Evidence map›Paper›PMID 27228163›Full record

ArticlePloS one2016

CD14 Is a Co-Receptor for TLR4 in the S100A9-Induced Pro-Inflammatory Response in Monocytes.

Zhifei He, Matteo Riva, Per Björk, Karl Swärd, Matthias Mörgelin, Tomas Leanderson, Fredrik Ivars

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
2.8field-weighted citation impact, top 10% 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

35 citing papers in PubMed, 54 citations in OpenAlex.

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  12. Evolutionary entrenchment in immune proteins selects against stabilizing mutations.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  13. Evolution avoids a pathological stabilizing interaction in the immune protein S100A9.Proceedings of the National Academy of Sciences of the United States of America · 2022
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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

7 authors at 2 institutions in 1 country.

Zhifei HeImmunology group, Section for Immunology, Department of Experimental Medical Science, Lund University, Lund, Sweden.
Matteo RivaImmunology group, Section for Immunology, Department of Experimental Medical Science, Lund University, Lund, Sweden.
Per BjörkActive Biotech AB, Lund, Sweden.
Karl SwärdSection for Cell and Tissue Biology, Department of Experimental Medical Science, Lund University, Lund, Sweden.
Matthias MörgelinSection for Infection Biology, Department of Clinical Sciences, Lund University, Lund, Sweden.
Tomas LeandersonImmunology group, Section for Immunology, Department of Experimental Medical Science, Lund University, Lund, Sweden.
Fredrik IvarsImmunology group, Section for Immunology, Department of Experimental Medical Science, Lund University, Lund, Sweden.
Lund University · SEActive Biotech (Sweden) · SE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The cytosolic Ca2+-binding S100A9 and S100A8 proteins form heterodimers that are primarily expressed in human neutrophils and monocytes. We have recently shown that S100A9 binds to TLR4 in vitro and induces TLR4-dependent NF-κB activation and a pro-inflammatory cytokine response in monocytes. In the present report we have further investigated the S100A9-mediated stimulation of TLR4 in monocytes. Using transmission immunoelectron microscopy, we detected focal binding of S100A9 to monocyte membrane subdomains containing the caveolin-1 protein and TLR4. Furthermore, the S100A9 protein was detected in early endosomes of the stimulated cells, indicating that the protein could be internalized by endocytosis. Although stimulation of monocytes with S100A9 was strictly TLR4-dependent, binding of S100A9 to the plasma membrane and endocytosis of S100A9 was still detectable and coincided with CD14 expression in TLR4-deficient cells. We therefore investigated whether CD14 would be involved in the TLR4-dependent stimulation and could show that the S100A9-induced cytokine response was inhibited both in CD14-deficient cells and in cells exposed to CD14 blocking antibodies. Further, S100A9 was not internalized into CD14-deficient cells suggesting a direct role of CD14 in endocytosis of S100A9. Finally, we could detect satiable binding of S100A9 to CD14 in surface plasmon resonance experiments. Taken together, these results indicate that CD14 is a co-receptor of TLR4 in the S100A9-induced cytokine response.

Indexed as

AnimalsCalgranulin BCaveolin 1Cell Line, TumorCell MembraneCytokinesHumansInflammationLipopolysaccharide ReceptorsMiceMice, KnockoutMonocytesProtein BindingSurface Plasmon ResonanceToll-Like Receptor 4Calgranulin BCaveolin 1CytokinesLipopolysaccharide ReceptorsS100A9 protein, mouseTLR4 protein, humanTlr4 protein, mouseToll-Like Receptor 4

Identifiers

PMID27228163
PMCPMC4881898
OpenAlexW2394486499

What OpenQuestion holds

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LicenceCC BY
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.