Evidence map›Paper›PMID 40259641›Full record

ArticleMolecular oncology2025

Aberrant expression of nuclear prothymosin α contributes to epithelial-mesenchymal transition in lung cancer.

Liyun Chen, Chung-Teng Wang, Jia-Ming Chang, Ai-Li Shiau, Gia-Shing Shieh, Yau-Lin Tseng, Yi-Ting Yen, Tang-Hsiu Huang, Li-Hsin Cheng, Yu-Chih Wu and 3 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Molecular oncology, 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

13 authors.

Liyun ChenDepartment of Biochemistry and Molecular Biology, College of Medicine, National Cheng Kung University, Tainan, Taiwan.
Chung-Teng WangDepartment of Microbiology and Immunology, College of Medicine, National Cheng Kung University, Tainan, Taiwan.
Jia-Ming ChangThoracic Division, Department of Surgery, Ditmanson Medical Foundation Chiayi Christian Hospital, Taiwan.
Ai-Li ShiauDepartment of Microbiology and Immunology, College of Medicine, National Cheng Kung University, Tainan, Taiwan.
Gia-Shing ShiehDepartment of Biochemistry and Molecular Biology, College of Medicine, National Cheng Kung University, Tainan, Taiwan.
Yau-Lin TsengDivision of Thoracic Surgery, Department of Surgery, National Cheng Kung University Hospital, College of Medicine, National Cheng Kung University, Tainan, Taiwan.
Yi-Ting YenDivision of Thoracic Surgery, Department of Surgery, National Cheng Kung University Hospital, College of Medicine, National Cheng Kung University, Tainan, Taiwan.
Tang-Hsiu HuangDivision of Chest Medicine, Department of Internal Medicine, National Cheng Kung University Hospital, College of Medicine, National Cheng Kung University, Tainan, Taiwan.
Li-Hsin ChengCore Laboratory of Organoids Technology, Office of R&D, Taipei Medical University, Taiwan.
Yu-Chih WuSchool of Respiratory Therapy, College of Medicine, Taipei Medical University, Taiwan.
Chao-Liang WuDepartment of Biochemistry and Molecular Biology, College of Medicine, National Cheng Kung University, Tainan, Taiwan.
Bing-Hua SuSchool of Respiratory Therapy, College of Medicine, Taipei Medical University, Taiwan.ORCID 0000-0003-4810-1567
Pensee WuKeele Medical School, Keele University, UK.

Funding

National Science and Technology Council MOST 103-2320-B-006-047-MY3National Science and Technology Council MOST 110-2314-B-038-143-MY3National Science and Technology Council NSTC 113-2314-B-038-130-MY3Taipei Medical University TMU107-AE1-B26Taipei Medical University TMU112-AE1-B37Taipei Medical University TMU113-F-011
6 · The paper itself

Abstract

Elevated expression of prothymosin α (ProT) is frequently observed in cancers, but the underlying molecular mechanism remains poorly understood. Here, we report the clinical relevance of ProT expression and its correlation with lung cancer progression. We have shown that ProT was highly expressed in early-stage lung cancer, exhibiting nuclear localization; on the contrary, a loss of nuclear ProT expression was detected in late-stage tumor specimens. Furthermore, the expression of nuclear ProT impaired lung cancer cell migration, suppressed TGF-β-induced epithelial-to-mesenchymal transition (EMT)-associated transcription factor expression, and inhibited in vivo tumor metastasis. The suppressive effect of ProT was further found to trigger Smad7 acetylation-dependent deregulation of TGF-β signaling. ProT enhanced Smad7 stability by promoting its lysine acetylation, thereby competing with the binding of Smad2 to the SNAI1, TWIST1, and ZEB1 promoters. Eventually, the binding of Smad7 in the presence of ProT resulted in reduced expression of the EMT transcription factors, leading to the inhibition of TGF-β-induced EMT and tumor metastasis. Collectively, this study unravels the role of ProT in lung cancer progression and highlights the potential of nuclear ProT as an indicator for monitoring tumor development.

Indexed as

Cell NucleusEpithelial-Mesenchymal TransitionLung NeoplasmsProtein PrecursorsThymosinAcetylationAnimalsCell Line, TumorCell MovementGene Expression Regulation, NeoplasticHumansMaleMiceSignal TransductionSmad7 ProteinSnail Family Transcription FactorsProtein Precursorsprothymosin alphaSmad7 ProteinSMAD7 protein, humanSnail Family Transcription FactorsThymosinTransforming Growth Factor betaTwist-Related Protein 1Zinc Finger E-box-Binding Homeobox 1epithelial–mesenchymal transitionlung cancerprothymosin αSmad7 acetylationTGF‐β

Identifiers

PMID40259641
PMCPMC12420368

What Socratic holds

Textmetadata
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 Socratic graph.