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Volumn 28, Issue 6, 2014, Pages 593-607

Temporal and spatial regulation of cAMP signaling in disease: Role of cyclic nucleotide phosphodiesterases

Author keywords

CAMP; Compartmentalization; Phosphodiesterase

Indexed keywords

CYCLIC AMP; CYCLIC NUCLEOTIDE PHOSPHODIESTERASE; PHOSPHODIESTERASE;

EID: 84911892966     PISSN: 07673981     EISSN: 14728206     Source Type: Journal    
DOI: 10.1111/fcp.12080     Document Type: Article
Times cited : (19)

References (234)
  • 1
    • 41449118891 scopus 로고    scopus 로고
    • Chapter 6 regulation of hippocampus-dependent memory by cyclic AMP-dependent protein kinase
    • Abel T., Nguyen P.V. Chapter 6 regulation of hippocampus-dependent memory by cyclic AMP-dependent protein kinase. Prog. Brain Res. (2008) 169 97-115.
    • (2008) Prog. Brain Res. , vol.169 , pp. 97-115
    • Abel, T.1    Nguyen, P.V.2
  • 2
    • 0035798238 scopus 로고    scopus 로고
    • The molecular biology of memory storage: a dialogue between genes and synapses
    • Kandel E.R. The molecular biology of memory storage: a dialogue between genes and synapses. Biosci. Rep. (2001) 294 1030-1038.
    • (2001) Biosci. Rep. , vol.294 , pp. 1030-1038
    • Kandel, E.R.1
  • 3
    • 84860806555 scopus 로고    scopus 로고
    • The molecular biology of memory: cAMP, PKA, CRE, CREB-1, CREB-2, and CPEB
    • Kandel E. The molecular biology of memory: cAMP, PKA, CRE, CREB-1, CREB-2, and CPEB. Mol. Brain (2012) 5 14.
    • (2012) Mol. Brain , vol.5 , pp. 14
    • Kandel, E.1
  • 4
    • 33645863768 scopus 로고    scopus 로고
    • Transcriptional regulation of metabolism
    • Desvergne B., Michalik L., Wahli W. Transcriptional regulation of metabolism. Physiol. Rev. (2006) 86 465-514.
    • (2006) Physiol. Rev. , vol.86 , pp. 465-514
    • Desvergne, B.1    Michalik, L.2    Wahli, W.3
  • 5
    • 77956211931 scopus 로고    scopus 로고
    • Distinct roles of adenylyl cyclase VII in regulating the immune responses in mice
    • Duan B., Davis R., Sadat E.L. et al. Distinct roles of adenylyl cyclase VII in regulating the immune responses in mice. J. Immunol. (2010) 185 335-344.
    • (2010) J. Immunol. , vol.185 , pp. 335-344
    • Duan, B.1    Davis, R.2    Sadat, E.L.3
  • 6
    • 0347990624 scopus 로고    scopus 로고
    • Epac: a new cAMP-binding protein in support of glucagon-like peptide-1 receptor-mediated signal transduction in the pancreatic β-cell
    • Holz G.G. Epac: a new cAMP-binding protein in support of glucagon-like peptide-1 receptor-mediated signal transduction in the pancreatic β-cell. Diabetes (2004) 53 5-13.
    • (2004) Diabetes , vol.53 , pp. 5-13
    • Holz, G.G.1
  • 9
    • 47849093381 scopus 로고    scopus 로고
    • Mechanisms underlying proglucagon gene expression
    • Jin T. Mechanisms underlying proglucagon gene expression. J. Endocrinol. (2008) 198 17-28.
    • (2008) J. Endocrinol. , vol.198 , pp. 17-28
    • Jin, T.1
  • 10
    • 36148965480 scopus 로고    scopus 로고
    • The funny current
    • DiFrancesco D., Borer J. The funny current. Drugs (2007) 67 15-24.
    • (2007) Drugs , vol.67 , pp. 15-24
    • DiFrancesco, D.1    Borer, J.2
  • 11
    • 50349096521 scopus 로고    scopus 로고
    • Genesis and regulation of the heart automaticity
    • Mangoni M.E., Nargeot J. Genesis and regulation of the heart automaticity. Physiol. Rev. (2008) 88 919-982.
    • (2008) Physiol. Rev. , vol.88 , pp. 919-982
    • Mangoni, M.E.1    Nargeot, J.2
  • 12
    • 61949445173 scopus 로고    scopus 로고
    • Distinct phosphodiesterase-4D variants integrate into protein kinase A-based signaling complexes in cardiac and vascular myocytes
    • Raymond D.R., Carter R.L., Ward C.A., Maurice D.H. Distinct phosphodiesterase-4D variants integrate into protein kinase A-based signaling complexes in cardiac and vascular myocytes. Am. J. Physiol. Heart Circ. Physiol. (2009) 296 H263-H271.
    • (2009) Am. J. Physiol. Heart Circ. Physiol. , vol.296 , pp. H263-H271
    • Raymond, D.R.1    Carter, R.L.2    Ward, C.A.3    Maurice, D.H.4
  • 13
    • 33750720277 scopus 로고    scopus 로고
    • PGE1 stimulation of HEK293 cells generates multiple contiguous domains with different [cAMP]: role of compartmentalized phosphodiesterases
    • Terrin A., Di Benedetto G., Pertegato V. et al. PGE1 stimulation of HEK293 cells generates multiple contiguous domains with different [cAMP]: role of compartmentalized phosphodiesterases. J. Cell Biol. (2006) 175 441-451.
    • (2006) J. Cell Biol. , vol.175 , pp. 441-451
    • Terrin, A.1    Di Benedetto, G.2    Pertegato, V.3
  • 14
    • 84858178131 scopus 로고    scopus 로고
    • Assessment of cellular mechanisms contributing to cAMP compartmentalization in pulmonary microvascular endothelial cells
    • Feinstein W.P., Zhu B., Leavesley S.J., Sayner S.L., Rich T.C. Assessment of cellular mechanisms contributing to cAMP compartmentalization in pulmonary microvascular endothelial cells. Am. J. Physiol. Cell Physiol. (2012) 302 C839-C852.
    • (2012) Am. J. Physiol. Cell Physiol. , vol.302 , pp. C839-C852
    • Feinstein, W.P.1    Zhu, B.2    Leavesley, S.J.3    Sayner, S.L.4    Rich, T.C.5
  • 15
    • 80052787459 scopus 로고    scopus 로고
    • Measuring spatiotemporal dynamics of cyclic AMP signalling in real-time using FRET-based biosensors
    • Gesellchen F., Stangherlin A., Surdo N., Terrin A., Zoccarato A., Zaccollo M. Measuring spatiotemporal dynamics of cyclic AMP signalling in real-time using FRET-based biosensors. Methods Mol. Biol. (2011) 746 297-316.
    • (2011) Methods Mol. Biol. , vol.746 , pp. 297-316
    • Gesellchen, F.1    Stangherlin, A.2    Surdo, N.3    Terrin, A.4    Zoccarato, A.5    Zaccollo, M.6
  • 16
    • 84884910340 scopus 로고    scopus 로고
    • Compartmentalization of cyclic nucleotide signaling: a question of when, where, and why?
    • Arora K., Sinha C., Zhang W. et al. Compartmentalization of cyclic nucleotide signaling: a question of when, where, and why? Pflügers Arch. (2013) 465 1397-1407.
    • (2013) Pflügers Arch. , vol.465 , pp. 1397-1407
    • Arora, K.1    Sinha, C.2    Zhang, W.3
  • 18
    • 38649120829 scopus 로고    scopus 로고
    • Drugs and their molecular targets: an updated overview
    • Landry Y., Gies J.-P. Drugs and their molecular targets: an updated overview. Fundam. Clin. Pharmacol. (2008) 22 1-18.
    • (2008) Fundam. Clin. Pharmacol. , vol.22 , pp. 1-18
    • Landry, Y.1    Gies, J.-P.2
  • 19
    • 0036729478 scopus 로고    scopus 로고
    • Cyclic nucleotide research [mdash] still expanding after half a century
    • Beavo J.A., Brunton L.L. Cyclic nucleotide research [mdash] still expanding after half a century. Nat. Rev. Mol. Cell Biol. (2002) 3 710-718.
    • (2002) Nat. Rev. Mol. Cell Biol. , vol.3 , pp. 710-718
    • Beavo, J.A.1    Brunton, L.L.2
  • 20
    • 0035413602 scopus 로고    scopus 로고
    • Physiological substrates of cAMP-dependent protein kinase
    • Shabb J.B. Physiological substrates of cAMP-dependent protein kinase. Chem. Rev. (2001) 101 2381-2411.
    • (2001) Chem. Rev. , vol.101 , pp. 2381-2411
    • Shabb, J.B.1
  • 21
    • 0033761535 scopus 로고    scopus 로고
    • Phosphodiesterases and cyclic nucleotide signaling in endocrine cells
    • Conti M. Phosphodiesterases and cyclic nucleotide signaling in endocrine cells. Mol. Endocrinol. (2000) 14 1317-1327.
    • (2000) Mol. Endocrinol. , vol.14 , pp. 1317-1327
    • Conti, M.1
  • 22
    • 3242793327 scopus 로고    scopus 로고
    • Historical review: a brief history and personal retrospective of seven-transmembrane receptors
    • Lefkowitz R.J. Historical review: a brief history and personal retrospective of seven-transmembrane receptors. Trends Pharmacol. Sci. (2004) 25 413-422.
    • (2004) Trends Pharmacol. Sci. , vol.25 , pp. 413-422
    • Lefkowitz, R.J.1
  • 23
    • 0037443097 scopus 로고    scopus 로고
    • PDE4 cAMP phosphodiesterases: modular enzymes that orchestrate signalling cross-talk, desensitization and compartmentalization
    • Houslay M.D., Adams D.R. PDE4 cAMP phosphodiesterases: modular enzymes that orchestrate signalling cross-talk, desensitization and compartmentalization. Biochem. J. (2003) 370 1-18.
    • (2003) Biochem. J. , vol.370 , pp. 1-18
    • Houslay, M.D.1    Adams, D.R.2
  • 24
    • 77956255305 scopus 로고    scopus 로고
    • Equilibrium between adenylyl cyclase and phosphodiesterase patterns adrenergic agonist dose-dependent spatiotemporal cAMP/protein kinase A activities in cardiomyocytes
    • De Arcangelis V., Liu S., Zhang D., Soto D., Xiang Y.K. Equilibrium between adenylyl cyclase and phosphodiesterase patterns adrenergic agonist dose-dependent spatiotemporal cAMP/protein kinase A activities in cardiomyocytes. Mol. Pharmacol. (2010) 78 340-349.
    • (2010) Mol. Pharmacol. , vol.78 , pp. 340-349
    • De Arcangelis, V.1    Liu, S.2    Zhang, D.3    Soto, D.4    Xiang, Y.K.5
  • 25
    • 0000682101 scopus 로고
    • The properties of an adenine ribonucleotide produced with cellular particles, ATP, Mg++, and epinephrine or glucagon
    • Sutherland E.W., Rall T.W. The properties of an adenine ribonucleotide produced with cellular particles, ATP, Mg++, and epinephrine or glucagon. J. Am. Chem. Soc. (1957) 79 3608.
    • (1957) J. Am. Chem. Soc. , vol.79 , pp. 3608
    • Sutherland, E.W.1    Rall, T.W.2
  • 26
    • 0032605044 scopus 로고    scopus 로고
    • The molecular biology of cyclic nucleotide phosphodiesterases
    • Conti M., Jin S.-L.C. The molecular biology of cyclic nucleotide phosphodiesterases. Prog. Nucleic Acid Res. Mol. Biol. (1999) 63 1-38.
    • (1999) Prog. Nucleic Acid Res. Mol. Biol. , vol.63 , pp. 1-38
    • Conti, M.1    Jin, S.-L.2
  • 27
    • 0034009080 scopus 로고    scopus 로고
    • Regulation of cAMP and cGMP signaling: new phosphodiesterases and new functions
    • Soderling S.H., Beavo J.A. Regulation of cAMP and cGMP signaling: new phosphodiesterases and new functions. Curr. Opin. Cell Biol. (2000) 12 174-179.
    • (2000) Curr. Opin. Cell Biol. , vol.12 , pp. 174-179
    • Soderling, S.H.1    Beavo, J.A.2
  • 29
    • 34447265905 scopus 로고    scopus 로고
    • Biochemistry and physiology of cyclic nucleotide phosphodiesterases: essential components in cyclic nucleotide signaling
    • Conti M., Beavo J. Biochemistry and physiology of cyclic nucleotide phosphodiesterases: essential components in cyclic nucleotide signaling. Annu. Rev. Biochem. (2007) 76 481-511.
    • (2007) Annu. Rev. Biochem. , vol.76 , pp. 481-511
    • Conti, M.1    Beavo, J.2
  • 30
    • 0025999955 scopus 로고
    • Cyclic nucleotide phosphodiesterases: pharmacology, biochemistry and function
    • Thompson W.J. Cyclic nucleotide phosphodiesterases: pharmacology, biochemistry and function. Pharmacol. Ther. (1991) 51 13-33.
    • (1991) Pharmacol. Ther. , vol.51 , pp. 13-33
    • Thompson, W.J.1
  • 31
    • 0028574848 scopus 로고
    • Molecular biology of the cyclic AMP-specific cyclic nucleotide phosphodiesterases: a diverse family of regulatory enzymes
    • Bolger G.B. Molecular biology of the cyclic AMP-specific cyclic nucleotide phosphodiesterases: a diverse family of regulatory enzymes. Cell. Signal. (1994) 6 851-859.
    • (1994) Cell. Signal. , vol.6 , pp. 851-859
    • Bolger, G.B.1
  • 32
    • 0030964062 scopus 로고    scopus 로고
    • Recombinant expression of a type IV, cAMP-specific phosphodiesterase: characterization and structure-function studies of deletion mutants
    • Kovala T., Sanwal B.D., Ball E.H. Recombinant expression of a type IV, cAMP-specific phosphodiesterase: characterization and structure-function studies of deletion mutants. Biochemistry (1997) 36 2968-2976.
    • (1997) Biochemistry , vol.36 , pp. 2968-2976
    • Kovala, T.1    Sanwal, B.D.2    Ball, E.H.3
  • 33
    • 0029820823 scopus 로고    scopus 로고
    • Phosphorylation of a cAMP-specific phosphodiesterase (HSPDE4B2B) by mitogen-activated protein kinase
    • Lenhard J.M., Kassel D.B., Rocque W.J. et al. Phosphorylation of a cAMP-specific phosphodiesterase (HSPDE4B2B) by mitogen-activated protein kinase. Biochem. J. (1996) 316 751-758.
