Vorinostat 100mg capsules
Requires a prescription from a doctor or prescriber
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Suspected adverse reactions reported for Vorinostat
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1 branded products available
Therapeutically similar medicines
Similarity is based on WHO Anatomical Therapeutic Chemical (ATC) classification and on a factual NHS dm+d therapeutic-grouping code prefix. Source data: NHS dm+d via TRUD (OGL v3.0), WHO ATC/DDD Index.
Guidelines from the National Institute for Health and Care Excellence
NICE clinical guidance(1)
Source: National Institute for Health and Care Excellence (NICE). Contains public sector information licensed under the Open Government Licence v3.0.
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Codes for healthcare professionals and prescribing systems
These codes are used by healthcare IT systems and prescribers to identify this medicine.
NHS UK identifiers
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SNOMED CT and dm+d codes from NHS TRUD (Technology Reference data Update Distribution), licensed under the Open Government Licence v3.0. BNF code shown is the factual mapping value distributed by NHS Business Services Authority (NHSBSA) in the dm+d supplementary file under OGL v3.0; it is not affiliated with, nor licensed from, the publishers of the British National Formulary. ATC codes from the WHO Collaborating Centre for Drug Statistics Methodology (whocc.no).
Active and completed clinical studies from ClinicalTrials.gov
Source: ClinicalTrials.gov, a database of the U.S. National Library of Medicine (NLM), National Institutes of Health (NIH). Data accessed via ClinicalTrials.gov API v2. Trial information is provided for research purposes and does not constitute medical advice.
Academic studies and reviews for this medicine's active substance
Showing all 28 studies.
Reviews & meta-analyses: 5 · Randomised trials: 2 · 2015–2026
Showing all 28 studies, sorted by most relevant.
Youn H. Kim, M. Bagot, L. Pinter-Brown, et al.
The Lancet. Oncology, 2018
- Antineoplastic Agents, Immunological
- Vorinostat
- Progression-Free Survival
S. DuBois, M. Granger, S. Groshen, et al.
Journal of Clinical Oncology, 2021
- Irinotecan
- Vorinostat
- Antineoplastic Combined Chemotherapy Protocols
M. Sekeres, M. Othus, A. List, et al.
Journal of clinical oncology : official journal of the American Society of Clinical Oncology, 2017
- Lenalidomide
- Vorinostat
- Antimetabolites, Antineoplastic
A. Wawruszak, L. Borkiewicz, Estera Okoń, et al.
Cancers, 2021
Vorinostat (SAHA), an inhibitor of class I and II of histone deacetylases, is the first histone deacetylase inhibitor (HDI) approved for the treatment of cutaneous T-cell lymphoma in 2006. HDIs are promising anticancer agents that inhibit the proliferation of many types of cancer cells including breast carcinoma (BC). BC is a heterogeneous disease with variable biological behavior, morphological features, and response to therapy. Although significant progress in the treatment of BC has been made, high toxicity to normal cells, serious side effects, and the occurrence of multi-drug resistance limit the effective therapy of BC patients. Therefore, new active agents which improve the effectiveness of currently used regimens are highly needed. This manuscript analyzes preclinical and clinical trials data of SAHA, applied individually or in combination with other anticancer agents, considering different histological subtypes of BC.
Abstract licence: CC BY
Silke Geurs, Dorien Clarisse, K. De Bosscher, et al.
Journal of medicinal chemistry, 2023
- Hydroxamic Acids
- Histone Deacetylase Inhibitors
- Vorinostat
C. Rodriguez, Qian Wu, J. Voutsinas, et al.
Clinical Cancer Research, 2019
- Squamous Cell Carcinoma of Head and Neck
- Vorinostat
- Antineoplastic Combined Chemotherapy Protocols
S. Patra, P. Praharaj, D. Klionsky, et al.
Drug discovery today, 2021
- Autophagic Cell Death
- Autophagy
- Neoplasms
Nasreddine El Omari, Asaad Khalid, H. Makeen, et al.
