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Vol. 55, Issue 5, 929-937, May 1999
Deutsches Krebsforschungszentrum, Heidelberg, Germany
The multidrug resistance protein MRP1 functions as an ATP-dependent
conjugate export pump and confers multidrug resistance. We cloned MRP2
(symbol ABCC2), a MRP family member localized to the apical membrane of
polarized cells. Stable expression of MRP2 in transfected human
embryonic kidney (HEK-293) and Madin-Darby canine kidney (MDCK) cells
was enhanced by inhibitors of histone deacetylase. In polarized MDCK
cells, both rat and human MRP2 were sorted to the apical plasma
membrane. An antibody raised against the amino terminus of rat MRP2
recognized the recombinant protein on the apical surface of
nonpermeabilized cells, providing direct evidence for the extracellular
localization of the amino terminus of MRP2. ATP-dependent transport by
recombinant human and rat MRP2 was measured with membrane vesicles from
stably transfected cells. The Km value of
human MRP2 was 1.0 ± 0.1 µM for leukotriene C4 and
7.2 ± 0.7 µM for 17
-glucuronosyl estradiol; the
Km values of human MRP1 were 0.1 ± 0.02 µM for leukotriene C4 and 1.5 ± 0.3 µM for
17-glucoronosyl estradiol. Thus, the
conjugate-transporting ATPases MRP2 and MRP1 differ not only by
their domain-specific localization but also by their kinetic
properties. Drug resistance conferred by recombinant MRP2 was studied
in MDCK and HEK-293 cells using cell viability assays. Expression of
human and rat MRP2 enhanced the resistance of MDCK cells to etoposide
5.0-fold and 3.8-fold and to vincristine 2.3- and 6.0-fold,
respectively. Buthionine sulfoximine reduced resistance to these drugs.
Human MRP2 overexpressed in HEK-293 cells enhanced the resistance to etoposide (4-fold), cisplatin (10-fold), doxorubicin (7.8-fold), and
epirubicin (5-fold). These results demonstrate that MRP2 confers resistance to cytotoxic drugs.
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