    • (1996) Biochem. J. , vol.316 , pp. 751-758
    • Lenhard, J.M.1    Kassel, D.B.2    Rocque, W.J.3
  • 34
    • 0042355363 scopus 로고    scopus 로고
    • Cyclic nucleotide phosphodiesterase activity, expression, and targeting in cells of the cardiovascular system
    • Maurice D.H., Palmer D., Tilley D.G. et al. Cyclic nucleotide phosphodiesterase activity, expression, and targeting in cells of the cardiovascular system. Mol. Pharmacol. (2003) 64 533-546.
    • (2003) Mol. Pharmacol. , vol.64 , pp. 533-546
    • Maurice, D.H.1    Palmer, D.2    Tilley, D.G.3
  • 35
    • 3142776354 scopus 로고    scopus 로고
    • The oligomerization state determines regulatory properties and inhibitor sensitivity of type 4 cAMP-specific phosphodiesterases
    • Richter W., Conti M. The oligomerization state determines regulatory properties and inhibitor sensitivity of type 4 cAMP-specific phosphodiesterases. J. Biol. Chem. (2004) 279 30338-30348.
    • (2004) J. Biol. Chem. , vol.279 , pp. 30338-30348
    • Richter, W.1    Conti, M.2
  • 36
    • 0036189968 scopus 로고    scopus 로고
    • In addition to the SH3 binding region, multiple regions within the N-terminal noncatalytic portion of the cAMP-specific phosphodiesterase, PDE4A5, contribute to its intracellular targeting
    • Beard M.B., Huston E., Campbell L. et al. In addition to the SH3 binding region, multiple regions within the N-terminal noncatalytic portion of the cAMP-specific phosphodiesterase, PDE4A5, contribute to its intracellular targeting. Cell. Signal. (2002) 14 453-465.
    • (2002) Cell. Signal. , vol.14 , pp. 453-465
    • Beard, M.B.1    Huston, E.2    Campbell, L.3
  • 37
    • 33746381639 scopus 로고    scopus 로고
    • AKAP signaling complexes: getting to the heart of the matter
    • McConnachie G., Langeberg L.K., Scott J.D. AKAP signaling complexes: getting to the heart of the matter. Trends Mol. Med. (2006) 12 317-323.
    • (2006) Trends Mol. Med. , vol.12 , pp. 317-323
    • McConnachie, G.1    Langeberg, L.K.2    Scott, J.D.3
  • 38
    • 0035901502 scopus 로고    scopus 로고
    • mAKAP assembles a protein kinase A/PDE4 phosphodiesterase cAMP signaling module
    • Dodge K.L., Khouangsathiene S., Kapiloff M.S. et al. mAKAP assembles a protein kinase A/PDE4 phosphodiesterase cAMP signaling module. EMBO J. (2001) 20 1921-1930.
    • (2001) EMBO J. , vol.20 , pp. 1921-1930
    • Dodge, K.L.1    Khouangsathiene, S.2    Kapiloff, M.S.3
  • 39
    • 25644452031 scopus 로고    scopus 로고
    • The protein kinase A anchoring protein mAKAP coordinates two integrated cAMP effector pathways
    • Dodge-Kafka K.L., Soughayer J., Pare G.C. et al. The protein kinase A anchoring protein mAKAP coordinates two integrated cAMP effector pathways. Nature (2005) 437 574-578.
    • (2005) Nature , vol.437 , pp. 574-578
    • Dodge-Kafka, K.L.1    Soughayer, J.2    Pare, G.C.3
  • 40
    • 0041836339 scopus 로고    scopus 로고
    • Epac: a new cAMP target and new avenues in cAMP research
    • Bos J.L. Epac: a new cAMP target and new avenues in cAMP research. Nat. Rev. Mol. Cell Biol. (2003) 4 733-738.
    • (2003) Nat. Rev. Mol. Cell Biol. , vol.4 , pp. 733-738
    • Bos, J.L.1
  • 41
    • 0029055761 scopus 로고
    • Components of a new human protein kinase signal transduction pathway
    • Zhou G., Bao Z.Q., Dixon J.E. Components of a new human protein kinase signal transduction pathway. J. Biol. Chem. (1995) 270 12665-12669.
    • (1995) J. Biol. Chem. , vol.270 , pp. 12665-12669
    • Zhou, G.1    Bao, Z.Q.2    Dixon, J.E.3
  • 42
    • 0037417890 scopus 로고    scopus 로고
    • β-Arrestin-mediated PDE4 cAMP phosphodiesterase recruitment regulates β-adrenoceptor switching from Gs to Gi
    • Baillie G.S., Sood A., McPhee I. et al. β-Arrestin-mediated PDE4 cAMP phosphodiesterase recruitment regulates β-adrenoceptor switching from Gs to Gi. Proc. Natl Acad. Sci. USA (2003) 100 940-945.
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 940-945
    • Baillie, G.S.1    Sood, A.2    McPhee, I.3
  • 43
    • 0014934492 scopus 로고
    • Cyclic 3',5'-nucleotide phosphodiesterase: demonstration of an activator
    • Cheung W.Y. Cyclic 3', 5'-nucleotide phosphodiesterase: demonstration of an activator. Biochem. Biophys. Res. Commun. (1970) 38 533-538.
    • (1970) Biochem. Biophys. Res. Commun. , vol.38 , pp. 533-538
    • Cheung, W.Y.1
  • 44
    • 0025823947 scopus 로고
    • Electron microscopic immunocytochemical evidence that the calmodulin-dependent cyclic nucleotide phosphodiesterase is localized predominantly at postsynaptic sites in the rat brain
    • Ludvig N., Burmeister V., Jobe P.C., Kincaid R.L. Electron microscopic immunocytochemical evidence that the calmodulin-dependent cyclic nucleotide phosphodiesterase is localized predominantly at postsynaptic sites in the rat brain. Neuroscience (1991) 44 491-500.
    • (1991) Neuroscience , vol.44 , pp. 491-500
    • Ludvig, N.1    Burmeister, V.2    Jobe, P.C.3    Kincaid, R.L.4
  • 45
    • 0035188826 scopus 로고    scopus 로고
    • Cyclic nucleotide phosphodiesterases
    • Essayan D.M. Cyclic nucleotide phosphodiesterases. J. Allergy Clin. Immunol. (2001) 108 671-680.
    • (2001) J. Allergy Clin. Immunol. , vol.108 , pp. 671-680
    • Essayan, D.M.1
  • 46
    • 0035010063 scopus 로고    scopus 로고
    • Stage and cell-specific expression of calmodulin-dependent phosphodiesterases in mouse testis
    • Yan C., Zhao A.Z., Sonnenburg W.K., Beavo J.A. Stage and cell-specific expression of calmodulin-dependent phosphodiesterases in mouse testis. Biol. Reprod. (2001) 64 1746-1754.
    • (2001) Biol. Reprod. , vol.64 , pp. 1746-1754
    • Yan, C.1    Zhao, A.Z.2    Sonnenburg, W.K.3    Beavo, J.A.4
  • 47
    • 25144456423 scopus 로고    scopus 로고
    • Identification of a new variant of PDE1A calmodulin-stimulated cyclic nucleotide phosphodiesterase expressed in mouse sperm
    • Vasta V., Sonnenburg W.K., Yan C., Soderling S.H., Shimizu-Albergine M., Beavo J.A. Identification of a new variant of PDE1A calmodulin-stimulated cyclic nucleotide phosphodiesterase expressed in mouse sperm. Biol. Reprod. (2005) 73 598-609.
    • (2005) Biol. Reprod. , vol.73 , pp. 598-609
    • Vasta, V.1    Sonnenburg, W.K.2    Yan, C.3    Soderling, S.H.4    Shimizu-Albergine, M.5    Beavo, J.A.6
  • 48
    • 0020405899 scopus 로고
    • Identification of cGMP-stimulated cyclic nucleotide phosphodiesterase in lung tissue with monoclonal antibodies
    • Mumby M.C., Martins T.J., Chang M.L., Beavo J.A. Identification of cGMP-stimulated cyclic nucleotide phosphodiesterase in lung tissue with monoclonal antibodies. J. Biol. Chem. (1982) 257 13283-13290.
    • (1982) J. Biol. Chem. , vol.257 , pp. 13283-13290
    • Mumby, M.C.1    Martins, T.J.2    Chang, M.L.3    Beavo, J.A.4
  • 49
    • 0036790852 scopus 로고    scopus 로고
    • 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. et al. The two GAF domains in phosphodiesterase 2A have distinct roles in dimerization and in cGMP binding. Proc. Natl Acad. Sci. USA (2002) 99 13260-13265.
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 13260-13265
    • Martinez, S.E.1    Wu, A.Y.2    Glavas, N.A.3
  • 50
    • 0028567796 scopus 로고
    • A novel cyclic GMP stimulated phosphodiesterase from rat brain
    • Yang Q., Paskind M., Bolger G. et al. A novel cyclic GMP stimulated phosphodiesterase from rat brain. Biochem. Biophys. Res. Commun. (1994) 205 1850-1858.
    • (1994) Biochem. Biophys. Res. Commun. , vol.205 , pp. 1850-1858
    • Yang, Q.1    Paskind, M.2    Bolger, G.3
  • 51
    • 0020038738 scopus 로고
    • Purification and characterization of a cyclic GMP-stimulated cyclic nucleotide phosphodiesterase from bovine tissues
    • Martins T.J., Mumby M.C., Beavo J.A. Purification and characterization of a cyclic GMP-stimulated cyclic nucleotide phosphodiesterase from bovine tissues. J. Biol. Chem. (1982) 257 1973-1979.
    • (1982) J. Biol. Chem. , vol.257 , pp. 1973-1979
    • Martins, T.J.1    Mumby, M.C.2    Beavo, J.A.3
  • 52
    • 0021023261 scopus 로고
    • Purification and characterization of cyclic GMP-stimulated cyclic nucleotide phosphodiesterase from calf liver. Effects of divalent cations on activity
    • Yamamoto T., Manganiello V.C., Vaughan M. Purification and characterization of cyclic GMP-stimulated cyclic nucleotide phosphodiesterase from calf liver. Effects of divalent cations on activity. J. Biol. Chem. (1983) 258 12526-12533.
    • (1983) J. Biol. Chem. , vol.258 , pp. 12526-12533
    • Yamamoto, T.1    Manganiello, V.C.2    Vaughan, M.3
  • 53
    • 0345735392 scopus 로고    scopus 로고
    • 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. Differentiation of human monocytes in vitro with granulocyte-macrophage colony-stimulating factor and macrophage colony-stimulating factor produces distinct changes in cGMP phosphodiesterase expression. Cell. Signal. (2004) 16 365-374.
    • (2004) Cell. Signal. , vol.16 , pp. 365-374
    • Bender, A.T.1    Ostenson, C.L.2    Giordano, D.3    Beavo, J.A.4
  • 55
    • 0030977764 scopus 로고    scopus 로고
    • Activation of cGMP-stimulated phosphodiesterase by nitroprusside limits cAMP accumulation in human platelets: effects on platelet aggregation
    • Dickinson N.T., Jang E.K., Haslam R.J. Activation of cGMP-stimulated phosphodiesterase by nitroprusside limits cAMP accumulation in human platelets: effects on platelet aggregation. Biochem. J. (1997) 323 371-377.
    • (1997) Biochem. J. , vol.323 , pp. 371-377
    • Dickinson, N.T.1    Jang, E.K.2    Haslam, R.J.3
  • 56
    • 0026032745 scopus 로고
    • High concentrations of a cGMP-stimulated phosphodiesterase mediate ANP-induced decreases in cAMP and steroidogenesis in adrenal glomerulosa cells
    • MacFarland R.T., Zelus B.D., Beavo J.A. High concentrations of a cGMP-stimulated phosphodiesterase mediate ANP-induced decreases in cAMP and steroidogenesis in adrenal glomerulosa cells. J. Biol. Chem. (1991) 266 136-142.
    • (1991) J. Biol. Chem. , vol.266 , pp. 136-142
    • MacFarland, R.T.1    Zelus, B.D.2    Beavo, J.A.3
  • 57
    • 0023890615 scopus 로고
    • Role of phosphodiesterase in regulation of calcium current in isolated cardiac myocytes
    • Simmons M.A., Hartzell H.C. Role of phosphodiesterase in regulation of calcium current in isolated cardiac myocytes. Mol. Pharmacol. (1988) 33 664-671.
    • (1988) Mol. Pharmacol. , vol.33 , pp. 664-671
    • Simmons, M.A.1    Hartzell, H.C.2
  • 58
    • 80052219693 scopus 로고    scopus 로고
    • A phosphodiesterase 2A isoform localized to mitochondria regulates respiration
    • Acin-Perez R., Russwurm M., Günnewig K. et al. A phosphodiesterase 2A isoform localized to mitochondria regulates respiration. J. Biol. Chem. (2011) 286 30423-30432.
    • (2011) J. Biol. Chem. , vol.286 , pp. 30423-30432
    • Acin-Perez, R.1    Russwurm, M.2    Günnewig, K.3
  • 60
    • 84872847888 scopus 로고    scopus 로고
    • Phosphodiesterase type 3A regulates basal myocardial contractility through interacting with sarcoplasmic reticulum calcium ATPase type 2a signaling complexes in mouse heart
    • Beca S., Ahmad F., Shen W. et al. Phosphodiesterase type 3A regulates basal myocardial contractility through interacting with sarcoplasmic reticulum calcium ATPase type 2a signaling complexes in mouse heart. Circ. Res. (2013) 112 289-297.
    • (2013) Circ. Res. , vol.112 , pp. 289-297
    • Beca, S.1    Ahmad, F.2    Shen, W.3
  • 61
    • 0026072848 scopus 로고
    • Effect of oral milrinone on mortality in severe chronic heart failure
    • Packer M., Carver J.R., Rodeheffer R.J. et al. Effect of oral milrinone on mortality in severe chronic heart failure. N. Engl. J. Med. (1991) 325 1468-1475.
    • (1991) N. Engl. J. Med. , vol.325 , pp. 1468-1475
    • Packer, M.1    Carver, J.R.2    Rodeheffer, R.J.3
  • 62
    • 33845348168 scopus 로고    scopus 로고
    • Alterations in regulation of energy homeostasis in cyclic nucleotide phosphodiesterase 3B-null mice
    • Choi Y.H., Park S., Hockman S. et al. Alterations in regulation of energy homeostasis in cyclic nucleotide phosphodiesterase 3B-null mice. J. Clin. Invest. (2006) 116 3240-3251.
    • (2006) J. Clin. Invest. , vol.116 , pp. 3240-3251
    • Choi, Y.H.1    Park, S.2    Hockman, S.3
  • 63
    • 82255192444 scopus 로고    scopus 로고
    • From PDE3B to the regulation of energy homeostasis
    • Degerman E., Ahmad F., Chung Y.W. et al. From PDE3B to the regulation of energy homeostasis. Curr. Opin. Pharmacol. (2011) 11 676-682.
