Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.1.4.3 (phospholipase C)
 18,461 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

1. The composition and metabolism of phospholipids were studied in various tissues from both normal and dystrophic mice of the 129 ReJ strain. Phospholipids extracted from forebrain, spinal cord, sciatic nerve and plasma were fractionated by t.l.c. and measured. 2. Very significant alterations were found in the choline phospholipids from these tissues, except forebrain. Plasma phosphatidylcholine in the dystrophic mouse was increased by 38%. There was a 2-fold increase in lysophosphatidylcholine in the spinal cord of dystrophic mice. The sciatic nerve showed a marked decrease in sphingomyelin content, which is approximately half of that in the controls. 3. Five enzymes involved in phosphatidylcholine metabolism [namely cholinephosphotransferase (EC 2.7.8.2); phospholipases A (EC 3.1.1.4, EC 3.1.1.32); lysophospholipase (EC 3.1.1.5); lysophosphatidylcholine acyltransferase (EC 2.3.1.23); phospholipase C (EC 3.1.4.3)] were studied in tissue preparations from forebrain, spinal cord, sciatic nerves, gastrocnemius muscles and liver. 4. Activities of phospholipases A and C were significantly increased, about 5-fold and 60% respectively, in gastrocnemius muscle of dystrophic mice compared with controls. Phospholipases A also showed 50% higher activity in the sciatic nerves of dystrophic than of normal mice. Lysophosphatidylcholine acyltransferase activities were significantly increased in the sciatic nerves and spinal cord, by 50-100% over that of the controls. The forebrain and spinal cord from dystrophic mice, however, had only 60% of lysophospholipase activities of that of the normal control. Cholinephosphotransferase activity was unchanged in these tissues from both normal and dystrophic mice. 5. It is suggested that are number of features of mouse muscular dystrophy related to altered membrane structure and function can be rationalized in terms of changes in lipid composition and metabolism.
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PMID:Phospholipid composition and metabolism in mouse muscular dystrophy. 72 3

Three kinds of phospholipase C [EC 3.1.4.3] were used to selectively hydrolyze phospholipids in rat liver microsomes, and their effects on the acyl-CoA: glycerophosphate and acyl-CoA: lysophospholipids acyltransferase systems were examined. The glycerophosphate acyltransferase [EC 2.3.1.15] system was inactivated rapidly by treatment with phospholipase C of Ps. aureofaciens or B. cereus and the loss of activity paralleled the degradation of phosphatidylcholine and phosphatidylethanolamine. The 1-acylglycerylphosphorylcholine acyltransferase [EC 2.3.1.23] system was only partially inactivated under the same conditions, whereas the 1-acylglycerophosphate acyltransferase [EC 2.3.1.51] system retained most of its activity even when more than 95% of phosphatidylcholine and phosphatidylethanolamine had been hydrolyzed. The results demonstrate the heterogeneity of acyltransferase systems with respect to their dependence on the intact membrane phospholipids. Hydrolysis of more than 80% of phosphatidylinositol by phosphoinositidase of B. cereus did not significantly affect these acyltransferase systems. The specificity for various acyl-CoA's of 1-acylglycerophosphate acyltransferase in microsomes treated with phospholipase C of Ps. aureofaciens was apparently different from that in untreated microsomes, while the specificity of 1-acylglycerylphosphorylcholine acyltransferase was unchanged. Saturation profiles of the acceptors were significantly different between the acyltransferase systems in phospholipase C-treated and untreated microsomes. These results suggest that 1-acylglycerophosphate and 1-acylglycerylphosphorylcholine acyltransferase systems do not require specific phospholipids such as phosphatidylcholine, phosphatidylethanolamine, and phosphatidylinositol for their catalytic activities, but the integrity of these phospholipids is necessary for the proper functioning and stability of the enzymes.
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PMID:Effect of phospholipase C hydrolysis of membrane phospholipids on acyltransferase systems in rat liver microsomes. 82 60

The effect of exposure of porcine pulmonary artery endothelial cells to hypoxic (0% O2) and normoxic (20% O2) conditions for 24 and 48 h on phospholipid metabolism was studied. Sonicates prepared from endothelial cells that were exposed to 24 h of hypoxia showed significant increases in phospholipase A1 (91%), phospholipase C (75%), and diacylglycerol lipase (57%) activities. Hypoxic exposure of cells for 48 h caused an increase in diacylglycerol lipase activity (54%) only. Hypoxia also caused significant decreases in ATP levels and ATP-dependent arachidonyl coenzyme A (CoA) synthetase activity. Phospholipase A2, lysophosphatidylcholine acyltransferase, and diacylglycerol acyltransferase activities were not influenced by 24 or 48 h of hypoxia. When endothelial cells were prelabeled with [3H]arachidonic acid and then exposed to hypoxia, increased counts were recovered from the free fatty acid fraction of medium and from the cell fatty acid esters, lysophospholipids, diacylglycerols, and triacylglycerols. There was a concomitant decreased recovery of counts from cell phospholipids. These results indicate that hypoxic exposure of endothelial cells altered phospholipid metabolism by activating deacylation pathways and inhibiting reacylation via ATP-dependent arachidonyl CoA synthetase.
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PMID:Effect of hypoxia on phospholipid metabolism in porcine pulmonary artery endothelial cells. 159 Apr 10

