ArticleOncogene2014
Nuclear loss of protein arginine N-methyltransferase 2 in breast carcinoma is associated with tumor grade and overexpression of cyclin D1 protein.
Article in Oncogene, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 36 citations in OpenAlex.
- Protein arginine methyltransferases in cancer: mechanisms, functions, and therapeutic opportunities.Journal of biomedical science · 2026Review
- Chromatin Remodeling Enzyme Cluster Predicts Prognosis and Clinical Benefit of Therapeutic Strategy in Breast Cancer.International journal of molecular sciences · 2023Article
- The Role of Protein Arginine Methyltransferases in DNA Damage Response.International journal of molecular sciences · 2022Review
- Structure, Activity and Function of the PRMT2 Protein Arginine Methyltransferase.Life (Basel, Switzerland) · 2021Review
- Protein arginine methyltransferases: promising targets for cancer therapy.Experimental & molecular medicine · 2021Review
- Transcriptional and Metabolomic Analysis of L-Arginine/Nitric Oxide Pathway in Inflammatory Bowel Disease and Its Association with Local Inflammatory and Angiogenic Response: Preliminary Findings.International journal of molecular sciences · 2020Article
- Protein arginine methyltransferases: insights into the enzyme structure and mechanism at the atomic level.Cellular and molecular life sciences : CMLS · 2019Review
- Protein arginine N-methyltransferase 2 reverses tamoxifen resistance in breast cancer cells through suppression of ER-α36.Oncology reports · 2018Article
- Protein arginine methylation: an emerging regulator of the cell cycle.Cell division · 2018Review
- TGF-β1 induces HMGA1 expression: The role of HMGA1 in thyroid cancer proliferation and invasion.International journal of oncology · 2017Article
- MicroRNA-32 promotes calcification in vascular smooth muscle cells: Implications as a novel marker for coronary artery calcification.PloS one · 2017Article
- Dysregulation of histone methyltransferases in breast cancer - Opportunities for new targeted therapies?Molecular oncology · 2016Review
- Protein arginine methylation/demethylation and cancer.Oncotarget · 2016Review
- The association between S100A13 and HMGA1 in the modulation of thyroid cancer proliferation and invasion.Journal of translational medicine · 2016Article
- Molecular Characterization and Potential Inhibitors Prediction of Protein Arginine Methyltransferase-2 in Carcinoma: An Insight from Molecular Docking, ADMET Profiling and Molecular Dynamics Simulation Studies.Euroasian journal of hepato-gastroenterologyArticle
Corrections and comments
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Authors and funding
15 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Human protein arginine N-methyltransferase 2 (PRMT2, HRMT1L1) is a protein that belongs to the arginine methyltransferase family, and it has diverse roles in transcriptional regulation through different mechanisms depending on its binding partners. In this study, we provide evidences for the negative effect of PRMT2 on breast cancer cell proliferation in vitro and in vivo. Morever, cyclin D1, one of the key modulators of cell cycle, was found to be downregulated by PRMT2, and PRMT2 was further shown to suppress the estrogen receptor α-binding affinity to the activator protein-1 (AP-1) site in cyclin D1 promoter through indirect binding with AP-1 site, resulting in the inhibition of cyclin D1 promoter activity in MCF-7 cells. Furthermore, a positive correlation between the expression of PRMT2 and cyclin D1 was confirmed in the breast cancer tissues by using tissue microarray assay. In addition, PRMT2 was found to show a high absent percentage in breast caner cell nuclei and the nuclear loss ratio of PRMT2 was demonstrated to positively correlate with cyclin D1 expression and the increasing tumor grade of invasive ductal carcinoma. Those results offer an essential insight into the effect of PRMT2 on breast carcinogenesis, and PRMT2 nuclear loss might be an important biological marker for the diagnosis of breast cancer.
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