PDE3A is a member of the phosphodiesterase family of proteins that play a critical role in regulating intracellular levels of cAMP and cGMP. PDE3A has high affinity for both cAMP and cGMP and shows competitive inhibition of the cAMP hydrolytic activity by cGMP (1). Deletion of the N-terminus of PDE3A enhances the hydrolysis of cGMP relative to cAMP suggesting that the role of divergent N-termini of various PDEs could be to exert substrate specificity. Stimulation of platelets with thrombin increases PDE3A activity via Akt signaling pathway and this increase can be diminished by dephosphorylation of PDE3A by protein phosphatase 1 (2).
1. Meacci E, et al: Molecular cloning and expression of human myocardial cGMP-inhibited cAMP phosphodiesterase. Proc. Nat. Acad. Sci. 89: 3721-3725, 1992.
2. Zhang W, et al: Thrombin regulates intracellular cyclic AMP concentration in human platelets through phosphorylation/activation of phosphodiesterase 3A. Blood. 2007 Sep 1;110(5):1475-82.
Sample Phosphodiesterase Activity Plot. For specific information on a given lot, see related technical data sheet.
Sample Purity Data. For specific information on a given lot, see related technical data sheet.
Storage, Stability and Shipping:
Store product at –70oC. For optimal storage, aliquot target into smaller quantities after centrifugation and store at recommended temperature. For most favorable performance, avoid repeated handling and multiple freeze/thaw cycles.
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Cardiovascular Disease, Inflammation, Phosphodiesterases