Molecular characterization of human and rat organic anion transporter OATP-D

Hisanobu Adachi, Takehiro Suzuki, Michiaki Abe, Naoki Asano, Hiroya Mizutamari, Masayuki Tanemoto, Toshiyuki Nishio, Tohru Onogawa, Takafumi Toyohara, Satoshi Kasai, Fumitoshi Satoh, Masanori Suzuki, Taro Tokui, Michiaki Unno, Tooru Shimosegawa, Seiki Matsuno, Sadayoshi Ito, Takaaki Abe

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83 Citations (Scopus)


We have isolated and characterized a novel human and rat organic anion transporter subtype, OATP-D. The isolated cDNA from human brain encodes a polypeptide of 710 amino acids (Mr 76,534) with 12 predicted transmembrane domains. The rat clone encodes 710 amino acids (Mr 76,821) with 97.6% amino acid sequence homology with human OATP-D. Human and rat OATP-D have moderate amino acid sequence homology with LST-1/rlst-1, the rat oatp family, the prostaglandin transporter, and moat1/MOAT1/KIAA0880/OATP-B. Phylogenetic tree analysis revealed that OATP-D is branched in a different position from all known organic anion transporters. OATP-D transports prostaglandin E1 (Km 48.5 nM), prostaglandin E 2 (Km 55.5 nM), and prostaglandin F, suggesting that, functionally, OATP-D encodes a protein that has similar characteristics to those of the prostaglandin transporter. Rat OATP-D also transports prostaglandins. The expression pattern of OATP-D mRNA was abundant mainly in the heart, testis, brain, and some cancer cells. Immunohistochemical analysis further revealed that rat OATP-D is widely expressed in the vascular, renal, and reproductive system at the protein level. These results suggest that OATP-D plays an important role in translocating prostaglandins in specialized tissues and cells.

Original languageEnglish
Pages (from-to)F1188-F1197
JournalAmerican Journal of Physiology - Renal Physiology
Issue number6 54-6
Publication statusPublished - 2003 Dec


  • Eicosanoid
  • Prostaglandin transporter

ASJC Scopus subject areas

  • Physiology
  • Urology


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