Cisplatin
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Identification
- Summary
Cisplatin is a platinum based chemotherapy agent used to treat various sarcomas, carcinomas, lymphomas, and germ cell tumors.
- Brand Names
- Platinol
- Generic Name
- Cisplatin
- DrugBank Accession Number
- DB00515
- Background
Cisplatin, cisplatinum or cis-diamminedichloroplatinum(II) (CDDP) is a platinum-based chemotherapy drug used to treat various types of cancers, including sarcomas, some carcinomas (e.g. small cell lung cancer, and ovarian cancer), lymphomas and germ cell tumors. It was the first member of its class, which now also includes carboplatin and oxaliplatin.
- Type
- Small Molecule
- Groups
- Approved
- Structure
- Weight
- Average: 300.05
Monoisotopic: 298.955596 - Chemical Formula
- Cl2H6N2Pt
- Synonyms
- (SP-4-2)-DIAMMINEDICHLOROPLATINUM
- CDDP
- Cis-DDP
- CIS-DIAMMINEDICHLOROPLATINUM
- CIS-DIAMMINEDICHLOROPLATINUM II
- cis-diamminedichloroplatinum(II)
- Cisplatin
- cisplatino
- INT-230-6 COMPONENT CISPLATIN
- INT230-6 COMPONENT CISPLATIN
- PLATINUM, DIAMMINEDICHLORO-, (SP-4-2)-
Pharmacology
- Indication
For the treatment of metastatic testicular tumors, metastatic ovarian tumors and advanced bladder cancer.
Reduce drug development failure ratesBuild, train, & validate machine-learning modelswith evidence-based and structured datasets.Build, train, & validate predictive machine-learning models with structured datasets.- Associated Conditions
Indication Type Indication Combined Product Details Approval Level Age Group Patient Characteristics Dose Form Treatment of Advanced ovarian cancer •••••••••••• ••••••••• Used in combination to treat Ovarian cancer metastatic •••••••••••• •••••••••• •• •••••••• ••••••••• ••••••••• Treatment of Advanced bladder cancer •••••••••••• ••••••••• Treatment of Advanced testicular cancer •••••••••••• ••••••••• Used in combination to treat Metastatic testicular cancer •••••••••••• ••••••••• - Contraindications & Blackbox Warnings
- Prevent Adverse Drug Events TodayTap into our Clinical API for life-saving information on contraindications & blackbox warnings, population restrictions, harmful risks, & more.Avoid life-threatening adverse drug events with our Clinical API
- Pharmacodynamics
Cisplatin is an antineoplastic in the class of alkylating agents and is used to treat various forms of cancer. Alkylating agents are so named because of their ability to add alkyl groups to many electronegative groups under conditions present in cells. They stop tumor growth by cross-linking guanine bases in DNA double-helix strands - directly attacking DNA. This makes the strands unable to uncoil and separate. As this is necessary in DNA replication, the cells can no longer divide. In addition, these drugs add methyl or other alkyl groups onto molecules where they do not belong which in turn inhibits their correct utilization by base pairing and causes a miscoding of DNA. Alkylating agents are cell cycle-nonspecific. Alkylating agents work by three different mechanisms all of which achieve the same end result - disruption of DNA function and cell death.
- Mechanism of action
Alkylating agents work by three different mechanisms: 1) attachment of alkyl groups to DNA bases, resulting in the DNA being fragmented by repair enzymes in their attempts to replace the alkylated bases, preventing DNA synthesis and RNA transcription from the affected DNA, 2) DNA damage via the formation of cross-links (bonds between atoms in the DNA) which prevents DNA from being separated for synthesis or transcription, and 3) the induction of mispairing of the nucleotides leading to mutations.
Target Actions Organism ADNA cross-linking/alkylationHumans UDNA-3-methyladenine glycosylase Not Available Humans UAlpha-2-macroglobulin Not Available Humans USerotransferrin Not Available Humans UCopper transport protein ATOX1 Not Available Humans - Absorption
Following cisplatin doses of 20 to 120 mg/m^2, the concentrations of platinum are highest in liver, prostate, and kidney; somewhat lower in bladder, muscle, testicle, pancreas, and spleen; and lowest in bowel, adrenal, heart, lung, cerebrum, and cerebellum. Platinum is present in tissues for as long as 180 days after the last administration.
- Volume of distribution
Volume of distribution at steady state = 11-12 L/m^2
- Protein binding
Cisplatin does not undergo instantaneous and reversible binding to plasma protein that is characteristic of normal drug-protein binding. However, the platinum itself is capable of binding to plasma proteins, including albumin, transferrin, and gamma globulin. Three hours after a bolus injection and two hours after the end of a three-hour infusion, 90% of the plasma platinum is protein bound.
- Metabolism
- Not Available
- Route of elimination
The parent compound, cisplatin, is excreted in the urine. Although small amounts of platinum are present in the bile and large intestine after administration of cisplatin, the fecal excretion of platinum appears to be insignificant.
- Half-life
Cisplatin decays monoexponentially with a half life of 20 to 30 minutes following administrations of 50 or 100 mg/m^2. Cisplatin has a plasma half-life of 30 minutes. The complexes between albumin and the platinum from cisplatin do not dissociate to a significant extent and are slowly eliminated with a minimum half-life of five days or more.
- Clearance
- 15-16 L/h/m^2 [total body clearance, 7-hour infusion of 100 mg/m^2]
- 62 mL/min/m^2 [renal clearance, 2-hour infusion of 100 mg/m^2]
- 50 mL/min/m^2 [renal clearance, 6- to 7-hour infusion of 100 mg/m^2] The renal clearance of free (ultrafilterable) platinum also exceeds the glomerular filtration rate indicating that cisplatin or other platinum-containing molecules are actively secreted by the kidneys. The renal clearance of free platinum is nonlinear and variable and is dependent on dose, urine flow rate, and individual variability in the extent of active secretion and possible tubular reabsorption.
- Adverse Effects
- Improve decision support & research outcomesWith structured adverse effects data, including: blackbox warnings, adverse reactions, warning & precautions, & incidence rates. View sample adverse effects data in our new Data Library!Improve decision support & research outcomes with our structured adverse effects data.
- Toxicity
Not Available
- Pathways
- Not Available
- Pharmacogenomic Effects/ADRs
Interacting Gene/Enzyme Allele name Genotype(s) Defining Change(s) Type(s) Description Details Glutathione S-transferase Mu 1 GSTM1 Not Available presence of functional GSTM1 ADR Directly Studied Patients with this genotype have increased risk of ototoxicity with [durg: cisplatin]. Details Low-density lipoprotein receptor-related protein 2 --- (A;A) / (A;G) --- ADR Directly Studied Patients with this genotype have increased risk of ototoxicity with [durg: cisplatin]. Details Glutathione S-transferase P --- (A;G) / (G;G) --- ADR Directly Studied Patients with this genotype have increased risk of ototoxicity with [durg: cisplatin]. Details DNA repair protein complementing XP-C cells --- (C;C) --- ADR Directly Studied Patients with this genotype have increased risk of ototoxicity with [durg: cisplatin]. Details
Interactions
- Drug Interactions
- This information should not be interpreted without the help of a healthcare provider. If you believe you are experiencing an interaction, contact a healthcare provider immediately. The absence of an interaction does not necessarily mean no interactions exist.
Drug Interaction Integrate drug-drug
interactions in your softwareAbacavir Abacavir may decrease the excretion rate of Cisplatin which could result in a higher serum level. Abatacept The risk or severity of adverse effects can be increased when Cisplatin is combined with Abatacept. Abciximab The risk or severity of bleeding can be increased when Abciximab is combined with Cisplatin. Acebutolol Cisplatin may increase the bradycardic activities of Acebutolol. Aceclofenac Aceclofenac may decrease the excretion rate of Cisplatin which could result in a higher serum level. - Food Interactions
- Avoid echinacea. Echinacea should be used with caution, if at all, in patients receiving therapeutic immunosuppressants. Monitor for reduced efficacy of the immunosuppressant during concomitant use.
Products
- Drug product information from 10+ global regionsOur datasets provide approved product information including:dosage, form, labeller, route of administration, and marketing period.Access drug product information from over 10 global regions.
