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Information on EC 3.1.4.53 - 3',5'-cyclic-AMP phosphodiesterase and Organism(s) Rattus norvegicus and UniProt Accession P14646
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3.1.4.53 3',5'-cyclic-AMP phosphodiesteraseIUBMB Comments
Requires Mg2+ or Mn2+ for activity . This enzyme is specific for 3',5'-cAMP and does not hydrolyse other nucleoside 3',5'-cyclic phosphates such as cGMP (cf. EC 3.1.4.17, 3,5-cyclic-nucleotide phosphodiesterase and EC 3.1.4.35, 3,5-cyclic-GMP phosphodiesterase). It is involved in modulation of the levels of cAMP, which is a mediator in the processes of cell transformation and proliferation .
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The taxonomic range for the selected organisms is: Rattus norvegicus
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
pde4b, phosphodiesterase 4, phosphodiesterase-4, camp-phosphodiesterase, camp-specific phosphodiesterase, pde4d3, pde4d5, phosphodiesterase type 4, pde7b, pde7a, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
PDE4
PDE4A
PDE4B
PDE4B1
PDE4B2
PDE4B3
PDE4B4
PDE4D
PATHWAY SOURCE
PATHWAYS
KEGG
SYSTEMATIC NAME
IUBMB Comments
3',5'-cyclic-AMP 5'-nucleotidohydrolase
Requires Mg2+ or Mn2+ for activity [2]. This enzyme is specific for 3',5'-cAMP and does not hydrolyse other nucleoside 3',5'-cyclic phosphates such as cGMP (cf. EC 3.1.4.17, 3,5-cyclic-nucleotide phosphodiesterase and EC 3.1.4.35, 3,5-cyclic-GMP phosphodiesterase). It is involved in modulation of the levels of cAMP, which is a mediator in the processes of cell transformation and proliferation [3].
CAS REGISTRY NUMBER
COMMENTARY
9036-21-9
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
adenosine 3',5'-cyclic phosphate + H2O
adenosine 5'-phosphate
-
-
-
?
adenosine 3',5'-cyclic phosphate + H2O
adenosine 5'-phosphate
PDE4B4 isoform may have a distinct functional role in regulating cAMP levels in specific cell types
-
-
?
3',5'-cAMP + H2O
5'-AMP
-
-
-
-
?
adenosine 3',5'-cyclic phosphate + H2O
adenosine 5'-phosphate
-
-
-
-
?
adenosine 3',5'-cyclic phosphate + H2O
adenosine 5'-phosphate
-
-
-
?
adenosine 3',5'-cyclic phosphate + H2O
adenosine 5'-phosphate
-
attenuation of the activity of the cAMP-specific phosphodiesterase PDE4A5 by interaction with the immunophilin XAP2
-
-
?
additional information
?
-
-
during development PDE4 is the major PDE
-
-
?
additional information
?
-
-
almost all the PDE4D isoforms, known as the main cAMP-regulated rolipramsensitive PDE in Sertoli cells, are expressed throughout the early postpartum period, whereas only the short PDE4D isoforms (PDE4D1 and PDE4D2) are transcriptionally regulated by FSH
-
-
?
additional information
?
-
-
increased PDE4 activity, specifically phosphodiesterase 4B4 activity, reduces beta-adrenergic signaling in the kidney and contributes to salt-sensitive hypertension in the Dahl salt-sensitive rat
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
adenosine 3',5'-cyclic phosphate + H2O
adenosine 5'-phosphate
PDE4B4 isoform may have a distinct functional role in regulating cAMP levels in specific cell types
-
-
?
additional information
?
-
-
during development PDE4 is the major PDE
-
-
?
additional information
?
-
-
almost all the PDE4D isoforms, known as the main cAMP-regulated rolipramsensitive PDE in Sertoli cells, are expressed throughout the early postpartum period, whereas only the short PDE4D isoforms (PDE4D1 and PDE4D2) are transcriptionally regulated by FSH
-
-
?
additional information
?