    • (2011) Curr. Opin. Pharmacol. , vol.11 , pp. 676-682
    • Degerman, E.1    Ahmad, F.2    Chung, Y.W.3
  • 64
    • 77955590833 scopus 로고    scopus 로고
    • Phosphatidic acid induces ligand-independent epidermal growth factor receptor endocytic traffic through PDE4 activation
    • Norambuena A., Metz C., Jung J.E. et al. Phosphatidic acid induces ligand-independent epidermal growth factor receptor endocytic traffic through PDE4 activation. Mol. Biol. Cell (2010) 21 2916-2929.
    • (2010) Mol. Biol. Cell , vol.21 , pp. 2916-2929
    • Norambuena, A.1    Metz, C.2    Jung, J.E.3
  • 65
    • 0031601339 scopus 로고    scopus 로고
    • The multienzyme PDE4 cyclic adenosine monophosphate-specific phosphodiesterase family: intracellular targeting, regulation, and selective inhibition by compounds exerting anti-inflammatory and antidepressant actions
    • Houslay M.D., Sullivan M., Bolgerz G.B. The multienzyme PDE4 cyclic adenosine monophosphate-specific phosphodiesterase family: intracellular targeting, regulation, and selective inhibition by compounds exerting anti-inflammatory and antidepressant actions. Adv. Pharmacol. (1998) 44 225-342.
    • (1998) Adv. Pharmacol. , vol.44 , pp. 225-342
    • Houslay, M.D.1    Sullivan, M.2    Bolgerz, G.B.3
  • 67
    • 0029960693 scopus 로고    scopus 로고
    • Role of multiple cAMP-specific phosphodiesterase variants
    • Bushnik T., Conti M. Role of multiple cAMP-specific phosphodiesterase variants. Biochem. Soc. Trans. (1996) 24 1014-1019.
    • (1996) Biochem. Soc. Trans. , vol.24 , pp. 1014-1019
    • Bushnik, T.1    Conti, M.2
  • 68
    • 0029959276 scopus 로고    scopus 로고
    • The N-terminal alternately spliced regions of PDE4A cAMP-specific phosphodiesterases determine intracellular targeting and regulation of catalytic activity
    • Houslay M.D. The N-terminal alternately spliced regions of PDE4A cAMP-specific phosphodiesterases determine intracellular targeting and regulation of catalytic activity. Biochem. Soc. Trans. (1996) 24 980-986.
    • (1996) Biochem. Soc. Trans. , vol.24 , pp. 980-986
    • Houslay, M.D.1
  • 69
    • 0035815666 scopus 로고    scopus 로고
    • Myomegalin is a novel protein of the Golgi/centrosome that interacts with a cyclic nucleotide phosphodiesterase
    • Verde I., Pahlke G., Salanova M. et al. Myomegalin is a novel protein of the Golgi/centrosome that interacts with a cyclic nucleotide phosphodiesterase. J. Biol. Chem. (2001) 276 11189-11198.
    • (2001) J. Biol. Chem. , vol.276 , pp. 11189-11198
    • Verde, I.1    Pahlke, G.2    Salanova, M.3
  • 70
    • 0035933817 scopus 로고    scopus 로고
    • Phosphodiesterase 4D and protein kinase A type II constitute a signaling unit in the centrosomal area
    • Taskén K.A., Collas P., Kemmner W.A., Witczak O., Conti M., Taskén K. Phosphodiesterase 4D and protein kinase A type II constitute a signaling unit in the centrosomal area. J. Biol. Chem. (2001) 276 21999-22002.
    • (2001) J. Biol. Chem. , vol.276 , pp. 21999-22002
    • Taskén, K.A.1    Collas, P.2    Kemmner, W.A.3    Witczak, O.4    Conti, M.5    Taskén, K.6
  • 71
    • 0019205204 scopus 로고
    • Characteristics of a new binding protein distinct from the kinase for guanosine 3':5'-monophosphate in rat platelets
    • Coquil J.-F., Franks D.J., Wells J.N., Dupuis M., Hamet P. Characteristics of a new binding protein distinct from the kinase for guanosine 3':5'-monophosphate in rat platelets. Biochim. Biophys. Acta (1980) 631 148-165.
    • (1980) Biochim. Biophys. Acta , vol.631 , pp. 148-165
    • Coquil, J.-F.1    Franks, D.J.2    Wells, J.N.3    Dupuis, M.4    Hamet, P.5
  • 72
    • 0018871466 scopus 로고
    • Characterization of a novel cGMP binding protein from rat lung
    • Francis S.H., Lincoln T.M., Corbin J.D. Characterization of a novel cGMP binding protein from rat lung. J. Biol. Chem. (1980) 255 620-626.
    • (1980) J. Biol. Chem. , vol.255 , pp. 620-626
    • Francis, S.H.1    Lincoln, T.M.2    Corbin, J.D.3
  • 73
    • 0033564377 scopus 로고    scopus 로고
    • Genomic origin and transcriptional regulation of two variants of cGMP-binding cGMP-specific phosphodiesterases
    • Kotera J., Fujishige K., Imai Y. et al. Genomic origin and transcriptional regulation of two variants of cGMP-binding cGMP-specific phosphodiesterases. Eur. J. Biochem. (1999) 262 866-873.
    • (1999) Eur. J. Biochem. , vol.262 , pp. 866-873
    • Kotera, J.1    Fujishige, K.2    Imai, Y.3
  • 74
    • 0034673250 scopus 로고    scopus 로고
    • Expression of three isoforms of cGMP-binding cGMP-specific phosphodiesterase (PDE5) in human penile cavernosum
    • Lin C.-S., Lau A., Tu R., Lue T.F. Expression of three isoforms of cGMP-binding cGMP-specific phosphodiesterase (PDE5) in human penile cavernosum. Biochem. Biophys. Res. Commun. (2000) 268 628-635.
    • (2000) Biochem. Biophys. Res. Commun. , vol.268 , pp. 628-635
    • Lin, C.-S.1    Lau, A.2    Tu, R.3    Lue, T.F.4
  • 75
    • 0032541484 scopus 로고    scopus 로고
    • Isolation and characterization of cDNAs encoding PDE5A, a human cGMP-binding, cGMP-specific 3',5'-cyclic nucleotide phosphodiesterase
    • Loughney K., Hill T.R., Florio V.A. et al. Isolation and characterization of cDNAs encoding PDE5A, a human cGMP-binding, cGMP-specific 3', 5'-cyclic nucleotide phosphodiesterase. Gene (1998) 216 139-147.
    • (1998) Gene , vol.216 , pp. 139-147
    • Loughney, K.1    Hill, T.R.2    Florio, V.A.3
  • 76
    • 0035962999 scopus 로고    scopus 로고
    • Expression of cGMP-binding cGMP-specific phosphodiesterase (PDE5) in mouse tissues and cell lines using an antibody against the enzyme amino-terminal domain
    • Giordano D., De Stefano M.E., Citro G., Modica A., Giorgi M. Expression of cGMP-binding cGMP-specific phosphodiesterase (PDE5) in mouse tissues and cell lines using an antibody against the enzyme amino-terminal domain. Biochim. Biophys. Acta - Mol. Cell. Res. (2001) 1539 16-27.
    • (2001) Biochim. Biophys. Acta - Mol. Cell. Res. , vol.1539 , pp. 16-27
    • Giordano, D.1    De Stefano, M.E.2    Citro, G.3    Modica, A.4    Giorgi, M.5
  • 77
    • 0034063871 scopus 로고    scopus 로고
    • Immunohistochemical localization of cGMP-binding cGMP-specific phosphodiesterase (PDE5) in rat tissues
    • Kotera J., Fujishige K., Omori K. Immunohistochemical localization of cGMP-binding cGMP-specific phosphodiesterase (PDE5) in rat tissues. J. Histochem. Cytochem. (2000) 48 685-693.
    • (2000) J. Histochem. Cytochem. , vol.48 , pp. 685-693
    • Kotera, J.1    Fujishige, K.2    Omori, K.3
  • 78
    • 0032543366 scopus 로고    scopus 로고
    • Molecular cloning and expression of human cGMP-binding cGMP-specific phosphodiesterase (PDE5)
    • Stacey P., Rulten S., Dapling A., Phillips S.C. Molecular cloning and expression of human cGMP-binding cGMP-specific phosphodiesterase (PDE5). Biochem. Biophys. Res. Commun. (1998) 247 249-254.
    • (1998) Biochem. Biophys. Res. Commun. , vol.247 , pp. 249-254
    • Stacey, P.1    Rulten, S.2    Dapling, A.3    Phillips, S.C.4
  • 79
    • 7344243173 scopus 로고    scopus 로고
    • Expression, structure and chromosomal localization of the human cGMP-binding cGMP-specific phosphodiesterase PDE5A gene
    • Yanaka N., Kotera J., Ohtsuka A. et al. Expression, structure and chromosomal localization of the human cGMP-binding cGMP-specific phosphodiesterase PDE5A gene. Eur. J. Biochem. (1998) 255 391-399.
    • (1998) Eur. J. Biochem. , vol.255 , pp. 391-399
    • Yanaka, N.1    Kotera, J.2    Ohtsuka, A.3
  • 80
    • 78549285356 scopus 로고    scopus 로고
    • An update on new oral PDE5 inhibitors for the treatment of erectile dysfunction
    • Palit V., Eardley I. An update on new oral PDE5 inhibitors for the treatment of erectile dysfunction. Nat. Rev. Urol. (2010) 7 603-609.
    • (2010) Nat. Rev. Urol. , vol.7 , pp. 603-609
    • Palit, V.1    Eardley, I.2
  • 81
    • 26444534291 scopus 로고    scopus 로고
    • Sildenafil citrate therapy for pulmonary arterial hypertension
    • Galiè N., Ghofrani H.A., Torbicki A. et al. Sildenafil citrate therapy for pulmonary arterial hypertension. N. Engl. J. Med. (2005) 353 2148-2157.
    • (2005) N. Engl. J. Med. , vol.353 , pp. 2148-2157
    • Galiè, N.1    Ghofrani, H.A.2    Torbicki, A.3
  • 82
    • 0042859823 scopus 로고    scopus 로고
    • Cyclic GMP phosphodiesterases and regulation of smooth muscle function
    • Rybalkin S.D., Yan C., Bornfeldt K.E., Beavo J.A. Cyclic GMP phosphodiesterases and regulation of smooth muscle function. Circ. Res. (2003) 93 280-291.
    • (2003) Circ. Res. , vol.93 , pp. 280-291
    • Rybalkin, S.D.1    Yan, C.2    Bornfeldt, K.E.3    Beavo, J.A.4
  • 83
    • 33748686575 scopus 로고    scopus 로고
    • Cyclic nucleotide phosphodiesterases: molecular regulation to clinical use
    • Bender A.T., Beavo J.A. Cyclic nucleotide phosphodiesterases: molecular regulation to clinical use. Pharmacol. Rev. (2006) 58 488-520.
    • (2006) Pharmacol. Rev. , vol.58 , pp. 488-520
    • Bender, A.T.1    Beavo, J.A.2
  • 84
    • 0018595710 scopus 로고
    • Isolation and characterization of cGMP phosphodiesterase from bovine rod outer segments
    • Baehr W., Devlin M.J., Applebury M.L. Isolation and characterization of cGMP phosphodiesterase from bovine rod outer segments. J. Biol. Chem. (1979) 254 11669-11677.
    • (1979) J. Biol. Chem. , vol.254 , pp. 11669-11677
    • Baehr, W.1    Devlin, M.J.2    Applebury, M.L.3
  • 85
    • 0023918102 scopus 로고
    • Characterization of a bovine cone photoreceptor phosphodiesterase purified by cyclic GMP-sepharose chromatography
    • Gillespie P.G., Beavo J.A. Characterization of a bovine cone photoreceptor phosphodiesterase purified by cyclic GMP-sepharose chromatography. J. Biol. Chem. (1988) 263 8133-8141.
    • (1988) J. Biol. Chem. , vol.263 , pp. 8133-8141
    • Gillespie, P.G.1    Beavo, J.A.2
  • 86
    • 0023991808 scopus 로고
    • cGMP phosphodiesterase of retinal rods is regulated by two inhibitory subunits
    • Deterre P., Bigay J., Forquet F., Robert M., Chabre M. cGMP phosphodiesterase of retinal rods is regulated by two inhibitory subunits. Proc. Natl Acad. Sci. USA (1988) 85 2424-2428.
    • (1988) Proc. Natl Acad. Sci. USA , vol.85 , pp. 2424-2428
    • Deterre, P.1    Bigay, J.2    Forquet, F.3    Robert, M.4    Chabre, M.5
  • 87
    • 0028128535 scopus 로고
    • Heterozygous missense mutation in the rod cGMP phosphodiesterase [beta]-subunit gene in autosomal dominant stationary night blindness
    • Gal A., Orth U., Baehr W., Schwinger E., Rosenberg T. Heterozygous missense mutation in the rod cGMP phosphodiesterase [beta]-subunit gene in autosomal dominant stationary night blindness. Nat. Genet. (1994) 7 64-68.
    • (1994) Nat. Genet. , vol.7 , pp. 64-68
    • Gal, A.1    Orth, U.2    Baehr, W.3    Schwinger, E.4    Rosenberg, T.5
  • 88
    • 0027270053 scopus 로고
    • Recessive mutations in the gene encoding the [beta]-subunit of rod phosphodiesterase in patients with retinitis pigmentosa
    • McLaughlin M.E., Sandberg M.A., Berson E.L., Dryja T.P. Recessive mutations in the gene encoding the [beta]-subunit of rod phosphodiesterase in patients with retinitis pigmentosa. Nat. Genet. (1993) 4 130-134.
    • (1993) Nat. Genet. , vol.4 , pp. 130-134
    • McLaughlin, M.E.1    Sandberg, M.A.2    Berson, E.L.3    Dryja, T.P.4
  • 89
    • 0027164208 scopus 로고
    • Isolation and characterization of a previously undetected human cAMP phosphodiesterase by complementation of cAMP phosphodiesterase-deficient Saccharomyces cerevisiae
    • Michaeli T., Bloom T.J., Martins T. et al. Isolation and characterization of a previously undetected human cAMP phosphodiesterase by complementation of cAMP phosphodiesterase-deficient Saccharomyces cerevisiae. J. Biol. Chem. (1993) 268 12925-12932.
    • (1993) J. Biol. Chem. , vol.268 , pp. 12925-12932
    • Michaeli, T.1    Bloom, T.J.2    Martins, T.3
  • 90
    • 0030971045 scopus 로고    scopus 로고
    • Alternative splicing of the high affinity cAMP-specific phosphodiesterase (PDE7A) mRNA in human skeletal muscle and heart
    • Han P., Zhu X., Michaeli T. Alternative splicing of the high affinity cAMP-specific phosphodiesterase (PDE7A) mRNA in human skeletal muscle and heart. J. Biol. Chem. (1997) 272 16152-16157.