- International/Other Brands
- Abiplatin / Cisplatyl / Platidiam / Platin (Cadila Healthcare)
- Brand Name Prescription Products
Name Dosage Strength Route Labeller Marketing Start Marketing End Region Image CISplatin Injection, solution 1 mg/1mL Intravenous WG Critical Care, LLC 2015-04-15 Not applicable US CISplatin Injection, solution 50 mg/50mL Intravenous Apotex Corporation 2023-06-06 Not applicable US CISplatin Injection, solution 1 mg/1mL Intravenous WG Critical Care, LLC 2012-01-13 Not applicable US CISplatin Injection, solution 1 mg/1mL Intravenous WG Critical Care, LLC 2012-01-13 Not applicable US Cisplatin Injection, solution 1 mg/1mL Intravenous Fresenius Kabi Italia S.R.L. 2023-09-01 Not applicable US - Generic Prescription Products
Name Dosage Strength Route Labeller Marketing Start Marketing End Region Image Cisplatin Injection 1 mg/1mL Intravenous BluePoint Laboratories 2016-08-02 Not applicable US Cisplatin Injection, solution 1 mg/1mL Intravenous Bedford Pharmaceuticals 2001-01-15 2011-01-31 US Cisplatin Injection, solution 50 mg/50mL Intravenous Alvogen Inc. 2017-09-25 2020-03-01 US Cisplatin Injection 1 mg/1mL Intravenous Mylan Institutional Inc. 2012-04-19 2017-12-31 US Cisplatin Injection, solution 1 mg/1mL Intravenous Gland Pharma Limited 2017-04-03 Not applicable US - Unapproved/Other Products
Name Ingredients Dosage Route Labeller Marketing Start Marketing End Region Image Cisplatin Cisplatin (1 mg/1mL) Injection, solution Intravenous Fresenius Kabi Italia S.R.L. 2023-09-01 Not applicable US CISplatin Cisplatin (50 mg/50mL) Injection, solution Intravenous Apotex Corporation 2023-06-06 Not applicable US CISPLATIN DBL 100 ML 100 MG FLAKON, 1 ADET Cisplatin (100 mg/100ml) Injection, solution Intravenous ORNA İLAÇ TEKSTİL KİMYEVİ MAD. SAN. VE DIŞ TİC. LTD. ŞTİ. 2019-11-26 Not applicable Turkey CISPLATIN DBL 50 ML 50 MG FLAKON, 1 ADET Cisplatin (50 mg/50ml) Injection, solution Intravenous ORNA İLAÇ TEKSTİL KİMYEVİ MAD. SAN. VE DIŞ TİC. LTD. ŞTİ. 2018-07-31 Not applicable Turkey
Categories
- ATC Codes
- L01XA01 — Cisplatin
- Drug Categories
- Antineoplastic Agents
- Antineoplastic and Immunomodulating Agents
- BCRP/ABCG2 Substrates
- Cardiotoxic antineoplastic agents
- Chlorine Compounds
- Cholinesterase Inhibitors
- Compounds used in a research, industrial, or household setting
- Cross-Linking Reagents
- Cytochrome P-450 CYP2B6 Inhibitors
- Cytochrome P-450 CYP2B6 Inhibitors (strength unknown)
- Cytochrome P-450 CYP2C9 Inhibitors
- Cytochrome P-450 CYP2C9 Inhibitors (strength unknown)
- Cytochrome P-450 Enzyme Inhibitors
- Drugs that are Mainly Renally Excreted
- Drugs that are Mainly Renally Excreted with a Narrow Therapeutic Index
- Immunosuppressive Agents
- Indicators and Reagents
- Laboratory Chemicals
- Myelosuppressive Agents
- Narrow Therapeutic Index Drugs
- Nephrotoxic agents
- Nitrogen Compounds
- OCT2 Inhibitors
- OCT2 Substrates
- OCT2 Substrates with a Narrow Therapeutic Index
- Platinum Compounds
- Radiation-Sensitizing Agents
- Chemical TaxonomyProvided by Classyfire
- Description
- This compound belongs to the class of inorganic compounds known as transition metal chlorides. These are inorganic compounds in which the largest halogen atom is Chlorine, and the heaviest metal atom is a transition metal.
- Kingdom
- Inorganic compounds
- Super Class
- Mixed metal/non-metal compounds
- Class
- Transition metal salts
- Sub Class
- Transition metal chlorides
- Direct Parent
- Transition metal chlorides
- Alternative Parents
- Inorganic chloride salts
- Substituents
- Inorganic chloride salt / Inorganic salt / Transition metal chloride
- Molecular Framework
- Not Available
- External Descriptors
- diamminedichloroplatinum (CHEBI:27899)
- Affected organisms
- Humans and other mammals
Chemical Identifiers
- UNII
- Q20Q21Q62J
- CAS number
- 15663-27-1
- InChI Key
- LXZZYRPGZAFOLE-UHFFFAOYSA-L
- InChI
- InChI=1S/2ClH.2H3N.Pt/h2*1H;2*1H3;/q;;;;+2/p-2
- IUPAC Name
- dichloroplatinumdiamine
- SMILES
- [H][N]([H])([H])[Pt](Cl)(Cl)[N]([H])([H])[H]
References
- Synthesis Reference
Murray A. Kaplan, Alphonse P. Granatek, "Process for the preparation of microcrystalline cisplatin." U.S. Patent US4322391, issued March 30, 1982.
US4322391- General References
- External Links
- Human Metabolome Database
- HMDB0014656
- KEGG Drug
- D00275
- KEGG Compound
- C06911
- PubChem Compound
- 2767
- PubChem Substance
- 46504561
- ChemSpider
- 76401
- BindingDB
- 50028111
- 2555
- ChEBI
- 27899
- ChEMBL
- CHEMBL11359
- Therapeutic Targets Database
- DAP000215
- PharmGKB
- PA449014
- PDBe Ligand
- CPT
- RxList
- RxList Drug Page
- Drugs.com
- Drugs.com Drug Page
- Wikipedia
- Cisplatin
- PDB Entries
- 1a2e / 1a84 / 1aio / 1au5 / 1ckt / 1da4 / 1da5 / 1ddp / 1i1p / 1ksb … show 57 more
- FDA label
- Download (413 KB)
- MSDS
- Download (76.1 KB)
Clinical Trials
- Clinical Trials
Clinical Trial & Rare Diseases Add-on Data Package
Explore 4,000+ rare diseases, orphan drugs & condition pairs, clinical trial why stopped data, & more. Preview package Phase Status Purpose Conditions Count Start Date Why Stopped 100+ additional columns Unlock 175K+ rows when you subscribe.View sample dataNot Available Active Not Recruiting Not Available Brain and Central Nervous System Tumors / Cognitive/Functional Effects / Long-Term Effects Secondary to Cancer Therapy in Children / Ototoxicity 1 somestatus stop reason just information to hide Not Available Active Not Recruiting Not Available HPV-Mediated (P16-Positive) Oropharyngeal Carcinoma by AJCC V8 Clinical Stage / Oropharyngeal Cancer 1 somestatus stop reason just information to hide Not Available Active Not Recruiting Not Available Malnutrition / Nasopharyngeal Carcinoma (NPC) 1 somestatus stop reason just information to hide Not Available Active Not Recruiting Treatment Esophageal Cancer 1 somestatus stop reason just information to hide Not Available Approved for Marketing Not Available Mesothelioma 1 somestatus stop reason just information to hide
Pharmacoeconomics
- Manufacturers
- App pharmaceuticals llc
- Bedford laboratories div ben venue laboratories inc
- Pharmachemie bv
- Teva parenteral medicines inc
- Bristol myers co
- Packagers
- APP Pharmaceuticals
- APPD
- Baxter International Inc.
- Bedford Labs
- Ben Venue Laboratories Inc.
- Bristol-Myers Squibb Co.
- Mead Johnson and Co.
- Pharmachemie BV
- Sicor Pharmaceuticals
- Teva Pharmaceutical Industries Ltd.
