Stimulation of cyclic nucleotide phosphodiesterase by products of phosphatidylinositol metabolism catalyzed by phospholipase A2 |
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Authors: | H H Tai C L Tai |
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Institution: | Department of Biochemistry, North Texas State University Health Science Center/Texas College of Osteopathic Medicine, Denton, Texas 76203 USA |
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Abstract: | Products of phospholipase A2-catalyzed hydrolysis of phosphatidylinositol, lysophosphatidylinositol, and unsaturated fatty acid are very effective stimulators of a partially purified bovine brain cyclic nucleotide phosphodiesterase. More than 10-fold of calcium-independent stimulation can be achived by lysophatidylinositol or oleic acid. The degree of stimulation is comparable to that by calcium-mediated calmodulin. The other lysophospholipid which shows comparable stimulation is lysophosphatidylserine although at a higher concentration. Diacylphosphoglycerides are inactive. Kinetic studies showed that lysophosphatidylinositol, like calmodulin, increased the Vmax without affecting the apparent Km for adenosine 3′,5′-cyclic phosphate (cAMP). |
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Keywords: | To whom correspondence concerning this paper should be addressed at the present address: College of Pharmacy University of Kentucky Lexington Ky 40506 |
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