메뉴 건너뛰기




Volumn 232, Issue 1, 2007, Pages 38-51

Cyclic nucleotide phosphodiesterase (PDE) inhibitors: Novel therapeutic agents for progressive renal disease

Author keywords

cAMP; cGMP; Phosphodiesterase; Progressive renal disease

Indexed keywords

1 [6 CHLORO 4 (3,4 METHYLENEDIOXYBENZYLAMINO) 2 QUINAZOLINYL] 4 PIPERIDINECARBOXYLIC ACID; 2 METHYL 5 NITROBENZENESULFONIC ACID DIMETHYLAMIDE; 4 (3 BUTOXY 4 METHOXYBENZYL) 2 IMIDAZOLIDINONE; 4 [3 [6 AMINO 9 (5 ETHYLCARBAMOYL 3,4 DIHYDROXYTETRAHYDRO 2 FURYL) 9H PURIN 2 YL] 2 PROPYNYL]CYCLOHEXANECARBOXYLIC ACID METHYL ESTER; CILOMILAST; CILOSTAMIDE; CILOSTAZOL; CYCLIC NUCLEOTIDE PHOSPHODIESTERASE; DENBUFYLLINE; DIPYRIDAMOLE; LIXAZINONE; MILRINONE; N (3,5 DICHLORO 4 PYRIDYL) [1 (4 FLUOROBENZYL) 5 HYDROXY 3 INDOLYL]GLYOXYLIC ACID AMIDE; NICARDIPINE; PAPAVERINE; PENTOXIFYLLINE; PHOSPHODIESTERASE III INHIBITOR; PHOSPHODIESTERASE INHIBITOR; PHOSPHODIESTERASE IV INHIBITOR; PHOSPHODIESTERASE V INHIBITOR; PHOSPHODIESTERASE VII INHIBITOR; ROFLUMILAST; ROLIPRAM; SILDENAFIL; TADALAFIL; THIADIAZOLE DERIVATIVE; UNINDEXED DRUG; VARDENAFIL; VINPOCETINE; ZAPRINAST;

EID: 33846129423     PISSN: 15353702     EISSN: 15353699     Source Type: Journal    
DOI: None     Document Type: Short Survey
Times cited : (67)

References (162)
  • 1
    • 0035224418 scopus 로고    scopus 로고
    • PDE4 cAMP-specific phosphodiesterases
    • Houslay MD. PDE4 cAMP-specific phosphodiesterases. Prog Nucleic Acid Res Mol Biol 69:249-315, 2001.
    • (2001) Prog Nucleic Acid Res Mol Biol , vol.69 , pp. 249-315
    • Houslay, M.D.1
  • 2
    • 0032924098 scopus 로고    scopus 로고
    • Dousa T. Cyclic-3′,5′-nucleotide phosphodiesterase isozymes in cell biology and pathophysiology of the kidney. Kidney Int 55:29-62, 1999.
    • Dousa T. Cyclic-3′,5′-nucleotide phosphodiesterase isozymes in cell biology and pathophysiology of the kidney. Kidney Int 55:29-62, 1999.
  • 3
    • 0031626904 scopus 로고    scopus 로고
    • Signaling role of PDE isozymes in pathobiology of glomerular mesangial cells: Studies in vitro and in vivo
    • Dousa T. Signaling role of PDE isozymes in pathobiology of glomerular mesangial cells: studies in vitro and in vivo. Cell Biochem Biophys 29:19-34, 1998.
    • (1998) Cell Biochem Biophys , vol.29 , pp. 19-34
    • Dousa, T.1
  • 5
    • 25444495661 scopus 로고    scopus 로고
    • TGF-beta1 stimulates monocyte chemoattractant protein-1 expression in mesangial cells through a phosphodiesterase isoenzyme 4-dependent process
    • Cheng J, Diaz Encarnacion MM, Warner GM, Gray CE, Nath KA, Grande JP. TGF-beta1 stimulates monocyte chemoattractant protein-1 expression in mesangial cells through a phosphodiesterase isoenzyme 4-dependent process. Am J Physiol Cell Physiol 289:C959-C970, 2005.
    • (2005) Am J Physiol Cell Physiol , vol.289
    • Cheng, J.1    Diaz Encarnacion, M.M.2    Warner, G.M.3    Gray, C.E.4    Nath, K.A.5    Grande, J.P.6
  • 6
    • 0035952734 scopus 로고    scopus 로고
    • In vivo functions of heterotrimeric G-proteins: Studies in Galpha deficient mice
    • Offermanns S. In vivo functions of heterotrimeric G-proteins: studies in Galpha deficient mice. Oncogene 20:1635-1642, 2001.
    • (2001) Oncogene , vol.20 , pp. 1635-1642
    • Offermanns, S.1
  • 7
    • 0036729478 scopus 로고    scopus 로고
    • Cyclic nucleotide research - still expanding after half a century
    • Beavo JA, Brunton LL. Cyclic nucleotide research - still expanding after half a century. Nat Rev Mol Cell Biol 3:710-718, 2002.
    • (2002) Nat Rev Mol Cell Biol , vol.3 , pp. 710-718
    • Beavo, J.A.1    Brunton, L.L.2
  • 11
    • 0347359224 scopus 로고    scopus 로고
    • Localized effects of cAMP mediated by distinct routes of protein kinase A
    • Tasken K, Aandahl EM. Localized effects of cAMP mediated by distinct routes of protein kinase A. Physiol Rev 84:137-167, 2004.
    • (2004) Physiol Rev , vol.84 , pp. 137-167
    • Tasken, K.1    Aandahl, E.M.2
  • 13
    • 21644449363 scopus 로고    scopus 로고
    • In resting COS1 cells a dominant negative approach shows that specific, anchored PDE4 cAMP phosphodiesterase isoforms gate the activation, by basal cyclic AMP production, of AKAP-tethered protein kinase A type II located in the centrosomal region
    • McCahill A, McSorley T, Huston E, Hill EV, Lynch MJ, Gall I, Keryer G, Lygren B, Tasken K, van Heeke G, Houslay MD. In resting COS1 cells a dominant negative approach shows that specific, anchored PDE4 cAMP phosphodiesterase isoforms gate the activation, by basal cyclic AMP production, of AKAP-tethered protein kinase A type II located in the centrosomal region. Cell Signal 17: 1158-1173, 2005.
    • (2005) Cell Signal , vol.17 , pp. 1158-1173
    • McCahill, A.1    McSorley, T.2    Huston, E.3    Hill, E.V.4    Lynch, M.J.5    Gall, I.6    Keryer, G.7    Lygren, B.8    Tasken, K.9    van Heeke, G.10    Houslay, M.D.11
  • 15
    • 0033021636 scopus 로고    scopus 로고
    • AKAPs: From structure to function
    • Colledge M, Scott JD. AKAPs: from structure to function. Trends Cell Biol 9:216-221, 1999.
    • (1999) Trends Cell Biol , vol.9 , pp. 216-221
    • Colledge, M.1    Scott, J.D.2
  • 16
    • 0028588997 scopus 로고
    • A kinase anchor proteins and the intracellular targeting of signals carried by cyclic AMP
    • Rubin CS. A kinase anchor proteins and the intracellular targeting of signals carried by cyclic AMP. Biochim Biophys Acta 1224:467-479, 1994.
    • (1994) Biochim Biophys Acta , vol.1224 , pp. 467-479
    • Rubin, C.S.1
  • 17
    • 0035004612 scopus 로고    scopus 로고
    • AKAP signaling complexes at the cytoskeleton
    • Diviani D, Scott JD. AKAP signaling complexes at the cytoskeleton. J Cell Sci 114:1431-1437, 2001.
    • (2001) J Cell Sci , vol.114 , pp. 1431-1437
    • Diviani, D.1    Scott, J.D.2
  • 18
    • 0035818473 scopus 로고    scopus 로고
    • A uniform extracellular stimulus triggers distinct cAMP signals in different compartments of a simple cell
    • Rich TC, Fagan KA, Tse TE, Schaack J, Cooper DM, Karpen JW. A uniform extracellular stimulus triggers distinct cAMP signals in different compartments of a simple cell. Proc Natl Acad Sci U S A 98: 13049-13054, 2001.
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 13049-13054
    • Rich, T.C.1    Fagan, K.A.2    Tse, T.E.3    Schaack, J.4    Cooper, D.M.5    Karpen, J.W.6
  • 20
    • 0037166283 scopus 로고    scopus 로고
    • Protein kinase A-independent activation of ERK and H,K-ATPase by cAMP in native kidney cells: Role of Epac I
    • Laroche-Joubert N, Marsy S, Michelet S, Imbert-Teboul M, Doucet A. Protein kinase A-independent activation of ERK and H,K-ATPase by cAMP in native kidney cells: role of Epac I. J Biol Chem 277:18598-18604, 2002.
