PuSH - Publication Server of Helmholtz Zentrum München: Functional characterization of the mouse organic-anion-transporting polypeptide 2.

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van Montfoort, J.E.* ; Schmid, T.E. ; Adler, I.-D. ; Meier, P.J.* ; Hagenbuch, B.*

Functional characterization of the mouse organic-anion-transporting polypeptide 2.

Biochim. Biophys. Acta-Biomembr. 1564, 183-188 (2002)

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We have isolated and functionally characterized an additional murine member of the organic-anion-transporting polypeptide (Oatp) family of membrane transport proteins from mouse liver. The 3.6 kb cDNA insert contains an open reading frame of 2010 bp coding for a 670 amino acid protein. Based on its amino acid identity of 88% to the rat Oatp2, it is considered the mouse Oatp2 orthologue. Functional expression in Xenopus laevis oocytes demonstrated that mouse Oatp2 transports several general Oatp substrates such as estrone-3-sulfate, dehydroepiandrosterone sulfate (DHEAS), ouabain and BQ-123 but hardly any taurocholate nor rocuronium or deltorphin II. The high-affinity rat Oatp2 substrate digoxin is transported with a rather low affinity with an apparent K_m value of 5.7 μM. Bromosulfophthalein (BSP), a substrate not transported by the rat Oatp2, is transported very well by mouse Oatp2. Northern blot analysis demonstrated a predominant expression in the liver with additional signals in kidney and brain. Using fluorescence in situ hybridization, the Oatp2 gene (gene symbol Slc21a5) was mapped to chromosome 6G1–G3.

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