-
-
increased PDE4 activity, specifically phosphodiesterase 4B4 activity, reduces beta-adrenergic signaling in the kidney and contributes to salt-sensitive hypertension in the Dahl salt-sensitive rat
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
CI-1044
-
i.e. (R)-N-[9-amino-3,4,6,7-tetrahydro-4-oxo-1-phenylpyrrolo[3,2,1-j,k][1,4] benzodiazepin-3-yl]-3-pyridinecarboxamide, selective inhibitor of PDE4, administration of 160 mg/kg of CI-1044 causes perivascular and interstitial inflammation, with infiltrates of admixed neutrophils and macrophages but without evidence of vascular necrosis, PDE4 inhibitor CI-1044 induces changes of vascular tone that could lead to histological alterations in the mesenteric area
DC-TA 46
-
the inhibitor affects memory retention in a visible/hidden-platform water maze task. This memory impairment can be correlated to the decrease of cAMP nucleotide, due to the induction of a PDE4D cAMP-specific PDE isoform
XAP2
-
noncompetitive inhibition, aryl-hydrocarbon receptor-interacting protein XAP2 inhibits PDE4A5 activity by XAP2 does not require any intermediate proteins. XAP2 inhibits PDE4A5 and not other PDE4 isoforms
-
Zl-n-91
-
selective PDE4 inhibitor, Zl-n-91 at 0.03, 0.3 or 3 mg/kg dose dependently inhibits PDE4 activity
rolipram
-
the inhibitor affects memory retention in a visible/hidden-platform water maze task. This memory impairment can be correlated to the decrease of cAMP nucleotide, due to the induction of a PDE4D cAMP-specific PDE isoform
additional information
-
removal of the last 35 amino acids of an N-terminal 80-residue highly conserved region (UCR2) results in a 6fold increase in PDE activity, providing evidence that this part of the molecule acts as an intramolecular inhibitor
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
extract of Ginkgo biloba
-
some beneficial effects of extract of Ginkgo biloba might be due to its modulating influences on cellular cyclic AMP levels via activation of membrane-bound PDE
-
haloperidol
-
chronic treatment with 20 mg/kg clozapine increases PDE4B2 and PDE4B4 expression by 102 and 71%, respectively
additional information
-
PDE4B1, PDE4B2, PDE4B3, and PDE4B4 are not changed by chronic haloperidol treatment
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
age-related increases in isoforms PDE8A3, PDE8A4/5 protein expression are confirmed in hippocampus of old versus young rodents. Relative to young rats, the hippocampi of old rats demonstrate strikingly decreased phosphorylation of GluR1, CaMKIIalpha, and CaMKIIbeta, decreased expression of the transmembrane AMPA regulatory proteins gamma2 (a.k.a. stargazin) and gamma8, and increased trimethylation of H3K27. Expression of isoforms of PDE8A4/5, PDE8A3 correlate with these functional endpoints in young but not old rats
-
PDE4 is present in young and adult gland. During development PDE4 is the major PDE
additional information
-
isoforms PDE4A, PDE4D, PDE7A, PDE8A, PDE8B show an age-related increase or decrease in mRNA expression in at least 1 of the 4 brain regions examined (hippocampus, cortex, striatum, and cerebellum). mRNA expression of isoforms PDE7A, PDE7B does not change with age. Age-related increases in PDE11A4, PDE8A3, PDE8A4/5, and PDE1C1 protein expression are confirmed in hippocampus of old versus young rodents, as are age-related increases in PDE8A3 protein expression in the striatum
-
age-related increases in isoform PDE8A3 protein expression are confirmed in hippocampus of old versus young rodents
-
the phosphodiesterase 4B4 isoform present in kidney tissue from spontaneously hypertensive rats, hypertensive Dahl salt-sensitive rats, and Dahl salt-resistant rats, phosphodiesterase 4B expression is detected in the renal vasculature, proximal tubules, and distal tubules
-
immature cell. Almost all PDE4D variants are expressed throughout the early postpartum period with a specific increase in PDE4 activity in both soluble and particulate fraction of 20 day old Sertoli cells
-
isolated from 10-, 20-, and 30-days-old rats. Specific increase in PDE4 activity in both the soluble and particulate subcellular fractions of 20-days-old Sertoli cells. Almost all the PDE4D isoforms, known as the main cAMP-regulated rolipramsensitive PDE in Sertoli cells, are expressed throughout the early postpartum period, whereas only the short PDE4D isoforms (PDE4D1 and PDE4D2) are transcriptionally regulated by FSH. The subcellular distribution and expression of PDE4D proteins are unaffected by the developmental status of the Sertoli cells. Only the expression of short PDE4D1 appears to be upregulated by FSH and only in 20-days-old Sertoli cells, which suggests phenotype-dependent differential regulation of Pde4d1 mRNA translation
