Cantharidin 0.7% collodion
Prescription only
Requires a prescription from a doctor or prescriber
Active ingredients:
Cantharidin
No active safety alerts
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Data from the MHRA Yellow Card scheme. A reported reaction does not necessarily mean the medicine caused it. Contains public sector information licensed under the Open Government Licence v3.0.
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2 branded products available
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Supply & safety information
Official UK regulator monitoring and safety alerts
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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
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.
Active and completed clinical studies from ClinicalTrials.gov
Searching UK clinical trials...
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 the 50 most relevant studies.
Reviews & meta-analyses: 25 · Randomised trials: 2 · 1929–2025
Showing the 50 most relevant studies, sorted by most relevant.
Efficacy and Safety of Topical Cantharidin Treatment for Molluscum Contagiosum and Warts: A Systematic Review (opens in a new tab)
Paras P. Vakharia, R. Chopra, Nanette B. Silverberg, et al.
American Journal of Clinical Dermatology, 2018
Systematic review
Cited by 43- Administration, Cutaneous
- Blister
- Cantharidin
Off-label use of sodium cantharidinate and vitamin B6 injection in cancer: a protocol for a systematic review and meta-analysis. (opens in a new tab)
Jin W, Zhang Y, Pang S, et al.
2025
Systematic review
- Neoplasms
- Cantharidin
- Vitamin B 6
Dramatic rate accelerations of Diels-Alder reactions in 5 M lithium perchlorate-diethyl ether: the cantharidin problem reexamined (opens in a new tab)
Paul A. Grieco, Joseph J. Nunes, Micheal D. Gaul
Journal of the American Chemical Society, 1990
Highly cited for its field
Cited by 325Cantharidin, another natural toxin that inhibits the activity of serine/threonine protein phosphatases types 1 and 2A (opens in a new tab)
Richard E. Honkanen
FEBS Letters, 1993
Cited by 287
- Cantharidin
- Cations, Divalent
- Cattle
Cantharidin-binding protein: identification as protein phosphatase 2A. (opens in a new tab)
Y M Li, John E. Casida
Proceedings of the National Academy of Sciences, 1992
Cited by 257
- Amino Acid Sequence
- Cantharidin
- Carrier Proteins
Effect of salicylic acid, methyl jasmonate, ethephon and cantharidin on anthraquinone production by Rubia cordifolia callus cultures transformed with the rolB and rolC genes (opens in a new tab)
Victor P. Bulgakov, G. K. Tchernoded, Natalia P. Mischenko, et al.
Journal of Biotechnology, 2002
Cited by 222
- Acetates
- Anthraquinones
- beta-Glucosidase
Cantharidin Revisited (opens in a new tab)
Lisa Moed, Tor Shwayder, Mary Wu Chang
Archives of Dermatology, 2001
Cited by 209
- Medicine, Traditional
- Coleoptera
- Cantharidin
Safety and efficacy of topical cantharidin for the treatment of pediatric molluscum contagiosum: a prospective, randomized, double‐blind, placebo‐controlled pilot trial (opens in a new tab)
A. Guzman, David O. Schairer, Jessica Garelik, et al.
International Journal of Dermatology, 2018
Randomised trial
Cited by 24Synthesen in der hydro‐aromatischen Reihe, II. Mitteilung: Über Cantharidin (opens in a new tab)
Otto Diels, Kurt Alder
Berichte der deutschen chemischen Gesellschaft (A and B Series), 1929
Highly cited for its field
Cited by 192Cantharidin is Superior to Trichloroacetic Acid for the Treatment of Non-mucosal Genital Warts: A Pilot Randomized Controlled Trial (opens in a new tab)
Maurice-Andre Recanati, Katherine J Kramer, J. J. Maggio, et al.
Clinical and experimental obstetrics & gynecology, 2018
Randomised trial
Cited by 15Sources: 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
Not available
Mechanism
Cantharidin is specifically absorbed by lipids in the membrane of epidermal kera…
Food interactions
None known
Human targets
2 targets
Data: DrugBank · CC BY-NC 4.0
Pharmacokinetics at a glance
Absorption
Cantharidin is absorbed from the gastrointestinal tract, and, to a limited extent from the skin as well.
