Tumor Necrosis Factor (TNF)-α Induction of CXCL10 in Endothelial Cells Requires Protein Arginine Methyltransferase 5 (PRMT5)-mediated Nuclear Factor (NF)-κB p65 Methylation

ABSTRACT The anti-inflammatory activities of three quinolones, levofloxacin, moxifloxacin, and gatifloxacin, were investigated with an in vitro model of transendothelial migration (TEM). Human umbilical vein endothelial cells (HUVEC) were seeded in Transwell inserts, treated with serial dilutions of antibiotics, infected with Chlamydia pneumoniae, or stimulated with tumor necrosis factor alpha (TNF-α). Neutrophils or monocytes were also preincubated with serial dilutions of each antibiotic. TEM was assessed by light microscopic examination of the underside of the polycarbonate membrane, and levels of interleukin-8 (IL-8) and monocyte chemotactic protein 1 (MCP-1) were measured by enzyme-linked immunosorbent assay. In HUVEC infected with C. pneumoniae or stimulated with TNF-α, all fluoroquinolones significantly decreased neutrophil and monocyte TEM, compared to antibiotic-free controls. Moxifloxacin and gatifloxacin produced a significant decrease in IL-8 in C. pneumoniae-infected and TNF-α-stimulated HUVEC; however, moxifloxacin was the only fluoroquinolone that produced a significant decrease in MCP-1 levels under both conditions. Results from this study indicate similarities in the anti-inflammatory activities of these fluoroquinolones, although no statistically significant decrease in chemokine secretion was observed when levofloxacin was used. Mechanisms of neutrophil and monocyte TEM inhibition by fluoroquinolone antibiotics are unknown but may be partially due to inhibition of IL-8 and MCP-1 production, respectively.

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Tumor Necrosis Factor Alpha (TNF-α), Nuclear Factor of kappa B (NF-kB) p65 and Calcineurin Expression play a role in the regulation of muscle regeneration process through aerobic exercise in HIV patients

Bali Medical Journal ◽

10.15562/bmj.v6i2.607 ◽

2017 ◽

Vol 6 (2) ◽

pp. 421

Author(s):

Sri Mardjiati Mei Wulan ◽

Hening Laswati ◽

Windhu Purnomo ◽

Alex Pangkahila ◽

Nasronudin Nasronudin ◽

...

Keyword(s):

Tumor Necrosis Factor ◽

Aerobic Exercise ◽

Tumor Necrosis Factor Alpha ◽

Muscle Regeneration ◽

Tumor Necrosis ◽

Nuclear Factor ◽

Necrosis Factor Alpha ◽

Tnf Α ◽

Factor Alpha ◽

Necrosis Factor

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Elevated Tumor Necrosis Factor (TNF)-α mRNA Expression Correlates with Nuclear Factor Kappa B Expression in Peripheral Blood Mononuclear Cells in Preeclampsia

Journal of College of Physicians And Surgeons Pakistan ◽

10.29271/jcpsp.2020.02.158 ◽

2020 ◽

Vol 30 (02) ◽

pp. 158-162

Author(s):

Zaima Ali ◽

Uzma Zafar ◽

Saba Khaliq ◽

Khalid Lone

Keyword(s):

Tumor Necrosis Factor ◽

Peripheral Blood Mononuclear Cells ◽

Tumor Necrosis ◽

Nuclear Factor Kappa B ◽

Mononuclear Cells ◽

Nuclear Factor ◽

Peripheral Blood Mononuclear ◽

Tnf Α ◽

Blood Mononuclear Cells ◽

Necrosis Factor

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Fluid Shear Stress Attenuates Tumor Necrosis Factor-α–Induced Tissue Factor Expression in Cultured Human Endothelial Cells

Blood ◽

10.1182/blood.v91.11.4164 ◽

1998 ◽

Vol 91 (11) ◽

pp. 4164-4172 ◽

Cited By ~ 26

Author(s):

Yutaka Matsumoto ◽

Yohko Kawai ◽

Kiyoaki Watanabe ◽

Kazuo Sakai ◽

Mitsuru Murata ◽

...

