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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

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Uniprot ID:ICE_DROME
Synonyms:
Caspase
drICE
EC-Numbers:3.4.22.-
Organism:Drosophila melanogaster
Fruit fly
PDB IDs:-

Binding Affinities:

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

12819185
The roles of JNK and apoptotic signaling pathways in PEITC-mediated responses in human HT-29 colon adenocarcinoma cells.. Rong Hu; Bok Ryang Kim; Chi Chen; Vidya Hebbar; A-N Tony Kong (2003) Carcinogenesis display abstract
Phenethyl isothiocyanate (PEITC) is a potential chemopreventive agent that is present naturally in widely consumed vegetables, especially in watercress. It has been extensively investigated for its anticancer activities against lung, forestomach and esophageal tumorigenesis. Here we investigated the pro-apoptotic effect of PEITC in HT-29 human colorectal carcinoma cell line, and the mechanism of apoptosis induced by PEITC. PEITC-induced apoptosis was determined by DNA fragmentation assay and diamidino-2-phenylindole (DAPI) staining technique. To understand the mechanisms of apoptosis induced by PEITC, we studied the role of caspases, mitochondria-cytochrome c release, and mitogen-activated protein kinase (MAPK) signaling pathways involved in PEITC-induced apoptosis in HT-29 cells. Both the caspase-3 and -9 activities were stimulated by PEITC. The release of cytochrome c from the mitochondrial inter-space was time- and dose-dependent, with a maximal release at 50 micro M after 10 h treatment. Three MAPKs [JNK (c-Jun N-terminal kinase), extracellular signal-regulated protein kinase (ERK) and p38 kinase] were activated shortly after PEITC treatment in HT-29 cells. Importantly, the SP600125 compound, an anthrapyrazolone inhibitor of JNK, but not the ERK and p38 inhibitor, suppressed apoptosis induced by PEITC. Similarly, this JNK inhibitor attenuated both cytochrome c release and caspase-3 activation induced by PEITC. In summary, this study shows that PEITC can induce apoptosis in HT-29 cells in a time- and dose-dependent manner via the mitochondria caspase cascade, and the activation of JNK is critical for the initiation of the apoptotic processes. This mechanism of PEITC may play an important role in the killing of cancerous cells and offer a potential mechanism for its anticancer action in vivo.
16613495
Inhibition of UVA-induced c-Jun N-terminal kinase activity results in caspase-dependent apoptosis in human keratinocytes.. Amy L Silvers; Joanne S Finch; G Timothy Bowden (2006) Photochemistry and photobiology display abstract
Inhibition of c-Jun N-terminal kinase (JNK) with the pharmacologic inhibitor SP600125 in UVA-irradiated HaCaT cells and human primary keratinocytes resulted in dramatic phenotypic changes indicative of cell death. These phenotypic changes correlated with caspase 8, 9 and 3 activations as well as cleavage of the caspase substrate polyADP-ribose polymerase (PARP). Morphologic analysis and analysis of sub-G0 DNA content confirmed apoptotic cell death in these keratinocytes after combination treatment. Addition of the general caspase inhibitor zVAD-fmk to combination-treated HaCaT cells was able to completely block caspase activation, PARP cleavage, the increase in sub-G0 DNA content and the classic morphologic features of apoptosis, indicating that this combination treatment resulted in caspase-dependent apoptotic cell death. zVAD-fmk treatment of primary keratinocytes was able to completely inhibit caspase activation and PARP cleavage, reduce morphologic apoptosis at lower concentrations of SP600125 and decrease the sub-G(0) DNA content detected after UVA + SP600125 treatment. However, cell death and a significant amount of debris was still detected after caspase inhibitor treatment, particularly with 125 nM SP600125. At subconfluent conditions and low passage, primary keratinocytes were more sensitive to UVA irradiation alone than HaCaT cells. In conclusion, we have observed that inhibition of UVA-induced JNK activity with the pharmacologic inhibitor SP600125 resulted in caspase-dependent apoptotic cell death in both the immortalized keratinocyte cell line HaCaT and primary keratinocytes. However, the increased sensitivity of primary keratinocytes to experimental stress may have also resulted in direct cellular injury and caspase-independent cell death.