Am J Physiol Cell Physiol Ad Instruments
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
QUICK SEARCH:   [advanced]


     

Am J Physiol Cell Physiol (May 10, 2006). doi:10.1152/ajpcell.00090.2006
This Article
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
291/4/C678    most recent
00090.2006v3
00090.2006v2
00090.2006v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Haisa, M.
Right arrow Articles by Mariyama, Y.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Haisa, M.
Right arrow Articles by Mariyama, Y.
Submitted on February 24, 2006
Accepted on April 14, 2006

Wide variety of locations for rodent MATE1, a transporter protein that mediates the final excretion step for toxic organic cations

Miki Haisa1, Takuya Matsumoto1, Toshinori Komatsu2, and Yoshinori Mariyama1*

1 Dentistry and Pharmaceutical Sciences,Membrane Biochemistry, Okayama University Graduate School of Medicine, Japan
2 Dentistry and Pharmaceutical Sciences,Membrane Biochemistry, Okayama University Graduate School of Medicine, United States

* To whom correspondence should be addressed. E-mail: moriyama{at}pheasant.pharm.okayama-c.ac.jp.

MATE1 was the first mammalian example of the multidrug and toxin extrusion (MATE) protein family to be identified. Human MATE1 (hMATE1) is predominantly expressed and localized to the luminal membranes of the urinary tubules and bile canaliculi and mediates H+-coupled electroneutral excretion of toxic organic cations (OCs) into urine and bile (Otsuka M et al., (2005) Proc. Natl. Acad. Sci. USA, 102, 17923-17928). mMATE1, a mouse MATE orthologue, is also predominantly expressed in kidney and liver, although its transport properties are not yet characterized. In the present study, we investigated the transport properties and localization of mMATE1. Upon expression of this protein in HEK293 cells, mMATE1 mediated electroneutral H+/tetraethylammonium (TEA) exchange and showed a substrate specificity similar to that of hMATE1. Immunological techniques with specific antibodies against mMATE1 combined with RT-PCR revealed that mMATE1 is also expressed in various cells, including brain glia-like cells and capillaries, pancreatic duct cells, urinary bladder epithelium, adrenal gland cortex, {alpha} cells of the islets of Langerhans, Leydig cells and vitamin A-storing Ito cells. These results indicate that mMATE1 is a polyspecific H+/OCs exchanger. The unexpectedly wide distribution of mMATE1 suggests involvement of this transporter protein in diverse biological functions other than excretion of OCs from the body.




This article has been cited by other articles:


Home page
 Am. J. Physiol. Renal Physiol.Home page
X. Zhang and S. H. Wright
MATE1 has an external COOH terminus, consistent with a 13-helix topology
Am J Physiol Renal Physiol, August 1, 2009; 297(2): F263 - F271.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Pharmacol.Home page
M. Tsuda, T. Terada, T. Mizuno, T. Katsura, J. Shimakura, and K.-i. Inui
Targeted Disruption of the Multidrug and Toxin Extrusion 1 (Mate1) Gene in Mice Reduces Renal Secretion of Metformin
Mol. Pharmacol., June 1, 2009; 75(6): 1280 - 1286.
[Abstract] [Full Text] [PDF]

Home page
 Drug Metab. Dispos.Home page
S. Matsushima, K. Maeda, K. Inoue, K.-y. Ohta, H. Yuasa, T. Kondo, H. Nakayama, S. Horita, H. Kusuhara, and Y. Sugiyama
The Inhibition of Human Multidrug and Toxin Extrusion 1 Is Involved in the Drug-Drug Interaction Caused by Cimetidine
Drug Metab. Dispos., March 1, 2009; 37(3): 555 - 559.
[Abstract] [Full Text] [PDF]

Home page
 Toxicol SciHome page
S. A. Reisman, R. L. Yeager, M. Yamamoto, and C. D. Klaassen
Increased Nrf2 Activation in Livers from Keap1-Knockdown Mice Increases Expression of Cytoprotective Genes that Detoxify Electrophiles more than those that Detoxify Reactive Oxygen Species
Toxicol. Sci., March 1, 2009; 108(1): 35 - 47.
[Abstract] [Full Text] [PDF]

Home page
 Am. J. Physiol. Cell Physiol.Home page
T. Matsumoto, T. Kanamoto, M. Otsuka, H. Omote, and Y. Moriyama
Role of glutamate residues in substrate recognition by human MATE1 polyspecific H+/organic cation exporter
Am J Physiol Cell Physiol, April 1, 2008; 294(4): C1074 - C1078.
[Abstract] [Full Text] [PDF]

Home page
 Am. J. Physiol. Cell Physiol.Home page
M. Hiasa, T. Matsumoto, T. Komatsu, H. Omote, and Y. Moriyama
Functional characterization of testis-specific rodent multidrug and toxic compound extrusion 2, a class III MATE-type polyspecific H+/organic cation exporter
Am J Physiol Cell Physiol, November 1, 2007; 293(5): C1437 - C1444.
[Abstract] [Full Text] [PDF]

Home page
 Am. J. Physiol. Renal Physiol.Home page
X. Zhang, N. J. Cherrington, and S. H. Wright
Molecular identification and functional characterization of rabbit MATE1 and MATE2-K
Am J Physiol Renal Physiol, July 1, 2007; 293(1): F360 - F370.
[Abstract] [Full Text] [PDF]

Home page
 Am. J. Physiol. Renal Physiol.Home page
M. Tsuda, T. Terada, J.-i. Asaka, M. Ueba, T. Katsura, and K.-i. Inui
Oppositely directed H+ gradient functions as a driving force of rat H+/organic cation antiporter MATE1
Am J Physiol Renal Physiol, February 1, 2007; 292(2): F593 - F598.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
Visit Other APS Journals Online
Copyright © 1977 by the American Physiological Society.