The multispecific organic anion transporter (OAT) family

被引:261
作者
Sekine, T [1 ]
Cha, SH [1 ]
Endou, H [1 ]
机构
[1] Kyorin Univ, Sch Med, Dept Pharmacol & Toxicol, Tokyo 1818611, Japan
来源
PFLUGERS ARCHIV-EUROPEAN JOURNAL OF PHYSIOLOGY | 2000年 / 440卷 / 03期
关键词
organic anion; p-aminohippurate; multispecific organic anion transporter; tubular secretion; xenobiotics; pharmacokinetics;
D O I
10.1007/s004240000297
中图分类号
Q4 [生理学];
学科分类号
071003 ;
摘要
Organic anion transporters play important roles in the elimination of a variety of endogenous substances, xenobiotics and their metabolites from the body. During the last decade, molecular cloning has identified several families of multispecific organic anion transporters mediating the renal and hepatic elimination of organic anions and, most recently, the OAT (organic anion transporter) family, the founding member of which (OAT1) is the basolateral p-aminohippurate (PAH) transporter in the renal proximal tubule. So far, four isoforms have been identified. OATs are membrane proteins with 12 putative membrane-spanning domains and function as sodium-independent exchangers or facilitators. OATs show weak structural similarity to organic cation transporters (OCTs) and OCTN/carnitine transporters. OATs are multispecific organic anion transporters, the substrates of which include both endogenous (e.g. cyclic nucleotides, prostaglandins, urate, dicarboxylates) and exogenous anions (various anionic drugs and environmental substances). All members of the OAT family are expressed in the kidney, while some are also expressed in the liver, brain and placenta. The OAT family represents the renal secretory pathway for organic anions and is also involved in the distribution of organic anions in the body.
引用
收藏
页码:337 / 350
页数:14
相关论文
共 115 条
[1]   Identification of a novel gene family encoding human liver-specific organic anion transporter LST-1 [J].
Abe, T ;
Kakyo, M ;
Tokui, T ;
Nakagomi, R ;
Nishio, T ;
Nakai, D ;
Nomura, H ;
Unno, M ;
Suzuki, M ;
Naitoh, T ;
Matsuno, S ;
Yawo, H .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1999, 274 (24) :17159-17163
[2]   Molecular characterization and tissue distribution of a new organic anion transporter subtype (oatp3) that transports thyroid hormones and taurocholate and comparison with oatp2 [J].
Abe, T ;
Kakyo, M ;
Sakagami, H ;
Tokui, T ;
Nishio, T ;
Tanemoto, M ;
Nomura, H ;
Hebert, SC ;
Matsuno, S ;
Kondo, H ;
Yawo, H .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1998, 273 (35) :22395-22401
[3]   The choroid plexus epithelium is the site of the organic anion transport protein in the brain [J].
Angeletti, RH ;
Novikoff, PM ;
Juvvadi, SR ;
Fritschy, JM ;
Meier, PJ ;
Wolkoff, AW .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1997, 94 (01) :283-286
[4]  
Apiwattanakul N, 1999, MOL PHARMACOL, V55, P847
[5]  
ARONSON PS, 1989, ANNU REV PHYSIOL, V51, P419
[6]  
Bennett WM, 1991, KIDNEY, P1430
[7]   Immunologic distribution of an organic anion transport protein in rat liver and kidney [J].
Bergwerk, AJ ;
Shi, XY ;
Ford, AC ;
Kanai, N ;
Jacquemin, E ;
Burk, RD ;
Bai, S ;
Novikoff, PM ;
Stieger, B ;
Meier, PJ ;
Schuster, VL ;
Wolkoff, AW .
AMERICAN JOURNAL OF PHYSIOLOGY-GASTROINTESTINAL AND LIVER PHYSIOLOGY, 1996, 271 (02) :G231-G238
[8]  
BISSIG M, 1994, J BIOL CHEM, V269, P3017
[9]   PH GRADIENT-STIMULATED TRANSPORT OF URATE AND PARA-AMINOHIPPURATE IN DOG RENAL MICROVILLUS MEMBRANE-VESICLES [J].
BLOMSTEDT, JW ;
ARONSON, PS .
JOURNAL OF CLINICAL INVESTIGATION, 1980, 65 (04) :931-934
[10]  
Bossuyt X, 1996, J PHARMACOL EXP THER, V276, P891