Heliyon, 2024
K. V. Athira, P. Sadanandan, S. Chakravarty
NeuroMolecular Medicine, 2021
- Hydroxamic Acids
- Drug Repositioning
- Vorinostat
J. Gray, A. Saltos, T. Tanvetyanon, et al.
Clinical cancer research : an official journal of the American Association for Cancer Research, 2019
- Vorinostat
- Antineoplastic Combined Chemotherapy Protocols
- Biopsy
Sources: aggregated from Europe PMC (EMBL-EBI), OpenAlex, Crossref, PubMed and other open scholarly databases. Retracted articles are excluded. Study information is provided for research purposes and does not constitute medical advice.
Pharmacology and chemical data from DrugBank
Key facts
Drug status
Approved
Major interactions
None known
Half-life
2 hours
Mechanism
Vorinostat inhibits the enzymatic activity of histone deacetylases HDAC1, HDAC2…
Food interactions
1 warning
Human targets
6 targets
Data: DrugBank · CC BY-NC 4.0
Pharmacokinetics at a glance
Half-life
2 hours
Protein binding
71%
Metabolism
Elimination
1%
Pharmacokinetic data: DrugBank · CC BY-NC 4.0
Known interactions with other medications. Always consult a healthcare professional.
Showing 50 of 985 interactions
How the body processes this drug — absorption, distribution, metabolism, and elimination
Compared to vorinostat, the mean steady state serum exposures in humans of the O-glucuronide of vorinostat and 4-anilino-4-oxobutanoic acid were 4-fold and 13-fold higher, respectively. In vitro studies using human liver microsomes indicate negligible biotransformation by cytochromes P450 (CYP).
Proteins and enzymes this drug interacts with in the body
PMID:16762839 PMID:17704056 PMID:28497810
Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events .
PMID:16762839 PMID:17704056
Histone deacetylases act via the formation of large multiprotein complexes .
PMID:16762839 PMID:17704056
Acts as a component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin .
PMID:16428440 PMID:28977666
As part of the SIN3B complex is recruited downstream of the constitutively active genes transcriptional start sites through interaction with histones and mitigates histone acetylation and RNA polymerase II progression within transcribed regions contributing to the regulation of transcription .
PMID:21041482
Also functions as a deacetylase for non-histone targets, such as NR1D2, RELA, SP1, SP3, STAT3 and TSHZ3 .
PMID:12837748 PMID:16285960 PMID:16478997 PMID:17996965 PMID:19343227
Deacetylates SP proteins, SP1 and SP3, and regulates their function .
PMID:12837748 PMID:16478997
Component of the BRG1-RB1-HDAC1 complex, which negatively regulates the CREST-mediated transcription in resting neurons .
PMID:19081374
Upon calcium stimulation, HDAC1 is released from the complex and CREBBP is recruited, which facilitates transcriptional activation .
PMID:19081374
Deacetylates TSHZ3 and regulates its transcriptional repressor activity .
PMID:19343227
Deacetylates 'Lys-310' in RELA and thereby inhibits the transcriptional activity of NF-kappa-B .
PMID:17000776
Deacetylates NR1D2 and abrogates the effect of KAT5-mediated relieving of NR1D2 transcription repression activity .
PMID:17996965
Component of a RCOR/GFI/KDM1A/HDAC complex that suppresses, via histone deacetylase (HDAC) recruitment, a number of genes implicated in multilineage blood cell development (By similarity). Involved in CIART-mediated transcriptional repression of the circadian transcriptional activator: CLOCK-BMAL1 heterodimer (By similarity). Required for the transcriptional repression of circadian target genes, such as PER1, mediated by the large PER complex or CRY1 through histone deacetylation (By similarity).
In addition to protein deacetylase activity, also has protein-lysine deacylase activity: acts as a protein decrotonylase and delactylase by mediating decrotonylation ((2E)-butenoyl) and delactylation (lactoyl) of histones, respectively PMID:28497810 PMID:35044827
PMID:28497810
Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events (By similarity). Histone deacetylases act via the formation of large multiprotein complexes (By similarity). Forms transcriptional repressor complexes by associating with MAD, SIN3, YY1 and N-COR .
PMID:12724404
Component of a RCOR/GFI/KDM1A/HDAC complex that suppresses, via histone deacetylase (HDAC) recruitment, a number of genes implicated in multilineage blood cell development (By similarity).
Acts as a component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin .
PMID:16428440 PMID:28977666
Component of the SIN3B complex that represses transcription and counteracts the histone acetyltransferase activity of EP300 through the recognition H3K27ac marks by PHF12 and the activity of the histone deacetylase HDAC2 .
PMID:37137925
Also deacetylates non-histone targets: deacetylates TSHZ3, thereby regulating its transcriptional repressor activity .
PMID:19343227
May be involved in the transcriptional repression of circadian target genes, such as PER1, mediated by CRY1 through histone deacetylation (By similarity). Involved in MTA1-mediated transcriptional corepression of TFF1 and CDKN1A .
PMID:21965678
In addition to protein deacetylase activity, also acts as a protein-lysine deacylase by recognizing other acyl groups: catalyzes removal of (2E)-butenoyl (crotonyl), lactoyl (lactyl) and 2-hydroxyisobutanoyl (2-hydroxyisobutyryl) acyl groups from lysine residues, leading to protein decrotonylation, delactylation and de-2-hydroxyisobutyrylation, respectively PMID:28497810 PMID:29192674 PMID:35044827
PMID:21030595 PMID:21444723 PMID:23911289 PMID:25301942 PMID:28167758 PMID:28497810 PMID:32404892 PMID:22230954
Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events .
PMID:23911289
Histone deacetylases act via the formation of large multiprotein complexes, such as N-Cor repressor complex, which activate the histone deacetylase activity .
PMID:23911289 PMID:22230954
Participates in the BCL6 transcriptional repressor activity by deacetylating the H3 'Lys-27' (H3K27) on enhancer elements, antagonizing EP300 acetyltransferase activity and repressing proximal gene expression .
PMID:23911289
Acts as a molecular chaperone for shuttling phosphorylated NR2C1 to PML bodies for sumoylation (By similarity). Contributes, together with XBP1 isoform 1, to the activation of NFE2L2-mediated HMOX1 transcription factor gene expression in a PI(3)K/mTORC2/Akt-dependent signaling pathway leading to endothelial cell (EC) survival under disturbed flow/oxidative stress .
PMID:25190803
Regulates both the transcriptional activation and repression phases of the circadian clock in a deacetylase activity-independent manner (By similarity). During the activation phase, promotes the accumulation of ubiquitinated BMAL1 at the E-boxes and during the repression phase, blocks FBXL3-mediated CRY1/2 ubiquitination and promotes the interaction of CRY1 and BMAL1 (By similarity).
The NCOR1-HDAC3 complex regulates the circadian expression of the core clock gene BMAL1 and the genes involved in lipid metabolism in the liver (By similarity). Also functions as a deacetylase for non-histone targets, such as KAT5, MEF2D, MAPK14, RARA and STAT3 .
PMID:15653507 PMID:21030595 PMID:21444723 PMID:25301942 PMID:28167758
Serves as a corepressor of RARA, mediating its deacetylation and repression, leading to inhibition of RARE DNA element binding .
PMID:28167758
In association with RARA, plays a role in the repression of microRNA-10a and thereby in the inflammatory response .
PMID:28167758
In addition to protein deacetylase activity, also acts as a protein-lysine deacylase by recognizing other acyl groups: catalyzes removal of (2E)-butenoyl (crotonyl), lactoyl (lactyl) and 2-hydroxyisobutanoyl (2-hydroxyisobutyryl) acyl groups from lysine residues, leading to protein decrotonylation, delactylation and de-2-hydroxyisobutyrylation, respectively .
PMID:28497810 PMID:29192674 PMID:34608293 PMID:35044827
Catalyzes decrotonylation of MAPRE1/EB1 .
PMID:34608293
Mediates delactylation NBN/NBS1, thereby inhibiting DNA double-strand breaks (DSBs) via homologous recombination (HR) PMID:38961290
PMID:12024216 PMID:18606987 PMID:20308065 PMID:24882211 PMID:26246421 PMID:30538141 PMID:31857589 PMID:30770470 PMID:38534334 PMID:39567688
Plays a central role in microtubule-dependent cell motility by mediating deacetylation of tubulin .
PMID:12024216 PMID:20308065 PMID:26246421
Required for cilia disassembly via deacetylation of alpha-tubulin .
