard
Keyword(s):  
Tumor Necrosis Factor ◽  
Polymorphonuclear Leukocytes ◽  
Tumor Necrosis ◽  
Polymorphonuclear Neutrophils ◽  
Opportunistic Fungi ◽  
Produce Tumor Necrosis Factor ◽  
Human Polymorphonuclear Leukocytes ◽  
Block Protein Synthesis ◽  
Granular Lymphocytes ◽  
Necrosis Factor

Abstract Evidence is presented that human polymorphonuclear neutrophils (PMN) can be induced to produce tumor necrosis factor (TNF). Other investigators have previously reported that TNF has been induced from macrophages by bacteria and, more recently, from natural killer cells by certain tumor cells. Our laboratory has reported that the opportunistic fungi, Candida albicans, can induce TNF, not only from human monocytes, but also from Percoll-fractionated large granular lymphocytes. We now report that incubation of PMN with C albicans for 3 hours was sufficient for detection of TNF release, and peak induction was observed at 8 to 18 hours. This release was inhibitable by actinomycin D, an inhibitor of RNA synthesis, as well as by emetine and cycloheximide, which block protein synthesis. The TNF produced by PMN was neutralized by specific monoclonal antibodies against human TNF. These results represent an important finding that TNF production is a normal response of PMN to stimulation by fungi such as C albicans and suggest that the release of TNF may be related to autocrine activation of PMN effector function to control Candida growth.

scholarly journals Alpha-Lipoic Acid Suppresses Extracellular Histone-Induced Release of the Infammatory Mediator Tumor Necrosis Factor-α by Macrophages

2017 ◽  
Vol 42 (6) ◽  
pp. 2559-2568 ◽  
Author(s):  
Ping Chang ◽  
Juan Liu ◽  
Ying Yu ◽  
Shao-Ye Cui ◽  
Zhen-Hui Guo ◽  
...  
Keyword(s):  
Tumor Necrosis Factor ◽  
Signaling Pathways ◽  
Tumor Necrosis ◽  
Tumor Necrosis Factor Α ◽  
Raw 264.7 ◽  
Alpha Lipoic Acid ◽  
Tnf Α ◽  
Extracellular Histones ◽  
Factor Α ◽  
Necrosis Factor

Background/Aims: This study investigated signaling pathways via which extracellular histones induce the pro-inflammatory cytokine tumor necrosis factor-α (TNF-α) release from the macrophage cell line RAW 264.7 and the anti-inflammatory efficacy of the antioxidant alpha-lipoic acid (ALA). Methods: ELISA and western blotting analyses were conducted to detect the release of TNF-α from histone-stimulated RAW 264.7 macrophages and the associated phospho-activation of MAPKs (ERK and p38) and NF-κB p65. The effects of ALA on the release of TNF-α and phospho-activation of the MAPKs and NF-κB p65 were studied. P < 0.05 was considered statistically significant. Results: Extracellular histones dose-dependently induced TNF-α release from RAW 264.7 cells and increased the phosphorylation of p38, ERK, and NF-κB p65. TNF-α release was markedly suppressed by p38, ERK, and NF-kB inhibitors. ALA reduced histone-induced TNF-α release, ERK/p38 MAPK activation, and NF-kB activation without affecting macrophage viability. Conclusion: Histones induce TNF-α release from macrophages by activating the MAPK and NF-kB signaling pathways, while ALA suppresses this response by inhibiting ERK, p38 and NF-kB. These findings identify potentially critical inflammatory signaling pathways in sepsis and molecular targets for sepsis treatment.

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