Evidence map›Paper›PMID 27025255›Full record

ArticleScientific reports2016

Soluble alpha-enolase activates monocytes by CD14-dependent TLR4 signalling pathway and exhibits a dual function.

Clément Guillou, Manuel Fréret, Emeline Fondard, Céline Derambure, Gilles Avenel, Marie-Laure Golinski, Mathieu Verdet, Olivier Boyer, Frédérique Caillot, Philippe Musette and 2 more

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

24 citing papers in PubMed, 30 citations in OpenAlex.

  1. Article
  2. Enolase-1 and Inflammation.Biomolecules · 2026
    Review
  3. Review
  4. Article
  5. Article
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  8. Article
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  13. Article
  14. Implications of enolase in the RANKL-mediated osteoclast activity following spinal cord injury.Biocell : official journal of the Sociedades Latinoamericanas de Microscopia Electronica ... et. al · 2021
    Article
  15. Article
  16. Enolase 1, a Moonlighting Protein, as a Potential Target for Cancer Treatment.International journal of biological sciences · 2021
    Review
  17. Review
  18. Review
  19. When Place Matters: Shuttling of Enolase-1 Across Cellular Compartments.Frontiers in cell and developmental biology · 2019
    Review
  20. Article
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

12 authors at 3 institutions in 1 country.

Clément GuillouINSERM, U905 &Normandy University, Institute for Research and Innovation in Biomedicine (IRIB), Rouen, France.
Manuel FréretINSERM, U905 &Normandy University, Institute for Research and Innovation in Biomedicine (IRIB), Rouen, France.
Emeline FondardINSERM, U905 &Normandy University, Institute for Research and Innovation in Biomedicine (IRIB), Rouen, France.
Céline DerambureINSERM, U905 &Normandy University, Institute for Research and Innovation in Biomedicine (IRIB), Rouen, France.
Gilles AvenelRouen University Hospital, Department of Rheumatology, Rouen, France.
Marie-Laure GolinskiINSERM, U905 &Normandy University, Institute for Research and Innovation in Biomedicine (IRIB), Rouen, France.
Mathieu VerdetRouen University Hospital, Department of Rheumatology, Rouen, France.
Olivier BoyerINSERM, U905 &Normandy University, Institute for Research and Innovation in Biomedicine (IRIB), Rouen, France.
Frédérique CaillotINSERM, U905 &Normandy University, Institute for Research and Innovation in Biomedicine (IRIB), Rouen, France.
Philippe MusetteINSERM, U905 &Normandy University, Institute for Research and Innovation in Biomedicine (IRIB), Rouen, France.
Thierry LequerréINSERM, U905 &Normandy University, Institute for Research and Innovation in Biomedicine (IRIB), Rouen, France.
Olivier VittecoqINSERM, U905 &Normandy University, Institute for Research and Innovation in Biomedicine (IRIB), Rouen, France.
Inserm · FRUniversité de Rouen Normandie · FRInstitute for Research and Innovation in Biomedicine · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Rheumatoid arthritis (RA) is the most common form of chronic inflammatory rheumatism. Identifying auto-antigens targeted by RA auto-antibodies is of major interest. Alpha-enolase (ENO1) is considered to be a pivotal auto-antigen in early RA but its pathophysiologic role remains unknown. The main objective of this study was to investigate the in vitro effects of soluble ENO1 on peripheral blood mononuclear cells (PBMC) from healthy donors and RA patients in order to determine the potential pathogenic role of ENO1. ELISA, transcriptomic analysis, experiments of receptor inhibition and flow cytometry analysis were performed to determine the effect, the target cell population and the receptor of ENO1. We showed that ENO1 has the ability to induce early production of pro-inflammatory cytokines and chemokines with delayed production of IL-10 and to activate the innate immune system. We demonstrated that ENO1 binds mainly to monocytes and activates the CD14-dependent TLR4 pathway both in healthy subjects and in RA patients. Our results establish for the first time that ENO1 is able to activate in vitro the CD14-dependent TLR4 pathway on monocytes involving a dual mechanism firstly pro-inflammatory and secondly anti-inflammatory. These results contribute to elucidating the role of this auto-antigen in the pathophysiologic mechanisms of RA.

Indexed as

AnimalsBiomarkers, TumorCattleCells, CulturedDNA-Binding ProteinsHumansInterleukin-10Leukocytes, MononuclearLipopolysaccharide ReceptorsLipopolysaccharidesPhosphopyruvate HydrataseSignal TransductionToll-Like Receptor 4Tumor Necrosis Factor-alphaTumor Suppressor ProteinsBiomarkers, TumorDNA-Binding ProteinsENO1 protein, humanIL10 protein, humanInterleukin-10Lipopolysaccharide ReceptorsLipopolysaccharidesPhosphopyruvate HydrataseTLR4 protein, humanTNF protein, humanToll-Like Receptor 4Tumor Necrosis Factor-alphaTumor Suppressor Proteins

Identifiers

PMID27025255
PMCPMC4824496
OpenAlexW2323466180

What OpenQuestion holds

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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.