Evidence map›Paper›PMID 24269611›Full record

ArticleNeuroscience2014

The role of DAPK-BimEL pathway in neuronal death induced by oxygen-glucose deprivation.

C He, A R Stroink, C X Wang

Abstract read
In one paragraph

Article in Neuroscience, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.1field-weighted citation impact, top 25% 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

13 citing papers in PubMed, 19 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Pegylated IFN-α suppresses hepatitis C virus by promoting the DAPK-mTOR pathway.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  12. Article
  13. 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

3 authors at 2 institutions in 1 country.

C HeSchool of Biological Sciences, Illinois State University, Normal, IL 61790, USA; Central Illinois Neuroscience Foundation, Bloomington, IL 61701, USA.
A R StroinkCentral Illinois Neuroscience Foundation, Bloomington, IL 61701, USA.
C X WangSchool of Biological Sciences, Illinois State University, Normal, IL 61790, USA; Central Illinois Neuroscience Foundation, Bloomington, IL 61701, USA. Electronic address: cwang3@ilstu.edu.
Central Illinois Neuroscience Foundation · USIllinois State University · US

Funding

MMPs contribute to hyperthermia-enhanced vascular injuryR15NS072858 · NINDS · ILLINOIS STATE UNIVERSITY · PI WANG, CHEN XU · 2011 to 2011
$432k
NINDS NIH HHS R15 NS072858NINDS NIH HHS R15NS072858
6 · The paper itself

Abstract

Death-associated protein kinase (DAPK) has been found promoting cell death under stress conditions, including cell death during brain ischemia. However, little is known about the mechanisms how DAPK is involved in the neuronal death-promoting process during ischemia. The present study was to examine the DAPK signal transduction pathways using an ischemia mimicking model, oxygen glucose deprivation (OGD). OGD was induced by incubating SH-SY5Y neuroblastoma cells in glucose-free culture medium flushed with a mixture of N₂ and CO₂. DAPK expression was inhibited by transfection of SH-SY5Y cells with DAPK short hairpin RNA (shRNA). Cell death induced by OGD exposure was assessed by Annexin V-FITC and propidium iodide (PI) assay. Protein expressions were examined by Western blot and protein interactions were detected with immunoprecipitation followed by Western blot. OGD treatment resulted in neuronal death and led to DAPK activation as demonstrated by increase of DAPK (active form) and decrease of phospho-DAPK (inactive form). The activation of DAPK in turn led to BimEL up-regulation and endoplasmic reticulum (ER) stress activation. Further analyses showed that DAPK mediated BimEL expression through extracellular signal-regulated protein kinase1/2 (ERK1/2) inactivation and c-Jun-N-terminal kinase1/2 (JNK1/2) activation. These findings revealed novel signal transduction pathways leading to neuronal death in response to OGD.

Indexed as

Apoptosis Regulatory ProteinsBcl-2-Like Protein 11Cell DeathCell Line, TumorDeath-Associated Protein KinasesEndoplasmic Reticulum StressGlucoseHumansHypoxiaMAP Kinase Signaling SystemMembrane ProteinsMitogen-Activated Protein Kinase 8Mitogen-Activated Protein Kinase 9NeuronsProto-Oncogene ProteinsSignal TransductionApoptosis Regulatory ProteinsBCL2L11 protein, humanBcl-2-Like Protein 11Death-Associated Protein KinasesGlucoseMembrane ProteinsMitogen-Activated Protein Kinase 8Mitogen-Activated Protein Kinase 9Proto-Oncogene ProteinsC/EBP homologous proteinCHOPc-Jun-N-terminal kinase1/2DAPKdeath-associated protein kinaseDMEMDulbecco’s modified Eagle’s mediumEDTAendoplasmic reticulumERERK1/2ethylenediaminetetraacetic acidextracellular signal-regulated protein kinase1/2FBSfetal bovine serumimmunoprecipitationIPischemiaJNK1/2MAPKMitogen-activated protein kinaseneuronal deathOGDoxygen glucose deprivationPBSPERKPhosphate-buffered salinePIPKDpropidium iodideprotein kinase Dprotein kinase RNA (PKR)-like ER kinaseshort hairpin RNAshRNAultravioletunfolded protein responseUPRUV

Identifiers

PMID24269611
PMCPMC3947223
OpenAlexW1980658087

What OpenQuestion holds

Textmetadata
LicenceTDM
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.