[L2648]
Little…
[L2648]
Little…
Half-life
Little pharmacodynamic and pharmacokinetic data regarding cantharidin in the human body currently exists; recruitment for First-Time-In-Human…
Protein binding
Little pharmacodynamic and pharmacokinetic data regarding cantharidin in the human body currently exists; recruitment for First-Time-In-Human…
Volume of distribution
After oral or IP injection of (3)H-labeled cantharidin, high levels of radioactivity were distributed to and exhibited in the bile, kidney, liver,…
Metabolism
Little pharmacodynamic and pharmacokinetic data regarding cantharidin in the human body currently exists; recruitment for First-Time-In-Human…
Elimination
It has been observed that absorbed cantharidin is excreted by the kidney.
[L2648]
Little…
[L2648]
Little…
Clearance
Little pharmacodynamic and pharmacokinetic data regarding cantharidin in the human body currently exists; recruitment for First-Time-In-Human…
Pharmacokinetic data: DrugBank · CC BY-NC 4.0
Status:
Approved
Small molecule
About this compound
Cantharidin is a naturally occurring odorless, colorless fatty substance of the terpenoid class that is produced as an oral fluid in the alimentary canal of the male blister beetle.[A32891][A32892] For its natural purpose, the male blister beetle secretes and presents the cantharidin to a female beetle as a copulatory gift during mating. Post-copulation, the female beetle places the cantharidin over her eggs as protection against any potential predators.[A32891][A32892]
Topical cantharidin products do not necessarily demonstrate any particular better effectiveness at treating topical skin conditions like warts than other commonly available vesicant and/or keratolytics although various studies have also investigated the possibility of using cantharidin as an inflammatory model or in cancer treatment.[A32892] Regardless, the ongoing lack of FDA approval is likely related to certain toxic effects that were observed following oral ingestion, which include ulceration of the gastrointestinal and genitourinary tracts, along with electrolyte and renal function disturbance in humans and animals [A32891].
Available synthetically since the 1950s, topical applications of cantharidin have been used predominantly as a treatment for cutaneous warts since that time. [A32891][A32892] In 1962 however, marketers of cantharidin failed to produce sufficient efficacy data, resulting in the FDA revision of approval of cantharidin.[A32892] Nevertheless, it gained its first FDA approval on Jul 21, 2023, under the brand name YCANTH™ by Verrica Pharmaceuticals for the treatment of molluscum contagiosum in adult and pediatric patients.[L47496] The approval was based on positive results from 2 phase III trials, CAMP-1 and CAMP-2, where 46% and 52% of patients treated with cantharidin achieved complete molluscum clearance, respectively.[L47496]
Topical cantharidin products do not necessarily demonstrate any particular better effectiveness at treating topical skin conditions like warts than other commonly available vesicant and/or keratolytics although various studies have also investigated the possibility of using cantharidin as an inflammatory model or in cancer treatment.[A32892] Regardless, the ongoing lack of FDA approval is likely related to certain toxic effects that were observed following oral ingestion, which include ulceration of the gastrointestinal and genitourinary tracts, along with electrolyte and renal function disturbance in humans and animals [A32891].
Available synthetically since the 1950s, topical applications of cantharidin have been used predominantly as a treatment for cutaneous warts since that time. [A32891][A32892] In 1962 however, marketers of cantharidin failed to produce sufficient efficacy data, resulting in the FDA revision of approval of cantharidin.[A32892] Nevertheless, it gained its first FDA approval on Jul 21, 2023, under the brand name YCANTH™ by Verrica Pharmaceuticals for the treatment of molluscum contagiosum in adult and pediatric patients.[L47496] The approval was based on positive results from 2 phase III trials, CAMP-1 and CAMP-2, where 46% and 52% of patients treated with cantharidin achieved complete molluscum clearance, respectively.[L47496]
Properties:
Avg. mass: 196.20 Da
DrugBank indication
Cantharidin is approved by the FDA for the topical treatment of molluscum contagiosum in adult and pediatric patients 2 years of age and older.
[L47501]
It has also been approved by Health Canada for the treatment of common warts (verruca vulgaris), periungual warts, and molluscum contagiosum as a standalone product and resistant and heavily keratinized plantar warts as a combination product with [salicylic acid] and [podophyllin].
