Evidence map›Paper›PMID 11266442›Full record

ArticleThe Journal of cell biology2001

Essential role of voltage-dependent anion channel in various forms of apoptosis in mammalian cells.

S Shimizu, Y Matsuoka, Y Shinohara, Y Yoneda, Y Tsujimoto

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 118 papers.

0numbers the graph read from it
0cells of the map it votes in
118citing papers in PubMed
11.2field-weighted citation impact, top 1% 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

118 citing papers in PubMed, 363 citations in OpenAlex.

  1. Trial
  2. Amyloid-beta glycation induces neuronal mitochondrial dysfunction and Alzheimer's pathogenesis via VDAC1-dependent mtDNA efflux.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  3. Review
  4. Article
  5. Article
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  13. VDAC2 and the BCL-2 family of proteins.Biochemical Society transactions · 2021
    Review
  14. Article
  15. Article
  16. Regulated cell death in cisplatin-induced AKI: relevance ofAmerican journal of physiology. Renal physiology · 2021
    Article
  17. Mitochondrial outer membrane permeabilization at the single molecule level.Cellular and molecular life sciences : CMLS · 2021
    Review
  18. Article
  19. Review
  20. Review

58 more citing papers are in PubMed but not listed here.

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.

S ShimizuOsaka University Graduate School of Medicine, Biomedical Research Center, Department of Medical Genetics, Osaka 565-0871, Japan.
Y Matsuoka
Y Shinohara
Y Yoneda
Y Tsujimoto
Japan Science and Technology Agency · JPTokushima University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Through direct interaction with the voltage-dependent anion channel (VDAC), proapoptotic members of the Bcl-2 family such as Bax and Bak induce apoptogenic cytochrome c release in isolated mitochondria, whereas BH3-only proteins such as Bid and Bik do not directly target the VDAC to induce cytochrome c release. To investigate the biological significance of the VDAC for apoptosis in mammalian cells, we produced two kinds of anti-VDAC antibodies that inhibited VDAC activity. In isolated mitochondria, these antibodies prevented Bax-induced cytochrome c release and loss of the mitochondrial membrane potential (Deltapsi), but not Bid-induced cytochrome c release. When microinjected into cells, these anti-VDAC antibodies, but not control antibodies, also prevented Bax-induced cytochrome c release and apoptosis, whereas the antibodies did not prevent Bid-induced apoptosis, indicating that the VDAC is essential for Bax-induced, but not Bid-induced, apoptogenic mitochondrial changes and apoptotic cell death. In addition, microinjection of these anti-VDAC antibodies significantly inhibited etoposide-, paclitaxel-, and staurosporine-induced apoptosis. Furthermore, we used these antibodies to show that Bax- and Bak-induced lysis of red blood cells was also mediated by the VDAC on plasma membrane. Taken together, our data provide evidence that the VDAC plays an essential role in apoptogenic cytochrome c release and apoptosis in mammalian cells.

Indexed as

Amino Acid SequenceAnimalsAntibodiesAntibodies, MonoclonalApoptosisApoptosis Regulatory Proteinsbcl-2-Associated X Proteinbcl-2 Homologous Antagonist-Killer ProteinBH3 Interacting Domain Death Agonist ProteinCarrier ProteinsCytochrome c GroupErythrocytesEtoposideHeLa CellsHumansIon ChannelsAntibodiesAntibodies, MonoclonalApoptosis Regulatory ProteinsBAK1 protein, humanBak1 protein, ratBAX protein, humanBax protein, ratbcl-2-Associated X Proteinbcl-2 Homologous Antagonist-Killer ProteinBH3 Interacting Domain Death Agonist ProteinBID protein, humanBid protein, ratBIK protein, humanCarrier ProteinsCytochrome c GroupEtoposideIon ChannelsMembrane ProteinsMitochondrial ProteinsPaclitaxelPorinsProteinsProto-Oncogene ProteinsProto-Oncogene Proteins c-bcl-2Recombinant ProteinsStaurosporineVoltage-Dependent Anion Channels

Identifiers

PMID11266442
PMCPMC2199613
OpenAlexW2040155866

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.