Evidence map›Paper›PMID 25188516›Full record

ArticleCell death & disease2014

Glucose metabolism is inhibited by caspases upon the induction of apoptosis.

L A Pradelli, E Villa, B Zunino, S Marchetti, J-E Ricci

Open access · goldAbstract read
In one paragraph

Article in Cell death & disease, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.4field-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

18 citing papers in PubMed, 38 citations in OpenAlex.

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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

5 authors at 2 institutions in 1 country.

L A Pradelli1] Inserm, U1065, Centre Méditerranéen de Médecine Moléculaire (C3M), équipe 'contrôle métabolique des morts cellulaires', Nice, France [2] Faculté de Médecine, Université de Nice-Sophia-Antipolis, Nice, France.
E Villa1] Inserm, U1065, Centre Méditerranéen de Médecine Moléculaire (C3M), équipe 'contrôle métabolique des morts cellulaires', Nice, France [2] Faculté de Médecine, Université de Nice-Sophia-Antipolis, Nice, France.
B Zunino1] Inserm, U1065, Centre Méditerranéen de Médecine Moléculaire (C3M), équipe 'contrôle métabolique des morts cellulaires', Nice, France [2] Faculté de Médecine, Université de Nice-Sophia-Antipolis, Nice, France [3] Département d'Anesthésie Réanimation, Centre Hospitalier Universitaire de Nice, Nice, France.
S Marchetti1] Faculté de Médecine, Université de Nice-Sophia-Antipolis, Nice, France [2] Inserm, U1065, Centre Méditerranéen de Médecine Moléculaire (C3M), équipe 'mort cellulaire, différenciation et cancer', Nice, France.
J-E Ricci1] Inserm, U1065, Centre Méditerranéen de Médecine Moléculaire (C3M), équipe 'contrôle métabolique des morts cellulaires', Nice, France [2] Faculté de Médecine, Université de Nice-Sophia-Antipolis, Nice, France [3] Département d'Anesthésie Réanimation, Centre Hospitalier Universitaire de Nice, Nice, France.
Inserm · FRUniversité Côte d'Azur · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Rapidly proliferating cells, such as cancer cells, have adopted aerobic glycolysis rather than oxidative phosphorylation to supply their energy demand; this phenomenon is known as 'the Warburg effect'. It is now widely accepted that during apoptosis the loss of energy production, orchestrated by caspases, contributes to the dismantling of the dying cell. However, how this loss of energy production occurs is still only partially known. In the present work, we established that during apoptosis the level of cellular ATP decreased in a caspase-dependent manner. We demonstrated that this decrease in ATP content was independent of any caspase modification of glucose uptake, ATP consumption or reactive oxygen species production but was dependent on a caspase-dependent inhibition of glycolysis. We found that the activity of the two glycolysis-limiting enzymes, phosphofructokinase and pyruvate kinase, were affected by caspases, whereas the activity of phosphoglycerate kinase was not, suggesting specificity of the effect. Finally, using a metabolomic analysis, we observed that caspases led to a decrease in several key metabolites, including phosphoserine, which is a major regulator of pyruvate kinase muscle isozyme activity. Thus, we have established that during apoptosis, caspases can shut down the main energy production pathway in cancer cells, leading to the impairment in the activity of the two enzymes controlling limiting steps of glycolysis.

Indexed as

Adenosine TriphosphateAmino Acid Chloromethyl KetonesApoptosisCaspase InhibitorsCaspasesDeoxyglucoseGlucoseGlycolysisHeLa CellsHumansPhosphofructokinase-1Pyruvate KinaseQuinolinesReactive Oxygen SpeciesRutamycinStaurosporineAdenosine TriphosphateAmino Acid Chloromethyl KetonesCaspase InhibitorsCaspasesDeoxyglucoseGlucosePhosphofructokinase-1Pyruvate KinaseQuinolinesquinoline-val-asp(OMe)-CH2-OPHReactive Oxygen SpeciesRutamycinStaurosporine

Identifiers

PMID25188516
PMCPMC4540195
OpenAlexW2054851635

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.