Roxadustat 150mg tablets
Prescription only
Requires a prescription from a doctor or prescriber
Tablet
150mg
Oral
Roxadustat is a first-in-class hypoxia-inducible factor prolyl hydroxylase inhibitor used to treat anemia associated with chronic kidney disease.
Active ingredients:
Roxadustat
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Safety monitoring data
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The MHRA Yellow Card scheme collects reports of suspected side effects from healthcare professionals and patients. View the Drug Analysis Profile (iDAP) for real-world adverse reaction data.
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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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Evrenzo 150mg tablets
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WHO defined daily dose (DDD)
43 mg
Not a recommended dose. The DDD is the assumed average maintenance dose per day for a drug used for its main indication in adults. It is a statistical measure used for research and comparison purposes only.
Source: WHO Collaborating Centre for Drug Statistics Methodology, distributed via NHS dm+d BNF mapping files. Contains public sector information licensed under the Open Government Licence v3.0.
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Vadadustat 300mg tablets
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Roxadustat 20mg tablets
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Roxadustat 50mg tablets
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50mg
Same therapeutic group
Roxadustat 70mg tablets
Tablet
70mg
Same therapeutic group
Similarity based on WHO Anatomical Therapeutic Chemical (ATC) classification and NHS BNF section grouping. Source data: NHS dm+d via TRUD (OGL v3.0), WHO ATC/DDD Index.
NHS prescribing volume and spending trends
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Clinical guidelines and formulary information
British National Formulary
Roxadustat
BNF
Drug monograph — bnf.nice.org.ukSource: British National Formulary, NICE. Joint Formulary Committee. Contains public sector information licensed under the Open Government Licence v3.0.
NICE clinical guidance(3)
Roxadustat for treating symptomatic anaemia in chronic kidney disease (TA807)
TA807
Technology appraisal
Updated Jul 2022Vadadustat for treating symptomatic anaemia in adults having dialysis for chronic kidney disease (TA1035)
TA1035
Technology appraisal
Updated Jan 2025Chronic kidney disease: assessment and management (NG203)
NG203
NICE guideline
Updated Nov 2021Source: 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
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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 codes from NHS Business Services Authority (NHSBSA). ATC codes from the WHO Collaborating Centre for Drug Statistics Methodology (whocc.no).
Active and completed clinical studies from ClinicalTrials.gov
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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.
Pharmacology and chemical data from DrugBank
Key facts
Drug status
Approved
Major interactions
None known
Half-life
15 hours
Mechanism
Anemia is a common complication of chronic kidney disease that may be caused by…
Food interactions
1 warning
Human targets
3 targets
Data: DrugBank · CC BY-NC 4.0
Pharmacokinetics at a glance
Absorption
25%
Roxadustat plasma exposure (AUC and Cmax) increases dose-proportionally within the recommended therapeutic dose range.…
Half-life
15 hours
The mean effective half-life of roxadustat is approximately 15 hours in patients with CKD.
[L40318]
[L40318]
Protein binding
99%
Roxadustat is highly bound to human plasma proteins (approximately 99%), mainly to albumin.
[L40318]
[L40318]
Volume of distribution
24 L
The blood-to-plasma ratio of roxadustat is 0.6. The apparent volume of distribution at steady-state is 24 L.
[L40318]
[L40318]
Metabolism
10%
In vitro, roxadustat is a substrate for CYP2C8 and UGT1A9 enzymes.…
Elimination
96%
Following oral administration of radiolabelled roxadustat in healthy subjects, the mean recovery of radioactivity was 96% (50% in feces, 46% in urine).…
Clearance
1.1 L/h
The apparent total body clearance (CL/F) of roxadustat is 1.1 L/h in patients with CKD not on dialysis and 1.4…
Pharmacokinetic data: DrugBank · CC BY-NC 4.0
Status:
Approved
Investigational
Small molecule
About this compound
Roxadustat is a first-in-class hypoxia-inducible factor prolyl hydroxylase inhibitor used to treat anemia associated with chronic kidney disease. It works by reducing the breakdown of the hypoxia-inducible factor (HIF), which is a transcription factor that stimulates red blood cell production in response to low oxygen levels.[A245393] Roxadustat was first approved by the European Commission in August 2021.[L40323]
Properties:
solid
Avg. mass: 352.35 Da
DrugBank indication
Roxadustat is indicated for the treatment of adult patients with symptomatic anemia associated with chronic kidney disease (CKD).
[L40318]
[L40318]
Also known as(88)
Roxadustat
Roxadustatum
1.14.11.29
C1orf12
HIF-PH2
HIF-prolyl hydroxylase 2
HPH-2
Hypoxia-inducible factor prolyl hydroxylase 2
Dosage forms(6)
Tablet (Oral) — 20.000 mg
Tablet, film coated (Oral) — 100 MG
Tablet, film coated (Oral) — 150 MG
Tablet, film coated (Oral) — 20 MG
Tablet, film coated (Oral) — 50 MG
Tablet, film coated (Oral) — 70 MG
Molecular properties(19)
Drug interactions(404)
Known interactions with other medications. Always consult a healthcare professional.
Mifepristone
Unknown severity
The serum concentration of Roxadustat can be increased when it is combined with Mifepristone.
Eluxadoline
Unknown severity
The serum concentration of Eluxadoline can be increased when it is combined with Roxadustat.
The metabolism of Roxadustat can be decreased when combined with Phenytoin.
Secobarbital
Moderate
The metabolism of Roxadustat can be increased when combined with Secobarbital.
The metabolism of Roxadustat can be decreased when combined with Rifampicin.
Troglitazone
Moderate
The metabolism of Roxadustat can be decreased when combined with Troglitazone.
Bexarotene
Moderate
The metabolism of Roxadustat can be decreased when combined with Bexarotene.
The metabolism of Roxadustat can be decreased when combined with Diltiazem.
Trimethoprim
Moderate
The metabolism of Roxadustat can be decreased when combined with Trimethoprim.
Levothyroxine
Moderate
The metabolism of Roxadustat can be decreased when combined with Levothyroxine.
Loratadine
Moderate
The metabolism of Roxadustat can be decreased when combined with Loratadine.
The metabolism of Roxadustat can be decreased when combined with Quinine.
The metabolism of Roxadustat can be decreased when combined with Ritonavir.
The metabolism of Roxadustat can be decreased when combined with Medroxyprogesterone acetate.
Nicardipine
Moderate
The metabolism of Roxadustat can be decreased when combined with Nicardipine.
The metabolism of Roxadustat can be decreased when combined with Efavirenz.
The serum concentration of Tamoxifen can be increased when it is combined with Roxadustat.
Ketoconazole
Moderate
The metabolism of Roxadustat can be decreased when combined with Ketoconazole.
