HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

J. Biol. Chem., Vol. 280, Issue 37, 32332-32339, September 16, 2005

This Article Full Text Full Text (PDF) All Versions of this Article: 280/37/32332    most recent M504246200v1 Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Kobayashi, Y. Articles by Yamamoto, T. Search for Related Content PubMed PubMed Citation Articles by Kobayashi, Y. Articles by Yamamoto, T. Social Bookmarking                      What's this?

Isolation and Functional Characterization of a Novel Organic Solute Carrier Protein, hOSCP1^*

From the Department of Clinical Pharmacy, School of Pharmaceutical Sciences, Showa University, 1-5-8 Hatanodai, Shinagawa-ku, Tokyo 142-8555, Japan

We succeeded in isolating a novel organic solute carrier from a human placenta cDNA library. The isolated cDNA consisted of 1137 base pairs that encoded a 379-amino acid protein, hOSCP1. Northern blot and reverse transcription PCR analyses revealed that the hOSCP1 mRNA is expressed in the placenta and testis and weakly expressed in the thymus and small intestine. When expressed in Xenopus laevis oocytes, hOSCP1 mediated the high affinity transport of p-aminohippurate (PAH) (K_m = 35.0 ± 7.5 µM) and tetraethylammonium (K_m = 62.3 ± 12.2 µM) in a sodium-independent manner. However, the hOSCP1-expressing oocyte did not mediate the transport of L-carnitine. The transport of PAH by hOSCP1 was sensitive to pH, but the tetraethylammonium was not transported at the high pH examined. hOSCP1 transported prostaglandin E₂, prostaglandin F₂, estrone sulfate, glutarate, L-leucine, L-ascorbic acid, and tetracycline. Thus, hOSCP1 also showed broad substrate specificity. A wide range of structurally unrelated organic compounds inhibited the hOSCP1-mediated PAH uptake. Immunohistochemical analysis revealed that the hOSCP1 protein is localized in the basal membrane of the syncytiotrophoblast in the human placenta. Our results suggest that hOSCP1 is a novel polyspecific organic solute carrier protein responsible for drug clearance from the human placenta.

Received for publication, April 19, 2005 , and in revised form, June 21, 2005.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBank^TM/EBI Data Bank with accession number(s) AB079075 and AB076694.

^* This work was supported in part by Japanese Ministry of Education Science, Sports and Culture Grant 16659042. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

¹ Present address: Dept. of Physiology and Biophysics, The University of Texas Medical Branch, Galveston, TX 77555-0641.

² To whom correspondence should be addressed. Tel.: 81-3-3784-8220; Fax: 81-3-3784-3838; E-mail: yamagen{at}pharm.showa-u.ac.jp.

CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				J. Geyer, B. Doring, K. Meerkamp, B. Ugele, N. Bakhiya, C. F. Fernandes, J. R. Godoy, H. Glatt, and E. Petzinger Cloning and Functional Characterization of Human Sodium-dependent Organic Anion Transporter (SLC10A6) J. Biol. Chem., July 6, 2007; 282(27): 19728 - 19741. [Abstract] [Full Text] [PDF]

				Y. Kobayashi, A. Tsuchiya, T. Hayashi, N. Kohyama, M. Ohbayashi, and T. Yamamoto Isolation and Characterization of Polyspecific Mouse Organic Solute Carrier Protein 1 (mOscp1) Drug Metab. Dispos., July 1, 2007; 35(7): 1239 - 1245. [Abstract] [Full Text] [PDF]