Molecular cloning and functional characterization of the mouse organic-anion-transporting polypeptide 1 (Oatp1) and mapping of the gene to chromosome X.

摘要: We have cloned a murine member of the organic-anion-transporting polypeptide (Oatp) family membrane-transport proteins from mouse liver. The cDNA insert 2783 bp with an open reading frame 2011 codes for 12-transmembrane 670-amino-acid protein highest amino acid identity rat Oatp1. When expressed in Xenopus laevis oocytes, Oatp exhibited same substrate specificity as Besides common substrates bromosulphophthalein, taurocholate, oestrone 3-sulphate and ouabain, new also mediates transport Oatp1-specific magnetic-resonance-imaging agent gadoxetate. Oatp2-specific cardiac glycoside digoxin, however, is not transported. Kinetic analyses performed taurocholate revealed apparent K(m) values 12 microM 5 respectively. Northern-blot analysis demonstrated predominant expression liver additional moderate kidney. Taken together, identity, functional characteristics tissue distribution suggest that we isolated orthologue Oatp1, consequently identified will be called Using fluorescence situ hybridization, Oatp1 gene was mapped to chromosome XA3-A5.