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1
Johns, L. D., T. Sarr et G. E. Ranges. « Inhibition of ceramide pathway does not affect ability of TNF-alpha to activate nuclear factor-kappa B. » Journal of Immunology 152, no 12 (15 juin 1994) : 5877–82. http://dx.doi.org/10.4049/jimmunol.152.12.5877.
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Abstract TNF-alpha is a multifunctional cytokine that has been shown to activate a number of intracellular second messenger pathways. Recent studies demonstrate that the sphingomyelinase-ceramide pathway plays a potential role in the activation of nuclear factor-kappa B (NF-kappa B) by TNF-alpha. The following experiments both confirm that the addition of ceramide to cells can activate NF-kappa B and demonstrate that a 48-h pretreatment with phorbol 12-myristate (PMA) results in the loss of the ceramide-induced NF-kappa B response. In parallel experiments, in which SW480 cells were pretreated with PMA, TNF-alpha provided a signal resulting in the nuclear translocation of NF-kappa B that was similar to untreated cells. These data combined suggest that additional pathways exist that TNF-alpha can use for the activation of NF-kappa B. Supplementary data demonstrates that TNF-alpha, ceramide, and PMA activate a human cytomegalovirus-(HCMV) beta gal construct (promoter is responsive to NF-kappa B) that was stably transfected into the TNF receptor-bearing tumor cell line, SW480. PMA pretreatment of these cells resulted in a significant decrease in both the PMA and ceramide generated responses, 6% and 0% of controls, respectively. However, the response generated by TNF-alpha was not inhibited significantly (96% of control cells). This data suggests that although ceramide and 1,2-diacylglycerol (DAG) pathways may contribute to TNF-alpha activation of NF-kappa B, impedance of these pathways does not block TNF-alpha from activating NF-kappa B nor induction of the functional activation of the NF-kappa B responsive reporter construct, HCMV.
2
Otieno, M. A., et M. W. Anders. « Cysteine S-conjugates activate transcription factor NF-kappa B in cultured renal epithelial cells ». American Journal of Physiology-Renal Physiology 273, no 1 (1 juillet 1997) : F136—F143. http://dx.doi.org/10.1152/ajprenal.1997.273.1.f136.
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Activation of NF-kappa B by the nephrotoxic and cytotoxic cysteine S-conjugate S-(1,2-dichlorovinyl)-L-cysteine (DCVC) was investigated in porcine kidney-derived LLC-PK1 cells. DCVC induced binding of nuclear proteins to an NF-kappa B consensus oligonucleotide from the immunoglobulin kappa-light chain enhancer region, as determined by electrophoretic mobility shift assays, and the activated proteins were identified as the p50/RelA heterodimeric complex of NF-kappa B. Transient transfection experiments with a kappa B-controlled luciferase reporter construct showed that the NF-kappa B complex activated by DCVC was transcriptionally active. NF-kappa B transactivation was blocked by inhibition of DCVC bioactivation with the cysteine conjugate beta-lyase inhibitor (aminooxy)acetic acid, by the antioxidants N,N'-diphenyl-p-phenylenediamine and N-acetyl-L-cysteine, and by the protein kinase inhibitor staurosporine. The cysteine S-conjugates S-(2-bromo-2-chloro-1,1-difluoroethyl)-L-cysteine and S-(2-chloro-1,1,2-trifluoroethyl)-L-cysteine also activated NF-kappa B in LLC-PK1 cells. These results demonstrate that the NF-kappa B pathway is present in LLC-PK1 cells and is induced by cysteine S-conjugates. Inhibition of DCVC-induced transactivation of NF-kappa B by staurosporine and by antioxidants indicate roles for protein kinases and oxidative stress in the NF-kappa B pathway.
3
Berberich, I., G. L. Shu et E. A. Clark. « Cross-linking CD40 on B cells rapidly activates nuclear factor-kappa B. » Journal of Immunology 153, no 10 (15 novembre 1994) : 4357–66. http://dx.doi.org/10.4049/jimmunol.153.10.4357.
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Abstract The B cell-associated surface molecule CD40 functions to regulate B cell responses. Cross-linking CD40 on B cells can lead to homotypic cell adhesion, IL-6 production, and, in combination with cytokines, to Ig isotype switching. Tyrosine kinase activity is increased shortly after engagement of this receptor. Little is known about how the very early events induced by CD40 cross-linking link to cellular responses. In this study, we demonstrate that nuclear factor (NF)-kappa B and NF-kappa B-like transcription factors are activated after cross-linking CD40 on resting human tonsillar B cells and on B cell lines. The activation is rapid and is mediated through a tyrosine kinase-dependent pathway. The complexes detected in electrophoretic mobility shift assays contain p50, p65 (RelA), c-Rel, and most likely other components. By using transient transfection assays, we found that cross-linking CD40 supports NF-kappa B-dependent gene expression. Our results define the NF-kappa B system as an intermediate event in CD40 signaling and suggest that the CD40 pathway can influence the expression of B cell-associated genes with NF-kappa B consensus sites.
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Lalmanach-Girard, A. C., T. C. Chiles, D. C. Parker et T. L. Rothstein. « T cell-dependent induction of NF-kappa B in B cells. » Journal of Experimental Medicine 177, no 4 (1 avril 1993) : 1215–19. http://dx.doi.org/10.1084/jem.177.4.1215.
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In comparison to B cell stimulation mediated by surface immunoglobulin (Ig) antigen receptor ligation, little is known about the intracellular events associated with T cell-dependent B cell responses. A model for the efferent phase of T cell-B cell interaction was used to examine the capacity of activated T cells to trigger nuclear expression of the trans-acting transcription factor, NF-kappa B, in B cells. Fixed, activated, but not fixed, resting Th2 cells were found to induce increased binding activity for a kappa B site-containing oligonucleotide in a time-dependent manner. This induction of NF-kappa B was eliminated by an antibody directed against a 39-kD cell interaction protein on activated T cells as well as by a soluble form of B cell CD40. Of particular relevance to intracellular signaling, NF-kappa B induction was not diminished by prior depletion of B cell protein kinase C (PKC) with phorbol myristate acetate. These results strongly suggest that T cell-dependent B cell stimulation is associated with NF-kappa B induction via p39-CD40 interaction and that this is brought about by non-PKC dependent signaling, in marked contrast to the previously documented requirement for PKC in sIg receptor-mediated stimulation. This suggest that NF-kappa B responds to more than one receptor-mediated intracellular signaling pathway in B cells and may be part of a "final common pathway" for B cell stimulation.
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Suzuki, Y. J., M. Mizuno et L. Packer. « Signal transduction for nuclear factor-kappa B activation. Proposed location of antioxidant-inhibitable step. » Journal of Immunology 153, no 11 (1 décembre 1994) : 5008–15. http://dx.doi.org/10.4049/jimmunol.153.11.5008.
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Abstract Reactive oxygen species are thought to be messengers for nuclear factor (NF)-kappa B activation because its activation can be abrogated by antioxidants. However, this study identifies, for the first time, NF-kappa B activators that are insensitive to antioxidants. NF-kappa B activation that is induced by either calyculin A or okadaic acid (inhibitors of serine/threonine protein phosphatases 1 and 2A) is not blocked by N-acetylcysteine or dihydrolipoate in Jurkat and U937 cells. Nonetheless, these antioxidants block induction by TNF-alpha, lymphotoxin, and PMA. Unlike okadaic acid and calyculin A, neither TNF-alpha, lymphotoxin, nor PMA inhibited activities of phosphatases 1 and 2A. NF-kappa B activation induced by okadaic acid or calyculin A was not blocked by a myosin light chain kinase inhibitor, but was prevented by a protease inhibitor. The mitochondrial inhibitor, rotenone, also inhibited NF-kappa B activation by calyculin A; however, this inhibition was accompanied by a depletion of cellular ATP. These results suggest that 1) phosphatase inhibitors either target a component of signal transduction, which occurs downstream to an antioxidant-sensitive step or use distinct signaling pathways; 2) inhibition of phosphatases 1 and 2A is not a step in the pathway of TNF-alpha-, lymphotoxin-, or PMA-induced NF-kappa B activation; 3) myosin light chain kinase does not participate in NF-kappa B activation; and 4) activation of NF-kappa B by phosphatase inhibitors is controlled by proteases.
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Dominguez, I., L. Sanz, F. Arenzana-Seisdedos, M. T. Diaz-Meco, J. L. Virelizier et J. Moscat. « Inhibition of protein kinase C zeta subspecies blocks the activation of an NF-kappa B-like activity in Xenopus laevis oocytes ». Molecular and Cellular Biology 13, no 2 (février 1993) : 1290–95. http://dx.doi.org/10.1128/mcb.13.2.1290-1295.1993.
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Nuclear factor kappa B (NF-kappa B) plays a critical role in the regulation of a large variety of cellular genes. However, the mechanism whereby this nuclear factor is activated remains to be determined. In this report, we present evidence that in oocytes from Xenopus laevis, (i) ras p21- and phospholipase C (PLC)-mediated phosphatidylcholine (PC) hydrolysis activates NF-kappa B and (ii) protein kinase C zeta subspecies is involved in the activation of NF-kappa B in response to insulin/ras p21/PC-PLC. Thus, the microinjection of either ras p21 or PC-PLC, or the exposure of oocytes to insulin, promotes a significant translocation to the nucleus of an NF-kappa B-like activity. This effect is not observed when oocytes are incubated with phorbol myristate acetate or progesterone, both of which utilize a ras p21-independent pathway for oocyte activation. These data strongly suggest a critical role of the insulin/ras p21/PC-PLC/protein kinase C zeta pathway in the control of NF-kappa B activation.