    • (2002) J Biol Chem , vol.277 , pp. 18598-18604
    • Laroche-Joubert, N.1    Marsy, S.2    Michelet, S.3    Imbert-Teboul, M.4    Doucet, A.5
  • 21
    • 0030025596 scopus 로고    scopus 로고
    • cAMP compartmentation is responsible for a local activation of cardiac Ca2+ channels by beta-adrenergic agonists
    • Jurevicius J, Fischmeister R. cAMP compartmentation is responsible for a local activation of cardiac Ca2+ channels by beta-adrenergic agonists. Proc Natl Acad Sci U S A 93:295-299, 1996.
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 295-299
    • Jurevicius, J.1    Fischmeister, R.2
  • 22
    • 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 295: 1711-1715, 2002.
    • (2002) Science , vol.295 , pp. 1711-1715
    • Zaccolo, M.1    Pozzan, T.2
  • 24
    • 27744564512 scopus 로고    scopus 로고
    • Improvement of a FRET-based indicator for cAMP by linker design and stabilization of donor-acceptor interaction
    • Lissandron V, Terrin A, Collini M, D'Alfonso L, Chirico G, Pantano S, Zaccolo M. Improvement of a FRET-based indicator for cAMP by linker design and stabilization of donor-acceptor interaction. J Mol Biol 354:546-555, 2005.
    • (2005) J Mol Biol , vol.354 , pp. 546-555
    • Lissandron, V.1    Terrin, A.2    Collini, M.3    D'Alfonso, L.4    Chirico, G.5    Pantano, S.6    Zaccolo, M.7
  • 28
    • 0031914520 scopus 로고    scopus 로고
    • Phosphodiesterase isozymes: Molecular targets for novel antiasthma agents
    • Torphy TJ. Phosphodiesterase isozymes: molecular targets for novel antiasthma agents. Am J Respir Crit Care Med 157:351-370, 1998.
    • (1998) Am J Respir Crit Care Med , vol.157 , pp. 351-370
    • Torphy, T.J.1
  • 29
    • 0032605044 scopus 로고    scopus 로고
    • The molecular biology of cyclic nucleotide phosphodiesterases
    • Conti M, Jin SL. The molecular biology of cyclic nucleotide phosphodiesterases. Prog Nucleic Acid Res Mol Biol 63:1-38, 1999.
    • (1999) Prog Nucleic Acid Res Mol Biol , vol.63 , pp. 1-38
    • Conti, M.1    Jin, S.L.2
  • 30
    • 0034009080 scopus 로고    scopus 로고
    • Regulation of cAMP and cGMP signaling: New phosphodiesterases and new functions
    • Soderling SH, Beavo JA. Regulation of cAMP and cGMP signaling: new phosphodiesterases and new functions. Curr Opin Cell Biol 12: 174-179, 2000.
    • (2000) Curr Opin Cell Biol , vol.12 , pp. 174-179
    • Soderling, S.H.1    Beavo, J.A.2
  • 31
    • 0030957594 scopus 로고    scopus 로고
    • Structure, localization, and regulation of cGMP-inhibited phosphodiesterase (PDE3)
    • Degerman E, Belfrage P, Manganiello V. Structure, localization, and regulation of cGMP-inhibited phosphodiesterase (PDE3). J Biol Chem 272:6823-6826, 1997.
    • (1997) J Biol Chem , vol.272 , pp. 6823-6826
    • Degerman, E.1    Belfrage, P.2    Manganiello, V.3
  • 32
    • 0032134209 scopus 로고    scopus 로고
    • Chemotherapeutic potential of phosphodiesterase inhibitors
    • Perry MJ, Higgs GA. Chemotherapeutic potential of phosphodiesterase inhibitors. Curr Opin Chem Biol 2:472-481, 1998.
    • (1998) Curr Opin Chem Biol , vol.2 , pp. 472-481
    • Perry, M.J.1    Higgs, G.A.2
  • 33
    • 0037443097 scopus 로고    scopus 로고
    • Houslay MD, Adams DR. PDE4 cAMP phosphodiesterases: modular enzymes that orchestrate signalling cross-talk, desensitization and compartmentalization. Biochem J 370:1-18, 2003.
    • Houslay MD, Adams DR. PDE4 cAMP phosphodiesterases: modular enzymes that orchestrate signalling cross-talk, desensitization and compartmentalization. Biochem J 370:1-18, 2003.
  • 34
    • 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 MD, Sullivan M, Bolger GB. 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 44:225-342, 1998.
    • (1998) Adv Pharmacol , vol.44 , pp. 225-342
    • Houslay, M.D.1    Sullivan, M.2    Bolger, G.B.3
  • 35
    • 0141506110 scopus 로고    scopus 로고
    • Eicosapentaenoic acid inhibits Ca2+ mobilization and PKC activity in vascular smooth muscle cells
    • Nyby MD, Hori MT, Ormsby B, Gabrielian A, Tuck ML. Eicosapentaenoic acid inhibits Ca2+ mobilization and PKC activity in vascular smooth muscle cells. Am J Hypertens 16:708-714, 2003.
    • (2003) Am J Hypertens , vol.16 , pp. 708-714
    • Nyby, M.D.1    Hori, M.T.2    Ormsby, B.3    Gabrielian, A.4    Tuck, M.L.5
  • 36
    • 0030974622 scopus 로고    scopus 로고
    • Tailoring cAMP signalling responses through isoform multiplicity
    • Houslay M, Milligan G. Tailoring cAMP signalling responses through isoform multiplicity. Trends Pharmacol Sci 22:217-224, 1997.
    • (1997) Trends Pharmacol Sci , vol.22 , pp. 217-224
    • Houslay, M.1    Milligan, G.2
  • 38
    • 0023002533 scopus 로고
    • Regulation of particulate cAMP phosphodiesterase activity in 3T3-L1 adipocytes: The role of particulate phosphodiesterase in the antilipolytic action of insulin
    • Belfrage P, Donner J, Stralfors P, Eds, New York: Elsevier Science Publishers, pp
    • Manganiello V, Elks M. Regulation of particulate cAMP phosphodiesterase activity in 3T3-L1 adipocytes: the role of particulate phosphodiesterase in the antilipolytic action of insulin. In: Belfrage P, Donner J, Stralfors P, Eds. Mechanisms of Insulin Action. New York: Elsevier Science Publishers, pp147-166, 1986.
    • (1986) Mechanisms of Insulin Action , pp. 147-166
    • Manganiello, V.1    Elks, M.2
  • 39
    • 0030999236 scopus 로고    scopus 로고
    • Compartmentalization of cAMP signaling in mesangial cells by phosphodiesterase isozymes PDE3 and PDE4. Regulation of superoxidation and mitogenesis
    • Chini CCS, Grande JP, Chini EN, Dousa TP. Compartmentalization of cAMP signaling in mesangial cells by phosphodiesterase isozymes PDE3 and PDE4. Regulation of superoxidation and mitogenesis. J Biol Chem 272:9854-9859, 1997.
    • (1997) J Biol Chem , vol.272 , pp. 9854-9859
    • Chini, C.C.S.1    Grande, J.P.2    Chini, E.N.3    Dousa, T.P.4
  • 40
    • 0021218957 scopus 로고
    • Selective effects of phosphodiesterase inhibitors on different phosphodiesterases, adenosine 3′,5′- monophosphate metabolism, and lipolysis in 3T3-L1 adipocytes
    • Elks ML, Manganiello VC. Selective effects of phosphodiesterase inhibitors on different phosphodiesterases, adenosine 3′,5′- monophosphate metabolism, and lipolysis in 3T3-L1 adipocytes. Endocrinology 115:1262-1268, 1984.
    • (1984) Endocrinology , vol.115 , pp. 1262-1268
    • Elks, M.L.1    Manganiello, V.C.2
  • 43
    • 0034655448 scopus 로고    scopus 로고
    • Action of rolipram on specific PDE4 cAMP phosphodiesterase isoforms and on the phosphorylation of cAMP-response-element- binding protein (CREB) and p38 mitogen-activated protein (MAP) kinase in U937 monocytic cells
    • MacKenzie SJ, Houslay MD. Action of rolipram on specific PDE4 cAMP phosphodiesterase isoforms and on the phosphorylation of cAMP-response-element- binding protein (CREB) and p38 mitogen-activated protein (MAP) kinase in U937 monocytic cells. Biochem J 347:571-578, 2000.
    • (2000) Biochem J , vol.347 , pp. 571-578
    • MacKenzie, S.J.1    Houslay, M.D.2
  • 44
    • 0021822478 scopus 로고
    • Antilipolytic action of insulin: Role of cAMP phosphodiesterase activation
    • Elks ML, Manganiello VC. Antilipolytic action of insulin: role of cAMP phosphodiesterase activation. Endocrinology 116:2119-2121, 1985.
    • (1985) Endocrinology , vol.116 , pp. 2119-2121
    • Elks, M.L.1    Manganiello, V.C.2
  • 46
    • 10644280705 scopus 로고    scopus 로고
    • Negative feedback exerted by cAMP-dependent protein kinase and cAMP phosphodiesterase on subsarcolemmal cAMP signals in intact cardiac myocytes: An in vivo study using adenovirus-mediated expression of CNG channels
    • Rochais F, Vandecasteele G, Lefebvre F, Lugnier C, Lum H, Mazet JL, Cooper DM, Fischmeister R. Negative feedback exerted by cAMP-dependent protein kinase and cAMP phosphodiesterase on subsarcolemmal cAMP signals in intact cardiac myocytes: an in vivo study using adenovirus-mediated expression of CNG channels. J Biol Chem 279:52095-52105, 2004.