additional information
mRNA expression levels of PDEs 4A, 4B, 4C and 4D are significantly higher in rats than in humans. Higher PDE4 expression levels are correlated with a higher enzyme activity level in rat leukocytes
additional information
mRNA expression levels of PDEs 4A, 4B, 4C and 4D are significantly higher in rats than in humans. Higher PDE4 expression levels are correlated with a higher enzyme activity level in rat leukocytes
additional information
mRNA expression levels of PDEs 4A, 4B, 4C and 4D are significantly higher in rats than in humans. Higher PDE4 expression levels are correlated with a higher enzyme activity level in rat leukocytes
additional information
mRNA expression levels of PDEs 4A, 4B, 4C and 4D are significantly higher in rats than in humans. Higher PDE4 expression levels are correlated with a higher enzyme activity level in rat leukocytes
additional information
mRNA expression levels of PDEs 4A, 4B, 4C and 4D are significantly higher in rats than in humans. Higher PDE4 expression levels are correlated with a higher enzyme activity level in rat leukocytes
additional information
mRNA expression levels of PDEs 4A, 4B, 4C and 4D are significantly higher in rats than in humans. Higher PDE4 expression levels are correlated with a higher enzyme activity level in rat leukocytes
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
PDE4A splice variant RD1 contains a membrane-association signal which allows the targeted expression of RD1 within the Golgi complex of human follicular thyroid carcinoma cell lines FTC133 and FTC236
additional information
-
the soluble PDE4 activities are mainly related to the long PDE4D isoforms and short PDE4D1 is predominantly particulate
-
helix-1 is important for intracellular targeting of PDE4A1 in living cells, facilitating membrane association, targeting to the trans-Golgi stack and conferring Ca2+-stimulated intracellular redistribution in a manner that is dependent on the phospholipase-D-mediated generation of phosphatidic acid
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
-
a transmembrane-adenylyl-cyclase-cAMP-protein kinase A cascade modulated by isoform PDE1C is critical in regulating platelet-derived growth factor -receptor-beta degradation
physiological function
malfunction
-
effects of acute hypoxia on cAMP accumulation induced by PDE inhibitors in oxygen-specific chemosensors, the carotid bodies and in non-chemosensitive CB-related structures: carotid arteries and superior cervical ganglia, overview. Acute hypoxia enhances the effects of IBMX and PDE4 inhibitors on cAMP accumulation in carotid arteries and bodies, while in superior cervical ganglia In SCG, acute hypoxia reduces cAMP accumulation induced by all the four PDE inhibitors
malfunction
-
in cultured smooth muscle cells, isoform PDE1C deficiency or PDE1 inhibition attenuates smooth muscle cell proliferation and migration
physiological function
-
phosphodiesterase 4 contributes to maintenance of retinal vascular tone
physiological function
cAMP-specific PDE 4 isoforms underpin compartmentalized cAMP signalling in mammalian cells through targeting to specific signalling complexes. Phosphorylation of PDE4A5 by MK2 confers the amplification of intracellular cAMP accumulation in response to adenylate cyclase activation by attenuating a major desensitization system to cAMP. Long PDE4 isoforms thus provide a novel node for cross-talk between the cAMP and p38 MAPK signalling systems at the level of MK2
physiological function
-
cAMP-phosphodiesterase 1C plays a role in regulating growth factor receptor stability, vascular smooth muscle cell growth, migration, and neointimal hyperplasia
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PDE4B_RAT
736
0
83375
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
87000
-
PDE4B1 or PDE4B3 recombinant protein, SDS-PAGE, the 87000 Da band is termed PDE4B1/B3 due to difficulty of resolving it into separate bands using SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
treatment of COS7 cells with forskolin, to elevate cAMP levels, produced activation of PDE4B4, which is associated with the phosphorylation of PDE4B4 on Ser-56 within UCR1
phosphoprotein
