Evidence map›Paper›PMID 19627396›Full record

ArticleJournal of cellular and molecular medicine2010

Fibroblast growth factor 2-antagonist activity of a long-pentraxin 3-derived anti-angiogenic pentapeptide.

Daria Leali, Roberta Bianchi, Antonella Bugatti, Stefania Nicoli, Stefania Mitola, Laura Ragona, Simona Tomaselli, Grazia Gallo, Sergio Catello, Vincenzo Rivieccio and 2 more

Open access · greenAbstract read
In one paragraph

Article in Journal of cellular and molecular medicine, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.5field-weighted citation impact, top 18% 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

21 citing papers in PubMed, 45 citations in OpenAlex.

  1. Review
  2. Review
  3. Role of long pentraxin PTX3 in cancer.Clinical and experimental medicine · 2023
    Review
  4. Article
  5. FGF/FGFR signaling in health and disease.Signal transduction and targeted therapy · 2020
    Review
  6. Review
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Anti-angiogenic peptides for cancer therapeutics.Current pharmaceutical biotechnology · 2011
    Review
  17. Article
  18. 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

12 authors at 3 institutions in 1 country.

Daria LealiUnit of General Pathology and Immunology, Department of Biomedical Sciences and Biotechnology, School of Medicine, University of Brescia, Brescia, Italy.
Roberta Bianchi
Antonella Bugatti
Stefania Nicoli
Stefania Mitola
Laura Ragona
Simona Tomaselli
Grazia Gallo
Sergio Catello
Vincenzo Rivieccio
Lucia Zetta
Marco Presta
University of Brescia · ITInstitute for Macromolecular Studies · ITSigma Tau (Italy) · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Fibroblast growth factor-2 (FGF2) plays a major role in angiogenesis. The pattern recognition receptor long-pentraxin 3 (PTX3) inhibits the angiogenic activity of FGF2. To identify novel FGF2-antagonistic peptide(s), four acetylated (Ac) synthetic peptides overlapping the FGF2-binding region PTX3-(97-110) were assessed for their FGF2-binding capacity. Among them, the shortest pentapeptide Ac-ARPCA-NH(2) (PTX3-[100-104]) inhibits the interaction of FGF2 with PTX3 immobilized to a BIAcore sensorchip and suppresses FGF2-dependent proliferation in endothelial cells, without affecting the activity of unrelated mitogens. Also, Ac-ARPCA-NH(2) inhibits angiogenesis triggered by FGF2 or by tumorigenic FGF2-overexpressing murine endothelial cells in chick and zebrafish embryos, respectively. Accordingly, the peptide hampers the binding of FGF2 to Chinese Hamster ovary cells overexpressing the tyrosine-kinase FGF receptor-1 (FGFR1) and to recombinant FGFR1 immobilized to a BIAcore sensorchip without affecting heparin interaction. In all the assays the mutated Ac-ARPSA-NH(2) peptide was ineffective. In keeping with the observation that hydrophobic interactions dominate the interface between FGF2 and the FGF-binding domain of the Ig-like loop D2 of FGFR1, amino acid substitutions in Ac-ARPCA-NH(2) and saturation transfer difference-nuclear magnetic resonance analysis of its mode of interaction with FGF2 implicate the hydrophobic methyl groups of the pentapeptide in FGF2 binding. These results will provide the basis for the design of novel PTX3-derived anti-angiogenic FGF2 antagonists.

Indexed as

Amino Acid SequenceAngiogenesis InhibitorsAnimalsBinding SitesCell ProliferationCell TransplantationChick EmbryoCHO CellsC-Reactive ProteinCricetinaeCricetulusEndothelial CellsFemaleFibroblast Growth Factor 2HumansMagnetic Resonance SpectroscopyAngiogenesis InhibitorsC-Reactive ProteinFibroblast Growth Factor 2OligopeptidesPentraxinsReceptor, Fibroblast Growth Factor, Type 1Serum Amyloid P-Component

Identifiers

PMID19627396
PMCPMC3823002
OpenAlexW2088684743

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.