Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

The G protein-coupled pH-sensing receptor OGR1 is a regulator of intestinal inflammation

ABSTRACT: OGR1 is a pH sensing G protein-coupled receptor involved in intestinal homeostasis and inflammation. Up-regulation of genes, mediated by OGR1, in response to extracellular acidification were enriched for inflammation, immune response, actin cytoskeleton and cell adhesion pathways.

ORGANISM(S): Mus musculus

PROVIDER: GSE60295 | GEO | 2015/04/12

SECONDARY ACCESSION(S): PRJNA257971

REPOSITORIES: GEO

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
		Other

Items per page:

1 - 1 of 1

Similar Datasets

The G protein-coupled pH-sensing receptor OGR1 is a regulator of intestinal inflammation

Project description:OGR1 is a pH sensing G protein-coupled receptor involved in intestinal homeostasis and inflammation. Up-regulation of genes, mediated by OGR1, in response to extracellular acidification were enriched for inflammation, immune response, actin cytoskeleton and cell adhesion pathways. Microarray profiling was performed to compare global gene expression of Ogr1 KO and WT residential peritoneal macrophages in response to an acidic pH shift (pH 6.7, 24 h)

2015-04-12 | E-GEOD-60295 | biostudies-arrayexpress

The pH-sensing receptor OGR1 improves barrier function of CaCo-2 cells and inhibits migration in an acidic environment

Project description:OGR1 is a pH-sensing G-protein coupled receptor involved in intestinal homeostasis and inflammation Proton activation of OGR1 increases barrier function in Caco2 cells Microarray profiling was performed on OGR1 stable overexpressing Caco-2 cells during acidic pH shift

2015-08-13 | E-GEOD-60294 | biostudies-arrayexpress

The pH-sensing receptor OGR1 improves barrier function of CaCo-2 cells and inhibits migration in an acidic environment

Project description:OGR1 is a pH-sensing G-protein coupled receptor involved in intestinal homeostasis and inflammation Proton activation of OGR1 increases barrier function in Caco2 cells

2015-08-13 | GSE60294 | GEO

microarray analysis in SREBP2-knockdown cells under low pH (pH 6,8) culture conditions

Project description:The conditions of the tumor microenvironment, such as hypoxia and nutrient starvation, play critical roles in cancer progression. However, the role of acidic extracellular pH in cancer progression is not studied as extensively as that of hypoxia. Here, we show that extracellular acidic pH (pH 6.8) triggered activation of sterol regulatory element-binding protein 2 (SREBP2) by stimulating nuclear translocation and promoter binding to its targets along with intracellular acidification. Interestingly, inhibition of SREBP2, but not SREBP1, suppressed the upregulation of low pH-induced cholesterol biosynthesis-related genes. Moreover, acyl-CoA synthetase short-chain family member 2 (ACSS2), a direct SREBP2 target, provided a growth advantage to cancer cells under acidic pH. Furthermore, acidic pH-responsive SREBP2 target genes were associated with reduced overall survival of cancer patients. Thus, our findings show that SREBP2 is a key transcriptional regulator of metabolic genes and progression of cancer cells, partly in response to extracellular acidification.

2017-01-25 | GSE93980 | GEO

pH dependence of a GPR4 selective antagonist hampers its therapeutic potential

Project description:Inflammatory bowel disease (IBD) is characterized by chronic mucosal inflammation of the gastrointestinal tract and is associated with extracellular acidification of mucosal tissue. Several extracellular pH-sensing receptors, including G protein-coupled receptor 4 (GPR4), play an important role in the regulation of inflammatory and immune responses and GPR4 deficiency has been shown to be protective in IBD animal models. To confirm the therapeutic potential of GPR4 antagonism in IBD, we tested Compound 13, a selective GPR4 antagonist, in the IL10-/- mouse model of colitis. Despite reasonable bioavailability, Compound 13 treatment did not improve colitis in this model and there were no signs of target engagement. Interestingly, Compound 13 behaved as an “orthosteric” antagonist, i.e., its potency was pH-dependent and mostly inactive at pH levels lower than 6.8 with preferential binding to the inactive conformation of GPR4. Mutagenesis studies confirmed Compound 13 likely binds to the conserved orthosteric binding site in G protein-coupled receptors, where a histidine sits in GPR4 likely preventing Compound 13 binding when protonated in acidic conditions. While the exact mucosal pH in the human disease and relevant IBD mice models is unknown, it is well established that the degree of acidosis is positively correlated with the degree of inflammation, suggesting Compound 13 is not an ideal tool to study the role of GPR4 in moderate-to-severe inflammatory conditions.

2024-01-03 | GSE225694 | GEO

Measuring the dependence of the yeast heat shock response on intracellular pH during stress

Project description:S. cerevisiae cells acidify when they experience stressful temperatures. To determine whether this heat-shock associated acidification is important for the cellular response, we manipulated intracellular pH, heat shocked cells, and sequenced the transcriptome.

2020-06-30 | GSE143292 | GEO

Gene expression in PANC-1 and AsPC-1 human pancreatic carcinoma cells under hypoxia, nutrient starvation and low pH culture condition.

2017-01-25 | GSE93988 | GEO

Measuring the dependence of the yeast heat shock response on intracellular pH and translation during stress

Project description:S. cerevisiae cells acidify when they experience stressful temperatures. In addition, newly-translated proteins are thought to misfold, triggering the heat shock response. To determine whether heat-shock associated acidification and translation state are important for the cellular response, we manipulated intracellular pH, blocked translation, heat shocked cells, and sequenced the transcriptome.

2020-06-30 | GSE152916 | GEO

HUVECs with endogenous or overexpressed GPR4 treated with pH 8.4 (control) or pH 6.4 for 5 h

Project description:Acidic tissue microenvironment is commonly found in a variety of pathophysiological conditions. GPR4 is a proton-sensing G protein-coupled receptor that is fully activated by acidic extracellular pH but has lesser activity at the physiological pH 7.4 and minimal activity at more alkaline pH. To determine the effects of GPR4 activation by acidosis on vascular endothelial cells, we examined the global gene expression of the acidosis response in primary human umbilical vein endothelial cells (HUVEC) with varying level of GPR4.

2013-04-25 | GSE40060 | GEO