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Otsuka, Masato Okayama University
Matsumoto, Takuya Okayama University
Morimoto, Riyo Okayama University
Arioka, Shigeo Okayama University
Omote, Hiroshi Okayama University
Moriyama, Yoshinori Okayama University
In mammals, toxic electrolytes of endogenous and exogenous origin are excreted through the urine and bile. Before excretion, these compounds cross numerous cellular membranes in a transporter-mediated manner. However, the protein transporters involved in the final excretion step are poorly understood. Here, we show that MATE1, a human and mouse orthologue of the multidrug and toxin extrusion (MATE) family conferring multidrug resistance on bacteria, is primarily expressed in the kidney and liver, where it is localized to the luminal membranes of the urinary tubules and bile canaliculi. When expressed in HEK293 cells, MATE1 mediates H+-coupled electroneutral exchange of tetraethylammonium (TEA) and 1-methyl-4-phenylpyridinium (MPP). Its substrate specificity is similar to those of renal and hepatic H+-coupled organic cations (OCs) export. Thus, MATE1 appears to be the long searched for polyspecific OC exporter that directly transports toxic OCs into urine and bile.
Digital Object Identifier:10.1073/pnas.0506483102
Published with permission from the copyright holder. This is the institute's copy, as published in PNAS, Dec 2005, Volume 102, Issue 50, Pages 17923-17928.
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Copyright © 2005 the National Academy of Sciences
Proceedings of the National Academy of Sciences of the United States of America