Abstract
Platelets play a central role in thrombosis and hemostasis. In human platelets, an increase in intracellular levels of cAMP and cGMP is associated with the inhibition of agonist-evoked platelet responses including change of cell shape, adhesion, aggregation, and release of granule content (for a review see Siess 1989). Cyclic nucleotide phosphodiesterases (PDEs) catalyze the hydrolysis of 3′–5′-cyclic nucleotides to the corresponding nucleoside 5′-monophosphates and thereby play a crucial part in the regulation of cyclic nucleotide concentrations (Beavo and Reifsnyder 1990; Beltman et al. 1993). Currently, seven different but homologous PDE families are recognized, and most of these families contain multiple isoforms (Beavo 1995). In human platelets three distinct forms of cyclic nucleotide PDEs exist that differ in their kinetic and physical characteristics, substrate selectivities (cAMP or cGMP) as well as their regulation by various natural and pharmacological agents. These three PDEs are cGMP-stimulated phosphodiesterase type II (cGS-PDE) with a Km of 35 µM for cGMP and 50 µM for cAMP (Grant et al. 1990), the cGMP-inhibited phosphodiesterase type III (cGI-PDE) with the lowest Km (0.02 μM) for cGMP and a Km of 0.2 µM for cAMP (Grant et al. 1992), and the cGMP-specific PDE type V. PDE V hydrolyzes cGMP (Km = 5 µM) at a rate approximately 100 times faster than the hydrolytic rate for cAMP (Hamet et al. 1984; Table 1).
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Butt, E., Walter, U. (1997). Platelet Phosphodiesterases. In: von Bruchhausen, F., Walter, U. (eds) Platelets and Their Factors. Handbook of Experimental Pharmacology, vol 126. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-60639-7_10
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DOI: https://doi.org/10.1007/978-3-642-60639-7_10
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