    • (1997) J. Biol. Chem. , vol.272 , pp. 16152-16157
    • Han, P.1    Zhu, X.2    Michaeli, T.3
  • 91
    • 0030459832 scopus 로고    scopus 로고
    • Identification and tissue-specific expression of PDE7 phosphodiesterase splice variants
    • Bloom T.J., Beavo J.A. Identification and tissue-specific expression of PDE7 phosphodiesterase splice variants. Proc. Natl Acad. Sci. USA (1996) 93 14188-14192.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 14188-14192
    • Bloom, T.J.1    Beavo, J.A.2
  • 92
    • 31144433061 scopus 로고    scopus 로고
    • Cyclic nucleotide phosphodiesterase (PDE) superfamily: a new target for the development of specific therapeutic agents
    • Lugnier C. Cyclic nucleotide phosphodiesterase (PDE) superfamily: a new target for the development of specific therapeutic agents. Pharmacol. Ther. (2006) 109 366-398.
    • (2006) Pharmacol. Ther. , vol.109 , pp. 366-398
    • Lugnier, C.1
  • 95
    • 0033524977 scopus 로고    scopus 로고
    • CD3- and CD28-dependent induction of PDE7 required for T cell activation
    • Li L., Yee C., Beavo J.A. CD3- and CD28-dependent induction of PDE7 required for T cell activation. Science (1999) 283 848-851.
    • (1999) Science , vol.283 , pp. 848-851
    • Li, L.1    Yee, C.2    Beavo, J.A.3
  • 96
    • 0036277784 scopus 로고    scopus 로고
    • Potential role of phosphodiesterase 7 in human T cell function: comparative effects of two phosphodiesterase inhibitors
    • Nakata A., Ogawa K., Sasaki T. et al. Potential role of phosphodiesterase 7 in human T cell function: comparative effects of two phosphodiesterase inhibitors. Clin. Exp. Immunol. (2002) 128 460-466.
    • (2002) Clin. Exp. Immunol. , vol.128 , pp. 460-466
    • Nakata, A.1    Ogawa, K.2    Sasaki, T.3
  • 97
    • 6344221448 scopus 로고    scopus 로고
    • A-kinase anchoring proteins interact with phosphodiesterases in T lymphocyte cell lines
    • Asirvatham A.L., Galligan S.G., Schillace R.V. et al. A-kinase anchoring proteins interact with phosphodiesterases in T lymphocyte cell lines. J. Immunol. (2004) 173 4806-4814.
    • (2004) J. Immunol. , vol.173 , pp. 4806-4814
    • Asirvatham, A.L.1    Galligan, S.G.2    Schillace, R.V.3
  • 99
    • 0032578624 scopus 로고    scopus 로고
    • Molecular cloning and characterization of human PDE8B, a novel thyroid-specific isozyme of 3',5'-cyclic nucleotide phosphodiesterase
    • Hayashi M., Matsushima K., Ohashi H. et al. Molecular cloning and characterization of human PDE8B, a novel thyroid-specific isozyme of 3', 5'-cyclic nucleotide phosphodiesterase. Biochem. Biophys. Res. Commun. (1998) 250 751-756.
    • (1998) Biochem. Biophys. Res. Commun. , vol.250 , pp. 751-756
    • Hayashi, M.1    Matsushima, K.2    Ohashi, H.3
  • 100
    • 77957883715 scopus 로고    scopus 로고
    • PDE8 regulates rapid Teff cell adhesion and proliferation independent of ICER
    • Vang A.G., Ben-Sasson S.Z., Dong H. et al. PDE8 regulates rapid Teff cell adhesion and proliferation independent of ICER. PLoS One (2010) 5 e12011.
    • (2010) PLoS One , vol.5 , pp. e12011
    • Vang, A.G.1    Ben-Sasson, S.Z.2    Dong, H.3
  • 101
  • 102
    • 77953718408 scopus 로고    scopus 로고
    • Phosphodiesterase 8A (PDE8A) regulates excitation-contraction coupling in ventricular myocytes
    • Patrucco E., Albergine M.S., Santana L.F., Beavo J.A. Phosphodiesterase 8A (PDE8A) regulates excitation-contraction coupling in ventricular myocytes. J. Mol. Cell. Cardiol. (2010) 49 330-333.
    • (2010) J. Mol. Cell. Cardiol. , vol.49 , pp. 330-333
    • Patrucco, E.1    Albergine, M.S.2    Santana, L.F.3    Beavo, J.A.4
  • 103
    • 39049101528 scopus 로고    scopus 로고
    • Mutation in PDE8B, a cyclic AMP-specific phosphodiesterase in adrenal hyperplasia
    • Horvath A., Mericq V., Stratakis C.A. Mutation in PDE8B, a cyclic AMP-specific phosphodiesterase in adrenal hyperplasia. N. Engl. J. Med. (2008) 358 750-752.
    • (2008) N. Engl. J. Med. , vol.358 , pp. 750-752
    • Horvath, A.1    Mericq, V.2    Stratakis, C.A.3
  • 104
    • 0037436281 scopus 로고    scopus 로고
    • Identification and distribution of different mRNA variants produced by differential splicing in the human phosphodiesterase 9A gene
    • Rentero C., Monfort A., Puigdomènech P. Identification and distribution of different mRNA variants produced by differential splicing in the human phosphodiesterase 9A gene. Biochem. Biophys. Res. Commun. (2003) 301 686-692.
    • (2003) Biochem. Biophys. Res. Commun. , vol.301 , pp. 686-692
    • Rentero, C.1    Monfort, A.2    Puigdomènech, P.3
  • 105
    • 0032546779 scopus 로고    scopus 로고
    • Isolation and characterization of PDE9A, a novel human cGMP-specific phosphodiesterase
    • Fisher D.A., Smith J.F., Pillar J.S., St Denis S.H., Cheng J.B. Isolation and characterization of PDE9A, a novel human cGMP-specific phosphodiesterase. J. Biol. Chem. (1998) 273 15559-15564.
    • (1998) J. Biol. Chem. , vol.273 , pp. 15559-15564
    • Fisher, D.A.1    Smith, J.F.2    Pillar, J.S.3    St Denis, S.H.4    Cheng, J.B.5
  • 106
    • 0141425593 scopus 로고    scopus 로고
    • Identification and characterization of a new human type 9 cGMP-specific phosphodiesterase splice variant (PDE9A5): differential tissue distribution and subcellular localization of PDE9A variants
    • Wang P., Wu P., Egan R.W., Billah M.M. Identification and characterization of a new human type 9 cGMP-specific phosphodiesterase splice variant (PDE9A5): differential tissue distribution and subcellular localization of PDE9A variants. Gene (2003) 314 15-27.
    • (2003) Gene , vol.314 , pp. 15-27
    • Wang, P.1    Wu, P.2    Egan, R.W.3    Billah, M.M.4
  • 107
    • 33646379135 scopus 로고    scopus 로고
    • cAMP is a ligand for the tandem GAF domain of human phosphodiesterase 10 and cGMP for the tandem GAF domain of phosphodiesterase 11
    • Gross-Langenhoff M., Hofbauer K., Weber J., Schultz A., Schultz J.E. cAMP is a ligand for the tandem GAF domain of human phosphodiesterase 10 and cGMP for the tandem GAF domain of phosphodiesterase 11. J. Biol. Chem. (2006) 281 2841-2846.
    • (2006) J. Biol. Chem. , vol.281 , pp. 2841-2846
    • Gross-Langenhoff, M.1    Hofbauer, K.2    Weber, J.3    Schultz, A.4    Schultz, J.E.5
  • 108
    • 84655170136 scopus 로고    scopus 로고
    • Discovery of orally active pyrazoloquinolines as potent PDE10 inhibitors for the management of schizophrenia
    • Yang S.-W., Smotryski J., McElroy W.T. et al. Discovery of orally active pyrazoloquinolines as potent PDE10 inhibitors for the management of schizophrenia. Bioorg. Med. Chem. Lett. (2012) 22 235-239.
    • (2012) Bioorg. Med. Chem. Lett. , vol.22 , pp. 235-239
    • Yang, S.-W.1    Smotryski, J.2    McElroy, W.T.3
  • 109
    • 0034724177 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a distinct human phosphodiesterase gene family: PDE11A
    • Fawcett L., Baxendale R., Stacey P. et al. Molecular cloning and characterization of a distinct human phosphodiesterase gene family: PDE11A. Proc. Natl Acad. Sci. USA (2000) 97 3702-3707.
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 3702-3707
    • Fawcett, L.1    Baxendale, R.2    Stacey, P.3
  • 110
    • 78650898282 scopus 로고    scopus 로고
    • Frequent phosphodiesterase 11A gene (PDE11A) defects in patients with Carney complex (CNC) caused by PRKAR1A mutations: PDE11A may contribute to adrenal and testicular tumors in CNC as a modifier of the phenotype
    • Libé R., Horvath A., Vezzosi D. et al. Frequent phosphodiesterase 11A gene (PDE11A) defects in patients with Carney complex (CNC) caused by PRKAR1A mutations: PDE11A may contribute to adrenal and testicular tumors in CNC as a modifier of the phenotype. J. Clin. Endocrinol. Metab. (2011) 96 E208-E214.
    • (2011) J. Clin. Endocrinol. Metab. , vol.96 , pp. E208-E214
    • Libé, R.1    Horvath, A.2    Vezzosi, D.3
  • 111
    • 84868611190 scopus 로고    scopus 로고
    • Phosphodiesterase 11A (PDE11A) gene defects in patients with ACTH-independent macronodular adrenal hyperplasia (AIMAH): functional variants may contribute to genetic susceptibility of bilateral adrenal tumors
    • Vezzosi D., Libé R., Baudry C. et al. Phosphodiesterase 11A (PDE11A) gene defects in patients with ACTH-independent macronodular adrenal hyperplasia (AIMAH): functional variants may contribute to genetic susceptibility of bilateral adrenal tumors. J. Clin. Endocrinol. Metab. (2012) 97 E2063-E2069.
    • (2012) J. Clin. Endocrinol. Metab. , vol.97 , pp. E2063-E2069
    • Vezzosi, D.1    Libé, R.2    Baudry, C.3
  • 112
    • 79955664087 scopus 로고    scopus 로고
    • Mammalian cyclic nucleotide phosphodiesterases: molecular mechanisms and physiological functions
    • Francis S.H., Blount M.A., Corbin J.D. Mammalian cyclic nucleotide phosphodiesterases: molecular mechanisms and physiological functions. Physiol. Rev. (2011) 91 651-690.
    • (2011) Physiol. Rev. , vol.91 , pp. 651-690
    • Francis, S.H.1    Blount, M.A.2    Corbin, J.D.3
  • 113
    • 33847068206 scopus 로고    scopus 로고
    • Overview of PDEs and their regulation
    • Omori K., Kotera J. Overview of PDEs and their regulation. Circ. Res. (2007) 100 309-327.
    • (2007) Circ. Res. , vol.100 , pp. 309-327
    • Omori, K.1    Kotera, J.2
  • 114
    • 33747193528 scopus 로고    scopus 로고
    • Layers of organization of cAMP microdomains in a simple cell
    • Martin A.C., Cooper D.M. Layers of organization of cAMP microdomains in a simple cell. Biochem. Soc. Trans. (2006) 34 480-483.
    • (2006) Biochem. Soc. Trans. , vol.34 , pp. 480-483
    • Martin, A.C.1    Cooper, D.M.2
  • 115
    • 0036500494 scopus 로고    scopus 로고
    • Discrete microdomains with high concentration of cAMP in stimulated rat neonatal cardiac myocytes
    • Zaccolo M., Pozzan T. Discrete microdomains with high concentration of cAMP in stimulated rat neonatal cardiac myocytes. Science (2002) 295 1711-1715.
    • (2002) Science , vol.295 , pp. 1711-1715
    • Zaccolo, M.1    Pozzan, T.2
  • 116
    • 45449112757 scopus 로고    scopus 로고
    • Real-time monitoring of phosphodiesterase inhibition in intact cells
    • Herget S., Lohse M.J., Nikolaev V.O. Real-time monitoring of phosphodiesterase inhibition in intact cells. Cell. Signal. (2008) 20 1423-1431.
    • (2008) Cell. Signal. , vol.20 , pp. 1423-1431
    • Herget, S.1    Lohse, M.J.2    Nikolaev, V.O.3
  • 117
    • 3142723295 scopus 로고    scopus 로고
    • Fluorescence resonance energy transfer-based analysis of cAMP dynamics in live neonatal rat cardiac myocytes reveals distinct functions of compartmentalized phosphodiesterases
    • Mongillo M., McSorley T., Evellin S. et al. Fluorescence resonance energy transfer-based analysis of cAMP dynamics in live neonatal rat cardiac myocytes reveals distinct functions of compartmentalized phosphodiesterases. Circ. Res. (2004) 95 67-75.
    • (2004) Circ. Res. , vol.95 , pp. 67-75
    • Mongillo, M.1    McSorley, T.2    Evellin, S.3
  • 118
    • 25144446880 scopus 로고    scopus 로고
    • Alterations in cAMP. Mediated signaling and their role in the pathophysiology of dilated cardiomyopathy
    • Movsesian M.A., Bristow M.R. Alterations in cAMP. Mediated signaling and their role in the pathophysiology of dilated cardiomyopathy. Curr. Top. Dev. Biol. (2005) 68 25-48.
    • (2005) Curr. Top. Dev. Biol. , vol.68 , pp. 25-48
    • Movsesian, M.A.1    Bristow, M.R.2
  • 119
    • 33947494913 scopus 로고    scopus 로고
    • Regulation of phosphodiesterase 3 and inducible cAMP early repressor in the heart
    • Yan C., Miller C.L., Abe J. Regulation of phosphodiesterase 3 and inducible cAMP early repressor in the heart. Circ. Res. (2007) 100 489-501.
    • (2007) Circ. Res. , vol.100 , pp. 489-501
    • Yan, C.1    Miller, C.L.2    Abe, J.3
  • 120
    • 34250156365 scopus 로고    scopus 로고
    • cAMP and cGMP signaling cross-talk: role of phosphodiesterases and implications for cardiac pathophysiology
    • Zaccolo M., Movsesian M.A. cAMP and cGMP signaling cross-talk: role of phosphodiesterases and implications for cardiac pathophysiology. Circ. Res. (2007) 100 1569-1578.
    • (2007) Circ. Res. , vol.100 , pp. 1569-1578
    • Zaccolo, M.1    Movsesian, M.A.2
  • 121
    • 34247105883 scopus 로고    scopus 로고
    • cAMP-specific phosphodiesterase-4 enzymes in the cardiovascular system: a molecular toolbox for generating compartmentalized cAMP signaling
    • Houslay M.D., Baillie G.S., Maurice D.H. cAMP-specific phosphodiesterase-4 enzymes in the cardiovascular system: a molecular toolbox for generating compartmentalized cAMP signaling. Circ. Res. (2007) 100 950-966.
