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)

Human red blood cells were treated with phospholipase C from Clostridium welchii. Lipase concentrations which produced less than 1% hemolysis and 10-15% hydrolysis of the membrane phospholipids reduced markedly (greater than 80%) the accessibility of membrane proteins to the external surface as measured by lactoperoxidase-catalyzed iodination.
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PMID:Decreased iodination of the red cell surface following phospholipase C treatment. 19 10

The intracellular location of various enzymes involved in the metabolism of phospholipids of Candida albicans was studied. Among the biosynthetic enzymes, phosphatidylserine synthetase was found to be localized in the microsomes; choline kinase and ethanolamine kinase were cytosolic; acyltransferase was localized in the particulate fraction and glycerol kinase and phosphatidic acid phosphatase were distributed in both the microsomal and cytosolic fractions. Phospholipase A and phospholipase C were abundant in the microsomes and phospholipase C was also detected in the cytosol. Lysophospholipase and glycerophosphocholine diesterase were distributed mainly in the mitochondria. Lipase activity was also detected in this fungus. Based on the enzymes detected in this study we have postulated pathways of phospholipid metabolism in C. albicans.
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PMID:Subcellular localization of enzymes of phospholipid metabolism in Candida albicans. 228 83

Diacylglycerols can accumulate transiently in intact cells as a consequence of the degradation of phosphatidylinositol by phospholipase C, but little information is available concerning their metabolic fate in the vascular endothelium. Diacylglycerol lipase and kinase activities were measured in rat brain microvessel preparations. Lipase activity, measured by the release of free fatty acids, was much greater at pH 4.5 than at pH 7. The acid lipase was predominantly particulate and likely originated in lysosomes, whereas the neutral lipase was mainly soluble. The fatty acid at the sn-1 position of the diacylglycerol substrate was hydrolyzed faster than that at the sn-2 position at both pH 4.5 and 7. The 2-monoacylglycerol accumulated at pH 4.5 but not at 7 due to the presence of a monoacylglycerol lipase activity with a neutral pH optimum. The formation of phosphatidic acid (kinase activity) was also measured in microvessels. When lipase and kinase activities were measured simultaneously, the formation of phosphatidic acid from a 1-palmitoyl-2-[1-14C]oleoyl-sn-glycerol substrate was 4-fold greater than the release of fatty acid (oleate) from the sn-2 position. Introduction of arachidonic acid to the sn-2 position of the diacylglycerol substrate increased kinase activity but reduced lipase activity. The release of fatty acids from the sn-2 position of phosphatidic acid could not be detected.
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PMID:Diacylglycerol lipase and kinase activities in rat brain microvessels. 298 64

Ten clinical isolates of Pseudomonas cepacia from the sputum of cystic fibrosis patients were examined for the ability to produce lipase. Lipase substrates used included egg yolk agar, four different polyoxyethylene sorbitans (Tweens), and p-nitrophenylphosphorylcholine, a chromogenic substrate used to assay for phospholipase C. Lipase activity was detected in the filtrates of organisms grown to the exponential phase in either tryptose minimal medium or chemically defined medium. Lipase activity increased in the filtrates if the cultures were allowed to proceed into the stationary phase. None of the isolates produced phospholipase C. Lipase activity on Tween 20 ranged from 41.6 X 10(-3) to 640.0 X 10(-3) U/micrograms of protein. The activity was similar or slightly lower when Tween 40, 60, or 80 was used as the substrate. There was no correlation between lipase activity on Tween and that demonstrated on egg yolk agar. Lipase activity increased as pH increased from 7.0 to 9.0. Boiling for 5 min resulted in 66% loss of enzyme activity. The remaining activity continued to decrease with increasing boiling time. The enzyme was purified by gel filtration on Sephadex G-200, and the resultant preparation, when subjected to polyacrylamide gel electrophoresis, resulted in a single protein band (molecular weight, approximately 25,000) from which lipase activity could be eluted. The purified lipase was not cytotoxic to HeLa cells, nor was it toxic when injected intravenously into mice.
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PMID:Production of lipase by clinical isolates of Pseudomonas cepacia. 338 18

Lipase and phospholipase C from Staphylococcus aureus of different origin were demonstrated qualitatively by agar diffusion on tributyrin- and lecithin agar. On test media with either 0,3% Na-azide or 0,3% KCN lipase-activity was not inhibited, phospholipase C, on the other hand, completely blocked (Table 1, Fig. 2). In this manner a tentative differentiation was possible between lipase and phospholipase C. For the quantitative determination of lipase the hydrolysis of p-nitrophenyl palmitate proved to be most useful (Fig. 1). S. aureus-cultures of human origin produced more often and more actively lipase and phospholipase C than those from cattle (Table 2).
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PMID:[Lipase and phospholipase C from Staphylococcus aureus of different origin. I. Determination and occurrence (author's transl)]. 678 82

