scholarly journals Identification of a Novel Organic Anion Transporter Mediating Carnitine Transport in Mouse Liver and Kidney

2010 ◽  
Vol 25 (4-5) ◽  
pp. 511-522 ◽  
Author(s):  
Hiroki Tsuchida ◽  
Naohiko Anzai ◽  
Ho Shin ◽  
Michael Wempe ◽  
Promsuk Jutabha ◽  
...  
Keyword(s):  
Mouse Liver ◽  
Organic Anion ◽  
Organic Anion Transporter ◽  
Anion Transporter ◽  
Carnitine Transport ◽  
Liver And Kidney

scholarly journals Analysis of a large cluster of SLC22 transporter genes, including novel USTs, reveals species-specific amplification of subsets of family members

2009 ◽  
Vol 38 (2) ◽  
pp. 116-124 ◽  
Author(s):  
Wei Wu ◽  
Michael E. Baker ◽  
Satish A. Eraly ◽  
Kevin T. Bush ◽  
Sanjay K. Nigam
Keyword(s):  
Transmembrane Domain ◽  
Organic Anion ◽  
Tissue Expression ◽  
Organic Anion Transporter ◽  
Preferential Expression ◽  
Environmental Selection ◽  
Anion Transporter ◽  
Liver And Kidney ◽  
Specific Amplification ◽  
Species Specific

When the organic anion transporter Oat1 was first identified as NKT (Lopez-Nieto CE, You G, Bush KT, Barros EJ, Beier DR, Nigam SK. J Biol Chem 272: 6471–6478, 1997), it was argued that it, together with Oct1, may be part of a larger subfamily (now known as SLC22) involved in organic ion and xenobiotic transport. The least studied among SLC22 transporters are the so-called unknown substrate transporters ( USTs). Here, five novel genes located in a cluster on mouse chromosome 19, immediately between Slc22a8 ( Oat3)/ Slc22a6 ( Oat1) and Slc22a19 ( Oat5), were identified as homologs of human USTs. These genes display preferential expression in liver and kidney, and one gene, AB056422, has several splicing variants with differential tissue expression and embryonic expression. Along with Slc22a6, Slc22a8, and Slc22a19, these Usts define the largest known cluster of mammalian Slc22 genes. Given the established functions of Oats, these genes may also be involved in organic anion transport. Usts have characteristic motifs and share a signature residue in the possible active site of transmembrane domain 7, a conserved, positively charged, amino acid, Arg356, possibly a site for interaction with organic anions. In certain species, Oat1 and Oat3 appeared to be highly conserved, whereas the Ust part of this cluster appeared to undergo repeated species-specific amplification, suggesting strong environmental selection pressure, and perhaps providing an explanation for copy number variation in the human locus. One Ust amplification in mouse appears to be recent. This cluster may be coordinately regulated and under selective pressure in a species-specific manner.

Ontogenic expression of the Na+-independent organic anion transporter (oatp) in rat liver and kidney

1995 ◽  
Vol 108 (4) ◽  
pp. A1059
Author(s):  
C. Dubuisson ◽  
M. Desrochers ◽  
D. Cresteil ◽  
D. Decimo ◽  
A. Wolkoff ◽  
...  
Keyword(s):  
Rat Liver ◽  
Organic Anion ◽  
Organic Anion Transporter ◽  
Anion Transporter ◽  
Liver And Kidney ◽  
Ontogenic Expression

Induction of the multispecific organic anion transporter (cMoat/mrp2) gene and biliary glutathione secretion by the herbicide 2,4,5-trichlorophenoxyacetic acid in the mouse liver

1999 ◽  
Vol 341 (1) ◽  
pp. 105-111 ◽  
Author(s):  
Ana M. WIELANDT ◽  
Valeska VOLLRATH ◽  
Marlene MANZANO ◽  
Soledad MIRANDA ◽  
Luigi ACCATINO ◽  
...  
Keyword(s):  
Bile Acid ◽  
Bile Flow ◽  
Mouse Liver ◽  
Organic Anion ◽  
Fold Increase ◽  
Organic Anion Transporter ◽  
Peroxisome Proliferator ◽  
Mrna Levels ◽  
Anion Transporter ◽  
Trichlorophenoxyacetic Acid

The canalicular multispecific organic anion transporter, cMoat, is an ATP-binding-cassette protein expressed in the canalicular domain of hepatocytes. In addition to the transport of endo- and xenobiotics, cMoat has also been proposed to transport GSH into bile, the major driving force of bile-acid-independent bile flow. We have shown previously that the herbicide 2,4,5-trichlorophenoxyacetic acid (2,4,5-T), a peroxisome-proliferator agent, significantly increases bile-acid-independent bile flow in mice. On this basis, the effect of the herbicide on cMoat gene expression was studied. A 3.6-fold increase in cMoat mRNA levels and a 2.5-fold increase in cMoat protein content were observed in the liver of mice fed on a diet supplemented with 0.125% 2,4,5-T. These effects were due to an increased rate of gene transcription (3.9-fold) and were not associated with peroxisome proliferation. Significant increases in bile flow (2.23±0.39 versus 1.13±0.15 μl/min per g of liver; P < 0.05) and biliary GSH output (7.40±3.30 versus 2.65±0.34 nmol/min per g of liver; P < 0.05) were observed in treated animals. The hepatocellular concentration of total glutathione also increased in hepatocytes of treated mice (10.95±0.84 versus 5.12±0.47 mM; P < 0.05), because of the induction (2.4-fold) of the heavy subunit of the γ-glutamylcysteine synthetase (GCS-HS) gene. This is the first model of co-induction of cMoat and GCS-HS genes in vivo in the mouse liver, associated with increased glutathione synthesis and biliary glutathione output. Our observations are consistent with the hypothesis that the cMoat transporter plays a crucial role in the secretion of biliary GSH.

Characterization of hepatobiliary organic anion transporter regulation in the Zucker rat

2004 ◽  
Vol 42 (08) ◽  
Author(s):  
A Geier ◽  
CG Dietrich ◽  
C Gartung ◽  
F Lammert ◽  
HE Wasmuth ◽  
...  
Keyword(s):  
Organic Anion ◽  
Organic Anion Transporter ◽  
Zucker Rat ◽  
Anion Transporter
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