Irbesartan
Moderate
The metabolism of Roxadustat can be decreased when combined with Irbesartan.
Oxybutynin
Moderate
The metabolism of Roxadustat can be decreased when combined with Oxybutynin.
Fluvastatin
Unknown severity
The serum concentration of Fluvastatin can be increased when it is combined with Roxadustat.
Pioglitazone
Moderate
The metabolism of Roxadustat can be decreased when combined with Pioglitazone.
Saquinavir
Moderate
The metabolism of Roxadustat can be decreased when combined with Saquinavir.
The metabolism of Roxadustat can be decreased when combined with Genistein.
Topiroxostat
Moderate
The metabolism of Roxadustat can be decreased when combined with Topiroxostat.
Abiraterone
Moderate
The metabolism of Roxadustat can be decreased when combined with Abiraterone.
Eltrombopag
Moderate
The metabolism of Roxadustat can be decreased when combined with Eltrombopag.
Teriflunomide
Unknown severity
The serum concentration of Teriflunomide can be increased when it is combined with Roxadustat.
Enzalutamide
Moderate
The metabolism of Roxadustat can be decreased when combined with Enzalutamide.
The metabolism of Roxadustat can be decreased when combined with Sorafenib.
The metabolism of Roxadustat can be decreased when combined with Erlotinib.
Fluticasone propionate
Moderate
The metabolism of Roxadustat can be decreased when combined with Fluticasone propionate.
Clopidogrel
Moderate
The metabolism of Roxadustat can be decreased when combined with Clopidogrel.
Candesartan cilexetil
Moderate
The metabolism of Roxadustat can be decreased when combined with Candesartan cilexetil.
Salmeterol
Moderate
The metabolism of Roxadustat can be decreased when combined with Salmeterol.
Felodipine
Moderate
The metabolism of Roxadustat can be decreased when combined with Felodipine.
Gemfibrozil
Moderate
The metabolism of Roxadustat can be decreased when combined with Gemfibrozil.
Dabrafenib
Moderate
The metabolism of Roxadustat can be decreased when combined with Dabrafenib.
Fluticasone
Moderate
The metabolism of Roxadustat can be decreased when combined with Fluticasone.
Mometasone furoate
Moderate
The metabolism of Roxadustat can be decreased when combined with Mometasone furoate.
Folic acid
Unknown severity
The serum concentration of Folic acid can be increased when it is combined with Roxadustat.
Pravastatin
Unknown severity
The serum concentration of Pravastatin can be increased when it is combined with Roxadustat.
Conjugated estrogens
Unknown severity
The serum concentration of Conjugated estrogens can be increased when it is combined with Roxadustat.
The serum concentration of Gefitinib can be increased when it is combined with Roxadustat.
Allopurinol
Unknown severity
The serum concentration of Allopurinol can be increased when it is combined with Roxadustat.
Cerivastatin
Unknown severity
The serum concentration of Cerivastatin can be increased when it is combined with Roxadustat.
Teniposide
Unknown severity
The serum concentration of Teniposide can be increased when it is combined with Roxadustat.
The serum concentration of Prazosin can be increased when it is combined with Roxadustat.
Raloxifene
Unknown severity
The serum concentration of Raloxifene can be increased when it is combined with Roxadustat.
The serum concentration of Celecoxib can be increased when it is combined with Roxadustat.
Showing 50 of 404 interactions
Food & lifestyle interactions
Advice
Take with or without food. Food can decrease Cmax but not to a clinically significant extent.
Toxicity & overdose
There are limited information on the LD50 values of roxadustat.
Single doses of roxadustat 5 mg/kg (up to 510 mg) in healthy subjects led to a transient increase in heart rate, an increased frequency of mild to moderate musculoskeletal pain, headaches, sinus tachycardia, and less commonly, low blood pressure. All these effects were non-serious in nature. Roxadustat overdose can elevate hemoglobin levels above the desired level (10 - 12 g/dL), which should be managed with discontinuation of roxadustat treatment or reduction of drug dosage with careful monitoring and appropriate supportive treatment.
Roxadustat and its metabolites are not significantly removed by hemodialysis.
[L40318]
Single doses of roxadustat 5 mg/kg (up to 510 mg) in healthy subjects led to a transient increase in heart rate, an increased frequency of mild to moderate musculoskeletal pain, headaches, sinus tachycardia, and less commonly, low blood pressure. All these effects were non-serious in nature. Roxadustat overdose can elevate hemoglobin levels above the desired level (10 - 12 g/dL), which should be managed with discontinuation of roxadustat treatment or reduction of drug dosage with careful monitoring and appropriate supportive treatment.
Roxadustat and its metabolites are not significantly removed by hemodialysis.
[L40318]
How it works
Mechanism of action
Anemia is a common complication of chronic kidney disease that may be caused by reduced production of renal erythropoietin (EPO), functional iron deficiency due to increased levels of hepcidin, blood loss, reduced erythrocyte survival duration, and inflammation.[A245363][A245393] Hypoxia-inducible factor (HIF) is a transcription factor that induces several target oxygen-sensitive genes in response to low oxygen levels in the cellular environment, or hypoxia. Target genes are involved in erythropoiesis, such as those for EPO, EPO receptor, proteins promoting iron absorption, iron transport, and haem synthesis.[A245363] Activation of the HIF pathway is an important adaptive responsive to hypoxia to increase red blood cell production.[L40318] HIF is heterodimeric and contains an oxygen-regulated α-subunit. The α-subunit houses an oxygen-dependent degradation (ODD) domain that is regulated and hydroxylated by HIF-prolyl hydroxylase (HIF-PHD) enzymes under normoxic cellular conditions.[A245398] HIF-PHD enzymes play a crucial role in maintaining a balance between oxygen availability and HIF activity.[A245363]
Roxadustat is a reversible and potent inhibitor of HIF-PHD enzymes: inhibition of HIF-PHD leads to the accumulation of functional HIF, an increase in plasma endogenous EPO production, enhanced erythropoiesis, and indirect suppression of hepcidin, which is an iron regulator protein that is increased during inflammation in chronic kidney disease.[L40318] Roxadustat can also regulate iron transporter proteins [L40318] and regulates iron metabolism by increasing serum transferrin, intestinal iron absorption and the release of stored iron in patients with anemia associated with dialysis-dependent or dialysis-independent CKD.[A245363] Overall, roxadustat improves iron bioavailability, increases Hb production, and increases red cell mass.[A245363][L40318]
Roxadustat is a reversible and potent inhibitor of HIF-PHD enzymes: inhibition of HIF-PHD leads to the accumulation of functional HIF, an increase in plasma endogenous EPO production, enhanced erythropoiesis, and indirect suppression of hepcidin, which is an iron regulator protein that is increased during inflammation in chronic kidney disease.[L40318] Roxadustat can also regulate iron transporter proteins [L40318] and regulates iron metabolism by increasing serum transferrin, intestinal iron absorption and the release of stored iron in patients with anemia associated with dialysis-dependent or dialysis-independent CKD.[A245363] Overall, roxadustat improves iron bioavailability, increases Hb production, and increases red cell mass.[A245363][L40318]
Pharmacodynamics
Roxadustat dose-dependently improves iron bioavailability, increases hemoglobin production, and increases red blood cell mass in patients with anemia.[L40318] In non-dialysis-dependent CKD patients with anemia, roxadustat maintained Hb for up to 2 years. It has a comparable efficacy to erythropoietin-stimulating agents in achieving Hb response.[A245393] Roxadustat also reduces cholesterol levels from baseline, regardless of the use of statins or other lipid-lowering agents.[A245363]
Pharmacokinetics
How the body processes this drug — absorption, distribution, metabolism, and elimination
Absorption
Roxadustat plasma exposure (AUC and Cmax) increases dose-proportionally within the recommended therapeutic dose range. In a three times per week dosing regimen, steady-state roxadustat plasma concentrations are achieved within one week (three doses) with minimal accumulation. Maximum plasma concentrations (Cmax) are usually achieved at two hours post dose in the fasted state.