- Dosage Forms
Form Route Strength Solution Intravenous 1.000 mg Solution Intravenous 10.000 mg Injection, powder, lyophilized, for solution Intravenous 50 mg Solution Intravenous 1 mg Solution Parenteral Solution Parenteral 1 mg/mL Injection Parenteral 1 MG/ML Injection 1 MG/ML Injection 1 mg/10ml Injection Intravenous 1 mg/1mL Injection, powder, lyophilized, for solution Intravenous 1 mg/1mL Injection, solution Intravenous 1 mg/1mL Injection, solution Intravenous 100 mg/100mL Injection, solution Intravenous 50 mg/50mL Injection Parenteral Injection, solution, concentrate Intravenous Injection 1 mg Injection, solution 1 mg/mL Injection, solution Intravenous 10 mg/10ml Solution Intravenous 10 mg/20ml Solution Intravenous 100 mg/100ml Injection, solution, concentrate Intravenous 25 mg/50ml Solution Intravenous 50 mg/100ml Injection, solution, concentrate Intravenous 1 mg/ml Liquid Intravenous .5 mg / mL Liquid Intravenous 1 mg / mL Solution Intravenous 1.0 mg / mL Injection Intravenous 1 mg/ml Solution Intravenous 1 mg / mL Injection Intravenous 25 mg/50ml Injection Intravenous 50 mg/100ml Injection Parenteral 1 mg Injection, powder, for suspension Parenteral 10 mg Injection, powder, lyophilized, for solution Parenteral 10 mg Solution Parenteral 10 mg Injection, powder, lyophilized, for solution Parenteral 25 mg Injection, powder, lyophilized, for solution Parenteral 50 mg Injection, solution, concentrate Intravenous; Parenteral 1 MG/ML Injection, solution, concentrate Intravenous 0.5 MG/ML Solution Intravenous 10 mg Solution Parenteral 0.5 mg Solution Intravenous 50 mg Injection, solution Injection, solution, concentrate Intravenous; Parenteral 0.5 MG/ML Injection Intravenous 10 mg Injection, solution Intravenous Solution Intravenous 0.5 mg Injection Intravenous 50 mg Injection 10 mg/20ml Injection 25 mg/50ml Injection 50 mg/100ml Solution Parenteral 50 mg Injection 1 MG/1ML Injection, solution Intravenous 10 mg Injection, solution Intravenous 50 mg Injection, solution, concentrate Intravenous 1 mg/1ml Injection, powder, lyophilized, for solution Intravenous 10 mg Injection, solution Intravenous 1 MG/ML Injection Parenteral 10 mg Injection Parenteral 0.5 mg Injection, powder, for solution Intravenous 10 MG Injection, powder, for solution Intravenous 25 MG Injection, powder, for solution Intravenous 50 MG Powder, for solution Intravenous Injection, powder, lyophilized, for solution Intravenous 10 mg/10mL Injection, powder, lyophilized, for solution Intravenous 50 mg/50mL Injection 0.5 MG/ML Injection, solution, concentrate Intravenous 50 mg/50mL Injection Injection, solution Parenteral 10 MG/20ML Injection, solution Parenteral 25 MG/50ML Injection, solution Parenteral 50 MG/100ML Solution Parenteral 10.000 mg Injection, solution 1 mg/1ml Solution 1 mg/1ml - Prices
Unit description Cost Unit Cisplatin 1 mg/ml vial 0.41USD ml DrugBank does not sell nor buy drugs. Pricing information is supplied for informational purposes only.- Patents
- Not Available
Properties
- State
- Solid
- Experimental Properties
Property Value Source melting point (°C) 270 dec °C PhysProp water solubility 2530 mg/L (at 25 °C) AMUNDSEN,AR & STERN,EW (1982) logP -2.19 HANSCH,C ET AL. (1995) - Predicted Properties
Property Value Source Water Solubility 69.6 mg/mL ALOGPS logP -0.04 ALOGPS logS -0.64 ALOGPS Physiological Charge 0 Chemaxon Hydrogen Acceptor Count 0 Chemaxon Hydrogen Donor Count 0 Chemaxon Polar Surface Area 55.28 Å2 Chemaxon Rotatable Bond Count 0 Chemaxon Refractivity 43.3 m3·mol-1 Chemaxon Polarizability 10.95 Å3 Chemaxon Number of Rings 0 Chemaxon Bioavailability 1 Chemaxon Rule of Five No Chemaxon Ghose Filter No Chemaxon Veber's Rule No Chemaxon MDDR-like Rule No Chemaxon - Predicted ADMET Features
Property Value Probability Human Intestinal Absorption + 0.9637 Blood Brain Barrier + 0.9469 Caco-2 permeable - 0.5704 P-glycoprotein substrate Non-substrate 0.8714 P-glycoprotein inhibitor I Non-inhibitor 0.9763 P-glycoprotein inhibitor II Non-inhibitor 0.9843 Renal organic cation transporter Non-inhibitor 0.9211 CYP450 2C9 substrate Non-substrate 0.8069 CYP450 2D6 substrate Non-substrate 0.7874 CYP450 3A4 substrate Non-substrate 0.7495 CYP450 1A2 substrate Non-inhibitor 0.7733 CYP450 2C9 inhibitor Non-inhibitor 0.7808 CYP450 2D6 inhibitor Non-inhibitor 0.9075 CYP450 2C19 inhibitor Non-inhibitor 0.7995 CYP450 3A4 inhibitor Non-inhibitor 0.8562 CYP450 inhibitory promiscuity Low CYP Inhibitory Promiscuity 0.9204 Ames test Non AMES toxic 0.5661 Carcinogenicity Carcinogens 0.5146 Biodegradation Not ready biodegradable 0.9213 Rat acute toxicity 2.7612 LD50, mol/kg Not applicable hERG inhibition (predictor I) Weak inhibitor 0.9774 hERG inhibition (predictor II) Non-inhibitor 0.9344
Spectra
- Mass Spec (NIST)
- Not Available
- Spectra
- Not Available
- Chromatographic Properties
Collision Cross Sections (CCS)
Not Available
Targets
References
- Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [Article]
- Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [Article]
- Garcia Sar D, Montes-Bayon M, Aguado Ortiz L, Blanco-Gonzalez E, Sierra LM, Sanz-Medel A: In vivo detection of DNA adducts induced by cisplatin using capillary HPLC-ICP-MS and their correlation with genotoxic damage in Drosophila melanogaster. Anal Bioanal Chem. 2008 Jan;390(1):37-44. Epub 2007 Oct 12. [Article]
- Sharma S, Gong P, Temple B, Bhattacharyya D, Dokholyan NV, Chaney SG: Molecular dynamic simulations of cisplatin- and oxaliplatin-d(GG) intrastand cross-links reveal differences in their conformational dynamics. J Mol Biol. 2007 Nov 9;373(5):1123-40. Epub 2007 Aug 23. [Article]
- Bloemink MJ, Reedijk J: Cisplatin and derived anticancer drugs: mechanism and current status of DNA binding. Met Ions Biol Syst. 1996;32:641-85. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Hydrolysis of the deoxyribose N-glycosidic bond to excise 3-methyladenine, and 7-methylguanine from the damaged DNA polymer formed by alkylation lesions
- Specific Function
- alkylbase DNA N-glycosylase activity
- Gene Name
- MPG
- Uniprot ID
- P29372
- Uniprot Name
- DNA-3-methyladenine glycosylase
- Molecular Weight
- 32868.365 Da
References
- Kartalou M, Samson LD, Essigmann JM: Cisplatin adducts inhibit 1,N(6)-ethenoadenine repair by interacting with the human 3-methyladenine DNA glycosylase. Biochemistry. 2000 Jul 11;39(27):8032-8. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Is able to inhibit all four classes of proteinases by a unique 'trapping' mechanism. This protein has a peptide stretch, called the 'bait region' which contains specific cleavage sites for different proteinases. When a proteinase cleaves the bait region, a conformational change is induced in the protein which traps the proteinase. The entrapped enzyme remains active against low molecular weight substrates (activity against high molecular weight substrates is greatly reduced). Following cleavage in the bait region, a thioester bond is hydrolyzed and mediates the covalent binding of the protein to the proteinase
- Specific Function
- brain-derived neurotrophic factor binding
- Gene Name
- A2M
- Uniprot ID
- P01023
- Uniprot Name
- Alpha-2-macroglobulin
- Molecular Weight
- 163289.945 Da
References
- Khalaila I, Bergamo A, Bussy F, Sava G, Dyson PJ: The role of cisplatin and NAMI-A plasma-protein interactions in relation to combination therapy. Int J Oncol. 2006 Jul;29(1):261-8. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Transferrins are iron binding transport proteins which can bind two Fe(3+) ions in association with the binding of an anion, usually bicarbonate. It is responsible for the transport of iron from sites of absorption and heme degradation to those of storage and utilization. Serum transferrin may also have a further role in stimulating cell proliferation
- Specific Function
- enzyme binding
- Gene Name
- TF
- Uniprot ID
- P02787
- Uniprot Name
- Serotransferrin
- Molecular Weight
- 77049.175 Da
References
- Khalaila I, Bergamo A, Bussy F, Sava G, Dyson PJ: The role of cisplatin and NAMI-A plasma-protein interactions in relation to combination therapy. Int J Oncol. 2006 Jul;29(1):261-8. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Curator comments
- Atox1 protein blocks cisplatin transport to DNA and may lead to drug resistance
- General Function
- Binds and deliver cytosolic copper to the copper ATPase proteins. May be important in cellular antioxidant defense
- Specific Function
- copper chaperone activity
- Gene Name
- ATOX1
- Uniprot ID
- O00244
- Uniprot Name
- Copper transport protein ATOX1
- Molecular Weight
- 7401.575 Da
References
- Xi Z, Guo W, Tian C, Wang F, Liu Y: Copper binding modulates the platination of human copper chaperone Atox1 by antitumor trans-platinum complexes. Metallomics. 2014 Mar;6(3):491-7. doi: 10.1039/c3mt00338h. Epub 2014 Jan 28. [Article]
Enzymes
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Inducer
- General Function
- Part of the host defense system of polymorphonuclear leukocytes. It is responsible for microbicidal activity against a wide range of organisms. In the stimulated PMN, MPO catalyzes the production of hypohalous acids, primarily hypochlorous acid in physiologic situations, and other toxic intermediates that greatly enhance PMN microbicidal activity (PubMed:9922160). Mediates the proteolytic cleavage of alpha-1-microglobulin to form t-alpha-1-microglobulin, which potently inhibits oxidation of low-density lipoprotein particles and limits vascular damage (PubMed:25698971)
