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Am J Physiol Gastrointest Liver Physiol 281: G1034-G1043, 2001;
0193-1857/01 $5.00
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Vol. 281, Issue 4, G1034-G1043, October 2001

Single amino acid substitution of rat MRP2 results in acquired transport activity for taurocholate

Kousei Ito, Hiroshi Suzuki, and Yuichi Sugiyama

Graduate School of Pharmaceutical Sciences, University of Tokyo, Tokyo 113-0033, Japan

Multidrug resistance-associated protein 3 (MRP3), unlike other MRPs, transports taurocholate (TC). The difference in TC transport activity between rat MRP2 and MRP3 was studied, focusing on the cationic amino acids in the transmembrane domains. For analysis, transport into membrane vesicles from Sf9 cells expressing wild-type and mutated MRP2 was examined. Substitution of Arg at position 586 with Leu and Ile and substitution of Arg at position 1096 with Lys, Leu, and Met resulted in the acquisition of TC transport activity, while retaining transport activity for glutathione and glucuronide conjugates. Substitution of Leu at position 1084 of rat MRP3 (which corresponds to Arg-1096 in rat MRP2) with Lys, but not with Val or Met, resulted in the loss of transport activity for TC and glucuronide conjugates. These results suggest that the presence of the cationic charge at Arg-586 and Arg-1096 in rat MRP2 prevents the transport of TC, whereas the presence of neutral amino acids at the corresponding position of rat MRP3 is required for the transport of substrates.

adenosine 5'-triphosphate-binding cassette transporter superfamily; bile acid; site-directed mutagenesis; multidrug resistance-associated protein 2


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