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Dominguez, I., L. Sanz, F. Arenzana-Seisdedos, M. T. Diaz-Meco, J. L. Virelizier et J. Moscat. « Inhibition of protein kinase C zeta subspecies blocks the activation of an NF-kappa B-like activity in Xenopus laevis oocytes. » Molecular and Cellular Biology 13, no 2 (février 1993) : 1290–95. http://dx.doi.org/10.1128/mcb.13.2.1290.
Texte intégralRésumé :
Nuclear factor kappa B (NF-kappa B) plays a critical role in the regulation of a large variety of cellular genes. However, the mechanism whereby this nuclear factor is activated remains to be determined. In this report, we present evidence that in oocytes from Xenopus laevis, (i) ras p21- and phospholipase C (PLC)-mediated phosphatidylcholine (PC) hydrolysis activates NF-kappa B and (ii) protein kinase C zeta subspecies is involved in the activation of NF-kappa B in response to insulin/ras p21/PC-PLC. Thus, the microinjection of either ras p21 or PC-PLC, or the exposure of oocytes to insulin, promotes a significant translocation to the nucleus of an NF-kappa B-like activity. This effect is not observed when oocytes are incubated with phorbol myristate acetate or progesterone, both of which utilize a ras p21-independent pathway for oocyte activation. These data strongly suggest a critical role of the insulin/ras p21/PC-PLC/protein kinase C zeta pathway in the control of NF-kappa B activation.
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Singh, Shareen, et Thakur Gurjeet Singh. « Role of Nuclear Factor Kappa B (NF-κB) Signalling in Neurodegenerative Diseases : An Mechanistic Approach ». Current Neuropharmacology 18, no 10 (4 novembre 2020) : 918–35. http://dx.doi.org/10.2174/1570159x18666200207120949.
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A transcriptional regulatory nuclear factor kappa B (NF-κB) protein is a modulator of cellular biological activity via binding to a promoter region in the nucleus and transcribing various protein genes. The recent research implicated the intensive role of nuclear factor kappa B (NF-κB) in diseases like autoimmune disorder, inflammatory, cardiovascular and neurodegenerative diseases. Therefore, targeting the nuclear factor kappa B (NF-κB) protein offers a new opportunity as a therapeutic approach. Activation of IκB kinase/NF-κB signaling pathway leads to the development of various pathological conditions in human beings, such as neurodegenerative, inflammatory disorders, autoimmune diseases, and cancer. Therefore, the transcriptional activity of IκB kinase/NF- κB is strongly regulated at various cascade pathways. The nuclear factor NF-kB pathway plays a major role in the expression of pro-inflammatory genes, including cytokines, chemokines, and adhesion molecules. In response to the diverse stimuli, the cytosolic sequestered NF-κB in an inactivated form by binding with an inhibitor molecule protein (IkB) gets phosphorylated and translocated into the nucleus further transcribing various genes necessary for modifying various cellular functions. The various researches confirmed the role of different family member proteins of NF-κB implicated in expressing various genes products and mediating various cellular cascades. MicroRNAs, as regulators of NF- κB microRNAs play important roles in the regulation of the inflammatory process. Therefore, the inhibitor of NF-κB and its family members plays a novel therapeutic target in preventing various diseases. Regulation of NF- κB signaling pathway may be a safe and effective treatment strategy for various disorders.
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Lin, K. I., S. H. Lee, R. Narayanan, J. M. Baraban, J. M. Hardwick et R. R. Ratan. « Thiol agents and Bcl-2 identify an alphavirus-induced apoptotic pathway that requires activation of the transcription factor NF-kappa B. » Journal of Cell Biology 131, no 5 (1 décembre 1995) : 1149–61. http://dx.doi.org/10.1083/jcb.131.5.1149.
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Oxidative stress has been proposed as a common mediator of apoptotic death. To investigate further the role of oxidants in this process we have studied the effects of antioxidants on Sindbis virus (SV)-induced apoptosis in two cell lines, AT-3 (a prostate carcinoma line) and N18 (a neuroblastoma line). The thiol antioxidant, N-acetylcysteine (NAC), at concentrations above 30 mM, completely abrogates SV-induced apoptosis in AT-3 and N18 cells. The effects of NAC cannot be attributed to inhibition of viral entry or viral replication, changes in extracellular osmolarity or to increases in cellular glutathione levels, nor can they be mimicked by chelators of trace metals, inhibitors of lipid peroxidation or peroxide scavengers. In contrast, other thiol agents including pyrrolidine dithiocarbamate (PDTC, 75 microM) are protective. Because NAC and PDTC are among the most effective inhibitors of the transcription factor NF-kappa B, we examined SV's ability to activate NF-kappa B before the onset of morphologic or biochemical evidence of apoptosis. Within hours of infection, SV induced a robust increase in nuclear NF-kappa B activity in AT-3 and N18 cells; this activation was suppressible by NAC and PDTC. Over-expression of bcl-2 in AT-3 cells, which has been shown to inhibit SV-induced apoptosis, also inhibits SV-induced NF-kappa B activation. To determine if NF-kappa B activation is necessary for SV-induced apoptosis in these cells, we used double stranded oligonucleotides with consensus NF-kappa B sequences as transcription factor decoys (TFDs) to inhibit NF-kappa B binding to native DNA sites. Wild-type, but not mutant, TFDs inhibit SV-induced apoptosis in AT-3 cells. In contrast, TFD inhibition of NF-kappa B nuclear activity in N18 cells did not prevent SV-induced apoptosis. Taken together, these observations define a cell type-specific, transcription factor signaling pathway necessary for SV-induced apoptosis. Understanding the precise mechanism by which Bcl-2 and thiol agents inhibit SV-induced nuclear NF-kappa B activity in AT-3 cells may provide insights into the pluripotent antiapoptotic actions of these agents.
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Blackwell, T. S., T. R. Blackwell, E. P. Holden, B. W. Christman et J. W. Christman. « In vivo antioxidant treatment suppresses nuclear factor-kappa B activation and neutrophilic lung inflammation. » Journal of Immunology 157, no 4 (15 août 1996) : 1630–37. http://dx.doi.org/10.4049/jimmunol.157.4.1630.
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Abstract We hypothesized that endotoxin injection in rats would stimulate in vivo nuclear factor-kappa B (NF-kappa B) activation in lung tissue and that antioxidant treatment before endotoxin injection would attenuate endotoxin-induced NF-kappa B activation, chemokine gene expression, and neutrophilic lung inflammation. We studied NF-kappa B activation in rat lung tissue following a single i.p. injection of endotoxin (6 mg/kg). After in vivo endotoxin treatment, lung NF-kappa B activation peaked at 2 h and temporally correlated with the expression of cytokine-induced neutrophil chemoattractant mRNA in lung tissue. Treatment with the antioxidant N-acetylcysteine (NAC) 1 h before endotoxin resulted in decreased lung NF-kappa B activation in a dose-dependent manner (from 200-1000 mg/kg) and diminished cytokine-induced neutrophil chemoattractant mRNA expression in lung tissue. Treatment with NAC significantly suppressed endotoxin-induced neutrophilic alveolitis. The average total lung lavage neutrophil count was 5.5 x 10(6) with endotoxin treatment vs 0.9 x 10(6) with NAC treatment before endotoxin. The NF-kappa B pathway represents an attractive therapeutic target for strategies to control neutrophilic inflammation and lung injury.
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Lederer, J. A., J. S. Liou, S. Kim, N. Rice et A. H. Lichtman. « Regulation of NF-kappa B activation in T helper 1 and T helper 2 cells. » Journal of Immunology 156, no 1 (1 janvier 1996) : 56–63. http://dx.doi.org/10.4049/jimmunol.156.1.56.
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Abstract In most cell types, NF-kappa B is activated by release from a cytoplasmic inhibitor protein, I kappa B, followed by its translocation to the nucleus where it binds to the regulatory regions of many genes, including the IL-2 gene in T lymphocytes. We have previously shown by electrophoretic mobility shift assays that nuclear extracts prepared from activated, non-IL-2-producing Th2 cell clones. We show here that Th-1 and Th2 cells have similar levels of cytoplasmic p65(RelA) and p50, but TCR stimulation fails to induce the nuclear translocation of p65(RelA) in Th2 cells. Nuclear translocation of p65(RelA) can be induced by IL-1 stimulation of Th2 cells, indicating that a basic mechanism of NF-Kappa B activation common to many cells is intact in Th2 cells. We demonstrate that IL-1 and TNF induce rapid nuclear translocation of p65(RelA) in T cell clones, whereas TCR-induced NF-Kappa B activation in Th1 cells is delayed and may be longer in duration. This suggests that the TCR pathway of NF-Kappa B activation is different from the cytokine pathway. Furthermore, we show that Th1 and Th2 cells express different levels and/or different forms of I kappa B alpha, and that cytokines, but not TCR stimuli, significantly modulate detectable levels of cytoplasmic I kappa B alpha.
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Xia, Longzheng, Shiming Tan, Yujuan Zhou, Jingguan Lin, Heran Wang, Linda Oyang, Yutong Tian et al. « Role of the NFκB-signaling pathway in cancer ». OncoTargets and Therapy Volume 11 (avril 2018) : 2063–73. http://dx.doi.org/10.2147/ott.s161109.