- Specific Function
- chromatin binding
- Gene Name
- MPO
- Uniprot ID
- P05164
- Uniprot Name
- Myeloperoxidase
- Molecular Weight
- 83867.71 Da
References
- Erdogan S, Tosyali E, Duzguner V, Kucukgul A, Aslantas O, Celik S: Cisplatin reduces Brucella melitensis-infected cell number by inducing apoptosis, oxidant and pro-inflammatory cytokine production. Res Vet Sci. 2010 Apr;88(2):218-26. doi: 10.1016/j.rvsc.2009.09.002. Epub 2009 Oct 8. [Article]
- Ozen S, Akyol O, Iraz M, Sogut S, Ozugurlu F, Ozyurt H, Odaci E, Yildirim Z: Role of caffeic acid phenethyl ester, an active component of propolis, against cisplatin-induced nephrotoxicity in rats. J Appl Toxicol. 2004 Jan-Feb;24(1):27-35. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Inducer
- General Function
- Key enzyme in purine degradation. Catalyzes the oxidation of hypoxanthine to xanthine. Catalyzes the oxidation of xanthine to uric acid. Contributes to the generation of reactive oxygen species. Has also low oxidase activity towards aldehydes (in vitro)
- Specific Function
- 2 iron, 2 sulfur cluster binding
- Gene Name
- XDH
- Uniprot ID
- P47989
- Uniprot Name
- Xanthine dehydrogenase/oxidase
- Molecular Weight
- 146422.99 Da
References
- Yilmaz HR, Sogut S, Ozyurt B, Ozugurlu F, Sahin S, Isik B, Uz E, Ozyurt H: The activities of liver adenosine deaminase, xanthine oxidase, catalase, superoxide dismutase enzymes and the levels of malondialdehyde and nitric oxide after cisplatin toxicity in rats: protective effect of caffeic acid phenethyl ester. Toxicol Ind Health. 2005 May;21(3-4):67-73. [Article]
- Cetin R, Devrim E, Kilicoglu B, Avci A, Candir O, Durak I: Cisplatin impairs antioxidant system and causes oxidation in rat kidney tissues: possible protective roles of natural antioxidant foods. J Appl Toxicol. 2006 Jan-Feb;26(1):42-6. [Article]
- Erdogan S, Tosyali E, Duzguner V, Kucukgul A, Aslantas O, Celik S: Cisplatin reduces Brucella melitensis-infected cell number by inducing apoptosis, oxidant and pro-inflammatory cytokine production. Res Vet Sci. 2010 Apr;88(2):218-26. doi: 10.1016/j.rvsc.2009.09.002. Epub 2009 Oct 8. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Inducer
- General Function
- A cytochrome P450 monooxygenase involved in the metabolism of fatty acids and their oxygenated derivatives (oxylipins) (PubMed:10553002, PubMed:10660572, PubMed:15611369, PubMed:1739747, PubMed:7679927, PubMed:8914854). Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (CPR; NADPH-ferrihemoprotein reductase) (PubMed:10553002, PubMed:10660572, PubMed:15611369, PubMed:1739747, PubMed:7679927, PubMed:8914854). Catalyzes predominantly the oxidation of the terminal carbon (omega-oxidation) of saturated and unsaturated fatty acids, the catalytic efficiency decreasing in the following order: dodecanoic > tetradecanoic > (9Z)-octadecenoic > (9Z,12Z)-octadecadienoic > hexadecanoic acid (PubMed:10553002, PubMed:10660572). Acts as a major omega-hydroxylase for dodecanoic (lauric) acid in liver (PubMed:15611369, PubMed:1739747, PubMed:7679927, PubMed:8914854). Participates in omega-hydroxylation of (5Z,8Z,11Z,14Z)-eicosatetraenoic acid (arachidonate) to 20-hydroxyeicosatetraenoic acid (20-HETE), a signaling molecule acting both as vasoconstrictive and natriuretic with overall effect on arterial blood pressure (PubMed:10620324, PubMed:10660572, PubMed:15611369). Can also catalyze the oxidation of the penultimate carbon (omega-1 oxidation) of fatty acids with lower efficiency (PubMed:7679927). May contribute to the degradation of saturated very long-chain fatty acids (VLCFAs) such as docosanoic acid, by catalyzing successive omega-oxidations to the corresponding dicarboxylic acid, thereby initiating chain shortening (PubMed:18182499). Omega-hydroxylates (9R,10S)-epoxy-octadecanoate stereoisomer (PubMed:15145985). Plays a minor role in omega-oxidation of long-chain 3-hydroxy fatty acids (PubMed:18065749). Has little activity toward prostaglandins A1 and E1 (PubMed:7679927)
- Specific Function
- alkane 1-monooxygenase activity
- Gene Name
- CYP4A11
- Uniprot ID
- Q02928
- Uniprot Name
- Cytochrome P450 4A11
- Molecular Weight
- 59347.31 Da
References
- Nakamura M, Imaoka S, Tanaka E, Misawa S, Funae Y: cis-Diamminedichloroplatinum induces peroxisomes as well as CYP4A1 in rat kidney. Res Commun Mol Pathol Pharmacol. 1998 Jan;99(1):23-32. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Inhibitor
- General Function
- Dual cyclooxygenase and peroxidase in the biosynthesis pathway of prostanoids, a class of C20 oxylipins mainly derived from arachidonate ((5Z,8Z,11Z,14Z)-eicosatetraenoate, AA, C20:4(n-6)), with a particular role in the inflammatory response (PubMed:11939906, PubMed:16373578, PubMed:19540099, PubMed:22942274, PubMed:26859324, PubMed:27226593, PubMed:7592599, PubMed:7947975, PubMed:9261177). The cyclooxygenase activity oxygenates AA to the hydroperoxy endoperoxide prostaglandin G2 (PGG2), and the peroxidase activity reduces PGG2 to the hydroxy endoperoxide prostaglandin H2 (PGH2), the precursor of all 2-series prostaglandins and thromboxanes (PubMed:16373578, PubMed:22942274, PubMed:26859324, PubMed:27226593, PubMed:7592599, PubMed:7947975, PubMed:9261177). This complex transformation is initiated by abstraction of hydrogen at carbon 13 (with S-stereochemistry), followed by insertion of molecular O2 to form the endoperoxide bridge between carbon 9 and 11 that defines prostaglandins. The insertion of a second molecule of O2 (bis-oxygenase activity) yields a hydroperoxy group in PGG2 that is then reduced to PGH2 by two electrons (PubMed:16373578, PubMed:22942274, PubMed:26859324, PubMed:27226593, PubMed:7592599, PubMed:7947975, PubMed:9261177). Similarly catalyzes successive cyclooxygenation and peroxidation of dihomo-gamma-linoleate (DGLA, C20:3(n-6)) and eicosapentaenoate (EPA, C20:5(n-3)) to corresponding PGH1 and PGH3, the precursors of 1- and 3-series prostaglandins (PubMed:11939906, PubMed:19540099). In an alternative pathway of prostanoid biosynthesis, converts 2-arachidonoyl lysophopholipids to prostanoid lysophopholipids, which are then hydrolyzed by intracellular phospholipases to release free prostanoids (PubMed:27642067). Metabolizes 2-arachidonoyl glycerol yielding the glyceryl ester of PGH2, a process that can contribute to pain response (PubMed:22942274). Generates lipid mediators from n-3 and n-6 polyunsaturated fatty acids (PUFAs) via a lipoxygenase-type mechanism. Oxygenates PUFAs to hydroperoxy compounds and then reduces them to corresponding alcohols (PubMed:11034610, PubMed:11192938, PubMed:9048568, PubMed:9261177). Plays a role in the generation of resolution phase interaction products (resolvins) during both sterile and infectious inflammation (PubMed:12391014). Metabolizes docosahexaenoate (DHA, C22:6(n-3)) to 17R-HDHA, a precursor of the D-series resolvins (RvDs) (PubMed:12391014). As a component of the biosynthetic pathway of E-series resolvins (RvEs), converts eicosapentaenoate (EPA, C20:5(n-3)) primarily to 18S-HEPE that is further metabolized by ALOX5 and LTA4H to generate 18S-RvE1 and 18S-RvE2 (PubMed:21206090). In vascular endothelial cells, converts docosapentaenoate (DPA, C22:5(n-3)) to 13R-HDPA, a precursor for 13-series resolvins (RvTs) shown to activate macrophage phagocytosis during bacterial infection (PubMed:26236990). In activated leukocytes, contributes to oxygenation of hydroxyeicosatetraenoates (HETE) to diHETES (5,15-diHETE and 5,11-diHETE) (PubMed:22068350, PubMed:26282205). Can also use linoleate (LA, (9Z,12Z)-octadecadienoate, C18:2(n-6)) as substrate and produce hydroxyoctadecadienoates (HODEs) in a regio- and stereospecific manner, being (9R)-HODE ((9R)-hydroxy-(10E,12Z)-octadecadienoate) and (13S)-HODE ((13S)-hydroxy-(9Z,11E)-octadecadienoate) its major products (By similarity). During neuroinflammation, plays a role in neuronal secretion of specialized preresolving mediators (SPMs) 15R-lipoxin A4 that regulates phagocytic microglia (By similarity)
- Specific Function
- enzyme binding
- Gene Name
- PTGS2
- Uniprot ID
- P35354
- Uniprot Name
- Prostaglandin G/H synthase 2
- Molecular Weight
- 68995.625 Da
References
- Tusgaard B, Norregaard R, Jensen AM, Wang G, Topcu SO, Wang Y, Nielsen S, Frokiaer J: Cisplatin decreases renal cyclooxygenase-2 expression and activity in rats. Acta Physiol (Oxf). 2011 May;202(1):79-90. doi: 10.1111/j.1748-1716.2011.02257.x. Epub 2011 Mar 22. [Article]
- Kind
- Protein
- Organism
- Mycobacterium tuberculosis
- Pharmacological action
- Unknown
- Actions
- Inhibitor
- General Function
- Catalyzes the transfer of the acetyl group from acetyl coenzyme A to the free amino group of arylamines and hydrazines (PubMed:18795795). Is able to utilize not only acetyl-CoA, but also n-propionyl-CoA and acetoacetyl-CoA as acyl donors, although at a lower rate (PubMed:19014350). As acetyl-CoA and propionyl-CoA are products of cholesterol catabolism and the nat gene is likely present in the same operon than genes involved in cholesterol degradation, this enzyme could have a role in the utilization and regulation of these CoA species (PubMed:19014350).