Keyword(s):

Endothelial Cells ◽

Shear Stress ◽

Tumor Necrosis Factor ◽

Tissue Factor ◽

Shear Force ◽

Tumor Necrosis ◽

Shear Stresses ◽

Dependent Manner ◽

Tnf Α ◽

Necrosis Factor

Abstract Hemodynamic forces modulate various endothelial cell functions under gene regulation. Previously, we have shown that fibrinolytic activity of endothelial cells is enhanced by the synergistic effects of shear stress and cytokines. In this study, we investigated the effect of shear stress on tumor necrosis factor (TNF)-α–induced tissue factor (TF) expression in cultured human umbilical vein endothelial cells (HUVECs), using a modified cone-plate viscometer. Shear stresses at physiological levels reduced TNF-α (100 U/mL)–induced TF expression at both mRNA and antigen levels, in a shear-intensity and exposure-time dependent manner, whereas shear stress itself did not induce TF expression in HUVECs. TF expressed on the cell surfaces measured by flow cytometry using an anti-TF monoclonal antibody (HTF-K180) was also decreased to one third by shear force applied at 18 dynes/cm2 for 15 hours before and 6 hours after TNF-α stimulation. Furthermore, functional activity of TF, as assessed by the activation of factor X in the presence of FVIIa and Ca2+, was also decreased by shear application. However, the stability of TF mRNA was not decreased in the presence of shear stress. These results suggest that shear force acts as an important regulator of TF expression in endothelium at the transcriptional level.

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Characterization of rabbit SP-B promoter region responsive to downregulation by tumor necrosis factor-α

AJP Lung Cellular and Molecular Physiology ◽

10.1152/ajplung.2000.279.5.l806 ◽

2000 ◽

Vol 279 (5) ◽

pp. L806-L814 ◽

Cited By ~ 20

Author(s):

Kiflu Berhane ◽

Ramgopal K. Margana ◽

Vijayakumar Boggaram

Keyword(s):

Tumor Necrosis Factor ◽

Tumor Necrosis ◽

Promoter Activity ◽

Tumor Necrosis Factor Α ◽

Surfactant Protein ◽

Nuclear Factor ◽

Tnf Α ◽

Nuclear Levels ◽

Factor Α ◽

Necrosis Factor

Surfactant protein B (SP-B) is essential for the maintenance of biophysical properties and physiological function of pulmonary surfactant. Tumor necrosis factor-α (TNF-α), an important mediator of lung inflammation, inhibits surfactant phospholipid and surfactant protein synthesis in the lung. In the present study, we investigated the TNF-α inhibition of rabbit SP-B promoter activity in a human lung adenocarcinoma cell line (NCI-H441). Deletion experiments indicated that the TNF-α response elements are located within −236 bp of SP-B 5′-flanking DNA. The TNF-α response region contained binding sites for nuclear factor-κB (NF-κB), Sp1/Sp3, thyroid transcription factor (TTF)-1, and hepatocyte nuclear factor (HNF)-3 transcription factors. Inhibitors of NF-κB activation such as dexamethasone and N-tosyl-l-phenylalanine chloromethyl ketone and mutation of the NF-κB element did not reverse TNF-α inhibition of SP-B promoter, indicating that TNF-α inhibition of SP-B promoter activity occurs independently of NF-κB activation. TNF-α treatment decreased the binding activities of TTF-1 and HNF-3 elements without altering the nuclear levels of TTF-1 and HNF-3α proteins. Pretreatment of cells with okadaic acid reversed TNF-α inhibition of SP-B promoter activity. Taken together these data indicated that in NCI-H441 cells 1) TNF-α inhibition of SP-B promoter activity may be caused by decreased binding activities of TTF-1 and HNF-3 elements, 2) the decreased binding activities of TTF-1 and HNF-3α are not due to decreased nuclear levels of the proteins, and 3) okadaic acid-sensitive phosphatases may be involved in mediating TNF-α inhibition of SP-B promoter activity.

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