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Kichina, Julia V. « Transposons find a small RIP in NFκB pathway ». Cell Cycle 7, no 14 (15 juillet 2008) : 2081–82. http://dx.doi.org/10.4161/cc.7.14.6598.
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王, 文静. « Regulation of NF-Kappa B Signaling Pathway by Hepatitis Viruses ». Hans Journal of Biomedicine 10, no 03 (2020) : 35–42. http://dx.doi.org/10.12677/hjbm.2020.103006.
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Salles, Angeles, Arturo Romano et Ramiro Freudenthal. « Synaptic NF-kappa B pathway in neuronal plasticity and memory ». Journal of Physiology-Paris 108, no 4-6 (septembre 2014) : 256–62. http://dx.doi.org/10.1016/j.jphysparis.2014.05.002.
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Law, R. E., J. B. Stimmel, M. A. Damore, C. Carter, S. Clarke et R. Wall. « Lipopolysaccharide-induced NF-kappa B activation in mouse 70Z/3 pre-B lymphocytes is inhibited by mevinolin and 5'-methylthioadenosine : roles of protein isoprenylation and carboxyl methylation reactions ». Molecular and Cellular Biology 12, no 1 (janvier 1992) : 103–11. http://dx.doi.org/10.1128/mcb.12.1.103-111.1992.
Texte intégralRésumé :
We show that both the lipopolysaccharide (LPS)-induced activation of NF-kappa DNA binding and kappa gene expression are blocked by treating murine pre-B lymphocyte 70Z/3 cells with 5'-methylthioadenosine (MTA), an inhibitor of several S-adenosylmethionine-dependent methylation reactions. We further show that the LPS-induced incorporation of radioactivity from [methyl-3H]methionine into methyl ester-like linkages on a group of membrane polypeptides is also inhibited by MTA treatment, suggesting the involvement of protein methylation reactions in the LPS signal transduction pathway. We also find that NF-kappa B and kappa gene activation in LPS-treated 70Z/3 cells is blocked by mevinolin, an inhibitor that prevents protein isoprenylation. Interestingly, mevinolin-treated cells also exhibited a marked reduction in the methylation of membrane proteins. Neither MTA nor mevinolin significantly inhibited NF-kappa B activation by phorbol myristate acetate, suggesting that these agents act early in signal transduction. These results provide the first evidence that carboxyl methylated and/or isoprenylated proteins play an essential role in the LPS-signaling pathway.
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Law, R. E., J. B. Stimmel, M. A. Damore, C. Carter, S. Clarke et R. Wall. « Lipopolysaccharide-induced NF-kappa B activation in mouse 70Z/3 pre-B lymphocytes is inhibited by mevinolin and 5'-methylthioadenosine : roles of protein isoprenylation and carboxyl methylation reactions. » Molecular and Cellular Biology 12, no 1 (janvier 1992) : 103–11. http://dx.doi.org/10.1128/mcb.12.1.103.
Texte intégralRésumé :
We show that both the lipopolysaccharide (LPS)-induced activation of NF-kappa DNA binding and kappa gene expression are blocked by treating murine pre-B lymphocyte 70Z/3 cells with 5'-methylthioadenosine (MTA), an inhibitor of several S-adenosylmethionine-dependent methylation reactions. We further show that the LPS-induced incorporation of radioactivity from [methyl-3H]methionine into methyl ester-like linkages on a group of membrane polypeptides is also inhibited by MTA treatment, suggesting the involvement of protein methylation reactions in the LPS signal transduction pathway. We also find that NF-kappa B and kappa gene activation in LPS-treated 70Z/3 cells is blocked by mevinolin, an inhibitor that prevents protein isoprenylation. Interestingly, mevinolin-treated cells also exhibited a marked reduction in the methylation of membrane proteins. Neither MTA nor mevinolin significantly inhibited NF-kappa B activation by phorbol myristate acetate, suggesting that these agents act early in signal transduction. These results provide the first evidence that carboxyl methylated and/or isoprenylated proteins play an essential role in the LPS-signaling pathway.
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Murray, Susan E., Alexander M. Rowe, Soumen Basak, Alexander Hoffmann et David C. Parker. « The alternative NF-kappa B pathway is essential for OX40-induced CD4 T cell differentiation and effector function (47.19) ». Journal of Immunology 182, no 1_Supplement (1 avril 2009) : 47.19. http://dx.doi.org/10.4049/jimmunol.182.supp.47.19.
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Abstract Nuclear factor-kappa B (NF-κB) is an evolutionarily conserved signaling pathway that alerts the immune system to infection and danger. NF-κB can be divided broadly into two pathways-the canonical pathway regulated by IκB and the alternative pathway that depends on NF-κB inducing kinase (NIK) and IKKα. Mediators as divergent as pathogen-associated antigens, reactive oxygen species, UV light, and cytokines can activate the canonical NF-κB pathway. Activation of the alternative pathway seems to be limited to a subset of TNFRs, the best studied of which are LTβR, BAFFR, and CD40. Mice with lesions in the alternative NF-κB pathway have disorganized lymphoid structures and few peripheral B cells, but T cell responses in these mice have been less well-studied. Here, we show that the costimulatory TNFR, OX40 (CD134), activates the alternative NF-κB pathway in primary CD4 T cells. Activation of the alternative NF-κB pathway is necessary for OX40-induced differentiation and acquisition of effector function in vivo. Moreover, inability to activate the alternative NF-κB pathway rendered T cells unable to induce lethal GVHD. These results demonstrate a critical role for the alternative NF-κB pathway in CD4 T cell responses, and suggest that interventions targeting this pathway may have therapeutic potential. Supported by NIH R21 AI077032 (D.C.P.) and NIH T32 HL007781 (S.E.M.)
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Yokoo, T., et M. Kitamura. « Antioxidant PDTC induces stromelysin expression in mesangial cells via a tyrosine kinase-AP-1 pathway ». American Journal of Physiology-Renal Physiology 270, no 5 (1 mai 1996) : F806—F811. http://dx.doi.org/10.1152/ajprenal.1996.270.5.f806.
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We found that pyrrolidine dithiocarbamate (PDTC) induces the matrix metalloproteinase stromelysin in cultured glomerular mesangial cells. Although PDTC is a well-known inhibitor of nuclear factor-kappa B (NF-kappa B), this effect was independent of the NF-kappa B activity, since overexpression of a dominant negative mutant of p50 NF-kappa B subunit repressed activity of the kappa B site, whereas it failed to induce stromelysin. To elucidate the intracellular mechanisms involved, we focused on the role of activator protein 1 (AP-1), since its binding site, the 12-O-tetradecanoylphorbol 13-acetate (TPA) response element (TRE), is located in the 5'-flanking region of the stromelysin gene. Northern blot analysis revealed that PDTC upregulated expression of c-jun and c-fos before the expression of stromelysin. Transient transfection studies using a TRE-LacZ reporter plasmid elucidated that activity of AP-1 was significantly increased by PDTC. Stable transfection with a c-jun antisense cDNA or pretreatment with curcumin, a pharmacological inhibitor of c-Jun/AP-1, revealed that inactivation of AP-1 diminished the induction of stromelysin by PDTC. To identify the machinery involved upstream of AP-1 activation, the role of tyrosine kinases was investigated. Western blot analysis showed that PDTC induced phosphorylation of tyrosine kinases. Treatment of mesangial cells with tyrosine kinase inhibitors suppressed activation of AP-1 as well as induction of stromelysin by PDTC. These findings demonstrate that the antioxidant PDTC induces stromelysin expression via stimulation of the tyrosine kinase-AP-1 pathway independent of its suppressive action on NF-kappa B.
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Scheinman, R. I., A. A. Beg et A. S. Baldwin. « NF-kappa B p100 (Lyt-10) is a component of H2TF1 and can function as an I kappa B-like molecule ». Molecular and Cellular Biology 13, no 10 (octobre 1993) : 6089–101. http://dx.doi.org/10.1128/mcb.13.10.6089-6101.1993.
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NF-kappa B is an important transcription factor regulating expression of genes involved in immune function, inflammation, and cellular growth control. NF-kappa B activity is induced by numerous stimuli, such as phorbol esters, B- and T-cell mitogens, the cytokines tumor necrosis factor and interleukin-1, and serum growth factors. The standard model for the induction of NF-kappa B activity involves the release of the transcription factor from a cytoplasmic inhibitor termed I kappa B, allowing translocation of NF-kappa B to the nucleus. I kappa B contains multiple copies of the so-called ankyrin repeat, which are apparently necessary for its function. Subunits comprising NF-kappa B and related binding activities are members of the Rel multigene family. Two such subunits, p50 and p52 (also called p50B), are proteolytically processed from precursors of 105 kDa (also called p105 and NFKB1) and 100 kDa (also called p100, NFKB2, and Lyt-10), respectively. Both contain N-terminal Rel-homologous domains as well as multiple copies of C-terminal ankyrin repeats. We show here that NF-kappa B p100 is a component of the previously identified DNA-binding activity H2TF1. In addition, we show that p100 is localized in the cytoplasm in HeLa cells, where it is associated with c-Rel, p50, or p65 (RelA). In transient-transfection assays, p100 represses the ability of NF-kappa B p65 to activate a kappa B-containing reporter construct. Transfection of p100 also results in a loss of nuclear p65 DNA binding to a kappa B probe, as measured by an electrophoretic mobility shift assay, and a loss of nuclear p65 immunoreactivity, as measured by immunoblotting. This loss of nuclear p65 is paralleled by a gain of p65 DNA-binding activity and immunoreactivity in the cytoplasm. We interpret these data as demonstrating that p100 functions as an I kappa B-like molecule to sequester Rel family members in the cytoplasm. Proteolytic processing of p100 to the activator p52 is predicted to generate several new forms of Rel family heterodimers and therefore represents a form of regulation of NF-kappa B activity distinct from the classic I kappa B pathway.
