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Am J Physiol Gastrointest Liver Physiol (December 15, 2005). doi:10.1152/ajpgi.00492.2005
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Submitted on October 20, 2005
Accepted on December 9, 2005

Localization of the sulfate-anion exchanger (sat-1) in rat liver

Fabio Quondamatteo1, Wolfgang Krick2, Yohannes Hagos2, Marie-Helen Kruger1, Katrin Neubauer-Saile3, Rainer Herken1, Giuliano Ramadori3, Gerhard Burckhardt2, and Birgitta C. Burckhardt2*

1 Department of Histology, University of Goettingen, Goettingen, Germany
2 Department of Physiology and Pathophysiology, University of Goettingen, Goettingen, Germany
3 Department of Gastroenterology and Endocrinology, University of Goettingen, Goettingen, Germany

* To whom correspondence should be addressed. E-mail: bcburckhardt{at}physiol.med.uni-goettingen.de.

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 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, 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 the hepatocytes to enable sulfation reactions. In hepatocytes and endothelial cells sat-1 may also supply sulfate for proteoglycan synthesis.




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