ArticleThe Journal of pharmacology and experimental therapeutics2013
Substrate-dependent inhibition of human MATE1 by cationic ionic liquids.
Article in The Journal of pharmacology and experimental therapeutics, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 44 citations in OpenAlex.
- Substrate Specificity of the Organic Cation Transporters MATE1 and MATE2K and Functional Overlap with OCT1 and OCT2.Journal of medicinal chemistry · 2025Article
- Computational Approaches for Predicting Drug Interactions with Human Organic Anion Transporter 4 (OAT4).Molecular pharmaceutics · 2025Article
- Characterization of Human Organic Anion Transporter 4 (hOAT4) and Mouse Oat5 (mOat5) As Functional Orthologs for Renal Anion Uptake and Efflux Transport.The Journal of pharmacology and experimental therapeutics · 2024Article
- The Competitive Counterflow Assay for Identifying Drugs Transported by Solute Carriers: Principle, Applications, Challenges/Limits, and Perspectives.European journal of drug metabolism and pharmacokinetics · 2024Review
- Interaction and Transport of Benzalkonium Chlorides by the Organic Cation and Multidrug and Toxin Extrusion Transporters.Drug metabolism and disposition: the biological fate of chemicals · 2024Article
- Interaction of ALK Inhibitors with Polyspecific Organic Cation Transporters and the Impact of Substrate-Dependent Inhibition on the Prediction of Drug-Drug Interactions.Pharmaceutics · 2023Article
- Kidney Drug Transporters in Pharmacotherapy.International journal of molecular sciences · 2023Review
- Substrate-DependentInternational journal of molecular sciences · 2021Article
- Characterization ofMolecular pharmacology · 2020Article
- Current Advances in Studying Clinically Relevant Transporters of the Solute Carrier (SLC) Family by Connecting Computational Modeling and Data Science.Computational and structural biotechnology journal · 2019Review
- Molecular Modeling of Drug-Transporter Interactions-An International Transporter Consortium Perspective.Clinical pharmacology and therapeutics · 2018Review
- Ligand-dependent modulation of hOCT1 transport reveals discrete ligand binding sites within the substrate translocation channel.Biochemical pharmacology · 2018Article
- Effect of tyrosine kinase inhibitors on renal handling of creatinine by MATE1.Scientific reports · 2018Article
- Physiologically Based Pharmacokinetic (PBPK) Modeling of Pitavastatin and Atorvastatin to Predict Drug-Drug Interactions (DDIs).European journal of drug metabolism and pharmacokinetics · 2017Article
- Inhibition of Human Drug Transporter Activities by the Pyrethroid Pesticides Allethrin and Tetramethrin.PloS one · 2017Article
- Impact of Substrate-Dependent Inhibition on Renal Organic Cation Transporters hOCT2 and hMATE1/2-K-Mediated Drug Transport and Intracellular Accumulation.The Journal of pharmacology and experimental therapeutics · 2016Article
- Lack of Influence of Substrate on Ligand Interaction with the Human Multidrug and Toxin Extruder, MATE1.Molecular pharmacology · 2016Article
- Renal drug transporters and their significance in drug-drug interactions.Acta pharmaceutica Sinica. B · 2016Review
- Combinatorial Pharmacophore Modeling of Multidrug and Toxin Extrusion Transporter 1 Inhibitors: a Theoretical Perspective for Understanding Multiple Inhibitory Mechanisms.Scientific reports · 2015Article
- Common drugs inhibit human organic cation transporter 1 (OCT1)-mediated neurotransmitter uptake.Drug metabolism and disposition: the biological fate of chemicals · 2014Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The multidrug and toxin extruders 1- and 2-K (MATE1 and MATE2-K) are expressed in the luminal membrane of renal proximal tubule cells and provide the active step in the secretion of molecules that carry a net positive charge at physiologic pH, so-called organic cations. The present study tested whether structurally distinct MATE substrates can display different quantitative profiles of inhibition when interacting with structurally distinct ligands. The tested ligands were three structurally similar cationic ionic liquids (ILs, salts in the liquid state: N-butylpyridinium, NBuPy; 1-methyl-3-butylimidazolium, Bmim; and N-butyl-N-methylpyrrolidinium, BmPy). Uptake was measured using Chinese hamster ovary cells that stably expressed MATE1 or MATE2-K. By trans-stimulation, all three ILs were transported by both MATE transporters. The three ILs also inhibited uptake of three structurally distinct MATE substrates: 1-methyl-4-phenylpyridinium (MPP), triethylmethylammonium (TEMA), and N,N,N-trimethyl-2-[methyl(7-nitrobenzo[c][1,2,5]oxadiazol-4-yl)amino]ethanaminium (NBD-MTMA). MATE1 displayed a higher affinity for the pyridinium-based NBuPy (IC50 values, 2-4 µM) than for either the pyrrolidinium- (BmPy; 20-70 µM) or imidazolium-based ILs (Bmim; 15-60 µM). Inhibition of MPP, TEMA, and NBD-MTMA transport by NBuPy was competitive, with comparable Ki values against all substrates. Bmim also competitively blocked the three substrates but with Ki values that differed significantly (20 µM against MPP and 30 µM against NBD-MTMA versus 60 µM against TEMA). Together, these data indicate that renal secretion of ILs by the human kidney involves MATE transporters and suggest that the mechanism of transport inhibition is ligand-dependent, supporting the hypothesis that the binding of substrates to MATE transporters involves interaction with a binding surface with multiple binding sites.
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