scholarly journals Asbestos induces nuclear factor kappa B (NF-kappa B) DNA-binding activity and NF-kappa B-dependent gene expression in tracheal epithelial cells.

1995 ◽  
Vol 92 (18) ◽  
pp. 8458-8462 ◽  
Author(s):  
Y. M. Janssen ◽  
A. Barchowsky ◽  
M. Treadwell ◽  
K. E. Driscoll ◽  
B. T. Mossman
Keyword(s):  
Gene Expression ◽  
Dna Binding ◽  
Epithelial Cells ◽  
Nuclear Factor Kappa B ◽  
Binding Activity ◽  
Nuclear Factor ◽  
Nf Kappa B ◽  
Tracheal Epithelial Cells ◽  
Dna Binding Activity ◽  
Tracheal Epithelial

scholarly journals UV-A-induced decrease in nuclear factor-κB activity in human keratinocytes

1999 ◽  
Vol 338 (3) ◽  
pp. 607-613 ◽  
Author(s):  
Mojgan DJAVAHERI-MERGNY ◽  
Marie-Pierre GRAS ◽  
Jean-Louis MERGNY ◽  
Louis DUBERTRET
Keyword(s):  
Gene Expression ◽  
Dna Binding ◽  
Uv Radiation ◽  
Human Keratinocytes ◽  
Nuclear Factor Κb ◽  
Binding Activity ◽  
Luciferase Reporter ◽  
Nuclear Factor ◽  
Protein Subunits ◽  
Dna Binding Activity

Previous reports have demonstrated an increase in nuclear factor-κB (NF-κB) activity in response to UV radiation. These studies have essentially focused on the DNA-damaging fraction of solar UV radiation (UV-B and UV-C). In contrast, the effects of UV-A radiation (320–400 nm) on NF-κB are not well known. In this study, we present evidence that UV-A radiation induces a marked decrease in NF-κB DNA-binding activity in NCTC 2544 human keratinocytes. In addition, NCTC 2544 keratinocytes pretreated with UV-A fail to respond to NF-κB inducers. Moreover, UV-A radiation induces a decrease in NF-κB-driven luciferase reporter gene expression in NCTC 2544 keratinocytes. The expression of the gene encoding IκBα (IκB is the NF-κB inhibitor), which is closely associated with NF-κB activity, is also reduced (3-fold) upon UV-A treatment. Our results indicate that the UV-A-induced decrease in NF-κB DNA-binding activity is associated with a decrease in the levels of the p50 and p65 protein subunits. This is the first evidence that an oxidative stress, such as UV-A radiation, may induce a specific decrease in NF-κB activity in mammalian cells, probably through degradation of NF-κB protein subunits. These findings suggest that UV-A could modulate the NF-κB-dependent gene expression.

IL-1 beta increases laminin B2 chain mRNA levels and activates NF-kappa B in rat glomerular epithelial cells

1995 ◽  
Vol 268 (2) ◽  
pp. F273-F278 ◽  
Author(s):  
C. A. Richardson ◽  
K. L. Gordon ◽  
W. G. Couser ◽  
K. Bomsztyk
Keyword(s):  
Gene Expression ◽  
Epithelial Cells ◽  
Binding Activity ◽  
Mrna Levels ◽  
Nf Kappa B ◽  
Enhancer Element ◽  
Immunoglobulin Kappa ◽  
Dna Binding Activity ◽  
Nuclear Extracts ◽  
Glomerular Epithelial Cells

The amount and distribution of laminin in the glomerular basement membrane (GBM) change in the course of many types of glomerular disease. Because interleukin-1 (IL-1) is thought to play a role in the pathogenesis of glomerulonephritis, it raises the possibility that this and other cytokines might regulate laminin gene expression. To determine whether laminin B2 chain mRNA levels change in response to cytokines, total mRNA from rat glomerular epithelial cells (GEC) grown in culture was analyzed by Northern blots. These studies showed an increase in laminin B2 chain mRNA levels in GEC treated with IL-1 beta. Nuclear factor kappa B (NF-kappa B) is a cytokine-responsive factor that regulates transcription of many genes from the cognate kappa B enhancer element. The mouse laminin B2 chain promoter contains several kappa B-like motifs, suggesting that NF-kappa B might be involved in IL-1-induced laminin B2 chain gene expression. Nuclear extracts from IL-1 beta-treated GEC showed increased binding to the immunoglobulin kappa B enhancer element and to a kappa B consensus sequence from the murine laminin B2 chain promoter in an electrophoretic mobility-shift assay (EMSA). The immunoglobulin kappa B and the laminin B2 chain kappa B-like motifs competed for the same DNA binding activity in nuclear extracts from IL-1 beta-treated GEC. Pretreatment of these nuclear extracts with antibodies to either the p50 or p65 subunits of NF-kappa B abrogated the DNA binding activity recognized by either of the two DNA motifs.(ABSTRACT TRUNCATED AT 250 WORDS)

UV stimulation induces nuclear factor κB (NF-κB) DNA-binding activity but not transcriptional activation

