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Vol. 57, Issue 4, 760-768, April 2000
National Institute of Haematology and Immunology, Research
Group of the Hungarian Academy of Sciences, Budapest, Hungary (E.B.,
E.S., B.S.); Institute of Enzymology, Biological Research Center,
Hungarian Academy of Sciences, Budapest, Hungary (E.B., A.V.); and The
Netherlands Cancer Institute, Amsterdam, The Netherlands (R.E., P.B.)
The human multidrug resistance protein MRP1 and its homolog, MRP2, are
both suggested as being involved in cancer drug resistance and the
transport of organic anions. We expressed MRP1 and MRP2 in
Spodoptera frugiperda ovarian cells and compared their
ATP-dependent transport properties and vanadate-sensitive ATPase
activities in isolated membrane vesicles. Both MRP1 and MRP2 actively
transported leukotriene C4 and
N-ethylmaleimide glutathione (NEM-GS), although the
relative affinity of MRP2 for these substrates was found to be
significantly lower than that of MRP1. Methotrexate was actively transported by both proteins, although more efficiently by MRP2. ATP-dependent NEM-GS transport by MRP1 and MRP2 was variably modulated by organic anions. Probenecid and furosemide inhibited, whereas under
certain conditions sulfinpyrazone, penicillin G, and indomethacin greatly stimulated, MRP2-mediated NEM-GS uptake. Vanadate-sensitive ATPase activity in isolated membranes containing MRP1 or MRP2 was
significantly stimulated by NEM-GS and reduced GS, although these
compounds acted only at higher concentrations in MRP2. ATP hydrolysis
by MRP2 was also effectively stimulated by methotrexate. Probenecid,
sulfinpyrazone, indomethacin, furosemide, and penicillin G all
significantly increased MRP2-ATPase activity, whereas these compounds
acted more as ATPase inhibitors on MRP1. These results indicate that
MRP1 is a more efficient transporter of glutathione conjugates and free
glutathione than MRP2, whereas several anions are preferred substrates
for MRP2. Our data suggest that MRP2 may be responsible for the active
secretion of pharmacologically relevant organic anions, such as
diuretics and antibiotics, and indicate different modulation
possibilities for MRP1 or MRP2 in drug-resistant tumor cells.
e 42-44, 60596 Frankfurt a. M, Germany.
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K.-i. Ito, S. L. Olsen, W. Qiu, R. G. Deeley, and S. P. C. Cole Mutation of a Single Conserved Tryptophan in Multidrug Resistance Protein 1 (MRP1/ABCC1) Results in Loss of Drug Resistance and Selective Loss of Organic Anion Transport J. Biol. Chem., May 4, 2001; 276(19): 15616 - 15624. [Abstract] [Full Text] [PDF]
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E. M. Leslie, K.-i. Ito, P. Upadhyaya, S. S. Hecht, R. G. Deeley, and S. P. C. Cole Transport of the beta -O-Glucuronide Conjugate of the Tobacco-specific Carcinogen 4-(Methylnitrosamino)-1-(3-pyridyl)-1-butanol (NNAL) by the Multidrug Resistance Protein 1 (MRP1). REQUIREMENT FOR GLUTATHIONE OR A NON-SULFUR-CONTAINING ANALOG J. Biol. Chem., July 20, 2001; 276(30): 27846 - 27854. [Abstract] [Full Text] [PDF]
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K.-i. Ito, C. J. Oleschuk, C. Westlake, M. Z. Vasa, R. G. Deeley, and S. P. C. Cole Mutation of Trp1254 in the Multispecific Organic Anion Transporter, Multidrug Resistance Protein 2 (MRP2) (ABCC2), Alters Substrate Specificity and Results in Loss of Methotrexate Transport Activity J. Biol. Chem., October 5, 2001; 276(41): 38108 - 38114. [Abstract] [Full Text] [PDF]
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