Pflügers Archiv

, Volume 440, Issue 3, pp 337–350

The multispecific organic anion transporter (OAT) family

  • Takashi Sekine
  • Seok Ho Cha
  • Hitoshi Endou
Invited Review

DOI: 10.1007/s004240000297

Cite this article as:
Sekine, T., Cha, S. & Endou, H. Eur J Physiol (2000) 440: 337. doi:10.1007/s004240000297

Abstract.

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.

Organic anion p-Aminohippurate Multispecific organic anion transporter Tubular secretion Xenobiotics Pharmacokinetics 

Copyright information

© Springer-Verlag 2000

Authors and Affiliations

  • Takashi Sekine
    • 1
  • Seok Ho Cha
    • 1
  • Hitoshi Endou
    • 1
  1. 1.Department of Pharmacology and Toxicology, Kyorin University School of Medicine, 6-20-2 Shinkawa, Mitaka, Tokyo 181-8611, Japan

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