    • (2007) Circ. Res. , vol.100 , pp. 950-966
    • Houslay, M.D.1    Baillie, G.S.2    Maurice, D.H.3
  • 122
    • 77951245640 scopus 로고    scopus 로고
    • cAMP-stimulated protein phosphatase 2A activity associated with muscle A kinase-anchoring protein (mAKAP) signaling complexes inhibits the phosphorylation and activity of the cAMP-specific phosphodiesterase PDE4D3
    • Dodge-Kafka K.L., Bauman A., Mayer N. et al. cAMP-stimulated protein phosphatase 2A activity associated with muscle A kinase-anchoring protein (mAKAP) signaling complexes inhibits the phosphorylation and activity of the cAMP-specific phosphodiesterase PDE4D3. J. Biol. Chem. (2010) 285 11078-11086.
    • (2010) J. Biol. Chem. , vol.285 , pp. 11078-11086
    • Dodge-Kafka, K.L.1    Bauman, A.2    Mayer, N.3
  • 123
    • 70350133628 scopus 로고    scopus 로고
    • Decreased expression and activity of cAMP phosphodiesterases in cardiac hypertrophy and its impact on β-adrenergic cAMP signals
    • Abi-Gerges A., Richter W., Lefebvre F. et al. Decreased expression and activity of cAMP phosphodiesterases in cardiac hypertrophy and its impact on β-adrenergic cAMP signals. Circ. Res. (2009) 105 784-792.
    • (2009) Circ. Res. , vol.105 , pp. 784-792
    • Abi-Gerges, A.1    Richter, W.2    Lefebvre, F.3
  • 124
    • 84886059882 scopus 로고    scopus 로고
    • Phosphodiesterase-2 is up-regulated in human failing hearts and blunts β-adrenergic responses in cardiomyocytes
    • Mehel H., Emons J., Vettel C. et al. Phosphodiesterase-2 is up-regulated in human failing hearts and blunts β-adrenergic responses in cardiomyocytes. J. Am. Coll. Cardiol. (2013) 62 1596-1606.
    • (2013) J. Am. Coll. Cardiol. , vol.62 , pp. 1596-1606
    • Mehel, H.1    Emons, J.2    Vettel, C.3
  • 125
    • 0027232199 scopus 로고
    • Growth factors in glomerulonephritis
    • Abboud H.E. Growth factors in glomerulonephritis. Kidney Int. (1993) 43 252-267.
    • (1993) Kidney Int. , vol.43 , pp. 252-267
    • Abboud, H.E.1
  • 126
    • 67449083682 scopus 로고    scopus 로고
    • The mesangial cell revisited: no cell is an Island
    • Schlöndorff D., Banas B. The mesangial cell revisited: no cell is an Island. J. Am. Soc. Nephrol. (2009) 20 1179-1187.
    • (2009) J. Am. Soc. Nephrol. , vol.20 , pp. 1179-1187
    • Schlöndorff, D.1    Banas, B.2
  • 127
    • 6344260591 scopus 로고    scopus 로고
    • Differential regulation of mesangial cell mitogenesis by cAMP phosphodiesterase isozymes 3 and 4
    • Cheng J., Thompson M.A., Walker H.J. et al. Differential regulation of mesangial cell mitogenesis by cAMP phosphodiesterase isozymes 3 and 4. Am. J. Physiol. Renal Physiol. (2004) 287 F940-F953.
    • (2004) Am. J. Physiol. Renal Physiol. , vol.287 , pp. F940-F953
    • Cheng, J.1    Thompson, M.A.2    Walker, H.J.3
  • 128
    • 0030999236 scopus 로고    scopus 로고
    • Compartmentalization of cAMP signaling in mesangial cells by phosphodiesterase isozymes PDE3 and PDE4 regulation of superoxidation and mitogenesis
    • Chini C.C., Grande J.P., Chini E.N., Dousa T.P. Compartmentalization of cAMP signaling in mesangial cells by phosphodiesterase isozymes PDE3 and PDE4 regulation of superoxidation and mitogenesis. J. Biol. Chem. (1997) 272 9854-9859.
    • (1997) J. Biol. Chem. , vol.272 , pp. 9854-9859
    • Chini, C.C.1    Grande, J.P.2    Chini, E.N.3    Dousa, T.P.4
  • 129
    • 0037264053 scopus 로고    scopus 로고
    • Compartmentalization of bicarbonate-sensitive adenylyl cyclase in distinct signaling microdomains
    • Zippin J.H., Chen Y., Nahirney P. et al. Compartmentalization of bicarbonate-sensitive adenylyl cyclase in distinct signaling microdomains. FASEB J. (2003) 17 82-84.
    • (2003) FASEB J. , vol.17 , pp. 82-84
    • Zippin, J.H.1    Chen, Y.2    Nahirney, P.3
  • 130
    • 0033956710 scopus 로고    scopus 로고
    • Differential activation of mitogen-activated protein kinases in experimental mesangioproliferative glomerulonephritis
    • Bokemeyer D., Ostendorf T., Kunter U., Lindemann M., Kramer H.J., Floege J. Differential activation of mitogen-activated protein kinases in experimental mesangioproliferative glomerulonephritis. J. Am. Soc. Nephrol. (2000) 11 232-240.
    • (2000) J. Am. Soc. Nephrol. , vol.11 , pp. 232-240
    • Bokemeyer, D.1    Ostendorf, T.2    Kunter, U.3    Lindemann, M.4    Kramer, H.J.5    Floege, J.6
  • 131
    • 0030664140 scopus 로고    scopus 로고
    • cAMP-dependent protein kinase inhibits the mitogenic action of vascular endothelial growth factor and fibroblast growth factor in capillary endothelial cells by blocking Raf activation
    • D'Angelo G., Lee H., Weiner R.I. cAMP-dependent protein kinase inhibits the mitogenic action of vascular endothelial growth factor and fibroblast growth factor in capillary endothelial cells by blocking Raf activation. J. Cell. Biochem. (1997) 67 353-366.
    • (1997) J. Cell. Biochem. , vol.67 , pp. 353-366
    • D'Angelo, G.1    Lee, H.2    Weiner, R.I.3
  • 132
    • 0028124505 scopus 로고
    • Mechanism of inhibition of Raf-1 by protein kinase A
    • Häfner S., Adler H.S., Mischak H. et al. Mechanism of inhibition of Raf-1 by protein kinase A. Mol. Cell. Biol. (1994) 14 6696-6703.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 6696-6703
    • Häfner, S.1    Adler, H.S.2    Mischak, H.3
  • 133
    • 0027485031 scopus 로고
    • Increasing cAMP attenuates activation of mitogen-activated protein kinase
    • Sevetson B.R., Kong X., Lawrence J.C. Increasing cAMP attenuates activation of mitogen-activated protein kinase. Proc. Natl Acad. Sci. USA (1993) 90 10305-10309.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 10305-10309
    • Sevetson, B.R.1    Kong, X.2    Lawrence, J.C.3
  • 134
    • 0028244071 scopus 로고
    • Formation of reactive oxygen metabolites in glomeruli is suppressed by inhibition of cAMP phosphodiesterase isozyme type IV
    • Chini C.C., Chini E.N., Williams J.M., Matousovic K., Dousa T.P. Formation of reactive oxygen metabolites in glomeruli is suppressed by inhibition of cAMP phosphodiesterase isozyme type IV. Kidney Int. (1994) 46 28-36.
    • (1994) Kidney Int. , vol.46 , pp. 28-36
    • Chini, C.C.1    Chini, E.N.2    Williams, J.M.3    Matousovic, K.4    Dousa, T.P.5
  • 135
    • 0342626743 scopus 로고    scopus 로고
    • Role of reactive oxygen species in glomerulonephritis
    • Gwinner W., Gröne H. Role of reactive oxygen species in glomerulonephritis. Nephrol. Dial. Transplant. (2000) 15 1127-1132.
    • (2000) Nephrol. Dial. Transplant. , vol.15 , pp. 1127-1132
    • Gwinner, W.1    Gröne, H.2
  • 136
    • 35348919486 scopus 로고    scopus 로고
    • Disrupted in schizophrenia 1 and phosphodiesterase 4B: towards an understanding of psychiatric illness
    • Millar J.K., Mackie S., Clapcote S.J. et al. Disrupted in schizophrenia 1 and phosphodiesterase 4B: towards an understanding of psychiatric illness. J. Physiol. (2007) 584 401-405.
    • (2007) J. Physiol. , vol.584 , pp. 401-405
    • Millar, J.K.1    Mackie, S.2    Clapcote, S.J.3
  • 137
    • 84939210523 scopus 로고    scopus 로고
    • Rapid publication by inhibitors of cAMP phosphodiesterase isozymes types III and IV
    • Tsuboi Y., Shankland S.J., Grande J.P. et al. Rapid publication by inhibitors of cAMP phosphodiesterase isozymes types III and IV, 1996.
    • (1996)
    • Tsuboi, Y.1    Shankland, S.J.2    Grande, J.P.3
  • 139
    • 27944502874 scopus 로고    scopus 로고
    • DISC1 and PDE4B are interacting genetic factors in schizophrenia that regulate cAMP signaling
    • Millar J.K., Pickard B.S., Mackie S. et al. DISC1 and PDE4B are interacting genetic factors in schizophrenia that regulate cAMP signaling. Science (2005) 310 1187-1191.
    • (2005) Science , vol.310 , pp. 1187-1191
    • Millar, J.K.1    Pickard, B.S.2    Mackie, S.3
  • 140
    • 34548389858 scopus 로고    scopus 로고
    • Isoform-selective susceptibility of DISC1/phosphodiesterase-4 complexes to dissociation by elevated intracellular cAMP levels
    • Murdoch H., Mackie S., Collins D.M. et al. Isoform-selective susceptibility of DISC1/phosphodiesterase-4 complexes to dissociation by elevated intracellular cAMP levels. J. Neurosci. (2007) 27 9513-9524.
    • (2007) J. Neurosci. , vol.27 , pp. 9513-9524
    • Murdoch, H.1    Mackie, S.2    Collins, D.M.3
  • 141
  • 143
    • 77951093706 scopus 로고    scopus 로고
    • Soluble adenylyl cyclase defines a nuclear cAMP microdomain in keratinocyte hyperproliferative skin diseases
    • Zippin J.H., Chadwick P.A., Levin L.R., Buck J., Magro C.M. Soluble adenylyl cyclase defines a nuclear cAMP microdomain in keratinocyte hyperproliferative skin diseases. J. Invest. Dermatol. (2010) 130 1279-1287.
    • (2010) J. Invest. Dermatol. , vol.130 , pp. 1279-1287
    • Zippin, J.H.1    Chadwick, P.A.2    Levin, L.R.3    Buck, J.4    Magro, C.M.5
  • 145
    • 1242285150 scopus 로고    scopus 로고
    • Bicarbonate-responsive "soluble" adenylyl cyclase defines a nuclear cAMP microdomain
    • Zippin J.H., Farrell J., Huron D. et al. Bicarbonate-responsive "soluble" adenylyl cyclase defines a nuclear cAMP microdomain. J. Cell Biol. (2004) 164 527-534.
    • (2004) J. Cell Biol. , vol.164 , pp. 527-534
    • Zippin, J.H.1    Farrell, J.2    Huron, D.3
  • 146
    • 33646472249 scopus 로고    scopus 로고
    • Two domains are critical for the nuclear localization of soluble adenylyl cyclase
    • Feng Q., Zhang Y., Li Y., Liu Z., Zuo J., Fang F. Two domains are critical for the nuclear localization of soluble adenylyl cyclase. Biochimie (2006) 88 319-328.
    • (2006) Biochimie , vol.88 , pp. 319-328
    • Feng, Q.1    Zhang, Y.2    Li, Y.3    Liu, Z.4    Zuo, J.5    Fang, F.6
  • 148
    • 0035888074 scopus 로고    scopus 로고
    • Estimating the world cancer burden: Globocan 2000
    • Parkin D.M., Bray F., Ferlay J., Pisani P. Estimating the world cancer burden: Globocan 2000. Int. J. Cancer (2001) 94 153-156.
    • (2001) Int. J. Cancer , vol.94 , pp. 153-156
    • Parkin, D.M.1    Bray, F.2    Ferlay, J.3    Pisani, P.4
  • 149
    • 0345701291 scopus 로고    scopus 로고
    • Bacterial enterotoxins are associated with resistance to colon cancer
    • Pitari G.M., Zingman L.V., Hodgson D.M. et al. Bacterial enterotoxins are associated with resistance to colon cancer. Proc. Natl Acad. Sci. USA (2003) 100 2695-2699.
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 2695-2699
    • Pitari, G.M.1    Zingman, L.V.2    Hodgson, D.M.3
  • 150
    • 0031041098 scopus 로고    scopus 로고
    • Guanosine 3',5'-cyclic monophosphate-dependent protein kinase II mediates heat-stable enterotoxin-provoked chloride secretion in rat intestine
    • Vaandrager A.B., Bot A.G., De Jonge H.R. Guanosine 3', 5'-cyclic monophosphate-dependent protein kinase II mediates heat-stable enterotoxin-provoked chloride secretion in rat intestine. Gastroenterology (1997) 112 437-443.
    • (1997) Gastroenterology , vol.112 , pp. 437-443
    • Vaandrager, A.B.1    Bot, A.G.2    De Jonge, H.R.3
  • 151
    • 0033000111 scopus 로고    scopus 로고
    • Guanylin regulatory peptides: structures, biological activities mediated by cyclic GMP and pathobiology
    • Forte L.R. Guanylin regulatory peptides: structures, biological activities mediated by cyclic GMP and pathobiology. Regul. Pept. (1999) 81 25-39.
    • (1999) Regul. Pept. , vol.81 , pp. 25-39
    • Forte, L.R.1
  • 152
    • 0033976962 scopus 로고    scopus 로고
    • Differential role of cyclic GMP-dependent protein kinase II in ion transport in murine small intestine and colon
    • Vaandrager A.B., Bot A.G., Ruth P., Pfeifer A., Hofmann F., De Jonge H.R. Differential role of cyclic GMP-dependent protein kinase II in ion transport in murine small intestine and colon. Gastroenterology (2000) 118 108-114.
    • (2000) Gastroenterology , vol.118 , pp. 108-114
    • Vaandrager, A.B.1    Bot, A.G.2    Ruth, P.3    Pfeifer, A.4    Hofmann, F.5    De Jonge, H.R.6
  • 153
    • 84866176492 scopus 로고    scopus 로고
    • Inhibition of phosphodiesterase-4 (PDE4) activity triggers luminal apoptosis and AKT dephosphorylation in a 3-D colonic-crypt model
    • Tsunoda T., Ota T., Fujimoto T. et al. Inhibition of phosphodiesterase-4 (PDE4) activity triggers luminal apoptosis and AKT dephosphorylation in a 3-D colonic-crypt model. Mol. Cancer (2012) 11 46.
