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At least 145 records · Page 8Linked to original sources
PubMed1985

Manganese stimulates incorporation of [3H]inositol into an agonist-insensitive pool of phosphatidylinositol in brain membranes.

In a particulate preparation from rat brain, manganese ions stimulate the incorporation of [3H]inositol into inositol phospholipids in a concentration-dependent manner. Incubation with CDP-diacylglycerol (0.5 mM) alone had no effect on the incorporation of [3H]inositol but potentiated the stimulatory effect of manganese. Despite the increase in [3H]inositol incorporation into phosphatidylinositol, the carbachol-induced accumulation of [3H]inositol-1-phosphate was unaltered in membranes preincubated with manganese but when coincubated with CDP-diacylglycerol the carbachol-induced accumulation of [3H]inositol-1-phosphate was increased. These data suggest that manganese stimulates the incorporation of [3H]inositol into an agonist-insensitive pool of phosphatidylinositol.

Animals↗
PubMed1991

Deoxycytidine is salvaged not only into DNA but also into phospholipid precursors. III. dCOP-diacylglycerol formation in tonsillar lymphocytes.

In addition to the water-soluble deoxyliponucleotides (Spasokukotskaja et al. (1988), Biochem. Biophys. Res. Commun. 155, 923), a lipid compound was shown to be labeled from external 3H-deoxycytidine (5-3H-CdR) in infant tonsillar lymphocytes. Chlorpromazine enhanced the labeling of this compound, identified by TLC as 3H-dCDP-diacylglycerol (3H-dCOP-DAG). The deoxynucleotide salvage pathway seems to be the main source for dCDP-DAG synthesis, as hydroxyurea increased its labeling from CdR. myo-Inositol induced the disappearance of 5-3H-dCOP-DAG, suggesting its utilization for phosphatidylinositol synthesis. 3H-Arabinosyl-Cytosine (araC) is also incorporated into the lipidic fraction at a rate comparable to its incorporation into DNA, supporting the effect of araC on membrane functions.

Chlorpromazine↗
PubMed1994

Muscarinic receptor-dependent activation of phospholipase C in the developing human fetal central nervous system.

The coupling of muscarinic-cholinergic receptors (mAChR) to adenylate cyclase and phospholipase C (PLC) second messenger systems has been demonstrated in many animal species. However, little is known about this association in the developing human central nervous system. Because of the proposed role of acetylcholine in the regulation of development and differentiation of neural cells, an understanding of these relationships during human fetal development gains importance. We report, in this communication, the coupling of mAChR with PLC in the human fetal brain. This coupling was determined using two independent approaches that relied upon estimating the accumulation of inositol phosphates (IPs) and cytidine diphosphate diacylglycerol (CDP-DAG). Carbachol treatment of brain slices, in the presence of lithium, resulted in the accumulation of IPs. Analysis of the kinetics of this accumulation showed that IP3 and IP2 increased rapidly, reaching a peak or plateau before IP. The results also showed that agonist-stimulated PLC produced two second messengers, IP3 and DAG. The production of DAG was strongly supported by the carbachol-dependent increase of CDP-DAG. The accumulation of IP and CDP-DAG was dependent on agonist concentration. The obtained EC50 values were approximately: carbachol 47 microM; acetylcholine 6 microM; and oxotremorine 25 microM. Unexpectedly, all three agonists demonstrated a similar efficacy. The cholinergic stimulation of inositide hydrolysis appears to be the result of activation of the m1 muscarinic receptor.

Atropine↗
PubMed1991

An improved synthesis of 7-nitrobenz-2-oxa-1,3-diazole analogs of CDP-diacylglycerol and phosphatidylinositol.

A protocol utilizing chemical and enzymatic steps to synthesize several fluorescent (7-nitrobenz-2-oxa-1,3 diazole) analogs of cytidine diphosphate diacylglycerol and phosphatidylinositol in high yields is described. The fluorescent analogs were characterized by phospholipase C digestion, fast atom bombardment mass spectrometry, and HPLC analysis. Studies of the metabolism and intracellular distribution of the fluorescent phosphatidylinositol analogs in Swiss 3T3 cells further revealed that all the analogs were substrates for a previously described cell surface phosphatidylinositol-specific phospholipase C (A.E. Ting and R.E. Pagano (1990) J. Biol. Chem. 265, 5337-5340). These fluorescent lipids should serve as useful tools for studying phosphatidylinositol metabolism and transport in cells.