    • (2004) J Biol Chem , vol.279 , pp. 52095-52105
    • Rochais, F.1    Vandecasteele, G.2    Lefebvre, F.3    Lugnier, C.4    Lum, H.5    Mazet, J.L.6    Cooper, D.M.7    Fischmeister, R.8
  • 47
    • 23944494162 scopus 로고    scopus 로고
    • RNA silencing identifies PDE4D5 as the functionally relevant cAMP phosphodiesterase interacting with beta arrestin to control the protein kinase A/AKAP79-mediated switching of the beta2-adrenergic receptor to activation of ERK in HEK293B2 cells
    • Lynch MJ, Baillie GS, Mohamed A, Li X, Maisonneuve C, Klussmann E, van Heeke G, Houslay MD. RNA silencing identifies PDE4D5 as the functionally relevant cAMP phosphodiesterase interacting with beta arrestin to control the protein kinase A/AKAP79-mediated switching of the beta2-adrenergic receptor to activation of ERK in HEK293B2 cells. J Biol Chem 280:33178-33189, 2005.
    • (2005) J Biol Chem , vol.280 , pp. 33178-33189
    • Lynch, M.J.1    Baillie, G.S.2    Mohamed, A.3    Li, X.4    Maisonneuve, C.5    Klussmann, E.6    van Heeke, G.7    Houslay, M.D.8
  • 48
    • 30044446499 scopus 로고    scopus 로고
    • Cyclic nucleotide phosphodiesterases as targets for treatment of haematological malignancies
    • Lerner A, Epstein PM. Cyclic nucleotide phosphodiesterases as targets for treatment of haematological malignancies. Biochem J 393:21-41, 2006.
    • (2006) Biochem J , vol.393 , pp. 21-41
    • Lerner, A.1    Epstein, P.M.2
  • 49
    • 27344449614 scopus 로고    scopus 로고
    • Keynote review: Phosphodiesterase-4 as a therapeutic target
    • Houslay MD, Schafer P, Zhang KY. Keynote review: phosphodiesterase-4 as a therapeutic target. Drug Discov Today 10:1503-1519, 2005.
    • (2005) Drug Discov Today , vol.10 , pp. 1503-1519
    • Houslay, M.D.1    Schafer, P.2    Zhang, K.Y.3
  • 50
    • 0027454556 scopus 로고
    • A family of human phosphodiesterases homologous to the dunce learning and memory gene product of Drosophila melanogaster are potential targets for antidepressant drugs
    • Bolger G, Michaeli T, Martins T, St John T, Steiner B, Rodgers L, Riggs M, Wigler M, Ferguson K. A family of human phosphodiesterases homologous to the dunce learning and memory gene product of Drosophila melanogaster are potential targets for antidepressant drugs. Mol Cell Biol 13:6558-6571, 1993.
    • (1993) Mol Cell Biol , vol.13 , pp. 6558-6571
    • Bolger, G.1    Michaeli, T.2    Martins, T.3    St John, T.4    Steiner, B.5    Rodgers, L.6    Riggs, M.7    Wigler, M.8    Ferguson, K.9
  • 51
    • 33744975520 scopus 로고    scopus 로고
    • Hypoxia-induced remodelling of PDE4 isoform expression and cAMP handling in human pulmonary artery smooth muscle cells
    • Millen J, MacLean MR, Houslay MD. Hypoxia-induced remodelling of PDE4 isoform expression and cAMP handling in human pulmonary artery smooth muscle cells. Eur J Cell Biol 85:679-691, 2006.
    • (2006) Eur J Cell Biol , vol.85 , pp. 679-691
    • Millen, J.1    MacLean, M.R.2    Houslay, M.D.3
  • 52
    • 15044353649 scopus 로고    scopus 로고
    • Arrestin times for compartmentalised cAMP signalling and phosphodiesterase-4 enzymes
    • Baillie GS, Houslay MD. Arrestin times for compartmentalised cAMP signalling and phosphodiesterase-4 enzymes. Curr Opin Cell Biol 17: 129-134, 2005.
    • (2005) Curr Opin Cell Biol , vol.17 , pp. 129-134
    • Baillie, G.S.1    Houslay, M.D.2
  • 53
    • 0037458648 scopus 로고    scopus 로고
    • Cyclic AMP-specific PDE4 phosphodiesterases as critical components of cyclic AMP signaling
    • Conti M, Richter W, Mehats C, Livera G, Park JY, Jin C. Cyclic AMP-specific PDE4 phosphodiesterases as critical components of cyclic AMP signaling. J Biol Chem 278:5493-5496, 2003.
    • (2003) J Biol Chem , vol.278 , pp. 5493-5496
    • Conti, M.1    Richter, W.2    Mehats, C.3    Livera, G.4    Park, J.Y.5    Jin, C.6
  • 54
    • 17744398004 scopus 로고    scopus 로고
    • Membrane localization of cyclic nucleotide phosphodiesterase 3 (PDE3). Two N-terminal domains are required for the efficient targeting to, and association of, PDE3 with endoplasmic reticulum
    • Shakur Y, Takeda K, Kenan Y, Yu ZX, Rena G, Brandt D, Houslay MD, Degerman E, Ferrans VJ, Manganiello VC. Membrane localization of cyclic nucleotide phosphodiesterase 3 (PDE3). Two N-terminal domains are required for the efficient targeting to, and association of, PDE3 with endoplasmic reticulum. J Biol Chem 275: 38749-38761, 2000.
    • (2000) J Biol Chem , vol.275 , pp. 38749-38761
    • Shakur, Y.1    Takeda, K.2    Kenan, Y.3    Yu, Z.X.4    Rena, G.5    Brandt, D.6    Houslay, M.D.7    Degerman, E.8    Ferrans, V.J.9    Manganiello, V.C.10
  • 55
    • 0033597139 scopus 로고    scopus 로고
    • Association with the SRC family tyrosyl kinase LYN triggers a conformational change in the catalytic region of human cAMP-specific phosphodiesterase HSPDE4A4B
    • McPhee I, Yarwood S, Scotland G, Huston E, Beard M, Ross A, Houslay E, Houslay M. Association with the SRC family tyrosyl kinase LYN triggers a conformational change in the catalytic region of human cAMP-specific phosphodiesterase HSPDE4A4B. J Biol Chem 274:11796-11810, 1999.
    • (1999) J Biol Chem , vol.274 , pp. 11796-11810
    • McPhee, I.1    Yarwood, S.2    Scotland, G.3    Huston, E.4    Beard, M.5    Ross, A.6    Houslay, E.7    Houslay, M.8
  • 57
    • 0033591233 scopus 로고    scopus 로고
    • The RACK1 signaling scaffold protein selectively interacts with the cAMP-specific phosphodiesterase PDE4D5 isoform
    • Yarwood SJ, Steele MR, Scotland G, Houslay MD, Bolger GB. The RACK1 signaling scaffold protein selectively interacts with the cAMP-specific phosphodiesterase PDE4D5 isoform. J Biol Chem 274:14909-14917, 1999.
    • (1999) J Biol Chem , vol.274 , pp. 14909-14917
    • Yarwood, S.J.1    Steele, M.R.2    Scotland, G.3    Houslay, M.D.4    Bolger, G.B.5
  • 58
    • 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, Zhang G, Wang S, Coletti D, Onuffer J, Jin SL, Conti M. Myomegalin is a novel protein of the golgi/centrosome that interacts with a cyclic nucleotide phosphodiesterase. J Biol Chem 276:11189-11198, 2001.
    • (2001) J Biol Chem , vol.276 , pp. 11189-11198
    • Verde, I.1    Pahlke, G.2    Salanova, M.3    Zhang, G.4    Wang, S.5    Coletti, D.6    Onuffer, J.7    Jin, S.L.8    Conti, M.9
  • 60
    • 0035933817 scopus 로고    scopus 로고
    • Phosphodiesterase 4D and protein kinase A type II constitute a signaling unit in the centrosomal area
    • Tasken KA, Collas P, Kemmner WA, Witczak O, Conti M, Tasken K. Phosphodiesterase 4D and protein kinase A type II constitute a signaling unit in the centrosomal area. J Biol Chem 276:21999-22002, 2001.
    • (2001) J Biol Chem , vol.276 , pp. 21999-22002
    • Tasken, K.A.1    Collas, P.2    Kemmner, W.A.3    Witczak, O.4    Conti, M.5    Tasken, K.6
  • 61
    • 21144437565 scopus 로고    scopus 로고
    • Phosphodiesterase: Overview of protein structures, potential therapeutic applications and recent progress in drug development
    • Jeon YH, Heo YS, Kim CM, Hyun YL, Lee TG, Ro S, Cho JM. Phosphodiesterase: overview of protein structures, potential therapeutic applications and recent progress in drug development. Cell Mol Life Sci 62:1198-1220, 2005.