- Specific Function
- arylamine N-acetyltransferase activity
- Gene Name
- nat
- Uniprot ID
- P9WJI5
- Uniprot Name
- Arylamine N-acetyltransferase
- Molecular Weight
- 31028.88 Da
References
- Ragunathan N, Dairou J, Pluvinage B, Martins M, Petit E, Janel N, Dupret JM, Rodrigues-Lima F: Identification of the xenobiotic-metabolizing enzyme arylamine N-acetyltransferase 1 as a new target of cisplatin in breast cancer cells: molecular and cellular mechanisms of inhibition. Mol Pharmacol. 2008 Jun;73(6):1761-8. doi: 10.1124/mol.108.045328. Epub 2008 Feb 29. [Article]
- Holzer AK, Samimi G, Katano K, Naerdemann W, Lin X, Safaei R, Howell SB: The copper influx transporter human copper transport protein 1 regulates the uptake of cisplatin in human ovarian carcinoma cells. Mol Pharmacol. 2004 Oct;66(4):817-23. Epub 2004 Jun 30. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Inhibitor
- General Function
- A cytochrome P450 monooxygenase involved in the metabolism of various endogenous substrates, including fatty acids and steroids (PubMed:12865317, PubMed:15766564, PubMed:19965576, PubMed:21576599, PubMed:7574697, PubMed:9435160, PubMed:9866708). Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (NADPH--hemoprotein reductase) (PubMed:12865317, PubMed:15766564, PubMed:19965576, PubMed:21576599, PubMed:7574697, PubMed:9435160, PubMed:9866708). Catalyzes the epoxidation of double bonds of polyunsaturated fatty acids (PUFA) (PubMed:15766564, PubMed:19965576, PubMed:7574697, PubMed:9866708). Catalyzes the hydroxylation of carbon-hydrogen bonds. Metabolizes cholesterol toward 25-hydroxycholesterol, a physiological regulator of cellular cholesterol homeostasis (PubMed:21576599). Exhibits low catalytic activity for the formation of catechol estrogens from 17beta-estradiol (E2) and estrone (E1), namely 2-hydroxy E1 and E2 (PubMed:12865317). Catalyzes bisallylic hydroxylation and hydroxylation with double-bond migration of polyunsaturated fatty acids (PUFA) (PubMed:9435160, PubMed:9866708). Also metabolizes plant monoterpenes such as limonene. Oxygenates (R)- and (S)-limonene to produce carveol and perillyl alcohol (PubMed:11950794). Contributes to the wide pharmacokinetics variability of the metabolism of drugs such as S-warfarin, diclofenac, phenytoin, tolbutamide and losartan (PubMed:25994031)
- Specific Function
- (R)-limonene 6-monooxygenase activity
- Gene Name
- CYP2C9
- Uniprot ID
- P11712
- Uniprot Name
- Cytochrome P450 2C9
- Molecular Weight
- 55627.365 Da
References
- Masek V, Anzenbacherova E, Machova M, Brabec V, Anzenbacher P: Interaction of antitumor platinum complexes with human liver microsomal cytochromes P450. Anticancer Drugs. 2009 Jun;20(5):305-11. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Inhibitor
- General Function
- A cytochrome P450 monooxygenase involved in the metabolism of endocannabinoids and steroids (PubMed:12865317, PubMed:21289075). Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (NADPH--hemoprotein reductase). Catalyzes the epoxidation of double bonds of arachidonoylethanolamide (anandamide) to 8,9-, 11,12-, and 14,15-epoxyeicosatrienoic acid ethanolamides (EpETrE-EAs), potentially modulating endocannabinoid system signaling (PubMed:21289075). Hydroxylates steroid hormones, including testosterone at C-16 and estrogens at C-2 (PubMed:12865317, PubMed:21289075). Plays a role in the oxidative metabolism of xenobiotics, including plant lipids and drugs (PubMed:11695850, PubMed:22909231). Acts as a 1,4-cineole 2-exo-monooxygenase (PubMed:11695850)
- Specific Function
- anandamide 11,12 epoxidase activity
- Gene Name
- CYP2B6
- Uniprot ID
- P20813
- Uniprot Name
- Cytochrome P450 2B6
- Molecular Weight
- 56277.81 Da
References
- Masek V, Anzenbacherova E, Machova M, Brabec V, Anzenbacher P: Interaction of antitumor platinum complexes with human liver microsomal cytochromes P450. Anticancer Drugs. 2009 Jun;20(5):305-11. [Article]
- Walsky RL, Astuccio AV, Obach RS: Evaluation of 227 drugs for in vitro inhibition of cytochrome P450 2B6. J Clin Pharmacol. 2006 Dec;46(12):1426-38. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Inhibitor
- General Function
- Esterase with broad substrate specificity. Contributes to the inactivation of the neurotransmitter acetylcholine. Can degrade neurotoxic organophosphate esters
- Specific Function
- acetylcholinesterase activity
- Gene Name
- BCHE
- Uniprot ID
- P06276
- Uniprot Name
- Cholinesterase
- Molecular Weight
- 68417.575 Da
References
- Bodur E: Human serum butyrylcholinesterase interactions with cisplatin and cyclophosphamide. Biochimie. 2010 Aug;92(8):979-84. doi: 10.1016/j.biochi.2010.04.010. Epub 2010 Apr 24. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Substrate
- General Function
- Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Acts on 1,2-epoxy-3-(4-nitrophenoxy)propane, phenethylisothiocyanate 4-nitrobenzyl chloride and 4-nitrophenethyl bromide. Displays glutathione peroxidase activity with cumene hydroperoxide
- Specific Function
- glutathione peroxidase activity
- Gene Name
- GSTT1
- Uniprot ID
- P30711
- Uniprot Name
- Glutathione S-transferase theta-1
- Molecular Weight
- 27334.755 Da
References
- Peters U, Preisler-Adams S, Hebeisen A, Hahn M, Seifert E, Lanvers C, Heinecke A, Horst J, Jurgens H, Lamprecht-Dinnesen A: Glutathione S-transferase genetic polymorphisms and individual sensitivity to the ototoxic effect of cisplatin. Anticancer Drugs. 2000 Sep;11(8):639-43. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Substrate
- General Function
- Metallothioneins have a high content of cysteine residues that bind various heavy metals; these proteins are transcriptionally regulated by both heavy metals and glucocorticoids
- Specific Function
- metal ion binding
- Gene Name
- MT1A
- Uniprot ID
- P04731
- Uniprot Name
- Metallothionein-1A
- Molecular Weight
- 6120.19 Da
References
- Meijer C, Timmer A, De Vries EG, Groten JP, Knol A, Zwart N, Dam WA, Sleijfer DT, Mulder NH: Role of metallothionein in cisplatin sensitivity of germ-cell tumours. Int J Cancer. 2000 Mar 15;85(6):777-81. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Substrate
- General Function
- Metallothioneins have a high content of cysteine residues that bind various heavy metals; these proteins are transcriptionally regulated by both heavy metals and glucocorticoids
- Specific Function
- metal ion binding
- Gene Name
- MT2A
- Uniprot ID
- P02795
- Uniprot Name
- Metallothionein-2
- Molecular Weight
- 6042.05 Da
References
- Meijer C, Timmer A, De Vries EG, Groten JP, Knol A, Zwart N, Dam WA, Sleijfer DT, Mulder NH: Role of metallothionein in cisplatin sensitivity of germ-cell tumours. Int J Cancer. 2000 Mar 15;85(6):777-81. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Substrate
- General Function
- Destroys radicals which are normally produced within the cells and which are toxic to biological systems
- Specific Function
- copper ion binding
- Gene Name
- SOD1
- Uniprot ID
- P00441
- Uniprot Name
- Superoxide dismutase [Cu-Zn]
- Molecular Weight
- 15935.685 Da
References
- Link [Link]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Substrate
- General Function
- Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Involved in the formation of glutathione conjugates of both prostaglandin A2 (PGA2) and prostaglandin J2 (PGJ2) (PubMed:9084911). Participates in the formation of novel hepoxilin regioisomers (PubMed:21046276). Negatively regulates CDK5 activity via p25/p35 translocation to prevent neurodegeneration
- Specific Function
- dinitrosyl-iron complex binding
- Gene Name
- GSTP1
- Uniprot ID
