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J. Biol. Chem., Vol. 269, Issue 45, 27807-27810, Nov, 1994
I Leier, G Jedlitschky, U Buchholz, SP Cole, RG Deeley and D Keppler
The multidrug resistance-associated protein (MRP) is the product of an
ATP-binding cassette transporter gene overexpressed in some tumor cells
resistant to antineoplastic agents. We studied the transport function of
MRP in membrane vesicles prepared from HeLa cells transfected with an MRP
expression vector and overexpressing this 190-kDa membrane glycoprotein.
ATP-dependent primary-active transport into the vesicles was demonstrated
for leukotriene C4 (LTC4), LTD4, LTE4, and S-(2,4-
dinitrophenyl)glutathione with relative rates, at a substrate concentration
of 50 nM, of 1.0, 0.27, 0.14, and 0.16, respectively. The endogenous
glutathione conjugate LTC4 had the highest affinity for this transporter
with a Km of 97 nM. The Km for ATP was 19 microM. Direct photoaffinity
labeling with [3H]LTC4 labeled a 190-kDa membrane protein predominantly in
the MRP-transfected HeLa cells. ATP-dependent LTC4 transport was
effectively inhibited by the LTD4 receptor antagonist MK 571, whereas
cyclosporin A and, particularly, its analog PSC 833 were much less potent.
The respective Ki values were 0.6, 5, and 27 microM, respectively. In
addition, MK 571 preferentially inhibited photoaffinity labeling of the
190-kDa protein in the MRP transfectants. Our results provide direct
evidence that the MRP gene encodes a primary- active ATP-dependent export
pump for conjugates of lipophilic compounds with glutathione and several
other anionic residues. We conclude that the biosynthetic release of LTC4
from cells is mediated by the 190-kDa product of the MRP gene.
The MRP gene encodes an ATP-dependent export pump for leukotriene C4 and structurally related conjugates
Division of Tumor Biochemistry, Deutsches Krebsforschungszentrum, Heidelberg, Federal Republic of Germany.
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