Evidence map›Paper›PMID 30959460›Full record

ArticleRedox biology2019

Enhanced autophagic-lysosomal activity and increased BAG3-mediated selective macroautophagy as adaptive response of neuronal cells to chronic oxidative stress.

Debapriya Chakraborty, Vanessa Felzen, Christof Hiebel, Elisabeth Stürner, Natarajan Perumal, Caroline Manicam, Elisabeth Sehn, Franz Grus, Uwe Wolfrum, Christian Behl

Open access · goldAbstract read
In one paragraph

Article in Redox biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed, 1 pooled it
3.0field-weighted citation impact, top 9% 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

22 citing papers in PubMed, 1 synthesis or guideline pooled it, 38 citations in OpenAlex.

  1. Pooled it
  2. Depletion of BIS in astrocytes aggravates reactive gliosis following photothrombotic brain injury.The Korean journal of physiology & pharmacology : official journal of the Korean Physiological Society and the Korean Society of Pharmacology · 2026
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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

10 authors at 2 institutions in 1 country.

Debapriya ChakrabortyInstitute of Pathobiochemistry, University Medical Center Mainz of the Johannes Gutenberg University, 55099, Mainz, Germany. Electronic address: debapriya222@gmail.com.
Vanessa FelzenInstitute of Pathobiochemistry, University Medical Center Mainz of the Johannes Gutenberg University, 55099, Mainz, Germany. Electronic address: Vanessa.felzen@gmail.com.
Christof HiebelInstitute of Pathobiochemistry, University Medical Center Mainz of the Johannes Gutenberg University, 55099, Mainz, Germany. Electronic address: christof.hiebel@gmail.com.
Elisabeth StürnerInstitute of Pathobiochemistry, University Medical Center Mainz of the Johannes Gutenberg University, 55099, Mainz, Germany. Electronic address: estuerne@uni-mainz.de.
Natarajan PerumalExperimental and Translational Ophthalmology, University Medical Center Mainz, 55131, Mainz, Germany. Electronic address: nperumal@eye-research.org.
Caroline ManicamExperimental and Translational Ophthalmology, University Medical Center Mainz, 55131, Mainz, Germany. Electronic address: caroline.manicam@unimedizin-mainz.de.
Elisabeth SehnInstitute for Molecular Physiology, Johannes Gutenberg University, 55128, Mainz, Germany. Electronic address: sehn@uni-mainz.de.
Franz GrusExperimental and Translational Ophthalmology, University Medical Center Mainz, 55131, Mainz, Germany. Electronic address: fgrus@eye-research.org.
Uwe WolfrumInstitute for Molecular Physiology, Johannes Gutenberg University, 55128, Mainz, Germany. Electronic address: wolfrum@uni-mainz.de.
Christian BehlInstitute of Pathobiochemistry, University Medical Center Mainz of the Johannes Gutenberg University, 55099, Mainz, Germany. Electronic address: cbehl@uni-mainz.de.
Johannes Gutenberg University Mainz · DEUniversity Medical Center of the Johannes Gutenberg University Mainz · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Oxidative stress and a disturbed cellular protein homeostasis (proteostasis) belong to the most important hallmarks of aging and of neurodegenerative disorders. The proteasomal and autophagic-lysosomal degradation pathways are key measures to maintain proteostasis. Here, we report that hippocampal cells selected for full adaptation and resistance to oxidative stress induced by hydrogen peroxide (oxidative stress-resistant cells, OxSR cells) showed a massive increase in the expression of components of the cellular autophagic-lysosomal network and a significantly higher overall autophagic activity. A comparative expression analysis revealed that distinct key regulators of autophagy are upregulated in OxSR cells. The observed adaptive autophagic response was found to be independent of the upstream autophagy regulator mTOR but is accompanied by a significant upregulation of further downstream components of the canonical autophagy network such as Beclin1, WIPI1 and the transmembrane ATG9 proteins. Interestingly, the expression of the HSP70 co-chaperone BAG3, mediator of BAG3-mediated selective macroautophagy and highly relevant for the clearance of aggregated proteins in cells, was found to be increased in OxSR cells that were consequently able to effectively overcome proteotoxic stress. Overexpression of BAG3 in oxidative stress-sensitive HT22 wildtype cells partly established the vesicular phenotype and the enhanced autophagic flux seen in OxSR cells suggesting that BAG3 takes over an important part in the adaptation process. A full proteome analysis demonstrated additional changes in the expression of mitochondrial proteins, metabolic enzymes and different pathway regulators in OxSR cells as consequence of the adaptation to oxidative stress in addition to autophagy-related proteins. Taken together, this analysis revealed a wide variety of pathways and players that act as adaptive response to chronic redox stress in neuronal cells.

Indexed as

Oxidative StressAdaptor Proteins, Signal TransducingApoptosis Regulatory ProteinsAutophagosomesAutophagyCell LineHumansLysosomesMacroautophagyMitochondriaModels, BiologicalNeuronsPhosphorylationProteasome Endopeptidase ComplexTOR Serine-Threonine KinasesAdaptor Proteins, Signal TransducingApoptosis Regulatory ProteinsBAG3 protein, humanMTOR protein, humanProteasome Endopeptidase ComplexTOR Serine-Threonine KinasesAdaptationAutophagyBAG3Oxidative stressProtein homeostasis

Identifiers

PMID30959460
PMCPMC6454062
OpenAlexW2922171655

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.