Administration of roxadustat with food decreased Cmax by 25% but did not alter AUC as compared with the fasted state.
[L40318]
Administration of roxadustat with food decreased Cmax by 25% but did not alter AUC as compared with the fasted state.
[L40318]
Half-life
The mean effective half-life of roxadustat is approximately 15 hours in patients with CKD.
[L40318]
[L40318]
Protein binding
Roxadustat is highly bound to human plasma proteins (approximately 99%), mainly to albumin.
[L40318]
[L40318]
Volume of distribution
The blood-to-plasma ratio of roxadustat is 0.6. The apparent volume of distribution at steady-state is 24 L.
[L40318]
[L40318]
Metabolism
In vitro, roxadustat is a substrate for CYP2C8 and UGT1A9 enzymes. Roxadustat is primarily metabolized to hydroxy-roxadustat and roxadustat O-glucuronide. Unchanged roxadustat was the major circulating component in human plasma and detectable metabolites in human plasma constituted less than 10% of total drug-related material exposure.
No human-specific metabolites were observed [L40318] but roxadustat O-glucuronide was detected in human urine sample.
[A245403]
No human-specific metabolites were observed [L40318] but roxadustat O-glucuronide was detected in human urine sample.
[A245403]
Route of elimination
Following oral administration of radiolabelled roxadustat in healthy subjects, the mean recovery of radioactivity was 96% (50% in feces, 46% in urine). In feces, 28% of the dose was excreted as unchanged roxadustat. Less than 2% of the dose was recovered in urine as unchanged roxadustat.
[L40318]
[L40318]
Clearance
The apparent total body clearance (CL/F) of roxadustat is 1.1 L/h in patients with CKD not on dialysis and 1.4 L/h in patients with CKD on dialysis.
[L40318]
[L40318]
Drug targets(3)
Proteins and enzymes this drug interacts with in the body
Egl nine homolog 1
EGLN1
inhibitor
Specific function2-oxoglutarate-dependent dioxygenase activity
Cellular location
Cytoplasm
General function & pharmacology
Cellular oxygen sensor that catalyzes, under normoxic conditions, the post-translational formation of 4-hydroxyproline in hypoxia-inducible factor (HIF) alpha proteins. Hydroxylates a specific proline found in each of the oxygen-dependent degradation (ODD) domains (N-terminal, NODD, and C-terminal, CODD) of HIF1A. Also hydroxylates HIF2A.
Has a preference for the CODD site for both HIF1A and HIF1B. Hydroxylated HIFs are then targeted for proteasomal degradation via the von Hippel-Lindau ubiquitination complex. Under hypoxic conditions, the hydroxylation reaction is attenuated allowing HIFs to escape degradation resulting in their translocation to the nucleus, heterodimerization with HIF1B, and increased expression of hypoxy-inducible genes.
EGLN1 is the most important isozyme under normoxia and, through regulating the stability of HIF1, involved in various hypoxia-influenced processes such as angiogenesis in retinal and cardiac functionality. Target proteins are preferentially recognized via a LXXLAP motif
Has a preference for the CODD site for both HIF1A and HIF1B. Hydroxylated HIFs are then targeted for proteasomal degradation via the von Hippel-Lindau ubiquitination complex. Under hypoxic conditions, the hydroxylation reaction is attenuated allowing HIFs to escape degradation resulting in their translocation to the nucleus, heterodimerization with HIF1B, and increased expression of hypoxy-inducible genes.
EGLN1 is the most important isozyme under normoxia and, through regulating the stability of HIF1, involved in various hypoxia-influenced processes such as angiogenesis in retinal and cardiac functionality. Target proteins are preferentially recognized via a LXXLAP motif
Prolyl hydroxylase EGLN2
EGLN2
inhibitor
Specific function2-oxoglutarate-dependent dioxygenase activity
Cellular location
Nucleus
General function & pharmacology
Prolyl hydroxylase that mediates hydroxylation of proline residues in target proteins, such as ATF4, IKBKB, CEP192 and HIF1A .
PMID:11595184 PMID:12039559 PMID:15925519 PMID:16509823 PMID:17114296 PMID:23932902
Target proteins are preferentially recognized via a LXXLAP motif .
PMID:11595184 PMID:12039559 PMID:15925519
Cellular oxygen sensor that catalyzes, under normoxic conditions, the post-translational formation of 4-hydroxyproline in hypoxia-inducible factor (HIF) alpha proteins .
PMID:11595184 PMID:12039559 PMID:12181324 PMID:15925519 PMID:19339211
Hydroxylates a specific proline found in each of the oxygen-dependent degradation (ODD) domains (N-terminal, NODD, and C-terminal, CODD) of HIF1A .
PMID:11595184 PMID:12039559 PMID:12181324 PMID:15925519
Also hydroxylates HIF2A .
PMID:11595184 PMID:12039559 PMID:15925519
Has a preference for the CODD site for both HIF1A and HIF2A .
PMID:11595184 PMID:12039559 PMID:15925519
Hydroxylated HIFs are then targeted for proteasomal degradation via the von Hippel-Lindau ubiquitination complex .
PMID:11595184 PMID:12039559 PMID:15925519
Under hypoxic conditions, the hydroxylation reaction is attenuated allowing HIFs to escape degradation resulting in their translocation to the nucleus, heterodimerization with HIF1B, and increased expression of hypoxy-inducible genes .
PMID:11595184 PMID:12039559 PMID:15925519
EGLN2 is involved in regulating hypoxia tolerance and apoptosis in cardiac and skeletal muscle .
