scholarly journals Malate Ameliorates Unilateral Ureter Obstruction (UUO)‐Induced Nephropathy Through Stimulation of Nuclear Factor Erythroid‐2 (Nrf2) and its Related Genes

2021 ◽  
Vol 35 (S1) ◽  
Author(s):  
Osaze Edosuyi ◽  
Ighodaro Igbe ◽  
Myung Choi ◽  
Adebayo Oyekan
Keyword(s):  
Nuclear Factor ◽  
Ureter Obstruction ◽  
Stimulation Of

scholarly journals NF-κB signaling and crosstalk during carcinogenesis

4open ◽  
2019 ◽  
Vol 2 ◽  
pp. 13 ◽  
Author(s):  
Björn L.D.M. Brücher ◽  
Florian Lang ◽  
Ijaz S. Jamall
Keyword(s):  
Cell Proliferation ◽  
Dna Sequences ◽  
Genetic Information ◽  
Normal Cell ◽  
Cell Types ◽  
Nuclear Factor ◽  
Kappa Light Chain ◽  
Sequence Of Events ◽  
Light Chain Enhancer ◽  
Stimulation Of

Transcription factors (TFs) are proteins that control the transcription of genetic information from DNA to mRNA by binding to specific DNA sequences either on their own or with other proteins as a complex. TFs thus support or suppress the recruitment of the corresponding RNA polymerase. In general, TFs are classified by structure or function. The TF, Nuclear factor kappa-light-chain-enhancer of activated B cells (NF-κB), is expressed in all cell types and tissues. NF-κB signaling and crosstalk are involved in several steps of carcinogenesis including in sequences involving pathogenic stimulus, chronic inflammation, fibrosis, establishment of its remodeling to the precancerous niche (PCN) and transition of a normal cell to a cancer cell. Triggered by various inflammatory cytokines, NF-κB is activated along with other TFs with subsequent stimulation of cell proliferation and inhibition of apoptosis. The involvement of NF-κB in carcinogenesis provides an opportunity to develop anti-NF-κB therapies. The complexity of these interactions requires that we elucidate those aspects of NF-κB interactions that play a role in carcinogenesis, the sequence of events leading to cancer.

scholarly journals Withaferin A Inhibits Nuclear Factor-κB-Dependent Pro-Inflammatory and Stress Response Pathways in the Astrocytes

2015 ◽  
Vol 2015 ◽  
pp. 1-9 ◽  
Author(s):  
Francesca Martorana ◽  
Giulia Guidotti ◽  
Liliana Brambilla ◽  
Daniela Rossi
Keyword(s):  
Stress Response ◽  
Cell Types ◽  
Nuclear Factor Κb ◽  
Withaferin A ◽  
Nuclear Factor ◽  
Lps Challenge ◽  
Wide Range ◽  
Cox 2 ◽  
The Impact ◽  
Stimulation Of

Several lines of evidence suggest that astrocytes play a key role in modulating the immune responses of the central nervous system (CNS) to infections, injuries, or pathologies. Yet, their contribution to these processes remains mostly elusive. Astroglia are endowed with a wide range of toll-like receptors (TLR) by which they can sense infectious agents as well as endogenous danger signals released by damaged cells. Here we demonstrate that the activation of astrocytic TLR4 by bacterial lipopolysaccharide (LPS) challenge can promote nuclear factorκB (NF-κB)-dependent induction of pro-inflammatory and stress response mediators, particularly Tumor Necrosis Factorα(TNFα), cyclooxygenase 2 (COX-2), and inducible nitric oxide synthase (iNOS). Since the steroid lactone Withaferin A was described to inhibit NF-κB activity in different cell types, we next determined the impact of this natural compound towards the identified astrocytic signalling pathway. Innate immune activation was induced by stimulation of the LPS/TLR4 axis in spinal cord astrocytes. We provide evidence that both pre-treating and post-treating the cells with Withaferin A attenuate astrocytic NF-κB activity as well as the consequent production of TNFα, COX-2, and iNOS induced by stimulation of the LPS/TLR4 pathway. This study suggests that Withaferin A may be an eligible candidate for the treatment of neuroinflammatory and stress conditions characterized by an important astrocytic input.

scholarly journals Thrombin Stimulation of the Vascular Cell Adhesion Molecule-1 Promoter in Endothelial Cells Is Mediated by Tandem Nuclear Factor-κB and GATA Motifs

2001 ◽  
Vol 276 (50) ◽  
pp. 47632-47641 ◽  
Author(s):  
Takashi Minami ◽  
William C. Aird
Keyword(s):  
Endothelial Cells ◽  
Adhesion Molecule ◽  
Umbilical Vein ◽  
Fold Increase ◽  
Nuclear Factor Κb ◽  
Nuclear Factor ◽  
Mobility Shift ◽  
Response Element ◽  
Vascular Adhesion ◽  
Stimulation Of

