Evidence map›Paper›PMID 31547381›Full record

ArticleBiomolecules2019

Sulfated Glycoaminoglycans and Proteoglycan Syndecan-4 Are Involved in Membrane Fixation of LL-37 and Its Pro-Migratory Effect in Breast Cancer Cells.

Chahrazed Habes, Günther Weber, Caroline Goupille

Open access · goldAbstract read
In one paragraph

Article in Biomolecules, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing 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

18 citing papers in PubMed, 32 citations in OpenAlex.

  1. Review
  2. Article
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  4. Review
  5. Review
  6. iPSC-derived cells for whole liver bioengineering.Frontiers in bioengineering and biotechnology · 2024
    Review
  7. Article
  8. Article
  9. Syndecan-4 is a maestro of gastric cancer cell invasion and communication that underscores poor survival.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  10. Article
  11. Review
  12. Review
  13. Review
  14. Review
  15. Article
  16. Aconitine Induces TRPV2-Mediated CaEvidence-based complementary and alternative medicine : eCAM · 2021
    Article
  17. Article
  18. 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

3 authors at 1 institution in 1 country.

Chahrazed HabesINSERM, Université de Tours, UMR 1069 Nutrition, Growth and Cancer, 37032 Tours, France. chahrazed.habes@etu.univ-tours.fr.
Günther WeberINSERM, Université de Tours, UMR 1069 Nutrition, Growth and Cancer, 37032 Tours, France. gunther.weber@univ-tours.fr.ORCID 0000-0002-3861-808X
Caroline GoupilleINSERM, Université de Tours, UMR 1069 Nutrition, Growth and Cancer, 37032 Tours, France. caroline.goupille@univ-tours.fr.
Université de Tours · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Initially characterized by its antimicrobial activities, LL-37 has also been shown to significantly contribute to tumor development. On breast cancer cell lines, LL-37 increases intracellular calcium via the TRPV2 channel and their migration via the activation of PI3K/AKT signaling. Its all-d enantiomer d-LL-37 induces similar effects, which excludes a protein-protein interaction of LL-37 in a classic ligand-receptor manner. Its net charge of +6 gave rise to the hypothesis that the peptide uses the negative charges of sulfoglycans or sialic acids to facilitate its attachment to the cell membrane and to induce its activities. Whereas several vegetal lectins, specifically attaching to sialylated or sulfated structures, blocked the activities of LL-37 on both calcium increase and cell migration, several sialidases had no effect. However, the competitive use of free sulfated glycoaminoglycans (GAGs) as chrondroitin and heparin, or treatment of the cell surface with chondroitinase and heparinase resulted in an activity loss of 50-100% for LL-37. Concordant results were obtained by blocking the synthesis of GAGs with 4-Methylumbelliferyl-β-d-xyloside, and by suppression of glycan sulfatation by sodium chlorate. Using a candidate approach by suppressing proteoglycan synthesis using RNA interference, syndecan-4 was shown to be required for the activities of LL-37 and its binding to the cell surface. This leads to the conclusion that syndecan-4, by means of sulfated GAGs, could act as a receptor for LL-37.

Indexed as

Antimicrobial Cationic PeptidesBreast NeoplasmsCalciumCathelicidinsCell Line, TumorCell MembraneCell MovementFemaleGene Expression Regulation, NeoplasticGlycosaminoglycansHumansMCF-7 CellsSignal TransductionSulfatesSyndecan-4TRPV Cation ChannelsAntimicrobial Cationic PeptidesCalciumCathelicidinsGlycosaminoglycansSDC4 protein, humanSulfatesSyndecan-4TRPV2 protein, humanTRPV Cation Channelsbreast cancercell migrationglycosaminoglycansLL-37syndecan

Identifiers

PMID31547381
PMCPMC6769752
OpenAlexW2972440577

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

Registered trials

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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.