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Vol. 273, Issue 3, 1684-1688, January 16, 1998
From the Transport of many organic anions across the bile
canalicular membrane is mediated by the canalicular multispecific
organic anion transporter (cMOAT). Previously, we cloned cDNA that
may encode cMOAT from Sprague-Dawley rat liver (Ito, K., Suzuki, H., Hirohashi, T., Kume, K., Shimizu, T., and Sugiyama, Y. (1997) Am. J. Physiol. 272, G16-G22). In the present study,
the function of this cloned cDNA was investigated by examining the
ATP-dependent uptake of
S-(2,4-dinitrophenyl)-glutathione (DNP-SG) into membrane vesicles isolated from an NIH/3T3 cell line transfected with an expression vector containing the cloned cDNA. Although the membrane vesicles from the control NIH/3T3 cells exhibited endogenous activity in transporting DNP-SG and leukotriene C4 in an
ATP-dependent manner, the transfection of cMOAT cDNA
resulted in a significant increase in the transport activity for these
ligands. The uptake of DNP-SG into membrane vesicles was osmotically
sensitive and was stimulated to some extent by other nucleotide
triphosphates (GTP, UTP, and CTP) but not by AMP or ADP. The
Km and Vmax values for the
uptake of DNP-SG by the membrane vesicles were 0.175 ± 0.031 µM and 11.0 ± 0.73 pmol/min/mg protein,
respectively, for the transfected rat cMOAT and 0.141 ± 0.036 µM and 3.51 ± 0.39 pmol/min/mg protein,
respectively, for the endogenous transporter expressed on control
NIH/3T3 cells. These results suggest that the product of the previously
cloned cDNA has cMOAT activity being able to transport organic
anions in an ATP-dependent manner. Alternatively, it is
possible that the cDNA product encodes an activator of endogenous transporter since the Km value for DNP-SG was
comparable between the vector- and cMOAT-transfected cells. The
transport activity found in the control NIH/3T3 cells may be ascribed
to mouse cMOAT since Northern blot analysis indicated the presence of a
transcript that hybridyzed to the carboxyl-terminal ATP-binding cassette sequence of the murine protein.
Functional Analysis of a Canalicular Multispecific Organic Anion
Transporter Cloned from Rat Liver
,,,
Faculty of Pharmaceutical Sciences and the
§ Faculty of Medicine, The University of Tokyo, Hongo,
Bunkyo-ku, Tokyo 113, Japan
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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