    • (2012) Mol. Cancer , vol.11 , pp. 46
    • Tsunoda, T.1    Ota, T.2    Fujimoto, T.3
  • 154
    • 0027905014 scopus 로고
    • Altered growth of human colon cancer cell lines disrupted at activated Ki-ras
    • Shirasawa S., Furuse M., Yokoyama N., Sasazuki T. Altered growth of human colon cancer cell lines disrupted at activated Ki-ras. Science (1993) 260 85-88.
    • (1993) Science , vol.260 , pp. 85-88
    • Shirasawa, S.1    Furuse, M.2    Yokoyama, N.3    Sasazuki, T.4
  • 155
    • 66249125722 scopus 로고    scopus 로고
    • Identification of PDE4D as a proliferation promoting factor in prostate cancer using a sleeping beauty transposon-based somatic mutagenesis screen
    • Rahrmann E.P., Collier L.S., Knutson T.P. et al. Identification of PDE4D as a proliferation promoting factor in prostate cancer using a sleeping beauty transposon-based somatic mutagenesis screen. Cancer Res. (2009) 69 4388-4397.
    • (2009) Cancer Res. , vol.69 , pp. 4388-4397
    • Rahrmann, E.P.1    Collier, L.S.2    Knutson, T.P.3
  • 157
    • 84855663258 scopus 로고    scopus 로고
    • Can β2-adrenoceptor agonists, anticholinergic drugs, and theophylline contribute to the control of pulmonary inflammation and emphysema in COPD?
    • Zhang W.-H., Zhang Y., Cui Y.-Y. et al. Can β2-adrenoceptor agonists, anticholinergic drugs, and theophylline contribute to the control of pulmonary inflammation and emphysema in COPD? Fundam. Clin. Pharmacol. (2012) 26 118-134.
    • (2012) Fundam. Clin. Pharmacol. , vol.26 , pp. 118-134
    • Zhang, W.-H.1    Zhang, Y.2    Cui, Y.-Y.3
  • 158
    • 78651457445 scopus 로고    scopus 로고
    • Oncogenic BRAF induces melanoma cell invasion by downregulating the cGMP-specific phosphodiesterase PDE5A
    • Arozarena I., Sanchez-Laorden B., Packer L. et al. Oncogenic BRAF induces melanoma cell invasion by downregulating the cGMP-specific phosphodiesterase PDE5A. Cancer Cell (2011) 19 45-57.
    • (2011) Cancer Cell , vol.19 , pp. 45-57
    • Arozarena, I.1    Sanchez-Laorden, B.2    Packer, L.3
  • 159
    • 78651446644 scopus 로고    scopus 로고
    • Hard times for oncogenic BRAF-expressing melanoma cells
    • Houslay M.D. Hard times for oncogenic BRAF-expressing melanoma cells. Cancer Cell (2011) 19 3-4.
    • (2011) Cancer Cell , vol.19 , pp. 3-4
    • Houslay, M.D.1
  • 160
    • 73149104650 scopus 로고    scopus 로고
    • Sulindac sulfide selectively inhibits growth and induces apoptosis of human breast tumor cells by phosphodiesterase 5 inhibition, elevation of cyclic GMP, and activation of protein kinase G
    • Tinsley H.N., Gary B.D., Keeton A.B. et al. Sulindac sulfide selectively inhibits growth and induces apoptosis of human breast tumor cells by phosphodiesterase 5 inhibition, elevation of cyclic GMP, and activation of protein kinase G. Mol. Cancer Ther. (2009) 8 3331-3340.
    • (2009) Mol. Cancer Ther. , vol.8 , pp. 3331-3340
    • Tinsley, H.N.1    Gary, B.D.2    Keeton, A.B.3
  • 161
    • 84876083813 scopus 로고    scopus 로고
    • cAMP/PKA signaling defects in tumors: genetics and tissue-specific pluripotential cell-derived lesions in human and mouse
    • Stratakis C.A. cAMP/PKA signaling defects in tumors: genetics and tissue-specific pluripotential cell-derived lesions in human and mouse. Mol. Cell. Endocrinol. (2013) 371 208-220.
    • (2013) Mol. Cell. Endocrinol. , vol.371 , pp. 208-220
    • Stratakis, C.A.1
  • 162
    • 59849101194 scopus 로고    scopus 로고
    • New genes and/or molecular pathways associated with adrenal hyperplasias and related adrenocortical tumors
    • Stratakis C.A. New genes and/or molecular pathways associated with adrenal hyperplasias and related adrenocortical tumors. Mol. Cell. Endocrinol. (2009) 300 152-157.
    • (2009) Mol. Cell. Endocrinol. , vol.300 , pp. 152-157
    • Stratakis, C.A.1
  • 163
    • 33747183132 scopus 로고    scopus 로고
    • Protection from apoptotic cell death by cilostazol, phosphodiesterase type III inhibitor, via cAMP-dependent protein kinase activation
    • Kim M.J., Lee J.H., Park S.Y. et al. Protection from apoptotic cell death by cilostazol, phosphodiesterase type III inhibitor, via cAMP-dependent protein kinase activation. Pharmacol. Res. (2006) 54 261-267.
    • (2006) Pharmacol. Res. , vol.54 , pp. 261-267
    • Kim, M.J.1    Lee, J.H.2    Park, S.Y.3
  • 165
    • 0021207286 scopus 로고
    • Demonstration of bovine brain calmodulin-dependent cyclic nucleotide phosphodiesterase isozymes by monoclonal antibodies
    • Sharma R.K., Adachi A.M., Adachi K., Wang J.H. Demonstration of bovine brain calmodulin-dependent cyclic nucleotide phosphodiesterase isozymes by monoclonal antibodies. J. Biol. Chem. (1984) 259 9248-9254.
    • (1984) J. Biol. Chem. , vol.259 , pp. 9248-9254
    • Sharma, R.K.1    Adachi, A.M.2    Adachi, K.3    Wang, J.H.4
  • 166
    • 0029590775 scopus 로고
    • Identification of inhibitory and calmodulin-binding domains of the PDE1A1 and PDE1A2 calmodulin-stimulated cyclic nucleotide phosphodiesterases
    • Sonnenburg W.K., Seger D., Kwak K.S., Huang J., Charbonneau H., Beavo J.A. Identification of inhibitory and calmodulin-binding domains of the PDE1A1 and PDE1A2 calmodulin-stimulated cyclic nucleotide phosphodiesterases. J. Biol. Chem. (1995) 270 30989-31000.
    • (1995) J. Biol. Chem. , vol.270 , pp. 30989-31000
    • Sonnenburg, W.K.1    Seger, D.2    Kwak, K.S.3    Huang, J.4    Charbonneau, H.5    Beavo, J.A.6
  • 168
    • 0022559490 scopus 로고
    • +-dependent phosphorylation and dephosphorylation of 63-kDa subunit-containing bovine brain calmodulin-stimulated cyclic nucleotide phosphodiesterase isozyme
    • +-dependent phosphorylation and dephosphorylation of 63-kDa subunit-containing bovine brain calmodulin-stimulated cyclic nucleotide phosphodiesterase isozyme. J. Biol. Chem. (1986) 261 1322-1328.
    • (1986) J. Biol. Chem. , vol.261 , pp. 1322-1328
    • Sharma, R.K.1    Wang, J.H.2
  • 169
    • 12244313740 scopus 로고    scopus 로고
    • Selective up-regulation of PDE1B2 upon monocyte-to-macrophage differentiation
    • Bender A.T., Ostenson C.L., Wang E.H., Beavo J.A. Selective up-regulation of PDE1B2 upon monocyte-to-macrophage differentiation. Proc. Natl Acad. Sci. USA (2005) 102 497-502.
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 497-502
    • Bender, A.T.1    Ostenson, C.L.2    Wang, E.H.3    Beavo, J.A.4
  • 170
    • 0023683480 scopus 로고
    • Purification of calmodulin-stimulated cyclic nucleotide phosphodiesterase by monoclonal antibody affinity chromatography
    • Hansen R.S., Charbonneau H., Beavo J.A.. Purification of calmodulin-stimulated cyclic nucleotide phosphodiesterase by monoclonal antibody affinity chromatography. Methods Enzymol. (1988) 159 543-557.
    • (1988) Methods Enzymol. , vol.159 , pp. 543-557
    • Hansen, R.S.1    Charbonneau, H.2    Beavo, J.A.3
  • 171
    • 0030064790 scopus 로고    scopus 로고
    • 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.S. et al. Isolation and characterization of cDNAs corresponding to two human calcium, calmodulin-regulated, 3', 5'-cyclic nucleotide phosphodiesterases. J. Biol. Chem. (1996) 271 796-806.
    • (1996) J. Biol. Chem. , vol.271 , pp. 796-806
    • Loughney, K.1    Martins, T.J.2    Harris, E.A.S.3
  • 172
    • 0029845929 scopus 로고    scopus 로고
    • The calmodulin-dependent phosphodiesterase gene PDE1C encodes several functionally different splice variants in a tissue-specific manner
    • Yan C., Zhao A.Z., Bentley J.K., Beavo J.A. The calmodulin-dependent phosphodiesterase gene PDE1C encodes several functionally different splice variants in a tissue-specific manner. J. Biol. Chem. (1996) 271 25699-25706.
    • (1996) J. Biol. Chem. , vol.271 , pp. 25699-25706
    • Yan, C.1    Zhao, A.Z.2    Bentley, J.K.3    Beavo, J.A.4
  • 173
    • 0020354593 scopus 로고
    • Interaction of calcium antagonists with cyclic AMP phosphodiesterases and calmodulin
    • Epstein P.M., Fiss K., Hachisu R., Andrenyak D.M. Interaction of calcium antagonists with cyclic AMP phosphodiesterases and calmodulin. Biochem. Biophys. Res. Commun. (1982) 105 1142-1149.
    • (1982) Biochem. Biophys. Res. Commun. , vol.105 , pp. 1142-1149
    • Epstein, P.M.1    Fiss, K.2    Hachisu, R.3    Andrenyak, D.M.4
  • 174
    • 0021337094 scopus 로고
    • Effects of vinpocetine on cyclic nucleotide metabolism in vascular smooth muscle
    • Hagiwara M., Endo T., Hidaka H. Effects of vinpocetine on cyclic nucleotide metabolism in vascular smooth muscle. Biochem. Pharmacol. (1984) 33 453-457.
    • (1984) Biochem. Pharmacol. , vol.33 , pp. 453-457
    • Hagiwara, M.1    Endo, T.2    Hidaka, H.3
  • 175
    • 24144491356 scopus 로고    scopus 로고
    • The role of cyclic nucleotide phosphodiesterases in the regulation of adipocyte lipolysis
    • Snyder P.B., Esselstyn J.M., Loughney K., Wolda S.L., Florio V.A. The role of cyclic nucleotide phosphodiesterases in the regulation of adipocyte lipolysis. J. Lipid Res. (2005) 46 494-503.
    • (2005) J. Lipid Res. , vol.46 , pp. 494-503
    • Snyder, P.B.1    Esselstyn, J.M.2    Loughney, K.3    Wolda, S.L.4    Florio, V.A.5
  • 176
    • 10544224533 scopus 로고    scopus 로고
    • Antiplatelet and antiproliferative effects of SCH 51866, a novel type 1 and type 5 phosphodiesterase inhibitor
    • Vemulapalli S., Watkins R.W., Chintala M. et al. Antiplatelet and antiproliferative effects of SCH 51866, a novel type 1 and type 5 phosphodiesterase inhibitor. J. Cardiovasc. Pharmacol. (1996) 28 862-869.
    • (1996) J. Cardiovasc. Pharmacol. , vol.28 , pp. 862-869
    • Vemulapalli, S.1    Watkins, R.W.2    Chintala, M.3
  • 177
    • 0031006150 scopus 로고    scopus 로고
    • 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. Isolation and characterization of human cDNAs encoding a cGMP-stimulated 3', 5'-cyclic nucleotide phosphodiesterase. Gene (1997) 191 89-95.
    • (1997) Gene , vol.191 , pp. 89-95
    • Rosman, G.J.1    Martins, T.J.2    Sonnenburg, W.K.3    Beavo, J.A.4    Ferguson, K.5    Loughney, K.6
  • 178
    • 0029088562 scopus 로고
    • Isozyme selective inhibition of cGMP-stimulated cyclic nucleotide phosphodiesterases by erythro-9-(2-hydroxy-3-nonyl) adenine
    • Podzuweit T., Nennstiel P., Müller A. Isozyme selective inhibition of cGMP-stimulated cyclic nucleotide phosphodiesterases by erythro-9-(2-hydroxy-3-nonyl) adenine. Cell. Signal. (1995) 7 733-738.
    • (1995) Cell. Signal. , vol.7 , pp. 733-738
    • Podzuweit, T.1    Nennstiel, P.2    Müller, A.3
  • 179
    • 8844220521 scopus 로고    scopus 로고
    • Inhibition of phosphodiesterase 2 increases neuronal cGMP, synaptic plasticity and memory performance
    • Boess F.G., Hendrix M., van der Staay F.-J. et al. Inhibition of phosphodiesterase 2 increases neuronal cGMP, synaptic plasticity and memory performance. Neuropharmacology (2004) 47 1081-1092.
    • (2004) Neuropharmacology , vol.47 , pp. 1081-1092
    • Boess, F.G.1    Hendrix, M.2    van der Staay, F.-J.3
  • 180
    • 20944438000 scopus 로고    scopus 로고
    • Tumor necrosis factor-α-dependent expression of phosphodiesterase 2: role in endothelial hyperpermeability
    • Seybold J., Thomas D., Witzenrath M. et al. Tumor necrosis factor-α-dependent expression of phosphodiesterase 2: role in endothelial hyperpermeability. Blood (2005) 105 3569-3576.
    • (2005) Blood , vol.105 , pp. 3569-3576
    • Seybold, J.1    Thomas, D.2    Witzenrath, M.3
  • 181
    • 1542544909 scopus 로고    scopus 로고
    • cGMP-phosphodiesterase activity is up-regulated in response to pressure overload of rat ventricles
    • Yanaka N., Kurosawa Y., Minami K., Kawai E., Omori K. cGMP-phosphodiesterase activity is up-regulated in response to pressure overload of rat ventricles. Biosci. Biotechnol. Biochem. (2003) 67 973-979.
    • (2003) Biosci. Biotechnol. Biochem. , vol.67 , pp. 973-979
    • Yanaka, N.1    Kurosawa, Y.2    Minami, K.3    Kawai, E.4    Omori, K.5
  • 182
    • 0032811473 scopus 로고    scopus 로고
    • Evidence for the presence of several phosphodiesterase isoforms in brown adipose tissue of Zucker rats: modulation of PDE2 by the fa gene expression
    • Coudray C., Charon C., Komas N. et al. Evidence for the presence of several phosphodiesterase isoforms in brown adipose tissue of Zucker rats: modulation of PDE2 by the fa gene expression. FEBS Lett. (1999) 456 207-210.
