Evidence map›Paper›PMID 34440533›Full record

ArticleLife (Basel, Switzerland)2021

Arginine Methyltransferase PRMT1 Regulates p53 Activity in Breast Cancer.

Li-Ming Liu, Qiang Tang, Xin Hu, Jing-Jing Zhao, Yuan Zhang, Guo-Guang Ying, Fei Zhang

Abstract read
In one paragraph

Article in Life (Basel, Switzerland), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing 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

16 citing papers in PubMed.

  1. Article
  2. Review
  3. Review
  4. Review
  5. Article
  6. Review
  7. Review
  8. Role of PRMT1 and PRMT5 in Breast Cancer.International journal of molecular sciences · 2024
    Review
  9. Article
  10. Review
  11. Dysregulation of arginine methylation in tumorigenesis.Frontiers in molecular biosciences · 2024
    Review
  12. Article
  13. Article
  14. [PRMT1 inhibits apoptosis of nasopharyngeal carcinoma cells by promoting RRM2 expression].Nan fang yi ke da xue xue bao = Journal of Southern Medical University · 2022
    Article
  15. Article
  16. 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

7 authors.

Li-Ming LiuTianjin Medical University Cancer Institute and Hospital, Tianjin 300060, China.
Qiang TangTianjin Medical University Cancer Institute and Hospital, Tianjin 300060, China.
Xin HuTianjin Medical University Cancer Institute and Hospital, Tianjin 300060, China.
Jing-Jing ZhaoTianjin Medical University Cancer Institute and Hospital, Tianjin 300060, China.
Yuan ZhangDepartment of International Medical Services, Peking Union Medical College Hospital, Chinese Academy of Medical Sciences, Beijing 100005, China.
Guo-Guang YingTianjin Medical University Cancer Institute and Hospital, Tianjin 300060, China.
Fei ZhangTianjin Medical University Cancer Institute and Hospital, Tianjin 300060, China.ORCID 0000-0001-7434-7339

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The protein p53 is one of the most important tumor suppressors, responding to a variety of stress signals. Mutations in p53 occur in about half of human cancer cases, and dysregulation of the p53 function by epigenetic modifiers and modifications is prevalent in a large proportion of the remainder. PRMT1 is the main enzyme responsible for the generation of asymmetric-dimethylarginine, whose upregulation or aberrant splicing has been observed in many types of malignancies. Here, we demonstrate that p53 function is regulated by PRMT1 in breast cancer cells. PRMT1 knockdown activated the p53 signal pathway and induced cell growth-arrest and senescence. PRMT1 could directly bind to p53 and inhibit the transcriptional activity of p53 in an enzymatically dependent manner, resulting in a decrease in the expression levels of several key downstream targets of the p53 pathway. We were able to detect p53 asymmetric-dimethylarginine signals in breast cancer cells and breast cancer tissues from patients, and the signals could be significantly weakened by silencing of PRMT1 with shRNA, or inhibiting PRMT1 activity with a specific inhibitor. Furthermore, PRMT1 inhibitors significantly impeded cell growth and promoted cellular senescence in breast cancer cells and primary tumor cells. These results indicate an important role of PRMT1 in the regulation of p53 function in breast tumorigenesis.

Indexed as

arginine methylationbreast cancerp53PRMT1

Identifiers

PMID34440533
PMCPMC8400051

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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.