scholarly journals Characterization of Garden Cress Mucilage and its Prophylactic Effect Against Indomethacin-Induced Enter-Colitis in Rats

2021 ◽  
Vol 11 (6) ◽  
pp. 13911-13923
Keyword(s):  
Antioxidant Activity ◽  
Oral Administration ◽  
Oil Industry ◽  
Garden Cress ◽  
Industry Waste ◽  
Tnf Α ◽  
Pre Treatment ◽  
Factor Α ◽  
Necrosis Factor

The utilization of industrial waste such as oil industry waste in the production of natural nutraceuticals is a very beneficial issue. So, the current study was established to assess the characteristics of the mucilage extracted from garden cress seeds meal and evaluate its efficacy in the protection against enter-colitis. A defatted powder meal of garden cress seeds was dissolved in distilled water to extract the mucilage either by heating at 80°C or by ultrasonication. Functional and chemical characteristics of the two types of mucilage were assessed. Rats received oral administration of the mucilage extracted by ultrasonication, which afforded the most promising antioxidant activity, for two weeks before and during the 7 days of oral administration by indomethacin (6 mg/kg/day). Compared with the rats injected with indomethacin without the pre-treatment with the mucilage, rats administrated with the mucilage showed a decrease in the erythrocyte sedimentation rate (ESR), intestinal tumor necrosis factor-α (TNF-α), and plasma lactate dehydrogenase (LDH) activity. Also, rats administered with the mucilage recorded lower intestinal malodealdehyde (MDA) and higher intestinal reduced glutathione (GSH) compared to those of rats injected with indomethacin without the pre-treatment with the mucilage. It can be concluded that the mucilage extracted from garden cress seeds meal can be considered as a natural nutraceutical with potent antioxidant activity exhibiting protective effect against enter-colitis.

Effects of tumor necrosis factor α on leptin-sensitive intestinal vagal mechanoreceptors in the cat

2013 ◽  
Vol 91 (11) ◽  
pp. 941-950 ◽  
Author(s):  
Nathalie Quinson ◽  
Véronique Vitton ◽  
Michel Bouvier ◽  
Jean-Charles Grimaud ◽  
Anne Abysique
Keyword(s):  
Tumour Necrosis ◽  
Discharge Frequency ◽  
Tumour Necrosis Factor Α ◽  
Tnf Α ◽  
Inflammatory Bowel ◽  
Pre Treatment ◽  
Factor Α ◽  
Necrosis Factor

The involvement of tumour necrosis factor α (TNF-α) in inflammatory bowel disease (IBD) has been established, and anti-TNF-α has been suggested as a therapeutic approach for the treatment of these pathologies. We studied the effects of TNF-α on leptin-sensitive intestinal vagal units to determine whether TNF-α exerts its effects through the intestinal vagal mechanoreceptors and to investigate its interactions with substances regulating food intake. The activity of intestinal vagal mechanoreceptors was recorded via microelectrodes implanted into the nodose ganglion in anesthetized cats. TNF-α (1 μg, i.a.) increased the discharge frequency of leptin-activated units (type 1 units; P < 0.05) and had no effect on the discharge frequency of leptin-inhibited units (type 2 units). When TNF-α was administered 20 min after sulfated cholecystokinin-8 (CCK), its excitatory effects on type 1 units were significantly enhanced (P < 0.0001) and type 2 units were significantly (P < 0.05) activated. Pre-treatment with Il-1ra (250 μg, i.a.) blocked the excitatory effects of TNF-α on type 1 units whereas the excitatory effects of TNF-α administration after CCK treatment on type 2 units were not modified. The activation of leptin-sensitive units by TNF-α may explain, at least in part, the weight loss observed in IBD.

scholarly journals THP-1 Cells and Pro-inflammatory Cytokine Production: An in Vitro Tool for Functional Characterization of NOD1/NOD2 Antagonists

