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

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

PROVIDER: PRJNA1125608 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR29462231_1.fastq.gz	Fastqsanger.gz
	SRR29462231_2.fastq.gz	Fastqsanger.gz
	SRR29462232_1.fastq.gz	Fastqsanger.gz
	SRR29462232_2.fastq.gz	Fastqsanger.gz
	SRR29462233_1.fastq.gz	Fastqsanger.gz

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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

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

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. PRMT5-targeting drugs markedly inhibited CCA cells proliferation, synergizing with cisplatin and gemcitabine, and hindered the growth of cholangiocarcinoma organoids. PRMT5 inhibition blunted the expression of oncogenic genes involved in chromatin remodeling and DNA repair, consistently inducing the formation of RNA-loops and promoting DNA damage. Our findings support the evaluation of PRMT5 inhibitors in clinical trials.

2025-06-17 | GSE270017 | GEO

Identification of PRMT5 as a therapeutic target in cholangiocarcinoma

Project description:Identification of PRMT5 as a therapeutic target in cholangiocarcinoma

| PRJNA1125385 | ENA

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

Project description:Identification of PRMT5 as a therapeutic target in cholangiocarcinoma [RNA-seq I]

| PRJNA1124869 | ENA

Identification of PRMT5 as a therapeutic target in cholangiocarcinoma

Project description:This SuperSeries is composed of the SubSeries listed below.

2025-06-17 | GSE270182 | GEO

Validation of protein arginine methyltransferase 5 (PRMT5) as a candidate therapeutic target in the spontaneous canine model of non-Hodgkin lymphoma [array]

Project description:Targeting PRMT5 in canine lymphoma: we characterized expression patterns of PRMT5 in canine lymphomas and correlated these with histological subtypes using tissue microarrays. We characterized expression of PRMT5 in three canine lymphoma-derived cell lines and primary lymph node biopsies. We have demonstrated that inhibition of PRMT5 leads to growth suppression and induction of apoptosis in canine lymphoma cell lines and primary canine lymphoma cells in a time and dose-dependent manner, while selectively decreasing global marks of symmetric dimethylarginine (SDMA) and histone H4 arginine 3 symmetric di-methylation. We performed ATAC-sequencing with pathway enrichment analysis to characterize genome-wide changes in chromatin accessibility after PRMT5 inhibition. We performed gene expression microarrays with pathway analysis to characterize whole transcriptome changes in canine lymphoma cell lines treated with PRMT5 inhibitors. This work validates PRMT5 as a promising therapeutic target for canine lymphoma and supports the continued used of the spontaneously occurring canine lymphoma model for the preclinical development of PRMT5 inhibitors for the treatment of human NHL.

2021-04-20 | GSE155599 | GEO

Validation of protein arginine methyltransferase 5 (PRMT5) as a candidate therapeutic target in the spontaneous canine model of non-Hodgkin lymphoma [ATAC-seq]

2021-04-20 | GSE156084 | GEO

Protein arginine methyltransferase 5 (PRMT5) is an actionable therapeutic target in CDK4/6 inhibitor-resistant ER+/RB-deficient breast cancer [pSer2 Pol II ChIP-seq]

Project description:CDK4/6 inhibitors (CDK4/6i) have improved survival of patients with estrogen receptor-positive (ER+) breast cancer. However, patients treated with CDK4/6i eventually develop drug resistance and progress. RB1 loss-of-function alterations confer resistance to CDK4/6i, but the optimal therapy for these patients is unclear. Through a genome-wide CRISPR screen, we identified protein arginine methyltransferase 5 (PRMT5) as a molecular vulnerability in ER+/RB1-knockout (RBKO) breast cancer cells. Inhibition of PRMT5 blocked the G1-to-S transition in the cell cycle independent of RB, leading to growth arrest in RBKO cells. Proteomics analysis uncovered fused in sarcoma (FUS) as a downstream effector of PRMT5. Inhibition of PRMT5 resulted in dissociation of FUS from RNA polymerase II (Pol II), which led to Ser2 Pol II hyperphosphorylation, intron retention, and subsequent downregulation of proteins involved in DNA synthesis. Furthermore, treatment with the PRMT5 inhibitor pemrametostat and a selective ER degrader fulvestrant synergistically inhibited growth of ER+/RB-deficient cell-derived and patient-derived xenografts. These findings highlight the potential of dual ER and PRMT5 blockade as a novel therapeutic strategy to overcome resistance to CDK4/6i in ER+/RB-deficient breast cancer.

2023-07-11 | GSE236496 | GEO

Targeting LCK utilizing a selective inhibitor as a therapeutic approach in Cholangiocarcinoma

Project description:There is an unmet need to develop novel, effective medical therapies for cholangiocarcinoma (CCA). The Hippo pathway effector, YAP, is oncogenic in cholangiocarcinoma; however, attempts to therapeutically target YAP in vivo have been unsuccessful thus far. Recently, we described a novel role for the Src-family kinase LCK in activating YAP through tyrosine phosphorylation. This led to the hypothesis that LCK may be a viable therapeutic target in cholangiocarcinoma to regulate YAP activity. NTRC 0652-0 is a novel tyrosine kinase inhibitor with specificity for LCK. NTRC 0652-0 demonstrated selectivity for LCK inhibition in vitro and in cholangiocarcinoma cells. NTRC 0652-0 treatment led to decreased tyrosine phosphorylation of YAP, inhibition of its activity and apoptotic cell death in cholangiocarcinoma cell lines, associated with inhibition of MCL1 expression - consider rephrasing this last part to make the sentence read better. The extent of sensitivity of patient-derived organoids to NTRC 0652-0 correlated with basal YAP tyrosine phosphorylation and suppression of YAP co-transcriptional activity following drug treatment. In a patient-derived xenograft CCA model bearing an FGFR2 fusion, daily oral treatment with NTRC 0652-0 produced stable tumor drug levels, acceptable toxicity, and significantly decreased tumor growth. Overall, a novel LCK inhibitor, NTRC 0652-0, inhibited YAP signaling and demonstrated preclinical efficacy in CCA cell-lines, organoids, and patient derived xenograft models.

2025-05-06 | PXD026925 | Pride

Protein Arginine Methyltransferase 5 (PRMT5) has prognostic relevance and is a druggable target in Multiple Myeloma

Project description:Arginine methyltransferases critically regulate cellular homeostasis by modulating the functional outcome of their substrates. The protein arginine methyltransferase 5 (PRMT5) is an enzyme involved in growth and survival pathways promoting tumorigenesis. However, little is known about the biologic function of PRMT5 and its therapeutic potential in multiple myeloma (MM). In the present study, we identified and validated PRMT5 as a new therapeutic target in MM. PRMT5 is overexpressed in patient MM cells and associated with decreased progression free survival and overall survival. Either genetic knockdown or pharmacological inhibition of PRMT5 with the inhibitor EPZ015666 significantly inhibited growth of both cell lines and patient MM cells. Furthermore, PRMT5 inhibition abrogated NF-kB signaling. Interestingly, mass spectrometry identified a tripartite motif-containing protein 21 TRIM-21 as a new PRMT5-partner, and we delineated a TRIM21-dependent mechanism of NF-kB inhibition. Importantly, oral administration of EPZ015666 significantly decreased MM growth in a humanized murine model of MM. These data both demonstrate the oncogenic role and prognostic relevance of PRMT5 in MM pathogenesis, and provide the rationale for novel therapies targeting PRMT5 to improve patient outcome.

2017-09-19 | GSE103966 | GEO

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