    • (2005) Cell Mol Life Sci , vol.62 , pp. 1198-1220
    • Jeon, Y.H.1    Heo, Y.S.2    Kim, C.M.3    Hyun, Y.L.4    Lee, T.G.5    Ro, S.6    Cho, J.M.7
  • 66
    • 0034595707 scopus 로고    scopus 로고
    • ERK2 mitogen-activated protein kinase binding, phosphorylation, and regulation of the PDE4D cAMP-specific phosphodiesterases. The involvement of COOH-terminal docking sites and NH2-terminal UCR regions
    • MacKenzie SJ, Baillie GS, McPhee I, Bolger GB, Houslay MD. ERK2 mitogen-activated protein kinase binding, phosphorylation, and regulation of the PDE4D cAMP-specific phosphodiesterases. The involvement of COOH-terminal docking sites and NH2-terminal UCR regions. J Biol Chem 275:16609-16617, 2000.
    • (2000) J Biol Chem , vol.275 , pp. 16609-16617
    • MacKenzie, S.J.1    Baillie, G.S.2    McPhee, I.3    Bolger, G.B.4    Houslay, M.D.5
  • 67
    • 0033558010 scopus 로고    scopus 로고
    • The MAP kinase ERK2 inhibits the cyclic AMP-specific phosphodiesterase HSPDE4D3 by phosphorylating it at Ser579
    • Hoffmann R, Baillie GS, MacKenzie SJ, Yarwood SJ, Houslay MD. The MAP kinase ERK2 inhibits the cyclic AMP-specific phosphodiesterase HSPDE4D3 by phosphorylating it at Ser579. EMBO J 18: 893-903, 1999.
    • (1999) EMBO J , vol.18 , pp. 893-903
    • Hoffmann, R.1    Baillie, G.S.2    MacKenzie, S.J.3    Yarwood, S.J.4    Houslay, M.D.5
  • 68
    • 0034714376 scopus 로고    scopus 로고
    • Expression of phosphodiesterase 4D (PDE4D) is regulated by both the cyclic AMP-dependent protein kinase and mitogen-activated protein kinase signaling pathways. A potential mechanism allowing for the coordinated regulation of PDE4D activity and expression in cells
    • Liu H, Palmer D, Jimmo SL, Tilley DG, Dunkerley HA, Pang SC, Maurice DH. Expression of phosphodiesterase 4D (PDE4D) is regulated by both the cyclic AMP-dependent protein kinase and mitogen-activated protein kinase signaling pathways. A potential mechanism allowing for the coordinated regulation of PDE4D activity and expression in cells. J Biol Chem 275:26615-26624, 2000.
    • (2000) J Biol Chem , vol.275 , pp. 26615-26624
    • Liu, H.1    Palmer, D.2    Jimmo, S.L.3    Tilley, D.G.4    Dunkerley, H.A.5    Pang, S.C.6    Maurice, D.H.7
  • 69
    • 0034766764 scopus 로고    scopus 로고
    • Phorbol 12-myristate 13-acetate triggers the protein kinase A-mediated phosphorylation and activation of the PDE4D5 cAMP phosphodiesterase in human aortic smooth muscle cells through a route involving extracellular signal regulated kinase (ERK)
    • Baillie G, MacKenzie SJ, Houslay MD. Phorbol 12-myristate 13-acetate triggers the protein kinase A-mediated phosphorylation and activation of the PDE4D5 cAMP phosphodiesterase in human aortic smooth muscle cells through a route involving extracellular signal regulated kinase (ERK). Mol Pharmacol 60:1100-1111, 2001.
    • (2001) Mol Pharmacol , vol.60 , pp. 1100-1111
    • Baillie, G.1    MacKenzie, S.J.2    Houslay, M.D.3
  • 70
    • 0035224063 scopus 로고    scopus 로고
    • Sub-family selective actions in the ability of Erk2 MAP kinase to phosphorylate and regulate the activity of PDE4 cyclic AMP-specific phosphodiesterases
    • Baillie GS, MacKenzie SJ, McPhee I, Houslay MD. Sub-family selective actions in the ability of Erk2 MAP kinase to phosphorylate and regulate the activity of PDE4 cyclic AMP-specific phosphodiesterases. Br J Pharmacol 131:811-819, 2000.
    • (2000) Br J Pharmacol , vol.131 , pp. 811-819
    • Baillie, G.S.1    MacKenzie, S.J.2    McPhee, I.3    Houslay, M.D.4
  • 71
    • 0346158373 scopus 로고    scopus 로고
    • The role of ERK2 docking and phosphorylation of PDE4 cAMP phosphodiesterase isoforms in mediating cross-talk between the cAMP and ERK signalling pathways
    • Houslay MD, Baillie GS. The role of ERK2 docking and phosphorylation of PDE4 cAMP phosphodiesterase isoforms in mediating cross-talk between the cAMP and ERK signalling pathways. Biochem Soc Trans 31:1186-1190, 2003.
    • (2003) Biochem Soc Trans , vol.31 , pp. 1186-1190
    • Houslay, M.D.1    Baillie, G.S.2
  • 72
    • 24644488394 scopus 로고    scopus 로고
    • Investigation of extracellular signal-regulated kinase 2 mitogen-activated protein kinase phosphorylation and regulation of activity of PDE4 cyclic adenosine monophosphate-specific phosphodiesterases
    • Hill EV, Houslay MD, Baillie GS. Investigation of extracellular signal-regulated kinase 2 mitogen-activated protein kinase phosphorylation and regulation of activity of PDE4 cyclic adenosine monophosphate-specific phosphodiesterases. Methods Mol Biol 307:225-237, 2005.
    • (2005) Methods Mol Biol , vol.307 , pp. 225-237
    • Hill, E.V.1    Houslay, M.D.2    Baillie, G.S.3
  • 73
    • 0034646689 scopus 로고    scopus 로고
    • Short term feedback regulation of cAMP in FRTL-5 thyroid cells. Role of PDE4D3 phosphodiesterase activation
    • Oki N, Takahashi SI, Hidaka H, Conti M. Short term feedback regulation of cAMP in FRTL-5 thyroid cells. Role of PDE4D3 phosphodiesterase activation. J Biol Chem 275:10831-10837, 2000.
    • (2000) J Biol Chem , vol.275 , pp. 10831-10837
    • Oki, N.1    Takahashi, S.I.2    Hidaka, H.3    Conti, M.4
  • 74
    • 0037096253 scopus 로고    scopus 로고
    • Phosphodiesterase 1B knock-out mice exhibit exaggerated locomotor hyperactivity and DARPP-32 phosphorylation in response to dopamine agonists and display impaired spatial learning
    • Reed TM, Repaske DR, Snyder GL, Greengard P, Vorhees CV. Phosphodiesterase 1B knock-out mice exhibit exaggerated locomotor hyperactivity and DARPP-32 phosphorylation in response to dopamine agonists and display impaired spatial learning. J Neurosci 22:5188-5197, 2002.
    • (2002) J Neurosci , vol.22 , pp. 5188-5197
    • Reed, T.M.1    Repaske, D.R.2    Snyder, G.L.3    Greengard, P.4    Vorhees, C.V.5
  • 76
    • 10344242415 scopus 로고    scopus 로고
    • Nonredundant function of phosphodiesterases 4D and 4B in neutrophil recruitment to the site of inflammation
    • Ariga M, Neitzert B, Nakae S, Mottin G, Bertrand C, Pruniaux MP, Jin SL, Conti M. Nonredundant function of phosphodiesterases 4D and 4B in neutrophil recruitment to the site of inflammation. J Immunol 173:7531-7538, 2004.
    • (2004) J Immunol , vol.173 , pp. 7531-7538
    • Ariga, M.1    Neitzert, B.2    Nakae, S.3    Mottin, G.4    Bertrand, C.5    Pruniaux, M.P.6    Jin, S.L.7    Conti, M.8
  • 77
    • 24644485431 scopus 로고    scopus 로고
    • Generation of PDE4 knockout mice by gene targeting
    • Jin SL, Latour AM, Conti M. Generation of PDE4 knockout mice by gene targeting. Methods Mol Biol 307:191-210, 2005.
    • (2005) Methods Mol Biol , vol.307 , pp. 191-210
    • Jin, S.L.1    Latour, A.M.2    Conti, M.3
  • 78
    • 0037188511 scopus 로고    scopus 로고
    • Induction of the cyclic nucleotide phosphodiesterase PDE4B is essential for LPS-activated TNF-alpha responses
    • Jin SL, Conti M. Induction of the cyclic nucleotide phosphodiesterase PDE4B is essential for LPS-activated TNF-alpha responses. Proc Natl Acad Sci U S A 99:7628-7633, 2002.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 7628-7633
    • Jin, S.L.1    Conti, M.2
  • 79
    • 0032692936 scopus 로고    scopus 로고
    • Impaired growth and fertility of cAMP-specific phosphodiesterase PDE4D-deficient mice
    • Jin SL, Richard FJ, Kuo WP, D'Ercole AJ, Conti M. Impaired growth and fertility of cAMP-specific phosphodiesterase PDE4D-deficient mice. Proc Natl Acad Sci U S A 96:11998-12003, 1999.
