VF‐4 and DR‐8 derived from salted egg white inhibit inflammatory activity via NF‐κB/PI3K‐Akt/MAPK signal transduction pathways in HT‐29 cells induced by TNF‐α

2021 ◽  
pp. 2100682
Author(s):  
Na Zhou ◽  
Yao Yao ◽  
Na Wu ◽  
Huaying Du ◽  
Mingsheng Xu ◽  
...  
Keyword(s):  
Signal Transduction ◽  
Egg White ◽  
Inflammatory Activity ◽  
Signal Transduction Pathways ◽  
Tnf Α ◽  
Ht 29

scholarly journals Opposing effects of tumour necrosis factor α and hyperosmolarity on Na+/myo-inositol co-transporter mRNA levels and myo-inositol accumulation by 3T3-L1 adipocytes

1998 ◽  
Vol 336 (2) ◽  
pp. 317-325 ◽  
Author(s):  
Mark A. YOREK ◽  
Joyce A. DUNLAP ◽  
William L. LOWE
Keyword(s):  
Signal Transduction ◽  
Tumour Necrosis ◽  
Actinomycin D ◽  
Signal Transduction Pathways ◽  
Mrna Levels ◽  
Tumour Necrosis Factor Α ◽  
Tnf Α ◽  
Factor Α ◽  
Opposing Effects ◽  
Necrosis Factor

Tumour necrosis factor α (TNF-α) regulates the transport of myo-inositol in 3T3-L1 adipocytes. Treating 3T3-L1 adipocytes with TNF-α decreases Na+/myo-inositol co-transporter (SMIT) mRNA levels and myo-inositol accumulation in a concentration-and time-dependent manner. TNF-α decreases the V′max for high-affinity myo-inositol transport with little change in the K′m. Studies with actinomycin D suggest that RNA synthesis is required for the TNF-α-induced effect on SMIT mRNA levels. In contrast with the effect of TNF-α, hyperosmolarity increases SMIT mRNA levels and myo-inositol accumulation in 3T3-L1 adipocytes. Hyperosmolarity increases SMIT gene expression as evidenced by the inhibition of hyperosmotic induction of SMIT mRNA levels by actinomycin D, and of myo-inositol accumulation by actinomycin D and cycloheximide. TNF-α and osmotic stress have previously been shown to activate similar signal transduction pathways in mammalian cells. In 3T3-L1 adipocytes, both TNF-α and hyperosmolarity increase mitogen-activated protein kinase kinase pathway activity; however, with the possible exception of c-Jun N-terminal kinase, this pathway does not seem to regulate SMIT mRNA levels or myo-inositol accumulation. TNF-α activates nuclear factor κB (NF-κB) in 3T3-L1 adipocytes but, unlike the effect of TNF-α on cultured endothelial cells, NF-κB does not seem to contribute to the regulation by TNF-α of SMIT gene expression in 3T3-L1 adipocytes. Therefore other signal transduction pathways must be considered in the regulation by TNF-α of SMIT mRNA levels and activity. Thus TNF-α and hyperosmolarity have opposing effects on SMIT mRNA levels and activity in 3T3-L1 adipocytes. Because myo-inositol in the form of phosphoinositides is an important component of membranes and signal transduction pathways, the regulation of myo-inositol metabolism by TNF-α might represent another mechanism by which TNF-α regulates adipocyte function.

Fibronectin and cytokines increase JNK, ERK, AP-1 activity, and transin gene expression in rat hepatic stellate cells

1997 ◽  
Vol 273 (4) ◽  
pp. G804-G811 ◽  
Author(s):  
John E. Poulos ◽  
Jason D. Weber ◽  
Joseph M. Bellezzo ◽  
Adrian M. Di Bisceglie ◽  
Robert S. Britton ◽  
...  
Keyword(s):  
Gene Expression ◽  
Signal Transduction ◽  
Matrix Metalloproteinase ◽  
Inflammatory Cytokines ◽  
Hepatic Stellate Cells ◽  
Fold Increase ◽  
Stellate Cells ◽  
Signal Transduction Pathways ◽  
Tnf Α ◽  
Erk Activity

