Does ABCG2 Need a Heterodimer Partner? Expression and Functional Evaluation of ABCG2 (Arg 482)*

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  • YOSHIKAWA Megumi
    Department of Biomolecular Engineering, Graduate School of Bioscience and Biotechnology, Tokyo Institute of Technology Department of Drug Metabolism and Disposition, Meiji Pharmaceutical University
  • KASAMATSU Shiho
    Department of Biomolecular Engineering, Graduate School of Bioscience and Biotechnology, Tokyo Institute of Technology
  • YASUNAGA Masa
    Department of Biomolecular Engineering, Graduate School of Bioscience and Biotechnology, Tokyo Institute of Technology
  • WANG Guizhi
    Department of Biomolecular Engineering, Graduate School of Bioscience and Biotechnology, Tokyo Institute of Technology GS PlatZ Co. Ltd., Nihonbashi
  • IKEGAMI Yoji
    Department of Drug Metabolism and Disposition, Meiji Pharmaceutical University
  • YOSHIDA Hisahiro
    Department of Drug Metabolism and Disposition, Meiji Pharmaceutical University
  • TARUI Shigeki
    GS PlatZ Co. Ltd., Nihonbashi
  • YABUUCHI Hikaru
    Department of Biomolecular Engineering, Graduate School of Bioscience and Biotechnology, Tokyo Institute of Technology
  • ISHIKAWA Toshihisa
    Department of Biomolecular Engineering, Graduate School of Bioscience and Biotechnology, Tokyo Institute of Technology

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  Accumulating evidence suggests that several ATP-binding cassette (ABC) transporters mediate the elimination of anticancer drugs from cancer cells and thereby confer drug resistance. SN-38-selected PC-6/SN2-5H human lung carcinoma cells were shown to overexpress ABCG2 with the reduced intracellular accumulation of SN-38, the active metabolite of irinotecan. We have recently demonstrated that plasma membrane vesicles prepared from those cells transported SN-38 in an ATP-dependent manner, and it was suggested that ABCG2 is involved in the active extrusion of SN-38 from cancer cells. In the present study, we have cloned the cDNA of ABCG2 from PC-6/SN2-5H human lung carcinoma cells, expressed ABCG2 in Sf9 insect cells, and characterized its function. Sequence analysis has revealed that the cloned ABCG2 has an arginine at the amino acid position 482, as does the wild type. Expression of the cloned ABCG2 in Sf9 cell membranes was detected by immunoblotting with the BXP-21 antibody. Contrary to our expectation, however, ATPase activity in the cell membranes expressing ABCG2 was stimulated by neither SN-38 nor rhodamine 123. It is suggested that there is a partner protein of ABCG2 required for heterodimer formation to exhibit transport activity toward SN-38.<br>

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