Evidence map›Paper›PMID 23884416›Full record

ArticleThe Journal of biological chemistry2013

MicroRNA-24 suppression of N-deacetylase/N-sulfotransferase-1 (NDST1) reduces endothelial cell responsiveness to vascular endothelial growth factor A (VEGFA).

Zsolt Kasza, Peder Fredlund Fuchs, Christoffer Tamm, Anna S Eriksson, Paul O'Callaghan, Femke Heindryckx, Dorothe Spillmann, Erik Larsson, Sébastien Le Jan, Inger Eriksson and 3 more

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
2.1field-weighted citation impact, top 15% 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

12 citing papers in PubMed, 27 citations in OpenAlex.

  1. miRVim: Three-dimensional miRNA Structure Database.MicroRNA (Shariqah, United Arab Emirates) · 2025
    Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Integrative Analysis IdentifiedFrontiers in neurology · 2019
    Article
  7. Article
  8. Review
  9. miRNA proxy approach reveals hidden functions of glycosylation.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  10. Article
  11. Insights into miRNA regulation of the human glycome.Biochemical and biophysical research communications · 2014
    Article
  12. Mapping posttranscriptional regulation of the human glycome uncovers microRNA defining the glycocode.Proceedings of the National Academy of Sciences of the United States of America · 2014
    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

13 authors at 3 institutions in 1 country.

Zsolt KaszaFrom the Department of Medical Biochemistry and Microbiology, Science for Life Laboratory, Uppsala University, Husargatan 3, P. O. Box 582, SE-751 23 Uppsala.
Peder Fredlund FuchsFrom the Department of Medical Biochemistry and Microbiology, Science for Life Laboratory, Uppsala University, Husargatan 3, P. O. Box 582, SE-751 23 Uppsala.
Christoffer TammFrom the Department of Medical Biochemistry and Microbiology, Science for Life Laboratory, Uppsala University, Husargatan 3, P. O. Box 582, SE-751 23 Uppsala.
Anna S ErikssonFrom the Department of Medical Biochemistry and Microbiology, Science for Life Laboratory, Uppsala University, Husargatan 3, P. O. Box 582, SE-751 23 Uppsala.
Paul O'CallaghanFrom the Department of Medical Biochemistry and Microbiology, Science for Life Laboratory, Uppsala University, Husargatan 3, P. O. Box 582, SE-751 23 Uppsala.
Femke HeindryckxFrom the Department of Medical Biochemistry and Microbiology, Science for Life Laboratory, Uppsala University, Husargatan 3, P. O. Box 582, SE-751 23 Uppsala.
Dorothe SpillmannFrom the Department of Medical Biochemistry and Microbiology, Science for Life Laboratory, Uppsala University, Husargatan 3, P. O. Box 582, SE-751 23 Uppsala.
Erik Larssonthe Department of Medical Biochemistry and Cell Biology, Institute of Biomedicine, Sahlgrenska Academy, University of Gothenburg, SE-405 30 Göteborg, and.
Sébastien Le JanFrom the Department of Medical Biochemistry and Microbiology, Science for Life Laboratory, Uppsala University, Husargatan 3, P. O. Box 582, SE-751 23 Uppsala.
Inger ErikssonFrom the Department of Medical Biochemistry and Microbiology, Science for Life Laboratory, Uppsala University, Husargatan 3, P. O. Box 582, SE-751 23 Uppsala.
Pär GerwinsFrom the Department of Medical Biochemistry and Microbiology, Science for Life Laboratory, Uppsala University, Husargatan 3, P. O. Box 582, SE-751 23 Uppsala,; the Department of Radiology, Uppsala University Hospital, SE-751 85 Uppsala, Sweden.
Lena KjellénFrom the Department of Medical Biochemistry and Microbiology, Science for Life Laboratory, Uppsala University, Husargatan 3, P. O. Box 582, SE-751 23 Uppsala.
Johan KreugerFrom the Department of Medical Biochemistry and Microbiology, Science for Life Laboratory, Uppsala University, Husargatan 3, P. O. Box 582, SE-751 23 Uppsala,. Electronic address: Johan.Kreuger@imbim.uu.se.
Uppsala University · SEScience for Life Laboratory · SEUniversity of Gothenburg · SE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Heparan sulfate (HS) proteoglycans, present at the plasma membrane of vascular endothelial cells, bind to the angiogenic growth factor VEGFA to modulate its signaling through VEGFR2. The interactions between VEGFA and proteoglycan co-receptors require sulfated domains in the HS chains. To date, it is essentially unknown how the formation of sulfated protein-binding domains in HS can be regulated by microRNAs. In the present study, we show that microRNA-24 (miR-24) targets NDST1 to reduce HS sulfation and thereby the binding affinity of HS for VEGFA. Elevated levels of miR-24 also resulted in reduced levels of VEGFR2 and blunted VEGFA signaling. Similarly, suppression of NDST1 using siRNA led to a reduction in VEGFR2 expression. Consequently, not only VEGFA binding, but also VEGFR2 protein expression is dependent on NDST1 function. Furthermore, overexpression of miR-24, or siRNA-mediated reduction of NDST1, reduced endothelial cell chemotaxis in response to VEGFA. These findings establish NDST1 as a target of miR-24 and demonstrate how such NDST1 suppression in endothelial cells results in reduced responsiveness to VEGFA.

Indexed as

ChemotaxisGene Expression Regulation, EnzymologicHeparan SulfateHumansHuman Umbilical Vein Endothelial CellsMicroRNAsSulfotransferasesVascular Endothelial Growth Factor AVascular Endothelial Growth Factor Receptor-2Heparan Sulfateheparitin sulfotransferaseMicroRNAsMIRN24 microRNA, humanSulfotransferasesVascular Endothelial Growth Factor AVascular Endothelial Growth Factor Receptor-2VEGFA protein, humanAngiogenesisBiosynthesisHeparan SulfateMicroRNAmiR-24NDST1Vascular Endothelial Growth Factor (VEGF)

Identifiers

PMID23884416
PMCPMC3764800
OpenAlexW1996376751

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.