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Edelfosine and wortmannin effect at 22°c and 4°c-PI4-kinase and phospholipase C signaling in cold response

ABSTRACT: 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

ORGANISM(S): Arabidopsis thaliana

PROVIDER: GSE19850 | GEO | 2010/08/01

SECONDARY ACCESSION(S): PRJNA122121

REPOSITORIES: GEO

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edelfosine and wortmannin effect at 22°c and 4°c-PI4-kinase and phospholipase C signaling in cold response

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

Arabidopsis thaliana

Project description:edelfosine and wortmannin effect at 22°c and 4°c-PI4-kinase and phospholipase C signaling in cold response

| PRJNA122121 | ENA

Inhibition of the PI-PLC by U73122

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

Inhibition of the PI-PLC by U73122

2013-09-01 | GSE46941 | GEO

Dynamics of allosteric regulation of the phospholipase C-gamma isoform

Project description:we used hydrogen deuterium exchange masss spec (HDX-MS) to define the exchange kinetics of PLC-y1 as it interacts with the kinase domain of FGFR1, and liposomes containing PIP2, in order to understand how PLC-y isozymes operate at membranes. We show that the binding of FGFR1k to PLC-y1 increases deuterium incorporation within the interface between the regulatory domains and the catalytic core. Importantly, the addition of liposomes further increase deuterium exchange within the same region.

2022-06-14 | PXD030492 | Pride

Transcription profiling of cold and phosphlipase treated Arabidopsis tto analyse the effect of Phospholipases C and D

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: 4 °C 22 °C 4 °C + 0.9% primary-ethanol 4 °C + 0.9% tertiary-butanol 4 °C + 60 micromolaire U73122 4 °C + 60 micromolaire U73343 The exposure at 4 °C was 4 hours.

2005-08-26 | E-MEXP-259 | biostudies-arrayexpress

Arabidopsis thaliana

Project description:The effect of PLC inhibitor on cold responsive transcriptome.

| PRJNA109505 | ENA

Expression analysis with Phospholipase C over expression

Project description:The regulation of phospholipid biosynthesis in Saccharomyces cerevisiae through cis-acting upstream activating sequence inositol (UASino) and trans-acting elements, such as the INO2-INO4 complex and OPI1 by inositol supplementation in growth is thoroughly studied. In this study, we provide evidence for the regulation of lipid biosynthesis by phosphatidylinositol-specific phospholipase C (PLC) through UASino and two trans-acting elements. Gene expression analysis and radiolabelling experiments demonstrated that the overexpression of rice PLC in yeast cells altered phospholipid biosynthesis at the levels of transcriptional and enzyme activity.

2012-09-01 | GSE35745 | GEO

Expression analysis with Phospholipase C over expression

2012-04-24 | GSE35677 | GEO

Ileal Crohn’s disease exhibits reduced activity of phospholipase C-β3 (PLC-β3)-dependent Wnt/b-catenin signaling pathway [microarray]

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

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