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Treatment of LNCaP cells with novel PRMT5:MEP50 protein:protein interaction inhibitors

ABSTRACT: Treatment of LNCaP cells with novel PRMT5:MEP50 protein:protein interaction inhibitors

PROVIDER: PRJNA851032 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR19753644_1.fastq.gz	Fastqsanger.gz
	SRR19753644_2.fastq.gz	Fastqsanger.gz
	SRR19753645_1.fastq.gz	Fastqsanger.gz
	SRR19753645_2.fastq.gz	Fastqsanger.gz
	SRR19753646_1.fastq.gz	Fastqsanger.gz

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Treatment of LNCaP cells with novel PRMT5:MEP50 protein:protein interaction inhibitors

Project description:We developed a novel compound for inhibition of PRMT5:MEP50 protein:protein interaction. LNCaP prostate cancer cells were treated with Compound 17 for 72 hours. Cells were harvested, RNA isolated, and then submitted for RNA-sequencing,

2025-06-17 | GSE206460 | GEO

shRNA-mediated knockdown of PRMT5 gene in LNCaP cells

Project description:We performed shRNA-mediated knockdown of PRMT5 in LNCaP cells via dox-inducible expression system. We sought to compare transcriptome with- and without PRMT5 knockdown across three biological replicates

2025-06-13 | GSE206111 | GEO

PRMT5 knockdown changes gene expression in prostate cancer cells

Project description:PRMT5 is the major type II protein arginine methyltransferase catalyzing the symmetric dimethylation of arginine. Recent reports have indicated that PRMT5 is overexpressed in multiple cancer types, including prostate. However, the exact contribution of PRMT5 to prostate tumorigenesis is unknown. To explore the functional role of PRMT5 in prostate cancer (PCa), we knocked down PRMT5 by lentiviral shRNAs in both AR-dependent LNCaP cells and AR-independent PC3 cells. Our data suggests that PRMT5 regulates PCa cell biology. To further identify PRMT5-regulated genes in PCa, we performed paired-end RNA-seq analysis in PC3 and LNCaP cells with or without PRMT5-knockdown.

2023-12-25 | GSE117596 | GEO

shRNA-mediated knockdown of PRMT5 gene in LNCaP cells

Project description:shRNA-mediated knockdown of PRMT5 gene in LNCaP cells

| PRJNA849221 | ENA

PRMT5 regulated transcriptome in prostate cancer cells

Project description:Compared to intensely studied DNA methylation, protein methylation is less studied. PRMT5 is the major type II protein arginine methyltransferase catalyzing the symmetric dimethylation of arginine. Recent reports have indicated that PRMT5 is overexpressed in multiple cancer types, including prostate. However, the exact contribution of PRMT5 to prostate tumorigenesis is unknown. To explore PRMT5 in prostate cancer (PCa) therapeutically, we utilized a recently developed selective small molecule PRMT5 inhibitor (PRMT5i, EPZ015666) that has shown in vivo potency in MCL models. To understand the molecular mechanisms of action of PRMT5i in PCa, we performed deep RNA-seq analysis in PC3 and LNCaP cells treated with or without PRMT5i at 4 μM for 4 days in vitro.

2023-12-25 | GSE114151 | GEO

MTA-cooperative PRMT5 inhibitors enhance T cell-mediated antitumor activity in MTAP-loss tumors

Project description:Background: Hyperactivated protein arginine methyltransferases (PRMTs) are implicated in human cancers. Inhibiting tumor intrinsic PRMT5 was reported to potentiate antitumor immune responses, highlighting the possibility of combining PRMT5 inhibitors (PRMT5i) with cancer immunotherapy. However, global suppression of PRMT5 activity impairs the effector functions of immune cells. Here, we sought to identify strategies to specifically inhibit PRMT5 activity in tumor tissues and develop effective PRMT5i-based immuno-oncology (IO) combinations for cancer treatment, particularly for methylthioadenosine phosphorylase (MTAP)-loss cancer. Methods: Isogeneic tumor lines with and without MTAP loss were generated by CRISPR/Cas9 knockout. The effects of two PRMT5 inhibitors (GSK3326595 and MRTX1719) were evaluated in these isogenic tumor lines and T cells in vitro and in vivo. Transcriptomic and proteomic changes in tumors and T cells were characterized in response to PRMT5i treatment. Results: transcriptomic and proteomic profiling analysis reveals that MRTX1719 successfully reduces activation of the PI3K pathway, a well-documented immune-resistant pathway. It highlights the potential of MRTX1719 to overcome immune resistance in MTAP-loss tumors. Conclusion: Collectively, our results provide a strong rationale and mechanistic insights for the clinical development of MRTX1719-based IO combinations in MTAP-loss tumors.

