Evidence map›Paper›PMID 8065357›Full record

ArticleMolecular and cellular biology1994

YY1 represses rat serum amyloid A1 gene transcription and is antagonized by NF-kappa B during acute-phase response.

S Y Lu, M Rodriguez, W S Liao

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
5.1field-weighted citation impact, top 4% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

33 citing papers in PubMed, 114 citations in OpenAlex.

  1. Article
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  7. Transcriptome profiling of the cancer and adjacent nontumor tissues from cervical squamous cell carcinoma patients by RNA sequencing.Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine · 2015
    Article
  8. Characterization of rat serum amyloid A4 (SAA4): a novel member of the SAA superfamily.Biochemical and biophysical research communications · 2014
    Article
  9. Article
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  15. Role of the E1A Rb-binding domain in repression of the NF-kappa B-dependent defense against tumor necrosis factor-alpha.Proceedings of the National Academy of Sciences of the United States of America · 2002
    Article
  16. Review
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors at 1 institution in 1 country.

S Y LuDepartment of Biochemistry and Molecular Biology, University of Texas M.D. Anderson Cancer Center, Houston 77030.
M Rodriguez
W S Liao
The University of Texas MD Anderson Cancer Center · US

Funding

Tumor Evolution and Metastasis ProgramP30CA016672 · NCI · UNIVERSITY OF TX MD ANDERSON CAN CTR · PI Kathrin Milbury · 1985 to 2026
$290.8M
MOLECULAR ASPECTS OF AMYLOIDOSISR01AR038858 · NIAMS · UNIVERSITY OF TEXAS MD ANDERSON CAN CTR · PI LIAO, WARREN S. · 1992 to 1999
–
MOLECULAR ASPECTS OF AMYLOIDOSISR29AR038858 · NIAMS · UNIVERSITY OF TEXAS MD ANDERSON CAN CTR · PI LIAO, WARREN S. · 1987 to 1991
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NCI NIH HHS CA 16672NIAMS NIH HHS AR 38858
6 · The paper itself

Abstract

Serum amyloid A (SAA), one of the major acute-phase proteins, increases several hundredfold in concentration in plasma following acute inflammation, primarily as a result of a 200-fold increase in its transcriptional rate. Functional analysis of the rat SAA1 promoter has identified a 65-bp cytokine response unit (CRU; positions -135 to -71) that could confer cytokine responsiveness on a heterologous promoter. Within this CRU, two cis-regulatory elements, corresponding to NF-kappa B- and C/EBP-binding sites, were found to be functionally important and exerted synergistic effects on induced SAA1 expression. In this report, we show that a third transcription factor interacts with the CRU through a region located between the NF-kappa B- and C/EBP-binding sites. On the basis of its gel mobility shift patterns, ubiquitous binding activity, sequence specificity of DNA binding, zinc-dependent binding activity, and gel mobility supershift by specific antibodies, we concluded that this factor is identical to YY1. Methylation interference studies revealed that YY1 binding sequences overlapped with those of NF-kappa B, and gel mobility studies showed that NF-kappa binding to the CRU was effectively inhibited by YY1. Consistent with its presumed antagonistic role to NF-kappa B, YY1 exerted a negative effect on SAA1 expression, whereas disruption of its binding in the promoter elevated basal and cytokine-induced activities. Furthermore, overexpression of YY1 trans-repressed SAA1 promoter activity. Thus, our results demonstrate that SAA1 expression is tightly regulated by an on-off switch of activators and repressors, presumably to ensure that it is expressed only under appropriate physiological conditions.

Indexed as

Acute-Phase ReactionAnimalsBase SequenceBinding, CompetitiveCCAAT-Enhancer-Binding ProteinsCytokinesDNA-Binding ProteinsErythroid-Specific DNA-Binding FactorsGene Expression RegulationMolecular Sequence DataMutagenesis, Site-DirectedNF-kappa BNuclear ProteinsOligodeoxyribonucleotidesPromoter Regions, GeneticRatsCCAAT-Enhancer-Binding ProteinsCytokinesDNA-Binding ProteinsErythroid-Specific DNA-Binding FactorsNF-kappa BNuclear ProteinsOligodeoxyribonucleotidesRepressor ProteinsRNA, MessengerSerum Amyloid A ProteinTranscription FactorsYy1 protein, ratYY1 Transcription Factor

Identifiers

PMID8065357
PMCPMC359152
OpenAlexW2102039858

What Socratic holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the Socratic graph.