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Am J Physiol Gastrointest Liver Physiol 278: G156-G164, 2000;
0193-1857/00 $5.00
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Vol. 278, Issue 1, G156-G164, January 2000

A novel human organic anion transporting polypeptide localized to the basolateral hepatocyte membrane

Jörg König, Yunhai Cui, Anne T. Nies, and Dietrich Keppler

Division of Tumor Biochemistry, Deutsches Krebsforschungszentrum, D-69120 Heidelberg, Germany

We cloned and expressed a new organic anion transporting polypeptide (OATP), termed human OATP2, (OATP-C, LST-1; symbol SLC21A6), involved in the uptake of various lipophilic anions into human liver. The cDNA encoding OATP2 comprised 2073 base pairs, corresponding to a protein of 691 amino acids, which were 44% identical to the known human OATP. An antibody directed against the carboxy terminus localized OATP2 to the basolateral membrane of human hepatocytes. Northern blot analysis indicated a strong expression of OATP2 only in human liver. Transport mediated by recombinant OATP2 and its localization were studied in stably transfected Madin-Darby canine kidney strain II (MDCKII) and HEK293 cells. Confocal microscopy localized recombinant OATP2 protein to the lateral membrane of MDCKII cells. Substrates included 17beta -glucuronosyl estradiol, monoglucuronosyl bilirubin, dehydroepiandrosterone sulfate, and cholyltaurine. 17beta -Glucuronosyl estradiol was a preferred substrate, with a Michaelis-Menten constant value of 8.2 µM; its uptake was Na+ independent and was inhibited by sulfobromophthalein, with a inhibition constant value of 44 nM. Our results indicate that OATP2 is important for the uptake of organic anions, including bilirubin conjugates and sulfobromophthalein, in human liver.

bilirubin conjugates; 17beta -glucuronosyl estradiol; hepatic transport; SLC21A6; sulfobromophthalein


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