Protein Arginine Methyltransferase 1-mediated Histone H4R3 Dimethyl Asymmetric enhances Epidermal Growth Factor Receptor signaling to promote Peritoneal Fibrosis
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View abstract on PubMed
Summary
This summary is machine-generated.Protein arginine methyltransferase 1 (PRMT1) is elevated in peritoneal fibrosis (PF) patients. Inhibiting PRMT1 reduces fibrosis and epithelial-to-mesenchymal transition, suggesting PRMT1 as a potential therapeutic target for PF.
Area Of Science
- Nephrology
- Molecular Biology
- Pathology
Background
- Peritoneal fibrosis (PF) is a serious complication of peritoneal dialysis (PD) with limited treatment options.
- Protein arginine methyltransferase 1 (PRMT1) is implicated in various diseases, but its role in PF is unclear.
Purpose Of The Study
- To investigate the role of PRMT1 in the pathogenesis of peritoneal fibrosis.
- To explore PRMT1 as a potential therapeutic target for PF.
Main Methods
- Analysis of PRMT1 expression in human PD patients and murine models.
- Genetic and pharmacological inhibition of PRMT1 in cellular and animal models.
- RNA sequencing to identify PRMT1 targets and downstream pathways.
Main Results
- PRMT1 is highly expressed in PD patients and correlates with fibrosis markers.
- PRMT1 inhibition reduces extracellular matrix deposition and alleviates PF in mice.
- PRMT1 inhibition mitigates TGF-β1-induced epithelial-to-mesenchymal transition (EMT) in vitro.
- EGFR was identified as a PRMT1 target, with PRMT1 inhibition deactivating EGFR signaling.
Conclusions
- PRMT1 plays a critical role in PF development by activating EGFR signaling.
- Targeting PRMT1 offers a promising therapeutic strategy for peritoneal fibrosis.
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