Category Ranking
98%
Total Visits
921
Avg Visit Duration
2 minutes
Citations
20
Article Abstract
The family of protein arginine methyltransferases (PRMTs) occupies an important position in biology, especially during the initiation and development of cancer. PRMT3 and CARM1(also known as PRMT4), being type I protein arginine methyltransferases, are key in controlling tumour progression by catalysing the mono-methylation and asymmetric di-methylation of both histone and non-histone substrates. This paper reviews the functions and potential therapeutic target value of PRMT3 and CARM1 in a variety of cancers. Studies have identified abnormal expressions of PRMT3 and CARM1 in several malignancies, closely linked to cancer progression, advancement, and resistance to treatment. Such as hepatocellular carcinoma, colorectal cancer, ovarian cancer, and endometrial cancer. These findings offer new strategies and directions for cancer treatment, especially in enhancing the effectiveness of conventional treatment methods.
Download full-text PDF |
Source |
|---|---|
| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC11834966 | PMC |
| http://dx.doi.org/10.1111/jcmm.70386 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
PRMT3 and CARM1: Emerging Epigenetic Targets in Cancer.
J Cell Mol Med
February 2025
NHC Key Laboratory of Carcinogenesis and the Key Laboratory of Carcinogenesis and Cancer Invasion of the Chinese Ministry of Education, Cancer Research Institute, School of Basic Medical Science, Central South University, Changsha, China.
The family of protein arginine methyltransferases (PRMTs) occupies an important position in biology, especially during the initiation and development of cancer. PRMT3 and CARM1(also known as PRMT4), being type I protein arginine methyltransferases, are key in controlling tumour progression by catalysing the mono-methylation and asymmetric di-methylation of both histone and non-histone substrates. This paper reviews the functions and potential therapeutic target value of PRMT3 and CARM1 in a variety of cancers.
View Article and Find Full Text PDFThe macromolecular complexes of histones affect protein arginine methyltransferase activities.
J Biol Chem
October 2021
Department of Pharmaceutical and Biomedical Sciences, College of Pharmacy, The University of Georgia, Athens, Georgia, USA. Electronic address:
Histone arginine methylation is a key post-translational modification that mediates epigenetic events that activate or repress gene transcription. Protein arginine methyltransferases (PRMTs) are the driving force for the process of arginine methylation, and the core histone proteins have been shown to be substrates for most PRMT family members. However, previous reports of the enzymatic activities of PRMTs on histones in the context of nucleosomes seem contradictory.
View Article and Find Full Text PDFCisplatin-induced ototoxicity involves interaction of PRMT3 and cannabinoid system.
Arch Toxicol
August 2019
College of Veterinary Medicine (BK21 Plus Project Team), Chonnam National University, Gwangju, 61186, Republic of Korea.
This study investigated whether protein arginine methyltransferase (PRMT) and the cannabinoid system are involved in cisplatin-induced ototoxicity. Cisplatin increased cytosine-cytosine-adenosine-adenosine-thymidine-enhancer-binding protein homologous protein expression. This effect is indicative of an increase in endoplasmic reticulum (ER) stress, and apoptosis signaling including cleavage of caspase-3, caspase-9, poly-adenosine diphosphate-ribose polymerase, and phospho-p53, as well as expression of PRMT3, PRMT4 and fatty acid amide hydrolase (FAAH)1 in House Ear Institute-Organ of Corti 1 (HEI-OC1) cells.
View Article and Find Full Text PDF[Transcription of protein arginine N-methyltransferase genes in mouse dorsal root ganglia following peripheral nerve injury].
Nan Fang Yi Ke Da Xue Xue Bao
December 2017
Department of Anesthesiology, Zhujiang Hospital, Southern Medical University, Guangzhou 510282, China. E-mail:
Objective: To investigate the changes in the transcription of protein arginine methylation enzyme family genes in the dorsal root ganglia (DRG) following peripheral nerve injury in mice.
Methods: C57BL6 mouse models of neuropathic pain induced by peripheral nerve injury were established by bilateral L4 spinal nerve ligation (SNL). At 7 days after SNL or sham operation, the DRG tissue was collected for transcriptional analysis of 9 protein arginine methylation enzyme genes (Prmt1?3, Carm1, and Prmt5?9) using RNA?Seq to identify the differentially expressed genes in the injured DRGs.
Characterization of Protein Methyltransferases Rkm1, Rkm4, Efm4, Efm7, Set5 and Hmt1 Reveals Extensive Post-Translational Modification.
J Mol Biol
January 2018
Systems Biology Initiative, School of Biotechnology and Biomolecular Sciences, University of New South Wales, Sydney, New South Wales 2052, Australia. Electronic address:
Article Synopsis
- Protein methylation is a key post-translational modification in cells, with over 20 methyltransferases identified in yeast, but how these enzymes are regulated is still unclear.
- The study focused on six methyltransferases in yeast, identifying 48 potential post-translational modification sites, 42 of which were previously unknown, that could influence enzyme activity.
- A comparison with human methyltransferase homologs revealed conserved and unique modification sites, and the findings are available in a public proteomics database.