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Scheinman, R. I., A. A. Beg et A. S. Baldwin. « NF-kappa B p100 (Lyt-10) is a component of H2TF1 and can function as an I kappa B-like molecule. » Molecular and Cellular Biology 13, no 10 (octobre 1993) : 6089–101. http://dx.doi.org/10.1128/mcb.13.10.6089.
Texte intégralRésumé :
NF-kappa B is an important transcription factor regulating expression of genes involved in immune function, inflammation, and cellular growth control. NF-kappa B activity is induced by numerous stimuli, such as phorbol esters, B- and T-cell mitogens, the cytokines tumor necrosis factor and interleukin-1, and serum growth factors. The standard model for the induction of NF-kappa B activity involves the release of the transcription factor from a cytoplasmic inhibitor termed I kappa B, allowing translocation of NF-kappa B to the nucleus. I kappa B contains multiple copies of the so-called ankyrin repeat, which are apparently necessary for its function. Subunits comprising NF-kappa B and related binding activities are members of the Rel multigene family. Two such subunits, p50 and p52 (also called p50B), are proteolytically processed from precursors of 105 kDa (also called p105 and NFKB1) and 100 kDa (also called p100, NFKB2, and Lyt-10), respectively. Both contain N-terminal Rel-homologous domains as well as multiple copies of C-terminal ankyrin repeats. We show here that NF-kappa B p100 is a component of the previously identified DNA-binding activity H2TF1. In addition, we show that p100 is localized in the cytoplasm in HeLa cells, where it is associated with c-Rel, p50, or p65 (RelA). In transient-transfection assays, p100 represses the ability of NF-kappa B p65 to activate a kappa B-containing reporter construct. Transfection of p100 also results in a loss of nuclear p65 DNA binding to a kappa B probe, as measured by an electrophoretic mobility shift assay, and a loss of nuclear p65 immunoreactivity, as measured by immunoblotting. This loss of nuclear p65 is paralleled by a gain of p65 DNA-binding activity and immunoreactivity in the cytoplasm. We interpret these data as demonstrating that p100 functions as an I kappa B-like molecule to sequester Rel family members in the cytoplasm. Proteolytic processing of p100 to the activator p52 is predicted to generate several new forms of Rel family heterodimers and therefore represents a form of regulation of NF-kappa B activity distinct from the classic I kappa B pathway.
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Tao, Li, Xiaomeng Ren, Wenhui Zhai et Zheng Chen. « Progress and Prospects of Non-Canonical NF-κB Signaling Pathway in the Regulation of Liver Diseases ». Molecules 27, no 13 (2 juillet 2022) : 4275. http://dx.doi.org/10.3390/molecules27134275.
Texte intégralRésumé :
Non-canonical nuclear factor kappa B (NF-κB) signaling pathway regulates many physiological and pathological processes, including liver homeostasis and diseases. Recent studies demonstrate that non-canonical NF-κB signaling pathway plays an essential role in hyperglycemia, non-alcoholic fatty liver disease, alcoholic liver disease, liver regeneration, liver injury, autoimmune liver disease, viral hepatitis, and hepatocellular carcinoma. Small-molecule inhibitors targeting to non-canonical NF-κB signaling pathway have been developed and shown promising results in the treatment of liver injuries. Here, the recent advances and future prospects in understanding the roles of the non-canonical NF-κB signaling pathways in the regulation of liver diseases are discussed.
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Van Antwerp, D. J., et I. M. Verma. « Signal-induced degradation of I(kappa)B(alpha) : association with NF-kappaB and the PEST sequence in I(kappa)B(alpha) are not required. » Molecular and Cellular Biology 16, no 11 (novembre 1996) : 6037–45. http://dx.doi.org/10.1128/mcb.16.11.6037.
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Signal-induced degradation of I(kappa)B(alpha) via the ubiquitin-proteasome pathway requires phosphorylation on residues serine 32 and serine 36 followed by ubiquitination on lysines 21 and 22. We investigated the role of other regions of I(kappa)B(alpha) which may be involved in its degradation. Here we report that the carboxy-terminal PEST sequence is not required for I(kappa)B(alpha) signal-induced degradation. However, removal of the PEST sequence stabilizes free I(kappa)B(alpha) in unstimulated cells. We further report that a PEST deletion mutant does not associate well with NF-(kappa)B proteins but is degraded in response to signal. Therefore, we conclude that both association with NF-(kappa)B and a PEST sequence are not required for signal-induced I(kappa)B(alpha) degradation. Additionally, the PEST sequence may be required for constitutive turnover of free I(kappa)B(alpha).
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Reus, Joshua B., Emily A. Rex et Don B. Gammon. « How to Inhibit Nuclear Factor-Kappa B Signaling : Lessons from Poxviruses ». Pathogens 11, no 9 (18 septembre 2022) : 1061. http://dx.doi.org/10.3390/pathogens11091061.
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The Nuclear Factor-kappa B (NF-κB) family of transcription factors regulates key host inflammatory and antiviral gene expression programs, and thus, is often activated during viral infection through the action of pattern-recognition receptors and cytokine–receptor interactions. In turn, many viral pathogens encode strategies to manipulate and/or inhibit NF-κB signaling. This is particularly exemplified by vaccinia virus (VV), the prototypic poxvirus, which encodes at least 18 different inhibitors of NF-κB signaling. While many of these poxviral NF-κB inhibitors are not required for VV replication in cell culture, they virtually all modulate VV virulence in animal models, underscoring the important influence of poxvirus–NF-κB pathway interactions on viral pathogenesis. Here, we review the diversity of mechanisms through which VV-encoded antagonists inhibit initial NF-κB pathway activation and NF-κB signaling intermediates, as well as the activation and function of NF-κB transcription factor complexes.
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Sun, S., P. Ganchi, D. Ballard et W. Greene. « NF-kappa B controls expression of inhibitor I kappa B alpha : evidence for an inducible autoregulatory pathway ». Science 259, no 5103 (26 mars 1993) : 1912–15. http://dx.doi.org/10.1126/science.8096091.
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Kato, Motohiro, Masashi Sanada, Itaru Kato, Yasuharu Sato, Junko Takita, Ryoichiro Kawahata, Kengo Takeuchi et al. « Aberrations of Genes Regulating NF Kappa B Pathway in B-Cell Malignant Lymphoma. » Blood 114, no 22 (20 novembre 2009) : 971. http://dx.doi.org/10.1182/blood.v114.22.971.971.
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Abstract Abstract 971 NFκB is a tightly regulated transcription factor of lymphocyte activation, proliferation and development. Controlled activity of NF κ B signaling pathway plays critical roles in coordination of immune and inflammatory response. Constitutive NFκB activation is recognized as a key pathological feature in several subsets of B-cell malignant lymphoma, and it is well known that lymphoma frequently occurred in association with chronic inflammation. Recently, our group showed frequent inactivation of A20, a negative regulator of NF κ B, in B-lineage malignant lymphomas. However, the molecular mechanism underlying the aberrant NF κ B activation in lymphomagenesis has not fully understood. In this study, to clarify the genetic basis of the aberrant NFκB activation, we performed genome-wide analysis of copy number alterations as well as allelic imbalances of primary B-lineage lymphoma specimens using Affymetrix GeneChip 250K genomic microarray with the CNAG/AsCNAR algorithm. We also searched for possible mutations in CARD11, CYLD, IKK and TRAF family genes and IκB genes, to obtain comprehensive registry of lesions in genes regulating NFκB pathway. This study included 238 primary lymphoma samples, including 64 samples of diffuse large B-cell lymphomas (DLBCL), 52 of follicular lymphomas (FL), 35 of mantle cell lymphomas (MCL), and 87 of mucosa-associated tissue (MALT) lymphomas. Five Hodgkin lymphoma-derived cell line (KM-H2, L1236, HDLM2, RPMI1666, L540) was also analyzed. Through a genome-wide analysis, we identified that each histology type had a unique genomic signature, suggesting a distinctive underlying molecular pathogenesis for different histology types. In contrast to the fact that A20 mutation was highly associated with loss of heterozygosity at 6q23.3, mutations of CARD11 (5 cases of DLBCL, 2 cases of MALT lymphoma) and IκB family genes (2 cases of DLBCL and 1 cases of MALT lymphoma) had no association with copy number abnormality at the locus of the genes. In total, mutations and copy number alterations in genes regulating NFκB pathway were found in more than 40% of B-cell lymphomas, which underpinned the importance of aberrant NFκB activation in lymphomagenesis. To also assess the role of uncontrolled signaling of NFκB pathway in lymphomagenesis, we re-expressed wild-type A20 in two lymphoma-derived cell lines without normal functional A20 alleles (KM-H2 and L1236). In both cells, re-expression of wild-type A20 resulted in suppression of cell growth and induction of apoptosis, accompanied by down-regulation of NFκB activation. The A20-deficient KM-H2 stably generated tumors in immunodeficient mice, whereas the tumorigenicity was effectively suppressed by re-expression of A20. We further investigated the role of A20 inactivation during clonal expansion of lymphoma by competitive proliferation assays using A20-deficient lymphoma-derived cell lines with or without re-expression of A20. The proportion of A20-expressing cells gradually decreased during competitive cell culture, and A20-expressing cells outgrew control cells in NOG mice, indicating the importance of A20 inactivation in clonal evolution of lymphoma. We demonstrated that uncontrolled NFκB signaling caused by alterations of multiple genes is a common feature of B-lineage lymphomas. Considering the physiological function of NFκB activation induced upon a variety of upstream stimuli, our observations provide an intriguing insight into and the pathogenesis of lymphoma. Our study also indicated that NFκB inhibition may have a role in lymphoma therapeutics. Disclosures: No relevant conflicts of interest to declare.