Animals↗
PubMed1987

The enhanced 32P labeling of CDP-diacylglycerol in c-myc gene expressed human kidney cancer cells.

Correlation between c-myc gene expression and phosphatidylinositol (PI) metabolism was studied using seven human kidney cancer cell lines. We found that the exceptional incorporation of 32P into CDP-diacylglycerol (CDP-DG) was observed in only two cell lines, in which c-myc expression was increased among seven cell lines tested. In these two cell lines, PI was also labeled. The other five cell lines indicated the accumulation of radioactive PI, whereas CDP-DG was unlabeled.

Cell Division↗
PubMed1992

CDP-diacylglycerol synthesis in rat liver mitochondria.

CDP-diacylglycerol for polyglycerophosphatide biogenesis can be synthesized within rat liver mitochondria. This membrane-associated enzyme was predominantly located in the inner mitochondrial membrane. GTP had a significant effect in activating the microsomal CDP-diacylglycerol synthase, especially if the microsomes were preincubated with GTP in the presence of phosphatidic acid. This stimulatory effect of GTP on the microsomal enzyme was not detected in the mitochondrial fractions. The enzymes could be solubilized from the membrane fractions using CHAPS, and the detergent-soluble activity partially restored by addition of phospholipids. Mitochondrial and microsomal CDP-diacylglycerol synthase activity could be completely separated by anion-exchange column chromatography. The mitochondrial and microsomal CDP-diacylglycerol synthases appear to be two distinct enzymes with different localization and regulatory characteristics.

Animals↗
PubMed1993

Characterization of reactions catalysed by yeast phosphatidylinositol synthase.

The nature of reactions catalysed by yeast phosphatidylinositol synthase expressed in E. coli has been investigated. The single enzyme is shown to carry both CDP-diacylglycerol-dependent incorporation of inositol into phosphatidylinositol (Km for inositol of 0.090 mM) and a CDP-diacylglycerol-independent exchange reaction between phosphatidylinositol and inositol (Km for inositol of 0.066 mM). The exchange reaction and reversal of phosphatidylinositol synthase were both stimulated by CMP, but had different optimum pH and requirements for substrates. These results suggest that CMP-stimulated exchange and CMP-dependent reverse reactions are distinct processes catalysed by the same enzyme, phosphatidylinositol synthase.

CDP-Diacylglycerol-Inositol 3-Phosphatidyltransfer↗
PubMed1994

Palmitoylation but not the extreme amino-terminus of Gq alpha is required for coupling to the NK2 receptor.

Gq alpha and G11 alpha differ from other G protein alpha subunits in that they have unique, conserved 6 residue amino-terminal extensions. Wild-type and amino-terminal mutants of Gq alpha expressed in COS cells were analyzed for their ability to functionally couple with co-expressed neurokinin NK2 receptor. Wild-type, T2A and delta 2-7 Gq alpha were able to stimulate agonist driven phospholipase C (PLC) activity in identical manners. Other activities of these two amino-terminal mutants including aluminum fluoride stimulated PLC activity, palmitoylation, interaction with G beta gamma subunits and GTP gamma S-induced trypsin resistance are also similar to the wild-type alpha subunit. This demonstrates that the NK2 receptor is able to functionally interact with the alpha subunit of Gq and that the first seven amino-acids of Gq alpha are not required for any of the alpha subunit functions tested. In contrast to the T2A and delta 2-7 mutants, a C9,10A Gq alpha mutant was not able to couple to either the NK2 receptor or PLC, as assessed by high-affinity agonist binding and activation of PLC either in intact cells or in vitro. The C9,10A protein was able to assume a GTP gamma S-induced trypsin-resistant conformation and partitioned primarily to the pelletable fraction in a manner similar to the wild-type protein. However, it was not labeled with [3H]palmitic acid. This suggests that blocking palmitoylation at the amino-terminus of Gq alpha results in a loss of functional activity which reflects an inability to interact with both the receptor and downstream signaling targets.

Aluminum Compounds↗