Evidence map›Paper›PMID 27602963›Full record

ArticleOncotarget2016

The TAT-RasGAP317-326 anti-cancer peptide can kill in a caspase-, apoptosis-, and necroptosis-independent manner.

Mathieu Heulot, Nadja Chevalier, Julien Puyal, Christiane Margue, Sébastien Michel, Stephanie Kreis, Dagmar Kulms, David Barras, Aimable Nahimana, Christian Widmann

Open access · diamondAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Oncotarget, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
0.9field-weighted citation impact, top 23% 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

11 citing papers in PubMed, 23 citations in OpenAlex.

  1. Article
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  8. TAT-RasGAPProceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  9. Article
  10. Article
  11. The Anticancer Peptide TAT-RasGAPFrontiers in microbiology · 2017
    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

10 authors at 4 institutions in 3 countries.

Mathieu HeulotDepartment of Physiology, University of Lausanne, Lausanne, Switzerland.
Nadja ChevalierDepartment of Physiology, University of Lausanne, Lausanne, Switzerland.
Julien PuyalDepartment of Fundamental Neurosciences, University of Lausanne, Lausanne, Switzerland.
Christiane MargueSignal Transduction Laboratory, Life Sciences Research Unit, University of Luxembourg, Luxembourg, Luxembourg.
Sébastien MichelDepartment of Physiology, University of Lausanne, Lausanne, Switzerland.
Stephanie KreisSignal Transduction Laboratory, Life Sciences Research Unit, University of Luxembourg, Luxembourg, Luxembourg.
Dagmar KulmsExperimental Dermatology, Department of Dermatology, TU-Dresden, Dresden, Germany.
David BarrasBioinformatics Core Facility, Swiss Institute of Bioinformatics, Lausanne, Switzerland.
Aimable NahimanaService and Central Laboratory of Hematology, University Hospital of Lausanne, Lausanne, Switzerland.
Christian WidmannDepartment of Physiology, University of Lausanne, Lausanne, Switzerland.
University of Lausanne · CHUniversity of Luxembourg · LUSIB Swiss Institute of Bioinformatics · CHTU Dresden · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Tumor cell resistance to apoptosis, which is triggered by many anti-tumor therapies, remains a major clinical problem. Therefore, development of more efficient therapies is a priority to improve cancer prognosis. We have previously shown that a cell-permeable peptide derived from the p120 Ras GTPase-activating protein (RasGAP), called TAT-RasGAP317-326, bears anti-malignant activities in vitro and in vivo, such as inhibition of metastatic progression and tumor cell sensitization to cell death induced by various anti-cancer treatments. Recently, we discovered that this RasGAP-derived peptide possesses the ability to directly kill some cancer cells. TAT-RasGAP317-326 can cause cell death in a manner that can be either partially caspase-dependent or fully caspase-independent. Indeed, TAT-RasGAP317-326-induced toxicity was not or only partially prevented when apoptosis was inhibited. Moreover, blocking other forms of cell death, such as necroptosis, parthanatos, pyroptosis and autophagy did not hamper the killing activity of the peptide. The death induced by TAT-RasGAP317-326 can therefore proceed independently from these modes of death. Our finding has potentially interesting clinical relevance because activation of a death pathway that is distinct from apoptosis and necroptosis in tumor cells could lead to the generation of anti-cancer drugs that target pathways not yet considered for cancer treatment.

Indexed as

AnimalsAntineoplastic AgentsApoptosisCaspase InhibitorsCaspasesCell Line, TumorChlorocebus aethiopsDose-Response Relationship, DrugFemaleGTPase-Activating ProteinsHEK293 CellsHumansMaleNecrosisNeoplasmsPeptide FragmentsAntineoplastic AgentsCaspase InhibitorsCaspasesGTPase-Activating ProteinsPeptide FragmentsTAT-RasGAP(317-326)cell-permeable peptidesnon-apoptotic deathRasGAPtumor cell death

Identifiers

PMID27602963
PMCPMC5325447
OpenAlexW2514902107

What OpenQuestion holds

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LicenceCC BY
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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.