PMID:17604723 PMID:26246421
Alpha-tubulin deacetylation results in destabilization of dynamic microtubules (By similarity). Promotes deacetylation of CTTN, leading to actin polymerization, promotion of autophagosome-lysosome fusion and completion of autophagy .
PMID:30538141
Deacetylates SQSTM1 .
PMID:31857589
Deacetylates peroxiredoxins PRDX1 and PRDX2, decreasing their reducing activity .
PMID:18606987
Deacetylates antiviral protein RIGI in the presence of viral mRNAs which is required for viral RNA detection by RIGI (By similarity). Sequentially deacetylates and polyubiquitinates DNA mismatch repair protein MSH2 which leads to MSH2 degradation, reducing cellular sensitivity to DNA-damaging agents and decreasing cellular DNA mismatch repair activities .
PMID:24882211
Deacetylates DNA mismatch repair protein MLH1 which prevents recruitment of the MutL alpha complex (formed by the MLH1-PMS2 heterodimer) to the MutS alpha complex (formed by the MSH2-MSH6 heterodimer), leading to tolerance of DNA damage .
PMID:30770470
Deacetylates RHOT1/MIRO1 which blocks mitochondrial transport and mediates axon growth inhibition (By similarity).
Deacetylates transcription factor SP1 which leads to increased expression of ENG, positively regulating angiogenesis .
PMID:38534334
Deacetylates KHDRBS1/SAM68 which regulates alternative splicing by inhibiting the inclusion of CD44 alternate exons .
PMID:26080397
Acts as a valine sensor by binding to valine through the primate-specific SE14 repeat region .
PMID:39567688
In valine deprivation conditions, translocates from the cytoplasm to the nucleus where it deacetylates TET2 which promotes TET2-dependent DNA demethylation, leading to DNA damage .
PMID:39567688
Promotes odontoblast differentiation following IPO7-mediated nuclear import and subsequent repression of RUNX2 expression (By similarity). In addition to its protein deacetylase activity, plays a key role in the degradation of misfolded proteins: when misfolded proteins are too abundant to be degraded by the chaperone refolding system and the ubiquitin-proteasome, mediates the transport of misfolded proteins to a cytoplasmic juxtanuclear structure called aggresome .
PMID:17846173
Probably acts as an adapter that recognizes polyubiquitinated misfolded proteins and targets them to the aggresome, facilitating their clearance by autophagy .
PMID:17846173
Involved in the MTA1-mediated epigenetic regulation of ESR1 expression in breast cancer PMID:24413532
PMID:10748112 PMID:10922473 PMID:10926844 PMID:14701748 PMID:28497810
Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events .
PMID:10748112 PMID:10922473 PMID:10926844 PMID:14701748
Histone deacetylases act via the formation of large multiprotein complexes .
PMID:10748112 PMID:10922473 PMID:10926844 PMID:14701748
Also involved in the deacetylation of cohesin complex protein SMC3 regulating release of cohesin complexes from chromatin .
PMID:22885700
May play a role in smooth muscle cell contractility .
PMID:15772115
In addition to protein deacetylase activity, also has protein-lysine deacylase activity: acts as a protein decrotonylase by mediating decrotonylation ((2E)-butenoyl) of histones PMID:28497810
ATC L01XH01
Chemical identifiers
CAS, UNII, InChI Key and database cross-references
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Chemical identifiers
CAS, UNII, InChI Key and database cross-references
Linked compound data from DrugBank Open Data (CC BY-NC 4.0)
Vorinostat
Additional database identifiers
