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Solute carrier family 47, member 2

hMATE2-K, MATE2-K, H+/organic cation antiporter, SLC47A2
This gene encodes a protein belonging to a family of transporters involved in excretion of toxic electrolytes, both endogenous and exogenous, through urine and bile. This transporter family shares homology with the bacterial MATE (multidrug and toxin extrusion) protein family responsible for drug resistance. This gene is one of two members of the MATE transporter family located near each other on chromosome 17. Alternatively spliced transcript variants encoding different isoforms have been identified for this gene. [provided by RefSeq, Jul 2008] (from NCBI)
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Top mentioned proteins: Oct-2, Oct-1, CAN, HAD, OCT
Papers on hMATE2-K
The non-metabolized β-blocker nadolol is a substrate of OCT1, OCT2, MATE1, MATE2-K and P-glycoprotein, but not of OATP1B1 and OATP1B3.
Fromm et al., In Mol Pharm, Jan 2016
We therefore investigated nadolol as a potential substrate of the hepatic uptake transporters OATP1B1, OATP1B3, and OCT1 and of the renal transporters OCT2, MATE1, and MATE2-K expressed in HEK cells.
Evaluation of Ketoconazole and its Alternative Clinical CYP3A4/5 Inhibitors as Inhibitors of Drug Transporters: The In Vitro Effects of Ketoconazole, Ritonavir, Clarithromycin and Itraconazole on 13 Clinically-Relevant Drug Transporters.
Buckley et al., In Drug Metab Dispos, Jan 2016
In this study, the inhibitory effects of ketoconazole, clarithromycin, ritonavir and itraconazole (and its CYP3A4-inhibitory metabolites, hydroxy-, keto- and N-desalkyl itraconazole) towards 13 drug transporters (OATP1B1, OATP1B3, OAT1, OAT3, OCT1, OCT2, MATE1, MATE2-K, P-gp, BCRP, MRP2, MRP3 and BSEP) were systematically assessed in transporter-expressing HEK-293 cell lines or membrane vesicles.
Atenolol Renal Secretion Is Mediated by Human Organic Cation Transporter 2 and Multidrug and Toxin Extrusion Proteins.
Wang et al., Seattle, United States. In Drug Metab Dispos, Dec 2015
Using a panel of human embryonic kidney cell lines stably expressing human organic cation transporter (hOCT) 1-3, human organic anion transporter (hOAT) 1, hOAT3, human multidrug and toxin extrusion protein (hMATE) 1, and hMATE2-K, we found that atenolol interacted with both organic cation and anion transporters.
Renal tubular secretion of pramipexole.
Müller et al., Erlangen, Germany. In Eur J Pharm Sci, Dec 2015
Cimetidine, a potent inhibitor of multidrug and toxin extrusion proteins 1 (MATE1) and 2-K (MATE2-K), decreases renal pramipexole clearance in humans.
Drug interaction profile of the HIV integrase inhibitor cabotegravir: assessment from in vitro studies and a clinical investigation with midazolam.
Polli et al., United States. In Xenobiotica, Oct 2015
5. CAB is an inhibitor of OAT1 (IC50 0.81 µM) and OAT3 (IC50 0.41 µM) but did not or only weakly inhibited Pgp, BCRP, MRP2, MRP4, MATE1, MATE2-K, OATP1B1, OATP1B3, OCT1, OCT2 or BSEP.
The Use of Transporter Probe Drug Cocktails for the Assessment of Transporter-Based Drug-Drug Interactions in a Clinical Setting-Proposal of a Four Component Transporter Cocktail.
Taub et al., Biberach an der Riß, Germany. In J Pharm Sci, Sep 2015
Furosemide inhibited BCRP (50% inhibition of drug transport: 170 μM), but did not inhibit OATP1B1, OATP1B3, OCT2, MATE1, and MATE2-K at concentrations below 300 μM, and P-gp at concentrations below 2000 μM.
Metabolism and Disposition of Cabozantinib in Healthy Male Volunteers and Pharmacologic Characterization of Its Major Metabolites.
Nguyen et al., Rwanda. In Drug Metab Dispos, Aug 2015
In an in vitro drug transporter panel, cabozantinib inhibited most potently MATE1 and MATE2-K (IC50 = 5.94 and 3.12 µM, respectively) and was a MRP2 substrate; EXEL-1644 inhibited most potently OAT1, OAT3, OATP1B1, MATE1, and OATP1B3 (IC50 = 4.3, 4.3, 6.1, 16.7, and 20.6 µM, respectively) and was a substrate of MRP2, OAT3, OATP1B1, OATP1B3, and possibly P-gp.
Renal tubular secretion of tanshinol: molecular mechanisms, impact on its systemic exposure, and propensity for dose-related nephrotoxicity and for renal herb-drug interactions.
