Localization of the sulfate/anion exchanger in the rat liver

Although the sulfate/anion transporter (sat-1; SLC26A1) was isolated from a rat liver cDNA library by expression cloning, localization of sat-1 within the liver and its contribution to the transport of sulfate and organo sulfates have remained unresolved. In situ hybridization and immunohistochemica...

Full description

Saved in:
Bibliographic Details
Published in:American journal of physiology: Gastrointestinal and liver physiology 2006-05, Vol.290 (5), p.G1075-G1081
Main Authors: Quondamatteo, Fabio, Krick, Wolfgang, Hagos, Yohannes, Krüger, Marie-Helen, Neubauer-Saile, Katrin, Herken, Rainer, Ramadori, Giuliano, Burckhardt, Gerhard, Burckhardt, Birgitta C
Format: Article
Language:English
Subjects:
Amino Acid Transport System A - analysis
Amino Acid Transport System A - physiology
Animals
Bicarbonates - pharmacology
Dehydroepiandrosterone Sulfate - pharmacokinetics
Endothelial Cells - metabolism
Estrone - analogs & derivatives
Estrone - metabolism
Hepatocytes - metabolism
Liver - chemistry
Liver - metabolism
Male
Rats
Sulfates - metabolism
Unithiol - pharmacology
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Although the sulfate/anion transporter (sat-1; SLC26A1) was isolated from a rat liver cDNA library by expression cloning, localization of sat-1 within the liver and its contribution to the transport of sulfate and organo sulfates have remained unresolved. In situ hybridization and immunohistochemical studies were undertaken to demonstrate the localization of sat-1 in liver tissue. RT-PCR studies on isolated hepatocytes and liver endothelial and stellate cells in culture were performed to test for the presence of sat-1 in these cells. In sulfate uptake and efflux experiments, the substrate specificity of sat-1 was evaluated. Sat-1 mRNA was found in hepatocytes and endothelial cells. Sat-1 protein was localized in sinusoidal membranes and along the borders of hepatocytes. The canalicular region and bile capillaries were not stained. Sulfate uptake was only slightly affected by sulfamoyl diuretics or organo sulfates. Sulfate efflux from sat-1-expressing oocytes was enhanced in the presence of bicarbonate, indicating sulfate/bicarbonate exchange. Estrone sulfate was not transported by sat-1. Sat-1 may be responsible for the uptake of inorganic sulfate from the blood into hepatocytes to enable sulfation reactions. In hepatocytes and endothelial cells, sat-1 may also supply sulfate for proteoglycan synthesis.
ISSN:0193-1857
1522-1547
DOI:10.1152/ajpgi.00492.2005