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Gene Review

PDE1A  -  phosphodiesterase 1A, calmodulin-dependent

Homo sapiens

Synonyms: 61 kDa Cam-PDE, CAM-PDE-1A, Calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1A, Cam-PDE 1A, HCAM-1, ...
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Disease relevance of PDE1A

  • In 1321N1 human astrocytoma cells, the endogenous PDE1 (identified as PDE1A by reverse transcriptase-PCR) was largely insensitive to Ca2+ released from carbachol-sensitive stores but was robustly stimulated by a similar rise in [Ca2+]i due to carbachol-induced Ca2+ influx [1] .

High impact information on PDE1A

  • Remission on antidepressants was significantly associated with polymorphisms in PDE1A and PDE11A [2].
  • Gd3+, which effectively blocked thapsigargin-induced CCE and its effect on PDE1A, also inhibited the activation of PDE1A by carbachol-induced Ca2+ entry [1].
  • However, non-selective ionomycin-mediated Ca2+ entry also activated PDE1A, so that, unlike Ca2+-sensitive ACs, PDE1A cannot discriminate between the different sources of Ca2+ entry [1].
  • RNase protection studies indicated that Hcam1 is represented in human RNA from several tissues, including brain, kidney, testes, and heart [3].
  • The present data provide evidence of expression of PDE1 isoforms in mammalian retina with a complementary distribution of PDE1A and PDE1C, suggesting different roles in retinal function [4].

Biological context of PDE1A

  • We report here the identification of novel human PDE1A splice variants, their tissue distribution patterns, genomic structure, and chromosomal localization of the gene [5].
  • These findings suggest that the distinct expression patterns among PDE1A variants depend on the several promoters situated upstream of exons encoding 5' ends of the variants [5].
  • Reducing PDE1A function significantly attenuated VSMC growth by decreasing proliferation via G1 arrest and inducing apoptosis [6].
  • The PDE1A gene was located on human chromosome 2q32 by fluorescent in situ hybridization analysis [5].
  • The PDE1A gene spans over 120 kb of genomic DNA, and consists of at least 17 exons and 16 introns [5].

Anatomical context of PDE1A

  • These results suggest that PDE1A is permanently activated in human spermatozoa [7].
  • Immunocytochemical data indicated that PDE1A, a variant of PDE1, is localized on the equatorial segment of the sperm head as well as on the mid and principal pieces of the flagellum, and that PDE3A is found on the postacrosomal segment of the sperm head [7].
  • We examined the spatial and temporal expression profiles of three knownCaM-PDE genes, PDE1A, PDE1B, and PDE1C, in the testis [8].
  • Immunohistochemical analysis showed a distribution of PDE1A in the outer retina with a bright fluorescence in the outer segments of photoreceptors [4].
  • More specifically, PDE1A mRNA is found in round to elongated spermatids, with protein expression in the tails of elongated and maturing spermatids [8].

Associations of PDE1A with chemical compounds

  • PDE1A activity in whole sperm extract or after partial purification by anion-exchange chromatography was not stimulated by calcium + calmodulin [7].
  • The calcium surge associated with vasoconstrictor initiated contraction also activates a calcium/calmodulin-dependent PDE (PDE1A) [9].
  • These N- and C-termini, including the reported N-termini (N1 and N2) and C-termini (C1 and C2), combined to generate nine different PDE1A cDNAs [5].
  • In individual patients deficiencies or over-expression of the beta1 integrin chain, VLA-4, PECAM-1 or HCAM also occurred [10].
  • The Selectin family and HCAM are carbohydrate-binding proteins, and play a prominent role in the circulation of lymphocytes and neoplastic cells [11].

Other interactions of PDE1A

  • Presence of cyclic nucleotide phosphodiesterases PDE1A, existing as a stable complex with calmodulin, and PDE3A in human spermatozoa [7].
  • Together, PDE5 and PDE1A lower cGMP sufficiently to allow contraction [9].

Analytical, diagnostic and therapeutic context of PDE1A



  1. Sustained entry of Ca2+ is required to activate Ca2+-calmodulin-dependent phosphodiesterase 1A. Goraya, T.A., Masada, N., Ciruela, A., Cooper, D.M. J. Biol. Chem. (2004) [Pubmed]
  2. Phosphodiesterase genes are associated with susceptibility to major depression and antidepressant treatment response. Wong, M.L., Whelan, F., Deloukas, P., Whittaker, P., Delgado, M., Cantor, R.M., McCann, S.M., Licinio, J. Proc. Natl. Acad. Sci. U.S.A. (2006) [Pubmed]
  3. Isolation and characterization of cDNAs corresponding to two human calcium, calmodulin-regulated, 3',5'-cyclic nucleotide phosphodiesterases. Loughney, K., Martins, T.J., Harris, E.A., Sadhu, K., Hicks, J.B., Sonnenburg, W.K., Beavo, J.A., Ferguson, K. J. Biol. Chem. (1996) [Pubmed]
  4. Gene expression and protein localization of calmodulin-dependent phosphodiesterase in adult rat retina. Santone, R., Giorgi, M., Maccarone, R., Basso, M., Deplano, S., Bisti, S. J. Neurosci. Res. (2006) [Pubmed]
  5. Human Ca2+/calmodulin-dependent phosphodiesterase PDE1A: novel splice variants, their specific expression, genomic organization, and chromosomal localization. Michibata, H., Yanaka, N., Kanoh, Y., Okumura, K., Omori, K. Biochim. Biophys. Acta (2001) [Pubmed]
  6. Role of nuclear Ca2+/calmodulin-stimulated phosphodiesterase 1A in vascular smooth muscle cell growth and survival. Nagel, D.J., Aizawa, T., Jeon, K.I., Liu, W., Mohan, A., Wei, H., Miano, J.M., Florio, V.A., Gao, P., Korshunov, V.A., Berk, B.C., Yan, C. Circ. Res. (2006) [Pubmed]
  7. Presence of cyclic nucleotide phosphodiesterases PDE1A, existing as a stable complex with calmodulin, and PDE3A in human spermatozoa. Lefièvre, L., de Lamirande, E., Gagnon, C. Biol. Reprod. (2002) [Pubmed]
  8. Stage and cell-specific expression of calmodulin-dependent phosphodiesterases in mouse testis. Yan, C., Zhao, A.Z., Sonnenburg, W.K., Beavo, J.A. Biol. Reprod. (2001) [Pubmed]
  9. Cyclic GMP phosphodiesterases and regulation of smooth muscle function. Rybalkin, S.D., Yan, C., Bornfeldt, K.E., Beavo, J.A. Circ. Res. (2003) [Pubmed]
  10. Different expression of adhesion molecules on CD34+ cells in AML and B-lineage ALL and their normal bone marrow counterparts. De Waele, M., Renmans, W., Jochmans, K., Schots, R., Lacor, P., Trullemans, F., Otten, J., Balduck, N., Vander Gucht, K., Van Camp, B., Van Riet, I. Eur. J. Haematol. (1999) [Pubmed]
  11. Cell adhesion molecules: a unifying approach to topographic biology. Turner, M.L. Biological reviews of the Cambridge Philosophical Society. (1992) [Pubmed]
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