Protein Kinase C-mediated Phosphorylation and Activation of PDE3A Regulate cAMP Levels in Human Platelets

The elevation of [cAMP]i is an important mechanism of platelet inhibition and is regulated by the opposing activity of adenylyl cyclase and phosphodiesterase (PDE). In this study, we demonstrate that a variety of platelet agonists, including thrombin, significantly enhance the activity of PDE3A in a...

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Veröffentlicht in:	The Journal of biological chemistry 2009-05, Vol.284 (18), p.12339-12348
Hauptverfasser:	Hunter, Roger W., MacKintosh, Carol, Hers, Ingeborg
Format:	Artikel
Sprache:	eng
Schlagworte:	14-3-3 Proteins - metabolism Alprostadil - pharmacology Blood Platelets - enzymology Blood Proteins - metabolism Cyclic AMP - metabolism Cyclic Nucleotide Phosphodiesterases, Type 3 - metabolism Enzyme Activation - drug effects Enzyme Activation - physiology Hemostatics - pharmacology Humans Hydrolysis - drug effects Mechanisms of Signal Transduction Peptide Fragments - pharmacology Phosphoproteins - metabolism Phosphorylation - drug effects Phosphorylation - physiology Platelet Activation - drug effects Platelet Activation - physiology Platelet Aggregation Inhibitors - pharmacology Protein Binding - drug effects Protein Binding - physiology Protein Kinase C - metabolism Receptor, PAR-1 - agonists Receptor, PAR-1 - metabolism Thrombin - pharmacology
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