- P09211
- Uniprot Name
- Glutathione S-transferase P
- Molecular Weight
- 23355.625 Da
References
- Peters U, Preisler-Adams S, Hebeisen A, Hahn M, Seifert E, Lanvers C, Heinecke A, Horst J, Jurgens H, Lamprecht-Dinnesen A: Glutathione S-transferase genetic polymorphisms and individual sensitivity to the ototoxic effect of cisplatin. Anticancer Drugs. 2000 Sep;11(8):639-43. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Substrate
- General Function
- Flavin-containing quinone reductase that catalyzes two-electron reduction of quinones to hydroquinones using either NADH or NADPH as electron donors. In a ping-pong kinetic mechanism, the electrons are sequentially transferred from NAD(P)H to flavin cofactor and then from reduced flavin to the quinone, bypassing the formation of semiquinone and reactive oxygen species (By similarity) (PubMed:8999809, PubMed:9271353). Regulates cellular redox state primarily through quinone detoxification. Reduces components of plasma membrane redox system such as coenzyme Q and vitamin quinones, producing antioxidant hydroquinone forms. In the process may function as superoxide scavenger to prevent hydroquinone oxidation and facilitate excretion (PubMed:15102952, PubMed:8999809, PubMed:9271353). Alternatively, can activate quinones and their derivatives by generating redox reactive hydroquinones with DNA cross-linking antitumor potential (PubMed:8999809). Acts as a gatekeeper of the core 20S proteasome known to degrade proteins with unstructured regions. Upon oxidative stress, interacts with tumor suppressors TP53 and TP73 in a NADH-dependent way and inhibits their ubiquitin-independent degradation by the 20S proteasome (PubMed:15687255, PubMed:28291250)
- Specific Function
- cytochrome-b5 reductase activity, acting on NAD(P)H
- Gene Name
- NQO1
- Uniprot ID
- P15559
- Uniprot Name
- NAD(P)H dehydrogenase [quinone] 1
- Molecular Weight
- 30867.405 Da
References
- Link [Link]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Substrate
- General Function
- Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Involved in the formation of glutathione conjugates of both prostaglandin A2 (PGA2) and prostaglandin J2 (PGJ2) (PubMed:9084911). Participates in the formation of novel hepoxilin regioisomers (PubMed:21046276)
- Specific Function
- enzyme binding
- Gene Name
- GSTM1
- Uniprot ID
- P09488
- Uniprot Name
- Glutathione S-transferase Mu 1
- Molecular Weight
- 25711.555 Da
References
- Peters U, Preisler-Adams S, Hebeisen A, Hahn M, Seifert E, Lanvers C, Heinecke A, Horst J, Jurgens H, Lamprecht-Dinnesen A: Glutathione S-transferase genetic polymorphisms and individual sensitivity to the ototoxic effect of cisplatin. Anticancer Drugs. 2000 Sep;11(8):639-43. [Article]
Carriers
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- 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 (PubMed: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 (PubMed:6234017). Does not prevent iron uptake by the bacterial siderophore aerobactin (PubMed:6234017)
- Specific Function
- antioxidant activity
- Gene Name
- ALB
- Uniprot ID
- P02768
- Uniprot Name
- Albumin
- Molecular Weight
- 69365.94 Da
References
- Khalaila I, Bergamo A, Bussy F, Sava G, Dyson PJ: The role of cisplatin and NAMI-A plasma-protein interactions in relation to combination therapy. Int J Oncol. 2006 Jul;29(1):261-8. [Article]
Transporters
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Inducer
- General Function
- ATP-dependent transporter of the ATP-binding cassette (ABC) family that binds and hydrolyzes ATP to enable active transport of various substrates including many drugs, toxicants and endogenous compound across cell membranes (PubMed:10359813, PubMed:11581266, PubMed:15083066). Transports glucuronide conjugates such as bilirubin diglucuronide, estradiol-17-beta-o-glucuronide and GSH conjugates such as leukotriene C4 (LTC4) (PubMed:11581266, PubMed:15083066). Transports also various bile salts (taurocholate, glycocholate, taurochenodeoxycholate-3-sulfate, taurolithocholate- 3-sulfate) (By similarity). Does not contribute substantially to bile salt physiology but provides an alternative route for the export of bile acids and glucuronides from cholestatic hepatocytes (By similarity). May contribute to regulate the transport of organic compounds in testes across the blood-testis-barrier (Probable). Can confer resistance to various anticancer drugs, methotrexate, tenoposide and etoposide, by decreasing accumulation of these drugs in cells (PubMed:10359813, PubMed:11581266)
- Specific Function
- ABC-type bile acid transporter activity
- Gene Name
- ABCC3
- Uniprot ID
- O15438
- Uniprot Name
- ATP-binding cassette sub-family C member 3
- Molecular Weight
- 169341.14 Da
References
- Schrenk D, Baus PR, Ermel N, Klein C, Vorderstemann B, Kauffmann HM: Up-regulation of transporters of the MRP family by drugs and toxins. Toxicol Lett. 2001 Mar 31;120(1-3):51-7. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Inducer
- General Function
- ATP-dependent transporter of the ATP-binding cassette (ABC) family that actively extrudes physiological compounds, and xenobiotics from cells. Mediates ATP-dependent transport of endogenous metabolites such as cAMP and cGMP, folic acid and N-lactoyl-amino acids (in vitro) (PubMed:10893247, PubMed:12637526, PubMed:12695538, PubMed:15899835, PubMed:17229149, PubMed:25964343). Acts also as a general glutamate conjugate and analog transporter that can limit the brain levels of endogenous metabolites, drugs, and toxins (PubMed:26515061). Confers resistance to the antiviral agent PMEA (PubMed:12695538). Able to transport several anticancer drugs including methotrexate, and nucleotide analogs in vitro, however it does with low affinity, thus the exact role of ABCC5 in mediating resistance still needs to be elucidated (PubMed:10840050, PubMed:12435799, PubMed:12695538, PubMed:15899835). Acts as a heme transporter required for the translocation of cytosolic heme to the secretory pathway (PubMed:24836561). May play a role in energy metabolism by regulating the glucagon-like peptide 1 (GLP-1) secretion from enteroendocrine cells (By similarity)
- Specific Function
- ABC-type xenobiotic transporter activity
- Gene Name
- ABCC5
- Uniprot ID
- O15440
- Uniprot Name
- ATP-binding cassette sub-family C member 5
- Molecular Weight
- 160658.8 Da
References
- Schrenk D, Baus PR, Ermel N, Klein C, Vorderstemann B, Kauffmann HM: Up-regulation of transporters of the MRP family by drugs and toxins. Toxicol Lett. 2001 Mar 31;120(1-3):51-7. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Inducer
- General Function
- ATP-dependent transporter of the ATP-binding cassette (ABC) family that binds and hydrolyzes ATP to enable active transport of various substrates including many drugs, toxicants and endogenous compound across cell membranes. Transports a wide variety of conjugated organic anions such as sulfate-, glucuronide- and glutathione (GSH)-conjugates of endo- and xenobiotics substrates (PubMed:10220572, PubMed:10421658, PubMed:11500505, PubMed:16332456). Mediates hepatobiliary excretion of mono- and bis-glucuronidated bilirubin molecules and therefore play an important role in bilirubin detoxification (PubMed:10421658). Mediates also hepatobiliary excretion of others glucuronide conjugates such as 17beta-estradiol 17-glucosiduronic acid and leukotriene C4 (PubMed:11500505). Transports sulfated bile salt such as taurolithocholate sulfate (PubMed:16332456). Transports various anticancer drugs, such as anthracycline, vinca alkaloid and methotrexate and HIV-drugs such as protease inhibitors (PubMed:10220572, PubMed:11500505, PubMed:12441801). Confers resistance to several anti-cancer drugs including cisplatin, doxorubicin, epirubicin, methotrexate, etoposide and vincristine (PubMed:10220572, PubMed:11500505)
