Transcription factors NF-IL6 and CREB recognize a common essential site in the human prointerleukin 1 beta gene.

Tsukada, Junichi; Saito, Kazuyoshi; Waterman, Wayne R.; Webb, Andrew C.; Auron, Philip E.

doi:10.1128/mcb.14.11.7285

Cited by 143 publications

(111 citation statements)

References 48 publications

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“…For example, two groups have reported the targeted disruption of the c/ebp␤ gene (51,52) and have shown that this mutation has only minor effects on the expression of inflammatory cytokine genes. These results are surprising in light of previous data showing that C/EBP␤ plays a critical role in the expression of genes such as interleukin-1, interleukin-6, and monocyte chemoattractant protein-1 in cell lines (26,(53)(54)(55), and suggest that a redundant C/EBP activity compensates for the absence of C/EBP␤ in knockout animals. To demonstrate that the compensatory activity is provided by another member of the C/EBP family, one could create DN transgenic mice that express the C/EBP inhibitor specifically in hepatocytes or monocytic cells.…”

Section: Discussioncontrasting

confidence: 51%

Design of a C/EBP-specific, Dominant-negative bZIP Protein with Both Inhibitory and Gain-of-function Properties

Olive

Williams

Dezan

et al. 1996

Journal of Biological Chemistry

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We have developed a bZIP protein, GBF-F, with both dominant-negative (DN) and gain-of-function properties. GBF-F is a chimera consisting of two components: the DNA binding (basic) region from the plant bZIP protein GBF-1 (GBF) and a leucine zipper (F) designed to preferentially heterodimerize with the C/EBP␣ leucine zipper. Biochemical studies show that GBF-F preferentially forms heterodimers with C/EBP␣ and thus binds a chimeric DNA sequence composed of the half-sites recognized by the C/EBP and GBF basic regions. Transient transfections in HepG2 hepatoma cells show that both components of GBF-F are necessary for inhibition of C/EBP␣ transactivation. When the C/EBP␣ leucine zipper is replaced with that of either GCN4 or VBP, the resulting protein can transactivate a C/EBP cis-element but is not inhibited by GBF-F, indicating that the specificity of dominant-negative action is determined by the leucine zipper. All known members of the C/EBP family contain similar leucine zipper regions and are inhibited by GBF-F. GBF-F also exhibits gain-of-function properties, since, with the essential cooperation of a C/EBP family member, it can transactivate a promoter containing the chimeric C/EBPͦGBF site. This protein therefore has potential utility both as a dominant-negative inhibitor of C/EBP function and as an activator protein with novel DNA sequence specificity.

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Section: Discussioncontrasting

confidence: 51%

Design of a C/EBP-specific, Dominant-negative bZIP Protein with Both Inhibitory and Gain-of-function Properties

Olive

Williams

Dezan

et al. 1996

Journal of Biological Chemistry

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“…The human proIL-1␤ gene contains several cis-acting elements that are required for transcription of the gene. These included the binding sites for Spi-1, C/EBP/NF-IL6, AP-1, and C/EBP-CREB heterodimer (43)(44)(45). Baldassare et al (46) reported that p38 induced transcription of the IL-1␤ gene by acting through C/EBP/NF-IL6.…”

Section: Discussionmentioning

confidence: 99%

Amplification of the synovial inflammatory response through activation of mitogen‐activated protein kinases and nuclear factor κB using ligation of CD40 on CD14+ synovial cells from patients with rheumatoid arthritis

Harigai¹,

Hara²,

Kawamoto³

et al. 2004

Arthritis & Rheumatism

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Objective. To determine the signal transduction pathways in CD14؉ synovial cells from patients with rheumatoid arthritis (RA) after CD40 ligation, and to examine their role in amplifying synovial inflammation in affected joints.Methods. Expression of messenger RNA was analyzed using quantitative reverse transcriptionpolymerase chain reaction. Cytokines and chemokines were measured using enzyme-linked immunosorbent assay. Activation of kinases was detected using Western blotting. Nuclear translocation of NF-B was examined using immunohistochemistry. CD14؉ synovial cells were enriched using magnetic cell sorting. Fibroblastlike synoviocytes (FLS) were obtained by passaging primary synovial cell culture.Results. Stimulation of CD14؉ synovial cells from RA patients by recombinant soluble CD154 (rsCD154) significantly induced expression of tumor necrosis factor ␣ (TNF␣),

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“…This is important because C/EBP␤ has been shown to interact with other transcription factors, including Sp1, NF ␤, and CREB, in addition to other members of the C/EBP family. [38][39][40][41] Moreover, the state and site of phosphorylation of C/EBP␤, and of the transcription factors that interact with it play a key role in modulating their transcriptional activity. [42][43][44] Based on the results presented in this communication, as well as others presented elsewhere, 22,36 we propose the hypothesis that agents that induce the accumulation of H 2 O 2 , and/or enhanced binding of C/EBP␤, can be potentially fibrogenic and, thus, could induce the transcriptional activation of the col1a1 gene in HSC.…”

Section: Discussionmentioning

confidence: 99%

Hydrogen peroxide: A link between acetaldehyde-elicited α1(i) collagen gene up-regulation and oxidative stress in mouse hepatic stellate cells

Greenwel

Domínguez-Rosales²,

Mavi³

et al. 2000

Hepatology

182

145

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Ethanol induces liver fibrosis by several means that include, among others, the direct fibrogenic actions of acetaldehyde and the induction of an oxidative stress response. However, the mechanisms responsible for these activities, and the possible connections between oxidative stress and acetaldehyde-induced fibrosis are not well understood. In this communication we investigated the molecular mechanisms whereby acetaldehyde induces mouse ␣1(I) procollagen (col1a1) gene expression in cultured hepatic stellate cells. Transfection assays using reporter plasmids driven by different segments of the col1a1 promoter localized an acetaldehyde-responsive element (AcRE) between nucleotides ؊370 and ؊345. We also show that acetaldehyde enhances binding of a CCAAT/enhancer binding protein-␤ (C/EBP␤)-containing complex to this element, and that this effect is due, at least in part, to an increase in the concentration of nuclear p35C/EBP␤ protein. Although this element overlaps to a previously described transforming growth factor ␤1 (TGF-␤1)-responsive element, the stimulatory effect of acetaldehyde is not mediated through this cytokine, because addition of neutralizing anti-TGF-␤1 antibodies does not prevent acetaldehyde-elicited col1a1 up-regulation. On the other hand, this effect is blocked by the addition of catalase, an H 2 O 2 scavenger. Moreover, this ethanol metabolite stimulates production of H 2 O 2 in stellate cells. Thus, these results suggest that acetaldehyde-induced col1a1 up-regulation is mediated, at least in part, through H 2 O 2 . Altogether, these data suggest that the ؊370 to ؊344

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Transcription factors NF-IL6 and CREB recognize a common essential site in the human prointerleukin 1 beta gene.

Cited by 143 publications

References 48 publications

Design of a C/EBP-specific, Dominant-negative bZIP Protein with Both Inhibitory and Gain-of-function Properties

Design of a C/EBP-specific, Dominant-negative bZIP Protein with Both Inhibitory and Gain-of-function Properties

Amplification of the synovial inflammatory response through activation of mitogen‐activated protein kinases and nuclear factor κB using ligation of CD40 on CD14+ synovial cells from patients with rheumatoid arthritis

Hydrogen peroxide: A link between acetaldehyde-elicited α1(i) collagen gene up-regulation and oxidative stress in mouse hepatic stellate cells

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