Evidence map›Paper›PMID 40624183›Full record

ArticleScientific reports2025

Proteome changes associated with effect of high dose single-fractionation radiation on lung adenocarcinoma cell lines.

Elina Leis, Vijayachitra Modhukur, Helen Lust, Markus Vardja, Merilin Saarma, Ivar Ilves, Margaret Pütsepp, Sergei Kopanchuk, Jana Jaal, Darja Lavogina

Abstract read
In one paragraph

Article in Scientific reports, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact
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

1 citing paper in PubMed.

  1. 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

10 authors.

Elina LeisDepartment of Haematology and Oncology, Institute of Clinical Medicine, University of Tartu, L. Puusepa 8, 50406, Tartu, Estonia. elina.leis@ut.ee.
Vijayachitra ModhukurCelvia CC AS, Tartu, Estonia.
Helen LustDepartment of Haematology and Oncology, Institute of Clinical Medicine, University of Tartu, L. Puusepa 8, 50406, Tartu, Estonia.
Markus VardjaDepartment of Radiotherapy and Oncological Therapy, Tartu University Hospital, Tartu, Estonia.
Merilin SaarmaProteomics Core Facility, Institute of Technology, University of Tartu, Tartu, Estonia.
Ivar IlvesProteomics Core Facility, Institute of Technology, University of Tartu, Tartu, Estonia.
Margaret PütseppInstitute of Chemistry, University of Tartu, Tartu, Estonia.
Sergei KopanchukInstitute of Chemistry, University of Tartu, Tartu, Estonia.
Jana JaalDepartment of Haematology and Oncology, Institute of Clinical Medicine, University of Tartu, L. Puusepa 8, 50406, Tartu, Estonia.
Darja LavoginaDepartment of Haematology and Oncology, Institute of Clinical Medicine, University of Tartu, L. Puusepa 8, 50406, Tartu, Estonia. darja.lavogina@ut.ee.

Funding

Eesti Teadusagentuur PRG1076HORIZON EUROPE European Research Council 101120075Institute of Chemistry, University of Tartu PLTKTARENG21Institute of Clinical Medicine, University of Tartu PMVCMHO
6 · The paper itself

Abstract

Lung cancer is the leading cause of cancer-related mortality globally, with non-small cell lung cancer (NSCLC) representing 85% of cases. Advances in treatment modalities, including stereotactic radiation therapy, have improved outcomes. However, possible synergistic effects of these therapies remain underexplored at the molecular level. This study investigated high-dose radiation-induced proteomic changes in lung adenocarcinoma cell line HCC-44 grown adherently and cell line A549, grown as adherent cells or spheroids. Our hypothesis was that proteins upregulated by 10 Gy irradiation serve as resistance drivers in cancerous cells and can thus represent potential therapeutic targets. The label-free mass spectrometry revealed distinct proteomic responses to 10 Gy irradiation, varying by cell line and culturing conditions. Differentially expressed proteins elevated in the irradiated samples included ephrin type-A receptor 2 (EPHA2) in adherent cells and insulin-like growth factor 2 receptor, tetraspanin 3 as well as cathepsin D (CTSD) in spheroids. The validation of these targets was carried out via Western blot, immunofluorescence, viability assay and spheroid formation assay which demonstrated that irradiation sensitized adherent NSCLC cells to EPHA2 and CTSD inhibitors. These findings underscore the potential of integrating radiation and targeted therapies in NSCLC treatment, and highlight EPHA2 as a promising candidate for future therapeutic strategies.

Indexed as

Adenocarcinoma of LungLung NeoplasmsProteomeA549 CellsCarcinoma, Non-Small-Cell LungCathepsin DCell Line, TumorCell SurvivalDose Fractionation, RadiationGene Expression Regulation, NeoplasticHumansProteomicsReceptor, EphA2Spheroids, CellularCathepsin DProteomeReceptor, EphA23D cell cultureEphrin Type-A receptor 2High dose single-fractionation radiationLung adenocarcinomaProteomics

Identifiers

PMID40624183
PMCPMC12234733

What OpenQuestion holds

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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.