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ID 34233
フルテキストURL
著者
Matsumoto, Takuya Okayama University
Morimoto, Riyo Okayama University
Arioka, Shigeo Okayama University
抄録

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.

キーワード
MATE
multidrug export
excretion
toxin
urinary tubule
bile canaliculus
organic cation
H+/cation antiport.
備考
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.
Publisher URL:http://dx.doi.org/10.1073/pnas.0506483102
Direct access to Thomson Web of Science record
Copyright © 2005 the National Academy of Sciences
発行日
2007-09-25
出版物タイトル
Proceedings of the National Academy of Sciences of the United States of America
102巻
50号
開始ページ
17923
終了ページ
17928
資料タイプ
学術雑誌論文
言語
English
査読
有り
DOI
Submission Path
biochemistry/6