phosphoprotein
-
aryl-hydrocarbon receptor-interacting protein XAP2 attenuates the ability of cAMP-dependent protein kinase to phosphorylate PDE4A5
phosphoprotein
-
protein kinase A catalyzes phosphorylation (at Ser-54) and activation of isoform PDE4D3. Protein phosphatase 2A associated with muscle A kinase-anchoring protein complexes promotes PDE4D3 dephosphorylation at Ser-54
phosphoprotein
phosphorylation of cAMP-specific PDE4A5 by MAPK-activated protein kinase 2, also called MAPKAPK2. PDE4A5 is phosphorylated at Ser147, within the regulatory UCR1, ultraconserved region 1, domain conserved among PDE4 long isoforms. Phosphorylation by MK2, although not altering PDE4A5 activity, markedly attenuates PDE4A5 activation through phosphorylation by protein kinase A. Phosphorylation by MK2 also triggers a conformational change in PDE4A5 that attenuates PDE4A5 interaction with proteins whose binding involves UCR2, such as DISC1 and AIP, but not the UCR2-independent interacting scaffold protein beta-arrestin
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of PDE4B4 cDNA in COS7 cells. Treatment of COS7 cells with forskolin, to elevate cAMP levels, produced activation of PDE4B4, which is associated with the phosphorylation of PDE4B4 on Ser56 within UCR1
cells of two human follicular thyroid carcinoma cell lines (FTC133, FTC236) are stably transfected with a cDNA encoding the PDE4A cAMP-specific phosphodiesterase (PDE) splice variant RD1 (RNPDE4A1A) so as to generate the cloned cell lines, FTC133A and FTC236A
full coding sequence of the phosphodiesterase PDE4D1 is inserted in the bacterial expression vector pGEX-KG. N- and C-terminal truncations are also placed in the same vector, allowing the expression and purification of glutathione S-transferase (GST)-PDE fusion proteins using glutathione-Sepharose
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
forskolin treatment alone is unable to stimulate mAKAP-bound PDE4D3 activity significantly in HEK-293 cells, whereas forskolin (0.05 mM) and okadaic acid (0.3 mM) treatment together synergistically increase PDE4D3 activity
-
isoforms PDE1B, PDE1C, PDE2A, PDE4A, PDE4D, PDE5A, PDE7A, PDE8A, PDE8B, PDE10A, and PDE11A show an age-related increase or decrease in mRNA expression in at least 1 of the 4 brain regions examined (hippocampus, cortex, striatum, and cerebellum). mRNA expression of isoforms PDE1A, PDE3A, PDE3B, PDE4B, PDE7A, PDE7B, and PDE9A does not change with age
-
transcription factor Trps1 directly activates isoform Pde4d transcription
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
-
PDE5 inhibition improved short-term object recognition performance after an acute tryptophan depletion induced deficit
molecular biology
molecular biology
-
convenient and sensitive radioenzymatic assay for characterization and determining the contribution if the various PDE families in cell and tissue, PDE4
molecular biology
-
convenient and sensitive radioenzymatic assay for characterization and determining the contribution if the various PDE families in cell and tissue, PDE7
molecular biology
-
convenient and sensitive radioenzymatic assay for characterization and determining the contribution if the various PDE families in cell and tissue, PDE8
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Tanaka, S.; Shimooka, S.; Shimomura, H.
Changes in phosphodiesterase activity in the developing rat submandibular gland
Arch. Oral Biol.
47
567-576
2002
Rattus norvegicus
Giorgi, M.; Modica, A.; Pompili, A.; Pacitti, C.; Gasbarri, A.
The induction of cyclic nucleotide phosphodiesterase 4 gene (PDE4D) impairs memory in a water maze task
Behav. Brain Res.
154
99-106
2004
Rattus norvegicus
Keravis, T.; Thaseldar-Roumie, R.; Lugnier, C.
Assessment of phosphodiesterase isozyme contribution in cell and tissue extracts
Methods Mol. Biol.
307
63-74
2005
Rattus norvegicus
Levallet, G.; Levallet, J.; Bouraima-Lelong, H.; Bonnamy, P.J.
Expression of the cAMP-phosphodiesterase PDE4D isoforms and age-related changes in follicle-stimulating hormone-stimulated PDE4 activities in immature rat sertoli cells
Biol. Reprod.
76
794-803
2007
Rattus norvegicus
Fougier, S.; Nemoz, G.; Prigent, A.F.; Marivet, M.; Bourguignon, J.J.; Wermuth, C.; Pacheco, H.
Purification of cAMP-specific phosphodiesterase from rat heart by affinity chromatography on immobilized rolipram
Biochem. Biophys. Res. Commun.
138
205-214
1986
Rattus norvegicus
Pooley, L.; Shakur, Y.; Rena, G.; Houslay, M.D.