PMID:11595184 PMID:12039559 PMID:15925519
Also regulates susceptibility to normoxic oxidative neuronal death .
PMID:11595184 PMID:12039559 PMID:15925519
Links oxygen sensing to cell cycle and primary cilia formation by hydroxylating the critical centrosome component CEP192 which promotes its ubiquitination and subsequent proteasomal degradation .
PMID:23932902
Hydroxylates IKBKB, mediating NF-kappa-B activation in hypoxic conditions .
PMID:17114296
Also mediates hydroxylation of ATF4, leading to decreased protein stability of ATF4 (By similarity)
PMID:11595184 PMID:12039559 PMID:15925519 PMID:16509823 PMID:17114296 PMID:23932902
Target proteins are preferentially recognized via a LXXLAP motif .
PMID:11595184 PMID:12039559 PMID:15925519
Cellular oxygen sensor that catalyzes, under normoxic conditions, the post-translational formation of 4-hydroxyproline in hypoxia-inducible factor (HIF) alpha proteins .
PMID:11595184 PMID:12039559 PMID:12181324 PMID:15925519 PMID:19339211
Hydroxylates a specific proline found in each of the oxygen-dependent degradation (ODD) domains (N-terminal, NODD, and C-terminal, CODD) of HIF1A .
PMID:11595184 PMID:12039559 PMID:12181324 PMID:15925519
Also hydroxylates HIF2A .
PMID:11595184 PMID:12039559 PMID:15925519
Has a preference for the CODD site for both HIF1A and HIF2A .
PMID:11595184 PMID:12039559 PMID:15925519
Hydroxylated HIFs are then targeted for proteasomal degradation via the von Hippel-Lindau ubiquitination complex .
PMID:11595184 PMID:12039559 PMID:15925519
Under hypoxic conditions, the hydroxylation reaction is attenuated allowing HIFs to escape degradation resulting in their translocation to the nucleus, heterodimerization with HIF1B, and increased expression of hypoxy-inducible genes .
PMID:11595184 PMID:12039559 PMID:15925519
EGLN2 is involved in regulating hypoxia tolerance and apoptosis in cardiac and skeletal muscle .
PMID:11595184 PMID:12039559 PMID:15925519
Also regulates susceptibility to normoxic oxidative neuronal death .
PMID:11595184 PMID:12039559 PMID:15925519
Links oxygen sensing to cell cycle and primary cilia formation by hydroxylating the critical centrosome component CEP192 which promotes its ubiquitination and subsequent proteasomal degradation .
PMID:23932902
Hydroxylates IKBKB, mediating NF-kappa-B activation in hypoxic conditions .
PMID:17114296
Also mediates hydroxylation of ATF4, leading to decreased protein stability of ATF4 (By similarity)
Prolyl hydroxylase EGLN3
EGLN3
inhibitor
Specific function2-oxoglutarate-dependent dioxygenase activity
Cellular location
Nucleus
General function & pharmacology
Prolyl hydroxylase that mediates hydroxylation of proline residues in target proteins, such as PKM, TELO2, ATF4 and HIF1A .
PMID:19584355 PMID:20978507 PMID:21483450 PMID:21575608 PMID:21620138 PMID:22797300
Target proteins are preferentially recognized via a LXXLAP motif. Cellular oxygen sensor that catalyzes, under normoxic conditions, the post-translational formation of 4-hydroxyproline in hypoxia-inducible factor (HIF) alpha proteins .
PMID:11595184 PMID:12181324
Hydroxylates a specific proline found in each of the oxygen-dependent degradation (ODD) domains (N-terminal, NODD, and C-terminal, CODD) of HIF1A .
PMID:11595184 PMID:12181324
Also hydroxylates HIF2A .
PMID:11595184 PMID:12181324
Has a preference for the CODD site for both HIF1A and HIF2A .
PMID:11595184 PMID:12181324
Hydroxylation on the NODD site by EGLN3 appears to require prior hydroxylation on the CODD site .
PMID:11595184 PMID:12181324
Hydroxylated HIFs are then targeted for proteasomal degradation via the von Hippel-Lindau ubiquitination complex .
PMID:11595184 PMID:12181324
Under hypoxic conditions, the hydroxylation reaction is attenuated allowing HIFs to escape degradation resulting in their translocation to the nucleus, heterodimerization with HIF1B, and increased expression of hypoxy-inducible genes .
PMID:11595184 PMID:12181324
ELGN3 is the most important isozyme in limiting physiological activation of HIFs (particularly HIF2A) in hypoxia. Also hydroxylates PKM in hypoxia, limiting glycolysis .
PMID:21483450 PMID:21620138
Under normoxia, hydroxylates and regulates the stability of ADRB2 .
PMID:19584355
Regulator of cardiomyocyte and neuronal apoptosis.
In cardiomyocytes, inhibits the anti-apoptotic effect of BCL2 by disrupting the BAX-BCL2 complex .
PMID:20849813
In neurons, has a NGF-induced proapoptotic effect, probably through regulating CASP3 activity .
PMID:16098468
Also essential for hypoxic regulation of neutrophilic inflammation .
PMID:21317538
Plays a crucial role in DNA damage response (DDR) by hydroxylating TELO2, promoting its interaction with ATR which is required for activation of the ATR/CHK1/p53 pathway .
PMID:22797300
Also mediates hydroxylation of ATF4, leading to decreased protein stability of ATF4 (Probable)
PMID:19584355 PMID:20978507 PMID:21483450 PMID:21575608 PMID:21620138 PMID:22797300
Target proteins are preferentially recognized via a LXXLAP motif. Cellular oxygen sensor that catalyzes, under normoxic conditions, the post-translational formation of 4-hydroxyproline in hypoxia-inducible factor (HIF) alpha proteins .
PMID:11595184 PMID:12181324
Hydroxylates a specific proline found in each of the oxygen-dependent degradation (ODD) domains (N-terminal, NODD, and C-terminal, CODD) of HIF1A .
PMID:11595184 PMID:12181324
Also hydroxylates HIF2A .
PMID:11595184 PMID:12181324
Has a preference for the CODD site for both HIF1A and HIF2A .
PMID:11595184 PMID:12181324
Hydroxylation on the NODD site by EGLN3 appears to require prior hydroxylation on the CODD site .
PMID:11595184 PMID:12181324
Hydroxylated HIFs are then targeted for proteasomal degradation via the von Hippel-Lindau ubiquitination complex .
PMID:11595184 PMID:12181324
Under hypoxic conditions, the hydroxylation reaction is attenuated allowing HIFs to escape degradation resulting in their translocation to the nucleus, heterodimerization with HIF1B, and increased expression of hypoxy-inducible genes .
PMID:11595184 PMID:12181324
ELGN3 is the most important isozyme in limiting physiological activation of HIFs (particularly HIF2A) in hypoxia. Also hydroxylates PKM in hypoxia, limiting glycolysis .