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 11998-12003
    • Jin, S.L.1    Richard, F.J.2    Kuo, W.P.3    D'Ercole, A.J.4    Conti, M.5
  • 80
    • 0141445980 scopus 로고    scopus 로고
    • PDE4D plays a critical role in the control of airway smooth muscle contraction
    • Mehats C, Jin SL, Wahlstrom J, Law E, Umetsu DT, Conti M. PDE4D plays a critical role in the control of airway smooth muscle contraction. FASEB J 17:1831-1841, 2003.
    • (2003) FASEB J , vol.17 , pp. 1831-1841
    • Mehats, C.1    Jin, S.L.2    Wahlstrom, J.3    Law, E.4    Umetsu, D.T.5    Conti, M.6
  • 81
    • 0034612334 scopus 로고    scopus 로고
    • Absence of muscarinic cholinergic airway responses in mice deficient in the cyclic nucleotide phosphodiesterase PDE4D
    • Hansen G, Jin S, Umetsu DT, Conti M. Absence of muscarinic cholinergic airway responses in mice deficient in the cyclic nucleotide phosphodiesterase PDE4D. Proc Natl Acad Sci U S A 97:6751-6756, 2000.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 6751-6756
    • Hansen, G.1    Jin, S.2    Umetsu, D.T.3    Conti, M.4
  • 82
    • 0032919696 scopus 로고    scopus 로고
    • Phosphodiesterase 4B gene transcription is activated by lipopolysaccharide and inhibited by interleukin-10 in human monocytes
    • Ma D, Wu P, Egan RW, Billah MM, Wang P. Phosphodiesterase 4B gene transcription is activated by lipopolysaccharide and inhibited by interleukin-10 in human monocytes. Mol Pharmacol 55:50-57, 1999.
    • (1999) Mol Pharmacol , vol.55 , pp. 50-57
    • Ma, D.1    Wu, P.2    Egan, R.W.3    Billah, M.M.4    Wang, P.5
  • 83
    • 0033033913 scopus 로고    scopus 로고
    • Phosphodiesterase 4B2 is the predominant phosphodiesterase species and undergoes differential regulation of gene expression in human monocytes and neutrophils
    • Wang P, Wu P, Ohleth KM, Egan RW, Billah MM. Phosphodiesterase 4B2 is the predominant phosphodiesterase species and undergoes differential regulation of gene expression in human monocytes and neutrophils. Mol Pharmacol 56:170-174, 1999.
    • (1999) Mol Pharmacol , vol.56 , pp. 170-174
    • Wang, P.1    Wu, P.2    Ohleth, K.M.3    Egan, R.W.4    Billah, M.M.5
  • 84
    • 22544470866 scopus 로고    scopus 로고
    • Specific role of phosphodiesterase 4B in lipopolysaccharide-induced signaling in mouse macrophages
    • Jin SL, Lan L, Zoudilova M, Conti M. Specific role of phosphodiesterase 4B in lipopolysaccharide-induced signaling in mouse macrophages. J Immunol 175:1523-1531, 2005.
    • (2005) J Immunol , vol.175 , pp. 1523-1531
    • Jin, S.L.1    Lan, L.2    Zoudilova, M.3    Conti, M.4
  • 86
    • 33847612208 scopus 로고
    • Adenosine 3′,5′-phosphate in biological materials. I. Purification and properties of cyclic 3′,5′-nucleotide phosphodiesterase and use of this enzyme to characterize adenosine 3′,5′-phosphate in human urine
    • Butcher RW, Sutherland EW. Adenosine 3′,5′-phosphate in biological materials. I. Purification and properties of cyclic 3′,5′-nucleotide phosphodiesterase and use of this enzyme to characterize adenosine 3′,5′-phosphate in human urine. J Biol Chem 237:1244-1250, 1962.
    • (1962) J Biol Chem , vol.237 , pp. 1244-1250
    • Butcher, R.W.1    Sutherland, E.W.2
  • 87
    • 0014418452 scopus 로고
    • Adenyl cyclase and adenosine 3′,5′-cyclic phosphate phosphodiesterase in the receptor tissues of neurohypophysial hormones
    • Dousa T, Rychlik I. Adenyl cyclase and adenosine 3′,5′-cyclic phosphate phosphodiesterase in the receptor tissues of neurohypophysial hormones. Life Sci 7:1039-1044, 1968.
    • (1968) Life Sci , vol.7 , pp. 1039-1044
    • Dousa, T.1    Rychlik, I.2
  • 88
    • 0014954707 scopus 로고
    • The metabolism of adenosine 3′,5′-cyclic phosphate. II. Some properties of adenosine-3′,5′-cyclic-phosphate phosphodiesterase from the rat kidney
    • Dousa T, Rychlik I. The metabolism of adenosine 3′,5′-cyclic phosphate. II. Some properties of adenosine-3′,5′-cyclic-phosphate phosphodiesterase from the rat kidney. Biochim Biophys Acta 204: 10-17, 1970.
    • (1970) Biochim Biophys Acta , vol.204 , pp. 10-17
    • Dousa, T.1    Rychlik, I.2
  • 89
    • 0018789678 scopus 로고
    • Purification and characterization of high-affinity cyclic adenosine monophosphate phosphodiesterase from dog kidney
    • Thompson WJ, Epstein PM, Strada SJ. Purification and characterization of high-affinity cyclic adenosine monophosphate phosphodiesterase from dog kidney. Biochemistry 18:5228-5237, 1979.
    • (1979) Biochemistry , vol.18 , pp. 5228-5237
    • Thompson, W.J.1    Epstein, P.M.2    Strada, S.J.3
  • 90
    • 0026008409 scopus 로고
    • Differential modulation of tissue function and therapeutic potential of selective inhibitors of cyclic nucleotide phosphodiesterase isoenzymes
    • Nicholson CD, Challiss RAJ, Shahid M. Differential modulation of tissue function and therapeutic potential of selective inhibitors of cyclic nucleotide phosphodiesterase isoenzymes. TIPS 12:19-27, 1991.
    • (1991) TIPS , vol.12 , pp. 19-27
    • Nicholson, C.D.1    Challiss, R.A.J.2    Shahid, M.3
  • 91
    • 0025215525 scopus 로고
    • Primary sequence of cyclic nucleotide phosphodiesterase isozymes and the design of selective inhibitors
    • Beavo JA, Reifsnyder DH. Primary sequence of cyclic nucleotide phosphodiesterase isozymes and the design of selective inhibitors. Trends Pharmacol Sci Rev 11:150-155, 1990.
    • (1990) Trends Pharmacol Sci Rev , vol.11 , pp. 150-155
    • Beavo, J.A.1    Reifsnyder, D.H.2
  • 92
  • 94
    • 0031281836 scopus 로고    scopus 로고
    • Inhibitors of cyclic nucleotide phosphodiesterase isozymes block renal tubular cell proliferation induced by folic acid
    • Matousovic K, Tsuboi Y, Walker H, Grande JP, Dousa TP. Inhibitors of cyclic nucleotide phosphodiesterase isozymes block renal tubular cell proliferation induced by folic acid. J Lab Clin Med 130:487-495, 1997.
    • (1997) J Lab Clin Med , vol.130 , pp. 487-495
    • Matousovic, K.1    Tsuboi, Y.2    Walker, H.3    Grande, J.P.4    Dousa, T.P.5
  • 95
    • 0028244071 scopus 로고
    • Formation of reactive oxygen metabolites in glomeruli is suppressed by inhibition of cAMP phosphodiesterase isozyme type IV
    • Chini CCS, Chini EN, Williams JM, Matousovic K, Dousa TP. Formation of reactive oxygen metabolites in glomeruli is suppressed by inhibition of cAMP phosphodiesterase isozyme type IV. Kidney Int 46:28-36, 1994.
    • (1994) Kidney Int , vol.46 , pp. 28-36
    • Chini, C.C.S.1    Chini, E.N.2    Williams, J.M.3    Matousovic, K.4    Dousa, T.P.5
  • 96
    • 0018904117 scopus 로고
    • Cellular action of vasopressin in medullary tubules of mice with hereditary nephrogenic diabetes insipidus
    • Jackson BA, Edwards RM, Valtin H, Dousa TP. Cellular action of vasopressin in medullary tubules of mice with hereditary nephrogenic diabetes insipidus. J Clin Invest 66:110-122, 1980.
    • (1980) J Clin Invest , vol.66 , pp. 110-122
    • Jackson, B.A.1    Edwards, R.M.2    Valtin, H.3    Dousa, T.P.4
  • 97
    • 0026069808 scopus 로고
    • Role of cAMP-phosphodiesterase isozymes in pathogenesis of murine nephrogenic diabetes insipidus
    • Homma S, Gapstur SM, Coffey A, Valtin H, Dousa TP. Role of cAMP-phosphodiesterase isozymes in pathogenesis of murine nephrogenic diabetes insipidus. Am J Physiol 261:F345-F353, 1991.
