Evidence map›Paper›PMID 22351752›Full record

ArticleThe Journal of biological chemistry2012

Cell surface proteoglycans syndecan-1 and -4 bind overlapping but distinct sites in laminin α3 LG45 protein domain.

Sonia Carulli, Konrad Beck, Guila Dayan, Sophie Boulesteix, Hugues Lortat-Jacob, Patricia Rousselle

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
2.3field-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

30 citing papers in PubMed, 57 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Autoimmunity against laminin 332.Frontiers in immunology · 2023
    Review
  8. Coreceptor functions of cell surface heparan sulfate proteoglycans.American journal of physiology. Cell physiology · 2022
    Review
  9. Article
  10. An Atlas of Heparan Sulfate Proteoglycans in the Postnatal Rat Lens.Investigative ophthalmology & visual science · 2021
    Article
  11. Article
  12. Review
  13. Review
  14. Review
  15. Article
  16. Review
  17. The extracellular matrix in tumor progression and metastasis.Clinical & experimental metastasis · 2019
    Review
  18. Review
  19. Article
  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

6 authors at 3 institutions in 2 countries.

Sonia CarulliStructure Fédérative de Recherche BioSciences Gerland-Lyon Sud, Institut de Biologie et Chimie des Protéines, FRE 3310, CNRS, Université Lyon 1, 7 Passage du Vercors, 69367 Lyon, France.
Konrad Beck
Guila Dayan
Sophie Boulesteix
Hugues Lortat-Jacob
Patricia Rousselle
Université Claude Bernard Lyon 1 · FRCardiff University · GBCentre National de la Recherche Scientifique · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Keratinocyte migration during epidermal repair depends on interactions between cellular heparan sulfate proteoglycan receptors, syndecan-1 and -4, and the C-terminal globular domains (LG45) of the extracellular matrix protein laminin 332. This study investigates the molecular basis of the binding specificity of the syndecan-1 and -4 receptors expressed by human keratinocytes. We used site-directed mutagenesis to alter a recombinant LG45 protein by substituting the most critical basic residues with glutamine. All proteins were expressed in mammalian cells, purified, and characterized biochemically. We used in vitro binding assays, including surface plasmon resonance, to examine interactions between mutated LG45 and heparan sulfates, syndecan-1 and -4. We identify a major heparin binding domain on the outer edge of a β-strand of LG45 surrounded by a track of converging low affinity residues. This domain harbors distinctive syndecan-1 and -4 binding-specific sequences. This is the first study to demonstrate a binding specificity of two proteoglycans produced by a single cell type. In addition, we found that although syndecan-1 interacts exclusively through its glycosaminoglycan chains, syndecan-4 binding relies on both its core protein and its heparan sulfate chains. These results suggest that LG45 may trigger different signals toward keratinocytes depending on its interaction with syndecan-1 or -4.

Indexed as

Amino Acid SequenceAmino Acid SubstitutionBinding SitesCell AdhesionCell LineCell MovementChromatography, AffinityHeparan SulfateHeparinHumansImmobilized ProteinsKeratinocytesLamininMolecular Sequence DataMutagenesis, Site-DirectedProtein BindingHeparan SulfateHeparinImmobilized ProteinsLamininlaminin alpha 3Recombinant ProteinsSDC1 protein, humanSDC4 protein, humanSyndecan-1Syndecan-4

Identifiers

PMID22351752
PMCPMC3320972
OpenAlexW2112237230

What OpenQuestion holds

Textmetadata
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.