Evidence map›Paper›PMID 29643993›Full record

ArticleOncotarget2018

Relationship between the agonist activity of synthetic ligands of TRAIL-R2 and their cell surface binding modes.

Neila Chekkat, Caterina M Lombardo, Cendrine Seguin, Marie-Charlotte Lechner, Florent Dufour, Yves Nominé, Marcella De Giorgi, Benoit Frisch, Olivier Micheau, Gilles Guichard and 2 more

Open access · diamondAbstract read
In one paragraph

Article in Oncotarget, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.6field-weighted citation impact, top 35% 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

5 citing papers in PubMed, 11 citations in OpenAlex.

  1. Combination of multivalent DR5 receptor clustering agonists and histone deacetylase inhibitors for treatment of colon cancer.Journal of controlled release : official journal of the Controlled Release Society · 2024
    Article
  2. Review
  3. Amphiphilic Poly(Pharmaceutics · 2021
    Article
  4. Article
  5. 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 7 institutions in 1 country.

Neila ChekkatLaboratoire de Conception et Application de Molécules Bioactives, UMR 7199 CNRS, Université de Strasbourg, 67401 Illkirch, France.
Caterina M LombardoUniversité de Bordeaux, CBMN, UMR 5248, Institut Européen de Chimie et Biologie, 33607 Pessac, France.
Cendrine SeguinLaboratoire de Conception et Application de Molécules Bioactives, UMR 7199 CNRS, Université de Strasbourg, 67401 Illkirch, France.
Marie-Charlotte LechnerUniversité de Bordeaux, CBMN, UMR 5248, Institut Européen de Chimie et Biologie, 33607 Pessac, France.
Florent DufourCentre de Recherche Lipide, Nutrition et Cancer, UMR1231 Inserm, Université de Bourgogne Franche-Comté, UFR des Sciences de Santé, F21000 Dijon, France.
Yves NominéEquipe labellisée Ligue 2015, UMR 7242, Université de Strasbourg, CNRS, ESBS, 67412 Illkirch, France.
Marcella De GiorgiLaboratoire de Conception et Application de Molécules Bioactives, UMR 7199 CNRS, Université de Strasbourg, 67401 Illkirch, France.
Benoit FrischLaboratoire de Conception et Application de Molécules Bioactives, UMR 7199 CNRS, Université de Strasbourg, 67401 Illkirch, France.
Olivier MicheauCentre de Recherche Lipide, Nutrition et Cancer, UMR1231 Inserm, Université de Bourgogne Franche-Comté, UFR des Sciences de Santé, F21000 Dijon, France.
Gilles GuichardUniversité de Bordeaux, CBMN, UMR 5248, Institut Européen de Chimie et Biologie, 33607 Pessac, France.
Danièle AltschuhEquipe labellisée Ligue 2015, UMR 7242, Université de Strasbourg, CNRS, ESBS, 67412 Illkirch, France.
Sylvie FournelLaboratoire de Conception et Application de Molécules Bioactives, UMR 7199 CNRS, Université de Strasbourg, 67401 Illkirch, France.
Laboratoire de Chémo-biologie synthétique et thérapeutique · FRChimie et Biologie des Membranes et des Nanoobjects · FRInserm · FRUniversité de Strasbourg · FRCentre National de la Recherche Scientifique · FRInstitut de génétique et de biologie moléculaire et cellulaire · FRInstitut Européen de Chimie et Biologie · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Tumor Necrosis Factor Receptor Apoptosis Inducing Ligand (TRAIL) appears as an interesting candidate for targeted cancer therapy as it induces apoptosis in cancer cells without toxicity to normal cells. TRAIL elicits apoptosis through agonist death receptor TRAIL-R1 and TRAIL-R2 engagement. Nevertheless, recombinant soluble TRAIL and monoclonal antibodies against these receptors demonstrated insufficient efficacy in clinical trials. This may be explained by the cell-type dependency of the apoptotic response, itself influenced by the effect on ligand binding mode of factors such as the level of receptor oligomerization or glycosylation. To investigate the relation between binding mode and signaling, we used previously described synthetic divalent and monovalent peptides specific for TRAIL-R2. We measured their pro-apoptotic activity on three cancer cell lines sensitive to rhTRAIL induced-apoptosis and monitored their cell-surface binding kinetics. The two divalent peptides bound with strong affinity to TRAIL-R2 expressed on B lymphoma BJAB cells and induced a high degree of apoptosis. By contrast, the same peptides bound weakly to TRAIL-R2 expressed at the surface of the human colon cancer HCT116 or T lymphoma Jurkat cell lines and did not induce their apoptosis. Cross-linking experiments suggest that these differences could be afforded by variations in the TRAIL-R2 oligomerization state at cell surface before ligand addition. Moreover divalent peptides showed a different efficiency in BJAB apoptosis induction, and kinetic distribution analysis of the BJAB binding curves suggested subtle differences in binding mechanisms. Thus our data support a relation between the cell-surface binding mode of the peptides and their pro-apoptotic activity. In this case the precise characterization of ligand binding to the surface of living cells would be predictive of the therapeutic potential of TRAIL-R2 synthetic ligands prior to clinical trials.

Indexed as

agonist peptidesbinding modesinteractionssignalingTRAIL-R2

Identifiers

PMID29643993
PMCPMC5884648
OpenAlexW2789757575

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.