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PRMT5 knockdown changes gene expression in prostate cancer cells

ABSTRACT: PRMT5 knockdown changes gene expression in prostate cancer cells

PROVIDER: PRJNA482621 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR7586880_1.fastq.gz	Fastqsanger.gz
	SRR7586880_2.fastq.gz	Fastqsanger.gz
	SRR7586890_1.fastq.gz	Fastqsanger.gz
	SRR7586890_2.fastq.gz	Fastqsanger.gz
	SRR7586900_1.fastq.gz	Fastqsanger.gz

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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

Testing gene expression changes in VCaP cells following PRMT5 knockdown

Project description:VCaP cells expressing either NTC shRNA or PRMT5 shRNA 1 or shRNA 2 were treated with 100ng/ml doxycycline for 5 days This experiment is designed to see which genes and pathways are modulated by PRMT5 knockdown in VCaP cells VCaP cells were treated with 100ng/ml doxyxycline for 3 days.

2015-04-15 | E-GEOD-65965 | biostudies-arrayexpress

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

Testing gene expression changes in VCaP cells following PRMT5 knockdown

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RNA deep sequencing to compare genome-wide differences between PRMT5/knockdown and control AML cells

Project description:We report the pro-leukemic activities of PRMT5 in AML partly via modulating the transcription of key genes. The goal of this experiment is to confirm the changes observed in expression of genes targeted by PRMT5 activities. RNA Deep sequencing was employed to validate and reproduce the changes measured by quantitative reverse transcription polymerase chain reaction (qRTâPCR) techniques. Total RNA samples from MV4-11 cell line (FLT3-ITD AML) following PRMT5 knockdown using specific short hairpin RNA (shRNA) was used to compare gene expression pattern between PRMT5/Knockdown and control (control: MV4-11 cells transduced with scramble control).

2016-05-19 | E-GEOD-75215 | biostudies-arrayexpress

Genome-wide analysis of genes regulated by p44/wdr77 and PRMT5 in lung and prostate cancer cells

Project description:Analysis of gene expression in lung and prostate cancer cells expressing non-target (NT), p44/wdr77. or PRMT5 shRNA. Results provide important information on how p44/wdr77 and PRMT5 control cellular proliferation. Total RNA obtained from cells expressing NT, p44/wdr77, or PRMT5 shRNA.

2014-04-14 | E-GEOD-56757 | biostudies-arrayexpress

RNA-seq analysis of 22Rv1 cells with PRMT5, MEP50, pICln knockdown

Project description:PRMT5 is a methyltransferase that catalyzes symmetric dimethylation of arginine residues in histones (H4R3, H3R8, H3R2, and H2AR3) to regulate transcription of target genes. While PRMT5 is generally considered an epigenetic repressor, recent evidence from our lab and others demonstrate that PRMT5 also functions as an epigenetic activator. Although in vitro biochemical studies suggest that the PRMT5 interacting proteins methylosome protein 50 (MEP50) and methylosome subunit pICln enhance PRMT5 enzymatic activity, how these interacting proteins cooperate with PRMT5 to regulate gene transcription in vivo remains to be elucidated. Here we perform RNA-seq analysis of prostate cancer cells 22Rv1 with knockdown of PRMT5, MEP50, and pICln, in order to elucidate how these proteins control transcriptome.

2022-05-05 | GSE154951 | GEO

PRMT5 regulated transcriptome in prostate cancer cells

Project description:PRMT5 regulated transcriptome in prostate cancer cells

| PRJNA464885 | ENA

Genome-wide analysis of genes regulated by p44/wdr77 and PRMT5 in lung and prostate cancer cells

2014-04-14 | GSE56757 | GEO

Chromatin-occupancy profiling of PRMT5 and METTL3 in prostate cancer cells

Project description:Prostate cancer (PCa) is the most frequently diagnosed malignancy in men worldwide. Epigenetic regulation has been recognized as a main mechanism of cancer evolution. PRMT5 is the major type II protein arginine methyltransferase catalyzing the symmetric dimethylation of arginine, and METTL3 is the enzymatic component of the large N6-adenosine-methyltransferase complex in mammalian responsible for N6-methyladenosine (m6A) modification in diverse RNA species. Both genes are found upregulated in PCa. However, their exact functional contribution to prostate tumorigenesis is unknown. As both proteins can regulate transcription via binding to chromatin, we seek to explore their DNA binding profiles in both AR+ LNCaP and AR- PC3 cells via recently developed CUT&Tag technique. Antibodies we used were Active Motif #61001 for PRMT5 and Abcam #195352 for METTL3. Our data suggests that both proteins regulate PCa cell biology, at least partially, through chromatin-binding and subsequent transcriptional regulation. CUT&Tag assay for arginine methyltransferase PRMT5 and N6‐adenosine‐methyltransferase METTL3 in LNCaP and PC3 cells

2024-09-03 | GSE217412 | GEO

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