    • (1999) FEBS Lett. , vol.456 , pp. 207-210
    • Coudray, C.1    Charon, C.2    Komas, N.3
  • 183
    • 0030940907 scopus 로고    scopus 로고
    • A subset of olfactory neurons that selectively express cGMP-stimulated phosphodiesterase (PDE2) and guanylyl cyclase-D define a unique olfactory signal transduction pathway
    • Juilfs D.M., Fülle H.-J., Zhao A.Z., Houslay M.D., Garbers D.L., Beavo J.A. A subset of olfactory neurons that selectively express cGMP-stimulated phosphodiesterase (PDE2) and guanylyl cyclase-D define a unique olfactory signal transduction pathway. Proc. Natl Acad. Sci. USA (1997) 94 3388-3395.
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 3388-3395
    • Juilfs, D.M.1    Fülle, H.-J.2    Zhao, A.Z.3    Houslay, M.D.4    Garbers, D.L.5    Beavo, J.A.6
  • 185
    • 0021359546 scopus 로고
    • Purification and characterization of a human platelet cyclic nucleotide phosphodiesterase
    • Grant P.G., Colman R.W. Purification and characterization of a human platelet cyclic nucleotide phosphodiesterase. Biochemistry (1984) 23 1801-1807.
    • (1984) Biochemistry , vol.23 , pp. 1801-1807
    • Grant, P.G.1    Colman, R.W.2
  • 186
    • 0022454622 scopus 로고
    • Isolation and characterization of bovine cardiac muscle cGMP-inhibited phosphodiesterase: a receptor for new cardiotonic drugs
    • Harrison S.A., Reifsnyder D.H., Gallis B., Cadd G.G., Beavo J.A. Isolation and characterization of bovine cardiac muscle cGMP-inhibited phosphodiesterase: a receptor for new cardiotonic drugs. Mol. Pharmacol. (1986) 29 506-514.
    • (1986) Mol. Pharmacol. , vol.29 , pp. 506-514
    • Harrison, S.A.1    Reifsnyder, D.H.2    Gallis, B.3    Cadd, G.G.4    Beavo, J.A.5
  • 187
    • 0023178721 scopus 로고
    • Purification of the putative hormone-sensitive cyclic AMP phosphodiesterase from rat adipose tissue using a derivative of cilostamide as a novel affinity ligand
    • Degerman E., Belfrage P., Newman A.H., Rice K.C., Manganiello V.C. Purification of the putative hormone-sensitive cyclic AMP phosphodiesterase from rat adipose tissue using a derivative of cilostamide as a novel affinity ligand. J. Biol. Chem. (1987) 262 5797-5807.
    • (1987) J. Biol. Chem. , vol.262 , pp. 5797-5807
    • Degerman, E.1    Belfrage, P.2    Newman, A.H.3    Rice, K.C.4    Manganiello, V.C.5
  • 188
    • 0020352343 scopus 로고
    • HL 725, an extremely potent inhibitor of platelet phosphodiesterase and induced platelet aggregation in vitro
    • Ruppert D., Weithmann K.U. HL 725, an extremely potent inhibitor of platelet phosphodiesterase and induced platelet aggregation in vitro. Life Sci. (1982) 31 2037-2043.
    • (1982) Life Sci. , vol.31 , pp. 2037-2043
    • Ruppert, D.1    Weithmann, K.U.2
  • 189
    • 0023944556 scopus 로고
    • Effects of cilostazol, a selective cAMP phosphodiesterase inhibitor on the contraction of vascular smooth muscle
    • Tanaka T., Ishikawa T., Hagiwara M., Onoda K., Itoh H., Hidaka H. Effects of cilostazol, a selective cAMP phosphodiesterase inhibitor on the contraction of vascular smooth muscle. Pharmacology (1988) 36 313-320.
    • (1988) Pharmacology , vol.36 , pp. 313-320
    • Tanaka, T.1    Ishikawa, T.2    Hagiwara, M.3    Onoda, K.4    Itoh, H.5    Hidaka, H.6
  • 190
    • 0018640656 scopus 로고
    • Selective inhibitor of platelet cyclic adenosine monophosphate phosphodiesterase, cilostamide, inhibits platelet aggregation
    • Hidaka H., Hayashi H., Kohri H. et al. Selective inhibitor of platelet cyclic adenosine monophosphate phosphodiesterase, cilostamide, inhibits platelet aggregation. J. Pharmacol. Exp. Ther. (1979) 211 26-30.
    • (1979) J. Pharmacol. Exp. Ther. , vol.211 , pp. 26-30
    • Hidaka, H.1    Hayashi, H.2    Kohri, H.3
  • 191
    • 0033985281 scopus 로고    scopus 로고
    • Potent effects of novel anti-platelet aggregatory cilostamide analogues on recombinant cyclic nucleotide phosphodiesterase isozyme activity
    • Sudo T., Tachibana K., Toga K. et al. Potent effects of novel anti-platelet aggregatory cilostamide analogues on recombinant cyclic nucleotide phosphodiesterase isozyme activity. Biochem. Pharmacol. (2000) 59 347-356.
    • (2000) Biochem. Pharmacol. , vol.59 , pp. 347-356
    • Sudo, T.1    Tachibana, K.2    Toga, K.3
  • 192
    • 0031578230 scopus 로고    scopus 로고
    • Expression, purification, and characterization of human cAMP-specific phosphodiesterase (PDE4) subtypes A, B, C, and D
    • Wang P., Myers J.G., Wu P., Cheewatrakoolpong B., Egan R.W., Billah M.M. Expression, purification, and characterization of human cAMP-specific phosphodiesterase (PDE4) subtypes A, B, C, and D. Biochem. Biophys. Res. Commun. (1997) 234 320-324.
    • (1997) Biochem. Biophys. Res. Commun. , vol.234 , pp. 320-324
    • Wang, P.1    Myers, J.G.2    Wu, P.3    Cheewatrakoolpong, B.4    Egan, R.W.5    Billah, M.M.6
  • 193
    • 0031712906 scopus 로고    scopus 로고
    • Heterologous expression and purification of recombinant rolipram-sensitive cyclic AMP-specific phosphodiesterases
    • Salanova M., Jin S.-L.C., Conti M. Heterologous expression and purification of recombinant rolipram-sensitive cyclic AMP-specific phosphodiesterases. Methods (1998) 14 55-64.
    • (1998) Methods , vol.14 , pp. 55-64
    • Salanova, M.1    Jin, S.-L.2    Conti, M.3
  • 194
    • 0035030692 scopus 로고    scopus 로고
    • Molecular cloning, genomic positioning, promoter identification, and characterization of the novel cyclic AMP-specific phosphodiesterase PDE4A10
    • Rena G., Begg F., Ross A. et al. Molecular cloning, genomic positioning, promoter identification, and characterization of the novel cyclic AMP-specific phosphodiesterase PDE4A10. Mol. Pharmacol. (2001) 59 996-1011.
    • (2001) Mol. Pharmacol. , vol.59 , pp. 996-1011
    • Rena, G.1    Begg, F.2    Ross, A.3
  • 195
    • 21744438149 scopus 로고    scopus 로고
    • Identification and characterization of PDE4A11, a novel, widely expressed long isoform encoded by the human PDE4A cAMP phosphodiesterase gene
    • Wallace D.A., Johnston L.A., Huston E. et al. Identification and characterization of PDE4A11, a novel, widely expressed long isoform encoded by the human PDE4A cAMP phosphodiesterase gene. Mol. Pharmacol. (2005) 67 1920-1934.
    • (2005) Mol. Pharmacol. , vol.67 , pp. 1920-1934
    • Wallace, D.A.1    Johnston, L.A.2    Huston, E.3
  • 196
    • 0030697068 scopus 로고    scopus 로고
    • Molecular cloning and transient expression in COS7 cells of a novel human PDE4B cAMP-specific phosphodiesterase, HSPDE4B3
    • Huston E., Lumb S., Russell A. et al. Molecular cloning and transient expression in COS7 cells of a novel human PDE4B cAMP-specific phosphodiesterase, HSPDE4B3. Biochem. J. (1997) 328 549-558.
    • (1997) Biochem. J. , vol.328 , pp. 549-558
    • Huston, E.1    Lumb, S.2    Russell, A.3
  • 197
    • 0017120229 scopus 로고
    • 4-(3-cyclopentyloxy-4-methoxyphenyl)-2-pyrrolidone (ZK 62711): a potent inhibitor of adenosine cyclic 3',5'-monophosphate phosphodiesterases in homogenates and tissue slices from rat brain
    • Schwabe U., MiyakeI M., Ohga Y., Daly J.W. 4-(3-cyclopentyloxy-4-methoxyphenyl)-2-pyrrolidone (ZK 62711): a potent inhibitor of adenosine cyclic 3', 5'-monophosphate phosphodiesterases in homogenates and tissue slices from rat brain. Mol. Pharmacol. (1976) 12 900-910.
    • (1976) Mol. Pharmacol. , vol.12 , pp. 900-910
    • Schwabe, U.1    MiyakeI, M.2    Ohga, Y.3    Daly, J.W.4
  • 198
    • 0035084103 scopus 로고    scopus 로고
    • Anti-inflammatory and immunomodulatory potential of the novel PDE4 inhibitor roflumilast in vitro
    • Hatzelmann A., Schudt C. Anti-inflammatory and immunomodulatory potential of the novel PDE4 inhibitor roflumilast in vitro. J. Pharmacol. Exp. Ther. (2001) 297 267-279.
    • (2001) J. Pharmacol. Exp. Ther. , vol.297 , pp. 267-279
    • Hatzelmann, A.1    Schudt, C.2
  • 199
    • 0031911575 scopus 로고    scopus 로고
    • SB 207499 (Ariflo), a potent and selective second-generation phosphodiesterase 4 inhibitor. In vitro anti-inflammatory actions
    • Barnette M.S., Christensen S.B., Essayan D.M. et al. SB 207499 (Ariflo), a potent and selective second-generation phosphodiesterase 4 inhibitor. In vitro anti-inflammatory actions. J. Pharmacol. Exp. Ther. (1998) 284 420-426.
    • (1998) J. Pharmacol. Exp. Ther. , vol.284 , pp. 420-426
    • Barnette, M.S.1    Christensen, S.B.2    Essayan, D.M.3
  • 200
    • 0016768129 scopus 로고
    • Alterations in the hydrolytic activity, inhibitor sensitivity and molecular size of the rat erythrocyte cyclic AMP phosphodiesterase by calcium and hypertonic sodium chloride
    • Sheppard H., Tsien W.H. Alterations in the hydrolytic activity, inhibitor sensitivity and molecular size of the rat erythrocyte cyclic AMP phosphodiesterase by calcium and hypertonic sodium chloride. J. Cyclic Nucleotide Res. (1975) 1 237-242.
    • (1975) J. Cyclic Nucleotide Res. , vol.1 , pp. 237-242
    • Sheppard, H.1    Tsien, W.H.2
  • 201
    • 0034531342 scopus 로고    scopus 로고
    • The effect of selective and non-selective phosphodiesterase inhibitors on allergen- and leukotriene C(4)-induced contractions in passively sensitized human airways
    • Schmidt D.T., Watson N., Dent G. et al. The effect of selective and non-selective phosphodiesterase inhibitors on allergen- and leukotriene C(4)-induced contractions in passively sensitized human airways. Br. J. Pharmacol. (2000) 131 1607-1618.
    • (2000) Br. J. Pharmacol. , vol.131 , pp. 1607-1618
    • Schmidt, D.T.1    Watson, N.2    Dent, G.3
  • 202
    • 0037124189 scopus 로고    scopus 로고
    • Synthesis and profile of SCH351591, a novel PDE4 inhibitor
    • Billah M., Cooper N., Cuss F. et al. Synthesis and profile of SCH351591, a novel PDE4 inhibitor. Bioorg. Med. Chem. Lett. (2002) 12 1621-1623.
    • (2002) Bioorg. Med. Chem. Lett. , vol.12 , pp. 1621-1623
    • Billah, M.1    Cooper, N.2    Cuss, F.3
  • 203
    • 18744362427 scopus 로고    scopus 로고
    • Pharmacokinetic and pharmacodynamic profile following oral administration of the phosphodiesterase (PDE)4 inhibitor V11294A in healthy volunteers
    • Gale D.D., Landells L.J., Spina D. et al. Pharmacokinetic and pharmacodynamic profile following oral administration of the phosphodiesterase (PDE)4 inhibitor V11294A in healthy volunteers. Br. J. Clin. Pharmacol. (2002) 54 478-484.
    • (2002) Br. J. Clin. Pharmacol. , vol.54 , pp. 478-484
    • Gale, D.D.1    Landells, L.J.2    Spina, D.3
  • 204
    • 0031601339 scopus 로고    scopus 로고
    • The multienzyme PDE4 cyclic adenosine monophosphate-specific phosphodiesterase family: intracellular targeting, regulation, and selective inhibition by compounds exerting anti-inflammatory and antidepressant actions
    • Houslay M.D., Sullivan M., Bolger G.B. The multienzyme PDE4 cyclic adenosine monophosphate-specific phosphodiesterase family: intracellular targeting, regulation, and selective inhibition by compounds exerting anti-inflammatory and antidepressant actions. Adv. Pharmacol. (1998) 44 225-342.
    • (1998) Adv. Pharmacol. , vol.44 , pp. 225-342
    • Houslay, M.D.1    Sullivan, M.2    Bolger, G.B.3
  • 205
    • 0028887031 scopus 로고
    • Section review: cardiovascular & renal: cyclic nucleotide phosphodiesterases as therapeutic targets in cardiovascular diseases
    • Stoclet J.-C., Keravis T., Komas N., Lugnier C. Section review: cardiovascular & renal: cyclic nucleotide phosphodiesterases as therapeutic targets in cardiovascular diseases. Expert Opin. Investig. Drugs (1995) 4 1081-1100.
    • (1995) Expert Opin. Investig. Drugs , vol.4 , pp. 1081-1100
    • Stoclet, J.-C.1    Keravis, T.2    Komas, N.3    Lugnier, C.4
  • 206
    • 33646847852 scopus 로고    scopus 로고
    • Phosphodiesterase-5 Gln817 is critical for cGMP, vardenafil, or sildenafil affinity: its orientation impacts cGMP but not cAMP affinity
    • Zoraghi R., Corbin J.D., Francis S.H. Phosphodiesterase-5 Gln817 is critical for cGMP, vardenafil, or sildenafil affinity: its orientation impacts cGMP but not cAMP affinity. J. Biol. Chem. (2006) 281 5553-5558.
    • (2006) J. Biol. Chem. , vol.281 , pp. 5553-5558
    • Zoraghi, R.1    Corbin, J.D.2    Francis, S.H.3
  • 207
    • 0022548645 scopus 로고
    • Selective inhibition of cyclic nucleotide phosphodiesterases of human, bovine and rat aorta
    • Lugnier C., Schoeffter P., Le Bec A., Strouthou E., Stoclet J.-C. Selective inhibition of cyclic nucleotide phosphodiesterases of human, bovine and rat aorta. Biochem. Pharmacol. (1986) 35 1743-1751.