PMID:21483450 PMID:21620138
Under normoxia, hydroxylates and regulates the stability of ADRB2 .
PMID:19584355
Regulator of cardiomyocyte and neuronal apoptosis.
In cardiomyocytes, inhibits the anti-apoptotic effect of BCL2 by disrupting the BAX-BCL2 complex .
PMID:20849813
In neurons, has a NGF-induced proapoptotic effect, probably through regulating CASP3 activity .
PMID:16098468
Also essential for hypoxic regulation of neutrophilic inflammation .
PMID:21317538
Plays a crucial role in DNA damage response (DDR) by hydroxylating TELO2, promoting its interaction with ATR which is required for activation of the ATR/CHK1/p53 pathway .
PMID:22797300
Also mediates hydroxylation of ATF4, leading to decreased protein stability of ATF4 (Probable)
Metabolizing enzymes(2)
Enzymes involved in drug metabolism — important for understanding drug interactions
Enzyme activity key
substrate
inhibitor
inducer
CYP2C8Cytochrome P450 2C8
substrate
UGT1A9UDP-glucuronosyltransferase 1A9
substrate
Transporters(4)
Proteins that transport this drug across cell membranes
Broad substrate specificity ATP-binding cassette transporter ABCG2
ABCG2
inhibitor
Specific functionABC-type xenobiotic transporter activity
Cellular location
Cell membrane
General function & pharmacology
Broad substrate specificity ATP-dependent transporter of the ATP-binding cassette (ABC) family that actively extrudes a wide variety of physiological compounds, dietary toxins and xenobiotics from cells .
PMID:11306452 PMID:12958161 PMID:19506252 PMID:20705604 PMID:28554189 PMID:30405239 PMID:31003562
Involved in porphyrin homeostasis, mediating the export of protoporphyrin IX (PPIX) from both mitochondria to cytosol and cytosol to extracellular space, it also functions in the cellular export of heme .
PMID:20705604 PMID:23189181
Also mediates the efflux of sphingosine-1-P from cells .
PMID:20110355
Acts as a urate exporter functioning in both renal and extrarenal urate excretion .
PMID:19506252 PMID:20368174 PMID:22132962 PMID:31003562 PMID:36749388
In kidney, it also functions as a physiological exporter of the uremic toxin indoxyl sulfate (By similarity). Also involved in the excretion of steroids like estrone 3-sulfate/E1S, 3beta-sulfooxy-androst-5-en-17-one/DHEAS, and other sulfate conjugates .
PMID:12682043 PMID:28554189 PMID:30405239
Mediates the secretion of the riboflavin and biotin vitamins into milk (By similarity). Extrudes pheophorbide a, a phototoxic porphyrin catabolite of chlorophyll, reducing its bioavailability (By similarity).
Plays an important role in the exclusion of xenobiotics from the brain (Probable). It confers to cells a resistance to multiple drugs and other xenobiotics including mitoxantrone, pheophorbide, camptothecin, methotrexate, azidothymidine, and the anthracyclines daunorubicin and doxorubicin, through the control of their efflux .
PMID:11306452 PMID:12477054 PMID:15670731 PMID:18056989 PMID:31254042
In placenta, it limits the penetration of drugs from the maternal plasma into the fetus (By similarity). May play a role in early stem cell self-renewal by blocking differentiation (By similarity).
In inflammatory macrophages, exports itaconate from the cytosol to the extracellular compartment and limits the activation of TFEB-dependent lysosome biogenesis involved in antibacterial innate immune response
PMID:11306452 PMID:12958161 PMID:19506252 PMID:20705604 PMID:28554189 PMID:30405239 PMID:31003562
Involved in porphyrin homeostasis, mediating the export of protoporphyrin IX (PPIX) from both mitochondria to cytosol and cytosol to extracellular space, it also functions in the cellular export of heme .
PMID:20705604 PMID:23189181
Also mediates the efflux of sphingosine-1-P from cells .
PMID:20110355
Acts as a urate exporter functioning in both renal and extrarenal urate excretion .
PMID:19506252 PMID:20368174 PMID:22132962 PMID:31003562 PMID:36749388
In kidney, it also functions as a physiological exporter of the uremic toxin indoxyl sulfate (By similarity). Also involved in the excretion of steroids like estrone 3-sulfate/E1S, 3beta-sulfooxy-androst-5-en-17-one/DHEAS, and other sulfate conjugates .
PMID:12682043 PMID:28554189 PMID:30405239
Mediates the secretion of the riboflavin and biotin vitamins into milk (By similarity). Extrudes pheophorbide a, a phototoxic porphyrin catabolite of chlorophyll, reducing its bioavailability (By similarity).
Plays an important role in the exclusion of xenobiotics from the brain (Probable). It confers to cells a resistance to multiple drugs and other xenobiotics including mitoxantrone, pheophorbide, camptothecin, methotrexate, azidothymidine, and the anthracyclines daunorubicin and doxorubicin, through the control of their efflux .
PMID:11306452 PMID:12477054 PMID:15670731 PMID:18056989 PMID:31254042
In placenta, it limits the penetration of drugs from the maternal plasma into the fetus (By similarity). May play a role in early stem cell self-renewal by blocking differentiation (By similarity).
In inflammatory macrophages, exports itaconate from the cytosol to the extracellular compartment and limits the activation of TFEB-dependent lysosome biogenesis involved in antibacterial innate immune response
Solute carrier organic anion transporter family member 1B1
SLCO1B1
inhibitor
Specific functionbile acid transmembrane transporter activity
Cellular location
Basolateral cell membrane
General function & pharmacology
Mediates the Na(+)-independent uptake of organic anions .
PMID:10358072 PMID:15159445 PMID:17412826
Shows broad substrate specificity, can transport both organic anions such as bile acid taurocholate (cholyltaurine) and conjugated steroids (dehydroepiandrosterone 3-sulfate, 17-beta-glucuronosyl estradiol, and estrone 3-sulfate), as well as eicosanoids (prostaglandin E2, thromboxane B2, leukotriene C4, and leukotriene E4), and thyroid hormones (T4/L-thyroxine, and T3/3,3',5'-triiodo-L-thyronine) .
PMID:10358072 PMID:10601278 PMID:10873595 PMID:11159893 PMID:12196548 PMID:12568656 PMID:15159445 PMID:15970799 PMID:16627748 PMID:17412826 PMID:19129463 PMID:26979622
Can take up bilirubin glucuronides from plasma into the liver, contributing to the detoxification-enhancing liver-blood shuttling loop .
PMID:22232210
Involved in the clearance of endogenous and exogenous substrates from the liver .
