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

Miki Hiasa, Takuya Matsumoto, Toshinori Komatsu, Yoshinori Moriyama

Research output: Contribution to journalArticle

71 Citations (Scopus)

Abstract

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, Matsumoto T, Morimoto R, Arioka S, Omote H, and Moriyama Y. Proc Natl Acad Sci USA 102: 17923-17928, 2005). mMATE1, a mouse MATE ortholog, 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 HEK-293 cells, mMATE1 mediated electroneutral H+/tetraethylammonium 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, α cells of the islets of Langerhans, Leydig cells, and vitamin A-storing Ito cells. These results indicate that mMATE1 is a polyspecific H+/OC 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.

Original languageEnglish
JournalAmerican Journal of Physiology - Cell Physiology
Volume291
Issue number4
DOIs
Publication statusPublished - 2006

Fingerprint

Poisons
Cations
Rodentia
Transport properties
Extrusion
Proteins
Tetraethylammonium
Bile Canaliculi
Immunologic Techniques
Vitamin A
Liver
Hepatic Stellate Cells
Ducts
Langerhans Cells
Leydig Cells
HEK293 Cells
Pancreatic Ducts
Adrenal Cortex
Brain
Adrenal Glands

Keywords

  • Hydrophobic cation
  • Multidrug and toxin extrusion
  • Multidrug transport

ASJC Scopus subject areas

  • Clinical Biochemistry
  • Cell Biology
  • Physiology

Cite this

Wide variety of locations for rodent MATE1, a transporter protein that mediates the final excretion step for toxic organic cations. / Hiasa, Miki; Matsumoto, Takuya; Komatsu, Toshinori; Moriyama, Yoshinori.

In: American Journal of Physiology - Cell Physiology, Vol. 291, No. 4, 2006.

Research output: Contribution to journalArticle

@article{9262712212174444962a8142704014ce,
title = "Wide variety of locations for rodent MATE1, a transporter protein that mediates the final excretion step for toxic organic cations",
abstract = "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, Matsumoto T, Morimoto R, Arioka S, Omote H, and Moriyama Y. Proc Natl Acad Sci USA 102: 17923-17928, 2005). mMATE1, a mouse MATE ortholog, 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 HEK-293 cells, mMATE1 mediated electroneutral H+/tetraethylammonium 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, α cells of the islets of Langerhans, Leydig cells, and vitamin A-storing Ito cells. These results indicate that mMATE1 is a polyspecific H+/OC 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.",
keywords = "Hydrophobic cation, Multidrug and toxin extrusion, Multidrug transport",
author = "Miki Hiasa and Takuya Matsumoto and Toshinori Komatsu and Yoshinori Moriyama",
year = "2006",
doi = "10.1152/ajpcell.00090.2006",
language = "English",
volume = "291",
journal = "American Journal of Physiology",
issn = "0002-9513",
publisher = "American Physiological Society",
number = "4",

}

TY - JOUR

T1 - Wide variety of locations for rodent MATE1, a transporter protein that mediates the final excretion step for toxic organic cations

AU - Hiasa, Miki

AU - Matsumoto, Takuya

AU - Komatsu, Toshinori

AU - Moriyama, Yoshinori

PY - 2006

Y1 - 2006

N2 - 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, Matsumoto T, Morimoto R, Arioka S, Omote H, and Moriyama Y. Proc Natl Acad Sci USA 102: 17923-17928, 2005). mMATE1, a mouse MATE ortholog, 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 HEK-293 cells, mMATE1 mediated electroneutral H+/tetraethylammonium 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, α cells of the islets of Langerhans, Leydig cells, and vitamin A-storing Ito cells. These results indicate that mMATE1 is a polyspecific H+/OC 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.

AB - 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, Matsumoto T, Morimoto R, Arioka S, Omote H, and Moriyama Y. Proc Natl Acad Sci USA 102: 17923-17928, 2005). mMATE1, a mouse MATE ortholog, 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 HEK-293 cells, mMATE1 mediated electroneutral H+/tetraethylammonium 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, α cells of the islets of Langerhans, Leydig cells, and vitamin A-storing Ito cells. These results indicate that mMATE1 is a polyspecific H+/OC 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.

KW - Hydrophobic cation

KW - Multidrug and toxin extrusion

KW - Multidrug transport

UR - http://www.scopus.com/inward/record.url?scp=33749327002&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=33749327002&partnerID=8YFLogxK

U2 - 10.1152/ajpcell.00090.2006

DO - 10.1152/ajpcell.00090.2006

M3 - Article

C2 - 16641166

AN - SCOPUS:33749327002

VL - 291

JO - American Journal of Physiology

JF - American Journal of Physiology

SN - 0002-9513

IS - 4

ER -