ArticleThe Journal of biological chemistry2016
Severe Hypomyelination and Developmental Defects Are Caused in Mice Lacking Protein Arginine Methyltransferase 1 (PRMT1) in the Central Nervous System.
Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.
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Who cites it
40 citing papers in PubMed, 69 citations in OpenAlex.
- The protein arginine methyltransferase PRMT1 ameliorates cerebral ischemia-reperfusion injury by suppressing RIPK1-mediated necroptosis and apoptosis.Acta pharmaceutica Sinica. B · 2025Article
- Protein Arginine Methyltransferases from Regulatory Function to Clinical Implication in Central Nervous System.Cellular and molecular neurobiology · 2025Review
- PRMT1 Promotes the Self-renewal of Leukemia Stem Cells by Regulating Protein Synthesis.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Basic Epigenetic Mechanisms.Sub-cellular biochemistry · 2025Review
- Association Analysis ofGenes · 2024Article
- Protein arginine methyltransferase 1 is required for the maintenance of adult small intestinal and colonic epithelial cell homeostasis.International journal of biological sciences · 2024Article
- Critical Roles of Protein Arginine Methylation in the Central Nervous System.Molecular neurobiology · 2023Review
- Functional Implications of Protein Arginine Methyltransferases (PRMTs) in Neurodegenerative Diseases.Biology · 2023Review
- Protein arginine methyltransferase 1 regulates B cell fate after positive selection in the germinal center in mice.The Journal of experimental medicine · 2023Article
- Epigenetic and integrative cross-omics analyses of cerebral white matter hyperintensities on MRI.Brain : a journal of neurology · 2023Article
- Neuroblasts contribute to oligodendrocytes generation upon demyelination in the adult mouse brain.iScience · 2022Article
- PRMT1 is required for the generation of MHC-associated microglia and remyelination in the central nervous system.Life science alliance · 2022Article
- Review
- Regulation of neural stem cell proliferation and survival by protein arginine methyltransferase 1.Frontiers in neuroscience · 2022Article
- PRMT5 Interacting Partners and Substrates in Oligodendrocyte Lineage Cells.Frontiers in cellular neuroscience · 2022Article
- Protein arginine methylation: from enigmatic functions to therapeutic targeting.Nature reviews. Drug discovery · 2021Review
- Arginine methylation of METTL14 promotes RNA NNature communications · 2021Article
- Review
- Protein arginine methyltransferases: promising targets for cancer therapy.Experimental & molecular medicine · 2021Review
- Oligodendroglial Epigenetics, from Lineage Specification to Activity-Dependent Myelination.Life (Basel, Switzerland) · 2021Review
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Protein arginine methyltransferase 1 (PRMT1) is involved in cell proliferation, DNA damage response, and transcriptional regulation. Although PRMT1 is extensively expressed in the CNS at embryonic and perinatal stages, the physiological role of PRMT1 has been poorly understood. Here, to investigate the primary function of PRMT1 in the CNS, we generated CNS-specific PRMT1 knock-out mice by the Cre-loxP system. These mice exhibited postnatal growth retardation with tremors, and most of them died within 2 weeks after birth. Brain histological analyses revealed prominent cell reduction in the white matter tracts of the mutant mice. Furthermore, ultrastructural analysis demonstrated that myelin sheath was almost completely ablated in the CNS of these animals. In agreement with hypomyelination, we also observed that most major myelin proteins including myelin basic protein (MBP), 2',3'-cyclic-nucleotide 3'-phosphodiesterase (CNPase), and myelin-associated glycoprotein (MAG) were dramatically decreased, although neuronal and astrocytic markers were preserved in the brain of CNS-specific PRMT1 knock-out mice. These animals had a reduced number of OLIG2(+) oligodendrocyte lineage cells in the white matter. We found that expressions of transcription factors essential for oligodendrocyte specification and further maturation were significantly suppressed in the brain of the mutant mice. Our findings provide evidence that PRMT1 is required for CNS development, especially for oligodendrocyte maturation processes.
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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.