    • (1991) Am J Physiol , vol.261
    • Homma, S.1    Gapstur, S.M.2    Coffey, A.3    Valtin, H.4    Dousa, T.P.5
  • 98
    • 0025887912 scopus 로고
    • High activity of low-Michaelis-Menten constant 3′,5′-cyclic adenosine monophosphate-phosphodiesterase isozymes in renal inner medulla of mice with hereditary nephrogenic diabetes insipidus
    • Takeda S, Lin C-T, Morgano PG, McIntrye SJ, Dousa TP. High activity of low-Michaelis-Menten constant 3′,5′-cyclic adenosine monophosphate-phosphodiesterase isozymes in renal inner medulla of mice with hereditary nephrogenic diabetes insipidus. Endocrinology 129:287-294, 1991.
    • (1991) Endocrinology , vol.129 , pp. 287-294
    • Takeda, S.1    Lin, C.-T.2    Morgano, P.G.3    McIntrye, S.J.4    Dousa, T.P.5
  • 99
    • 0029737289 scopus 로고    scopus 로고
    • Phosphodiesterase activity as a mediator of renal resistance to ANP in pathological salt retention
    • Lee EY, Humphreys MH. Phosphodiesterase activity as a mediator of renal resistance to ANP in pathological salt retention. Am J Physiol 271:F3-F6, 1996.
    • (1996) Am J Physiol , vol.271
    • Lee, E.Y.1    Humphreys, M.H.2
  • 101
    • 0024458501 scopus 로고
    • A comparison of cyclic AMP signaling system in rat aortic myocytes in primary culture and aorta
    • Schoeffter P, Lugnier C, Travo C, Stoclet JC. A comparison of cyclic AMP signaling system in rat aortic myocytes in primary culture and aorta. Lab Invest 61:177-182, 1989.
    • (1989) Lab Invest , vol.61 , pp. 177-182
    • Schoeffter, P.1    Lugnier, C.2    Travo, C.3    Stoclet, J.C.4
  • 102
    • 0030017253 scopus 로고    scopus 로고
    • Suppression of mesangial proliferative glomerulonephritis development in rats by inhibitors of cAMP phosphodiesterase isozymes types III and IV
    • Tsuboi Y, Shankland SJ, Grande JP, Walker HJ, Johnson RJ, Dousa TP. Suppression of mesangial proliferative glomerulonephritis development in rats by inhibitors of cAMP phosphodiesterase isozymes types III and IV. J Clin Invest 98:262-270, 1996.
    • (1996) J Clin Invest , vol.98 , pp. 262-270
    • Tsuboi, Y.1    Shankland, S.J.2    Grande, J.P.3    Walker, H.J.4    Johnson, R.J.5    Dousa, T.P.6
  • 103
    • 0002014941 scopus 로고
    • Glomerular metabolism
    • Seldin D, Giebisch G, Eds, New York: Raven Press, pp
    • Dousa T. Glomerular metabolism. In: Seldin D, Giebisch G, Eds. The Kidney: Physiology and pathophysiology. New York: Raven Press, pp645-667, 1985.
    • (1985) The Kidney: Physiology and pathophysiology , pp. 645-667
    • Dousa, T.1
  • 104
    • 0028338877 scopus 로고
    • The glomerular response to injury: Progression or resolution?
    • Johnson RJ. The glomerular response to injury: progression or resolution? Kidney Int 45:1769-1782, 1994.
    • (1994) Kidney Int , vol.45 , pp. 1769-1782
    • Johnson, R.J.1
  • 105
    • 0029161583 scopus 로고
    • Inhibitors of cyclic nucleotide phosphodiesterase isozymes type-III and type-IV suppress mitogenesis of rat mesangial cells
    • Matousovic K, Grande JP, Chini CCS, Chini EN, Dousa TP. Inhibitors of cyclic nucleotide phosphodiesterase isozymes type-III and type-IV suppress mitogenesis of rat mesangial cells. J Clin Invest 96:401-410, 1995.
    • (1995) J Clin Invest , vol.96 , pp. 401-410
    • Matousovic, K.1    Grande, J.P.2    Chini, C.C.S.3    Chini, E.N.4    Dousa, T.P.5
  • 106
    • 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 RI. 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 67:353-366, 1997.
    • (1997) J Cell Biochem , vol.67 , pp. 353-366
    • D'Angelo, G.1    Lee, H.2    Weiner, R.I.3
  • 107
    • 0027485031 scopus 로고
    • Increasing cAMP attenuates activation of mitogen activated protein kinase
    • Sevetson BR, Kong X, Lawrence JC. Increasing cAMP attenuates activation of mitogen activated protein kinase. Proc Natl Acad Sci U S A 90:10305-10309, 1993.
    • (1993) Proc Natl Acad Sci U S A , vol.90 , pp. 10305-10309
    • Sevetson, B.R.1    Kong, X.2    Lawrence, J.C.3
  • 109
    • 0031039427 scopus 로고    scopus 로고
    • Rheb interacts with Raf-1 kinase and may function to integrate growth factor- and protein kinase A-dependent signals
    • Yee WM, Worley PF. Rheb interacts with Raf-1 kinase and may function to integrate growth factor- and protein kinase A-dependent signals. Mol Cell Biol 17:921-933, 1997.
    • (1997) Mol Cell Biol , vol.17 , pp. 921-933
    • Yee, W.M.1    Worley, P.F.2
  • 110
    • 0032091856 scopus 로고    scopus 로고
    • Chemokines in interstitial injury
    • Danoff TM. Chemokines in interstitial injury. Kidney Int 53:1807-1808, 1998.
    • (1998) Kidney Int , vol.53 , pp. 1807-1808
    • Danoff, T.M.1
  • 111
    • 0029064922 scopus 로고
    • Renal expression of genes that promote interstitial inflammation and fibrosis in rats with protein-overload proteinuria
    • Eddy AA, Giachelli CM. Renal expression of genes that promote interstitial inflammation and fibrosis in rats with protein-overload proteinuria. Kidney Int 47:1546-1557, 1995.
    • (1995) Kidney Int , vol.47 , pp. 1546-1557
    • Eddy, A.A.1    Giachelli, C.M.2
  • 112
    • 0030903307 scopus 로고    scopus 로고
    • RANTES and monocyte chemoattractant protein-1 (MCP-1) play an important role in the inflammatory phase of crescentic nephritis, but only MCP-1 is involved in crescent formation and interstitial fibrosis
    • Lloyd CM, Minto AW, Dorf ME, Proudfoot A, Wells TN, Salant DJ, Gutierrez-Ramos JC. RANTES and monocyte chemoattractant protein-1 (MCP-1) play an important role in the inflammatory phase of crescentic nephritis, but only MCP-1 is involved in crescent formation and interstitial fibrosis. J Exp Med 185:1371-1380, 1997.
    • (1997) J Exp Med , vol.185 , pp. 1371-1380
    • Lloyd, C.M.1    Minto, A.W.2    Dorf, M.E.3    Proudfoot, A.4    Wells, T.N.5    Salant, D.J.6    Gutierrez-Ramos, J.C.7
  • 114
    • 0027372767 scopus 로고
    • Increased expression of monocyte chemoattractant protein-1 in antithymocyte antibody-induced glomerulonephritis
    • Stahl RA, Thaiss F, Disser M, Helmchen U, Hora K, Schlondorff D. Increased expression of monocyte chemoattractant protein-1 in antithymocyte antibody-induced glomerulonephritis. Kidney Int 44:1036-1047, 1993.
    • (1993) Kidney Int , vol.44 , pp. 1036-1047
    • Stahl, R.A.1    Thaiss, F.2    Disser, M.3    Helmchen, U.4    Hora, K.5    Schlondorff, D.6
  • 115
    • 0032529159 scopus 로고    scopus 로고
    • Smads and early developmental signaling by the TGF-β superfamily
    • Whitman M. Smads and early developmental signaling by the TGF-β superfamily. Genes Dev 12:2445-2462, 1998.
    • (1998) Genes Dev , vol.12 , pp. 2445-2462
    • Whitman, M.1
  • 117
    • 4243470784 scopus 로고
    • Isoenzymes of cyclic-3′,5′-nucleotide phosphodiesterases (PDE) in rat glomerular epithelial cells (GEC) and mesangial cells (MC). (abstract)
    • Chini C, Grande J, Thompson M, Walker H, Dousa T. Isoenzymes of cyclic-3′,5′-nucleotide phosphodiesterases (PDE) in rat glomerular epithelial cells (GEC) and mesangial cells (MC). (abstract). FASEB J 8:A83, 1994.
    • (1994) FASEB J , vol.8
    • Chini, C.1    Grande, J.2    Thompson, M.3    Walker, H.4    Dousa, T.5
  • 118
    • 0026752462 scopus 로고
    • Cyclic 3′,5′-nucleotide diesterases in dynamics of cAMP and cGMP in rat collecting duct cells
    • Yamaki M, McIntyre S, Rassier ME, Schwartz JH, Dousa TP. Cyclic 3′,5′-nucleotide diesterases in dynamics of cAMP and cGMP in rat collecting duct cells. Am J Physiol 262:F957-F964, 1992.