[L47511]
At the same time, such topical cantharidin applications have also been used for a number of off-label indications like callus removal, cutaneous leishmaniasis, herpes zoster, and acquired perforating dermatosis.
[A32892]
Furthermore, since most topical cantharidin applications are most commonly available in a 0.7% formulation or a more potent 1% mixture, the 0.7% formulation is most commonly indicated for the treatment of common warts, periungual warts, and molluscum contagiosum while the more potent 1% mixture is typically limited only for use by healthcare professionals in a clinical setting for treating plantar warts and other more specialized off-label conditions.[A32891, A32892, F32]
Moreover, there have also been studies into whether or not cantharidin could be effective at being used as an inflammatory model or in cancer treatment - either of which has yet to elucidate any results formally.
[A32892]
[L47501]
It has also been approved by Health Canada for the treatment of common warts (verruca vulgaris), periungual warts, and molluscum contagiosum as a standalone product and resistant and heavily keratinized plantar warts as a combination product with [salicylic acid] and [podophyllin].
[L47511]
At the same time, such topical cantharidin applications have also been used for a number of off-label indications like callus removal, cutaneous leishmaniasis, herpes zoster, and acquired perforating dermatosis.
[A32892]
Furthermore, since most topical cantharidin applications are most commonly available in a 0.7% formulation or a more potent 1% mixture, the 0.7% formulation is most commonly indicated for the treatment of common warts, periungual warts, and molluscum contagiosum while the more potent 1% mixture is typically limited only for use by healthcare professionals in a clinical setting for treating plantar warts and other more specialized off-label conditions.[A32891, A32892, F32]
Moreover, there have also been studies into whether or not cantharidin could be effective at being used as an inflammatory model or in cancer treatment - either of which has yet to elucidate any results formally.
[A32892]
Also known as(13)
1,2-Dimethyl-3,6-epoxyperhydrophthalic anhydride
Cantharidin
Cantharidine
Cantharone
exo-1,2-cis-Dimethyl-3,6-epoxyhexahydrophthalic anhydride
Kantharidin
3.1.3.16
PP-1A
Molecular properties(18)
Toxicity & overdose
Side effects observed from the topical application of cantharidin include blistering, erythema, pain, bleeding, ring warts, post-inflammatory hyperpigmentation, lymphangitis, secondary bacterial cellulitis, scarring, and varicelliform vesicular dermatitis.
[A32892]
Oral ingestion of cantharidin has resulted in renal failure, blistering and severe damage to the gastrointestinal tract, coagulopathy, seizures, and flaccid paralysis. In the event that YCANTH topical solution is ingested, patients should seek medical attention immediately and contact a Poison Center (1-800-222-1222) or a medical toxicologist for additional overdosage management recommendations.
[L47501]
Carcinogenicity studies have not been conducted with cantharidin. Cantharidin was not mutagenic in a bacteria reverse mutation (Ames) assay.
An in vitro chromosomal aberration assay in human lymphocytes with cantharidin was inconclusive. Cantharidin was positive in an in vitro micronucleus assay in TK6 cells, primarily through an aneugenic mechanism. The effects of cantharidin on fertility have not been evaluated.
[L47501]
[A32892]
Oral ingestion of cantharidin has resulted in renal failure, blistering and severe damage to the gastrointestinal tract, coagulopathy, seizures, and flaccid paralysis. In the event that YCANTH topical solution is ingested, patients should seek medical attention immediately and contact a Poison Center (1-800-222-1222) or a medical toxicologist for additional overdosage management recommendations.
[L47501]
Carcinogenicity studies have not been conducted with cantharidin. Cantharidin was not mutagenic in a bacteria reverse mutation (Ames) assay.
An in vitro chromosomal aberration assay in human lymphocytes with cantharidin was inconclusive. Cantharidin was positive in an in vitro micronucleus assay in TK6 cells, primarily through an aneugenic mechanism. The effects of cantharidin on fertility have not been evaluated.