Cytokines, growth factors, and alterations in the extracellular matrix composition may play a role in maintaining hepatic stellate cells (HSC) in the activated state that is responsible for hepatic fibrogenesis. However, the signal transduction pathways that are stimulated by these factors in HSC remain to be fully elucidated. Recent evidence indicates that the mitogen-activated protein kinase (MAPK) family, including c-Jun NH2-terminal kinase (JNK) and extracellular signal-regulated kinase (ERK), plays an important role in the cellular response to stress. The aims of this study were to investigate whether fibronectin (FN) or the inflammatory cytokines interleukin-1α (IL-1α) and tumor necrosis factor-α (TNF-α) activate JNK, ERK, and AP-1 activity in HSC and induce the gene expression of the matrix metalloproteinase transin. Treatment of HSC with FN resulted in an up to 4.5-fold increase in ERK activity and a 2.1-fold increase in JNK activity. IL-1α and TNF-α produced up to a fourfold increase in JNK activity and a twofold increase in ERK activity. We then compared the effects of FN, IL-1α, and TNF-α on AP-1 activity and metalloproteinase mRNA induction. All three compounds increased AP-1 binding and promoter activity, and transin mRNA levels were increased 1.8-fold by FN, 2.2-fold by IL-1α, and 2.8-fold by TNF-α. Therefore, FN and inflammatory cytokines increase MAPK activity, stimulate AP-1 activity, and increase transin gene expression in HSC. Signal transduction pathways involving the MAPK family may play an important role in the regulation of matrix metalloproteinase expression by cytokines and FN in HSC.

TNF-α and IFN-γ-mediated signal transduction pathways: Effects on IRF-1 and MHC class I gene expression in oligodendrocytes

1997 ◽  
Vol 56 ◽  
pp. 465
Author(s):  
C. Agresti ◽  
A. Bernardo ◽  
N. Del Russo ◽  
G. Marziali ◽  
A. Battistini ◽  
...  
Keyword(s):  
Gene Expression ◽  
Signal Transduction ◽  
Mhc Class I ◽  
Class I ◽  
Signal Transduction Pathways ◽  
Tnf Α ◽  
Ifn Γ ◽  
I Gene ◽  
Mhc Class I Gene

scholarly journals Blood mononuclear cell production of TNF-α and IL-8: engagement of different signal transduction pathways including the p42 MAP kinase pathway

1998 ◽  
Vol 64 (1) ◽  
pp. 124-133 ◽  
Author(s):  
Jami L. Foreback ◽  
Vidya Sarma ◽  
Nicholas R. Yeager ◽  
Ellen M. Younkin ◽  
Daniel G. Remick ◽  
...  
Keyword(s):  
Signal Transduction ◽  
Map Kinase ◽  
Mononuclear Cell ◽  
Signal Transduction Pathways ◽  
Cell Production ◽  
Tnf Α ◽  
Map Kinase Pathway ◽  
Kinase Pathway

Signal-regulated oxidation of proteins via MICAL

2020 ◽  
Vol 48 (2) ◽  
pp. 613-620
Author(s):  
Clara Ortegón Salas ◽  
Katharina Schneider ◽  
Christopher Horst Lillig ◽  
Manuela Gellert
Keyword(s):  
Signal Transduction ◽  
Hydrogen Peroxide ◽  
Cell Death ◽  
Redox Regulation ◽  
Signal Transduction Pathways ◽  
Cellular Functions ◽  
Intracellular Signals ◽  
Amino Acid Side Chains ◽  
Specific Receptors ◽  
Sulfur Containing

Processing of and responding to various signals is an essential cellular function that influences survival, homeostasis, development, and cell death. Extra- or intracellular signals are perceived via specific receptors and transduced in a particular signalling pathway that results in a precise response. Reversible post-translational redox modifications of cysteinyl and methionyl residues have been characterised in countless signal transduction pathways. Due to the low reactivity of most sulfur-containing amino acid side chains with hydrogen peroxide, for instance, and also to ensure specificity, redox signalling requires catalysis, just like phosphorylation signalling requires kinases and phosphatases. While reducing enzymes of both cysteinyl- and methionyl-derivates have been characterised in great detail before, the discovery and characterisation of MICAL proteins evinced the first examples of specific oxidases in signal transduction. This article provides an overview of the functions of MICAL proteins in the redox regulation of cellular functions.

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