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Shi, Xi, Shiwei Qiu, Wei Zhuang, Caiji Wang, Shili Zhang, Na Yuan, Fukang Yuan et Yuehua Qiao. « Follicle-stimulating hormone inhibits cervical cancer via NF-κB pathway ». OncoTargets and Therapy Volume 11 (novembre 2018) : 8107–15. http://dx.doi.org/10.2147/ott.s173339.
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Jing, Nianshui, et Xinnan Li. « Retraction on “Dihydromyricetin attenuates inflammation through TLR4/NF-kappa B pathway” ». Open Medicine 16, no 1 (1 janvier 2021) : 1082. http://dx.doi.org/10.1515/med-2021-0331.
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Shimada, Kana, Makio Saeki, Hiroshi Egusa, Sho Fukuyasu, Yoshiaki Yura, Kazuhiro Iwai et Yoshinori Kamisaki. « RPAP3 enhances cytotoxicity of doxorubicin by impairing NF-kappa B pathway ». Biochemical and Biophysical Research Communications 404, no 4 (janvier 2011) : 910–14. http://dx.doi.org/10.1016/j.bbrc.2010.12.071.
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Yokoo, T., et M. Kitamura. « Dual regulation of IL-1 beta-mediated matrix metalloproteinase-9 expression in mesangial cells by NF-kappa B and AP-1 ». American Journal of Physiology-Renal Physiology 270, no 1 (1 janvier 1996) : F123—F130. http://dx.doi.org/10.1152/ajprenal.1996.270.1.f123.
Texte intégralRésumé :
Glomerular mesangial cells express matrix metalloproteinase-9 (MMP-9) in response to the proinflammatory cytokine interleukin-1 beta (IL-1 beta). To elucidate the signal transduction systems involved, we focused on the role of nuclear factor-kappa B (NF-kappa B) and activator protein-1 (AP-1), since the 5'-flanking region of MMP-9 gene contains binding sequences for these transacting molecules. In rat mesangial cells treated with an inhibitor of NF-kappa B, pyrrolidine dithiocarbamate, induction of MMP-9 by IL-1 beta was suppressed at both mRNA and protein levels. Mesangial cells stably transfected with a transdominant negative mutant of NF-kappa B also showed blunted induction of MMP-9. Transient transfection study with a kappa B reporter plasmid revealed that IL-1 beta indeed activated the kappa B site and that pyrrolidine dithiocarbamate abolished this activation. These results suggest that IL-1 beta induced MMP-9 via the stimulation of NF-kappa B pathway. to examine whether tyrosine kinase is involved in this pathway, mesangial cells were stimulated by IL-1 beta in the presence of a tyrosine kinase inhibitor genistein. This inhibitor dose dependently suppressed the expression of MMP-9, as well as the activation of the kappa B site by IL-1 beta, indicating the involvement of tyrosine kinase in the stimulation of NF-kappa B. Because mesangial cells stimulated by IL-1 beta transiently expressed c-fos and c-jun nRNAs prior to the expression of MMP-9, the role of these genes in mediating the IL-1 beta response was further examined. Transfection of mesangial cells with a c-jun antisense cDNA and treatment with a pharmacological inhibitor of c-Jun/ AP-1, curcumin, revealed that the induction of c-Jun/AP-1 is essential for the expression of MMP-9 by IL-1 beta. Although protein kinase C (PKC) is regarded as a potential inducer of AP-1, stimulation of mesangial cells with phorbol 12-myristate 13-acetate failed to induce MMP-9. Similarly, depletion of intracellular PKC did not obviously affect the induction of MMP-9 by IL-1 beta. These findings demonstrate that dual operation of tyrosine kinase-mediated NF-kappa B stimulation and c-Jun/AP-1 activation is essential to the induction of MMP-9 by IL-1 beta in cultured mesangial cells.
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Goebeler, M., J. Roth, E. B. Bröcker, C. Sorg et K. Schulze-Osthoff. « Activation of nuclear factor-kappa B and gene expression in human endothelial cells by the common haptens nickel and cobalt. » Journal of Immunology 155, no 5 (1 septembre 1995) : 2459–67. http://dx.doi.org/10.4049/jimmunol.155.5.2459.
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Abstract Nickel chloride (NiCl2) and cobalt chloride (CoCl2), two haptens frequently leading to contact hypersensitivity in industrialized countries, induce gene transcription of adhesion molecules ICAM-1, VCAM-1, and E-selectin in endothelial cells. In search of transcriptional mechanisms underlying their gene-inductive effects, we studied the capacity of both haptens to activate nuclear factor (NF)-kappa B, a transcription factor involved in inducible expression of adhesion molecules. Using electrophoretic mobility shift assays, a strong increase of NF-kappa B DNA binding was detected after stimulation of HUVEC with NiCl2 or CoCl2. Supershift analysis using antisera against p50 and p65 confirmed the authenticity of the induced NF-kappa B complex. Neutralizing Abs against TNF-alpha and IL-1 did not inhibit metal hapten-induced activation of NF-kappa B, thus ruling out action via an indirect autocrine pathway. In addition, NiCl2-induced activation of NF-kappa B and adhesion molecule expression was inhibited by the antioxidant pyrrolidine dithiocarbamate, indicating the involvement of redox-dependent mechanisms. Furthermore, NiCl2 was found to induce dose-dependency mRNA production and protein secretion of the NF-kappa B-controlled proinflammatory cytokine IL-6. Our data suggest that distinct allergens represent a new class of so far unknown agents that induce NH-kappa B binding activity that subsequently modulates transcription of cytokine and adhesion molecule genes. Thus, pathomechanisms leading to contact hypersensitivity to NiCl2 and CoCl2 appear to involve not only Ag-specific Langerhans- and T cell-dependent events but also include direct effects on other immunocompetent cells such as the endothelium.
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Moriuchi, H., M. Moriuchi et A. S. Fauci. « Nuclear factor-kappa B potently up-regulates the promoter activity of RANTES, a chemokine that blocks HIV infection. » Journal of Immunology 158, no 7 (1 avril 1997) : 3483–91. http://dx.doi.org/10.4049/jimmunol.158.7.3483.
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Abstract The complex network of cytokines that are involved in inflammatory and immunoregulatory responses plays a critical role in the pathogenesis of HIV infection. RANTES (regulated upon activation, normal T cell expressed and secreted) is a cytokine that belongs to the beta-chemokine family; it is chemoattractant for CD4+/CD45RO T cells, it is produced by various cell types including CD8+ and CD4+ T cells as well as monocytes/macrophages, and has recently been shown to suppress replication of macrophage-tropic strains of HIV in CD4+ T cells. To investigate the molecular mechanisms of RANTES expression, the RANTES promoter region was analyzed by transient expression and gel-mobility shift assays. We demonstrate that: 1) RANTES promoter activity is up-regulated by PMA plus ionomycin, coexpression of the p65 subunit of nuclear factor (NF)-kappa B, the proinflammatory cytokines TNF-alpha and IL-1 beta, and the CD28 costimulatory pathway; 2) the RANTES promoter region contains four NF-kappa B binding sites at positions -30, -44, -213, and -579 relative to the transcription start site; 3) one site (-213) is an NF-AT (nuclear factor of activated T cells) binding site that also has weak affinity to NF-kappa B, and the most distal site (-579) also serves as a CD28-responsive element; and 4) mutation on any of those NF-kappa B sites or coexpression of I kappa B alpha (cytoplasmic inhibitor of NF-kappa B) markedly reduced the promoter activity. Thus, NF-kappa B, a potent transcriptional activator of HIV expression, is also involved in the expression of RANTES, a chemokine that blocks infection by macrophage-tropic strains of HIV.
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Huang, Wei, Zheng Cao, Ye Wu, Zhenzhou Li, Li Li et Yantao Zhao. « Bone Marrow Mesenchymal Stem Cells (BMSCs) Promote Neuronal Cell Repair in Spinal Cord Injury by Regulating Toll-Like Receptor 4/Nuclear Factor-Kappa B Signaling Pathway ». Journal of Biomaterials and Tissue Engineering 11, no 10 (1 octobre 2021) : 2064–69. http://dx.doi.org/10.1166/jbt.2021.2791.