Li et al., Chile. In Drug Metab Dispos, May 2015
Other renal transporters (human organic anion-transporting polypeptide 4C1 [OATP4C1], organic cation transporter 2 [OCT2], carnitine/organic cation transporter 1 [OCTN1], multidrug and toxin extrusion protein 1 [MATE1], MATE2-K, multidrug resistance-associated protein 2 [MRP2], MRP4, and breast cancer resistance protein [BCRP], and rat Oct1, Oct2, Octn1, Octn2, Mate1, Mrp2, Mrp4, and Bcrp) showed either ambiguous ability to transport tanshinol or no transport activity.
Protein Kinase C-Independent Inhibition of Organic Cation Transporter 1 Activity by the Bisindolylmaleimide Ro 31-8220.
Fardel et al., Rennes, France. In Plos One, 2014
In addition to activity of OCT1, Ro 31-8220 inhibited those of other organic cation transporters such as multidrug and toxin extrusion protein (MATE) 1 and MATE2-K, whereas, by contrast, it stimulated that of OCT2.
Inhibitory Effects of Green Tea and (-)-Epigallocatechin Gallate on Transport by OATP1B1, OATP1B3, OCT1, OCT2, MATE1, MATE2-K and P-Glycoprotein.
Fromm et al., Erlangen, Germany. In Plos One, 2014
OCT1-, OCT2-, MATE1- and MATE2-K-mediated metformin uptake was significantly reduced in the presence of green tea and EGCG (P < 0.05).
Multidrug and toxin extrusion proteins (MATE/SLC47); role in pharmacokinetics.
Ceckova et al., Hradec Králové, Czech Republic. In Int J Biochem Cell Biol, 2013
Shortly after, other isoforms (MATE2 and MATE2-K, both encoded by SLC47A2 gene) were identified.
Transporter biology in drug approval: regulatory aspects.
Sugiyama et al., Tokyo, Japan. In Mol Aspects Med, 2013
Target transporters include OATP1B1 (SLCO1B1) and OATP1B3 (SLCO1B3) in the liver, and OAT1 (SLC22A6), OAT3 (SLC22A8), OCT2 (SLC22A2), MATE1 (SLC47A1), and MATE2-K (SLC47A2) in the kidney, and MDR1 (ABCB1) in the intestine.
Multidrug and toxin extrusion family SLC47: physiological, pharmacokinetic and toxicokinetic importance of MATE1 and MATE2-K.
Inui et al., Kyoto, Japan. In Mol Aspects Med, 2013
Kidney-specific MATE2-K was isolated from human kidney and localized at the brush-border membrane of proximal tubules.
Organic cation transporter OCTs (SLC22) and MATEs (SLC47) in the human kidney.
Inui et al., Kyoto, Japan. In Aaps J, 2013
In the human kidney, OCT2 mediates the uptake of drugs from the blood at the basolateral membrane of tubular epithelial cells, and MATE1 and MATE2-K secrete drugs from cells into the lumen of proximal tubules.
Exploring the transcriptome of ciliated cells using in silico dissection of human tissues.
Sergeeva et al., Moscow, Russia. In Plos One, 2011
MATE2, which facilitates extrusion of drugs and metabolites from blood into urine, is physically or functionally associated with cilia.
[Platinum agent-induced nephrotoxicity via organic cation transport system].
Yonezawa, Kyoto, Japan. In Yakugaku Zasshi, 2011
Oxaliplatin, which was a superior substrate of the luminal efflux transporter, MATE2-K as well as OCT2, did not show nephrotoxicity.
Evaluation of 4',6-diamidino-2-phenylindole as a fluorescent probe substrate for rapid assays of the functionality of human multidrug and toxin extrusion proteins.
Yuasa et al., Nagoya, Japan. In Drug Metab Dispos, 2010
4',6-diamidino-2-phenylindole (DAPI) can be used as a probe substrate for rapid assays of the functionality of the human MATE2
Heterozygous variants of multidrug and toxin extrusions (MATE1 and MATE2-K) have little influence on the disposition of metformin in diabetic patients.
Inui et al., Kyoto, Japan. In Pharmacogenet Genomics, 2010
The purpose of this study was to evaluate the effects of heterozygous MATE variants on the disposition of metformin in mice and humans.
Identification of multidrug and toxin extrusion (MATE1 and MATE2-K) variants with complete loss of transport activity.
Inui et al., Kyoto, Japan. In J Hum Genet, 2009
These findings suggested that the loss of transport activities of the MATE1 G64D and MATE2-K G211V variants were due to the alteration of protein expression in cell surface membranes.
Functional characteristics of two human MATE transporters: kinetics of cimetidine transport and profiles of inhibition by various compounds.
Yuasa et al., Nagoya, Japan. In J Pharm Pharm Sci, 2008
characterization of MATE2-K: kinetic analysis of transport of cimetidine and tetraethylammonium; inhibitors; comparison to hMATE1 and rMATE1
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