Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Sodium phenylbutyrate rescues thyroid hormone transport in brain endothelial cells

ABSTRACT: Sodium phenylbutyrate rescues thyroid hormone transport in brain endothelial cells

PROVIDER: PRJNA735236 | ENA |

REPOSITORIES: ENA

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	SRR14736215.fastq.gz	Fastqsanger.gz
	SRR14736216.fastq.gz	Fastqsanger.gz
	SRR14736217.fastq.gz	Fastqsanger.gz
	SRR14736218.fastq.gz	Fastqsanger.gz
	SRR14736219.fastq.gz	Fastqsanger.gz

Items per page:

1 - 5 of 19

Similar Datasets

Sodium phenylbutyrate rescues thyroid hormone transport in brain endothelial cells

Project description:Monocarboxylate transporter 8 (MCT8) deficiency is a rare genetic disease leading to a severe developmental delay. Some MCT8 deficient patients are not as severely affected than others due to residual thyroid hormone (TH) transport. Previously, we hypothesized that these patients’ mutations destabilize the MCT8 protein, which consequently will be sent for degradation. We have already demonstrated that the chemical chaperone sodium phenylbutyrate (NaPB) rescues the function of these mutants by stabilizing their protein expression in an overexpressing cell system. Here we expand our previous work and used human iPSC-derived brain microvascular endothelial-like cells (iBMECs) as a model. We could show that NaPB rescues decreased mutant MCT8 expression and restores transport function. Furthermore, we identified MCT10 as another TH transporter that contributes to T3 uptake. The decrease in mutant protein expression could be explained by the activation of components of the unfolded protein response (UPR) machinery. Increased expression after NaPB treatment is a consequence of UPR attenuation and the stabilization of MCT8 mRNA. In conclusion, we demonstrate that NaPB is suitable to stabilize pathogenic missense mutations and activate transport function in a human-derived cell model opening the possibility of repurposing the FDA-approved drug NaPB for MCT8 deficiency.

2024-12-02 | GSE176188 | GEO

mRNA Expression data from sodium butyrate or sodium phenylbutyrate treated A549 cells

Project description:As a histone deacetylase inhibitor, sodium butyrate and its derivative sodium phenylbutyrate involve in cellular events such as proliferation, differentiation, apoptosis and cell cycle control via reprogramming gene expression. However, the gene associated with the cell cycle control and molecular signaling triggering cell apopotosis and death are not well elucidated. Here, we treated A549 cells,a cell line belong to the non-small cells lung cancer,with high concentration of sodium butyrate or sodium phenylbutyrate and then used microarray identified differentially-expressed mRNA during this process.

2017-06-10 | GSE86928 | GEO

Targeting PARK7: Sodium 4-Phenylbutyrate Shields Endothelial Cells from GSDME-Mediated Pyroptosis in Acute Lung Injury

Project description:Summary Sodium 4-phenylbutyrate (Na-PBA), a histone deacetylase inhibitor, shows potential in mitigating acute lung injury (ALI) by addressing endothelial cell injury. In a lipopolysaccharide (LPS)-induced ALI mouse model, Na-PBA pretreatment reduced lung damage, pulmonary edema, and inflammatory markers, while decreasing oxidative stress and endothelial pyroptosis via the cytochrome c-caspase9-caspase3-GSDME pathway. In vitro studies with human umbilical vein endothelial cells (HUVECs) confirmed that Na-PBA enhanced PARK7 expression, which is crucial for its protective effects against oxidative damage and pyroptosis. The mechanism involves PARK7 stabilizing mitochondria and inhibiting cytochrome c leakage, leading to reduced caspase activation. Na-PBA's effects are mediated through upregulation of PARK7, potentially within a positive feedback loop involving NRF2. These findings identify a novel therapeutic strategy to alleviate endothelial injury in lung diseases.