2001 ◽  
Vol 29 (6) ◽  
pp. 688-691 ◽  
Author(s):  
K. J. Campbell ◽  
N. R. Chapman ◽  
N. D. Perkins
Keyword(s):  
Dna Binding ◽  
Transcriptional Activation ◽  
Cellular Response ◽  
Uv Light ◽  
Binding Protein ◽  
Nuclear Factor Κb ◽  
Camp Response Element Binding ◽  
Binding Activity ◽  
Nuclear Factor ◽  
Dna Binding Activity

The cellular response to DNA-damaging agents is partly mediated by DNA-binding transcription factors such as p53 and nuclear factor κB (NF-κB). Typically NF-κB activation is associated with resistance to apoptosis. Following stimulation with UV light however, NF-κB activation has been shown to be required for programmed cell death. To study this effect further and to determine the relationship between NF-κB and p53 function, we have examined the effect of UV light on U2OS cells. UV stimulation resulted in the activation of NF-κB DNA-binding and the induction of p53. Surprisingly, and in contrast with tumour necrosis factor α stimulation, this UV-induced NF-κB was transcriptionally inert. These observations suggest a model in which the NF-κB switch from an anti-apoptotic to a pro-apoptotic role within the cell results from modulation of its ability to stimulate gene expression, possibly as a result of the ability of p53 to sequester transcriptional co-activator proteins such as p300/CREB (cAMP-response-element-binding protein)-binding protein.

Extinction of insulin gene expression in hybrids between beta cells and fibroblasts is accompanied by loss of the putative beta-cell-specific transcription factor IEF1

1991 ◽  
Vol 11 (3) ◽  
pp. 1547-1552
Author(s):  
D Leshkowitz ◽  
M D Walker
Keyword(s):  
Gene Expression ◽  
Dna Binding ◽  
Binding Activity ◽  
Insulin Gene ◽  
Hybrid Cells ◽  
Dna Binding Activity ◽  
Insulin Producing Cells ◽  
Insulin Gene Expression ◽  
Insulinoma Cells

Insulin-producing cells and fibroblasts were fused to produce hybrid lines. In hybrids derived from both hamster and rat insulinoma cells, no insulin mRNA could be detected in any of seven lines examined by Northern (RNA) analysis despite the presence in each line of the insulin genes of both parental cells. Hybrid cells were transfected with recombinant chloramphenicol acetyltransferase plasmids containing defined segments of the rat insulin I gene 5' flank. We observed no transcriptional activity of the intact insulin enhancer or of IEB2, a critical cis-acting element of the insulin enhancer. IEB2 has previously been shown to interact in vitro with IEF1, a DNA-binding activity observed selectively in insulin-producing cells. Hybrid cells showed no detectable IEF1 activity. Furthermore, the insulin enhancer was unable to reduce transcription directed by the Moloney sarcoma virus enhancer in a double-enhancer construct. Thus, extinction of insulin gene expression in the hybrids apparently does not operate through a direct action of repressors on the insulin enhancer; rather, extinction is accompanied by, and may be caused by, reduced DNA-binding activity of the putative transcriptional activator IEF1.

scholarly journals Overexpression of mitogen-activated protein kinase (ERK1) enhances T- cell cytokine gene expression: role of AP1, NF-AT, and NF-KB

Blood ◽  
1993 ◽  
Vol 82 (8) ◽  
pp. 2470-2477 ◽  
Author(s):  
JH Park ◽  
L Levitt
Keyword(s):  
Gene Expression ◽  
T Cell ◽  
Dna Binding ◽  
Map Kinase ◽  
Binding Activity ◽  
Cytokine Gene Expression ◽  
Cytokine Gene ◽  
Dna Binding Activity ◽  
Mitogen Activated Protein

Abstract Transfected Jurkat cells overexpressing extracellular signal-regulated kinase (ERK1), also referred to as mitogen-activated protein (MAP) kinase, were selected by Western blotting assay using anti-ERK1 and antiphosphotyrosine antibodies in combination with a functional MAP kinase assay. We then asked whether enhanced ERK1 expression had any effect on induction of T-cell cytokine genes. The results show that overexpression of ERK1 enhances expression of T-cell interleukin-2 (IL- 2), IL-3, and granulocyte-macrophage colony-stimulating factor mRNA; no change was seen in expression of the alpha-actin gene. DNA-binding activities of the transcription factors AP1, NF-AT, and NF-kB were specifically increased twofold to fourfold in ERK1-overexpressing clones relative to nontransformed or vector-transformed cells, whereas no enhancement of CK1-CK2 protein DNA binding activity was detected after ERK1 overexpression. Additionally, increased NF-AT DNA binding activity was associated with functional enhancement of NF-AT transactivating activity in ERK1-overexpressing cells. These results provide direct evidence for the role of MAP kinase in the regulation of cytokine gene expression and indicate that such regulation is likely mediated through the enhanced DNA binding activity of specific nuclear transcription factors.

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