Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

RNA-seq of RPE cells that harbor a C-terminal GFP-tag on the splicing factor PRPF8 and the retinitis pigmentosa mutation Y2334N

ABSTRACT: RNA-seq of RPE cells that harbor a C-terminal GFP-tag on the splicing factor PRPF8 and the retinitis pigmentosa mutation Y2334N

PROVIDER: PRJNA882471 | ENA |

REPOSITORIES: ENA

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	SRR21642949.fastq.gz	Fastqsanger.gz
	SRR21642950.fastq.gz	Fastqsanger.gz
	SRR21642951.fastq.gz	Fastqsanger.gz
	SRR21642952.fastq.gz	Fastqsanger.gz

Items per page:

1 - 4 of 4

Similar Datasets

Mutant PRPF8 causes widespread splicing changes in spliceosome components in retinitis pigmentosa patient RPE cells

Project description:Retinitis pigmentosa is a rare, progressive disease which affects photoreceptors and retinal pigment epithelial (RPE) cells with blindness as a final outcome. Despite high medical and social impact, there is currently no therapeutic options to slow down the progression or cure the disease. The development of effective therapies was largely hindered by high genetic heterogeneity, inaccessible disease tissue and unfaithful model organisms. The fact that components of ubiquitously expressed splicing factors lead to the retina-specific disease is an additional intriguing question. Herein, we sought to correlate the retinal cell type-specific disease phenotype with the splicing profile shown by a patient with autosomal recessive RP, caused by a mutation in pre–mRNA splicing factor 8 (PRPF8). In order to get insight into the role of PRPF8 in homeostasis and disease, we capitalize on the ability to generate patient-specific RPE cells and reveal differentially expressed genes unique to RPE cells. We found that spliceosomal complex and ribosomal functions are crucial in determining cell type specificity through differential expression and alternative splicing (AS), and that PRPF8 mutation causes global changes in splice site selection and exon inclusion that particularly affect genes involved in these cellular functions. This finding corroborates the hypothesis that retinal tissue identity is conferred by specific splicing program, and identifies retinal AS events as a framework towards the design of novel therapeutic opportunities.

2021-03-05 | GSE165322 | GEO

RNA-seq of RPE cells that harbor a C-terminal GFP-tag on the splicing factor PRPF8 and the retinitis pigmentosa mutation Y2334N

Project description:RPE cells were edited using CRISPR/Cas9 to fuse a GFP-tag at the C-terminus of PRPF8 and additionally mutate amino acid 2334 from Y to N.

2025-03-12 | GSE213805 | GEO

Mutant PRPF8 causes widespread splicing changes in spliceosome components in retinitis pigmentosa patient RPE cells

Project description:Mutant PRPF8 causes widespread splicing changes in spliceosome components in retinitis pigmentosa patient RPE cells

| PRJNA694104 | ENA

PRPF8 CLIP seq for iPSC, kidney organoid, retinal organoid, and retinal epithelium derived from c.6926A>C RPE with Retinitis Pigmentosa patients and CRISPR/Cas9 corrected

Project description:Retinitis Pigmentosa is a group of inherited eye disorders characterized by progressive degeneration of photoreceptor cells in the retina, leading to vision loss and eventual blindness. One of the known genetic mutations associated with RP is the c.6926A>C mutation in the RPE (retinal pigment epithelium) cells. The dataset involves multiple experimental approaches and cell types, providing a comprehensive understanding of the disease and potential corrective strategies.

2024-03-13 | E-MTAB-13171 | biostudies-arrayexpress

Ablating VHL in Rod Photoreceptors Modulates RPE Glycolysis and Improves Preclinical Model of Retinitis Pigmentosa

Project description:Neuroretinal degenerations including retinitis pigmentosa (RP) comprise a heterogeneous collection of pathogenic mutations that ultimately result in blindness. Despite recent advances in precision medicine, therapies for rarer mutations are hindered by burdensome developmental costs. To this end, Von Hippel-Lindau (VHL) is an attractive therapeutic target to treat RP. By ablating VHL in rod photoreceptors and elevating hypoxia-inducible factor (HIF) levels, we demonstrate a path to therapeutically enhancing glycolysis independent of the underlying genetic variant that slows degeneration of both rod and cone photoreceptors in a preclinical model of retinitis pigmentosa. This rod-specific intervention also resulted in reciprocal, decreased glycolytic activity within the retinal pigment epithelium (RPE) cells despite no direct genetic modifications to the RPE. Suppressing glycolysis in the RPE provided notable, non-cell-autonomous therapeutic benefits to the photoreceptors, indicative of metabolically sensitive crosstalk between different cellular compartments of the retina. Surprisingly, targeting HIF2A in RPE cells did not impact RPE glycolysis, potentially implicating HIF1A as a major regulator in mouse RPE and providing a rationale for future therapeutic efforts aimed at modulating RPE metabolism.

2025-01-24 | GSE287734 | GEO

Nrf2 overexpression rescues RPE morphology in mouse models of retinitis pigmentosa

Project description:Nrf2 overexpression rescues RPE morphology in mouse models of retinitis pigmentosa

| PRJNA675578 | ENA

PRPF8-mediated dysregulation of hBrr2 helicase disrupts human spliceosome kinetics and 5´-splice-site selection causing tissue-specific defects

Project description:Mutations in the carboxy terminal of the core spliceosome factor PRPF8 cause autosomal dominant retinitis pigmentosa (RP) 13. Comprehensive cellular, biochemical, and molecular investigations of iPSC-derived retinal organoids, retinal pigment epithelium (RPE) and kidney organoids from four patients carrying the pathogenic PRPF8 RP type 13 c.6926A>C (p.H2309P) heterozygous missense mutation, revealed retinal tissue-specific effects including lower splicing specificity, ciliary abnormalities, altered apical-basal polarity, rod degeneration and loss of photoreceptors. The p.H2309P mutation affected the 5’ splice site recognition by PRPF8 of transcripts encoding ciliary proteins, altered spliceosome kinetics and organisation of nuclear speckles as well as PRPF8 binding to spliceosomal U6 snRNAs and snoRNAs, leading to accumulation of unspliced poly A+ mRNAs specifically in RPE cells and retinal organoids. Together these data provide the most comprehensive characterisation of splicing factor causing RP disease, providing molecular insights into the tissue specificity of pathomechanisms and informing future therapeutic approaches.

2024-02-29 | GSE235866 | GEO

RNA-seq and iCLIP-seq of cells that harbor retinitis pigmentosa mutations

Project description:RNA-seq and iCLIP-seq of cells that harbor retinitis pigmentosa mutations

| PRJNA882468 | ENA

Nrf2 overexpression rescues RPE morphology in mouse models of retinitis pigmentosa [CD1-p40_analysis]

Project description:Nrf2 overexpression rescues RPE morphology in mouse models of retinitis pigmentosa [CD1-p40_analysis]

| PRJNA675589 | ENA

Nrf2 overexpression rescues RPE morphology in mouse models of retinitis pigmentosa [rd1-p20_analysis]

Project description:Nrf2 overexpression rescues RPE morphology in mouse models of retinitis pigmentosa [rd1-p20_analysis]

| PRJNA675587 | ENA