Evidence map›Paper›PMID 35052687›Full record

ArticleBiomedicines2021

ALDH1A3 Segregated Expression and Nucleus-Associated Proteasomal Degradation Are Common Traits of Glioblastoma Stem Cells.

Julian Fauß, Bettina Sprang, Petra Leukel, Clemens Sommer, Teodora Nikolova, Florian Ringel, Ella L Kim

Open access · goldAbstract read
In one paragraph

Article in Biomedicines, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
0.9field-weighted citation impact, top 24% 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

9 citing papers in PubMed, 11 citations in OpenAlex.

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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

7 authors at 2 institutions in 1 country.

Julian FaußLaboratory of Experimental Neurooncology, Department of Neurosurgery, Johannes Gutenberg University Medical Centre, 55131 Mainz, Germany.
Bettina SprangLaboratory of Experimental Neurooncology, Department of Neurosurgery, Johannes Gutenberg University Medical Centre, 55131 Mainz, Germany.
Petra LeukelInstitute of Neuropathology, Johannes Gutenberg University Medical Centre, 55131 Mainz, Germany.
Clemens SommerInstitute of Neuropathology, Johannes Gutenberg University Medical Centre, 55131 Mainz, Germany.
Teodora NikolovaInstitute of Toxicology, Johannes Gutenberg University Medical Centre, 55131 Mainz, Germany.
Florian RingelDepartment of Neurosurgery, Johannes Gutenberg University Medical Centre, 55131 Mainz, Germany.
Ella L KimLaboratory of Experimental Neurooncology, Department of Neurosurgery, Johannes Gutenberg University Medical Centre, 55131 Mainz, Germany.
University Medical Center of the Johannes Gutenberg University Mainz · DEJohannes Gutenberg University Mainz · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Aldehyde dehydrogenase 1 isoforms A1 and A3 have been implicated as functional biomarkers associated with distinct molecular subtypes of glioblastoma and glioblastoma stem cells. However, the exact roles of these isoforms in different types of glioma cells remain unclear. The purpose of this study was to dissect the association of A1 or A3 isoforms with stem and non-stem glioblastoma cells. This study has undertaken a systematic characterization of A1 and A3 proteins in glioblastoma tissues and a panel of glioblastoma stem cells using immunocytochemical and immunofluorescence staining, Western blot and the subcellular fractionation methodology. Our main findings are (i) human GSCs express uniformly ALDH1A3 but not the ALDH1A1 isoform whereas non-stem glioma cells comparably express both isoforms; (ii) there is an abundance of ALDH1A3 peptides that prevail over the full-length form in glioblastoma stem cells but not in non-stem glioma cells; (iii) full-length ALDH1A3 and ALDH1A3 peptides are spatially segregated within the cell; and (vi) the abundance of full-length ALDH1A3 and ALDH1A3 peptides is sensitive to MG132-mediated proteasomal inhibition. Our study further supports the association of ALDH1A3 with glioblastoma stem cells and provide evidence for the regulation of ALDH1A3 activities at the level of protein turnover.

Indexed as

ALDH1glioblastomaglioma stem cellsproteasomal degradationprotein turnover

Identifiers

PMID35052687
PMCPMC8772809
OpenAlexW4200289879

What OpenQuestion holds

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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.