Evidence map›Paper›PMID 28783175›Full record

ArticleOncogene2017

Contribution of vascular endothelial growth factor receptor-2 sialylation to the process of angiogenesis.

P Chiodelli, S Rezzola, C Urbinati, F Federici Signori, E Monti, R Ronca, M Presta, M Rusnati

Abstract read
PubMed Publisher
In one paragraph

Article in Oncogene, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
1.3field-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

26 citing papers in PubMed, 48 citations in OpenAlex.

  1. Article
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  7. The role ofActa pharmaceutica Sinica. B · 2024
    Review
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  17. Review
  18. ST6Gal1: Oncogenic signaling pathways and targets.Frontiers in molecular biosciences · 2022
    Review
  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

8 authors at 1 institution in 1 country.

P ChiodelliUnits of Experimental Oncology and Immunology, University of Brescia, Brescia, Italy.
S RezzolaUnits of Experimental Oncology and Immunology, University of Brescia, Brescia, Italy.
C UrbinatiUnits of Experimental Oncology and Immunology, University of Brescia, Brescia, Italy.
F Federici SignoriUnits of Experimental Oncology and Immunology, University of Brescia, Brescia, Italy.
E MontiUnits of Biotechnology, Department of Molecular and Translational Medicine, University of Brescia, Brescia, Italy.
R RoncaUnits of Experimental Oncology and Immunology, University of Brescia, Brescia, Italy.
M PrestaUnits of Experimental Oncology and Immunology, University of Brescia, Brescia, Italy.
M RusnatiUnits of Experimental Oncology and Immunology, University of Brescia, Brescia, Italy.
University of Brescia · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Vascular endothelial growth factor receptor-2 (VEGFR2) is the main pro-angiogenic receptor expressed by endothelial cells (ECs). Using surface plasmon resonance, immunoprecipitation, enzymatic digestion, immunofluorescence and cross-linking experiments with specific sugar-binding lectins, we demonstrated that VEGFR2 bears both α,1-fucose and α(2,6)-linked sialic acid (NeuAc). However, only the latter is required for VEGF binding to VEGFR2 and consequent VEGF-dependent VEGFR2 activation and motogenic response in ECs. Notably, downregulation of β-galactoside α(2,6)-sialyltransferase expression by short hairpin RNA transduction inhibits VEGFR2 α(2,6) sialylation that is paralleled by an increase of β-galactoside α(2,3)-sialyltransferase expression. This results in an ex-novo α(2,3)-NeuAc sialylation of the receptor that functionally replaces the lacking α(2,6)-NeuAc, thus allowing VEGF/VEGFR2 interaction. In keeping with the role of VEGFR2 sialylation in angiogenesis, the α(2,6)-NeuAc-binding lectin Sambucus nigra (SNA) prevents VEGF-dependent VEGFR2 autophosphorylation and EC motility, proliferation and motogenesis. In addition, SNA exerts a VEGF-antagonist activity in tridimensional angiogenesis models in vitro and in the chick-embryo chorioallantoic membrane neovascularization assay and mouse matrigel plug assay in vivo. In conclusion, VEGFR2-associated NeuAc plays an important role in modulating VEGF/VEGFR2 interaction, EC pro-angiogenic activation and neovessel formation. VEGFR2 sialylation may represent a target for the treatment of angiogenesis-dependent diseases.

Indexed as

Protein Processing, Post-TranslationalAnimalsbeta-D-Galactoside alpha 2-6-Sialyltransferasebeta-Galactoside alpha-2,3-SialyltransferaseCell MovementCell ProliferationCells, CulturedChick EmbryoChorioallantoic MembraneDown-RegulationEndothelial CellsFemaleFluorescent Antibody TechniqueGalactosidesHumansHuman Umbilical Vein Endothelial Cellsbeta-D-Galactoside alpha 2-6-Sialyltransferasebeta-galactosidebeta-Galactoside alpha-2,3-SialyltransferaseGalactosidesKDR protein, humanKdr protein, mouseN-Acetylneuraminic AcidPlant LectinsRibosome Inactivating ProteinsRNA, Small InterferingSambucus nigra lectinsSialyltransferasesVascular Endothelial Growth Factor Avascular endothelial growth factor A, mouseVascular Endothelial Growth Factor Receptor-2VEGFA protein, human

Identifiers

PMID28783175
OpenAlexW2742298653

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.