Evidence map›Paper›PMID 30501030›Full record

ReviewInternational journal of molecular sciences2018

Caspase-8: A Novel Target to Overcome Resistance to Chemotherapy in Glioblastoma.

Giulia Fianco, Claudia Contadini, Alessandra Ferri, Claudia Cirotti, Venturina Stagni, Daniela Barilà

Open access · goldAbstract readReview
In one paragraph

Review in International journal of molecular sciences, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
1.3field-weighted citation impact, top 19% 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

35 citing papers in PubMed, 60 citations in OpenAlex.

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  5. The concealed side of caspases: beyond a killer of cells.Cellular and molecular life sciences : CMLS · 2024
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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

6 authors at 3 institutions in 1 country.

Giulia FiancoDepartment of Biology, University of Rome "Tor Vergata", 00133 Rome, Italy. giulia.fianco@gmail.com.
Claudia ContadiniDepartment of Biology, University of Rome "Tor Vergata", 00133 Rome, Italy. claudiacontadini@gmail.com.
Alessandra FerriDepartment of Biology, University of Rome "Tor Vergata", 00133 Rome, Italy. alessandraferri4@gmail.com.
Claudia CirottiDepartment of Biology, University of Rome "Tor Vergata", 00133 Rome, Italy. claudiacirotti89@gmail.com.
Venturina StagniDepartment of Biology, University of Rome "Tor Vergata", 00133 Rome, Italy. venturina.stagni@gmail.com.
Daniela BarilàDepartment of Biology, University of Rome "Tor Vergata", 00133 Rome, Italy. daniela.barila@uniroma2.it.
University of Rome Tor Vergata · ITFondazione Santa Lucia · ITIstituti di Ricovero e Cura a Carattere Scientifico · IT

Funding

Associazione Italiana per la Ricerca sul Cancro IG2016-n.19069Ministero della Salute RF-2016-02362022Ministero della Salute RF-2016-02363460Ministero dell'Istruzione, dell'Università e della Ricerca MIUR-JPI-HDHL-NUTRICOG-MiTyrAgeMinistero dell'Istruzione, dell'Università e della Ricerca PRIN_2015LZE9944_005
6 · The paper itself

Abstract

Caspase-8 was originally identified as a central player of programmed cell death triggered by death receptor stimulation. In that context, its activity is tightly regulated through several mechanisms, with the best established being the expression of FLICE-like inhibitory protein (FLIP) family proteins and the Src-dependent phosphorylation of Caspase-8 on Tyr380. Loss of apoptotic signaling is a hallmark of cancer and indeed Caspase-8 expression is often lost in tumors. This event may account not only for cancer progression but also for cancer resistance to radiotherapy and chemotherapy. Intriguingly, other tumors, such as glioblastoma, preferentially retain Caspase-8 expression, and high levels of Caspase-8 expression may correlate with a worse prognosis, suggesting that in this context this protease loses its apoptotic activity and gains additional functions. Using different cellular systems, it has been clearly shown that in cancer Caspase-8 can exhibit non-canonical functions, including promotion of cell adhesion, migration, and DNA repair. Intriguingly, in glioblastoma models, Caspase-8 can promote NF-κB-dependent expression of several cytokines, angiogenesis, and in vitro and in vivo tumorigenesis. Overall, these observations suggest that some cancer cells may hijack Caspase-8 function which in turn promote cancer progression and resistance to therapy. Here we aim to highlight the multiple functions of Caspase-8 and to discuss whether the molecular mechanisms that modulate the balance between those functions may be targeted to dismantle the aberrant activity of Caspase-8 and to restore its canonical apoptotic functionality.

Indexed as

AnimalsCaspase 8DNA DamageDrug Resistance, NeoplasmGlioblastomaHumansNF-kappa BSignal TransductionCaspase 8NF-kappa BapoptosisCaspase-8chemotherapy and radiotherapyDNA damageFLIPglioblastomaNF-κBSrc kinasetumor microenvironmenttyrosine phosphorylation

Identifiers

PMID30501030
PMCPMC6320982
OpenAlexW2902353350

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.