Abstract
Cyclic nucleotide phosphodiesterases (PDEs) constitute a complex group of enzymes, multiple forms of which are found in various amounts and proportions in most mammalian cells. These enzymes differ in subcellular localization, substrate affinities, kinetic characteristics, physiochemical properties, responsiveness to various effectors or drugs and mechanisms of regulation (Wells et al., 1977; Beavo et al., 1982; Manganiello et al., 1987). At least 6-7 distinct major classes of PDEs have been isolated, purified and characterized. One class, the cGMP inhibited low Km PDE (hereafter referred as cGI-PDE) is very sensitive to inhibition by a number of inotropic and antithrombotic agents including cilostamide and other OPC derivatives, imazodan, milrinone, fenoxamine, LY 195115, Y 590, anegrelide. Inhibition of cGI-PDEs from heart and platelets by therapeutically effective concentrations of these drugs correlates with physiological effects.
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Rascon, A. et al. (1990). Purification of a cGMP-inhibited cAMP Phosphodiesterase from Vascular Smooth Muscle. In: Jacobson, K.A., Daly, J.W., Manganiello, V. (eds) Purines in Cellular Signaling. Springer, New York, NY. https://doi.org/10.1007/978-1-4612-3400-5_51
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DOI: https://doi.org/10.1007/978-1-4612-3400-5_51
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