Evidence map›Paper›PMID 27292568›Full record

ArticleScientific reports2016

The Novel Antitubulin Agent TR-764 Strongly Reduces Tumor Vasculature and Inhibits HIF-1α Activation.

Elena Porcù, Luca Persano, Roberto Ronca, Stefania Mitola, Roberta Bortolozzi, Romeo Romagnoli, Paola Oliva, Giuseppe Basso, Giampietro Viola

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
1.0field-weighted citation impact, top 22% 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

2 citing papers in PubMed, 9 citations in OpenAlex.

  1. Article
  2. 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

9 authors at 3 institutions in 1 country.

Elena PorcùDipartimento di Salute della Donna e del Bambino, Laboratorio di Oncoematologia pediatrica, Università di Padova, 35128 Padova, Italy.
Luca PersanoDipartimento di Salute della Donna e del Bambino, Laboratorio di Oncoematologia pediatrica, Università di Padova, 35128 Padova, Italy.
Roberto RoncaDipartimento di Medicina molecolare e traslazionale Unità di oncologia sperimentale ed immunologia. Università di Brescia, 25123 Brescia, Italy.
Stefania MitolaDipartimento di Medicina molecolare e traslazionale Unità di oncologia sperimentale ed immunologia. Università di Brescia, 25123 Brescia, Italy.
Roberta BortolozziDipartimento di Salute della Donna e del Bambino, Laboratorio di Oncoematologia pediatrica, Università di Padova, 35128 Padova, Italy.
Romeo RomagnoliDipartimento di Scienze Chimiche e Farmaceutiche, Università di Ferrara, 44121 Ferrara, Italy.
Paola OlivaDipartimento di Scienze Chimiche e Farmaceutiche, Università di Ferrara, 44121 Ferrara, Italy.
Giuseppe BassoDipartimento di Salute della Donna e del Bambino, Laboratorio di Oncoematologia pediatrica, Università di Padova, 35128 Padova, Italy.
Giampietro ViolaDipartimento di Salute della Donna e del Bambino, Laboratorio di Oncoematologia pediatrica, Università di Padova, 35128 Padova, Italy.
University of Padua · ITUniversity of Brescia · ITUniversity of Ferrara · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Tubulin binding agents (TBAs) are commonly used in cancer therapy as antimitotics. It has been described that TBAs, like combretastatin A-4 (CA-4), present also antivascular activity and among its derivatives we identified TR-764 as a new inhibitor of tubulin polymerization, based on the 2-(alkoxycarbonyl)-3-(3',4',5'-trimethoxyanilino)benzo[b]thiophene molecular skeleton. The antiangiogenic activity of TR-764 (1-10 nM) was tested in vitro on human umbilical endothelial cells (HUVECs), and in vivo, on the chick embryo chorioallantoic membrane (CAM) and two murine tumor models. TR-764 binding to tubulin triggers cytoskeleton rearrangement without affecting cell cycle and viability. It leads to capillary tube disruption, increased cell permeability, and cell motility reduction. Moreover it disrupts adherens junctions and focal adhesions, through mechanisms involving VE-cadherin/β-catenin and FAK/Src. Importantly, TR-764 is active in hypoxic conditions significantly reducing HIF-1α. In vivo TR-764 (1-100 pmol/egg) remarkably blocks the bFGF proangiogenic activity on CAM and shows a stronger reduction of tumor mass and microvascular density both in murine syngeneic and xenograft tumor models, compared to the lead compound CA-4P. Altogether, our results indicate that TR-764 is a novel TBA with strong potential as both antivascular and antitumor molecule that could improve the common anticancer therapies, by overcoming hypoxia-induced resistance mechanisms.

Indexed as

Actin CytoskeletonAniline CompoundsAnimalsAntigens, CDbeta CateninCadherin 5CadherinsCell AdhesionCell Membrane PermeabilityCell MovementChick EmbryoChickensChorioallantoic MembraneFibroblast Growth FactorsHumansHuman Umbilical Vein Endothelial CellsAniline CompoundsAntigens, CDbeta CateninCadherin 5CadherinsFibroblast Growth FactorsfosbretabulinHypoxia-Inducible Factor 1, alpha SubunitStilbenesThiophenesTR-764Tubulin ModulatorsVascular Endothelial Growth Factor A

Identifiers

PMID27292568
PMCPMC4904223
OpenAlexW2422003189

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.