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Expression data from intestine samples of mice lacking intestinal Pcyt1a, which encodes an enzyme that regulates phosphatidylcholine synthesis.

ABSTRACT: Expression data from intestine samples of mice lacking intestinal Pcyt1a, which encodes an enzyme that regulates phosphatidylcholine synthesis.

PROVIDER: PRJNA433833 | ENA |

REPOSITORIES: ENA

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Expression data from intestine samples of mice lacking intestinal Pcyt1a, which encodes an enzyme that reguates phosphatidylcholine synthesis.

Project description:Expression data from intestine samples of mice lacking intestinal Pcyt1a, which encodes an enzyme that reguates phosphatidylcholine synthesis.

| PRJNA532759 | ENA

Expression data from intestine samples of mice lacking intestinal Pcyt1a, which encodes an enzyme that reguates phosphatidylcholine synthesis.

Project description:Phosphatidylcholine is a membrane lipid. To determine its role in the intestine, we deleted the gene that produces this lipid specificallly in intestinal epithelial cells and conducted expression analysis. We used microarray analysis to determine changes in gene expression that occur in the absence of intestinal phosphatidylcholine synthesis.

2021-02-04 | GSE129776 | GEO

Expression data from intestine samples of mice lacking intestinal Pcyt1a, which encodes an enzyme that regulates phosphatidylcholine synthesis.

2021-02-04 | GSE110474 | GEO

Global consequences of phosphatidylcholine reduction in Bradyrhizobium japonicum

Project description:Analysis of a Bradyrhizobium japonicum pmtA mutant. PmtA catalyzes the first of three consecutive methylation reactions leading to phosphatidylcholine (PC) formation in B. japonicum. Disruption of the pmtA gene results in a significantly reduced PC content causing a defect in symbiosis with the soybean host. This study provides the first insight into global transcriptomic changes of a bacterial phosphatidylcholine biosynthesis mutant. Cells of the pmtA mutant and the wild type were grown to mid-exponential phase in full medium (PSY) under aerobic culture conditions. Keywords: genetic modification Comparative analyis of the B. japonicum pmtA mutant and the wild type grown under aerobic culture conditions.

2008-04-17 | E-GEOD-11187 | biostudies-arrayexpress

Reciprocal regulation of phosphatidylcholine synthesis and H3K36 methylation programs metabolic adaptation

Project description:Reciprocal regulation of phosphatidylcholine synthesis and H3K36 methylation programs metabolic adaptation

| PRJNA752757 | ENA

Phosphatidylcholine synthesis in the developing small intestine.

Project description:1. Phosphatidylcholine synthesis in the foetal, newborn and adult small intestine of rats was studied by determination of cytidine diphosphocholine-1,2-diacylglycerocholine phosphotransferase (cholinephosphotransferase) and acyl-CoA-1-acyl-sn-glycerol-3-phosphocholine acyltransferase (lysophosphatidylcholine acyltransferase) activities and the incorporation of [1-14C]oleic acid into phosphatidylcholine. 2. Cholinephosphotransferase activity was low in foetal jejunum and ileum, increased 3-4 fold in the ileum by 6 days of age and by 12 days in the jejunum. Jejunal activity remained constant throughout weaning; ileal activity gradually decreased to values 25% of that of the jejunum. 3. Lysophosphatidylcholine acyltransferase activity was high in foetal jejunum and ileum, decreased 70% immediately after birth in the jejunum and increased to adult values by 12 days of age. Ileal activity decreased by 20% after birth, but decreased more rapidly at weaning to 30% of the activity in jejunum. 4. Initial rates and steady-state incorporation of [1-14C]oleic acid into phosphatidylcholine by jejunal rings of 10 day-old rats exceeded that observed in jejunal rings from adult rats by 2-4-fold. 5. In the postnatal jejunum, neither cholinephosphotransferase and lysophosphatidylcholine acyltransferase activities nor oleic acid incorporation were stimulated by cortisone administration in vivo.

| S-EPMC1161589 | biostudies-other

Global consequences of phosphatidylcholine reduction in Bradyrhizobium japonicum

2008-04-17 | GSE11187 | GEO

Reciprocal regulation of phosphatidylcholine synthesis and H3K36 methylation programs metabolic adaptation II

Project description:Reciprocal regulation of phosphatidylcholine synthesis and H3K36 methylation programs metabolic adaptation II

| PRJNA795416 | ENA

Transcriptomic characterization of a virulence-deficient phosphatidylcholine-negative Agrobacterium tumefaciens mutant

Project description:To learn more about the global effects of phosphatidylcholine (PC)-deficiency in A. tumefaciens, we performed transcriptomic studies comparing the wild type and a PC-deficient DpmtA Dpcs mutant. We expanded the number of affected virulence genes and showed that the loss of PC was correlated with altered expression of multiple genes encoding membrane or membrane-associated proteins and proteins which fulfil their function at the membrane. The PC-deficient mutant analyzed in this study is further described in Sonja Klüsener, Stephanie Hacker, Yun-Long Tsai, Julia E. Bandow, Ronald Gust, Erh-Min Lai and Franz Narberhaus. 2010. Proteomic and transcriptomic characterization of a virulence-deficient phosphatidylcholine-negative Agrobacterium tumefaciens mutant.

2010-04-07 | GSE21223 | GEO

The rate-limiting enzyme in phosphatidylcholine synthesis regulates proliferation of the nucleoplasmic reticulum.

Project description:The nucleus contains a network of tubular invaginations of the nuclear envelope (NE), termed the nucleoplasmic reticulum (NR), implicated in transport, gene expression, and calcium homeostasis. Here, we show that proliferation of the NR, measured by the frequency of NE invaginations and tubules, is regulated by CTP:phosphocholine cytidylyltransferase-alpha (CCTalpha), the nuclear and rate-limiting enzyme in the CDP-choline pathway for phosphatidylcholine (PtdCho) synthesis. In Chinese hamster ovary (CHO)-K1 cells, fatty acids triggered activation and translocation of CCTalpha onto intranuclear tubules characteristic of the NR. This was accompanied by a twofold increase in NR tubules quantified by immunostaining for lamin A/C or the NE. CHO MT58 cells expressing a temperature-sensitive CCTalpha allele displayed reduced PtdCho synthesis and CCTalpha expression and minimal proliferation of the NR in response to oleate compared with CHO MT58 cells stably expressing CCTalpha. Expression of CCTalpha mutants in CHO58 cells revealed that both enzyme activity and membrane binding promoted NR proliferation. In support of a direct role for membrane binding in NR tubule formation, recombinant CCTalpha caused the deformation of liposomes into tubules in vitro. This demonstrates that a key nuclear enzyme in PtdCho synthesis coordinates lipid synthesis and membrane deformation to promote formation of a dynamic nuclear-cytoplasmic interface.

| S-EPMC551478 | biostudies-literature

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