PMID:10358072 PMID:10601278
Transports coproporphyrin I and III, by-products of heme synthesis, and may be involved in their hepatic disposition .
PMID:26383540
May contribute to regulate the transport of organic compounds in testes across the blood-testis-barrier (Probable). Can transport HMG-CoA reductase inhibitors (also known as statins), such as pravastatin and pitavastatin, a clinically important class of hypolipidemic drugs .
PMID:10601278 PMID:15159445 PMID:15970799
May play an important role in plasma and tissue distribution of the structurally diverse chemotherapeutic drug methotrexate .
PMID:23243220
May also transport antihypertension agents, such as the angiotensin-converting enzyme (ACE) inhibitor prodrug enalapril, and the highly selective angiotensin II AT1-receptor antagonist valsartan, in the liver .
PMID:16624871 PMID:16627748
Shows a pH-sensitive substrate specificity towards prostaglandin E2 and T4 which may be ascribed to the protonation state of the binding site and leads to a stimulation of substrate transport in an acidic microenvironment .
PMID:19129463
Hydrogencarbonate/HCO3(-) acts as the probable counteranion that exchanges for organic anions PMID:19129463
PMID:10358072 PMID:15159445 PMID:17412826
Shows broad substrate specificity, can transport both organic anions such as bile acid taurocholate (cholyltaurine) and conjugated steroids (dehydroepiandrosterone 3-sulfate, 17-beta-glucuronosyl estradiol, and estrone 3-sulfate), as well as eicosanoids (prostaglandin E2, thromboxane B2, leukotriene C4, and leukotriene E4), and thyroid hormones (T4/L-thyroxine, and T3/3,3',5'-triiodo-L-thyronine) .
PMID:10358072 PMID:10601278 PMID:10873595 PMID:11159893 PMID:12196548 PMID:12568656 PMID:15159445 PMID:15970799 PMID:16627748 PMID:17412826 PMID:19129463 PMID:26979622
Can take up bilirubin glucuronides from plasma into the liver, contributing to the detoxification-enhancing liver-blood shuttling loop .
PMID:22232210
Involved in the clearance of endogenous and exogenous substrates from the liver .
PMID:10358072 PMID:10601278
Transports coproporphyrin I and III, by-products of heme synthesis, and may be involved in their hepatic disposition .
PMID:26383540
May contribute to regulate the transport of organic compounds in testes across the blood-testis-barrier (Probable). Can transport HMG-CoA reductase inhibitors (also known as statins), such as pravastatin and pitavastatin, a clinically important class of hypolipidemic drugs .
PMID:10601278 PMID:15159445 PMID:15970799
May play an important role in plasma and tissue distribution of the structurally diverse chemotherapeutic drug methotrexate .
PMID:23243220
May also transport antihypertension agents, such as the angiotensin-converting enzyme (ACE) inhibitor prodrug enalapril, and the highly selective angiotensin II AT1-receptor antagonist valsartan, in the liver .
PMID:16624871 PMID:16627748
Shows a pH-sensitive substrate specificity towards prostaglandin E2 and T4 which may be ascribed to the protonation state of the binding site and leads to a stimulation of substrate transport in an acidic microenvironment .
PMID:19129463
Hydrogencarbonate/HCO3(-) acts as the probable counteranion that exchanges for organic anions PMID:19129463
Solute carrier family 22 member 6
SLC22A6
substrate
Specific functionalpha-ketoglutarate transmembrane transporter activity
Cellular location
Basolateral cell membrane
General function & pharmacology
Secondary active transporter that functions as a Na(+)-independent organic anion (OA)/dicarboxylate antiporter where the uptake of one molecule of OA into the cell is coupled with an efflux of one molecule of intracellular dicarboxylate such as 2-oxoglutarate or glutarate .
PMID:11669456 PMID:11907186 PMID:14675047 PMID:22108572 PMID:23832370 PMID:28534121 PMID:9950961
Mediates the uptake of OA across the basolateral side of proximal tubule epithelial cells, thereby contributing to the renal elimination of endogenous OA from the systemic circulation into the urine .
PMID:9887087
Functions as a biopterin transporters involved in the uptake and the secretion of coenzymes tetrahydrobiopterin (BH4), dihydrobiopterin (BH2) and sepiapterin to urine, thereby determining baseline levels of blood biopterins .
PMID:28534121
Transports prostaglandin E2 (PGE2) and prostaglandin F2-alpha (PGF2-alpha) and may contribute to their renal excretion .
PMID:11907186
Also mediates the uptake of cyclic nucleotides such as cAMP and cGMP .
PMID:26377792
Involved in the transport of neuroactive tryptophan metabolites kynurenate (KYNA) and xanthurenate (XA) and may contribute to their secretion from the brain .
PMID:22108572 PMID:23832370
May transport glutamate .
PMID:26377792
Also involved in the disposition of uremic toxins and potentially toxic xenobiotics by the renal organic anion secretory pathway, helping reduce their undesired toxicological effects on the body .
PMID:11669456 PMID:14675047
Uremic toxins include the indoxyl sulfate (IS), hippurate/N-benzoylglycine (HA), indole acetate (IA), 3-carboxy-4- methyl-5-propyl-2-furanpropionate (CMPF) and urate .
PMID:14675047 PMID:26377792
Xenobiotics include the mycotoxin ochratoxin (OTA) .
PMID:11669456
May also contribute to the transport of organic compounds in testes across the blood-testis-barrier PMID:35307651
PMID:11669456 PMID:11907186 PMID:14675047 PMID:22108572 PMID:23832370 PMID:28534121 PMID:9950961
Mediates the uptake of OA across the basolateral side of proximal tubule epithelial cells, thereby contributing to the renal elimination of endogenous OA from the systemic circulation into the urine .
PMID:9887087
Functions as a biopterin transporters involved in the uptake and the secretion of coenzymes tetrahydrobiopterin (BH4), dihydrobiopterin (BH2) and sepiapterin to urine, thereby determining baseline levels of blood biopterins .
PMID:28534121
Transports prostaglandin E2 (PGE2) and prostaglandin F2-alpha (PGF2-alpha) and may contribute to their renal excretion .
PMID:11907186
Also mediates the uptake of cyclic nucleotides such as cAMP and cGMP .
PMID:26377792
Involved in the transport of neuroactive tryptophan metabolites kynurenate (KYNA) and xanthurenate (XA) and may contribute to their secretion from the brain .
PMID:22108572 PMID:23832370
May transport glutamate .
PMID:26377792
Also involved in the disposition of uremic toxins and potentially toxic xenobiotics by the renal organic anion secretory pathway, helping reduce their undesired toxicological effects on the body .
PMID:11669456 PMID:14675047
Uremic toxins include the indoxyl sulfate (IS), hippurate/N-benzoylglycine (HA), indole acetate (IA), 3-carboxy-4- methyl-5-propyl-2-furanpropionate (CMPF) and urate .
