The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)



Gene Review

PDE2A  -  phosphodiesterase 2A, cGMP-stimulated

Homo sapiens

Synonyms: CGS-PDE, Cyclic GMP-stimulated phosphodiesterase, PDE2A1, PED2A4, cGMP-dependent 3',5'-cyclic phosphodiesterase, ...
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of PDE2A

  • The design of more potent and selective inhibitors of PDE2A for the treatment of heart disease would be greatly aided by the identification of active site residues in PDE2A that determine substrate and inhibitor selectivity [1].

High impact information on PDE2A


Biological context of PDE2A

  • However, other GAF-PDEs, PDE2A and PDE10A, displayed different exon organization from PDE11A although these three PDEs are similar in their amino-acid sequences to each other [6].
  • Here we report an alternative approach to rapidly produce active site mutants of human PDE2A and identify their enzymatic properties using a wheat germ in vitro translation (IVT, also known as cell-free translation) system [1].
  • We also present the crystal structure of the catalytic domain of human PDE2A determined at 1.7 A resolution, which provided a framework for the rational design of active site mutants [1].
  • PDE2A is involved in the regulation of blood pressure and fluid homeostasis by the atrial natriuretic peptide (ANP), making PDE2-type enzymes important targets for drug discovery [1].
  • An inhibitor of platelet PDE2A increases cAMP more than inhibitors of PDE3A but has much less effect on platelet activation, suggesting that these enzymes are present in different compartments of the cell [7].

Anatomical context of PDE2A


Associations of PDE2A with chemical compounds


Other interactions of PDE2A

  • Platelets contain two cAMP phosphodiesterases (PDEs) which regulate intracellular cAMP levels, cGMP-inhibited cAMP PDE (PDE3A) and cGMP-stimulated PDE (PDE2A) [15].
  • Therefore, the GAFa domain of PDE5A adopts a structure similar to the GAFb domain of PDE2A, and provides the sole site for cGMP binding in PDE5A [16].

Analytical, diagnostic and therapeutic context of PDE2A


  1. Structural determinants for inhibitor specificity and selectivity in PDE2A using the wheat germ in vitro translation system. Iffland, A., Kohls, D., Low, S., Luan, J., Zhang, Y., Kothe, M., Cao, Q., Kamath, A.V., Ding, Y.H., Ellenberger, T. Biochemistry (2005) [Pubmed]
  2. Crystal structure of the tandem GAF domains from a cyanobacterial adenylyl cyclase: modes of ligand binding and dimerization. Martinez, S.E., Bruder, S., Schultz, A., Zheng, N., Schultz, J.E., Beavo, J.A., Linder, J.U. Proc. Natl. Acad. Sci. U.S.A. (2005) [Pubmed]
  3. The two GAF domains in phosphodiesterase 2A have distinct roles in dimerization and in cGMP binding. Martinez, S.E., Wu, A.Y., Glavas, N.A., Tang, X.B., Turley, S., Hol, W.G., Beavo, J.A. Proc. Natl. Acad. Sci. U.S.A. (2002) [Pubmed]
  4. Structure and function studies of the cGMP-stimulated phosphodiesterase. Stroop, S.D., Beavo, J.A. J. Biol. Chem. (1991) [Pubmed]
  5. Erythro-9-(2-hydroxy-3-nonyl)adenine inhibits cyclic GMP-stimulated phosphodiesterase in isolated cardiac myocytes. Méry, P.F., Pavoine, C., Pecker, F., Fischmeister, R. Mol. Pharmacol. (1995) [Pubmed]
  6. Genomic organization of the human phosphodiesterase PDE11A gene. Evolutionary relatedness with other PDEs containing GAF domains. Yuasa, K., Kanoh, Y., Okumura, K., Omori, K. Eur. J. Biochem. (2001) [Pubmed]
  7. Platelet cyclic adenosine monophosphate phosphodiesterases: targets for regulating platelet-related thrombosis. Colman, R.W. Semin. Thromb. Hemost. (2004) [Pubmed]
  8. Phenotype-based screening of mechanistically annotated compounds in combination with gene expression and pathway analysis identifies candidate drug targets in a human squamous carcinoma cell model. Fryknäs, M., Rickardson, L., Wickström, M., Dhar, S., Lövborg, H., Gullbo, J., Nygren, P., Gustafsson, M.G., Isaksson, A., Larsson, R. Journal of biomolecular screening : the official journal of the Society for Biomolecular Screening. (2006) [Pubmed]
  9. Isolation and characterization of human cDNAs encoding a cGMP-stimulated 3',5'-cyclic nucleotide phosphodiesterase. Rosman, G.J., Martins, T.J., Sonnenburg, W.K., Beavo, J.A., Ferguson, K., Loughney, K. Gene (1997) [Pubmed]
  10. Differentiation of human monocytes in vitro with granulocyte-macrophage colony-stimulating factor and macrophage colony-stimulating factor produces distinct changes in cGMP phosphodiesterase expression. Bender, A.T., Ostenson, C.L., Giordano, D., Beavo, J.A. Cell. Signal. (2004) [Pubmed]
  11. Differential expression of the cyclic GMP-stimulated phosphodiesterase PDE2A in human venous and capillary endothelial cells. Sadhu, K., Hensley, K., Florio, V.A., Wolda, S.L. J. Histochem. Cytochem. (1999) [Pubmed]
  12. GAF Domains: Two-Billion-Year-Old Molecular Switches that Bind Cyclic Nucleotides. Martinez, S.E., Beavo, J.A., Hol, W.G. Molecular interventions. (2002) [Pubmed]
  13. Bradykinin inhibition of cyclic AMP accumulation in D384 astrocytoma cells. Evidence against a role of cyclic GMP. Altiok, N., Fredholm, B.B. Neurochem. Int. (1992) [Pubmed]
  14. A novel PDE2A reporter cell line: characterization of the cellular activity of PDE inhibitors. Wunder, F., Gnoth, M.J., Geerts, A., Barufe, D. Mol. Pharm. (2009) [Pubmed]
  15. Differential regulation of human platelet responses by cGMP inhibited and stimulated cAMP phosphodiesterases. Manns, J.M., Brenna, K.J., Colman, R.W., Sheth, S.B. Thromb. Haemost. (2002) [Pubmed]
  16. Modeling and mutational analysis of the GAF domain of the cGMP-binding, cGMP-specific phosphodiesterase, PDE5. Sopory, S., Balaji, S., Srinivasan, N., Visweswariah, S.S. FEBS Lett. (2003) [Pubmed]
WikiGenes - Universities