[L47501]
How it works
Mechanism of action
Cantharidin is specifically absorbed by lipids in the membrane of epidermal keratinocytes, where it activates the release of neutral serine proteases.[A32891][A32892] These enzymes subsequently break the peptide bonds in surrounding proteins, leading to the progressive degeneration of desmosomal dense plaques, which are important cellular structures that participate in cell-to-cell adhesion.[A32891][A32892] Such degeneration results in the detachment of the tonofilaments that hold cells together. This process as a whole leads to selective acantholysis (loss of cellular connections) and blistering of the skin when the cantharidin topical application is applied upon specific topical developments like warts.[A32891][A32892] A blister(s) at the application site develops within 24 to 48 hours of application and typically resolves within 4 to 7 days.[A32891][A32892] Factors that can modify this proposed time frame include the volume or concentration of cantharidin used, physical contact time of the applied compound (usually between 4 to 24 hours), the presence of any occlusive dressings, or even patient sensitivity to cantharidin.[A32891][A32892] The blistered lesions ultimately heal without scarring.[A32891][A32892]
Finally, there are some studies that suggest cantharidin's chemical profile as a potent and selective inhibitor of protein phosphatase 2A confers upon it an oxidative stress-independent growth inhibition of pancreatic cancer cells through cancer cell-cycle arrest and apoptosis [A32900].
Nevertheless, the fact that little data regarding the pharmacodynamics and pharmacokinetics of cantharidin in the human body exists [L2647] and certain toxic effects of cantharidin that have been observed following oral ingestion in humans like ulceration of the gastrointestinal and genitourinary tracts, along with electrolyte and renal function disturbance [A32891] are strong reasons as to why the compound currently lacks FDA approval is used fairly limitedly for formal therapeutic indications.
Finally, there are some studies that suggest cantharidin's chemical profile as a potent and selective inhibitor of protein phosphatase 2A confers upon it an oxidative stress-independent growth inhibition of pancreatic cancer cells through cancer cell-cycle arrest and apoptosis [A32900].
Nevertheless, the fact that little data regarding the pharmacodynamics and pharmacokinetics of cantharidin in the human body exists [L2647] and certain toxic effects of cantharidin that have been observed following oral ingestion in humans like ulceration of the gastrointestinal and genitourinary tracts, along with electrolyte and renal function disturbance [A32891] are strong reasons as to why the compound currently lacks FDA approval is used fairly limitedly for formal therapeutic indications.
Pharmacodynamics
Cantharidin is a natural toxin produced by the blistering beetle that possesses both vesicant (blistering) and keratolytic effects.[A32891][A32892] The substance elicits these effects by inducing acantholysis (loss of intercellular connections) through the targeting of the desmosomal dense plaque, resulting in the detachment of the desmosomes from the tonofilaments.[A32891][A32892] Cantharidin's effectiveness against warts is proposed to be a result of the exfoliation of the wart body as a consequence of the compound's acantholytic action.F32 This acantholytic action generally does not go beyond the epidermal cells so that the basal layer remains intact and minimal effect occurs on the corium. There is consequently no scarring from the topical application of cantharidin.F32
Pharmacokinetics
How the body processes this drug — absorption, distribution, metabolism, and elimination
Absorption
Cantharidin is absorbed from the gastrointestinal tract, and, to a limited extent from the skin as well.
[L2648]
Little pharmacodynamic and pharmacokinetic data regarding cantharidin in the human body currently exists; recruitment for First-Time-In-Human clinical trials regarding such information has been ongoing in 2018.
[L2647]
There are however some studies regarding such data in animal models like beagle dogs.
[A32901]
[L2648]
Little pharmacodynamic and pharmacokinetic data regarding cantharidin in the human body currently exists; recruitment for First-Time-In-Human clinical trials regarding such information has been ongoing in 2018.
[L2647]
There are however some studies regarding such data in animal models like beagle dogs.
[A32901]
Half-life
Little pharmacodynamic and pharmacokinetic data regarding cantharidin in the human body currently exists; recruitment for First-Time-In-Human clinical trials regarding such information has been ongoing in 2018.
[L2647]
There are however some studies regarding such data in animal models like beagle dogs.
[A32901]
[L2647]
There are however some studies regarding such data in animal models like beagle dogs.
[A32901]
Protein binding
Little pharmacodynamic and pharmacokinetic data regarding cantharidin in the human body currently exists; recruitment for First-Time-In-Human clinical trials regarding such information has been ongoing in 2018.
[L2647]
There are however some studies regarding such data in animal models like beagle dogs.
[A32901]
[L2647]
There are however some studies regarding such data in animal models like beagle dogs.