2025-01-07 | GSE285730 | GEO

Tmprss2 maintains epithelial barrier integrity and transepithelial sodium transport

Project description:Tmprss2 maintains epithelial barrier integrity and transepithelial sodium transport

| PRJNA1040298 | ENA

Targeting PARK7: Sodium 4-Phenylbutyrate Shields Endothelial Cells from GSDME-Mediated Pyroptosis in Acute Lung Injury

Project description:Targeting PARK7: Sodium 4-Phenylbutyrate Shields Endothelial Cells from GSDME-Mediated Pyroptosis in Acute Lung Injury

| PRJNA1205726 | ENA

Transcriptomic profiles of testis from hindlimb unloaded mice treated with 4-phenylbutyrate

Project description:Transcriptomic profiles of Testis of hindlimb unloaded mice treated with vehicle or 4-phenylbutyrate (4-PBA)

2024-05-01 | GSE205126 | GEO

Tmprss2 maintains epithelial barrier integrity and transepithelial sodium transport

Project description:Membrane-bound serine proteases are well known regulators of ENaC. More recently, they have also been identified as regulators of tight junction complexes. Here, we demonstrate that within the kidney, the serine protease Tmprss2 is co-expressed with the alpha subunit of ENaC, whereas Furin is primarily expressed in ENaC-negative cortex cells. In mCCDcl1 kidney cells, aldosterone-induced ENaC and Scnn1a-specific overexpression is accompanied by increased Tmprss2 gene expression, whereas Scnn1a silencing does not alter Tmprss2 transcription, suggesting that ENaC depends on Tmprss2 expression. This was confirmed by CRISPR-Cas9 Tmprss2 knockout which significantly downregulates Scnn1a gene and protein expression, and thus ENaC-mediated transepithelial sodium transport. Additionally, RNA sequencing analyses unveiled a drastic downregulation in EpCAM and claudin-3 and -7 gene expression, resulting in reduced protein expression also confirmed by immunocytochemistry. In summary, our data clearly demonstrates that the serine protease Tmprss2 is important in maintaining the epithelial tight junction barrier, in addition to regulating ENaC function via Scnn1a expression.

2024-01-02 | GSE247775 | GEO

Transcriptomic profiles of gastrocnemius muscles from hindlimb unloaded mice treated with 4-phenylbutyrate

Project description:Transcriptomic profiles of gastrocnemius muscles from 18 weeks old, male, hind muscles unloaded mice treated with vehicle or4-phenylbutyrate (4-PBA)

2022-07-20 | GSE189455 | GEO

Phenylbutyrate rescues the transport defect of the Sec61α mutations V67G and T185A for renin.

Project description:The human Sec61 complex is a widely distributed and abundant molecular machine. It resides in the membrane of the endoplasmic reticulum to channel two types of cargo: protein substrates and calcium ions. The SEC61A1 gene encodes for the pore-forming Sec61α subunit of the Sec61 complex. Despite their ubiquitous expression, the idiopathic SEC61A1 missense mutations p.V67G and p.T185A trigger a localized disease pattern diagnosed as autosomal dominant tubulointerstitial kidney disease (ADTKD-SEC61A1). Using cellular disease models for ADTKD-SEC61A1, we identified an impaired protein transport of the renal secretory protein renin and a reduced abundance of regulatory calcium transporters, including SERCA2. Treatment with the molecular chaperone phenylbutyrate reversed the defective protein transport of renin and the imbalanced calcium homeostasis. Signal peptide substitution experiments pointed at targeting sequences as the cause for the substrate-specific impairment of protein transport in the presence of the V67G or T185A mutations. Similarly, dominant mutations in the signal peptide of renin also cause ADTKD and point to impaired transport of this renal hormone as important pathogenic feature for ADTKD-SEC61A1 patients as well.

| S-EPMC8807872 | biostudies-literature

Transcriptomic profiles of liver tissue from hindlimb unloaded mice treated with 4-phenylbutyrate

Project description:Bulk transcriptomic profiles of liver tissues from male, 18 weeks old c57Bl/6j mice, including ground-based controls, hindlimb-unloaded mice treated with vehicle, and hindlimb unloaded mice treated wit 4-phenylbutyrate (4-PBA)

2024-02-11 | GSE196560 | GEO

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