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Gene Review

PDE3B  -  phosphodiesterase 3B, cGMP-inhibited

Homo sapiens

Synonyms: CGI-PDE B, CGIP1, CGIPDE1, Cyclic GMP-inhibited phosphodiesterase B, HcGIP1, ...
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Disease relevance of PDE3B


High impact information on PDE3B

  • Moreover, the serine-273 mutant of PDE3B was not activated by insulin when expressed in adipocytes [6].
  • In contrast, PDE3B mutants in which alanine was substituted for either serine-296 or serine-421, each of which lies within a sequence (RRXS) preferentially phosphorylated by cAMP-dependent protein kinase, were phosphorylated by Akt in vitro or in response to insulin in intact cells [6].
  • Insulin activates the 3B isoform of PDE in adipocytes in a phosphoinositide 3-kinase-dependent manner; however, downstream effectors that mediate signaling to PDE3B remain unknown [6].
  • Finally, TNF-alpha decreased the expression of cyclic-nucleotide phosphodiesterase 3B (PDE3B) by approximately 50%, delineating a mechanism by which TNF-alpha could increase intracellular cAMP [7].
  • Ceramide is the suggested second messenger of TNF-alpha action, and in this study, we used 3T3-L1 adipocytes to investigate the effects of C(2)-ceramide (a short-chain ceramide analog) on the expression and regulation of PDE3B and lipolysis [8].

Biological context of PDE3B


Anatomical context of PDE3B


Associations of PDE3B with chemical compounds


Regulatory relationships of PDE3B

  • PI3Kgamma regulates cardiac cAMP homoeostasis by forming a macromolecular complex containing PDE3B (phosphodiesterase 3B) [16].