[A32901]
Volume of distribution
After oral or IP injection of (3)H-labeled cantharidin, high levels of radioactivity were distributed to and exhibited in the bile, kidney, liver, stomach, and tumor cells of ascites hepatoma-bearing mice. Such distribution suggests the agent has an affinity for liver and tumor tissues.
[L2648]
Little pharmacodynamic and pharmacokinetic data regarding cantharidin in the human body currently exists; recruitment for First-Time-In-Human clinical trials regarding such information has been ongoing in 2018.
[L2647]
There are however some studies regarding such data in animal models like beagle dogs.
[A32901]
[L2648]
Little pharmacodynamic and pharmacokinetic data regarding cantharidin in the human body currently exists; recruitment for First-Time-In-Human clinical trials regarding such information has been ongoing in 2018.
[L2647]
There are however some studies regarding such data in animal models like beagle dogs.
[A32901]
Metabolism
Little pharmacodynamic and pharmacokinetic data regarding cantharidin in the human body currently exists; recruitment for First-Time-In-Human clinical trials regarding such information has been ongoing in 2018.
[L2647]
There are however some studies regarding such data in animal models like beagle dogs.
[A32901]
[L2647]
There are however some studies regarding such data in animal models like beagle dogs.
[A32901]
Route of elimination
It has been observed that absorbed cantharidin is excreted by the kidney.
[L2648]
Little pharmacodynamic and pharmacokinetic data regarding cantharidin in the human body currently exists; recruitment for First-Time-In-Human clinical trials regarding such information has been ongoing in 2018.
[L2647]
There are however some studies regarding such data in animal models like beagle dogs.
[A32901]
[L2648]
Little pharmacodynamic and pharmacokinetic data regarding cantharidin in the human body currently exists; recruitment for First-Time-In-Human clinical trials regarding such information has been ongoing in 2018.
[L2647]
There are however some studies regarding such data in animal models like beagle dogs.
[A32901]
Clearance
Little pharmacodynamic and pharmacokinetic data regarding cantharidin in the human body currently exists; recruitment for First-Time-In-Human clinical trials regarding such information has been ongoing in 2018.
[L2647]
There are however some studies regarding such data in animal models like beagle dogs.
[A32901]
[L2647]
There are however some studies regarding such data in animal models like beagle dogs.
[A32901]
Drug targets(2)
Proteins and enzymes this drug interacts with in the body
Serine/threonine-protein phosphatase PP1-alpha catalytic subunit
PPP1CA
inhibitor
Specific functioncadherin binding involved in cell-cell adhesion
Cellular location
Cytoplasm
General function & pharmacology
Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets .
PMID:28216226 PMID:30158517 PMID:35768504 PMID:35830882 PMID:35831509 PMID:36175670 PMID:39603239 PMID:39603240
Protein phosphatase 1 (PP1) is essential for cell division, transcription elongation, and participates in the regulation of glycogen metabolism, muscle contractility and protein synthesis .
PMID:35768504 PMID:35830882 PMID:35831509 PMID:36175670 PMID:39603239 PMID:39603240
Involved in regulation of ionic conductances and long-term synaptic plasticity. May play an important role in dephosphorylating substrates such as the postsynaptic density-associated Ca(2+)/calmodulin dependent protein kinase II. Catalytic component of the PNUTS-PP1 protein phosphatase complex, a protein phosphatase 1 (PP1) complex that promotes RNA polymerase II transcription pause-release, allowing transcription elongation: the PNUTS-PP1 complex mediates the release of RNA polymerase II from promoter-proximal region of genes by catalyzing dephosphorylation of proteins involved in transcription, such as AFF4, CDK9, MEPCE, INTS12, NCBP1, POLR2M/GDOWN1 and SUPT6H .
PMID:39603239 PMID:39603240
The PNUTS-PP1 complex also regulates transcription termination by mediating dephosphorylation of SUPT5H in termination zones downstream of poly(A) sites, thereby promoting deceleration of RNA polymerase II transcription .
PMID:31677974
PNUTS-PP1 complex is also involved in the response to replication stress by mediating dephosphorylation of POLR2A at 'Ser-5' of the CTD, promoting RNA polymerase II degradation .
PMID:33264625
PNUTS-PP1 also plays a role in the control of chromatin structure and cell cycle progression during the transition from mitosis into interphase .