    • (1992) Am J Physiol , vol.262
    • Yamaki, M.1    McIntyre, S.2    Rassier, M.E.3    Schwartz, J.H.4    Dousa, T.P.5
  • 119
    • 0026517645 scopus 로고
    • Isozymes of cyclic-3′,5′-nucleotide phosphodiesterases in renal epithelial LLC-PK1 cells
    • Rassier ME, McIntyre SJ, Yamaki M, Takeda S, Lin J-T, Dousa TP. Isozymes of cyclic-3′,5′-nucleotide phosphodiesterases in renal epithelial LLC-PK1 cells. Kidney Int 41:88-99, 1992.
    • (1992) Kidney Int , vol.41 , pp. 88-99
    • Rassier, M.E.1    McIntyre, S.J.2    Yamaki, M.3    Takeda, S.4    Lin, J.-T.5    Dousa, T.P.6
  • 120
    • 0027160233 scopus 로고
    • ADH resistance of LLC-PK1 cells caused by overexpression of cAMP-phosphodiesterase type-IV
    • Yamaki M, McIntyre S, Murphy JM, Swinnen JV, Conti M, Dousa TP. ADH resistance of LLC-PK1 cells caused by overexpression of cAMP-phosphodiesterase type-IV. Kidney Int 43:1286-1297, 1993.
    • (1993) Kidney Int , vol.43 , pp. 1286-1297
    • Yamaki, M.1    McIntyre, S.2    Murphy, J.M.3    Swinnen, J.V.4    Conti, M.5    Dousa, T.P.6
  • 121
    • 0033756528 scopus 로고    scopus 로고
    • Nitric oxide and atrial natriuretic factor stimulate cGMP-dependent membrane insertion of aquaporin 2 in renal epithelial cells
    • Bouley R, Breton S, Sun T, McLaughlin M, Nsumu NN, Lin HY, Ausiello DA, Brown D. Nitric oxide and atrial natriuretic factor stimulate cGMP-dependent membrane insertion of aquaporin 2 in renal epithelial cells. J Clin Invest 106:1115-1126, 2000.
    • (2000) J Clin Invest , vol.106 , pp. 1115-1126
    • Bouley, R.1    Breton, S.2    Sun, T.3    McLaughlin, M.4    Nsumu, N.N.5    Lin, H.Y.6    Ausiello, D.A.7    Brown, D.8
  • 122
    • 0030723843 scopus 로고    scopus 로고
    • Renal accumulation and excretion of cyclic adenosine monophosphate in a murine model of slowly progressive polycystic kidney disease
    • Yamaguchi T, Nagao S, Kasahara M, Takahashi H, Grantham J. Renal accumulation and excretion of cyclic adenosine monophosphate in a murine model of slowly progressive polycystic kidney disease. Am J Kidney Dis 20:703-709, 1997.
    • (1997) Am J Kidney Dis , vol.20 , pp. 703-709
    • Yamaguchi, T.1    Nagao, S.2    Kasahara, M.3    Takahashi, H.4    Grantham, J.5
  • 123
    • 0031279241 scopus 로고    scopus 로고
    • Renal cell proliferation and the two faces of cyclic adenosine monophosphate
    • Grantham JJ. Renal cell proliferation and the two faces of cyclic adenosine monophosphate. J Lab Clin Med 130:459-460, 1997.
    • (1997) J Lab Clin Med , vol.130 , pp. 459-460
    • Grantham, J.J.1
  • 124
    • 0013537241 scopus 로고
    • Renal epithelial cyst formation and enlargement in vitro: Dependence on cAMP
    • Mangoo-Karim R, Uchic M, Lechene C, Grantham J. Renal epithelial cyst formation and enlargement in vitro: dependence on cAMP. Proc Natl Acad Sci U S A 86:6007-6011, 1989.
    • (1989) Proc Natl Acad Sci U S A , vol.86 , pp. 6007-6011
    • Mangoo-Karim, R.1    Uchic, M.2    Lechene, C.3    Grantham, J.4
  • 126
    • 0033983976 scopus 로고    scopus 로고
    • Pentoxifylline reduces in vitro renal myofibroblast proliferation and collagen secretion
    • Hewitson TD, Martic M, Kelynack KJ, Pedagogos E, Becker GJ. Pentoxifylline reduces in vitro renal myofibroblast proliferation and collagen secretion. Am J Nephrol 20:82-88, 2000.
    • (2000) Am J Nephrol , vol.20 , pp. 82-88
    • Hewitson, T.D.1    Martic, M.2    Kelynack, K.J.3    Pedagogos, E.4    Becker, G.J.5
  • 127
    • 0036740957 scopus 로고    scopus 로고
    • Dipyridamole inhibits in vitro renal fibroblast proliferation and collagen synthesis
    • Hewitson TD, Tait MG, Kelynack KJ, Martic M, Becker GJ. Dipyridamole inhibits in vitro renal fibroblast proliferation and collagen synthesis. J Lab Clin Med 140:199-208, 2002.
    • (2002) J Lab Clin Med , vol.140 , pp. 199-208
    • Hewitson, T.D.1    Tait, M.G.2    Kelynack, K.J.3    Martic, M.4    Becker, G.J.5
  • 129
    • 0033964770 scopus 로고    scopus 로고
    • Type IV phosphodiesterase inhibitor is effective in prevention and treatment of experimental crescentic glomerulonephritis
    • Tam FW, Smith J, Agarwal S, Karkar AM, Morel D, Thompson EM, Pusey CD. Type IV phosphodiesterase inhibitor is effective in prevention and treatment of experimental crescentic glomerulonephritis. Nephron 84:58-66, 2000.
    • (2000) Nephron , vol.84 , pp. 58-66
    • Tam, F.W.1    Smith, J.2    Agarwal, S.3    Karkar, A.M.4    Morel, D.5    Thompson, E.M.6    Pusey, C.D.7
  • 131
    • 0035019609 scopus 로고    scopus 로고
    • Enhanced protection from renal ischemia-reperfusion [correction of ischemia:reperfusion] injury with A(2A)-adenosine receptor activation and PDE 4 inhibition
    • Okusa MD, Linden J, Huang L, Rosin DL, Smith DF, Sullivan G. Enhanced protection from renal ischemia-reperfusion [correction of ischemia:reperfusion] injury with A(2A)-adenosine receptor activation and PDE 4 inhibition. Kidney Int 59:2114-2125, 2001.
    • (2001) Kidney Int , vol.59 , pp. 2114-2125
    • Okusa, M.D.1    Linden, J.2    Huang, L.3    Rosin, D.L.4    Smith, D.F.5    Sullivan, G.6
  • 132
    • 0033190943 scopus 로고    scopus 로고
    • Selective A2A adenosine receptor activation reduces ischemia-reperfusion injury in rat kidney
    • Okusa MD, Linden J, MacDonald T, Huang L. Selective A2A adenosine receptor activation reduces ischemia-reperfusion injury in rat kidney. Am J Physiol 277:F404-F412, 1999.
    • (1999) Am J Physiol , vol.277
    • Okusa, M.D.1    Linden, J.2    MacDonald, T.3    Huang, L.4
  • 133
    • 0030437941 scopus 로고    scopus 로고
    • Inhibition of type IV phosphodiesterase by Ro 20-1724 attenuates endotoxin-induced acute renal failure
    • Begany DP, Carcillo JA, Herzer WA, Mi Z, Jackson EK. Inhibition of type IV phosphodiesterase by Ro 20-1724 attenuates endotoxin-induced acute renal failure. J Pharmacol Exp Ther 278:37-41, 1996.
    • (1996) J Pharmacol Exp Ther , vol.278 , pp. 37-41
    • Begany, D.P.1    Carcillo, J.A.2    Herzer, W.A.3    Mi, Z.4    Jackson, E.K.5
  • 134
    • 0030441043 scopus 로고    scopus 로고
    • Treatment with the type IV phosphodiesterase inhibitor Ro 20-1724 protects renal and mesenteric blood flow in endotoxemic rats treated with norepinephrine
    • Carcillo JA, Herzer WA, Mi Z, Thomas NJ, Jackson EK. Treatment with the type IV phosphodiesterase inhibitor Ro 20-1724 protects renal and mesenteric blood flow in endotoxemic rats treated with norepinephrine. J Pharmacol Exp Ther 279:1197-1204, 1996.
    • (1996) J Pharmacol Exp Ther , vol.279 , pp. 1197-1204
    • Carcillo, J.A.1    Herzer, W.A.2    Mi, Z.3    Thomas, N.J.4    Jackson, E.K.5
  • 135
    • 0029020968 scopus 로고
    • Zaprinast accelerates recovery from established acute renal failure in the rat
    • Guan Z, Miller SB, Greenwald JE. Zaprinast accelerates recovery from established acute renal failure in the rat. Kidney Int 47:1569-1575, 1995.
