The effect of PLC inhibitor on cold responsive transcriptome.
Ontology highlight
ABSTRACT:
ORGANISM(S): Arabidopsis thaliana
PROVIDER: GSE13295 | GEO | 2009/03/03
SECONDARY ACCESSION(S): PRJNA109505
REPOSITORIES: GEO
Similar Datasets
Project description:Identification of genes induced with the cold via inhibition of the phospholipase C - To answer this question we chose a pharmacological approach. We decided to use molecules that are going to inhibit PLC. U73343 is an inactive homolog of U73122 (inhibitor of the phospholipase C pathway). Keywords: treated vs untreated comparison 3 dye-swap - CATMA arrays
2010-05-22 | E-GEOD-13295 | biostudies-arrayexpress
Project description:The study aims at determining the genes that are induced or repressed by cold in the suspension cells. It also aims at monitoring the effect of inhibitors of PLC (U73122 vs. U73343) and PLD (ethanol vs. tertiary butanol) on cold response at the transcription level. To answer this question we chose a pharmacological approach. We decided to use molecules that are going to inhibit PLC or PLD. For PLC we use U73122 and its inactive analog as a control; for PLD we used a primary alcohol (ethanol) and a tertiary alcohol (tert-butanol) as a control. We therefore extracted RNA after the following treatments:<br> 4 °C<br> 22 °C<br> 4 °C + 0.9% primary-ethanol<br> 4 °C + 0.9% tertiary-butanol<br> 4 °C + 60 micromolaire U73122<br> 4 °C + 60 micromolaire U73343<br> The exposure at 4 °C was 4 hours.
2005-08-26 | E-MEXP-259 | biostudies-arrayexpress
Project description:Crohn’s disease is a chronic, debilitating inflammatory bowel disease. Here we report a critical role for phospholipase C-β3 (PLC-β3) in intestinal homeostasis. In PLC-β3- deficient mice, exposure to oral dextran sodium sulfate induced lethality and severe inflammation in the small intestine. The lethality was due to PLC-β3 deficiency in multiple non-hematopoietic cell types. PLC-β3 deficiency resulted in reduced Wnt/β-catenin signaling, which is essential for homeostasis and regeneration of the intestinal epithelium. PLC-β3 regulated the Wnt/β-catenin pathway in small intestinal epithelial cells (IECs) at transcriptional, epigenetic, and potentially protein-protein interaction levels. PLC-β3- deficient IECs were unable to respond to stimulation by R-spondin 1, an enhancer of Wnt/β-catenin signaling. Reduced expression of PLC-β3 and its signature genes was found in biopsies of ileal Crohn’s disease patients. PLC-β regulation of Wnt signaling was evolutionally conserved in Drosophila. Our data indicate that reduction of PLC-β3- mediated Wnt/β-catenin signaling contributes to the pathogenesis of ileal Crohn’s disease.
2024-10-06 | GSE244937 | GEO
Project description:Crohn’s disease is a chronic, debilitating inflammatory bowel disease. Here we report a critical role for phospholipase C-β3 (PLC-β3) in intestinal homeostasis. In PLC-β3- deficient mice, exposure to oral dextran sodium sulfate induced lethality and severe inflammation in the small intestine. The lethality was due to PLC-3 deficiency in multiple non-hematopoietic cell types. PLC-β3 deficiency resulted in reduced Wnt/-catenin signaling, which is essential for homeostasis and regeneration of the intestinal epithelium. PLC-β3 regulated the Wnt/β-catenin pathway in small intestinal epithelial cells (IECs) at transcriptional, epigenetic, and potentially protein-protein interaction levels. PLC-β3- deficient IECs were unable to respond to stimulation by R-spondin 1, an enhancer of Wnt/β-catenin signaling. Reduced expression of PLC-β3 and its signature genes was found in biopsies of ileal Crohn’s disease patients. PLC-β regulation of Wnt signaling was evolutionally conserved in Drosophila. Our data indicate that reduction of PLC-β3- mediated Wnt/β-catenin signaling contributes to the pathogenesis of ileal Crohn’s disease.
2024-10-06 | GSE244936 | GEO
Project description:Crohn’s disease is a chronic, debilitating inflammatory bowel disease. Here we report a critical role for phospholipase C-β3 (PLC-β3) in intestinal homeostasis. In PLC-β3- deficient mice, exposure to oral dextran sodium sulfate induced lethality and severe inflammation in the small intestine. The lethality was due to PLC-3 deficiency in multiple non-hematopoietic cell types. PLC-β3 deficiency resulted in reduced Wnt/-catenin signaling, which is essential for homeostasis and regeneration of the intestinal epithelium. PLC-β3 regulated the Wnt/β-catenin pathway in small intestinal epithelial cells (IECs) at transcriptional, epigenetic, and potentially protein-protein interaction levels. PLC-β3- deficient IECs were unable to respond to stimulation by R-spondin 1, an enhancer of Wnt/β-catenin signaling. Reduced expression of PLC-β3 and its signature genes was found in biopsies of ileal Crohn’s disease patients. PLC-β regulation of Wnt signaling was evolutionally conserved in Drosophila. Our data indicate that reduction of PLC-β3- mediated Wnt/β-catenin signaling contributes to the pathogenesis of ileal Crohn’s disease.