2025-09-05 | GSE276571 | GEO

PROPER-seq (PROtein Protein intERaction sequencing)

Project description:PROPER-seq (PROtein Protein intERaction sequencing)

| PRJNA633786 | ENA

Identification of PRMT5 as a therapeutic target in cholangiocarcinoma [RNA-seq II]

Project description:Cholangiocarcinoma is a very aggressive cancer whose incidence is increasing. Moreover, chemotherapies are little effective and the response to immune checkpoint inhibitors is low. We have identified protein arginine-methyltransferase 5 (PRMT5) as a novel therapeutic target in cholangiocarcinoma. Treatment with PRMT5 inhibitor significantly restrains the growth of experimental cholangiocarcinoma model TAZ/AKT without adverse effects. Our findings support the evaluation of PRMT5 inhibitors in clinical trials.

2025-06-17 | GSE270181 | GEO

The Sm protein methyltransferase PRMT5, is not required for primordial germ cell specification in mice

Project description:PRMT5 is a type II protein arginine methyltransferase with roles in stem cell biology, reprogramming, cancer and neurogenesis. During embryogenesis in the mouse it was hypothesized that PRMT5 functions with the master germline determinant BLIMP1 to promote primordial germ cell (PGC) specification. Using a Blimp1-Cre germline conditional knockout, we discovered that Prmt5 has no major role in murine germline specification, or the first global epigenetic reprogramming event involving depletion of cytosine methylation from DNA and histone H3 lysine 9 dimethylation from chromatin. Instead, we discovered that PRMT5 functions at the conclusion of PGC reprogramming I to promote proliferation, survival and expression of the gonadal germline program as marked by MVH. We show that PRMT5 regulates gene expression by promoting methylation of the Sm spliceosomal proteins, and significantly altering the spliced repertoire of RNAs in mammalian embryonic cells and primordial cells. Examination of transcriptional profile of iPHet (Control) vs. iPKO (Prmt5 knock out) 2i Embryonic Stem Cells

2014-12-05 | E-GEOD-63800 | biostudies-arrayexpress

Small-molecule inhibition of PRMT5 activates p53 in erythropoiesis through perturbation of mRNA processing, transport and protein translation

Project description:The protein arginine methyltransferase PRMT5 catalyzes symmetric di-methylation of numerous proteins involved in epigenetic gene regulation, mRNA splicing and DNA repair. Several small molecule inhibitors of PRMT5 are in clinical trials for acute myeloid leukemia, myelodysplasia, lymphoma and metastatic solid tumors. Here, we report the development of a new potent and specific small molecule inhibitor of PRMT5 (CTX-034) that binds and competes for the arginine substrate binding pocket. CTX-034 suppresses erythroid progenitor growth 30-fold more potently than myeloid progenitor growth through activation of p53. Using a combination of RNA-seq and proteomics, we show that PRMT5 binds and methylates numerous proteins required for protein translation including RNA transport (Heterogeneous Nuclear Ribonucleoprotein A1), initiation of translation (Poly(A) Binding Protein Cytoplasmic 1) and ribosomal assembly (Ribosomal Protein S10). Using an in vivo mouse model of JAK2V617F-driven Polycythemia Vera, CTX-034 suppresses the formation of immature erythroblasts as effectively as the JAK inhibitor Ruxolitinib.

2024-02-01 | GSE145285 | GEO

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