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Drug-Target Interaction

Drug

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PubChem ID:3758
Structure:
Synonyms:
1 Methyl 3 isobutylxanthine
1-methyl-3-(2-methylpropyl)-1,3,7-trihydropurine-2,6-dione
1-methyl-3-(2-methylpropyl)-3,7-dihydro-1H-purine-2,6-dione
1-methyl-3-(2-methylpropyl)-3,9-dihydro-1H-purine-2,6-dione
1-methyl-3-(2-methylpropyl)-7H-purine-2,6-dione
1-methyl-3-(propan-2-yl)-3,7-dihydro-1H-purine-2,6-dione
1-methyl-3-(propan-2-yl)-3,9-dihydro-1H-purine-2,6-dione
1-METHYL-3-ISOBUTYLXANTHINE
1H-Purine-2,6-dione, 3,7-dihydro-1-methyl-3-(2-methylpropyl)-
1H-Purine-2,6-dione, 3,7-dihydro-1-methyl-3-(2-methylpropyl)-;
1zkl
1zkn
28822-58-4
2hd1
2r8q
3 Isobutyl 1 methylxanthine
3,7-Dihydro-1-methyl-3-(2-methylpropyl)-1H-purine-2,6-dione
3,7-Dihydro-3-isobutyl-1-methyl-1H-purine-2,6-dione
3-ISOBUTHYL-1-METHYLXANTHINE
3-Isobutyl 1-methylxanthine
3-Isobutyl-1-methyl-2,6(1H,3H)-purinedione
3-isobutyl-1-methyl-3,7-dihydro-1H-purine-2,6-dione
3-isobutyl-1-methyl-3,9-dihydro-1H-purine-2,6-dione
3-isobutyl-1-methyl-7H-xanthine
3-isobutyl-1-methyl-9H-xanthine
3-Isobutyl-1-methylxanthine
3-Isobutyl-1-methyxanthine
3ecn
AC1L1GNB
AC1Q1PM4
AIDS-008701
AIDS008701
AKOS003390599
BCBcMAP01_000110
Bio-0605
Bio1_000456
Bio1_000945
Bio1_001434
Bio2_000407
Bio2_000887
BRD-K94979336-001-06-9
BSPBio_001153
BSPBio_003558
C10H14N4O2
C13708
CCG-39513
CCG-39624
CCRIS 4290
CHEBI:34795
CHEBI:43253
CHEMBL275084
cMAP_000087
CPD-5461
D015056
DB07954
DivK1c_000922
EINECS 249-259-3
EU-0100642
HMS1362I15
HMS1792I15
HMS1990I15
HMS2090J10
HMS2231C11
HMS3262A05
HMS502O04
HSCI1_000261
I 5879
I5879_SIGMA
I7018_SIGMA
IBM
IBMX
IDI1_000922
IDI1_002162
IN1293
Isobutylmethylxanthine
Isobutyltheophylline
KBio1_000922
KBio2_000493
KBio2_002566
KBio2_003061
KBio2_005134
KBio2_005629
KBio2_007702
KBio3_000905
KBio3_000906
KBio3_002878
KBio3_003044
KBioGR_000493
KBioGR_001344
KBioGR_002566
KBioSS_000493
KBioSS_002575
L001156
Lopac-I-5879
Lopac0_000642
LS-162537
Methyl-isobutylxanthine
methylisobutylxanthine
MLS001056732
MLS001066424
MolMap_000030
MolPort-001-737-339
MolPort-001-792-510
NCGC00015559-01
NCGC00015559-02
NCGC00015559-03
NCGC00015559-04
NCGC00015559-05
NCGC00015559-06
NCGC00015559-07
NCGC00015559-08
NCGC00015559-09
NCGC00015559-10
NCGC00015559-11
NCGC00094009-01
NCGC00094009-02
NCGC00094009-03
NCGC00094009-04
NCGC00094009-05
NCGC00094009-06
NINDS_000922
NSC 165960
NSC165960
Oprea1_135287
Oprea1_228781
PDSP1_000324
PDSP2_000322
SMR000326697
SPBio_001690
SPBio_001810
SPECTRUM1505298
SPECTRUM2300204
Spectrum2_001705
Spectrum2_001735
Spectrum3_001958
Spectrum4_001052
Spectrum5_001856
ST055758
STOCK1N-14620
STOCK1N-23901
WLN: T56 BM DN FNVNVJ F1Y1&1 H1
Xanthine, 3-isobutyl-1-methyl-
ZINC03861807
[Eur J Pharmacol 170: 35 (1989)]

Target

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Uniprot ID:PDE10_RAT
Synonyms:
cAMP and cAMP-inhibited cGMP 3',5'-cyclic phosphodiesterase 10A
EC-Numbers:3.1.4.17
3.1.4.35
Organism:Rat
Rattus norvegicus
PDB IDs:2O8H 2OVV 2OVY 3HQW 3HQY 3HQZ 3HR1
Structure:
3HR1

Binding Affinities:

Ki: Kd:Ic 50:Ec50/Ic50:
----

References:

2423089
Selective inhibition of cyclic nucleotide phosphodiesterases of human, bovine and rat aorta.. C Lugnier; P Schoeffter; A Le Bec; E Strouthou; J C Stoclet (1986) Biochemical pharmacology display abstract
Cyclic nucleotide phosphodiesterase (PDE) activity from the 105,000 g supernatant of human, bovine and rat aorta smooth muscle cells was resolved by DEAE-trisacryl chromatography into three major forms showing similar properties in each species. In addition to the two PDE forms previously characterized in vascular tissues (a cAMP-PDE and a calmodulin-dependent PDE), a cGMP-PDE, insensitive to calmodulin, was isolated and characterized in the aorta of the three species. Each isolated PDE form was differently inhibited by various chemical compounds, and these compounds produced effects on cyclic nucleotide levels in isolated rat aorta which could be expected from their inhibitory effect on isolated PDE forms. At concentrations non-selectively inhibiting the three isolated PDE forms (including the calmodulin-dependent one), IBMX (3-isobutyl-1-methylxanthine) and trequinsin markedly and dose-dependently increased both cAMP and cGMP aorta levels (up to 7-fold, in presence of 500 microM IBMX). By contrast selective inhibitors of cGMP-PDE or cAMP-PDE could only induce a moderate elevation (by 1.5-3-fold) in cGMP or cAMP levels, respectively. In the case of M&B 22,948, a highly specific and potent inhibitor of cGMP-PDE, a concentration-dependent increase in tissue cGMP levels was produced by concentrations (in the microM range) active in inhibiting the isolated enzyme. In the case of selective cAMP-PDE inhibitors (rolipram and Ro 20-1724), however, a significant increase in aorta cAMP content was induced only in the presence of drug concentrations which were much higher (200 and 500 microM, respectively) than those inhibiting the isolated enzyme (IC50:5 and 18 microM, respectively). Inhibitors of both cGMP-PDE and cAMP-PDE (dipyridamole, cilostamide and its derivative AAL 05) produced the same moderate effects as did the combination of a selective cGMP-PDE inhibitor and a selective cAMP-PDE inhibitor on the levels of both cGMP and cAMP. These results show that the three forms of PDE isolated from aortic smooth muscle retain properties that they exhibit in the tissue and which are similar in the three species examined, including man. They suggest that each form participates in a specific manner to the regulation of cAMP and cGMP concentrations in aorta smooth muscle cells.