Formation of diacylglycerol by a phospholipase D-phosphatidate phosphatase pathway specific for phosphatidylcholine in endothelial cells
作者： Thomas W. Martin
DOI: 10.1016/0005-2760(88)90258-5
关键词: Phosphatidate phosphatase 、 Phosphatidylcholine 、 Phospholipase 、 Phospholipase D 、 Biochemistry 、 Phosphocholine 、 Phosphatase 、 Diacylglycerol kinase 、 Phosphatidate 、 Chemistry 、 Biophysics 、 Endocrinology
摘要: Abstract The conversion of phosphatidylcholine (PC) to diacylglycerol (DAG) was studied in sonicated endothelial cells and subcellular fractions the presence 0.05% Triton X-100 2 mM EDTA. DAG formation occurred predominantly an organelle fraction that sedimented at 15 000 × g. In parallel reactions with exogenous 1-oleoyl-2-[3H]oleoyl-PC ( sn-2-[ 3 H] DOPC ) phosphatidyl[3H]choline ([choline-3H]PC), [3H]DAG formed by a reaction pathway which [3H]choline only product derived from [choline-3H]PC. [3H]Choline not secondarily [3H]glycerophosphocholine or [3H]phosphocholine. Small amounts [3H]phosphatidate ([3H]PA) were isolated short incubation times, substantial PA phosphatase activity demonstrated. These data, taken together, supported phospholipase D-PA formation. Kinetic data established low ratio [3H]PA/[3H]DAG due 15-fold higher Vmax 7-fold lower apparent Km phosphatase. increased addition unlabeled selective extraction D X-100. characteristics indicated unique enzyme. Activity optimal EDTA almost totally dependent upon pH profile displayed peak 7.0. Of particular significance stringent substrate specificity. Phosphatidylinositol hydrolyzed, activities towards phosphatidylethanolamine sphingomyelin most 30- 50-fold than those PC. Phospholipase identified number rat tissues other cells. highest present lung partially purified anion exchange chromatography. When linked phosphatase, could initiate is highly specific for
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