Lipase and phospholipase C from Staphylococcus aureus could be isolated by gel filtration on Sephacryl S 200 (Fig. 1a, b) and completely separated by refiltration under the same conditions. Isoelectric focusing gave maximal enzyme-activities for lipase at pH 8.6 and 9.5 and for phospholipase C at pH 7.4 (Fig. 2). Thin-layer chromatography revealed that the reaction products in lecithin agar of the phospholipase C-preparations from S. aureus and Bacillus cereus were identical (Table 1).
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PMID:[Lipase and phospholipase from Staphylococcus aureus of different origin. II. Purification and characterization (author's transl)]. 722 22

The tegument of trematodes serves as a dynamic host-parasite interface where surface antigens are shed in a process of immune evasion. Phospholipases, which could provide an enzymatic mechanism for release of glycosylphosphatidylinositol (GPI)-anchored proteins, were detected in detergent extracts of adult worms of Fasciola hepatica and cercaria and adult worms of Schistosoma mansoni. The enzymatic activities were partially characterized from both adult worm species and demonstrated a preference for [3H]GPI substrate over [3H]PI. Lipase activities from both species were sensitive to sulfhydryl-modifying reagents and the detergents CHAPS and n-octylglucoside. The presence of 1 M ammonium sulfate increased the enzyme activity in adult worms of both species by 8-11-fold and in cercaria by 146-fold, whereas other conditions of high ionic strength were inhibitory. Such stimulation suggested dissociation of a negative inhibitor which is prominent in the cercarial stage. The schistosome extract, which was partially sensitive to cation chelators and o-phenanthroline, contained a GPI-phospholipase D activity. In contrast, the F. hepatica extract contained a cation-independent phospholipase C activity which was partially purified and shown by gel filtration to have a molecular mass of 30,000-80,000.
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PMID:Detection and partial characterization of glycosylphosphatidylinositol-specific phospholipase activities from Fasciola hepatica and Schistosoma mansoni. 839 Jun 13

Previously, we have shown that Pseudomonas aeruginosa lipase and phospholipase C (PLC), two extracellular lipolytic enzymes, interact with each other during 12-hydroxyeicosatetraenoic acid (HETE) generation from human platelets. In this regard. the addition of purified P. aeruginosa lipase to PLC-containing crude P. aeruginosa culture supernatants enhances the generation of the chemotactically active 12-HETE from human platelets. Therefore, we analyzed the interaction of purified P. aeruginosa lipase and purified hemolytic P. aeruginosa PLC with regard to inflammatory mediator release from human platelets, neutrophilic and basophilic granulocytes, and monocytes. Purified P. aeruginosa PLC, but not purified lipase by itself, induced 12-HETE generation from human platelets, the generation of leukotriene B4 (LTB4) and oxygen metabolites, enzyme release from human neutrophils, and histamine release from basophils but diminished interleukin-8 (IL-8) release from human monocytes in a dose-dependent manner. The addition of purified lipase enhanced PLC-induced 12-HETE and LTB4 generation, did not influence enzyme, histamine, or IL-8 release, but diminished the PLC-induced chemiluminescent response. Similar results were obtained when the hemolytic PLC from Clostridium perfringens was used instead of P. aeruginosa PLC. For further comparison, we used the well-defined calcium ionophore A23187 and phorbol-12-myristate-13-acetate (PMA) as stimuli. Lipase enhanced calcium ionophore-induced LTB4 generation and beta-glucuronidase release but reduced calcium ionophore-induced and PMA-induced chemiluminescence. In parallel, we analyzed the role of lipase in a crude P. aeruginosa culture supernatant containing PLC and lipase. Lipase activity in the P. aeruginosa culture supernatant was inhibited by treatment with the lipase-specific inhibitor hexadecylsulfonyl fluoride, leaving the activity of PLC unaffected. The capacity of "lipase-inactivated culture supernatant" to induce 12-HETE and LTB4 generation was diminished by 50 to 100%. Our results suggest that the simultaneous secretion of lipase and PLC by P. aeruginosa residing in an infected host may result in severe pathological effects which cannot be explained by the sole action of the individual virulence factor on inflammatory effector cells.
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PMID:Role of Pseudomonas aeruginosa lipase in inflammatory mediator release from human inflammatory effector cells (platelets, granulocytes, and monocytes. 875 61