Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

RNA sequencing in kidneys of MUC1 Kidney Disease mouse model with and without treatment

ABSTRACT: RNA sequencing in kidneys of MUC1 Kidney Disease mouse model with and without treatment

PROVIDER: PRJNA533238 | ENA |

REPOSITORIES: ENA

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	SRR8921490_1.fastq.gz	Fastqsanger.gz
	SRR8921490_2.fastq.gz	Fastqsanger.gz
	SRR8921491_1.fastq.gz	Fastqsanger.gz
	SRR8921491_2.fastq.gz	Fastqsanger.gz
	SRR8921492_1.fastq.gz	Fastqsanger.gz

Items per page:

1 - 5 of 16

Similar Datasets

RNA sequencing in kidneys of MUC1 Kidney Disease mouse model with and without treatment

Project description:MUC1 kidney disease mouse model generated by knock-in of the human mutated MUC1-fs gene. The mice were treated for 7 days, daily with either vehicle control or BRD4780, a compound showed to be beneficial to disease cells in-vitro. The kidneys were then removed and the bulk RNA was sequenced. The goal of this study was to undersand the effect of the compound on the diseased kidneys and to gain insights to its mechanism of action.

2019-04-18 | GSE129941 | GEO

Transcriptomic of MKD (MUC1 kidney disease) patient compares to normal derived kidney epithelial cells

Project description:bulk RNAseq of MUC1 kidney disease patient derived kidney epithelial cells compare to normal kidney cells. The goal of this study was to elucidate the biological mechanism underlying MUC1 kidney disease using MUC1 expressing cells derived from either a patient or a healthy individual kidney

2019-04-18 | GSE129943 | GEO

MUC1(insC) affects vesicular transport in renal epithelial cells

Project description:Autosomal dominant tubulointerstitial kidney disease associated to the MUC1 gene (ADTKD-MUC1; formerly MCKD1) belongs to a heterogenous group of rare hereditary kidney diseases that is prototypically caused by frameshift mutations in the MUC1 repeat domain. The mutant MUC1(insC) lacks the transmembrane domaine, exhibits aberant cellular topology and hence might gain a function during the pathological process. To get insight into potential pathomechanisms we performed differential proteomics of extracellular vesicles shed by renal epithelia into the urine of patients. The study was based on three ADTKD patients and individual controls applying iTRAQ/LC-MS/MS. A total of 727 proteins were identified across all biological and technical replicates. A proportion of 47 proteins (6.5%) were fold-changed species. GO Term Enrichment analysis revealed proteins with significantly changed expression in ADTKD-associated extracellular vesicles as vesicular transport-associated proteins. Among these VTA1 is involved in the multivesicular body (MVB) pathway similar to the charged multivesicular body protein CHMP2B. VTA1 is also claimed to play roles as a cofactor of the AAA ATPases VPS4A and B in the disassembly of ESCRT III. Protein interaction databases list VPS4B, CHMP2A and IST1 as VTA1 binding partners.

2018-02-23 | PXD008389 | Pride

MicroRNAs differentially expressed in MUC1 overexpressing cells

Project description:To determine if overexpression of MUC1 alters the microRNA profile of pancreatic cancer cells S2.013. Comparison of miRNAs differentially regulated in pancreatic cancer cell line S2.013 with and without MUC1 overexpression. MiRCURY LNA microarray was used to determine differential microRNA expression in one replicate of S2.013.Neo (control) cells compared to S2.013.MUC1 (experimental) cells. Confirmation with qRT-PCR was performed on a subset of microRNAs identified as differentially regulated between the two groups.

2013-08-10 | E-GEOD-48185 | biostudies-arrayexpress

MicroRNAs differentially expressed in MUC1 overexpressing cells

2013-08-10 | GSE48185 | GEO

Brain death associated activation of Calpain-Talin axis in donor kidneys underlies podocyte matrix degradation and graft dysfunction in kidney transplantation