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SCI (SCI) poses a challenge to nerve cell repair strategies. SCI injury can lead to the development of inflammation, which in turn can exacerbate nerve cell damage. The TLR4/NF-kappa B signaling pathway is a common inflammatory signaling pathway. Since BMSCs are involved in injury repair, whether they can promote the repair of SCI neuronal cells have not been reported. Spinal cord nerve cells were cultured in vitro and divided into mechanical injury group and BMSCs group followed by analysis of cell proliferation activity and detection of altered apoptotic activity. Changes in the concentrations of IL-6 and IL-1β were measured by ELISA and cellular mitochondrial alterations was assessed by JG-B staining along with analysis of NF-kappa B, TLR4, related neurodevelopmental factor BDNF, and NGF expression by western blot. Mechanical damage to neuronal cells resulted in decreased cell proliferation, increased apoptotic activity, decreased cellular mitochondrial activity, increased TLR4 and NF-kappa B expression, decreased BDNF and NGF expression, as well as increased secertions of IL-6 and IL-1β (P < 0.05). In contrast, co-culture with BMSCs resulted in increased proliferation and decreased apoptosis of mechanically injured neuronal cells, increased cellular mitochondrial activity, with observation of the inverse changes in other factors (P < 0.05). In conclusion, BMSCs can suppress inflammation and promote repair of injured neuronal cells by inhibiting TLR4/NF-kappa B signaling.
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Zuo, Jiahang, Hongbo Ye, He Lin, Guangfu Lv, Yuchen Wang, Xiaowei Huang et Zhe Lin. « Study on the Antipyretic Mechanism of Baihu Decoction : Network Pharmacology Prediction and Experimental Verification ». Journal of Biobased Materials and Bioenergy 15, no 3 (1 juin 2021) : 334–41. http://dx.doi.org/10.1166/jbmb.2021.2070.
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To better understand the antipyretic mechanism of Baihu decoction, the network pharmacology was used to predict its antipyretic components, targets, functions and pathways, and the prediction results were experimentally verified. BATMAN-TCM was used to obtain the components of Baihu decoction, GeneCards was used to screen fever related targets, STRING was used to analyze the protein interaction network of the selected targets. Bioconductor software was used to analyze the gene ontology (GO) and Kyoto encyclopedia of genes and genomes (KEGG) pathway, and one of the KEGG pathway analyses was performed by cell inflammation model, and was verified by experiments. In the results, total 263 compounds were screened out, 54 potential antipyretic targets were identified, 84 items were obtained by GO function analysis, and 29 pathways were obtained by KEGG analysis, including hypoxia inducible factor-1, Forkhead box O (FOXO) Ras related protein 1 (Rap1), nuclear factor-κ (NF-κB) and other signalling pathways. In the verification experiment of NF-κB signalling pathway, the expression of NF-κB, Inhibitory kappa B kinase beta (IκKβ) and IκBα protein were significantly difference between the Baihu decoction group (P < 0.01) and the model group (P < 0.05), suggesting that Baihu decoction plays the antipyretic effect by affecting IκKβ, Inhibitory kappa B alpha (IκBα) and NF-κB. In conclusion, the interaction of multiple targets in the antipyretic effect of Baihu Decoction and its biological function and pathways were preliminarily demonstrated.
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Das, Subhankar, Ramu Periyasamy et Kailash N. Pandey. « Activation of IKK/NF-κB provokes renal inflammatory responses in guanylyl cyclase/natriuretic peptide receptor-A gene-knockout mice ». Physiological Genomics 44, no 7 (1 avril 2012) : 430–42. http://dx.doi.org/10.1152/physiolgenomics.00147.2011.
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The present study was aimed at determining the consequences of the disruption of guanylyl cyclase/natriuretic peptide receptor-A (GC-A/NPRA) gene ( Npr1) on proinflammatory responses of nuclear factor kappa B, inhibitory kappa B kinase, and inhibitory kappa B alpha (NF-κB, IKK, IκBα) in the kidneys of mutant mice. The results showed that the disruption of Npr1 enhanced the renal NF-κB binding activity by 3.8-fold in 0-copy (−/−) mice compared with 2-copy (+/+) mice. In parallel, IKK activity and IκBα protein phosphorylation were increased by 8- and 11-fold, respectively, in the kidneys of 0-copy mice compared with wild-type mice. Interestingly, IκBα was reduced by 80% and the expression of proinflammatory cytokines and renal fibrosis were significantly enhanced in 0-copy mice than 2-copy mice. Treatment of 0-copy mice with NF-κB inhibitors andrographolide, pyrrolidine dithiocarbamate, and etanercept showed a substantial reduction in renal fibrosis, attenuation of proinflammatory cytokines gene expression, and significantly reduced IKK activity and IkBα phosphorylation. These findings indicate that the systemic disruption of Npr1 activates the renal NF-κB pathways in 0-copy mice, which transactivates the expression of various proinflammatory cytokines to initiate renal remodeling; however, inhibition of NF-κB pathway repairs the abnormal renal pathology in mutant mice.
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Venkataraman, L., S. J. Burakoff et R. Sen. « FK506 inhibits antigen receptor-mediated induction of c-rel in B and T lymphoid cells. » Journal of Experimental Medicine 181, no 3 (1 mars 1995) : 1091–99. http://dx.doi.org/10.1084/jem.181.3.1091.
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Stimulation of B and T cells via the antigen receptor, by phorbol ester or by phorbol ester and ionomycin, leads to nuclear translocation of the inducible transcription factor NF-kappa B, comprising the p50 and p65 rel-related polypeptides. In this report we show that c-rel is a component of the antigen receptor-induced kappa B binding proteins in both B and T cells. Whereas NF-kappa B can be induced by phorbol ester alone, optimal induction of c-rel requires stimulation by both phorbol ester and ionomycin, the dual signal that is necessary for proliferation of untransformed lymphocytes. Furthermore, c-rel induction is blocked by the immunosuppressive drug FK506 that is known to inhibit B and T cell activation. c-rel-dependent transactivation of the interleukin-2 receptor alpha chain (IL-2R alpha) promoter is augmented by coexpression of calcineurin, suggesting the involvement of a calcineurin-dependent intracellular pathway. Our results identify c-rel as a target of immunosuppressive agents and illustrate the similarity of activation pathways in both B and T cells.
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Alleboina, Satyanarayana, Thomas Wong, Madhu V. Singh et Ayotunde O. Dokun. « Inhibition of protein kinase C beta phosphorylation activates nuclear factor-kappa B and improves postischemic recovery in type 1 diabetes ». Experimental Biology and Medicine 245, no 9 (23 avril 2020) : 785–96. http://dx.doi.org/10.1177/1535370220920832.
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Peripheral artery disease (PAD) is a major health problem and is caused by atherosclerosis in arteries outside the heart leading to impaired blood flow. The presence of diabetes significantly increases the likelihood of having worse outcomes in PAD, and the molecular mechanisms involved are poorly understood. Hyperglycemia in diabetes activates the nuclear factor-kappa B (NF-κB) pathway, and chronic inflammation in diabetes is associated with vascular complications. Ischemia also activates NF-κB signaling that is important for perfusion recovery in experimental PAD. We hypothesized that prolonged exposure of endothelial cells to high glucose in diabetes impairs ischemic activation of the NF-κB pathway and contributes to poor perfusion recovery in experimental PAD. We assessed the effect of high glucose and ischemia on canonical and non-canonical NF-κB activation in endothelial cells and found both conditions activate both pathways. However, exposure of endothelial cells to high glucose impairs ischemia-induced activation of the canonical NF-κB pathway but not the non-canonical pathway. We probed an array of antibodies against signaling proteins in the NF-κB pathway to identify proteins whose phosphorylation status are altered in endothelial cells exposed to high glucose. Protein kinase C beta (PKCβ) was among the proteins identified, and its role in impaired ischemia-induced activation of NF-κB during hyperglycemia has not been previously described. Inhibition of PKCβ improves ischemia-induced NF-κB activation in vitroand in vivo. It also improves perfusion recovery in diabetic mice following experimental PAD. Thus, in diabetes, PKCβ phosphorylation contributes to impaired ischemic activation of NF-κB and likely a mechanism contributing to poor PAD outcomes. Impact statement Diabetes worsens the outcomes of peripheral arterial disease (PAD) likely in part through inducing chronic inflammation. However, in PAD, recovery requires the nuclear factor-kappa B (NF-κB) activation, a known contributor to inflammation. Our study shows that individually, both ischemia and high glucose activate the canonical and non-canonical arms of the NF-κB pathways. We show for the first time that prolonged high glucose specifically impairs ischemia-induced activation of the canonical NF-κB pathway through activation of protein kinase C beta (PKCβ). Accordingly, inhibition of PKCβ restores the ischemia-induced NF-κB activity both in vitroin endothelial cells and in vivoin hind limbs of type 1 diabetic mice and improves perfusion recovery after experimental PAD. Thus, this study provides a mechanistic insight into how diabetes contributes to poor outcomes in PAD and a potential translational approach to improve PAD outcomes.
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Han, Y. P., T. L. Tuan, H. Wu, M. Hughes et W. L. Garner. « TNF-alpha stimulates activation of pro-MMP2 in human skin through NF-(kappa)B mediated induction of MT1-MMP ». Journal of Cell Science 114, no 1 (1 janvier 2001) : 131–39. http://dx.doi.org/10.1242/jcs.114.1.131.