PMID:20516061
Regulates NEK2 function in terms of kinase activity and centrosome number and splitting, both in the presence and absence of radiation-induced DNA damage .
PMID:17283141
Regulator of neural tube and optic fissure closure, and enteric neural crest cell (ENCCs) migration during development (By similarity).
In balance with CSNK1D and CSNK1E, determines the circadian period length, through the regulation of the speed and rhythmicity of PER1 and PER2 phosphorylation .
PMID:21712997
May dephosphorylate CSNK1D and CSNK1E .
PMID:21712997
Dephosphorylates the 'Ser-418' residue of FOXP3 in regulatory T-cells (Treg) from patients with rheumatoid arthritis, thereby inactivating FOXP3 and rendering Treg cells functionally defective .
PMID:23396208
Dephosphorylates CENPA .
PMID:25556658
Dephosphorylates the 'Ser-139' residue of ATG16L1 causing dissociation of ATG12-ATG5-ATG16L1 complex, thereby inhibiting autophagy .
PMID:26083323
Together with PPP1CC (PP1-gamma subunit), dephosphorylates IFIH1/MDA5 and RIG-I leading to their activation and a functional innate immune response .
PMID:23499489
Core component of the SHOC2-MRAS-PP1c (SMP) holophosphatase complex that regulates the MAPK pathway activation .
PMID:35768504 PMID:35830882 PMID:35831509 PMID:36175670
The SMP complex specifically dephosphorylates the inhibitory phosphorylation at 'Ser-259' of RAF1 kinase, 'Ser-365' of BRAF kinase and 'Ser-214' of ARAF kinase, stimulating their kinase activities .
PMID:35768504 PMID:35830882 PMID:35831509 PMID:36175670
The SMP complex enhances the dephosphorylation activity and substrate specificity of PP1c PMID:35768504 PMID:36175670
PMID:28216226 PMID:30158517 PMID:35768504 PMID:35830882 PMID:35831509 PMID:36175670 PMID:39603239 PMID:39603240
Protein phosphatase 1 (PP1) is essential for cell division, transcription elongation, and participates in the regulation of glycogen metabolism, muscle contractility and protein synthesis .
PMID:35768504 PMID:35830882 PMID:35831509 PMID:36175670 PMID:39603239 PMID:39603240
Involved in regulation of ionic conductances and long-term synaptic plasticity. May play an important role in dephosphorylating substrates such as the postsynaptic density-associated Ca(2+)/calmodulin dependent protein kinase II. Catalytic component of the PNUTS-PP1 protein phosphatase complex, a protein phosphatase 1 (PP1) complex that promotes RNA polymerase II transcription pause-release, allowing transcription elongation: the PNUTS-PP1 complex mediates the release of RNA polymerase II from promoter-proximal region of genes by catalyzing dephosphorylation of proteins involved in transcription, such as AFF4, CDK9, MEPCE, INTS12, NCBP1, POLR2M/GDOWN1 and SUPT6H .
PMID:39603239 PMID:39603240
The PNUTS-PP1 complex also regulates transcription termination by mediating dephosphorylation of SUPT5H in termination zones downstream of poly(A) sites, thereby promoting deceleration of RNA polymerase II transcription .
PMID:31677974
PNUTS-PP1 complex is also involved in the response to replication stress by mediating dephosphorylation of POLR2A at 'Ser-5' of the CTD, promoting RNA polymerase II degradation .
PMID:33264625
PNUTS-PP1 also plays a role in the control of chromatin structure and cell cycle progression during the transition from mitosis into interphase .
PMID:20516061
Regulates NEK2 function in terms of kinase activity and centrosome number and splitting, both in the presence and absence of radiation-induced DNA damage .
PMID:17283141
Regulator of neural tube and optic fissure closure, and enteric neural crest cell (ENCCs) migration during development (By similarity).
In balance with CSNK1D and CSNK1E, determines the circadian period length, through the regulation of the speed and rhythmicity of PER1 and PER2 phosphorylation .
PMID:21712997
May dephosphorylate CSNK1D and CSNK1E .
PMID:21712997
Dephosphorylates the 'Ser-418' residue of FOXP3 in regulatory T-cells (Treg) from patients with rheumatoid arthritis, thereby inactivating FOXP3 and rendering Treg cells functionally defective .