Investigations were performed on the influence of the phospholipid composition and physicochemical properties of the rat liver microsomal membranes on acyl-CoA synthetase and acyl-CoA:1-acyl-sn-glycero-3-phosphocholine O-acyltransferase activities. The phospholipid composition of the membranes was modified by incubation with different phospholipids in the presence of lipid transfer proteins or by partial delipidation with exogenous phospholipase C and subsequent enrichment with phospholipids. The results indicated that the incorporation of phosphatidylglycerol, phosphatidylserine and phosphatidylethanolamine induced a marked activation of acyl-CoA synthetase for both substrates used--palmitic and oleic acids. Sphingomyelin occurred as specific inhibitor for this activity especially for palmitic acid. Palmitoyl-CoA: and oleoyl-CoA: 1-acyl-sn-glycero-3-phosphocholine acyltransferase activities were found to depend on the physical state of the membrane lipids. The alterations in the membrane physical state were estimated using two different fluorescent probes--1,6-diphenyl-1,3,5-hexatriene and pyrene. In all cases of membrane fluidization this activity was elevated. On the contrary, in more rigid membranes obtained by incorporation of sphingomyelin and dipalmitoylphosphatidylcholine, acyltransferase activity was reduced for both palmitoyl-CoA and oleoyl-CoA. We suggest a certain similarity in the way of regulation of membrane-bound acyltransferase and phospholipase A2 which both participate in the deacylation-reacylation cycle.
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PMID:Phospholipid dependence of rat liver microsomal acyl:CoA synthetase and acyl-CoA:1-acyl-sn-glycero-3-phosphocholine O-acyltransferase. 162 22

Alpha 1-Adrenergic receptors and bradykinin receptors are two distinct membrane receptors that stimulate phospholipid breakdown and arachidonic acid and arachidonic acid metabolite release. In the current studies, we have examined several mechanisms to assess their possible contribution to arachidonic acid release in the Madin-Darby canine kidney cell line by agonist stimulation of these receptors: 1) activation of phospholipase A2 (PLA2); 2) sequential activation of phospholipase C, diacylglycerol lipase, and monoacylglycerol lipase; and 3) inhibition of the sequential action of fatty acyl-CoA synthetase and lysophosphatide acyltransferase. Experiments were conducted to measure the stimulation of lysophospholipid production by epinephrine and bradykinin, the rate of incorporation of [3H]arachidonic acid into stimulated and unstimulated cells, and the effect on [3H]arachidonic acid release of treating cells with exogenous phospholipase C. The data indicate that stimulation of PLA2 activity is regulated by alpha 1-adrenergic and bradykinin receptors and that this stimulation is mediated, at least in part, by the activation of protein kinase C. We find that the role of diacylglycerol in arachidonic acid release is as an activator of protein kinase C and not as a substrate for a lipase. Moreover, the hormonal agonists do not appear to inhibit fatty acid reacylation. Experiments using the Ca2(+)-sensitive dye fura-2 and the intracellular Ca2+ chelator 1,2-bis(2-aminophenoxy)ethane-N,N,N',N'-tetraacetic acid suggest that bradykinin activates PLA2 by a transient elevation of intracellular Ca2+. This action appears to be less important for activation of PLA2 by epinephrine. Taken together, these data are consistent with the following conclusions. 1) Hormone-stimulated arachidonic acid release in Madin-Darby canine kidney-D1 cells occurs as a consequence of PLA2 activation. 2) The ability of an agonist both to mobilize Ca2+ and to activate protein kinase C contributes to its efficacy as a stimulator of PLA2-mediated arachidonic acid release.
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PMID:Intracellular Ca2+ and protein kinase C interact to regulate alpha 1-adrenergic- and bradykinin receptor-stimulated phospholipase A2 activation in Madin-Darby canine kidney cells. 184 14

