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Regulation of platelet phospholipase C [PDF]
Philosophical Transactions of the Royal Society of London. B, Biological Sciences, 1988 We have investigated factors affecting the activation of phospholipase C in human platelets. Prior exposure of platelets to phorbol esters that stimulate protein kinase C inhibits the activation of phospholipase C in response to a variety of receptor-directed agonists, including x- and y-thrombin and thromboxane A 2
S. E. Rittenhouse +4 more
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Inhibition of phospholipase A2 and phospholipase C by polyamines
Archives of Biochemistry and Biophysics, 1978Abstract The polyamines spermine, spermidine, and putrescine inhibit the activity of phospholipase A2 (Naja naja) and phospholipase C (Clostridium welchii) on phospholipid vesicles and mitochondrial membranes as sources of substrate phospholipids. The inhibitory effect is highest for spermine and lowest for putrescine.
P. Pasquali +4 more
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The effect of phospholipase C in sheep
Scandinavian Journal of Clinical & Laboratory Investigation, 1983Based on earlier studies in rats, phospholipase C (PLC) seemed to be a very promising prophylactic agent for certain types of thrombo-embolic disease. Recent studies in rabbits have, however, demonstrated that phospholipase C is more toxic than expected from the previous data.
E. Carlsen, C. F. Lindboe, Ø. Hetland
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Toxicity of phospholipase C in rabbits
Scandinavian Journal of Clinical and Laboratory Investigation, 1982Tissue thromboplastin is the most potent physiological trigger of blood coagulation and is probably involved in the pathogenesis of several forms of intravascular coagulation. Phospholipase C from Bacillus cereus is an effective inhibitor of thromboplastin.
Hans Prydz +4 more
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Regulation of phospholipase C isozymes
Progress in Growth Factor Research, 1992Phosphatidylinositol bisphosphate hydrolysis is an immediate response to many hormones, including growth factors. The hydrolysis of phosphatidylinositol bisphosphate is catalyzed by phosphatidylinositol-specific phospholipase C. A number of phospholipase C isozymes have been identified.
Gwenith Jones, Graham Carpenter
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Selective phospholipase C activation
BioEssays, 1991AbstractPhospholipase C is a family of cellular proteins believed to play a significant role in the intracellular signaling mechanisms utilized by diverse hormones. One class of hormones, polypeptide growth factors, elicits its influence on cellular function through stimulation of cell surface receptor tyrosine kinase activity.
Graham Carpenter, Matthew I. Wahl
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[23] Assay for phospholipase C
1981Publisher Summary This chapter discusses the different aspects of assay for phospholipase C. Phospholipase C has become a powerful tool for studying lipid–protein interactions and membrane structure and function. Use of phospholipase C for such studies necessitates the availability of a convenient assay for enzyme activity.
Claudia Kent, Edward L. Krug
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2003
Publisher Summary This chapter focuses on the phosphoinositide-specific phospholipase C (PLC) isozymes expressed in mammalian cells. It discusses molecular structure/function and activation mechanisms for phospholipase C enzymes and presents the physiologic consequences of PLC genetic knockouts.
Graham Carpenter, Hong-Jun Liao
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Publisher Summary This chapter focuses on the phosphoinositide-specific phospholipase C (PLC) isozymes expressed in mammalian cells. It discusses molecular structure/function and activation mechanisms for phospholipase C enzymes and presents the physiologic consequences of PLC genetic knockouts.
Graham Carpenter, Hong-Jun Liao
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A simplified assay for phospholipase C
Analytical Biochemistry, 1979Abstract A new assay for phospholipase C activity that uses alkaline phosphatase to convert phosphorylcholine to inorganic phosphate is described. The determination of inorganic phosphate is performed in the presence of phosphatidylcholine and protein after the addition of sodium dodecyl sulfate.
Nancy J. Truesdale +2 more
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Aspirin inhibits phospholipase C
Biochemical and Biophysical Research Communications, 1986We have shown previously that aspirin (ASA) ingestion by normal human volunteers inhibits peripheral blood monocyte phospholipase C (PLC) activities ex vivo. In order to explore further the mechanism of action of ASA, normal human monocytes and differentiated human U937 cells were treated with ASA and other salicylates. Cells preincubated with ASA were
Mike A. Clark +2 more
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