Intracellular localization of the PDE4A cAMP-specific phosphodiesterase splice variant RD1 (RNPDE4A1A) in stably transfected human thyroid carcinoma FTC cell lines
Biochem. J.
321 (Pt 1)
177-185
1997
Rattus norvegicus (P54748)
Shepherd, M.; McSorley, T.; Olsen, A.E.; Johnston, L.A.; Thomson, N.C.; Baillie, G.S.; Houslay, M.D.; Bolger, G.B.
Molecular cloning and subcellular distribution of the novel PDE4B4 cAMP-specific phosphodiesterase isoform
Biochem. J.
370
429-438
2003
Rattus norvegicus (P14646)
Bian, H.; Zhang, J.; Wu, P.; Lori, A.; Varty, Y.J.; Maywood, T.; Hey, J.A.; Wang, P.
Differential type 4 cAMP-specific phosphodiesterase (PDE4) expression and functional sensitivity to PDE4 inhibitors among rats, monkeys and humans
Biochem. Pharmacol.
68
2229-2236
2004
Rattus norvegicus (P14270), Rattus norvegicus (P14646), Rattus norvegicus (P54748), Homo sapiens (P27815), Homo sapiens (Q07343), Homo sapiens (Q08493), Homo sapiens (Q08499), Homo sapiens
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
36
2968-2976
1997
Rattus norvegicus
Bolger, G.B.; Peden, A.H.; Steele, M.R.; MacKenzie, C.; McEwan, D.G.; Wallace, D.A.; Huston, E.; Baillie, G.S.; Houslay, M.D.
Attenuation of the activity of the cAMP-specific phosphodiesterase PDE4A5 by interaction with the immunophilin XAP2
J. Biol. Chem.
278
33351-33363
2003
Rattus norvegicus
Huston, E.; Gall, I.; Houslay, T.M.; Houslay, M.D.
Helix-1 of the cAMP-specific phosphodiesterase PDE4A1 regulates its phospholipase-D-dependent redistribution in response to release of Ca2+
J. Cell Sci.
119
3799-3810
2006
Rattus norvegicus (P54748)
Macovschi, O.; Prigent, A.F.; Nemoz, G.; Pacheco, H.
Effects of an extract of Ginkgo biloba on the 3',5'-cyclic AMP phosphodiesterase activity of the brain of normal and triethyltin-intoxicated rats
J. Neurochem.
49
107-114
1987
Rattus norvegicus
Waddleton, D.; Wu, W.; Feng, Y.; Thompson, C.; Wu, M.; Zhou, Y.P.; Howard, A.; Thornberry, N.; Li, J.; Mancini, J.A.
Phosphodiesterase 3 and 4 comprise the major cAMP metabolizing enzymes responsible for insulin secretion in INS-1 (832/13) cells and rat islets
Biochem. Pharmacol.
76
884-893
2008
Rattus norvegicus
van Donkelaar, E.L.; Rutten, K.; Blokland, A.; Akkerman, S.; Steinbusch, H.W.; Prickaerts, J.
Phosphodiesterase 2 and 5 inhibition attenuates the object memory deficit induced by acute tryptophan depletion
Eur. J. Pharmacol.
600
98-104
2008
Rattus norvegicus
Tawar, U.; Kotlo, K.; Jain, S.; Shukla, S.; Setty, S.; Danziger, R.S.
Renal phosphodiesterase 4B is activated in the Dahl salt-sensitive rat
Hypertension
51
762-766
2008
Rattus norvegicus
Bopp, C.; Hofer, S.; Busch, C.; Spoehr, F.; Weigand, M.A.; Martin, E.; Klein, A.
Time-limited hyporesponsiveness to inhaled nitric oxide and pulmonary phosphodiesterase activity in endotoxemic rats
J. Surg. Res.
150
66-73
2008
Rattus norvegicus
Galindo-Tovar, A.; Vargas, M.L.; Kaumann, A.J.
Phosphodiesterases PDE3 and PDE4 jointly control the inotropic effects but not chronotropic effects of (-)-CGP12177 despite PDE4-evoked sinoatrial bradycardia in rat atrium
Naunyn Schmiedebergs Arch. Pharmacol.
379
379-384
2009
Rattus norvegicus
Dlaboga, D.; Hajjhussein, H.; ODonnell, J.M.
Chronic haloperidol and clozapine produce different patterns of effects on phosphodiesterase-1B, -4B, and -10A expression in rat striatum
Neuropharmacology
54
745-754
2008
Rattus norvegicus
Miwa, T.; Mori, A.; Nakahara, T.; Ishii, K.
