Evidence map›Paper›PMID 34145909›Full record

ArticleEuropean journal of immunology2021

Recognition of S100 proteins by Signal Inhibitory Receptor on Leukocytes-1 negatively regulates human neutrophils.

Matevž Rumpret, Helen J von Richthofen, Maarten van der Linden, Geertje H A Westerlaken, Cami Talavera Ormeño, Teck Y Low, Huib Ovaa, Linde Meyaard

Open access · hybridAbstract read
In one paragraph

Article in European journal of immunology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.6field-weighted citation impact, top 16% 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

16 citing papers in PubMed, 25 citations in OpenAlex.

  1. A first structural model for covalent dimerization of S100 proteins.Acta crystallographica. Section F, Structural biology communications · 2026
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  2. Review
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  11. Specific S100 Proteins Bind Tumor Necrosis Factor and Inhibit Its Activity.International journal of molecular sciences · 2022
    Article
  12. Article
  13. Article
  14. Inhibitory pattern recognition receptors.The Journal of experimental medicine · 2022
    Review
  15. Review
  16. Signal inhibitory receptor on leukocytes-1 recognizes bacterial and endogenous amphipathic α-helical peptides.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2021
    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

8 authors at 2 institutions in 2 countries.

Matevž RumpretCenter for Translational Immunology, University Medical Center Utrecht, Utrecht University, Utrecht, The Netherlands.ORCID 0000-0002-8631-8049
Helen J von RichthofenCenter for Translational Immunology, University Medical Center Utrecht, Utrecht University, Utrecht, The Netherlands.ORCID 0000-0002-2062-5986
Maarten van der LindenCenter for Translational Immunology, University Medical Center Utrecht, Utrecht University, Utrecht, The Netherlands.ORCID 0000-0001-8597-4151
Geertje H A WesterlakenCenter for Translational Immunology, University Medical Center Utrecht, Utrecht University, Utrecht, The Netherlands.
Cami Talavera OrmeñoOncode Institute, Utrecht, The Netherlands.ORCID 0000-0001-5502-2985
Teck Y LowBiomolecular Mass Spectrometry and Proteomics, Bijvoet Center for Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences and Netherlands Proteomics Center, Utrecht University, Utrecht, The Netherlands.ORCID 0000-0001-7878-7534
Huib OvaaOncode Institute, Utrecht, The Netherlands.
Linde MeyaardCenter for Translational Immunology, University Medical Center Utrecht, Utrecht University, Utrecht, The Netherlands.ORCID 0000-0003-0707-4793
Utrecht University · NLLeiden University Medical Center · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Signal inhibitory receptor on leukocytes-1 (SIRL-1) is an inhibitory receptor with a hitherto unknown ligand, and is expressed on human monocytes and neutrophils. SIRL-1 inhibits myeloid effector functions such as reactive oxygen species (ROS) production. In this study, we identify S100 proteins as SIRL-1 ligands. S100 proteins are composed of two calcium-binding domains. Various S100 proteins are damage-associated molecular patterns (DAMPs) released from damaged cells, after which they initiate inflammation by ligating activating receptors on immune cells. We now show that the inhibitory SIRL-1 recognizes individual calcium-binding domains of all tested S100 proteins. Blocking SIRL-1 on human neutrophils enhanced S100 protein S100A6-induced ROS production, showing that S100A6 suppresses neutrophil ROS production via SIRL-1. Taken together, SIRL-1 is an inhibitory receptor recognizing the S100 protein family of DAMPs. This may help limit tissue damage induced by activated neutrophils.

Indexed as

AlarminsHumansInflammationMonocytesNeutrophil ActivationNeutrophilsReactive Oxygen SpeciesReceptors, ImmunologicS100 ProteinsSignal TransductionAlarminsReactive Oxygen SpeciesReceptors, ImmunologicS100 ProteinsVSTM1 protein, humanDAMPimmune regulationinhibitory receptorS100SIRL-1

Identifiers

PMID34145909
PMCPMC8457157
OpenAlexW3172685342

What OpenQuestion holds

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LicenceCC BY-NC-ND
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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.