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Drug-Target Interaction

Drug

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PubChem ID:5311
Structure:
Synonyms:
149647-78-9
1zz1
4-Dimethylamino-N-(6-hydroxycarbamoylhexyl)benzamide
AC-1923
AC1L1K2K
AIDS-186714
AIDS186714
BRD-K81418486-001-10-3
C111237
CCRIS 8456
CHEBI:45716
CHEMBL98
D06320
DB02546
EC-000.2057
FT-0082592
HMS2219L20
HMS3264D20
LS-186548
LS-186997
LS-187780
M344
M344 compound
MK-0683
MK0683
MLS001065855
N'-hydroxy-N-phenyloctanediamide
N-Hydroxy-7-(4-dimethylaminobenzoyl)aminoheptanamide
N-Hydroxy-N'-phenyl octanediamide
N-hydroxy-N'-phenyl-octane-1,8-diotic acid diamide
N-hydroxy-N'-phenyloctanediamide
N-Hyrdroxy-N'-phenyloctanediamide
N1-hydroxy-N8-phenyloctanediamide
NCGC00168085-01
NCGC00168085-02
NCGC00168085-03
NCGC00168085-04
nchembio.275-comp2
nchembio.313-comp1
nchembio815-comp18
NHNPODA
NSC-701852
NSC701852
Octanediamide, N-hydroxy-N'-phenyl-
OCTANEDIOIC ACID HYDROXYAMIDE PHENYLAMIDE
P111011
S1047_Selleck
SAHA
SAHA cpd
SAHA, Suberoylanilide hydroxamic acid
SHH
SKI390
SMR000486344
Suberanilohydroxamic acid
Suberoylanilide hydroxamic acid
Suberoylanilide hydroxamic acid (SAHA)
SW-064652
UNII-58IFB293JI
Vorinostat
Vorinostat (JAN/USAN)
Vorinostat (USAN)
Vorinostat MSD
Vorinostat [USAN]
Vorinostat-Supplied by Selleck Chemicals
WIN64652
ZINC01543873
Zolinza
Zolinza (TN)
Zolinza, MK-0683, SAHA
ATC-Codes:

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:

18005386
Synergistic interaction of the histone deacetylase inhibitor SAHA with the proteasome inhibitor bortezomib in mantle cell lymphoma.. Ulrike Heider; Ivana von Metzler; Martin Kaiser; Marleen Rosche; Jan Sterz; Susanne Rötzer; Jessica Rademacher; Christian Jakob; Claudia Fleissner; Ulrike Kuckelkorn; Peter-Michael Kloetzel; Orhan Sezer (2008) European journal of haematology display abstract
OBJECTIVES: Mantle cell lymphoma (MCL) is an incurable B cell lymphoma, and novel treatment strategies are urgently needed. We evaluated the effects of combined treatment with the proteasome inhibitor bortezomib and the histone deacetylase inhibitor (HDACi) suberoylanilide hydroxamic acid (SAHA) on MCL. Bortezomib acts by targeting the proteasome, and--among other mechanisms--results in a reduced nuclear factor-kappa B (NF-kappaB) activity. HDACi promote histone acetylation, and also interfere with NF-kappaB signaling. METHODS: Human MCL cell lines (JeKo-1, Granta-519 and Hbl-2) were exposed to bortezomib and/or SAHA. Cell viability and apoptosis were quantified by the MTT and annexin-V assay, respectively. Reactive oxygen species (ROS) were analyzed using the fluorophore H2DCFDA. In addition, activated caspases, proteasome- and NF-kappaB activity were quantified. RESULTS: Combined incubation with bortezomib and SAHA resulted in synergistic cytotoxic effects, as indicated by combination index values
18025281
Histone deacetylase inhibitor suberoylanilide hydroxamic acid induces apoptosis through both mitochondrial and Fas (Cd95) signaling in head and neck squamous carcinoma cells.. Ann M Gillenwater; Meiling Zhong; Reuben Lotan (2007) Molecular cancer therapeutics display abstract
Alterations in histone acetylation status have been implicated in carcinogenesis. Histone deacetylase inhibitors, such as suberoylanilide hydroxamic acid (SAHA), can potentially reactivate aberrantly silenced genes by restoring histone acetylation and allowing gene transcription. However, the mechanisms underlying the effects of SAHA on cell growth, differentiation, and death remain unclear. In this study, we assessed the activity of SAHA in modulating cell growth and apoptosis in head and neck squamous cell carcinoma (HNSCC) cells compared with premalignant leukoplakia and normal oral cells. SAHA induced growth inhibition, cell cycle changes, and apoptosis in HNSCC cell lines but had limited effects on premalignant and normal cells. Although SAHA triggered the mitochondrial pathway of apoptosis, including cytochrome c release, caspase-3 and caspase-9 activation, and poly(ADP-ribose) polymerase cleavage in HNSCC cells, specific inhibition of caspase-9 only partially blocked the induction of apoptosis induction. SAHA also activated the extrinsic apoptosis pathway, including increased Fas and Fas ligand (FasL) expression, activation of caspase-8, and cleavage of Bid. Interfering with Fas signaling blocked apoptosis induction and blunted growth inhibition by SAHA. Our results show for the first time that SAHA induces apoptosis in HNSCC cells through activation of the Fas/FasL death pathway in addition to the intrinsic mitochondrial pathway although having comparatively little activity against precancerous and normal oral cells with intrinsic Fas and FasL expression.
18549473
Complex molecular mechanisms cooperate to mediate histone deacetylase inhibitors anti-tumour activity in neuroblastoma cells.. Annick Mühlethaler-Mottet; Roland Meier; Marjorie Flahaut; Katia Balmas Bourloud; Katya Nardou; Jean-Marc Joseph; Nicole Gross (2008) Molecular cancer display abstract
BACKGROUND: Histone deacetylase inhibitors (HDACi) are a new class of promising anti-tumour agent inhibiting cell proliferation and survival in tumour cells with very low toxicity toward normal cells. Neuroblastoma (NB) is the second most common solid tumour in children still associated with poor outcome in higher stages and, thus NB strongly requires novel treatment modalities. RESULTS: We show here that the HDACi Sodium Butyrate (NaB), suberoylanilide hydroxamic acid (SAHA) and Trichostatin A (TSA) strongly reduce NB cells viability. The anti-tumour activity of these HDACi involved the induction of cell cycle arrest in the G2/M phase, followed by the activation of the intrinsic apoptotic pathway, via the activation of the caspases cascade. Moreover, HDACi mediated the activation of the pro-apoptotic proteins Bid and BimEL and the inactivation of the anti-apoptotic proteins XIAP, Bcl-xL, RIP and survivin, that further enhanced the apoptotic signal. Interestingly, the activity of these apoptosis regulators was modulated by several different mechanisms, either by caspases dependent proteolytic cleavage or by degradation via the proteasome pathway. In addition, HDACi strongly impaired the hypoxia-induced secretion of VEGF by NB cells. CONCLUSION: HDACi are therefore interesting new anti-tumour agents for targeting highly malignant tumours such as NB, as these agents display a strong toxicity toward aggressive NB cells and they may possibly reduce angiogenesis by decreasing VEGF production by NB cells.