We have isolated a rat novel multispecific organic anion transporter, moat1. The isolated clones were originated by alternative splicing of the moat1 mRNA. The nucleotide sequences predict a protein of 682 amino acids with moderate sequence similarity to LST-1, the oatp family, and the prostaglandin transporter. Northern blot analysis of rat moat1 identified a predominant transcript of 4.4 kilonucleotides in all tissues. Northern blot and in situ hybridization analyses of rat brain further indicated that moat1 mRNA is widely distributed in neuronal cells of the central nervous system, especially in the hippocampus and cerebellum. moat1 transports prostaglandin D2 (K(m); 35.5 nM), leukotriene C4 (K(m); 3.2 μM) and taurocholate (K(m); 17.6 μM) in a sodium-independent manner. moat1 also transports prostaglandin E1, E2, thromboxane B2, and iloprost but not dehydroepiandrosterone sulfate and digoxin, of which the substrate specificity is similar, but definitively different from those of any other organic anion transporters. (C) 2000 Academic Press.
|Number of pages||8|
|Journal||Biochemical and biophysical research communications|
|Publication status||Published - 2000 Sep 7|
ASJC Scopus subject areas
- Molecular Biology
- Cell Biology