The goal of this study was to delineate the transcriptional mechanisms underlying thrombin-mediated induction of vascular adhesion molecule-1 (VCAM-1). Treatment of human umbilical vein endothelial cells with thrombin resulted in a 3.3-fold increase in VCAM-1 promoter activity. The upstream promoter region of VCAM-1 contains a thrombin response element, two nuclear factor κB (NF-κB) motifs, and a tandem GATA motif. In transient transfection assays, mutation of the thrombin response element had no effect on thrombin induction. In contrast, mutation of either NF-κB site resulted in a complete loss of induction, whereas a mutation of the two GATA motifs resulted in a significant reduction in thrombin stimulation. In electrophoretic mobility shift assays, nuclear extracts from thrombin-treated endothelial cells displayed markedly increased binding to the tandem NF-κB and GATA motifs. The NF-κB complex was supershifted with anti-p65 antibodies, but not with antibodies to RelB, c-Rel, p50, or p52. The GATA complex was supershifted with antibodies to GATA-2, but not GATA-3 or GATA-6. A construct containing tandem copies of the VCAM-1 GATA motifs linked to a minimal thymidine kinase promoter was induced 2.4-fold by thrombin. Taken together, these results suggest that thrombin stimulation of VCAM-1 in endothelial cells is mediated by the coordinate action of NF-κB and GATA transcription factors.

scholarly journals Transcription Stimulation of the Fas-encoding Gene by Nuclear Factor for Interleukin-6 Expression upon Influenza Virus Infection

1995 ◽  
Vol 270 (30) ◽  
pp. 18007-18012 ◽  
Author(s):  
Naoya Wada ◽  
Miho Matsumura ◽  
Yoshiki Ohba ◽  
Nobuyuki Kobayashi ◽  
Takenori Takizawa ◽  
...  
Keyword(s):  
Influenza Virus ◽  
Virus Infection ◽  
Interleukin 6 ◽  
Influenza Virus Infection ◽  
Nuclear Factor ◽  
Encoding Gene ◽  
Stimulation Of

Dexamethasone inhibits stimulation of pulmonary endothelins by proinflammatory cytokines: possible involvement of a nuclear factor κB dependent mechanism

2001 ◽  
Vol 27 (4) ◽  
pp. 751-756 ◽  
Author(s):  
Thomas Dschietzig ◽  
Christoph Richter ◽  
Gert Pfannenschmidt ◽  
Cornelia Bartsch ◽  
Michael Laule ◽  
...  
Keyword(s):  
Proinflammatory Cytokines ◽  
Nuclear Factor Κb ◽  
Nuclear Factor ◽  
Dependent Mechanism ◽  
Stimulation Of

scholarly journals Two regions within the DNA binding domain of nuclear factor I interact with DNA and stimulate adenovirus DNA replication independently.

1996 ◽  
Vol 16 (8) ◽  
pp. 4073-4080 ◽  
Author(s):  
J Dekker ◽  
J A van Oosterhout ◽  
P C van der Vliet
Keyword(s):  
Dna Replication ◽  
Dna Binding ◽  
Dna Polymerase ◽  
Binding Domain ◽  
Nuclear Factor ◽  
Dna Binding Domain ◽  
Factor I ◽  
Terminal Domain ◽  
Nuclear Factor I ◽  
Stimulation Of

The cellular transcription factor nuclear factor I (NFI) stimulates adenovirus DNA replication by up to 50-fold. The NFI DNA binding domain (NFI-BD) is sufficient for stimulation and interacts with the viral DNA polymerase, thereby recruiting the precursor terminal protein-DNA polymerase complex (pTP-pol) to the origin of replication. The mechanism of DNA binding by NFI is unknown. To examine DNA binding and stimulation of adenovirus DNA replication by NFI-BD in more detail, we generated a series of deletion mutants and show that the DNA binding domain of NFI consists of two subdomains: a highly basic N-terminal domain that binds nonspecifically to DNA and a C-terminal domain that binds specifically but with very low affinity to the NFI recognition site. Both of these subdomains stimulate DNA replication, although not to the same extent as the intact DNA binding domain. The N-terminal domain has an alpha-helical structure, as shown by circular dichroism spectroscopy. The C-terminal domain interacts with the pTP-pol complex and is able to recruit the pTP-pol complex to DNA, which leads to pTP-pol-dependent stimulation of replication. The N-terminal domain also stimulates replication in a pTP-pol-dependent manner and enhances binding of pTP-pol to DNA. Since we could not detect a direct protein-protein interaction between pTP-pol and the N-terminal domain, we suggest that this domain stimulates replication by inducing structural changes in the DNA.

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