At fertilization, the spermatozoon exocytoses its acrosomal granule in a Ca2(+)-dependent process known as the acrosome reaction. In mammalian spermatozoa, possibly because the acrosome is large and membrane fusion takes place between the outer acrosomal membrane and the overlying plasma membrane extensively over the anterior of the sperm head, the exocytotic process is slow and therefore amenable to biochemical dissection. By prelabelling sperm phospholipids with 32P and inducing the acrosome reaction with Ca2+ and the ionophore A23187, we have been able to show that membrane fusion occurs as the result of a sequence of events following Ca2+ entry; Ca2+ is required for at least 3 of these events. The process is initiated by a large-scale breakdown of polyphosphoinositides that is catalysed by a Ca2(+)-dependent phospholipase C. Of the resultant products, diacylglycerol is the essential one. Although its precise role remains to be established, this compound appears to stimulate a later process; it does not seem to act directly as a fusogen, nor does it act through a metabolite. However, it does not act through protein kinase C. At present we believe that diacylglycerol may simultaneously activate phospholipase A2 and inhibit lysophosphatide acyltransferase, to cause a large-scale build-up of fusogenic lysophospholipids in the acrosomal region; Ca2+ may bring about membrane fusion when the levels of these lipids have risen above a necessary threshold.
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PMID:Phosphoinositides and their products in the mammalian sperm acrosome reaction. 196 1

Changes of intracellular activity of lysolecithin acyltransferase (LAT) during an interaction between endothelial cells (EC) and low-density lipoprotein (LDL) were investigated. Following an incubation of EC with LDL, endothelial LAT activity was assayed using [3H]lysophosphatidylcholine as the substrate. Stimulation of EC with either thrombin (0.01-1 U/ml) or Ca(2+)-ionophore A23187 (10(-10)-10(-7) M) dose- and time-dependently enhanced LAT activity in the presence of LDL (1 mg protein/ml), but no enhancement was observed in quiescent cells. Ionomycin together with 1-oleoyl-2-acetyl glycerol, a synthetic analog of diacylglycerols enhanced LAT activity in a similar degree to thrombin in the presence of LDL. Either staurosporine, a protein kinase C inhibitor or neomycin, a phospholipase C inhibitor completely blocked an increase of LAT activity in stimulated EC. Stimulation of EC with various agonists including 12-o-tetradecanoylphorbol-13-acetate, an activator of protein kinase C caused a marked increase in cellular uptake of LDL, and staurosporine inhibited the uptake. These results suggest that the transport of LDL into EC is facilitated by stimulation with thrombin and other agonists, and LDL subsequently activates intracellular LAT. Protein kinase C seems to mediate LDL uptake into EC. Intracellular regulatory roles of LDL in the presence of vasoactive substances were discussed.
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PMID:Enhancement of lysolecithin acyltransferase activity by LDL in thrombin-stimulated porcine-cultured endothelial cells. 801 83

1. Treatment of rats with carbicron induced a reduction of the phospholipids in both microsomal and plasma membranes. 2. A decrease of the structural order parameter (SDPH) and an increase of the pyrene excimer-to-monomer fluorescence ratio (IE/IM) was also observed, indicating membrane fluidization. 3. The specific activity of membrane-bound phospholipase A2 and phospholipase C were decreased in both types of membranes, whereas acyl-CoA:lysophosphatidylcholine acyltransferase activity was augmented due to carbicron treatment.
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PMID:Influence of carbicron (O-[(2-butenoic acid)-N,N-dimethylamide-3-yl] O,O-dimethylphosphate) on some biochemical and biophysical parameters of rat liver membranes. 844 21

Schizochytrium sp. A-2 is a heterotrophic marine fungus used for the commercial production of docosahexaenoic acid (DHA). However, the pattern of the distribution of DHA and how DHA is channeled into phospholipid (PL) and triacylglycerol (TAG) are unknown. In this study, we systematically analyzed the distribution of DHA in TAG and PL during the growth of the cell. The migration of DHA from PL to TAG was presumed during the fermentation cycle. DHA and docosapentaenoic acid were accumulated in both TAG and phosphatidylcholine (PC), whereas eicosapentaenoic acid was mainly deposited in PC. RNA seq revealed that malic enzyme may provide lipogenic NADPH. In addition, long-chain acyl-CoA synthase and acyl-CoA:lysophosphatidylcholine acyltransferase may participate in the accumulation of DHA in PL. No phosphatidylcholine:diacylglycerol cholinephosphotransferase was identified from the genome sequence. In contrast, phospholipid:diacylglycerol acyltransferase-mediated acyl-CoA-independent TAG synthesis pathway and phospholipase C may contribute to the channeling of DHA from PC to TAG.
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PMID:Lipid Distribution Pattern and Transcriptomic Insights Revealed the Potential Mechanism of Docosahexaenoic Acid Traffics in Schizochytrium sp. A-2. 3137 60