Functional characterization of the mouse organic-anion-transporting polypeptide 2.
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van Montfoort JE, Schmid TE, Adler ID, Meier PJ, Hagenbuch B
Functional characterization of the mouse organic-anion-transporting polypeptide 2.
Biochim Biophys Acta. 2002 Aug 19;1564(1):183-8.
- PubMed ID
- 12101011 [ View in PubMed]
- Abstract
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.
DrugBank Data that Cites this Article
- Drug Transporters
Drug Transporter Kind Organism Pharmacological Action Actions Conjugated estrogens Solute carrier organic anion transporter family member 1B1 Protein Humans UnknownSubstrateInhibitorDetails Digoxin Solute carrier organic anion transporter family member 1B1 Protein Humans UnknownSubstrateInhibitorDetails Ouabain Solute carrier organic anion transporter family member 1B1 Protein Humans UnknownSubstrateInhibitorDetails