Effects of Polyphenolic Compounds on Tumor Necrosis Factor-α (TNF-α)-Induced Changes of Adipokines and Oxidative Stress in 3T3-L1 Adipocytes

Concurrent with the misbalance of oxidizing agents and antioxidants, high blood pressure is a major physical burden condition in the current scenario. Tumor necrosis factor-α (TNF-α) plays a vital role in the pathogenesis of hypertension. Tumor necrosis factor-α, inhibitor improves clinical symptoms however their outcome on high blood pressure has not been investigated. We investigated the inflammatory marker TNF-α, malondialdehyde (MDA) and ferric reducing antioxidant power (FRAP) in hypertensive patients. We measured randomly blood pressure using an ambulatory observe in hypertensive patients, measured systolic BP X 140 mmHg and/or diastolic BP X 90 mmHg were considered hypertensive. Total 60 cases were considered in the study that involves 30 hypertensive patients and 30 normal control. Measurements of serum concentrations of TNF-α, MDA, FRAP in hypertension patients was done in both the groups. Serum TNF-α was found to be remarkably increased in study subjects as compared to normal group (r=0.32, p<0.0001*). Serum MDA was also raised in hypertensive as compared to control (r=0.99**, p<0.0001*). While Serum FRAP was found to be decreased in hypertensive group in comparison to healthy control (r=0.23, p<0.0001*). It is concluded that high blood pressure leads to generation of oxidative stress with remarkable elevation of TNF-α and malondialdehyde levels. While reduced FRAP indicates its probable role in lipid peroxidation and in the pathogenesis of hypertension.

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Pulmonary injury and oxidative stress in rats induced by inhaled sulfur mustard is ameliorated by anti-tumor necrosis factor-α antibody

Toxicology and Applied Pharmacology ◽

10.1016/j.taap.2021.115677 ◽

2021 ◽

pp. 115677

Author(s):

Rama Malaviya ◽

Alyssa Bellomo ◽

Elena Abramova ◽

Claire R. Croutch ◽

Julie Roseman ◽

...

Keyword(s):

Oxidative Stress ◽

Tumor Necrosis Factor ◽

Tumor Necrosis ◽

Tumor Necrosis Factor Α ◽

Sulfur Mustard ◽

Pulmonary Injury ◽

Factor Α ◽

And Oxidative Stress ◽

Necrosis Factor

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Tumor necrosis factor-α alters integrins and metalloprotease ADAM12 levels and signaling in differentiating myoblasts

Polish Journal of Veterinary Sciences ◽

10.1515/pjvs-2016-0032 ◽

2016 ◽

Vol 19 (2) ◽

pp. 253-259

Author(s):

K. Grzelkowska-Kowalczyk ◽

J. Tokarska ◽

K. Grabiec ◽

M. Gajewska ◽

M. Milewska ◽

...

Keyword(s):

Tumor Necrosis Factor ◽

Tumor Necrosis ◽

Tumor Necrosis Factor Α ◽

Integrin Receptors ◽

Integrin Β1 ◽

Tnf Α ◽

Integrin Α5 ◽

Factor Α ◽

Induced Changes ◽

Necrosis Factor

AbstractThe extracellular matrix (ECM) is important in the regulation of myogenesis. We hypothesized that tumor necrosis factor-α (TNF-α) modifies ECM during differentiation of mouse C2C12 myoblasts. Exogenous TNF-α (1 ng/ml) stimulated myoblast fusion on the 3rdday (by 160% vs control) but not on the 5thday of myogenesis. The level of integrin α5 was significantly augmented by TNF-α during 5 day-differentiation; however, integrin β1 was higher than control only on the 3rdday of cytokine treatment. Both the abundance of integrin α5 bound to actin and the level of integrin β1 complexed with integrin α5 increased in the presence of TNF-α, especially on the 3rdday of differentiation. Similarly, the stimulatory effects of TNF-α on integrin α3, metalloprotease ADAM12 and kinases related to integrins, FAK and ILK, were limited to the 3rdday of differentiation. We concluded that TNF-α-induced changes in ECM components in differentiating myogenic cells, i.e. i) increased expression of integrin α5, β1, α3, and metalloprotease ADAM12, ii) enhanced formation of α5β1 integrin receptors and interaction of integrin α5-cytoskeleton, and iii) increased expression of kinases associated with integrin signaling, FAK and ILK, were temporarily associated with the onset of myocyte fusion.

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Tumor necrosis factor-α inhibits myogenesis through redox-dependent and -independent pathways

AJP Cell Physiology ◽

10.1152/ajpcell.00418.2001 ◽

2002 ◽

Vol 283 (3) ◽

pp. C714-C721 ◽

Cited By ~ 86

Author(s):

Ramon C. J. Langen ◽

Annemie M. W. J. Schols ◽

Marco C. J. M. Kelders ◽

Jos L. J. van der Velden ◽

Emiel F. M. Wouters ◽

...

