The DOI matches its Crossref record; 20 of the 20 references it cites were found in a registry or an index.
Identification and Functional Characterization of a New Human Kidney–Specific H+/Organic Cation Antiporter, Kidney-Specific Multidrug and Toxin Extrusion 2
Abstract
A cDNA coding a new H+/organic cation antiporter, human kidney-specific multidrug and toxin extrusion 2 (hMATE2-K), has been isolated from the human kidney. The hMATE2-K cDNA had an open reading frame that encodes a 566-amino acid protein, which shows 94, 82, 52, and 52% identity with the hMATE2, hMATE2-B, hMATE1, and rat MATE1, respectively. Reverse transcriptase-PCR revealed that hMATE2-K mRNA but not hMATE2 was expressed predominantly in the kidney, and hMATE2-B was ubiquitously found in all tissues examined except the kidney. The immunohistochemical analyses revealed that the hMATE2-K as well as the hMATE1 was localized at the brush border membranes of the proximal tubules. HEK293 cells that were transiently transfected with the hMATE2-K cDNA but not hMATE2-B exhibited the H+ gradient-dependent antiport of tetraethylammonium (TEA). Transfection of hMATE2-B had no affect on the hMATE2-K-mediated transport of TEA. hMATE2-K also transported cimetidine, 1-methyl-4-phenylpyridinium (MPP), procainamide, metformin, and N1-methylnicotinamide. Kinetic analyses demonstrated that the Michaelis-Menten constants for the hMATE2-K-mediated transport of TEA, MPP, cimetidine, metformin, and procainamide were 0.83 mM, 93.5 microM, 0.37 mM, 1.05 mM, and 4.10 mM, respectively. Ammonium chloride-induced intracellular acidification significantly stimulated the hMATE2-K-dependent transport of organic cations such as TEA, MPP, procainamide, metformin, N1-methylnicotinamide, creatinine, guanidine, quinidine, quinine, thiamine, and verapamil. These results indicate that hMATE2-K is a new human kidney-specific H+/organic cation antiporter that is responsible for the tubular secretion of cationic drugs across the brush border membranes.
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Citations
Cites
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Cloning and Characterization of Two Human Polyspecific Organic Cation Transporters
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A human transporter protein that mediates the final excretion step for toxic organic cations
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The SLC22 drug transporter family
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Self-citationCellular and molecular aspects of drug transport in the kidney
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Self-citationMetformin is a Superior Substrate for Renal Organic Cation Transporter OCT2 rather than Hepatic OCT1
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Cited by
Tanihara, Y., Masuda, S., Sato, T., Katsura, T., Ogawa, O., & Inui, K.-I. (2007) · Biochemical Pharmacology · doi:10.1016/j.bcp.2007.04.010 · Cited by 417
Self-citationSamuel, S., Varghese, E., Kubatka, P., Triggle, C., & Büsselberg, D. (2019) · Biomolecules · doi:10.3390/biom9120846 · Cited by 81
The Role of Solute Carrier Transporters in Efficient Anticancer Drug Delivery and Therapy
Puris, E., Fricker, G., & Gynther, M. (2023) · Pharmaceutics · doi:10.3390/pharmaceutics15020364 · Cited by 58
Principles of Alternating Access in Multidrug and Toxin Extrusion (MATE) Transporters
Claxton, D. P., Jagessar, K. L., & Mchaourab, H. S. (2021) · Journal of Molecular Biology · doi:10.1016/j.jmb.2021.166959 · Cited by 29
Metadata
- Authors
- Masuda, S., Terada, T., Yonezawa, A., Tanihara, Y., Kishimoto, K., Katsura, T., Ogawa, O., & Inui, K.-I.
- Venue
- Journal of the American Society of Nephrology
- Published
- 2006-08
- Volume
- 17
- Issue
- 8
- Pages
- 2127-2135
- ISSN
- 1046-6673 (ISSN-L)
- OpenAlex
- W2128358586
- Cited by
- 371
- References
- 20
- FWCI
- 8.37
- Type
- journal article
- Language
- en
- Open access
- closed
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- Masuda, S., Terada, T., Yonezawa, A., Tanihara, Y., Kishimoto, K., Katsura, T., Ogawa, O., & Inui, K.-I. (2006). Identification and Functional Characterization of a New Human Kidney–Specific H+/Organic Cation Antiporter, Kidney-Specific Multidrug and Toxin Extrusion 2. Journal of the American Society of Nephrology. https://doi.org/10.1681/asn.2006030205
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