Evidence map›Paper›PMID 23160308›Full record

ReviewCurrent opinion in allergy and clinical immunology2013

The role of lung epithelial ligands for Siglec-8 and Siglec-F in eosinophilic inflammation.

Takumi Kiwamoto, Toshihiko Katoh, Michael Tiemeyer, Bruce S Bochner

Open access · greenAbstract readReview
In one paragraph

Review in Current opinion in allergy and clinical immunology, 2013. 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
2.0field-weighted citation impact, top 13% 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, 36 citations in OpenAlex.

  1. Article
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  4. CCR3-dependent eosinophil recruitment is regulated by sialyltransferase ST3Gal-IV.Proceedings of the National Academy of Sciences of the United States of America · 2024
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  9. Review
  10. Observational
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  12. Structural basis for sulfation-dependent self-glycan recognition by the human immune-inhibitory receptor Siglec-8.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  13. Review
  14. Article
  15. Review
  16. Article
  17. 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

4 authors at 3 institutions in 1 country.

Takumi KiwamotoDivision of Allergy and Clinical Immunology, Department of Medicine, The Johns Hopkins University School of Medicine, Baltimore, Maryland 21224-6821, USA.
Toshihiko Katoh
Michael Tiemeyer
Bruce S Bochner
Johns Hopkins University · USJohns Hopkins Medicine · USUniversity of Georgia · US

Funding

Treating lung inflammation by targeting SiglecsP01HL107151 · NHLBI · JOHNS HOPKINS UNIVERSITY · PI SCHNAAR, RONALD L · 2011 to 2017
$15.4M
Targeting Siglec-8/Siglec-F Reduce Allergic Responses In Vitro and In VivoR01AI072265 · NIAID · NORTHWESTERN UNIVERSITY AT CHICAGO · PI BOCHNER, BRUCE S · 2007 to 2017
$3.9M
Targeting Siglec-8/-F to treat eosinophil and mast cell related disordersR56AI072265 · NIAID · JOHNS HOPKINS UNIVERSITY · PI BOCHNER, BRUCE S · 2012 to 2012
$405k
NHLBI NIH HHS HL107151NHLBI NIH HHS P01 HL107151NIAID NIH HHS AI72265NIAID NIH HHS R01 AI072265NIAID NIH HHS R56 AI072265
6 · The paper itself

Abstract

purpose of reviewSiglec-8 and Siglec-F are single pass transmembrane inhibitory receptors found on the surface of human and mouse eosinophils, respectively, but very little is known about their physiologic glycan ligands. This article reviews the latest knowledge on this topic and outlines the strategies being used to further define the production and glycobiochemical nature of these molecules in the lung. RECENT

findingsBoth Siglec-8 and Siglec-F recognize the same glycan structure, namely 6'-sulfated sialyl Lewis X, as determined using glycan array technologies. Studies have identified α2,3-linked sialylated glycoprotein structures localized to mouse airway epithelium in tissue sections, where their constitutive expression requires the specific sialyltransferase St3gal3. Expression of these ligands in lung is enhanced during allergic inflammation and by cytokines such as IL-13, and is maintained in primary air-liquid interface cultures of mouse lung epithelium. Further characterization suggests that they are high molecular weight sialylated proteins, putatively mucins. By combining analytic glycomics, glycoproteomic mapping, and further in-vitro eosinophil experimentation including the ability of candidate structures to enhance eosinophil apoptosis, a finely detailed appreciation of the structural requirements for productive Siglec-8 and Siglec-F engagement should soon emerge. SUMMARY: An enhanced understanding of Siglec-F, Siglec-8, and their ligands should improve our understanding of endogenous lung pathways limiting the survival of eosinophils within the airway in diseases such as asthma. Knowledge of this biology may also result in novel opportunities for drug development involving glycans and glycomimetics that selectively bind to Siglec-8 and induce eosinophil death.

Indexed as

AnimalsAntigens, CDAntigens, Differentiation, B-LymphocyteAntigens, Differentiation, MyelomonocyticAsthmaEosinophilsHumansLectinsLigandsLungMiceSialic Acid Binding Immunoglobulin-like LectinsAntigens, CDAntigens, Differentiation, B-LymphocyteAntigens, Differentiation, MyelomonocyticLectinsLigandsSialic Acid Binding Immunoglobulin-like LectinsSIGLEC8 protein, humanSiglecf protein, mouse

Identifiers

PMID23160308
PMCPMC4376104
OpenAlexW2328717099

What OpenQuestion holds

Textmetadata
LicenceTDM
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.