    • (1986) Biochem. Pharmacol. , vol.35 , pp. 1743-1751
    • Lugnier, C.1    Schoeffter, P.2    Le Bec, A.3    Strouthou, E.4    Stoclet, J.-C.5
  • 208
    • 0030154874 scopus 로고    scopus 로고
    • Sildenafil: an orally active type 5 cyclic GMP-specific phosphodiesterase inhibitor for the treatment of penile erectile dysfunction
    • Boolell M., Allen M.J., Ballard S.A. et al. Sildenafil: an orally active type 5 cyclic GMP-specific phosphodiesterase inhibitor for the treatment of penile erectile dysfunction. Int. J. Impot. Res. (1996) 8 47-52.
    • (1996) Int. J. Impot. Res. , vol.8 , pp. 47-52
    • Boolell, M.1    Allen, M.J.2    Ballard, S.A.3
  • 209
    • 0035092722 scopus 로고    scopus 로고
    • The oral efficacy of vardenafil hydrochloride for inducing penile erection in a conscious rabbit model
    • Bischoff E., Niewoehner U., Haning H., Es Sayed M., Schenke T., Schlemmer K.H. The oral efficacy of vardenafil hydrochloride for inducing penile erection in a conscious rabbit model. J. Urol. (2001) 165 1316-1318.
    • (2001) J. Urol. , vol.165 , pp. 1316-1318
    • Bischoff, E.1    Niewoehner, U.2    Haning, H.3    Es Sayed, M.4    Schenke, T.5    Schlemmer, K.H.6
  • 210
    • 0035070379 scopus 로고    scopus 로고
    • On-demand IC351 (Cialis) enhances erectile function in patients with erectile dysfunction
    • Padma-Nathan H., McMurray J.G., Pullman W.E. et al. On-demand IC351 (Cialis) enhances erectile function in patients with erectile dysfunction. Int. J. Impot. Res. (2001) 13 2-9.
    • (2001) Int. J. Impot. Res. , vol.13 , pp. 2-9
    • Padma-Nathan, H.1    McMurray, J.G.2    Pullman, W.E.3
  • 211
    • 0034305318 scopus 로고    scopus 로고
    • Erectogenic effect of the selective phosphodiesterase type 5 inhibitor, DA-8159
    • Oh T.Y., Kang K.K., Ahn B.O., Yoo M., Kim W.B. Erectogenic effect of the selective phosphodiesterase type 5 inhibitor, DA-8159. Arch. Pharm. Res. (2000) 23 471-476.
    • (2000) Arch. Pharm. Res. , vol.23 , pp. 471-476
    • Oh, T.Y.1    Kang, K.K.2    Ahn, B.O.3    Yoo, M.4    Kim, W.B.5
  • 212
    • 0028885519 scopus 로고
    • Characterization of a novel potent and specific inhibitor of type v phosphodiesterase
    • Coste H., Grondin P. Characterization of a novel potent and specific inhibitor of type v phosphodiesterase. Biochem. Pharmacol. (1995) 50 1577-1585.
    • (1995) Biochem. Pharmacol. , vol.50 , pp. 1577-1585
    • Coste, H.1    Grondin, P.2
  • 213
    • 0029084745 scopus 로고
    • Isoenzymes of cyclic nucleotide phosphodiesterase in the human aorta: characterization and the effects of E4021
    • Miyahara M., Ito M., Itoh H. et al. Isoenzymes of cyclic nucleotide phosphodiesterase in the human aorta: characterization and the effects of E4021. Eur. J. Pharmacol. (1995) 284 25-33.
    • (1995) Eur. J. Pharmacol. , vol.284 , pp. 25-33
    • Miyahara, M.1    Ito, M.2    Itoh, H.3
  • 214
    • 0028817177 scopus 로고
    • A selective type V phosphodiesterase inhibitor, E4021, dilates porcine large coronary artery
    • Saeki T., Adachi H., Takase Y., Yoshitake S., Souda S., Saito I. A selective type V phosphodiesterase inhibitor, E4021, dilates porcine large coronary artery. J. Pharmacol. Exp. Ther. (1995) 272 825-831.
    • (1995) J. Pharmacol. Exp. Ther. , vol.272 , pp. 825-831
    • Saeki, T.1    Adachi, H.2    Takase, Y.3    Yoshitake, S.4    Souda, S.5    Saito, I.6
  • 215
    • 0024306482 scopus 로고
    • Inhibition and stimulation of photoreceptor phosphodiesterases by dipyridamole and M&B 22,948
    • Gillespie P.G., Beavo J.A. Inhibition and stimulation of photoreceptor phosphodiesterases by dipyridamole and M&B 22, 948. Mol. Pharmacol. (1989) 36 773-781.
    • (1989) Mol. Pharmacol. , vol.36 , pp. 773-781
    • Gillespie, P.G.1    Beavo, J.A.2
  • 216
    • 0033054952 scopus 로고    scopus 로고
    • Potency and mechanism of action of E4021, a type 5 phosphodiesterase isozyme-selective inhibitor, on the photoreceptor phosphodiesterase depend on the state of activation of the enzyme
    • D'Amours M.R., Granovsky A.E., Artemyev N.O., Cote R.H. Potency and mechanism of action of E4021, a type 5 phosphodiesterase isozyme-selective inhibitor, on the photoreceptor phosphodiesterase depend on the state of activation of the enzyme. Mol. Pharmacol. (1999) 55 508-514.
    • (1999) Mol. Pharmacol. , vol.55 , pp. 508-514
    • D'Amours, M.R.1    Granovsky, A.E.2    Artemyev, N.O.3    Cote, R.H.4
  • 217
    • 3342981230 scopus 로고    scopus 로고
    • Characteristics of photoreceptor PDE (PDE6): similarities and differences to PDE5
    • Cote R.H. Characteristics of photoreceptor PDE (PDE6): similarities and differences to PDE5. Int. J. Impot. Res. (2004) 16(Suppl 1) S28-S33.
    • (2004) Int. J. Impot. Res. , vol.16 , Issue.Suppl 1 , pp. S28-S33
    • Cote, R.H.1
  • 219
    • 0037081859 scopus 로고    scopus 로고
    • Novel alternative splice variants of rat phosphodiesterase 7B showing unique tissue-specific expression and phosphorylation
    • Sasaki T., Kotera J., Omori K. Novel alternative splice variants of rat phosphodiesterase 7B showing unique tissue-specific expression and phosphorylation. Biochem. J. (2002) 361 211-220.
    • (2002) Biochem. J. , vol.361 , pp. 211-220
    • Sasaki, T.1    Kotera, J.2    Omori, K.3
  • 221
    • 0037163858 scopus 로고    scopus 로고
    • Crystal structure of phosphodiesterase 4D and inhibitor complex
    • Lee M.E., Markowitz J., Lee J.-O., Lee H. Crystal structure of phosphodiesterase 4D and inhibitor complex. FEBS Lett. (2002) 530 53-58.
    • (2002) FEBS Lett. , vol.530 , pp. 53-58
    • Lee, M.E.1    Markowitz, J.2    Lee, J.-O.3    Lee, H.4
  • 222
    • 0036151438 scopus 로고    scopus 로고
    • PDE7A is expressed in human B-lymphocytes and is up-regulated by elevation of intracellular cAMP
    • Lee R., Wolda S., Moon E., Esselstyn J., Hertel C., Lerner A. PDE7A is expressed in human B-lymphocytes and is up-regulated by elevation of intracellular cAMP. Cell. Signal. (2002) 14 277-284.
    • (2002) Cell. Signal. , vol.14 , pp. 277-284
    • Lee, R.1    Wolda, S.2    Moon, E.3    Esselstyn, J.4    Hertel, C.5    Lerner, A.6
  • 224
    • 0037409401 scopus 로고    scopus 로고
    • Comparison of enzymatic characterization and gene organization of cyclic nucleotide phosphodiesterase 8 family in humans
    • Gamanuma M., Yuasa K., Sasaki T., Sakurai N., Kotera J., Omori K. Comparison of enzymatic characterization and gene organization of cyclic nucleotide phosphodiesterase 8 family in humans. Cell. Signal. (2003) 15 565-574.
    • (2003) Cell. Signal. , vol.15 , pp. 565-574
    • Gamanuma, M.1    Yuasa, K.2    Sasaki, T.3    Sakurai, N.4    Kotera, J.5    Omori, K.6
  • 225
    • 0036407344 scopus 로고    scopus 로고
    • Genomic organization, chromosomal localization, and alternative splicing of the human phosphodiesterase 8B gene
    • Hayashi M., Shimada Y., Nishimura Y., Hama T., Tanaka T. Genomic organization, chromosomal localization, and alternative splicing of the human phosphodiesterase 8B gene. Biochem. Biophys. Res. Commun. (2002) 297 1253-1258.
    • (2002) Biochem. Biophys. Res. Commun. , vol.297 , pp. 1253-1258
    • Hayashi, M.1    Shimada, Y.2    Nishimura, Y.3    Hama, T.4    Tanaka, T.5
  • 226
    • 0032546924 scopus 로고    scopus 로고
    • Identification and characterization of a novel family of cyclic nucleotide phosphodiesterases
    • Soderling S.H., Bayuga S.J., Beavo J.A. Identification and characterization of a novel family of cyclic nucleotide phosphodiesterases. J. Biol. Chem. (1998) 273 15553-15558.
    • (1998) J. Biol. Chem. , vol.273 , pp. 15553-15558
    • Soderling, S.H.1    Bayuga, S.J.2    Beavo, J.A.3
  • 227
    • 0032555138 scopus 로고    scopus 로고
    • Cloning and characterization of a cAMP-specific cyclic nucleotide phosphodiesterase
    • Soderling S.H., Bayuga S.J., Beavo J.A. Cloning and characterization of a cAMP-specific cyclic nucleotide phosphodiesterase. Proc. Natl Acad. Sci. USA (1998) 95 8991-8996.
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 8991-8996
    • Soderling, S.H.1    Bayuga, S.J.2    Beavo, J.A.3
  • 228
    • 27844464469 scopus 로고    scopus 로고
    • Characterization of the first potent and selective PDE9 inhibitor using a cGMP reporter cell line
    • Wunder F., Tersteegen A., Rebmann A., Erb C., Fahrig T., Hendrix M. Characterization of the first potent and selective PDE9 inhibitor using a cGMP reporter cell line. Mol. Pharmacol. (2005) 68 1775-1781.
    • (2005) Mol. Pharmacol. , vol.68 , pp. 1775-1781
    • Wunder, F.1    Tersteegen, A.2    Rebmann, A.3    Erb, C.4    Fahrig, T.5    Hendrix, M.6
  • 229
    • 79959999316 scopus 로고    scopus 로고
    • The selective phosphodiesterase 9 (PDE9) inhibitor PF-04447943 (6-[(3S,4S)-4-methyl-1-(pyrimidin-2-ylmethyl)pyrrolidin-3-yl]-1-(tetrahydro-2H-pyran-4-yl)-1,5-dihydro-4H-pyrazolo[3,4-d]pyrimidin-4-one) enhances synaptic plasticity and cognitive function in rodents
    • Hutson P.H., Finger E.N., Magliaro B.C. et al. The selective phosphodiesterase 9 (PDE9) inhibitor PF-04447943 (6-[(3S, 4S)-4-methyl-1-(pyrimidin-2-ylmethyl)pyrrolidin-3-yl]-1-(tetrahydro-2H-pyran-4-yl)-1, 5-dihydro-4H-pyrazolo[3, 4-d]pyrimidin-4-one) enhances synaptic plasticity and cognitive function in rodents. Neuropharmacology (2011) 61 665-676.
    • (2011) Neuropharmacology , vol.61 , pp. 665-676
    • Hutson, P.H.1    Finger, E.N.2    Magliaro, B.C.3
  • 230
    • 0033603598 scopus 로고    scopus 로고
    • Cloning and characterization of a novel human phosphodiesterase that hydrolyzes both cAMP and cGMP (PDE10A)
    • Fujishige K., Kotera J., Michibata H. et al. Cloning and characterization of a novel human phosphodiesterase that hydrolyzes both cAMP and cGMP (PDE10A). J. Biol. Chem. (1999) 274 18438-18445.
    • (1999) J. Biol. Chem. , vol.274 , pp. 18438-18445
    • Fujishige, K.1    Kotera, J.2    Michibata, H.3
  • 231
    • 0033546738 scopus 로고    scopus 로고
    • Characterization and phosphorylation of PDE10A2, a novel alternative splice variant of human phosphodiesterase that hydrolyzes cAMP and cGMP
    • Kotera J., Fujishige K., Yuasa K., Omori K. Characterization and phosphorylation of PDE10A2, a novel alternative splice variant of human phosphodiesterase that hydrolyzes cAMP and cGMP. Biochem. Biophys. Res. Commun. (1999) 261 551-557.
    • (1999) Biochem. Biophys. Res. Commun. , vol.261 , pp. 551-557
    • Kotera, J.1    Fujishige, K.2    Yuasa, K.3    Omori, K.4
  • 232
    • 63449126507 scopus 로고    scopus 로고
    • Evaluating the antipsychotic profile of the preferential PDE10A inhibitor, papaverine
    • Weber M., Breier M., Ko D., Thangaraj N., Marzan D.E., Swerdlow N.R. Evaluating the antipsychotic profile of the preferential PDE10A inhibitor, papaverine. Psychopharmacology (2009) 203 723-735.
    • (2009) Psychopharmacology , vol.203 , pp. 723-735
    • Weber, M.1    Breier, M.2    Ko, D.3    Thangaraj, N.4    Marzan, D.E.5    Swerdlow, N.R.6
  • 233
    • 0034819381 scopus 로고    scopus 로고
    • Identification of rat cyclic nucleotide phosphodiesterase 11A (PDE11A): comparison of rat and human PDE11A splicing variants
    • Yuasa K., Ohgaru T., Asahina M., Omori K. Identification of rat cyclic nucleotide phosphodiesterase 11A (PDE11A): comparison of rat and human PDE11A splicing variants. Eur. J. Biochem. (2001) 268 4440-4448.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 4440-4448
    • Yuasa, K.1    Ohgaru, T.2    Asahina, M.3    Omori, K.4
  • 234
    • 84856393433 scopus 로고    scopus 로고
    • Identification of biologically active PDE11-selective inhibitors using a yeast-based high-throughput screen
    • Ceyhan O., Birsoy K., Hoffman C.S. Identification of biologically active PDE11-selective inhibitors using a yeast-based high-throughput screen. Chem. Biol. (2012) 19 155-163.
    • (2012) Chem. Biol. , vol.19 , pp. 155-163
    • Ceyhan, O.1    Birsoy, K.2    Hoffman, C.S.3


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