Cyclic nucleotide phosphodiesterase (PDE) was demonstrated after the discovery of cAMP (Sutherland and Rall 1958). In most tissues, PDE exists in multiple forms which differ in subcellular localization, relative substrate specificity toward cAMP and cGMP, regulatory and immunological properties (Beavo 1995; Kakkar et al. 1999; Goraya and Cooper 2005). Most tissues examined have been shown to contain Ca2+ and calmodulin (CaM)-dependent cyclic nucleotide phosphodiesterase 1 (PDE1) and this enzyme has been intensively studied (Beavo 1995; Kakkar et al. 1999). Earlier, it was suggested that PDE1 consists of a single species (Wells and Hardman 1977), but later found to exist as a tissue-specific and immunological distinct enzyme (Sharma et al. 1984). With the rapidly expanding list of PDE1 isozymes, a new nomenclature was developed based on the primary structure of different PDEs (Beavo et al. 1994...
- Beavo JA, Conti M, Healip RJ. Multiple cyclic nucleotide phosphodiesterases. Mol Pharmacol. 1994;75:399–405.Google Scholar
- Klee CB. Interaction of calmodulin with Ca2+ and target proteins. In: Cohen P, Klee CB, editors. Molecular aspects of cell regulation. 5 New York: Elsevier Science; 1988. p. 35–56.Google Scholar
- Zhang GY, Wang JH, Sharma RK. Purification and characterization of bovine brain calmodulin-dependent protein kinase II. The significance of autophosphorylation in the regulation of 63 kDa calmodulin-dependent cyclic nucleotide phosphodiesterase isozyme. Mol Cell Biochem. 1993a;122:159–69.CrossRefPubMedGoogle Scholar