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Volume 272, Number 25, Issue of June 20, 1997 pp. 15789-15795
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

Lipocalin-type Prostaglandin D Synthase (-Trace) Is a Newly Recognized Type of Retinoid Transporter

(Received for publication, December 17, 1996, and in revised form, March 21, 1997)

Toshiki Tanaka ^§ , Yoshihiro Urade , Hiromi Kimura , Naomi Eguchi ^** , Akemi Nishikawa ^§ and Osamu Hayaishi

From  Protein Engineering Research Institute, 6-2-3 Furuedai, Suita, Osaka 565, Japan, the ^§ Biomolecular Engineering Research Institute, 6-2-3 Furuedai, Suita, Osaka 565, Japan,  Osaka Bioscience Institute, 6-2-4 Furuedai, Suita, Osaka 565, Japan, and ^** PRESTO, Japan Science and Technology Corporation, 6-2-4 Furuedai, Suita, Osaka 565, Japan

Lipocalin-type prostaglandin D synthase is responsible for the biosynthesis of prostaglandin D₂ in the central nervous system and the genital organs and is secreted into the cerebrospinal fluid and the seminal plasma as -trace. Here we analyzed retinoids binding of the enzyme by monitoring the fluorescence quenching of an intrinsic tryptophan residue, and appearance of circular dichroism around 330 nm, and a red shift of the UV absorption spectra of retinoids. We found that the enzyme binds all-trans- or 9-cis-retinoic acid and all-trans- or 13-cis-retinal, but not all-trans-retinol, with affinities (K_d of 70-80 nM) sufficient for function as a retinoid transporter. All-trans-retinoic acid inhibited the enzyme activity in a noncompetitive manner, suggesting that it binds to the same hydrophobic pocket as prostaglandin H₂, the substrate for prostaglandin D synthase, but at a different site in this pocket. It is likely that this enzyme is a bifunctional protein that acts as both retinoid transporter and prostaglandin D₂-producing enzyme.

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