PMID:23396208
Dephosphorylates CENPA .
PMID:25556658
Dephosphorylates the 'Ser-139' residue of ATG16L1 causing dissociation of ATG12-ATG5-ATG16L1 complex, thereby inhibiting autophagy .
PMID:26083323
Together with PPP1CC (PP1-gamma subunit), dephosphorylates IFIH1/MDA5 and RIG-I leading to their activation and a functional innate immune response .
PMID:23499489
Core component of the SHOC2-MRAS-PP1c (SMP) holophosphatase complex that regulates the MAPK pathway activation .
PMID:35768504 PMID:35830882 PMID:35831509 PMID:36175670
The SMP complex specifically dephosphorylates the inhibitory phosphorylation at 'Ser-259' of RAF1 kinase, 'Ser-365' of BRAF kinase and 'Ser-214' of ARAF kinase, stimulating their kinase activities .
PMID:35768504 PMID:35830882 PMID:35831509 PMID:36175670
The SMP complex enhances the dephosphorylation activity and substrate specificity of PP1c PMID:35768504 PMID:36175670
Aryl hydrocarbon receptor
AHR
agonist
Specific functioncis-regulatory region sequence-specific DNA binding
Cellular location
Cytoplasm
General function & pharmacology
Ligand-activated transcription factor that enables cells to adapt to changing conditions by sensing compounds from the environment, diet, microbiome and cellular metabolism, and which plays important roles in development, immunity and cancer .
PMID:23275542 PMID:30373764 PMID:32818467 PMID:7961644
Upon ligand binding, translocates into the nucleus, where it heterodimerizes with ARNT and induces transcription by binding to xenobiotic response elements (XRE) .
PMID:23275542 PMID:30373764 PMID:7961644
Regulates a variety of biological processes, including angiogenesis, hematopoiesis, drug and lipid metabolism, cell motility and immune modulation .
PMID:12213388
Xenobiotics can act as ligands: upon xenobiotic-binding, activates the expression of multiple phase I and II xenobiotic chemical metabolizing enzyme genes (such as the CYP1A1 gene) .
PMID:7961644 PMID:33193710
Mediates biochemical and toxic effects of halogenated aromatic hydrocarbons .
PMID:34521881 PMID:7961644
Next to xenobiotics, natural ligands derived from plants, microbiota, and endogenous metabolism are potent AHR agonists .
PMID:18076143
Tryptophan (Trp) derivatives constitute an important class of endogenous AHR ligands .
PMID:32818467 PMID:32866000
Acts as a negative regulator of anti-tumor immunity: indoles and kynurenic acid generated by Trp catabolism act as ligand and activate AHR, thereby promoting AHR-driven cancer cell motility and suppressing adaptive immunity .
PMID:32818467
Regulates the circadian clock by inhibiting the basal and circadian expression of the core circadian component PER1 .
PMID:28602820
Inhibits PER1 by repressing the CLOCK-BMAL1 heterodimer mediated transcriptional activation of PER1 .
PMID:28602820
The heterodimer ARNT:AHR binds to core DNA sequence 5'-TGCGTG-3' within the dioxin response element (DRE) of target gene promoters and activates their transcription PMID:28602820
PMID:23275542 PMID:30373764 PMID:32818467 PMID:7961644
Upon ligand binding, translocates into the nucleus, where it heterodimerizes with ARNT and induces transcription by binding to xenobiotic response elements (XRE) .
PMID:23275542 PMID:30373764 PMID:7961644
Regulates a variety of biological processes, including angiogenesis, hematopoiesis, drug and lipid metabolism, cell motility and immune modulation .
PMID:12213388
Xenobiotics can act as ligands: upon xenobiotic-binding, activates the expression of multiple phase I and II xenobiotic chemical metabolizing enzyme genes (such as the CYP1A1 gene) .
PMID:7961644 PMID:33193710
Mediates biochemical and toxic effects of halogenated aromatic hydrocarbons .
PMID:34521881 PMID:7961644
Next to xenobiotics, natural ligands derived from plants, microbiota, and endogenous metabolism are potent AHR agonists .
PMID:18076143
Tryptophan (Trp) derivatives constitute an important class of endogenous AHR ligands .