PMID:14675047 PMID:26377792
Xenobiotics include the mycotoxin ochratoxin (OTA) .
PMID:11669456
May also contribute to the transport of organic compounds in testes across the blood-testis-barrier PMID:35307651
Organic anion transporter 3
SLC22A8
substrate
Specific functionorganic anion transmembrane transporter activity
Cellular location
Basolateral cell membrane
General function & pharmacology
Functions as an organic anion/dicarboxylate exchanger that couples organic anion uptake indirectly to the sodium gradient .
PMID:14586168 PMID:15644426 PMID:15846473 PMID:16455804 PMID:31553721
Transports organic anions such as estrone 3-sulfate (E1S) and urate in exchange for dicarboxylates such as glutarate or ketoglutarate (2-oxoglutarate) .
PMID:14586168 PMID:15846473 PMID:15864504 PMID:22108572 PMID:23832370
Plays an important role in the excretion of endogenous and exogenous organic anions, especially from the kidney and the brain .
PMID:11306713 PMID:14586168 PMID:15846473
E1S transport is pH- and chloride-dependent and may also involve E1S/cGMP exchange .
PMID:26377792
Responsible for the transport of prostaglandin E2 (PGE2) and prostaglandin F2(alpha) (PGF2(alpha)) in the basolateral side of the renal tubule .
PMID:11907186
Involved in the transport of neuroactive tryptophan metabolites kynurenate and xanthurenate .
PMID:22108572 PMID:23832370
Functions as a biopterin transporters involved in the uptake and the secretion of coenzymes tetrahydrobiopterin (BH4), dihydrobiopterin (BH2) and sepiapterin to urine, thereby determining baseline levels of blood biopterins .
PMID:28534121
May be involved in the basolateral transport of steviol, a metabolite of the popular sugar substitute stevioside .
PMID:15644426
May participate in the detoxification/ renal excretion of drugs and xenobiotics, such as the histamine H(2)-receptor antagonists fexofenadine and cimetidine, the antibiotic benzylpenicillin (PCG), the anionic herbicide 2,4-dichloro-phenoxyacetate (2,4-D), the diagnostic agent p-aminohippurate (PAH), the antiviral acyclovir (ACV), and the mycotoxin ochratoxin (OTA), by transporting these exogenous organic anions across the cell membrane in exchange for dicarboxylates such as 2-oxoglutarate .
PMID:11669456 PMID:15846473 PMID:16455804
Contributes to the renal uptake of potent uremic toxins (indoxyl sulfate (IS), indole acetate (IA), hippurate/N-benzoylglycine (HA) and 3-carboxy-4-methyl-5-propyl-2-furanpropionate (CMPF)), pravastatin, PCG, E1S and dehydroepiandrosterone sulfate (DHEAS), and is partly involved in the renal uptake of temocaprilat (an angiotensin-converting enzyme (ACE) inhibitor) .
PMID:14675047
May contribute to the release of cortisol in the adrenals .
PMID:15864504
Involved in one of the detoxification systems on the choroid plexus (CP), removes substrates such as E1S or taurocholate (TC), PCG, 2,4-D and PAH, from the cerebrospinal fluid (CSF) to the blood for eventual excretion in urine and bile (By similarity). Also contributes to the uptake of several other organic compounds such as the prostanoids prostaglandin E(2) and prostaglandin F(2-alpha), L-carnitine, and the therapeutic drugs allopurinol, 6-mercaptopurine (6-MP) and 5-fluorouracil (5-FU) (By similarity). Mediates the transport of PAH, PCG, and the statins pravastatin and pitavastatin, from the cerebrum into the blood circulation across the blood-brain barrier (BBB).
In summary, plays a role in the efflux of drugs and xenobiotics, helping reduce their undesired toxicological effects on the body (By similarity)
PMID:14586168 PMID:15644426 PMID:15846473 PMID:16455804 PMID:31553721
Transports organic anions such as estrone 3-sulfate (E1S) and urate in exchange for dicarboxylates such as glutarate or ketoglutarate (2-oxoglutarate) .
PMID:14586168 PMID:15846473 PMID:15864504 PMID:22108572 PMID:23832370
Plays an important role in the excretion of endogenous and exogenous organic anions, especially from the kidney and the brain .
PMID:11306713 PMID:14586168 PMID:15846473
E1S transport is pH- and chloride-dependent and may also involve E1S/cGMP exchange .
PMID:26377792
Responsible for the transport of prostaglandin E2 (PGE2) and prostaglandin F2(alpha) (PGF2(alpha)) in the basolateral side of the renal tubule .
PMID:11907186
Involved in the transport of neuroactive tryptophan metabolites kynurenate and xanthurenate .
PMID:22108572 PMID:23832370
Functions as a biopterin transporters involved in the uptake and the secretion of coenzymes tetrahydrobiopterin (BH4), dihydrobiopterin (BH2) and sepiapterin to urine, thereby determining baseline levels of blood biopterins .
PMID:28534121
May be involved in the basolateral transport of steviol, a metabolite of the popular sugar substitute stevioside .
PMID:15644426
May participate in the detoxification/ renal excretion of drugs and xenobiotics, such as the histamine H(2)-receptor antagonists fexofenadine and cimetidine, the antibiotic benzylpenicillin (PCG), the anionic herbicide 2,4-dichloro-phenoxyacetate (2,4-D), the diagnostic agent p-aminohippurate (PAH), the antiviral acyclovir (ACV), and the mycotoxin ochratoxin (OTA), by transporting these exogenous organic anions across the cell membrane in exchange for dicarboxylates such as 2-oxoglutarate .
PMID:11669456 PMID:15846473 PMID:16455804
Contributes to the renal uptake of potent uremic toxins (indoxyl sulfate (IS), indole acetate (IA), hippurate/N-benzoylglycine (HA) and 3-carboxy-4-methyl-5-propyl-2-furanpropionate (CMPF)), pravastatin, PCG, E1S and dehydroepiandrosterone sulfate (DHEAS), and is partly involved in the renal uptake of temocaprilat (an angiotensin-converting enzyme (ACE) inhibitor) .
PMID:14675047
May contribute to the release of cortisol in the adrenals .
PMID:15864504
Involved in one of the detoxification systems on the choroid plexus (CP), removes substrates such as E1S or taurocholate (TC), PCG, 2,4-D and PAH, from the cerebrospinal fluid (CSF) to the blood for eventual excretion in urine and bile (By similarity). Also contributes to the uptake of several other organic compounds such as the prostanoids prostaglandin E(2) and prostaglandin F(2-alpha), L-carnitine, and the therapeutic drugs allopurinol, 6-mercaptopurine (6-MP) and 5-fluorouracil (5-FU) (By similarity). Mediates the transport of PAH, PCG, and the statins pravastatin and pitavastatin, from the cerebrum into the blood circulation across the blood-brain barrier (BBB).