Project description:Deceased kidney donation after brain death (DBD) is the main source of transplants, yet these grafts yield inferior transplant outcomes when compared to living donation. In brain death, cerebral injury contributes to systemic biological dysregulation, causing significant cellular stress in donor kidneys that adversely impacts the quality of grafts. Here, we hypothesized that proteolytic processes in DBD kidneys might lead to podocyte damage with subsequent development of post-transplant dysfunction. Using protein topography and migration analysis platform (PROTOMAP), we mapped degradation profiles of cytoskeletal proteins in DBD kidneys. Cytoskeletal proteolytic degradation was further studied by Immunoblotting on a separate cohort of deceased and living donor kidney biopsies. To investigate potential mechanism of kidney cytoskeletal protein degradation, in-vitro human podocytes and ex-vivo precision-cut human kidney slices were employed. We found novel proteolytic profiles of key podocyte cytoskeletal proteins in donor kidneys associated with suboptimal posttransplant function. These were unique to brain-death and were not observed in circulatory-death or living-donor kidneys. Talin-specific protein degradation in DBD kidneys indicated Calpain-1 activation may have a key role in proteolytic processes observed in the dysfunctional kidneys. Investigation of the underlying mechanism suggests that Transforming-Growth Factor-Î² (TGFÎ²) induces Calpain-1 activation, leading to brain-death specific podocyte degradation patterns and dysregulation of actin cytoskeleton; events that were prevented, in-vitro, by Calpain inhibition. Conclusion Our data demonstrate that podocyte protein degradation impacts the quality of DBD kidneys, propose a role of TGFÎ² mediated Calpain-1 proteolytic processing of cytoskeletal Talin-1, suggesting therapeutic opportunities to prevent kidney dysfunction.

2022-08-12 | PXD022074 | Pride

Transcriptional analysis of Nphp1-/- KO mouse model kidneys

Project description:Bulk RNAseq of kidneys from 5 months-old mice invalidated for Nphp1 which is the main gene responsible for Nephronophtisis, a genetic kidney disease

2022-04-04 | E-MTAB-11594 | biostudies-arrayexpress

Transcriptomic of MKD (MUC1 kidney disease) patient compares to normal derived kidney epithelial cells

Project description:Transcriptomic of MKD (MUC1 kidney disease) patient compares to normal derived kidney epithelial cells

| PRJNA533239 | ENA

Expression data from the transplanted kidney and the native kidney of NEP25 mice with/without the treatment of LMB2

Project description:A previous study revealed the appropriate amount of LMB2 (1.75 ng/g body wt dissolved in 0.1 ml of PBS containing 0.1% bovine serum albumin [BSA]) needed to induce reproducible a focal segmental glomerulosclerosis (FSGS) lesions in NEP25 mice. We performed kidney transplantation between NEP25 mice and their wild-type littermates (WTm) which have the same genetic background (C57BL/6N). In this study, the transcriptomic profiles of transplanted and native kidneys with/without LMB2 in nephrotic model mice were investigated using the next-generation RNA sequencing (RNA-seq). Reads were mapped on mm10 mouse reference genome and quantified using CLC Genomics Workbench version 10.1.1 (QIAGEN).

2025-06-04 | GSE125840 | GEO

Sequencing the anti-MUC1 hybridoma antibody 139H2

Project description:Mucin 1 (MUC1) is a transmembrane mucin expressed at the apical surface of epithelial cells at different mucosal surfaces including breast and intestine. The MUC1 extracellular domain contains a variable number of tandem repeats (VNTR) of 20 amino acids, which are heavily O-linked glycosylated. Monoclonal antibodies against the MUC1 VNTR can be powerful tools because of their multiplicity of binding and possible applications in the diagnosis and treatment of MUC1-expressing cancers. One such antibody is the hybridoma mouse monoclonal 139H2 which is also widely used as a research tool to study non-cancer MUC1. Here we report direct mass spectrometry-based sequencing of hybridoma-derived 139H2 IgG, which enabled reverse engineering of a recombinant 139H2.

2024-03-18 | PXD043489 | Pride

OmicsDI is part of the ELIXIR infrastructure

OmicsDI is an Elixir interoperability service. Learn more ›

Tweets

OmicsDI Databases

PRIDE
PeptideAtlas
MassIVE
JPOST Repository
Physiome Model Repository

EGA
EVA
ENA
LINCS
PAXDB
Cell Collective

MetaboLights
Metabolomics Workbench
MetabolomeExpress
GNPS
BioModels
FAIRDOMHub

ArrayExpress
dbGaP
ExpressionAtlas
GEO
NODE

Information

Databases
Help
API
Contact us
Code on GitHub
Terms of use
Submit Data