Evidence map›Paper›PMID 21561871›Full record

ArticleThe Journal of biological chemistry2011

Identification of neutrophil granule glycoproteins as Lewis(x)-containing ligands cleared by the scavenger receptor C-type lectin.

Sarah A Graham, Aristotelis Antonopoulos, Paul G Hitchen, Stuart M Haslam, Anne Dell, Kurt Drickamer, Maureen E Taylor

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
1.5field-weighted citation impact, top 19% 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

22 citing papers in PubMed, 42 citations in OpenAlex.

  1. Article
  2. Article
  3. Glycoproteome remodeling and organelle-specificProceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  4. Article
  5. Article
  6. Loss of Function of Scavenger Receptor SCAV-5 ProtectsFrontiers in cellular and infection microbiology · 2021
    Article
  7. Article
  8. Article
  9. Observational
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Review
  18. Article
  19. Article
  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

7 authors at 1 institution in 3 countries.

Sarah A GrahamDivision of Molecular Biosciences, Department of Life Sciences, Imperial College, London SW7 2AZ, United Kingdom.
Aristotelis Antonopoulos
Paul G Hitchen
Stuart M Haslam
Anne Dell
Kurt Drickamer
Maureen E Taylor
Imperial College London · GB

Funding

Biotechnology and Biological Sciences Research Council B19088Biotechnology and Biological Sciences Research Council BBC5196701Biotechnology and Biological Sciences Research Council BBF0083091Biotechnology and Biological Sciences Research Council SF19107Wellcome TrustWellcome Trust 075565
6 · The paper itself

Abstract

The scavenger receptor C-type lectin (SRCL) is a glycan-binding receptor that has the capacity to mediate endocytosis of glycoproteins carrying terminal Lewis(x) groups (Galβ1-4(Fucα1-3)GlcNAc). A screen for glycoprotein ligands for SRCL using affinity chromatography on immobilized SRCL followed by mass spectrometry-based proteomic analysis revealed that soluble glycoproteins from secondary granules of neutrophils, including lactoferrin and matrix metalloproteinases 8 and 9, are major ligands. Binding competition and surface plasmon resonance analysis showed affinities in the low micromolar range. Comparison of SRCL binding to neutrophil and milk lactoferrin indicates that the binding is dependent on cell-specific glycosylation in the neutrophils, as the milk form of the glycoprotein is a much poorer ligand. Binding to neutrophil glycoproteins is fucose-dependent, and mass spectrometry-based glycomic analysis of neutrophil and milk lactoferrin was used to establish a correlation between high affinity binding to SRCL and the presence of multiple clustered terminal Lewis(x) groups on a heterogeneous mixture of branched glycans, some with poly N-acetyllactosamine extensions. The ability of SRCL to mediate uptake of neutrophil lactoferrin was confirmed using fibroblasts transfected with SRCL. The common presence of Lewis(x) groups in granule protein glycans can thus target granule proteins for clearance by SRCL. PCR and immunohistochemical analysis confirm that SRCL is widely expressed on endothelial cells and thus represents a distributed system that could scavenge released neutrophil glycoproteins both locally at sites of inflammation or systemically when they are released in the circulation.

Indexed as

CollectinsEndothelial CellsFibroblastsFucoseGene Expression RegulationGlycoproteinsHumansLewis X AntigenLigandsNeutrophilsOrgan SpecificityProtein BindingReceptors, ScavengerSecretory VesiclesTrisaccharidesCOLEC12 protein, humanCollectinsFucosegalactosyl-(1,4)-fucopyranosyl-(1,3)-N-acetylglucosamineGlycoproteinsLewis X AntigenLigandsReceptors, ScavengerTrisaccharides

Identifiers

PMID21561871
PMCPMC3129213
OpenAlexW2076081730

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.