Evidence map›Paper›PMID 25771395›Full record

ArticleNeurobiology of aging2015

Heat shock protein defenses in the neocortex and allocortex of the telencephalon.

Jessica M Posimo, Justin N Weilnau, Amanda M Gleixner, Matthew T Broeren, Nicole L Weiland, Jeffrey L Brodsky, Peter Wipf, Rehana K Leak

Open access · greenAbstract read
In one paragraph

Article in Neurobiology of aging, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
0.9field-weighted citation impact, top 26% 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

11 citing papers in PubMed, 13 citations in OpenAlex.

  1. Article
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  4. Article
  5. Heat Shock Protein 70 as a Sex-Skewed Regulator of α-Synucleinopathy.Neurotherapeutics : the journal of the American Society for Experimental NeuroTherapeutics · 2021
    Article
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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

8 authors at 2 institutions in 1 country.

Jessica M PosimoDivision of Pharmaceutical Sciences, Duquesne University, Pittsburgh, PA, USA.
Justin N WeilnauDivision of Pharmaceutical Sciences, Duquesne University, Pittsburgh, PA, USA.
Amanda M GleixnerDivision of Pharmaceutical Sciences, Duquesne University, Pittsburgh, PA, USA.
Matthew T BroerenDivision of Pharmaceutical Sciences, Duquesne University, Pittsburgh, PA, USA.
Nicole L WeilandDivision of Pharmaceutical Sciences, Duquesne University, Pittsburgh, PA, USA.
Jeffrey L BrodskyDepartment of Biological Sciences, University of Pittsburgh, Pittsburgh, PA, USA.
Peter WipfDepartment of Chemistry, University of Pittsburgh, Pittsburgh, PA, USA; Department of Pharmaceutical Sciences, University of Pittsburgh, Pittsburgh, PA, USA.
Rehana K LeakDivision of Pharmaceutical Sciences, Duquesne University, Pittsburgh, PA, USA. Electronic address: leakr@duq.edu.
Duquesne University · USUniversity of Pittsburgh · US

Funding

University of Pittsburgh Center for Chemical DiversityP50GM067082 · NIGMS · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI WIPF, PETER · 2002 to 2012
$18.6M
Single Nephron and MetabolomicsP30DK079307 · NIDDK · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI KLEYMAN, THOMAS R · 2008 to 2022
$13.4M
NIDDK NIH HHS DK79307NIDDK NIH HHS P30 DK079307NIGMS NIH HHS GM067082NIGMS NIH HHS P50 GM067082
6 · The paper itself

Abstract

The telencephalic allocortex develops protein inclusions before the neocortex in many age-related proteinopathies. One major defense mechanism against proteinopathic stress is the heat shock protein (Hsp) network. We therefore contrasted Hsp defenses in stressed primary neocortical and allocortical cells. Neocortical neurons were more resistant to the proteasome inhibitor MG132 than neurons from 3 allocortical subregions: entorhinal cortex, piriform cortex, and hippocampus. However, allocortical neurons exhibited higher MG132-induced increases in Hsp70 and heat shock cognate 70 (Hsc70). MG132-treated allocortical neurons also exhibited greater levels of protein ubiquitination. Inhibition of Hsp70/Hsc70 activity synergistically exacerbated MG132 toxicity in allocortical neurons more than neocortical neurons, suggesting that the allocortex is more reliant on these Hsp defenses. In contrast, astrocytes harvested from the neocortex or allocortex did not differ in their response to Hsp70/Hsc70 inhibition. Consistent with the idea that chaperones are maximally engaged in allocortical neurons, an increase in Hsp70/Hsc70 activity was protective only in neocortical neurons. Finally, the levels of select Hsps were altered in the neocortex and allocortex in vivo with aging.

Indexed as

TelencephalonAgingAnimalsCells, CulturedCerebral CortexFemaleHSC70 Heat-Shock ProteinsHSP70 Heat-Shock ProteinsLeupeptinsMolecular ChaperonesNeocortexNeuronsProteasome InhibitorsRats, Sprague-DawleyUbiquitinationbenzyloxycarbonylleucyl-leucyl-leucine aldehydeHSC70 Heat-Shock ProteinsHSP70 Heat-Shock ProteinsLeupeptinsMolecular ChaperonesProteasome InhibitorsAlzheimer's diseaseArchicortexBraakEntorhinal cortexHeme oxygenase-1HippocampusHsp70PaleocortexParkinson's diseasePiriform cortex

Identifiers

PMID25771395
PMCPMC4417007
OpenAlexW1973625428

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.