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Tumor necrosis factor-alpha (TNF-(alpha)) is an important mediator during the inflammatory phase of wound healing. Excessive amounts of pro-inflammatory cytokines such as TNF-(alpha) are associated with inflammatory diseases including chronic wounds. Matrix metalloproteinases (MMPs) are involved in matrix re-modeling during wound healing, angiogenesis and tumor metastasis. As with pro-inflammatory cytokines, high levels of MMPs have been found in inflammatory states such as chronic wounds. In this report we relate these two phenomena. TNF-(alpha) stimulates secretion of active MMP-2, a type IV collagenase, in organ-cultured full-thickness human skin. This suggests a mechanism whereby excess inflammation affects normal wound healing. To investigate this observation at the cellular and molecular levels, we examined TNF-(alpha) mediated activation of pro-MMP-2, induction of MT1-MMP, and the intracellular signaling pathways that regulate the proteinase in isolated human dermal fibroblasts. We found that TNF-(alpha) substantially promoted activation of pro-MMP-2 in dermal fibroblasts embedded in type-I collagen. In marked contrast, collagen or TNF-(alpha) individually had little influence on the fibroblast-mediated pro-MMP-2 activation. One well-characterized mechanism for pro-MMP-2 activation is through a membrane type matrix metalloproteinase, such as MT1-MMP. We report that TNF-(alpha) significantly induced MT1-MMP at the mRNA and protein levels when the dermal fibroblasts were grown in collagen. Although the intracellular signaling pathway regulating mt1-mmp gene expression is still obscure, both TNF-(alpha) and collagen activate the NF-(kappa)B pathway. In this report we provide three sets of evidence to support a hypothesis that activation of NF-(kappa)B is essential to induce MT1-MMP expression in fibroblasts after TNF-(alpha) exposure. First, SN50, a peptide inhibitor for NF-(kappa)B nuclear translocation, simultaneously blocked the TNF-(alpha) and collagen mediated MT1-MMP induction and pro-MMP-2 activation. Secondly, TNF-(alpha) induced I(kappa)B to breakdown in fibroblasts within the collagen lattice, a critical step leading to NF-(kappa)B activation. Lastly, a consensus binding site for p65 NF-(kappa)B (TGGAGCTTCC) was found in the 5′-flanking region of human mt1-mmp gene. Based on these results and previous reports, we propose a model to explain TNF-(alpha) activation of MMP-2 in human skin. Activation of NF(kappa)B signaling in fibroblasts embedded in collagen induces mt1-mmp gene expression, which subsequently activates the pro-MMP-2. The findings provide a specific mechanism whereby TNF-(alpha) may affect matrix remodeling during wound healing and other physiological and pathological processes.
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Wu, Hongjin, Weiwei Dai, Libo Wang, Jie Zhang et Chenglong Wang. « Effects of Reducing the South and Reinforcing the North Method on Inflammatory Injury Induced by Hyperlipidemia ». Evidence-Based Complementary and Alternative Medicine 2021 (20 septembre 2021) : 1–18. http://dx.doi.org/10.1155/2021/1860508.
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Inflammation is the pathophysiological basis of hyperlipidemia-related disease (HRD). Reducing the south and reinforcing the north method (RSRN) has a positive effect on HRD. However, the pharmacological mechanisms of RSRN are still unclear in the treatment of HRD. We obtained RSRN compounds from the Traditional Chinese Medicine Systems Pharmacology (TCMSP) and identified potential targets of these compounds through target fishing based on the TCMSP databases. Next, we identified the HRD targets by using multiple databases. Then, the overlapping genes between the RSRN potential targets and the HRD targets were used to establish a protein-protein interaction (PPI) network, and we further analyzed their interactions and identified the major hub genes in this network. Subsequently, the Metascape database was utilized to conduct the enrichment of Gene Ontology biological processes (GO) and Kyoto Encyclopedia of Genes and Genomes (KEGG) pathways. A total of 187 potential active components and 106 related core targets were obtained and identified overall. Then after the Metascape enrichment analysis, a total of 148 KEGG pathways were screened, which were mainly associated with AGE-RAGE signaling pathway, PI3K-Akt signaling pathway, TNF signaling pathway, and NF-kappa B signaling pathway. Furthermore, 34 hub genes, such as AKT1, NF-κBp65(RELA), IκBα(CHUK), MAPK8, and MAPK14, CCND1, were considered potential therapeutic targets. Furthermore, evaluations of protein levels of NF-κBp65, IκBα, TNF-α, IL-1 ß, and IL-6 were performed for experimental validation. RSRN can reduce the expression of NF-κBp65 protein, increase the level of IκBα protein, and reduce the protein levels of TNF-α, IL-1β, and IL-6 in ovariectomized rats. The results indicate that the mechanism of RSRN against inflammation may be related to AKT1, NF-κBp65, IκBα, MAPK8, and MAPK14, as well as TNF, NF-kappa B, PI3K-Akt signaling pathways.
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Geng, Hao, Wenhao Guo, Lei Feng, Dongdong Xie, Liangkuan Bi, Yi Wang, Tao Zhang, Zhaofeng Liang et Dexin Yu. « Diallyl trisulfide inhibited tobacco smoke-mediated bladder EMT and cancer stem cell marker expression via the NF-κB pathway in vivo ». Journal of International Medical Research 49, no 3 (mars 2021) : 030006052199290. http://dx.doi.org/10.1177/0300060521992900.
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Objective This study examined the effect of the NF-κB pathway on tobacco smoke-elicited bladder epithelial–mesenchymal transition (EMT) and cancer stem cell (CSC) marker expression in vivo. The effect of diallyl trisulfide (DATS) treatment was also examined. Methods BALB/c mice were exposed to tobacco smoke and treated with an NF-κB inhibitor and DATS. Western blotting, quantitative real-time PCR, and immunohistochemical staining were used to detect the changes of relevant indices. Results Phosphorylated inhibitor of kappa-B kinase alpha/beta expression and p65 and p50 nuclear transcription were increased by tobacco smoke exposure, whereas inhibitor of kappa-B expression was decreased. In addition, tobacco smoke reduced the expression of epithelial markers but increased that of mesenchymal and CSC markers. Our study further demonstrated that tobacco smoke-mediated EMT and CSC marker expression were attenuated by inhibition of the NF-κB pathway. Moreover, DATS reversed tobacco smoke-induced NF-κB pathway activation, EMT, and the acquisition of CSC properties in bladder tissues. Conclusions These data suggested that the NF-κB pathway regulated tobacco smoke-induced bladder EMT, CSC marker expression, and the protective effects of DATS.
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Lagunas, Vilma Maldonado, et Jorge Meléndez-Zajgla. « Nuclear Factor-kappa B as a Resistance Factor to Platinum-Based Antineoplasic Drugs ». Metal-Based Drugs 2008 (8 avril 2008) : 1–6. http://dx.doi.org/10.1155/2008/576104.
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Platinum drugs continue to be major chemotherapy drugs for cancer treatment. Nevertheless, acquired or intrinsic resistance to these compounds is common in human tumors. One important mechanism for this resistance is the avoidance of cells entering the apoptotic pathway. Nuclear factor-kappa B (NF-kappa B, NF-κB) is a pleiotropic transcription factor key in determining the death threshold of human cells. This factor is important in the final response of cells to platinum drugs, as exemplified by in vitro and in vivo models showing that inhibition of NF-κB sensitizes cancer cells to the effects of these drugs. New approaches focusing on the inhibition of NF-κB could help to minimize or even eliminate intrinsic or acquired resistance to platinum drugs.
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Anisowicz, A., M. Messineo, S. W. Lee et R. Sager. « An NF-kappa B-like transcription factor mediates IL-1/TNF-alpha induction of gro in human fibroblasts. » Journal of Immunology 147, no 2 (15 juillet 1991) : 520–27. http://dx.doi.org/10.4049/jimmunol.147.2.520.
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Abstract Normal human foreskin fibroblasts were used to examine transcriptional induction by IL-1 and TNF-alpha of the novel cytokine gro (melanoma growth-stimulating activity). Gro mRNA was expressed at levels 100-fold above background within 45 min of exposure to either IL-1 or TNF-alpha, in growing or serum-starved cells and a similar response was shown by IL-6. In contrast, as shown previously, gro mRNA was elevated only 10-fold by serum in starved but not in growing cells, similar to fos. Thus gro expression appears to be regulated by at least two signal transduction systems: a cytokine pathway, and a growth-related pathway. Three closely related gro genes (alpha, beta, and gamma) have been described. Their proximal 5' regulatory sequences presented here show close similarity in the region to -136, which includes the NF-kappa B site at -66 to -76 in gro alpha and gro gamma, and -64 to -74 in gro beta, and sequence diversity further upstream. Transient transfection of HeLa cells with CAT constructs localized the cytokine response to a region between -84 and -65 in gro beta. Gel retardation studies with FS-2 cells identified a cytokine-induced protein binding at the NF-kappa B site in all three gro genes as shown by competition studies with a pair of oligonucleotides representing wild-type and mutant sequences of the NF-kappa B binding site. Neither serum nor PMA induced a detectable gel shift at NF-kappa B or upstream to position -723. These results demonstrate conservation of the cytokine response element, NF-kappa B, in the three genes, consistent with the conservation of sequence in this region; and suggest that differential expression of the three gro genes may depend upon interactions with other sites located in the divergent upstream region.
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Orthner, CL, GM Rodgers et LA Fitzgerald. « Pyrrolidine dithiocarbamate abrogates tissue factor (TF) expression by endothelial cells : evidence implicating nuclear factor-kappa B in TF induction by diverse agonists ». Blood 86, no 2 (15 juillet 1995) : 436–43. http://dx.doi.org/10.1182/blood.v86.2.436.bloodjournal862436.