Keyword(s):

Oxidative Stress ◽

Tumor Necrosis Factor ◽

Tumor Necrosis ◽

Tumor Necrosis Factor Α ◽

Troponin I ◽

Myogenic Differentiation ◽

Inhibitory Effects ◽

Tnf Α ◽

Factor Α ◽

Necrosis Factor

Muscle wasting accompanies diseases that are associated with chronic elevated levels of circulating inflammatory cytokines and oxidative stress. We previously demonstrated that tumor necrosis factor-α (TNF-α) inhibits myogenic differentiation via the activation of nuclear factor-κB (NF-κB). The goal of the present study was to determine whether this process depends on the induction of oxidative stress. We demonstrate here that TNF-α causes a decrease in reduced glutathione (GSH) during myogenic differentiation of C2C12 cells, which coincides with an elevated generation of reactive oxygen species. Supplementation of cellular GSH with N-acetyl-l-cysteine (NAC) did not reverse the inhibitory effects of TNF-α on troponin I promoter activation and only partially restored creatine kinase activity in TNF-α-treated cells. In contrast, the administration of NAC before treatment with TNF-α almost completely restored the formation of multinucleated myotubes. NAC decreased TNF-α-induced activation of NF-κB only marginally, indicating that the redox-sensitive component of the inhibition of myogenic differentiation by TNF-α occurred independently, or downstream of NF-κB. Our observations suggest that the inhibitory effects of TNF-α on myogenesis can be uncoupled in a redox-sensitive component affecting myotube formation and a redox independent component affecting myogenic protein expression.

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

Reproductive Toxicology ◽

10.1016/j.reprotox.2019.05.068 ◽

2019 ◽

Vol 88 ◽

pp. 149-150 ◽

Cited By ~ 1

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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Tumor necrosis factor α Inhibition for Alzheimer’s Disease

Journal of Central Nervous System Disease ◽

10.1177/1179573517709278 ◽

2017 ◽

Vol 9 ◽

pp. 117957351770927 ◽

Cited By ~ 43

Author(s):

Rudy Chang ◽

Kei-Lwun Yee ◽

Rachita K Sumbria

Keyword(s):

Alzheimer’S Disease ◽

Alzheimer's Disease ◽

Tumor Necrosis Factor ◽

Tumor Necrosis ◽

Tumor Necrosis Factor Α ◽

Short Review ◽

Tnf Α ◽

Factor Α ◽

Ad Therapy ◽

Necrosis Factor

Tumor necrosis factor α (TNF-α) plays a central role in the pathophysiology of Alzheimer’s disease (AD). Food and Drug Administration–approved biologic TNF-α inhibitors are thus a potential treatment for AD, but they do not cross the blood-brain barrier. In this short review, we discuss the involvement of TNF-α in AD, challenges associated with the development of existing biologic TNF-α inhibitors for AD, and potential therapeutic strategies for targeting TNF-α for AD therapy.

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Tumor necrosis factor-α-associated lysosomal permeabilization is cathepsin B dependent

AJP Gastrointestinal and Liver Physiology ◽

10.1152/ajpgi.00151.2002 ◽

2002 ◽

Vol 283 (4) ◽

pp. G947-G956 ◽

Cited By ~ 113

Author(s):

Nathan W. Werneburg ◽

M. Eugenia Guicciardi ◽

Steven F. Bronk ◽

Gregory J. Gores

Keyword(s):

Tumor Necrosis Factor ◽

Cathepsin B ◽

Tumor Necrosis ◽

Tumor Necrosis Factor Α ◽

Fluorescent Protein ◽

Tnf Α ◽

Calcein Release ◽

Green Fluorescent ◽

Factor Α ◽

Necrosis Factor

Cathepsin B (Cat B) is released from lysososomes during tumor necrosis factor-α (TNF-α) cytotoxic signaling in hepatocytes and contributes to cell death. Sphingosine has recently been implicated in lysosomal permeabilization and is increased in the liver by TNF-α. Thus the aims of this study were to examine the mechanisms involved in TNF-α-associated lysosomal permeabilization, especially the role of sphingosine. Confocal microscopy demonstrated Cat B-green fluorescent protein and LysoTracker Red were both released from lysosomes after treatment of McNtcp.24 cells with TNF-α/actinomycin D, a finding compatible with lysosomal destabilization. In contrast, endosomes labeled with Texas Red dextran remained intact, suggesting lysosomes were specifically targeted for permeabilization. LysoTracker Red was released from lysosomes in hepatocytes treated with TNF-α or sphingosine in Cat B(+/+) but not Cat B(−/−) hepatocytes, as assessed by a fluorescence-based assay. With the use of a calcein release assay in isolated lysosomes, sphingosine permeabilized liver lysosomes isolated from Cat B(+/+) but not Cat B(−/−) liver. C6ceramide did not permeabilize lysosomes. In conclusion, these data implicate a sphingosine-Cat B interaction inducing lysosomal destabilization during TNF-α cytotoxic signaling.

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