Evidence map›Paper›PMID 22909049›Full record

ArticleJournal of neurochemistry2012

Over-expression of HSP70 attenuates caspase-dependent and caspase-independent pathways and inhibits neuronal apoptosis.

Boris Sabirzhanov, Bogdan A Stoica, Marie Hanscom, Chun-Shu Piao, Alan I Faden

Open access · greenAbstract read
In one paragraph

Article in Journal of neurochemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 61 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
61citing papers in PubMed, 1 pooled it
6.0field-weighted citation impact, top 3% 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

61 citing papers in PubMed, 1 synthesis or guideline pooled it, 115 citations in OpenAlex.

  1. Biomarkers for the Diagnosis of Cholangiocarcinoma: A Systematic Review.The American journal of tropical medicine and hygiene · 2018
    Pooled it
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1 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 1 institution in 1 country.

Boris SabirzhanovDepartment of Anesthesiology, Shock Trauma & Anesthesiology Research (STAR) Organized Research Center, University of Maryland School of Medicine, Baltimore, MD, USA. bsabirzhanov@anes.umm.edu
Bogdan A Stoica
Marie Hanscom
Chun-Shu Piao
Alan I Faden
University of Maryland, Baltimore · US

Funding

Mechanisms and Modulation of Cell Death in Traumatic Brain InjuryR01NS061839 · NINDS · UNIVERSITY OF MARYLAND BALTIMORE · PI FADEN, ALAN IRA · 2009 to 2012
$1.9M
APOPTOSIS INDUCED BY TRAUMATIC BRAIN INJURYR01NS036537 · NINDS · GEORGETOWN UNIVERSITY · PI FADEN, ALAN IRA · 1998 to 2005
$1.6M
Combination drug treatment to inhibit multiple cell death pathways after TBIRC1HD064758 · NICHD · UNIVERSITY OF MARYLAND BALTIMORE · PI FADEN, ALAN IRA · 2009 to 2010
$971k
NICHD NIH HHS 5 RC1 HD064758-03NICHD NIH HHS RC1 HD064758NINDS NIH HHS R01 NS036537NINDS NIH HHS R01 NS061839NINDS NIH HHS R01 NS061839-04
6 · The paper itself

Abstract

HSP70 is a member of the family of heat-shock proteins that are known to be up-regulated in neurons following injury and/or stress. HSP70 over-expression has been linked to neuroprotection in multiple models, including neurodegenerative disorders. In contrast, less is known about the neuroprotective effects of HSP70 in neuronal apoptosis and with regard to modulation of programmed cell death (PCD) mechanisms in neurons. We examined the effects of HSP70 over-expression by transfection with HSP70-expression plasmids in primary cortical neurons and the SH-SY5Y neuronal cell line using four independent models of apoptosis: etoposide, staurosporine, C2-ceramide, and β-Amyloid. In these apoptotic models, neurons transfected with the HSP70 construct showed significantly reduced induction of nuclear apoptotic markers and/or cell death. Furthermore, we demonstrated that HSP70 binds and potentially inactivates Apoptotic protease-activating factor 1, as well as apoptosis-inducing factor, key molecules involved in development of caspase-dependent and caspase-independent PCD, respectively. Markers of caspase-dependent PCD, including active caspase-3, caspase-9, and cleaved PARP were attenuated in neurons over-expressing HSP70. These data indicate that HSP70 protects against neuronal apoptosis and suggest that these effects reflect, at least in part, to inhibition of both caspase-dependent and caspase-independent PCD pathways.

Indexed as

Amyloid beta-PeptidesAnimalsApoptosisApoptosis Regulatory ProteinsCaspasesCells, CulturedCerebral CortexEmbryo, MammalianEtoposideGene Expression RegulationGreen Fluorescent ProteinsHSP70 Heat-Shock ProteinsHumansImmunoprecipitationNeural InhibitionNeuroblastomaAmyloid beta-Peptidesamyloid beta-protein (25-35)APIP protein, humanApoptosis Regulatory ProteinsCaspasesEtoposideGreen Fluorescent ProteinsHSP70 Heat-Shock ProteinsN-acetylsphingosineParp1 protein, ratPeptide FragmentsPoly (ADP-Ribose) Polymerase-1Poly(ADP-ribose) PolymerasesSphingosineStaurosporine

Identifiers

PMID22909049
PMCPMC3753080
OpenAlexW2009113642

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.