Drugs Product Database (DPD)
20475
ChemSpider
5120
BindingDB
19149
PDB
SHH
ZINC
ZINC000001543873
HUGO Gene Nomenclature Committee (HGNC)
HGNC:4852
GenAtlas
HDAC1
GeneCards
HDAC1
GenBank Gene Database
U50079
GenBank Protein Database
1277084
Guide to Pharmacology
2658
UniProt Accession
HDAC1_HUMAN
HUGO Gene Nomenclature Committee (HGNC)
HGNC:4853
GenAtlas
HDAC2
GeneCards
HDAC2
GenBank Gene Database
U31814
GenBank Protein Database
1667394
Guide to Pharmacology
2616
UniProt Accession
HDAC2_HUMAN
HUGO Gene Nomenclature Committee (HGNC)
HGNC:4854
GenAtlas
HDAC3
GeneCards
HDAC3
GenBank Gene Database
U66914
GenBank Protein Database
2326173
Guide to Pharmacology
2617
UniProt Accession
HDAC3_HUMAN
HUGO Gene Nomenclature Committee (HGNC)
HGNC:14064
GenAtlas
HDAC6
GeneCards
HDAC6
GenBank Gene Database
AF132609
GenBank Protein Database
4754911
Guide to Pharmacology
2618
UniProt Accession
HDAC6_HUMAN
HUGO Gene Nomenclature Committee (HGNC)
HGNC:13315
GenAtlas
HDAC8
GeneCards
HDAC8
GenBank Gene Database
AF230097
GenBank Protein Database
8118721
Guide to Pharmacology
2619
UniProt Accession
HDAC8_HUMAN
HUGO Gene Nomenclature Committee (HGNC)
HGNC:4852
GenAtlas
HDAC1
GeneCards
HDAC1
GenBank Gene Database
U50079
GenBank Protein Database
1277084
Guide to Pharmacology
2658
UniProt Accession
HDAC1_HUMAN
HUGO Gene Nomenclature Committee (HGNC)
HGNC:19086
GeneCards
HDAC11
Guide to Pharmacology
2615
UniProt Accession
HDA11_HUMAN
HUGO Gene Nomenclature Committee (HGNC)
HGNC:4853
GenAtlas
HDAC2
GeneCards
HDAC2
GenBank Gene Database
U31814
GenBank Protein Database
1667394
Guide to Pharmacology
2616
UniProt Accession
HDAC2_HUMAN
HUGO Gene Nomenclature Committee (HGNC)
HGNC:4854
GenAtlas
HDAC3
GeneCards
HDAC3
GenBank Gene Database
U66914
GenBank Protein Database
2326173
Guide to Pharmacology
2617
UniProt Accession
HDAC3_HUMAN
HUGO Gene Nomenclature Committee (HGNC)
HGNC:14063
GenAtlas
HDAC4
GeneCards
HDAC4
GenBank Gene Database
AF132607
Guide to Pharmacology
2659
UniProt Accession
HDAC4_HUMAN
HUGO Gene Nomenclature Committee (HGNC)
HGNC:14068
GenAtlas
HDAC5
GeneCards
HDAC5
GenBank Gene Database
BK000028
Guide to Pharmacology
2660
UniProt Accession
HDAC5_HUMAN
HUGO Gene Nomenclature Committee (HGNC)
HGNC:14067
GenAtlas
HDAC7
GeneCards
HDAC7
GenBank Gene Database
BC020505
Guide to Pharmacology
2661
UniProt Accession
HDAC7_HUMAN
HUGO Gene Nomenclature Committee (HGNC)
HGNC:13315
GenAtlas
HDAC8
GeneCards
HDAC8
GenBank Gene Database
AF230097
GenBank Protein Database
8118721
Guide to Pharmacology
2619
UniProt Accession
HDAC8_HUMAN
HUGO Gene Nomenclature Committee (HGNC)
HGNC:14065
GenAtlas
HDAC9
GeneCards
HDAC9
GenBank Gene Database
AY032737
GenBank Protein Database
15590680
Guide to Pharmacology
2620
UniProt Accession
HDAC9_HUMAN
HUGO Gene Nomenclature Committee (HGNC)
HGNC:18128
GenAtlas
HDAC10
GeneCards
HDAC10
GenBank Gene Database
AL512711
Guide to Pharmacology
2614
UniProt Accession
HDA10_HUMAN
HUGO Gene Nomenclature Committee (HGNC)
HGNC:14064
GenAtlas
HDAC6
GeneCards
HDAC6
GenBank Gene Database
AF132609
GenBank Protein Database
4754911
Guide to Pharmacology
2618
UniProt Accession
HDAC6_HUMAN
DrugBank citations
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Structured knowledge from the free knowledge base
ATC classifications (Wikidata)
Linked open data from Wikidata (Q905901), a free and open knowledge base operated by the Wikimedia Foundation. Data is available under the Creative Commons CC0 1.0 Public Domain Dedication. WHO INN from the World Health Organization.