- Specific Function
- ABC-type glutathione S-conjugate transporter activity
- Gene Name
- ABCC2
- Uniprot ID
- Q92887
- Uniprot Name
- ATP-binding cassette sub-family C member 2
- Molecular Weight
- 174205.64 Da
References
- Schrenk D, Baus PR, Ermel N, Klein C, Vorderstemann B, Kauffmann HM: Up-regulation of transporters of the MRP family by drugs and toxins. Toxicol Lett. 2001 Mar 31;120(1-3):51-7. [Article]
- Demeule M, Brossard M, Beliveau R: Cisplatin induces renal expression of P-glycoprotein and canalicular multispecific organic anion transporter. Am J Physiol. 1999 Dec;277(6 Pt 2):F832-40. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- SubstrateInhibitor
- General Function
- Electrogenic voltage-dependent transporter that mediates the transport of a variety of organic cations such as endogenous bioactive amines, cationic drugs and xenobiotics (PubMed:9260930, PubMed:9687576). Functions as a Na(+)-independent, bidirectional uniporter (PubMed:21128598, PubMed:9687576). Cation cellular uptake or release is driven by the electrochemical potential, i.e. membrane potential and concentration gradient (PubMed:15212162, PubMed:9260930, PubMed:9687576). However, may also engage electroneutral cation exchange when saturating concentrations of cation substrates are reached (By similarity). Predominantly expressed at the basolateral membrane of hepatocytes and proximal tubules and involved in the uptake and disposition of cationic compounds by hepatic and renal clearance from the blood flow (PubMed:15783073). Implicated in monoamine neurotransmitters uptake such as histamine, dopamine, adrenaline/epinephrine, noradrenaline/norepinephrine, serotonin and tyramine, thereby supporting a physiological role in the central nervous system by regulating interstitial concentrations of neurotransmitters (PubMed:16581093, PubMed:17460754, PubMed:9687576). Also capable of transporting dopaminergic neuromodulators cyclo(his-pro), salsolinol and N-methyl-salsolinol, thereby involved in the maintenance of dopaminergic cell integrity in the central nervous system (PubMed:17460754). Mediates the bidirectional transport of acetylcholine (ACh) at the apical membrane of ciliated cell in airway epithelium, thereby playing a role in luminal release of ACh from bronchial epithelium (PubMed:15817714). Also transports guanidine and endogenous monoamines such as vitamin B1/thiamine, creatinine and N-1-methylnicotinamide (NMN) (PubMed:12089365, PubMed:15212162, PubMed:17072098, PubMed:24961373, PubMed:9260930). Mediates the uptake and efflux of quaternary ammonium compound choline (PubMed:9260930). Mediates the bidirectional transport of polyamine agmatine and the uptake of polyamines putrescine and spermidine (PubMed:12538837, PubMed:21128598). Able to transport non-amine endogenous compounds such as prostaglandin E2 (PGE2) and prostaglandin F2-alpha (PGF2-alpha) (PubMed:11907186). Also involved in the uptake of xenobiotic 4-(4-(dimethylamino)styryl)-N-methylpyridinium (ASP) (PubMed:12395288, PubMed:16394027). May contribute to regulate the transport of organic compounds in testis across the blood-testis-barrier (Probable)
- Specific Function
- acetylcholine transmembrane transporter activity
- Gene Name
- SLC22A2
- Uniprot ID
- O15244
- Uniprot Name
- Solute carrier family 22 member 2
- Molecular Weight
- 62579.99 Da
References
- Pan BF, Sweet DH, Pritchard JB, Chen R, Nelson JA: A transfected cell model for the renal toxin transporter, rOCT2. Toxicol Sci. 1999 Feb;47(2):181-6. [Article]
- Burger H, Zoumaro-Djayoon A, Boersma AW, Helleman J, Berns EM, Mathijssen RH, Loos WJ, Wiemer EA: Differential transport of platinum compounds by the human organic cation transporter hOCT2 (hSLC22A2). Br J Pharmacol. 2010 Feb;159(4):898-908. doi: 10.1111/j.1476-5381.2009.00569.x. Epub 2010 Jan 8. [Article]
- Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Substrate
- General Function
- Uniporter that mediates the transport of copper(1+) from the extracellular space to the cytoplasm, across the plasma membrane (PubMed:11734551, PubMed:16135512, PubMed:17525160, PubMed:19740744, PubMed:20451502, PubMed:20569931, PubMed:23658018) and delivers directly copper(1+) to specific chaperone such as ATOX1, via a copper(1+)- mediated transient interaction between the C-terminal domain and a copper(1+) chaperone, thus controlling intracellular copper(1+) levels (PubMed:11734551, PubMed:16135512, PubMed:17525160, PubMed:19740744, PubMed:20451502, PubMed:20569931, PubMed:23658018, PubMed:26745413). May function in copper(1+) import from the apical membrane thus may drive intestinal copper absorption (By similarity). The copper(1+) transport mechanism is sodium-independent, saturable and of high-affinity (PubMed:11734551). Also mediates the uptake of silver(1+) (PubMed:20569931). May function in the influx of the platinum-containing chemotherapeutic agents (PubMed:20451502, PubMed:20569931). The platinum-containing chemotherapeutic agents uptake is saturable (By similarity). In vitro, mediates the transport of cadmium(2+) into cells (PubMed:33294387). Also participates in the first step of copper(2+) acquisition by cells through a direct transfer of copper(2+) from copper(2+) carriers in blood, such as ALB to the N-terminal domain of SLC31A1, leading to copper(2+) reduction and probably followed by copper(1+) stabilization (PubMed:30489586). In addition, functions as a redox sensor to promote angiogenesis in endothelial cells, in a copper(1+) transport independent manner, by transmitting the VEGF-induced ROS signal through a sulfenylation at Cys-189 leadin g to a subsequent disulfide bond formation between SLC31A1 and KDR (PubMed:35027734). The SLC31A1-KDR complex is then co-internalized to early endosomes, driving a sustained VEGFR2 signaling (PubMed:35027734)
- Specific Function
- copper ion binding
- Gene Name
- SLC31A1
- Uniprot ID
- O15431
- Uniprot Name
- High affinity copper uptake protein 1
- Molecular Weight
- 21090.545 Da
References
- Howell SB, Safaei R, Larson CA, Sailor MJ: Copper transporters and the cellular pharmacology of the platinum-containing cancer drugs. Mol Pharmacol. 2010 Jun;77(6):887-94. doi: 10.1124/mol.109.063172. Epub 2010 Feb 16. [Article]
- Kurokawa T, He G, Siddik ZH: Protein kinase inhibitors emodin and dichloro-ribofuranosylbenzimidazole modulate the cellular accumulation and cytotoxicity of cisplatin in a schedule-dependent manner. Cancer Chemother Pharmacol. 2010 Feb;65(3):427-36. doi: 10.1007/s00280-009-1045-2. Epub 2009 Jun 16. [Article]
- Jandial DD, Farshchi-Heydari S, Larson CA, Elliott GI, Wrasidlo WJ, Howell SB: Enhanced delivery of cisplatin to intraperitoneal ovarian carcinomas mediated by the effects of bortezomib on the human copper transporter 1. Clin Cancer Res. 2009 Jan 15;15(2):553-60. doi: 10.1158/1078-0432.CCR-08-2081. [Article]
- Liang ZD, Stockton D, Savaraj N, Tien Kuo M: Mechanistic comparison of human high-affinity copper transporter 1-mediated transport between copper ion and cisplatin. Mol Pharmacol. 2009 Oct;76(4):843-53. doi: 10.1124/mol.109.056416. Epub 2009 Jul 1. [Article]
- Rabik CA, Maryon EB, Kasza K, Shafer JT, Bartnik CM, Dolan ME: Role of copper transporters in resistance to platinating agents. Cancer Chemother Pharmacol. 2009 Jun;64(1):133-42. doi: 10.1007/s00280-008-0860-1. Epub 2008 Nov 8. [Article]
