Evidence map›Paper›PMID 30719818›Full record

ArticleCancer science2019

Prothymosin-α enhances phosphatase and tensin homolog expression and binds with tripartite motif-containing protein 21 to regulate Kelch-like ECH-associated protein 1/nuclear factor erythroid 2-related factor 2 signaling in human bladder cancer.

Yuh-Shyan Tsai, Yeong-Chin Jou, Hsin-Tzu Tsai, Ai-Li Shiau, Chao-Liang Wu, Tzong-Shin Tzai

Open access · goldAbstract read
In one paragraph

Article in Cancer science, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed, 1 pooled it
2.4field-weighted citation impact, top 12% 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

15 citing papers in PubMed, 1 synthesis or guideline pooled it, 20 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Review
  4. Review
  5. RNA-seq-based elucidation of lactylation in breast cancer.Archives of medical science : AMS · 2025
    Article
  6. Wogonin inhibits hepatoma cell proliferation by targeting miR-27b-5p/YWHAZ axis.Journal of biochemical and molecular toxicology · 2023
    Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. 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

6 authors at 4 institutions in 1 country.

Yuh-Shyan TsaiDepartment of Urology, National Cheng Kung University Hospital, College of Medicine, National Cheng Kung University, Tainan, Taiwan.ORCID https://orcid.org/0000-0001-7613-3772
Yeong-Chin JouDepartment of Urology, Chia-Yi Christian Hospital, Chia-Yi, Taiwan.
Hsin-Tzu TsaiDepartment of Urology, National Cheng Kung University Hospital, College of Medicine, National Cheng Kung University, Tainan, Taiwan.
Ai-Li ShiauDepartment of Microbiology and Immunology, College of Medicine, National Cheng Kung University, Tainan, Taiwan.
Chao-Liang WuDepartment of Biochemistry and Molecular biology, College of Medicine, National Cheng Kung University, Tainan, Taiwan.
Tzong-Shin TzaiDepartment of Urology, An-Nan Hospital, China Medical University, Tainan, Taiwan.
National Cheng Kung University · TWNational Cheng Kung University Hospital · TWChia-Yi Christian Hospital · TWChina Medical University · TW

Funding

Ministry of Science and Technology MOST 106-2314-B-006-047-MY3
6 · The paper itself

Abstract

Prothymosin-α (PTMA) is a small, acidic protein that is usually transported into the nucleus and involves many cellular and immunological functions. Previous studies demonstrated that aberrant location of PTMA expression exists in human bladder cancer, but the role of PTMA protein expression remains elusive. In this study, we created ectopic nuclear or cytoplasmic PTMA expression in human bladder cancer cells by infecting lentiviruses carrying wild type or deleted nuclear localization signal of the PTMA gene. The in vivo tumorigenesis assay showed PTMA protein with deleted nuclear localization signal promotes J82 xenograft tumor growth in mice and shortens their survival more so than the wild type. Chromatin immunoprecipitation showed that wild-type PTMA protein binds to the PTEN promoter and enhances phosphatase and tensin homolog (PTEN) expression. Through immunoblot proteomics and in vivo ubiquitination studies, PTMA protein can bind with tripartite motif-containing protein 21 (TRIM21) and block its ubiquitination. Also, TRIM21 can downregulate both forms of PTMA protein. In human bladder tumors, loss of nuclear PTMA expression was an unfavorable prognostic indicator for shorter disease-free survival (hazard ratio, 1.54; P = 0.009). Our data support that nuclear PTMA protein serves as a tumor suppressor in bladder cancer through upregulating PTEN and orchestrating TRIM21 for the regulation of Nrf2 signaling.

Indexed as

Signal TransductionAnimalsBiomarkersCell Line, TumorDisease Models, AnimalFemaleGene Expression Regulation, NeoplasticHeterograftsHumansKelch-Like ECH-Associated Protein 1MiceNF-E2-Related Factor 2PrognosisPromoter Regions, GeneticProtein PrecursorsPTEN PhosphohydrolaseBiomarkersKelch-Like ECH-Associated Protein 1NF-E2-Related Factor 2Protein Precursorsprothymosin alphaPTEN PhosphohydrolasePTEN protein, humanRibonucleoproteinsSS-A AntigenThymosinbladder cancernuclear factor erythroid 2-related factor 2 proteinphosphatase and tensin homolog proteinprothymosin-αtripartite motif-containing protein 21 protein

Identifiers

PMID30719818
PMCPMC6447842
OpenAlexW2913486808

What OpenQuestion holds

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LicenceCC BY-NC
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Registered trials

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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.