Cloning and characterization of organic anion transporter 2 from human and mouse

• Published in: Japanese Journal of Pharmacology 2000, Vol.82 (suppl.1), p.155-155
• Main Authors: Ohshiro, Naomi, Kobayashi, Yasuna, Tokuyama, Shogo, Sekine, Takashi, Endo, Hitoshi, Yamamoto, Toshinori
• Format: Article
• Language: eng ; jpn
• ISSN: 0021-5198
• DOI: 10.1016/S0021-5198(19)48083-9

Recent studies have revealed that organic anion transporters (OATs) play an important role in the pharmacokinetics of endogenous and exogenous organic anions including a wide range of drugs and environmental chemicals. We have reported that rat OAT2 (rOAT2) is predominantly expressed in the liver and mediates the uptake of various organic anions. However, there is no report on the structual and functional characteristics of OAT2 cloned from other species. Here, we report the isolation and characterization of human and mouse OAT2 (hOAT2 and mOAT2). cDNA libraries were constructed from mouse poly(A)^+ RNA derived from liver, kidney and that from human liver. These libraries were screened by using rOAT2 cDNA as a probe. Amino acid sequence of mOAT2 and hOAT2 exhibited about 90% and 80% identity to that of rOAT2, respectively. When expressed in Xenopus laevis oocytes, mOAT2 mediated uptake of [^^14 C]glutarate (Km=12.3±2.1 μM). Northem blot analysis revealed that hOAT2 mRNA is predominantly expressed in liver. These results suggest that mOAT2 and hOAT2 play a role in the transmembrane transport of organic anions in the liver. We now continue to characterize hOAT2 and mOAT2 more precisely.