cam-3

PDE1C belongs to the cyclic nucleotide phosphodiesterase family, PDE1 subfamily. Phosphodiesterases (PDEs) are a family of related phosphohydrolyases that selectively catalyze the hydrolysis of 3' cyclic phosphate bonds in adenosine and or guanine 3',5' cyclic monophosphate (cAMP and or cGMP). They regulate the cellular levels, localization and duration of action of these second messengers by controlling the rate of their degradation. PDEs are expressed ubiquitously, with each subtype having a specific tissue distribution. These enzymes are involved in many signal transduction pathways and their functions include vascular smooth muscle proliferation and contraction, cardiac contractility, platelet aggregation, hormone secretion, immune cell activation, and they are involved in learning and memory. PDE1C has a high affinity for both cAMP and cGMP. It is expressed in several tissues, including brain and heart. As a cyclic nucleotide phosphodiesterase, PDE1C has a dual-specificity for the second messengers cAMP and cGMP.

Calcium calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1B, also known as Cam-PDE 1B and PDE1B, is a cytoplasm protein that belongs to the cyclic nucleotide phosphodiesterase family and PDE1 subfamily. Phosphodiesterase-1A (PDE1A), Phosphodiesterase-1B (PDE1B), Phosphodiesterase-4B (PDE4B), and Phosphodiesterase-4A (PDE4A) are important regulators of signal transduction in striatum due to their catalysis of cyclic AMP and cyclic GMP. PDE1B is highly expressed in the striatum. It binds two divalent metal cations per subunit. Site one of PDE1B may preferentially bind zinc ions, while site two of PDE1B has a preference for magnesium and or manganese ions. PDE1B is a cyclic nucleotide phosphodiesterase with a dual-specificity for the second messengers cAMP and cGMP, which are key regulators of many important physiological processes. It has a preference for cGMP as a substrate.

Calmodulin (CaM) is a multifunctional intermediate calcium-binding messenger protein expressed in all eukaryotic cells. It is an intracellular target of the secondary messenger Ca2+, and the binding of Ca2+ is required for the activation of Calmodulin. Once bound to Ca2+, Calmodulin acts as part of a calcium signal transduction pathway by modifying its interactions with various target proteins such as kinases or phosphatases. Calmodulin is a small, highly conserved protein that is 148 amino acids long. The protein has two approximately symmetrical globular domains each containing a pair of EF-hand motifs (the N- and C-domain) separated by a flexible linker region for a total of four Ca2+ binding sites. Calmodulin mediates many crucial processes such as inflammation, metabolism, apoptosis, smooth muscle contraction, intracellular movement, short-term and long-term memory, and the immune response. Calmodulin is expressed in many cell types and can have different subcellular locations, including the cytoplasm, within organelles, or associated with the plasma or organelle membranes, but it is always found intracellularly.