Other interactions of PDE3B


Analytical, diagnostic and therapeutic context of PDE3B


  1. Crystal structure of human phosphodiesterase 3B: atomic basis for substrate and inhibitor specificity. Scapin, G., Patel, S.B., Chung, C., Varnerin, J.P., Edmondson, S.D., Mastracchio, A., Parmee, E.R., Singh, S.B., Becker, J.W., Van der Ploeg, L.H., Tota, M.R. Biochemistry (2004) [Pubmed]
  2. The role of tryptophan 1072 in human PDE3B inhibitor binding. Chung, C., Varnerin, J.P., Morin, N.R., MacNeil, D.J., Singh, S.B., Patel, S., Scapin, G., Van der Ploeg, L.H., Tota, M.R. Biochem. Biophys. Res. Commun. (2003) [Pubmed]
  3. Analysis of the insulin-sensitive phosphodiesterase 3B gene in type 2 diabetes. Sano, R., Miki, T., Suzuki, Y., Shimada, F., Taira, M., Kanatsuka, A., Makino, H., Hashimoto, N., Saito, Y. Diabetes Res. Clin. Pract. (2001) [Pubmed]
  4. Multisite phosphorylation of adipocyte and hepatocyte phosphodiesterase 3B. Lindh, R., Ahmad, F., Resjö, S., James, P., Yang, J.S., Fales, H.M., Manganiello, V., Degerman, E. Biochim. Biophys. Acta (2007) [Pubmed]
  5. Adenovirus-mediated overexpression of murine cyclic nucleotide phosphodiesterase 3B. Ahmad, F., Härndahl, L., Tang, Y., Holst, L.S., Manganiello, V.C. Methods Mol. Biol. (2005) [Pubmed]
  6. Insulin-induced phosphorylation and activation of cyclic nucleotide phosphodiesterase 3B by the serine-threonine kinase Akt. Kitamura, T., Kitamura, Y., Kuroda, S., Hino, Y., Ando, M., Kotani, K., Konishi, H., Matsuzaki, H., Kikkawa, U., Ogawa, W., Kasuga, M. Mol. Cell. Biol. (1999) [Pubmed]
  7. Tumor necrosis factor-alpha stimulates lipolysis in differentiated human adipocytes through activation of extracellular signal-related kinase and elevation of intracellular cAMP. Zhang, H.H., Halbleib, M., Ahmad, F., Manganiello, V.C., Greenberg, A.S. Diabetes (2002) [Pubmed]
  8. C(2)-ceramide influences the expression and insulin-mediated regulation of cyclic nucleotide phosphodiesterase 3B and lipolysis in 3T3-L1 adipocytes. Mei, J., Holst, L.S., Landström, T.R., Holm, C., Brindley, D., Manganiello, V., Degerman, E. Diabetes (2002) [Pubmed]
  9. Effect of type-selective inhibitors on cyclic nucleotide phosphodiesterase activity and insulin secretion in the clonal insulin secreting cell line BRIN-BD11. Ahmad, M., Abdel-Wahab, Y.H., Tate, R., Flatt, P.R., Pyne, N.J., Furman, B.L. Br. J. Pharmacol. (2000) [Pubmed]
  10. Cyclic AMP phosphodiesterases in human lymphocytes. Sheth, S.B., Chaganti, K., Bastepe, M., Ajuria, J., Brennan, K., Biradavolu, R., Colman, R.W. Br. J. Haematol. (1997) [Pubmed]
  11. Cyclic nucleotide phosphodiesterases in pancreatic islets. Pyne, N.J., Furman, B.L. Diabetologia (2003) [Pubmed]
  12. Dual expression and differential regulation of phosphodiesterase 3A and phosphodiesterase 3B in human vascular smooth muscle: implications for phosphodiesterase 3 inhibition in human cardiovascular tissues. Palmer, D., Maurice, D.H. Mol. Pharmacol. (2000) [Pubmed]
  13. Membrane localization of cyclic nucleotide phosphodiesterase 3 (PDE3). Two N-terminal domains are required for the efficient targeting to, and association of, PDE3 with endoplasmic reticulum. Shakur, Y., Takeda, K., Kenan, Y., Yu, Z.X., Rena, G., Brandt, D., Houslay, M.D., Degerman, E., Ferrans, V.J., Manganiello, V.C. J. Biol. Chem. (2000) [Pubmed]
  14. Inhibition of PDE3B augments PDE4 inhibitor-induced apoptosis in a subset of patients with chronic lymphocytic leukemia. Moon, E., Lee, R., Near, R., Weintraub, L., Wolda, S., Lerner, A. Clin. Cancer Res. (2002) [Pubmed]
  15. Characterization of the cDNA and gene encoding human PDE3B, the cGIP1 isoform of the human cyclic GMP-inhibited cyclic nucleotide phosphodiesterase family. Miki, T., Taira, M., Hockman, S., Shimada, F., Lieman, J., Napolitano, M., Ward, D., Taira, M., Makino, H., Manganiello, V.C. Genomics (1996) [Pubmed]
  16. Identification of the macromolecular complex responsible for PI3Kgamma-dependent regulation of cAMP levels. Perino, A., Ghigo, A., Damilano, F., Hirsch, E. Biochem. Soc. Trans. (2006) [Pubmed]
  17. Differential expression of PDE4 cAMP phosphodiesterase isoforms in inflammatory cells of smokers with COPD, smokers without COPD, and nonsmokers. Barber, R., Baillie, G.S., Bergmann, R., Shepherd, M.C., Sepper, R., Houslay, M.D., Heeke, G.V. Am. J. Physiol. Lung Cell Mol. Physiol. (2004) [Pubmed]
  18. Long-term regulation of cyclic nucleotide phosphodiesterase type 3B and 4 in 3T3-L1 adipocytes. Oknianska, A., Zmuda-Trzebiatowska, E., Manganiello, V., Degerman, E. Biochem. Biophys. Res. Commun. (2007) [Pubmed]
  19. Plasma membrane cyclic nucleotide phosphodiesterase 3B (PDE3B) is associated with caveolae in primary adipocytes. Nilsson, R., Ahmad, F., Swärd, K., Andersson, U., Weston, M., Manganiello, V., Degerman, E. Cell. Signal. (2006) [Pubmed]
  20. Expression, refolding, and purification of recombinant human phosphodiesterase 3B: definition of the N-terminus of the catalytic core. Varnerin, J.P., Chung, C.C., Patel, S.B., Scapin, G., Parmee, E.R., Morin, N.R., MacNeil, D.J., Cully, D.F., Van der Ploeg, L.H., Tota, M.R. Protein Expr. Purif. (2004) [Pubmed]
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