Evidence map›Paper›PMID 15153933›Full record

ArticleEMBO reports2004

Processed caspase-2 can induce mitochondria-mediated apoptosis independently of its enzymatic activity.

John D Robertson, Vladimir Gogvadze, Andrey Kropotov, Helin Vakifahmetoglu, Boris Zhivotovsky, Sten Orrenius

Open access · greenAbstract read
In one paragraph

Article in EMBO reports, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
7.7field-weighted citation impact, top 2% 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

34 citing papers in PubMed, 122 citations in OpenAlex.

  1. Article
  2. Caspase-2 Substrates: To Apoptosis, Cell Cycle Control, and Beyond.Frontiers in cell and developmental biology · 2020
    Review
  3. Article
  4. Review
  5. Article
  6. The PIDDosome, DNA-damage-induced apoptosis and beyond.Cell death and differentiation · 2012
    Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. The enigma of caspase-2: the laymen's view.Cell death and differentiation · 2009
    Review
  18. The PIDDosome mediates delayed death of hippocampal CA1 neurons after transient global cerebral ischemia in rats.Proceedings of the National Academy of Sciences of the United States of America · 2008
    Article
  19. Death receptors and caspases but not mitochondria are activated in the GDNF- or BDNF-deprived dopaminergic neurons.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2008
    Article
  20. 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

6 authors at 1 institution in 1 country.

John D RobertsonDivision of Toxicology, Institute of Environmental Medicine, Karolinska Institutet, 171 77 Stockholm, Sweden.
Vladimir Gogvadze
Andrey Kropotov
Helin Vakifahmetoglu
Boris Zhivotovsky
Sten Orrenius
Karolinska Institutet · SE

Funding

MITOCHONDRIAL COMMUNICATION IN CHEMICAL APOPTOSISF32CA083273 · NCI · KAROLINSKA INSTITUTE · PI ROBERTSON, JOHN D · 2000 to 2003
$114k
NCI NIH HHS 5 F32 CA83273NCI NIH HHS F32 CA083273
6 · The paper itself

Abstract

The mechanism by which caspase-2 executes apoptosis remains obscure. Recent findings indicate that caspase-2 is activated early in response to DNA-damaging antineoplastic agents and may be important for the engagement of the mitochondrial apoptotic pathway. We demonstrate here that fully processed caspase-2 stimulates mitochondrial release of cytochrome c and Smac/DIABLO, but not apoptosis-inducing factor (AIF). This event occurs independently of several Bcl-2 family proteins, including Bax, Bak and Bcl-2, and inactivation experiments reveal that the proteolytic activity of caspase-2 is not required for the effect. Further, functional studies of mitochondria indicate that processed caspase-2 stimulates state 4 respiration and decreases the respiratory control ratio as a result of, in large part, an uncoupling effect. Combined, our data suggest that caspase-2 retains a unique ability to engage directly the mitochondrial apoptotic pathway, an effect that requires processing of the zymogen but not the associated catalytic activity.

Indexed as

ApoptosisApoptosis Inducing FactorApoptosis Regulatory Proteinsbcl-2-Associated X Proteinbcl-2 Homologous Antagonist-Killer ProteinCarrier ProteinsCaspase 2CaspasesCytochromes cEnzyme ActivationFlavoproteinsHumansIntracellular Signaling Peptides and ProteinsJurkat CellsMembrane ProteinsMitochondriaAIFM1 protein, humanApoptosis Inducing FactorApoptosis Regulatory ProteinsBAK1 protein, humanBAX protein, humanbcl-2-Associated X Proteinbcl-2 Homologous Antagonist-Killer ProteinCarrier ProteinsCaspase 2CaspasesCytochromes cDIABLO protein, humanFlavoproteinsIntracellular Signaling Peptides and ProteinsMembrane ProteinsMitochondrial ProteinsProto-Oncogene Proteins c-bcl-2

Identifiers

PMID15153933
PMCPMC1299073
OpenAlexW2002555521

What OpenQuestion holds

Textmetadata
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.