Home
Drugs
Targets
Pathways
Ontologies
Cyp450s
Adv.search
Help/FAQ

Drug-Target Interaction

Drug

show drug details
PubChem ID:8515
Structure:
Synonyms:
"insolution™ jnk inhibitor ii"
1,9-Pyrazoloanthrone
129-56-6
14,15-diazatetracyclo[7.6.1.0^{2,7}.0^{13,16}]hexadeca-1(15),2(7),3,5,9,11
1pmv
2,6-DIHYDROANTHRA/1,9-CD/PYRAZOL-6-ONE
2H-Dibenzo[cd,g]indazol-6-one
AIDS-220090
AIDS220090
ANTHRA(1,9-cd)PYRAZOL-6(2H)-ONE
Anthra-1,9-pyrazol-6-none
Anthrapyrazolone
Anthra[1,9-cd]pyrazol-6(2H)-one
Anthra[1,9-cd]pyrazol-6(2H)-one & Z-100
BAS 00719687
BCBcMAP01_000053
Bio1_000335
Bio1_000824
Bio1_001313
Bio2_000373
Bio2_000853
BiomolKI2_000072
BiomolKI_000068
BRN 0746890
BSPBio_001066
C.I. 70300
C432165
CBiol_002049
dibenzo[cd,g]indazol-6(2H)-one
dihydroanthrapyrazole compound 4
EINECS 204-955-6
EU-0100473
HSCI1_000136
IDI1_002128
InSolution™ JNK Inhibitor II
JNK Inhibitor II
K00068
KBio2_000406
KBio2_002974
KBio2_005542
KBio3_000771
KBio3_000772
KBioGR_000406
KBioSS_000406
Lopac-S-5567
Lopac0_000473
LS-20607
MLS002153267
NCGC00015958-01
NCGC00025186-01
NCGC00025186-02
NCGC00025186-03
NCGC00025186-04
NCGC00025186-05
NSC 75890
NSC75890
Pyrazolanthrone
Pyrazoleanthrone
QTL1_000077
RH 00237
S5567_SIGMA
SAPK Inhibitor II
SBB000595
SMP2_000240
SMR000015440
SP 600125
SP 600125 & Z-100
SP600125
SR-01000637108-1
TL8000704
Tocris-1496
WLN: T C6665 1A P IV OMNJ
ZINC04335977

Target

show target details
Uniprot ID:Q9Y354_HUMAN
Synonyms:
Matrix metalloproteinase 9
EC-Numbers:3.4.24.35
Organism:Homo sapiens
Human
PDB IDs:-

Binding Affinities:

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

References:

12031798
An inhibitor of c-jun aminoterminal kinase (SP600125) represses c-Jun activation, DNA-binding and PMA-inducible 92-kDa type IV collagenase expression.. M Shin; C Yan; D Boyd (2002) Biochimica et biophysica acta display abstract
The 92-kDa type IV collagenase (MMP-9) contributes to tumor invasion and metastases and strategies to down-regulate its expression could ultimately be of clinical utility. Although the expression of this collagenase is regulated by numerous growth factors, the signaling pathways that transduce these signals are fewer in number and therefore represent pharmacological targets. In this regard, we previously reported that MMP-9 expression was regulated by the c-jun amino terminal kinase (JNK) signaling cascade. Therefore, we undertook a study to determine the efficacy of a novel compound (SP600125), which binds to the ATP binding site of all known JNKs, in repressing MMP-9 expression. In OVCAR-3 cells, SP600125 inhibited the PMA-dependent secretion of MMP-9 in a time-dependent manner and over a dose range that blocked c-Jun phosphorylation and AP-1 binding. SP600125 repressed the activity of a PMA-stimulated MMP-9 promoter-driven luciferase reporter, suggesting that diminished secretion of this collagenase reflected reduced transcription. Further, the activity of a GAL4-driven reporter in PMA-treated cells, co-transfected with an expression construct encoding the trans-activation domain of c-Jun fused to the DNA binding domain of GAL4, was repressed by SP600125. These findings indicate the efficacy of SP600125 in inhibiting c-Jun activation, DNA-binding and the PMA-dependent induction of MMP-9 expression.