2024-10-06 | GSE244935 | GEO
Project description:Phospholipase C gamma 1 (PLC-γ1) occupies a critically important position in the T cell signaling pathway. While its functions as a regulator of both Ca2+ signaling and PKC-family kinases are well characterized, PLC-γ1’s role in the regulation of early T cell receptor signaling events is incomplete. Activation of the T cell receptor leads to the formation of a signalosome complex between SLP-76, LAT, PLC-γ1, Itk, and Vav1. Recent studies have revealed the existence of both positive and negative feedback pathways from components of the signalosome complex to the apical kinase in the pathway, Lck. To determine the role, if any, of PLC-γ1 in these feedback networks, we performed a quantitative phosphoproteomic analysis of the PLC-γ1-deficient T cells. These data revealed a previously unappreciated role for PLC-γ1 in the positive regulation of Zap-70 and T cell receptor tyrosine phosphorylation. Conversely, PLC-γ1 negatively regulated the phosphorylation of signalosome associated proteins including previously established Lck substrate phosphorylation sites within this complex. While the positive and negative regulatory phosphorylation sites on Lck were largely unchanged, Tyr192 phosphorylation was elevated in Jgamma1. The data supports a model wherein Lck’s targeting, but not its kinase activity is altered by PLC-γ1, possibly through Lck Tyr192 phosphorylation.
2017-06-28 | PXD005165 | Pride
Project description:Overexpression (OE) of phospholipase C (PLC) promotes drought stress tolerance in various plant species. How PLC contributes to this phenotype is unknown. To investigate this, transcriptomic analyses of drought-stressed Arabidopsis plants were performed in wild type (WT) and four distinct PLC-OE backgrounds. To be able to measure the earliest responses in both root- and shoot tissues, a vermiculite-based assay was developed. Subsequent transcriptomics analyses revealed that WT plants responded relatively strongly to the drought, whereas all PLC-OEs lines responded to a lesser extent. Changes in various pathways were observed that were differentially regulated in WT. These include, i) several phospholipid metabolism genes, which may counteract the overexpression of PLC activity, ii) genes involved in the circadian rhythm, shifting to a more night-like expression pattern for the PLC-OE lines, iii) downregulation of several light reaction-related genes, and iv) upregulation of genes involved in the brassinosteroid signalling pathway. In the PLC-OE lines, a subset of genes involved in auxin signalling was found to be differently regulated under drought. Similarly, genes upstream of H2O2 production were found upregulated, while ROS-induced genes were downregulated. Though unable to pin point the primary cause of the drought tolerant phenotype in PLC-OE plants, several novel connections were identified, which are highlighted and discussed in more detail.
2024-07-01 | GSE270544 | GEO
Project description:au13-01_pi-plc What are the genes that are regulated by basal PI-PLC? Arabidopsis thaliana cells in suspension (5-days old). Cultivated in environment (middle) Gamborg+2,4-D. Added inhibitors 4 hr before extraction of the RNAs. We try to determine the role of phospholipases C ( PI-PLC) in the control of the basal expression of the genes of suspension of Arabidopsis thaliana. A first experience in which we used the edelfosine as inhibitor allowed us to identify numerous genes the basal expression of which is altered by this inhibition. We want to confirm these results with another inhibitor. 4 dye-swap - treated vs untreated comparison - treatment variations
2013-09-01 | E-GEOD-46941 | biostudies-arrayexpress
Project description:au13-01_pi-plc What are the genes that are regulated by basal PI-PLC? Arabidopsis thaliana cells in suspension (5-days old). Cultivated in environment (middle) Gamborg+2,4-D. Added inhibitors 4 hr before extraction of the RNAs. We try to determine the role of phospholipases C ( PI-PLC) in the control of the basal expression of the genes of suspension of Arabidopsis thaliana. A first experience in which we used the edelfosine as inhibitor allowed us to identify numerous genes the basal expression of which is altered by this inhibition. We want to confirm these results with another inhibitor.
2013-09-01 | GSE46941 | GEO
Project description:rs09-04_plc_2 - edelfosine and wortmannin effect at 22°c and 4°c - Is there an overlap between PI4-kinase and phospholipase C signaling in cold response ? - Experiments were carried out with Columbia suspension cells. Cells were treated or not with edelfosine (PLC inhibitor) or wortmannin (PI4-kinase inhibitor). These agents were added 15 min before cold stress. ARN were extracted 4h after stress. Controls were made at 22°C. Keywords: treated vs untreated comparison 11 dye-swap - CATMA arrays
2010-08-01 | E-GEOD-19850 | biostudies-arrayexpress