Evidence map›Paper›PMID 9199324›Full record

ArticleMolecular and cellular biology1997

Adhesion-dependent regulation of an A+U-rich element-binding activity associated with AUF1.

O I Sirenko, A K Lofquist, C T DeMaria, J S Morris, G Brewer, J S Haskill

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
4.8field-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

44 citing papers in PubMed, 144 citations in OpenAlex.

  1. Article
  2. Interleukin-1 Beta-A Friend or Foe in Malignancies?International journal of molecular sciences · 2018
    Review
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  7. Review
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  9. Article
  10. AUF1 isoform-specific regulation of anti-inflammatory IL10 expression in monocytes.Journal of interferon & cytokine research : the official journal of the International Society for Interferon and Cytokine Research · 2008
    Article
  11. Article
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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

6 authors at 3 institutions in 3 countries.

O I SirenkoLineberger Comprehensive Cancer Center, University of North Carolina, Chapel Hill 27599-7295, USA.
A K Lofquist
C T DeMaria
J S Morris
G Brewer
J S Haskill
University of North Carolina at Chapel Hill · USAtrium Health Wake Forest Baptist · USUniversity of Idaho · US

Funding

TRAINING PROGRAM IN IMMUNOLOGY AND PATHOGENESIST32AI007401 · NIAID · WAKE FOREST UNIVERSITY HEALTH SCIENCES · PI Martha Ann Alexander-Miller · 1991 to 2026
$4.4M
ADHERENCE REGULATED MONOCYTE GENESR01AI026774 · NIAID · UNIVERSITY OF NORTH CAROLINA CHAPEL HILL · PI HASKILL, JOHN S · 1989 to 1999
–
NIAID NIH HHS AI 26774NIAID NIH HHS T32-AI 07401
6 · The paper itself

Abstract

Monocyte adherence results in the rapid transcriptional activation and mRNA stabilization of numerous mediators of inflammation and tissue repair. While the enhancer and promoter elements associated with transcriptional activation have been studied, mechanisms linking adhesion, mRNA stabilization, and translation are unknown. GROalpha and interleukin-1beta (IL-1beta) mRNAs are highly labile in nonadhered monocytes but stabilize rapidly after adherence. GROalpha and IL-1beta transcripts both contain A+U-rich elements (AREs) in the 3' untranslated region (UTR) which have been directly associated with rapid mRNA turnover. To determine if the GROalpha ARE region was recognized by factors associated with mRNA degradation, we carried out mobility gel shift analyses using a series of RNA probes encompassing the entire GROalpha transcript. Stable complexes were formed only with the proximal 3' UTR which contained the ARE region. The two slower-moving complexes were rapidly depleted following monocyte adherence but not direct integrin engagement. Deadherence reactivated the two largest ARE-binding complexes and destabilized IL-1beta transcripts. Antibody supershift studies demonstrated that both of these ARE RNA-binding complexes contained AUF1. The formation of these complexes and the accelerated mRNA turnover are phosphorylation-dependent events, as both are induced in adherent monocytes by the tyrosine kinase inhibitor genistein and the p38 MAP kinase inhibitor of IL-1beta translation, SK&F 86002. These results demonstrate that cell adhesion and deadhesion rapidly and reversibly modify both cytokine mRNA stability and the RNA-binding complexes associated with AUF1.

Indexed as

Chemokines, CXCHeterogeneous-Nuclear Ribonucleoprotein DIntercellular Signaling Peptides and ProteinsCell AdhesionChemokine CXCL1Chemotactic FactorsCytokinesGene Expression RegulationGrowth SubstancesHeterogeneous Nuclear Ribonucleoprotein D0HumansInterleukin-1MonocytesPhosphorylationRNA-Binding ProteinsRNA, MessengerChemokine CXCL1Chemokines, CXCChemotactic FactorsCXCL1 protein, humanCytokinesGrowth SubstancesHeterogeneous-Nuclear Ribonucleoprotein DHeterogeneous Nuclear Ribonucleoprotein D0HNRNPD protein, humanIntercellular Signaling Peptides and ProteinsInterleukin-1RNA-Binding ProteinsRNA, Messenger

Identifiers

PMID9199324
PMCPMC232242
OpenAlexW2150827129

What OpenQuestion 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 OpenQuestion graph.