Click here to close Hello! We notice that you are using Internet Explorer, which is not supported by Xenbase and may cause the site to display incorrectly. We suggest using a current version of Chrome, FireFox, or Safari.
XB-ART-10374
Biochem Biophys Res Commun 2000 Sep 07;2753:831-8. doi: 10.1006/bbrc.2000.3377.
Show Gene links Show Anatomy links

Molecular identification of a rat novel organic anion transporter moat1, which transports prostaglandin D(2), leukotriene C(4), and taurocholate.

Nishio T , Adachi H , Nakagomi R , Tokui T , Sato E , Tanemoto M , Fujiwara K , Okabe M , Onogawa T , Suzuki T , Nakai D , Shiiba K , Suzuki M , Ohtani H , Kondo Y , Unno M , Ito S , Iinuma K , Nunoki K , Matsuno S , Abe T .


???displayArticle.abstract???
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 D(2) (K(m); 35.5 nM), leukotriene C(4) (K(m); 3.2 microM) and taurocholate (K(m); 17.6 microM) in a sodium-independent manner. moat1 also transports prostaglandin E(1), E(2), thromboxane B(2), 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.

???displayArticle.pubmedLink??? 10973807
???displayArticle.link??? Biochem Biophys Res Commun


Species referenced: Xenopus laevis
Genes referenced: slco1a2