2019 ◽  
Vol 20 (17) ◽  
pp. 4265 ◽  
Author(s):  
Jakopin ◽  
Corsini
Keyword(s):  
Inflammatory Cytokine ◽  
Functional Characterization ◽  
Toll Like Receptor 4 ◽  
Inflammatory Cytokine Production ◽  
Tnf Α ◽  
Factor Α ◽  
Necrosis Factor ◽  
Oligomerization Domain

THP-1 cells express high levels of native functional nucleotide-binding oligomerization domain 1 (NOD1), NOD2, and Toll-like receptor 4 (TLR4) receptors, and have often been used for investigating the immunomodulatory effects of small molecules. We postulated that they would represent an ideal cell-based model for our study, the aim of which was to develop a new in vitro tool for functional characterization of NOD antagonists. NOD antagonists were initially screened for their effect on NOD agonist-induced interleukin-8 (IL-8) release. Next, we examined the extent to which the selected NOD antagonists block the NOD-TLR4 synergistic crosstalk by measuring the effect of NOD antagonism on tumor necrosis factor-α (TNF-α) secretion from doubly activated THP-1 cells. Overall, the results obtained indicate that pro-inflammatory cytokine secretion from THP-1 provides a valuable, simple and reproducible in vitro tool for functional characterization of NOD antagonists.

Role of NF-κB in TNF-α-induced COX-2 Expression in Synovial Fibroblasts from Human TMJ

2007 ◽  
Vol 86 (4) ◽  
pp. 363-367 ◽  
Author(s):  
J. Ke ◽  
X. Long ◽  
Y. Liu ◽  
Y.F. Zhang ◽  
J. Li ◽  
...  
Keyword(s):  
Synovial Fibroblasts ◽  
Nuclear Factor Κb ◽  
Mobility Shift ◽  
Tnf Α ◽  
Cox 2 ◽  
Mobility Shift Assay ◽  
Pre Treatment ◽  
Factor Α ◽  
Necrosis Factor

In the temporomandibular joint (TMJ) synovium, cyclo-oxygenase-2 (COX-2) expression has been believed to be directly related to joint pain and synovitis. Here we investigated the role of Nuclear Factor κB (NF-κB) in the regulation of COX-2 expression in synovial fibroblasts from human TMJ induced by tumor necrosis factor-α (TNF-α). By reverse-transcriptase/polymerase chain-reaction (RT-PCR) and Western blotting analysis, TNF-α induced a dose- and time-dependent increase in COX-2 expression. Electrophoretic mobility shift assay (EMSA) revealed that transient NF-κB activation in the COX-2 promoter was triggered by TNF-α. In parallel with transient NF-κB activation, the rapid translocation of NF-κB, particularly the p65 subunit, from the cytoplasm into the nucleus was demonstrated. Pre-treatment with pyrolidine dithiocarbamate (PDTC), one of the NF-κB inhibitors, prevented binding to the COX-2 promoter and expression of COX-2 protein in response to TNF-α. These findings indicate that activation of NF-κB is responsible for TNF-α-induced COX-2 expression in synovial fibroblasts from the TMJ.

scholarly journals Degradation of STAT5 proteins in 3T3-L1 adipocytes is induced by TNF-α and cycloheximide in a manner independent of STAT5A activation

2007 ◽  
Vol 292 (2) ◽  
pp. E461-E468 ◽  
Author(s):  
Z. Elizabeth Floyd ◽  
Brant M. Segura ◽  
Fang He ◽  
Jacqueline M. Stephens
Keyword(s):  
Insulin Signaling ◽  
Causative Factor ◽  
Signal Transducer ◽  
Tnf Α ◽  
Wide Range ◽  
Initial Characterization ◽  
Factor Α ◽  
Necrosis Factor ◽  
Multifunctional Cytokine