Intravenously administered phosphodiesterase 4 inhibitors dilate retinal blood vessels in rats
Eur. J. Pharmacol.
602
112-116
2009
Rattus norvegicus
Wang, Y.J.; Jiang, Y.L.; Tang, H.F.; Zhao, C.Z.; Chen, J.Q.
Zl-n-91, a selective phosphodiesterase 4 inhibitor, suppresses inflammatory response in a COPD-like rat model
Int. Immunopharmacol.
10
252-258
2010
Rattus norvegicus
Dodge-Kafka, K.L.; Bauman, A.; Mayer, N.; Henson, E.; Heredia, L.; Ahn, J.; McAvoy, T.; Nairn, A.C.; Kapiloff, M.S.
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.
285
11078-11086
2010
Rattus norvegicus
Rock, E.M.; Benzaquen, J.; Limebeer, C.L.; Parker, L.A.
Potential of the rat model of conditioned gaping to detect nausea produced by rolipram, a phosphodiesterase-4 (PDE4) inhibitor
Pharmacol. Biochem. Behav.
91
537-541
2009
Rattus norvegicus
Korkmaz, S.; Maupoil, V.; Sobry, C.; Brunet, C.; Chevalier, S.; Freslon, J.L.
An increased regional blood flow precedes mesenteric inflammation in rats treated by a phosphodiesterase 4 inhibitor
Toxicol. Sci.
107
298-305
2009
Rattus norvegicus
MacKenzie, K.F.; Wallace, D.A.; Hill, E.V.; Anthony, D.F.; Henderson, D.J.; Houslay, D.M.; Arthur, J.S.; Baillie, G.S.; Houslay, M.D.
Phosphorylation of cAMP-specific PDE4A5 (phosphodiesterase-4A5) by MK2 (MAPKAPK2) attenuates its activation through protein kinase A phosphorylation
Biochem. J.
435
755-769
2011
Rattus norvegicus (P54748)
Nunes, A.R.; Batuca, J.R.; Monteiro, E.C.
Acute hypoxia modifies cAMP levels induced by inhibitors of phosphodiesterase-4 in rat carotid bodies, carotid arteries and superior cervical ganglia
Br. J. Pharmacol.
159
353-361
2010
Rattus norvegicus
Cheng, D.; Ren, J.; Gillespie, D.G.; Mi, Z.; Jackson, E.K.
Regulation of 3',5'-cAMP in preglomerular smooth muscle and endothelial cells from genetically hypertensive rats
Hypertension
56
1096-1101
2010
Rattus norvegicus
Kelly, M.P.; Adamowicz, W.; Bove, S.; Hartman, A.J.; Mariga, A.; Pathak, G.; Reinhart, V.; Romegialli, A.; Kleiman, R.J.
Select 3,5-cyclic nucleotide phosphodiesterases exhibit altered expression in the aged rodent brain
Cell. Signal.
26
383-397
2014
Mus musculus, Rattus norvegicus
Cai, Y.; Nagel, D.J.; Zhou, Q.; Cygnar, K.D.; Zhao, H.; Li, F.; Pi, X.; Knight, P.A.; Yan, C.
Role of cAMP-phosphodiesterase 1C signaling in regulating growth factor receptor stability, vascular smooth muscle cell growth, migration, and neointimal hyperplasia
Circ. Res.
116
1120-1132
2015
Homo sapiens, Mus musculus, Rattus norvegicus
Guo, L.; Luo, L.; Ju, R.; Chen, C.; Zhu, L.; Li, J.; Yu, X.; Ye, C.; Zhang, D.
Carboxyamidotriazole A novel inhibitor of both cAMP-phosphodiesterases and cGMP-phosphodiesterases
Eur. J. Pharmacol.
746
14-21
2015
Mus musculus, Rattus norvegicus
Ju-Rong, Y.; Ke-Hong, C.; Kun, H.; Bi-Qiong, F.; Li-Rong, L.; Jian-Guo, Z.; Kai-Long, L.; Ya-Ni, H.
Transcription factor Trps1 promotes tubular cell proliferation after ischemia-reperfusion injury through cAMP-specific 3',5'-cyclic phosphodiesterase 4D and AKT
J. Am. Soc. Nephrol.
28
532-544
2017
Rattus norvegicus (P14270)
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