PMID:32818467 PMID:32866000
Acts as a negative regulator of anti-tumor immunity: indoles and kynurenic acid generated by Trp catabolism act as ligand and activate AHR, thereby promoting AHR-driven cancer cell motility and suppressing adaptive immunity .
PMID:32818467
Regulates the circadian clock by inhibiting the basal and circadian expression of the core circadian component PER1 .
PMID:28602820
Inhibits PER1 by repressing the CLOCK-BMAL1 heterodimer mediated transcriptional activation of PER1 .
PMID:28602820
The heterodimer ARNT:AHR binds to core DNA sequence 5'-TGCGTG-3' within the dioxin response element (DRE) of target gene promoters and activates their transcription PMID:28602820
Scientific references(4)
Al-Dawsari N.A., Masterpol K.S.
Eponyms in Dermatology.
SKINmed: Dermatology for the Clinician
20043(1):11-12. doi: 10.1111/j.1540-9740.2004.03043.x
Torbeck R., Pan M., DeMoll E., Levitt J.
Cantharidin: a comprehensive review of the clinical literature.
Dermatology Online Journal
201420(6). doi: 10.5070/d3206022861
Li W., Xie L., Chen Z., Zhu Y., Sun Y., Miao Y., Xu Z., Han X.
Cantharidin, a potent and selective PP2A inhibitor, induces an oxidative stress-independent growth inhibition of pancreatic cancer cells through G2/M cell-cycle arrest and apoptosis.
Cancer Science
2010 May101(5):1226-33. doi: 10.1111/j.1349-7006.2010.01523.x. Epub 2010 Feb 5
Dang Y., Zhu C.
Determination of Trace Cantharidin in Plasma and Pharmacokinetic Study in Beagle Dogs Using Gas Chromatography-Mass Spectrometry.
Journal of Analytical Toxicology
200933(7):384-388. doi: 10.1093/jat/33.7.384
Affected organisms(1)
Humans and other mammals
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)
Cantharidin
Additional database identifiers
Drugs Product Database (DPD)
4322
ChemSpider
5731
BindingDB
50090505
ZINC
ZINC000017611186
HUGO Gene Nomenclature Committee (HGNC)
HGNC:9281
GeneCards
PPP1CA
GenBank Gene Database
X70848
GenBank Protein Database
35451
Guide to Pharmacology
3264
UniProt Accession
PP1A_HUMAN
HUGO Gene Nomenclature Committee (HGNC)
HGNC:348
GeneCards
AHR
GenBank Gene Database
D16354
GenBank Protein Database
533324
Guide to Pharmacology
2951
UniProt Accession
AHR_HUMAN
DrugBank citations
If you use DrugBank data in your research, please cite the following publications:
Knox C., Wilson M., Klinger C.M., et al
DrugBank 6.
0: the DrugBank Knowledgebase for 2024
Nucleic Acids Res. 2024 Jan 552(D1):D1265-D1275
Wishart D.S., Feunang Y.D., Guo A.C., et al
DrugBank 5.
0: a major update to the DrugBank database for 2018
Nucleic Acids Res. 2017 Nov 846(D1):D1074-D1082
Show earlier publications
Law V., Knox C., Djoumbou Y., et al
DrugBank 4.
0: shedding new light on drug metabolism
Nucleic Acids Res. 2014 Jan 142(1):D1091-7
Knox C., Law V., Jewison T., et al
DrugBank 3.
0: a comprehensive resource for 'omics' research on drugs
Nucleic Acids Res. 2011 Jan39(Database issue):D1035-41
Wishart D.S., Knox C., Guo A.C., et al
DrugBank: a knowledgebase for drugs, drug actions and drug targets.
Nucleic Acids Research
2008 Jan36(Database issue):D901-6
Wishart D.S., Knox C., Guo A.C., et al
DrugBank: a comprehensive resource for in silico drug discovery and exploration.
Nucleic Acids Research
2006 Jan 134(Database issue):D668-72
Source: go.drugbank.comCC BY-NC 4.0
Updated 4 months ago(8 Mar 2026)Structured knowledge from the free knowledge base
drugbank match (98%)
Linked open data from Wikidata (Q410884), a free and open knowledge base operated by the Wikimedia Foundation. Data is available under the Creative Commons CC0 1.0 Public Domain Dedication.