Tumor necrosis factor-α (TNF-α) is a multifunctional cytokine that has been implicated as a causative factor in obesity-linked insulin resistance. It is commonly accepted that macrophage-derived TNF-α acts in a paracrine manner on adjacent adipocytes to inhibit the expression of various adipocyte genes and to attenuate insulin signaling. Several studies have revealed that signal transducer and activator of transcription (STAT)5 proteins are modulated during adipogenesis and can modulate the transcription of some adipocyte genes. In this study, we demonstrate that TNF-α treatment, in the presence of cycloheximide, also results in the rapid turnover of STAT5A and STAT5B in a process that is independent of STAT5 activation by tyrosine phosphorylation. In addition, STAT5B is more labile than STAT5A under these conditions, suggesting that the COOH terminus of STAT5 may be involved in the turnover of each protein. Initial characterization of the TNF-α and cycloheximide-mediated degradation of STAT5 indicates that inhibition of the proteasome stabilizes both forms of STAT5 in the presence of TNF-α. In addition, the use of an NF-κB inhibitor results in the stabilization of STAT5A in the presence of TNF-α and cycloheximide, indicating that the degradation of STAT5 proteins under these conditions may involve the NF-κB pathway. STAT5 proteins are abundantly expressed in mature adipocytes and are normally extremely stable proteins under a wide range of conditions. However, our results demonstrate that the potentiation of TNF-α-mediated signaling in the presence of cyclohexmide is associated with a significant increase in the degradation of STAT5 proteins in 3T3-L1 adipocytes.

scholarly journals Anti-Inflammatory Effect of Simonsinol on Lipopolysaccharide Stimulated RAW264.7 Cells through Inactivation of NF-κB Signaling Pathway

Molecules ◽  
2020 ◽  
Vol 25 (16) ◽  
pp. 3573
Author(s):  
Lian-Chun Li ◽  
Zheng-Hong Pan ◽  
De-Sheng Ning ◽  
Yu-Xia Fu
Keyword(s):  
Nitric Oxide ◽  
Signaling Pathway ◽  
Morphological Changes ◽  
Raw264.7 Cells ◽  
Enzyme Linked Immunosorbent Assay ◽  
Tnf Α ◽  
Anti Inflammatory ◽  
Factor Α ◽  
Oxide Synthase ◽  
Necrosis Factor

Simonsinol is a natural sesqui-neolignan firstly isolated from the bark of Illicium simonsii. In this study, the anti-inflammatory activity of simonsinol was investigated with a lipopolysaccharide (LPS)-stimulated murine macrophages RAW264.7 cells model. The results demonstrated that simonsinol could antagonize the effect of LPS on morphological changes of RAW264.7 cells, and decrease the production of nitric oxide (NO), tumor necrosis factor α (TNF-α), and interleukin 6 (IL-6) in LPS-stimulated RAW264.7 cells, as determined by Griess assay and enzyme-linked immunosorbent assay (ELISA). Furthermore, simonsinol could downregulate transcription of inducible nitric oxide synthase (iNOS), TNF-α, and IL-6 as measured by reverse transcription polymerase chain reaction (RT-PCR), and inhibit phosphorylation of the alpha inhibitor of NF-κB (IκBα) as assayed by Western blot. In conclusion, these data demonstrate that simonsinol could inhibit inflammation response in LPS-stimulated RAW264.7 cells through the inactivation of the nuclear transcription factor kappa-B (NF-κB) signaling pathway.

#50 Gestational exposure of tumor necrosis factor-α (TNF-α) inhibitor drugs

2019 ◽  
Vol 88 ◽  
pp. 149-150 ◽  
Author(s):  
Erkoseoglu Ilknur ◽  
Kadioglu Mine ◽  
Cavusoglu Irem ◽  
Sisman Mulkiye ◽  
Aran Turhan ◽  
...  
Keyword(s):  
Tumor Necrosis Factor ◽  
Tumor Necrosis ◽  
Tumor Necrosis Factor Α ◽  
Gestational Exposure ◽  
Tnf Α ◽  
Factor Α ◽  
Necrosis Factor
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