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Originally published In Press as doi:10.1074/jbc.M107041200 on October 1, 2001

J. Biol. Chem., Vol. 276, Issue 49, 46400-46407, December 7, 2001
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Characterization of Drug Transport by the Human Multidrug Resistance Protein 3 (ABCC3)*

Noam ZelcerDagger , Tohru SaekiDagger §, Glen ReidDagger , Jos H. Beijnen, and Piet BorstDagger ||

From the Dagger  Division of Molecular Biology and Center of Biomedical Genetics, The Netherlands Cancer Institute, Plesmanlaan 121, 1066 CX and  Department of Pharmacy and Pharmacology, Slotervaart Hospital, Louwesweg 6, 1066 EC Amsterdam, The Netherlands

We have characterized the substrate specificity and mechanism of transport of the human multidrug resistance-associated protein 3 (MRP3). A murine fibroblast-like cell line generated from the kidneys of mice that lack Mdr1a/b and Mrp1 was retrovirally transduced with MRP3 cDNA. Stable clones overproducing MRP3 were resistant to the epipodophyllotoxins etoposide and teniposide but not to vincristine, doxorubicin, and cisplatin, drugs suggested to be MRP3 substrates by others. The resistance to etoposide was associated with reduced cellular accumulation and enhanced efflux of this drug and was not affected by depleting cells of glutathione but was inhibited by several common organic anion transport inhibitors. Membrane vesicles from infected insect cells expressing MRP3 mediated ATP-dependent transport of estradiol 17-beta -D-glucuronide, leukotriene C4, dinitrophenyl S-glutathione but not glutathione itself, and etoposide glucuronide, a major metabolite of etoposide in vivo. The transport of estradiol 17-beta -D-glucuronide by MRP3 was inhibited in a concentration-dependent manner by both etoposide and methotrexate. Even though etoposide glucuronide is an excellent substrate for MRP3, this compound is not involved in the etoposide resistance of our MRP3 cells, as these cells extrude unmodified etoposide rather than etoposide glucuronide.

* This work was supported by Dutch Cancer Society Grants NKI 2001-2474 and 1998-1794 (to P. B.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

§ Supported by a postdoctoral fellowship from the Japanese Society for the Promotion of Science. Current address: Laboratory of Molecular Nutrition, Dept. of Biological Resource Chemistry, Faculty of Agricultural Science, Kyoto Prefectural University, Nakaragi, Shimogamo, Sakyo-ku, Kyoto 606-8522, Japan.

|| To whom correspondence should be addressed. Tel.: 31-20-5122880; Fax: 31-20-6691383; E-mail: pborst@nki.nl.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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