Evidence map›Paper›PMID 23840868›Full record

ArticlePloS one2013

Caspase-2 short isoform interacts with membrane-associated cytoskeleton proteins to inhibit apoptosis.

Chunhua Han, Ran Zhao, John Kroger, Meihua Qu, Altaf A Wani, Qi-En Wang

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
0.7field-weighted citation impact, top 28% 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

14 citing papers in PubMed, 21 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. The Role of Nonerythroid SpectrinJournal of oncology · 2019
    Review
  10. Review
  11. Article
  12. The nuclear splicing factor RNA binding motif 5 promotes caspase activation in human neuronal cells, and increases after traumatic brain injury in mice.Journal of cerebral blood flow and metabolism : official journal of the International Society of Cerebral Blood Flow and Metabolism · 2015
    Article
  13. Article
  14. Review
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 2 countries.

Chunhua HanDepartment of Radiology, The Ohio State University Wexner Medical Center, Columbus, Ohio, United States of America.
Ran Zhao
John Kroger
Meihua Qu
Altaf A Wani
Qi-En Wang
The Ohio State University Wexner Medical Center · USThe Ohio State University · USWeifang Medical University · CN

Funding

Cross-talking pre-incision events of eukaryotic NERR01ES012991 · NIEHS · OHIO STATE UNIVERSITY · PI WANI, ALTAF A, ZHU, QIANZHENG · 2004 to 2020
$6.2M
DNA DAMAGE RESPONSES FOLLOWING GENOTOXIN EXPOSURER01ES002388 · NIEHS · OHIO STATE UNIVERSITY · PI WANI, ALTAF A · 1985 to 2016
$4.9M
Repair of Genotoxic Damage in ChromatinR01CA093413 · NCI · OHIO STATE UNIVERSITY · PI WANI, ALTAF A · 2002 to 2011
$3.0M
Role of DDB2 in chemotherapeutic agents-induced apoptosis and platinum resistanceR01CA151248 · NCI · OHIO STATE UNIVERSITY · PI WANG, QIEN · 2011 to 2014
$990k
NCI NIH HHS CA093413NCI NIH HHS CA151248NCI NIH HHS R01 CA093413NCI NIH HHS R01 CA151248NIEHS NIH HHS R01 ES002388NIEHS NIH HHS R01 ES012991
6 · The paper itself

Abstract

Caspase-2 (casp-2) is the most conserved caspase across species, and is one of the initiator caspases activated by various stimuli. The casp-2 gene produces several alternative splicing isoforms. It is believed that the long isoform, casp-2L, promotes apoptosis, whereas the short isoform, casp-2S, inhibits apoptosis. The actual effect of casp-2S on apoptosis is still controversial, however, and the underlying mechanism for casp-2S-mediated apoptosis inhibition is unclear. Here, we analyzed the effects of casp-2S on DNA damage induced apoptosis through "gain-of-function" and "loss-of-function" strategies in ovarian cancer cell lines. We clearly demonstrated that the over-expression of casp-2S inhibited, and the knockdown of casp-2S promoted, the cisplatin-induced apoptosis of ovarian cancer cells. To explore the mechanism by which casp-2S mediates apoptosis inhibition, we analyzed the proteins which interact with casp-2S in cells by using immunoprecipitation (IP) and mass spectrometry. We have identified two cytoskeleton proteins, Fodrin and α-Actinin 4, which interact with FLAG-tagged casp-2S in HeLa cells and confirmed this interaction through reciprocal IP. We further demonstrated that casp-2S (i) is responsible for inhibiting DNA damage-induced cytoplasmic Fodrin cleavage independent of cellular p53 status, and (ii) prevents cisplatin-induced membrane blebbing. Taken together, our data suggests that casp-2S affects cellular apoptosis through its interaction with membrane-associated cytoskeletal Fodrin protein.

Indexed as

Antineoplastic AgentsApoptosisCarrier ProteinsCaspase 2Cell Line, TumorCisplatinFemaleGene Expression Regulation, NeoplasticHumansMembrane ProteinsMicrofilament ProteinsOvarian NeoplasmsOvarySpectrinAntineoplastic AgentsCarrier ProteinsCaspase 2CisplatinMembrane ProteinsMicrofilament ProteinsSpectrin

Identifiers

PMID23840868
PMCPMC3698186
OpenAlexW2083207235

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.