| First Author | van Montfoort JE | Year | 2002 |
| Journal | Biochim Biophys Acta | Volume | 1564 |
| Issue | 1 | Pages | 183-8 |
| PubMed ID | 12101011 | Mgi Jnum | J:77839 |
| Mgi Id | MGI:2182694 | Doi | 10.1016/s0005-2736(02)00445-5 |
| Citation | van Montfoort JE, et al. (2002) Functional characterization of the mouse organic-anion-transporting polypeptide 2. Biochim Biophys Acta 1564(1):183-8 |
| abstractText | 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 microM. 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. |