    • (1995) Kidney Int , vol.47 , pp. 1569-1575
    • Guan, Z.1    Miller, S.B.2    Greenwald, J.E.3
  • 136
    • 0024354722 scopus 로고
    • Phosphodiesterase isozyme inhibition and the potentiation by zaprinast of endothelium-derived relaxing factor and guanylate cyclase stimulating agents in vascular smooth muscle
    • Harris AL, Lemp BM, Bentley RG, Perrone MH, Hamel LT, Silver PJ. Phosphodiesterase isozyme inhibition and the potentiation by zaprinast of endothelium-derived relaxing factor and guanylate cyclase stimulating agents in vascular smooth muscle. J Pharmacol Exp Ther 249:394-400, 1989.
    • (1989) J Pharmacol Exp Ther , vol.249 , pp. 394-400
    • Harris, A.L.1    Lemp, B.M.2    Bentley, R.G.3    Perrone, M.H.4    Hamel, L.T.5    Silver, P.J.6
  • 137
  • 139
    • 0026130307 scopus 로고
    • Efficacy and tolerance of vinpocetine in ambulant patients suffering from mild to moderate organic psychosyndromes
    • Hindmarch I, Fuchs HH, Erzigkeit H. Efficacy and tolerance of vinpocetine in ambulant patients suffering from mild to moderate organic psychosyndromes. Int Clin Psychopharmacol 6:31-43, 1991.
    • (1991) Int Clin Psychopharmacol , vol.6 , pp. 31-43
    • Hindmarch, I.1    Fuchs, H.H.2    Erzigkeit, H.3
  • 142
    • 0027433339 scopus 로고
    • Phosphodiesterase III inhibitors: Long-term risks and short-term benefits
    • Cruickshank JM. Phosphodiesterase III inhibitors: long-term risks and short-term benefits. Cardiovasc Drugs Ther 7:655-660, 1993.
    • (1993) Cardiovasc Drugs Ther , vol.7 , pp. 655-660
    • Cruickshank, J.M.1
  • 143
    • 0029891391 scopus 로고    scopus 로고
    • Milrinone: Basic and clinical pharmacology and acute and chronic management
    • Shipley JB, Tolman D, Hastillo A, Hess ML. Milrinone: basic and clinical pharmacology and acute and chronic management. Am J Med Sci 311:286-291, 1996.
    • (1996) Am J Med Sci , vol.311 , pp. 286-291
    • Shipley, J.B.1    Tolman, D.2    Hastillo, A.3    Hess, M.L.4
  • 144
    • 0029841867 scopus 로고    scopus 로고
    • Pharmacologic treatment of congestive heart failure
    • Carson P. Pharmacologic treatment of congestive heart failure. Clin Cardiol 19:271-277, 1996.
    • (1996) Clin Cardiol , vol.19 , pp. 271-277
    • Carson, P.1
  • 145
    • 0035544829 scopus 로고    scopus 로고
    • Cilostazol (pletal): A dual inhibitor of cyclic nucleotide phosphodiesterase type 3 and adenosine uptake
    • Liu Y, Shakur Y, Yoshitake M, Kambayashi J. Cilostazol (pletal): a dual inhibitor of cyclic nucleotide phosphodiesterase type 3 and adenosine uptake. Cardiovasc Drug Rev 19:369-386, 2001.
    • (2001) Cardiovasc Drug Rev , vol.19 , pp. 369-386
    • Liu, Y.1    Shakur, Y.2    Yoshitake, M.3    Kambayashi, J.4
  • 147
    • 0030988865 scopus 로고    scopus 로고
    • Phosphodiesterase inhibition improves agonist-induced relaxation of hypertensive pulmonary arteries
    • Wagner RS, Smith CJ, Taylor AM, Rhoades RA. Phosphodiesterase inhibition improves agonist-induced relaxation of hypertensive pulmonary arteries. J Pharmacol Exp Ther 282:1650-1657, 1997.
    • (1997) J Pharmacol Exp Ther , vol.282 , pp. 1650-1657
    • Wagner, R.S.1    Smith, C.J.2    Taylor, A.M.3    Rhoades, R.A.4
  • 148
    • 0026734249 scopus 로고
    • Could isoenzyme-selective phosphodiesterase inhibitors render bronchodilator therapy redundant in the treatment of bronchial asthma?
    • Giembycz MA. Could isoenzyme-selective phosphodiesterase inhibitors render bronchodilator therapy redundant in the treatment of bronchial asthma? Biochem Pharm 43:2041-2051, 1992.
    • (1992) Biochem Pharm , vol.43 , pp. 2041-2051
    • Giembycz, M.A.1
  • 149
    • 0030248274 scopus 로고    scopus 로고
    • Phosphodiesterase 4 and tolerance to beta 2-adrenoceptor agonists in asthma
    • Giembycz MA. Phosphodiesterase 4 and tolerance to beta 2-adrenoceptor agonists in asthma. Trends Pharmacol Sci 17:331-336, 1996.
    • (1996) Trends Pharmacol Sci , vol.17 , pp. 331-336
    • Giembycz, M.A.1
  • 150
    • 0025868447 scopus 로고
    • Phosphodiesterase inhibitors: New opportunities for the treatment of asthma
    • Torphy TJ, Undem BJ. Phosphodiesterase inhibitors: new opportunities for the treatment of asthma. Thorax 46:512-523, 1991.
    • (1991) Thorax , vol.46 , pp. 512-523
    • Torphy, T.J.1    Undem, B.J.2
  • 152
    • 0024833641 scopus 로고
    • Antidepressant effects of rolipram in a genetic animal model of depression: Cholinergic supersensitivity and weight gain
    • Overstreet DH, Double K, Schiller GD. Antidepressant effects of rolipram in a genetic animal model of depression: cholinergic supersensitivity and weight gain. Pharmacol Biochem Behav 34: 691-696, 1989.
    • (1989) Pharmacol Biochem Behav , vol.34 , pp. 691-696
    • Overstreet, D.H.1    Double, K.2    Schiller, G.D.3
  • 156
    • 0029844689 scopus 로고    scopus 로고
    • cAMP-mediated vascular protection in an orthotopic rat lung transplant model. Insights into the mechanism of action of prostaglandin E1 to improve lung preservation
    • Naka Y, Roy DK, Liao H, Chowdhury NC, Michler RE, Oz MC, Pinsky DJ. cAMP-mediated vascular protection in an orthotopic rat lung transplant model. Insights into the mechanism of action of prostaglandin E1 to improve lung preservation. Circ Res 79:773-783, 1996.
    • (1996) Circ Res , vol.79 , pp. 773-783
    • Naka, Y.1    Roy, D.K.2    Liao, H.3    Chowdhury, N.C.4    Michler, R.E.5    Oz, M.C.6    Pinsky, D.J.7
  • 157
    • 0030997571 scopus 로고    scopus 로고
    • Antagonists of cyclic nucleotide phosphodiesterase (PDE) isozymes PDE 3 and PDE 4 suppress lymphoblastic response to HLA class II alloantigens: A potential novel approach to preventing allograft rejection?
    • Dousa MK, Moore SB, Ploeger NA, DeGoey SR, Dousa TP. Antagonists of cyclic nucleotide phosphodiesterase (PDE) isozymes PDE 3 and PDE 4 suppress lymphoblastic response to HLA class II alloantigens: a potential novel approach to preventing allograft rejection? Clin Nephrol 47:187-189, 1997.
    • (1997) Clin Nephrol , vol.47 , pp. 187-189
    • Dousa, M.K.1    Moore, S.B.2    Ploeger, N.A.3    DeGoey, S.R.4    Dousa, T.P.5
  • 158
    • 0030296268 scopus 로고    scopus 로고
    • A selective type V phosphodiesterase inhibitor, E4021, protects the development of right ventricular overload and medial thickening of pulmonary arteries in a rat model of pulmonary hypertension
    • Takahashi T, Kanda T, Inoue M, Suzuki T, Kobayashi I, Kodama K, Nagai R. A selective type V phosphodiesterase inhibitor, E4021, protects the development of right ventricular overload and medial thickening of pulmonary arteries in a rat model of pulmonary hypertension. Life Sci 59:PL371-377, 1996.
    • (1996) Life Sci , vol.59
    • Takahashi, T.1    Kanda, T.2    Inoue, M.3    Suzuki, T.4    Kobayashi, I.5    Kodama, K.6    Nagai, R.7
  • 159
    • 0027406998 scopus 로고
    • M&B 22948, a cGMP phosphodiesterase inhibitor, is a pulmonary vasodilator in lambs
    • Braner DA, Fineman JR, Chang R, Soifer SJ. M&B 22948, a cGMP phosphodiesterase inhibitor, is a pulmonary vasodilator in lambs. Am J Physiol 264:H252-H258, 1993.
    • (1993) Am J Physiol , vol.264
    • Braner, D.A.1    Fineman, J.R.2    Chang, R.3    Soifer, S.J.4
  • 160
    • 0030438222 scopus 로고    scopus 로고
    • Boolell M, Gepi-Attee S, Gingell JC, Allen MJ. Sildenafil, a novel effective oral therapy for male erectile dysfunction. Br J Urol 78:257-261, 1996.
    • Boolell M, Gepi-Attee S, Gingell JC, Allen MJ. Sildenafil, a novel effective oral therapy for male erectile dysfunction. Br J Urol 78:257-261, 1996.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.