In summary, plays a role in the efflux of drugs and xenobiotics, helping reduce their undesired toxicological effects on the body (By similarity)
Carriers(1)
Proteins that carry this drug through the body
Albumin
ALB
binder
Specific functionantioxidant activity
Cellular location
Secreted
General function & pharmacology
Binds water, Ca(2+), Na(+), K(+), fatty acids, hormones, bilirubin and drugs (Probable). Its main function is the regulation of the colloidal osmotic pressure of blood (Probable). Major zinc transporter in plasma, typically binds about 80% of all plasma zinc .
PMID:19021548
Major calcium and magnesium transporter in plasma, binds approximately 45% of circulating calcium and magnesium in plasma (By similarity).
Potentially has more than two calcium-binding sites and might additionally bind calcium in a non-specific manner (By similarity). The shared binding site between zinc and calcium at residue Asp-273 suggests a crosstalk between zinc and calcium transport in the blood (By similarity). The rank order of affinity is zinc > calcium > magnesium (By similarity).
Binds to the bacterial siderophore enterobactin and inhibits enterobactin-mediated iron uptake of E.coli from ferric transferrin, and may thereby limit the utilization of iron and growth of enteric bacteria such as E.coli .
PMID:6234017
Does not prevent iron uptake by the bacterial siderophore aerobactin PMID:6234017
PMID:19021548
Major calcium and magnesium transporter in plasma, binds approximately 45% of circulating calcium and magnesium in plasma (By similarity).
Potentially has more than two calcium-binding sites and might additionally bind calcium in a non-specific manner (By similarity). The shared binding site between zinc and calcium at residue Asp-273 suggests a crosstalk between zinc and calcium transport in the blood (By similarity). The rank order of affinity is zinc > calcium > magnesium (By similarity).
Binds to the bacterial siderophore enterobactin and inhibits enterobactin-mediated iron uptake of E.coli from ferric transferrin, and may thereby limit the utilization of iron and growth of enteric bacteria such as E.coli .
PMID:6234017
Does not prevent iron uptake by the bacterial siderophore aerobactin PMID:6234017
Scientific references(4)
Dhillon S.
Roxadustat: First Global Approval.
Drugs
2019 Apr79(5):563-572. doi: 10.1007/s40265-019-01077-1
Barratt J., Andric B., Tataradze A., Schomig M., Reusch M., Valluri U., Mariat C.
Roxadustat for the treatment of anaemia in chronic kidney disease patients not on dialysis: a Phase 3, randomized, open-label, active-controlled study (DOLOMITES).
Nephrol Dial Transplant
2021 Aug 2736(9):1616-1628. doi: 10.1093/ndt/gfab191
Ziello J.E., Jovin I.S., Huang Y.
Hypoxia-Inducible Factor 1 (HIF-1) Pathway.
Science's STKE
20072007(407). doi: 10.1126/stke.4072007cm8
Hansson A., Thevis M., Cox H., Miller G., Eichner D., Bondesson U., Hedeland M.
Investigation of the metabolites of the HIF stabilizer FG-4592 (roxadustat) in five different in vitro models and in a human doping control sample using high resolution mass spectrometry.
Journal Pharmacy Biomed Anal
2017 Feb 5134:228-236. doi: 10.1016/j.jpba.2016.11.041. Epub 2016 Nov 27
ATC classification(1 code)
ATC B03XA05
Affected organisms(1)
Humans and other mammals
Experimental properties(1)
Commercial products(10)
Chemical identifiers
CAS, UNII, InChI Key and database cross-references
Show
Chemical identifiers
CAS, UNII, InChI Key and database cross-references
Linked compound data from DrugBank Open Data (CC BY-NC 4.0)
Roxadustat
Additional database identifiers
ChemSpider
9431690
BindingDB
50431015
PDB
8HO
ZINC
ZINC000071257465
HUGO Gene Nomenclature Committee (HGNC)
HGNC:1232
GenAtlas
EGLN1
GeneCards
EGLN1
GenBank Gene Database
AF246631
GenBank Protein Database
11345052
Guide to Pharmacology
2833
UniProt Accession
EGLN1_HUMAN
HUGO Gene Nomenclature Committee (HGNC)
HGNC:14660
GenAtlas
EGLN2
GeneCards
EGLN2
GenBank Gene Database
AJ310544
GenBank Protein Database
14547148
Guide to Pharmacology
2832
UniProt Accession
EGLN2_HUMAN
HUGO Gene Nomenclature Committee (HGNC)
HGNC:14661
GenAtlas
EGLN3
GeneCards
EGLN3
GenBank Gene Database
AJ310545
GenBank Protein Database
14547150
Guide to Pharmacology
2834
UniProt Accession
EGLN3_HUMAN
HUGO Gene Nomenclature Committee (HGNC)
HGNC:2622
GenAtlas
CYP2C8
GeneCards
CYP2C8
GenBank Gene Database
M17397
Guide to Pharmacology
1325
UniProt Accession
CP2C8_HUMAN
HUGO Gene Nomenclature Committee (HGNC)
HGNC:12541
GeneCards
UGT1A9
GenBank Gene Database
S55985
GenBank Protein Database
7690346
UniProt Accession
UD19_HUMAN
HUGO Gene Nomenclature Committee (HGNC)
HGNC:399
GenAtlas
ALB
GeneCards
ALB
GenBank Gene Database
V00494
GenBank Protein Database
28590
UniProt Accession
ALBU_HUMAN
HUGO Gene Nomenclature Committee (HGNC)
HGNC:74
GenAtlas
ABCG2
GeneCards
ABCG2
GenBank Gene Database
AF103796
GenBank Protein Database
4185796
Guide to Pharmacology
792
UniProt Accession
ABCG2_HUMAN
HUGO Gene Nomenclature Committee (HGNC)
HGNC:10959
GenAtlas
SLCO1B1
GeneCards
SLCO1B1
GenBank Gene Database
AF060500
GenBank Protein Database
5051630
Guide to Pharmacology
1220
UniProt Accession
SO1B1_HUMAN
HUGO Gene Nomenclature Committee (HGNC)
HGNC:10970
GenAtlas
hROAT1
GeneCards
SLC22A6
GenBank Gene Database
AF057039
GenBank Protein Database
3831566
Guide to Pharmacology
1025
UniProt Accession
S22A6_HUMAN
HUGO Gene Nomenclature Committee (HGNC)
HGNC:10972
GeneCards
SLC22A8
GenBank Gene Database
AF097491
GenBank Protein Database
4378059
Guide to Pharmacology
1027
UniProt Accession
S22A8_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 27 days ago(8 Mar 2026)