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Tissue factor (TF), a 46-kD glycoprotein receptor for coagulation factors VII and VIIa, is expressed on the surface of endothelial cells in response to a variety of agonists and is thought to play an important role in initiating the thrombosis associated with inflammation during infection, sepsis, and organ transplant rejection. The induction of TF activity by lipopolysaccharide (LPS) is regulated, at least partially, at a transcriptional level and an LPS response element containing two activator protein-1 sites and a nuclear factor- kappa B (NF kappa B)-like site has been localized to the 5′ flanking region of the TF gene by transfection studies of TF promoter/reporter gene constructs. We have examined the effect of pyrrolidine dithiocarbamate (PDTC), a specific inhibitor of the NF kappa B pathway on the expression of the endogenous TF gene in human umbilical vein endothelial cells (HUVEC). Preincubation of HUVEC for 60 minutes with PDTC inhibited LPS induction of TF activity on the cell surface in a dose-dependent manner, with 50% inhibition occurring at 10 mumol/L PDTC and 100% inhibition at higher concentrations (> or = 100 mumol/L). Furthermore, PDTC inhibited TF expression in response to tumor necrosis factor-alpha, interleukin-1 beta, and phorbol 12-myristate 13-acetate. The effect of PDTC was at the mRNA level, as seen by the complete abrogation of the large increase in TF mRNA observed in LPS-treated HUVEC. These results suggest that endothelial cell activation by diverse agonists initiates intracellular signaling events that converge upon a common pathway involving NF kappa B and, furthermore, that NF kappa B activation is an obligatory step induction of TF.
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Puvvada, Soham D., Jason Smith, Cassandra L. Jacobs et Sandeep Dave. « Selective IKKβ Inhibition of the NF-Kappab Pathway Is An Effective Therapeutic Strategy In Lymphomas ». Blood 116, no 21 (19 novembre 2010) : 1849. http://dx.doi.org/10.1182/blood.v116.21.1849.1849.
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Abstract Abstract 1849 Background: The NF-kappaB pathway is an essential and tightly regulated signaling cascade that mediates development, activation and survival of normal lymphocytes. In recent years, there has been convincing evidence implicating this pathway in several lymphoid malignancies including the activated B cell-like (ABC) subtype of Diffuse Large B cell Lymphoma(DLBCL), Primary Mediastinal B Cell Lymphoma(PMBL), marginal zone lymphoma, and Hodgkins lymphoma. These tumors frequently engage the classic NF-kappaB pathway in which the IKK β subunit phosphorylates IκBα triggering its ubiquitination and subsequent proteasomal degradation. Therefore, therapies targeting this pathway through selected IKKB inhibition may provide a novel approach for targeting NF-kappaB activity in lymphoid malignancies. We therefore decided to explore the efficacy of a novel IKKB inhibitor CMPDA in a broad group of lymphomas. Methods: We chose 37 cell lines that broadly represented a diverse group of lymphomas including Burkitt lymphoma, mantle cell lymphoma, Hodgkin lymphoma, multiple myeloma, prolymphocytic leukemia, and the activated B cell-like (ABC) and germinal center (GCB) subtypes of DLBCL. Cell viability assays using MTT were performed to identify the IC50 in these cell lines. We performed gene expression profiling on all cell lines using a GeneChip Human Gene 1.0 ST Array which comprises 33297 probes that target all known genes. Utilizing hierarchial clustering algorithms in conjunction with cox regression analysis, the cell lines were classified into 2 groups based on gene expression: the predicted sensitive(Group A: 20 cell lines) versus predicted less sensitive cell lines (Group B: 17 cell lines). Results: CMPDA was broadly effective in lymphomas demonstrating lethality in most lymphoma types at physiologically achievable concentrations with a mean IC50 of 9.15 micromoles (Range: 1.47 to 58.24 micromoles). The Mean IC50 for cell lines in Group A which were predicted as being sensitive by gene expression was 5 micromoles, whereas the mean IC50 for the cell lines in Group B which were predicted as being relatively resistant to NF-KB inhibition was 3-fold higher (∼15micromoles). Group A included a number of cell lines with known dependence on NF-kappa B activity including several ABC DLBCL cell lines. It is notable that while GCB DLBCL have generally been thought to have little dependence of NF -KB activity, we nevertheless found that there were 4 GCB DLCBL cell lines that were also sensitive to NFKB inhibition at IC50s comparable to a number of ABC DLBCLs. Group B comprised of a disproportionate number of Burkitt lymphoma cell lines (4/17), which is consistent with the known biology of this tumor as it typically expresses NF-KB at lower levels. Genes associated with response to NF-KB inhibition showed robust concordance with the known biology of the NF-kappaB pathway, with gene expression signatures related to CD40-stimulation (an upstream activator of NF-kappa B) and NF-kappa B activity showing the strongest associations with response to CMPDA (P=0.004 and P=0.01 respectively). Conclusions: Thus our data demonstrate that selective IKKβ inhibition of the NF-kappa B pathway using CMPDA is a promising therapeutic strategy in lymphoma. Gene expression profiling provides a useful tool for potentially identifying tumors that are most likely to respond to this therapy. Disclosures: No relevant conflicts of interest to declare.
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Liu, Ganlu, Jingfeng Lin, Lina Zhang, Qiang Gao, Zhenyi Wang, Ze Chang, Ying Gao, Dayong Ma et Zhenyun Han. « Uncovering the Mechanism of the Xingnaojing Injection against Ischemic Stroke Using a Combined Network Pharmacology Approach and Gut Microbiota Analysis ». Evidence-Based Complementary and Alternative Medicine 2022 (20 mai 2022) : 1–35. http://dx.doi.org/10.1155/2022/5886698.
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Objective. To explore the brain protection mechanism of Xingnaojing injection (XNJ) against ischemic stroke (IS) by the network pharmacology approach and gut microbiota analysis. Methods. We used network pharmacology analysis to identify the active components of XNJ and its potential targets against IS and inflammatory bowel disease (IBD) and carried out network analysis, functional annotation, and pathway enrichment analysis. Then, transient middle cerebral artery occlusion (tMCAO) mice model was used to verify the molecular mechanism of XNJ. Results. 36 active compounds were identified from XNJ, and the effect of XNJ against IS was related to the VEGF signaling pathway, NF-kappa B signaling pathway, and gap junction. The effect of XNJ against IBD was related to the T cell receptor signaling pathway, NF-kappa B signaling pathway, and gap junction. In vitro experiments showed that XNJ significantly improved the neurological function of tMCAO mice, reduced the size of cerebral infarction, decreased the permeability of blood-brain barrier (BBB), downregulated the expressions of TLR4, MyD88, and NF-kappa B in the ischemic site, and upregulated the expressions of occludin and ZO-1 in the colon. High-throughput 16S rDNA gene sequencing showed that XNJ upregulated the levels of Akkermansia and downregulated the levels of Flavobacteriaceae, Deferribacteraceae, and Deferribacteres. XNJ increased the concentrations of the short-chain fatty acids (SCFAs) PA (propionate), VA (valerate), IBA (isobutyrate), and IVA (isovalerate) in the feces of the sham germ-free experiment group (SGFEG) mice. Conclusion. IS causes dysbiosis of some specific bacteria in the gut microbiota. XNJ is an effective treatment for IS, and its mechanism was related to improving intestinal barrier function and regulating intestinal flora and SCFAs. Network pharmacology revealed that XNJ acts through multiple targets and multiple pathways.
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Zhou, Li, Zhe-Zhi Deng, Hai-Yan Li, Nan Jiang, Zhi-Sheng Wei, Ming-Fan Hong, Xiao-Dang Chen et al. « TRIM31 promotes glioma proliferation and invasion through activating NF-κB pathway ». OncoTargets and Therapy Volume 12 (mars 2019) : 2289–97. http://dx.doi.org/10.2147/ott.s183625.
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Shu, Chang, Jun Chen, Meiyan Lv, Yiyuan Xi, Jujia Zheng et Xiangwei Xu. « Plumbagin relieves rheumatoid arthritis through nuclear factor kappa-B (NF-κB) pathway ». Bioengineered 13, no 5 (2 mai 2022) : 13632–42. http://dx.doi.org/10.1080/21655979.2022.2081756.
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Dai, Yu-Qiao, Dao-Zhong Jin, Xing-Zu Zhu et De-Liang Lei. « Triptolide inhibits COX-2 expression via NF-kappa B pathway in astrocytes ». Neuroscience Research 55, no 2 (juin 2006) : 154–60. http://dx.doi.org/10.1016/j.neures.2006.02.013.
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Labouba, I., S. Mehairi, M. Latour, A. Mes-Masson et F. Saad. « Implication of the alternative NF-kappa B pathway in prostate cancer progression. » Journal of Clinical Oncology 28, no 15_suppl (20 mai 2010) : 10592. http://dx.doi.org/10.1200/jco.2010.28.15_suppl.10592.
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Wan, Ying, Heather L. Francis, Nan Wu, Kelly McDaniel, Tianhao Zhou, Julie Venter, Haibo Bai, Shannon Glaser, Gianfranco Alpini et Fanyin Meng. « 653 microRNA-34a Regulates Alcoholic Hepatitis Through SIRT1/NF-kappa;B Pathway ». Gastroenterology 150, no 4 (avril 2016) : S1043. http://dx.doi.org/10.1016/s0016-5085(16)33525-9.
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