Evidence map›Paper›PMID 22271244›Full record

ReviewAnnals of biomedical engineering2012

E-selectin ligands as mechanosensitive receptors on neutrophils in health and disease.

S D Chase, J L Magnani, S I Simon

Open access · greenAbstract readReview
In one paragraph

Review in Annals of biomedical engineering, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
4.0field-weighted citation impact, top 6% 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

39 citing papers in PubMed, 71 citations in OpenAlex.

  1. Trial
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  13. P- and E- selectin in venous thrombosis and non-venous pathologies.Journal of thrombosis and haemostasis : JTH · 2022
    Review
  14. Review
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  16. Article
  17. Epigenetic Regulation of Glycosylation in Cancer and Other Diseases.International journal of molecular sciences · 2021
    Review
  18. Review
  19. Review
  20. Review
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

3 authors at 2 institutions in 1 country.

S D ChaseUniversity of California Davis, Davis, CA, USA.
J L Magnani
S I Simon
University of California, Davis · USGlycoMimetics (United States) · US

Funding

Outside-in Mechanotransduced Inflammatory TargetsR01AI047294 · NIAID · UNIVERSITY OF CALIFORNIA DAVIS · PI SIMON, SCOTT IRWIN · 1999 to 2021
$7.0M
NIAID NIH HHS AI47294NIAID NIH HHS R01 AI047294
6 · The paper itself

Abstract

Application of mechanical force to bonds between selectins and their ligands is a requirement for these adhesion receptors to optimally perform functions that include leukocyte tethering and activation of stable adhesion. Although all three selectins are reported to signal from the outside-in subsequent to ligand binding, E-selectin is unique in its capacity to bind multiple sialyl Lewis x presenting ligands and mediate slow rolling on the order of a micron per second. A diverse set of ligands are recognized by E-selectin in the mouse, including ESL-1, CD44 (HCELL), and PSGL-1 which are critical in transition from slow rolling to arrest and for efficient transendothelial migration. The molecular recognition process is different in humans as L-selectin is a major ligand, which along with glycolipids constitute more than half of the E-selectin receptors on human polymorphonuclear neutrophils (PMN). In addition, E-selectin is most efficient at raising the affinity and avidity of CD18 integrins that supports PMN deceleration and trafficking to sites of acute inflammation. The mechanism is only partially understood but known to involve a rise in cytosolic calcium and tyrosine phosphorylation that activates p38 MAP kinase and Syk kinase, both of which transduce signals from clustered E-selectin ligands. In this review we highlight the molecular recognition and mechanical requirements of this process to reveal how E-selectin confers selectivity and efficiency of signaling for extravasation at sites of inflammation and the mechanism of action of a new glycomimetic antagonist targeted to the lectin domain that has shown efficacy in blocking neutrophil activation and adhesion on inflamed endothelium.

Indexed as

MAP Kinase Signaling SystemNeutrophil ActivationTransendothelial and Transepithelial MigrationAcute DiseaseAnimalsCalciumCD18 AntigensE-SelectinHumansHyaluronan ReceptorsInflammationLigandsMembrane GlycoproteinsMiceNeutrophilsp38 Mitogen-Activated Protein KinasesCalciumCD18 AntigensCD44 protein, humanE-SelectinHyaluronan ReceptorsLigandsMembrane Glycoproteinsp38 Mitogen-Activated Protein KinasesP-selectin ligand proteinSELE protein, human

Identifiers

PMID22271244
PMCPMC3680630
OpenAlexW2086708696

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.