Evidence map›Paper›PMID 30560942›Full record

ArticleScientific reports2018

A peptide mimicking the binding sites of VEGF-A and VEGF-B inhibits VEGFR-1/-2 driven angiogenesis, tumor growth and metastasis.

Maryam Farzaneh Behelgardi, Saber Zahri, Farhad Mashayekhi, Kamran Mansouri, S Mohsen Asghari

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
2.6field-weighted citation impact, top 9% 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

39 citing papers in PubMed, 67 citations in OpenAlex.

  1. Article
  2. Review
  3. Journal of ophthalmic & vision research · 2026
    Article
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  12. Observational
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  20. Structure-Based Design of Peptides Targeting VEGF/VEGFRs.Pharmaceuticals (Basel, Switzerland) · 2023
    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

5 authors at 3 institutions in 1 country.

Maryam Farzaneh BehelgardiDepartment of Biology, Faculty of Science, University of Mohaghegh Ardabili, Ardabil, Iran.
Saber ZahriDepartment of Biology, Faculty of Science, University of Mohaghegh Ardabili, Ardabil, Iran. Zahri@uma.ac.ir.
Farhad MashayekhiDepartment of Biology, Faculty of Sciences, University of Guilan, Rasht, Iran.
Kamran MansouriMedical Biology Research Center, Kermanshah University of Medical Sciences, Kermanshah, Iran.
S Mohsen AsghariDepartment of Biology, Faculty of Sciences, University of Guilan, Rasht, Iran. sm_asghari@guilan.ac.ir.
University of Guilan · IRUniversity of Mohaghegh Ardabili · IRKermanshah University of Medical Sciences · IR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Interfering with interactions of vascular endothelial growth factors (VEGFs) with their receptors (VEGFRs) effectively inhibits angiogenesis and tumor growth. We designed an antagonist peptide of VEGF-A and VEGF-B reproducing two discontinuous receptor binding regions of VEGF-B (loop 1 and loop3) covalently linked together by a receptor binding region of VEGF-A (loop3). The designed peptide (referred to as VGB4) was able to bind to both VEGFR1 and VEGFR2 on the Human Umbilical Vein Endothelial Cells (HUVECs) surface and inhibited VEGF-A driven proliferation, migration and tube formation in HUVECs through suppression of ERK1/2 and AKT phosphorylation. The whole-animal fluorescence imaging demonstrated that fluorescein isothiocyanate (FITC)-VGB4 accumulated in the mammary carcinoma tumors (MCTs). Administration of VGB4 led to the regression of 4T1 murine MCT growth through decreased expression of p-VEGFR1 and p-VEGFR2 and abrogation of ERK1/2 and AKT activation followed by considerable decrease of tumor cell proliferation (Ki67 expression) and angiogenesis (CD31 and CD34 expression), induction of apoptosis (increased p53 expression, TUNEL staining and decreased Bcl2 expression), and suppression of metastasis  (increased E-cadherin and decreased N-cadherin, NF-κB and MMP-9 expression). These findings indicate that VGB4 may be applicable for antiangiogenic and antitumor therapy.

Indexed as

Angiogenesis InhibitorsAnimalsAntineoplastic AgentsBinding SitesBiomimetic MaterialsBreast NeoplasmsCell Line, TumorCell MovementCell ProliferationDrug DesignFemaleHumansHuman Umbilical Vein Endothelial CellsInjections, IntraperitonealMicePeptidesAngiogenesis InhibitorsAntineoplastic AgentsFLT1 protein, humanKDR protein, humanPeptidesVascular Endothelial Growth Factor AVascular Endothelial Growth Factor BVascular Endothelial Growth Factor Receptor-1Vascular Endothelial Growth Factor Receptor-2VEGFA protein, humanVEGFB protein, human

Identifiers

PMID30560942
PMCPMC6298961
OpenAlexW2903831276

What OpenQuestion holds

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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.