- Pabla N, Murphy RF, Liu K, Dong Z: The copper transporter Ctr1 contributes to cisplatin uptake by renal tubular cells during cisplatin nephrotoxicity. Am J Physiol Renal Physiol. 2009 Mar;296(3):F505-11. doi: 10.1152/ajprenal.90545.2008. Epub 2009 Jan 14. [Article]
- Furukawa T, Komatsu M, Ikeda R, Tsujikawa K, Akiyama S: Copper transport systems are involved in multidrug resistance and drug transport. Curr Med Chem. 2008;15(30):3268-78. [Article]
- Holzer AK, Samimi G, Katano K, Naerdemann W, Lin X, Safaei R, Howell SB: The copper influx transporter human copper transport protein 1 regulates the uptake of cisplatin in human ovarian carcinoma cells. Mol Pharmacol. 2004 Oct;66(4):817-23. Epub 2004 Jun 30. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Substrate
- General Function
- Does not function as a copper(1+) importer in vivo (By similarity). However, in vitro functions as a low-affinity copper(1+) importer (PubMed:17617060, PubMed:17944601). Regulator of SLC31A1 which facilitates the cleavage of the SLC31A1 ecto-domain or which stabilizes the truncated form of SLC31A1 (Truncated CTR1 form), thereby drives the SLC31A1 truncated form-dependent endosomal copper export and modulates the copper and cisplatin accumulation via SLC31A1 (By similarity)
- Specific Function
- copper ion transmembrane transporter activity
- Gene Name
- SLC31A2
- Uniprot ID
- O15432
- Uniprot Name
- Protein SLC31A2
- Molecular Weight
- 15681.29 Da
References
- Blair BG, Larson CA, Safaei R, Howell SB: Copper transporter 2 regulates the cellular accumulation and cytotoxicity of Cisplatin and Carboplatin. Clin Cancer Res. 2009 Jul 1;15(13):4312-21. doi: 10.1158/1078-0432.CCR-09-0311. Epub 2009 Jun 9. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Substrate
- General Function
- ATP-dependent transporter of the ATP-binding cassette (ABC) family that actively extrudes physiological compounds, and xenobiotics from cells. Mediates ATP-dependent transport of glutathione conjugates such as leukotriene-c4 (LTC4) and N-ethylmaleimide S-glutathione (NEM-GS) (in vitro), and an anionic cyclopentapeptide endothelin antagonist, BQ-123 (PubMed:11880368, PubMed:12414644). May contribute to regulate the transport of organic compounds in testes across the blood-testis-barrier (Probable). Does not appear to actively transport drugs outside the cell. Confers low levels of cellular resistance to etoposide, teniposide, anthracyclines and cisplatin (PubMed:12414644)
- Specific Function
- ABC-type glutathione S-conjugate transporter activity
- Gene Name
- ABCC6
- Uniprot ID
- O95255
- Uniprot Name
- ATP-binding cassette sub-family C member 6
- Molecular Weight
- 164904.81 Da
References
- Belinsky MG, Chen ZS, Shchaveleva I, Zeng H, Kruh GD: Characterization of the drug resistance and transport properties of multidrug resistance protein 6 (MRP6, ABCC6). Cancer Res. 2002 Nov 1;62(21):6172-7. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Substrate
- General Function
- Copper ion transmembrane transporter involved in the export of copper out of the cells. It is involved in copper homeostasis in the liver, where it ensures the efflux of copper from hepatocytes into the bile in response to copper overload
- Specific Function
- ATP binding
- Gene Name
- ATP7B
- Uniprot ID
- P35670
- Uniprot Name
- Copper-transporting ATPase 2
- Molecular Weight
- 157261.34 Da
References
- Rabik CA, Maryon EB, Kasza K, Shafer JT, Bartnik CM, Dolan ME: Role of copper transporters in resistance to platinating agents. Cancer Chemother Pharmacol. 2009 Jun;64(1):133-42. doi: 10.1007/s00280-008-0860-1. Epub 2008 Nov 8. [Article]
- Mangala LS, Zuzel V, Schmandt R, Leshane ES, Halder JB, Armaiz-Pena GN, Spannuth WA, Tanaka T, Shahzad MM, Lin YG, Nick AM, Danes CG, Lee JW, Jennings NB, Vivas-Mejia PE, Wolf JK, Coleman RL, Siddik ZH, Lopez-Berestein G, Lutsenko S, Sood AK: Therapeutic Targeting of ATP7B in Ovarian Carcinoma. Clin Cancer Res. 2009 Jun 1;15(11):3770-80. doi: 10.1158/1078-0432.CCR-08-2306. Epub 2009 May 26. [Article]
- Furukawa T, Komatsu M, Ikeda R, Tsujikawa K, Akiyama S: Copper transport systems are involved in multidrug resistance and drug transport. Curr Med Chem. 2008;15(30):3268-78. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Substrate
- General Function
- ATP-driven copper (Cu(+)) ion pump that plays an important role in intracellular copper ion homeostasis (PubMed:10419525, PubMed:11092760, PubMed:28389643). Within a catalytic cycle, acquires Cu(+) ion from donor protein on the cytoplasmic side of the membrane and delivers it to acceptor protein on the lumenal side. The transfer of Cu(+) ion across the membrane is coupled to ATP hydrolysis and is associated with a transient phosphorylation that shifts the pump conformation from inward-facing to outward-facing state (PubMed:10419525, PubMed:19453293, PubMed:19917612, PubMed:28389643, PubMed:31283225). Under physiological conditions, at low cytosolic copper concentration, it is localized at the trans-Golgi network (TGN) where it transfers Cu(+) ions to cuproenzymes of the secretory pathway (PubMed:11092760, PubMed:28389643). Upon elevated cytosolic copper concentrations, it relocalizes to the plasma membrane where it is responsible for the export of excess Cu(+) ions (PubMed:10419525, PubMed:28389643). May play a dual role in neuron function and survival by regulating cooper efflux and neuronal transmission at the synapse as well as by supplying Cu(+) ions to enzymes such as PAM, TYR and SOD3 (By similarity) (PubMed:28389643). In the melanosomes of pigmented cells, provides copper cofactor to TYR to form an active TYR holoenzyme for melanin biosynthesis (By similarity)
- Specific Function
- ATP binding
- Gene Name
- ATP7A
- Uniprot ID
- Q04656
- Uniprot Name
- Copper-transporting ATPase 1
- Molecular Weight
- 163371.335 Da
References
- Rabik CA, Maryon EB, Kasza K, Shafer JT, Bartnik CM, Dolan ME: Role of copper transporters in resistance to platinating agents. Cancer Chemother Pharmacol. 2009 Jun;64(1):133-42. doi: 10.1007/s00280-008-0860-1. Epub 2008 Nov 8. [Article]
- Furukawa T, Komatsu M, Ikeda R, Tsujikawa K, Akiyama S: Copper transport systems are involved in multidrug resistance and drug transport. Curr Med Chem. 2008;15(30):3268-78. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Substrate
- General Function
- 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 (PubMed:11306452, PubMed:12958161, PubMed:19506252, PubMed:20705604, PubMed:28554189, PubMed:30405239, PubMed: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 (PubMed:20705604, PubMed:23189181). Also mediates the efflux of sphingosine-1-P from cells (PubMed:20110355). Acts as a urate exporter functioning in both renal and extrarenal urate excretion (PubMed:19506252, PubMed:20368174, PubMed:22132962, PubMed:31003562, PubMed: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 (PubMed:12682043, PubMed:28554189, PubMed: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 (PubMed:11306452, PubMed:12477054, PubMed:15670731, PubMed:18056989, PubMed: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)
- Specific Function
- ABC-type xenobiotic transporter activity
- Gene Name
- ABCG2
- Uniprot ID
- Q9UNQ0
- Uniprot Name
- Broad substrate specificity ATP-binding cassette transporter ABCG2
- Molecular Weight
- 72313.47 Da
References
- Ceckova M, Vackova Z, Radilova H, Libra A, Buncek M, Staud F: Effect of ABCG2 on cytotoxicity of platinum drugs: interference of EGFP. Toxicol In Vitro. 2008 Dec;22(8):1846-52. doi: 10.1016/j.tiv.2008.09.001. Epub 2008 Sep 9. [Article]
Drug created at June 13, 2005 13:24 / Updated at October 29, 2024 18:02