Arsenic transport by the human multidrug resistance protein 1 (MRP1/ABCC1). Evidence that a tri-glutathione conjugate is required

scientific article published on 25 May 2004

Arsenic transport by the human multidrug resistance protein 1 (MRP1/ABCC1). Evidence that a tri-glutathione conjugate is required is …
instance of (P31):
scholarly articleQ13442814

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P356DOI10.1074/JBC.M404912200
P698PubMed publication ID15161912

P50authorMichael P. WaalkesQ113460555
P2093author name stringElaine M Leslie
Anass Haimeur
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The MRP1-mediated effluxes of arsenic and antimony do not require arsenic-glutathione and antimony-glutathione complex formation.Q34129121
The MRP-related and BCRP/ABCG2 multidrug resistance proteins: biology, substrate specificity and regulationQ34298925
Toxicological relevance of the multidrug resistance protein 1, MRP1 (ABCC1) and related transporters.Q34369690
Reactive intermediates and the dynamics of glutathione transferasesQ34849031
Biochemistry of arsenic detoxificationQ34922203
An ATP-dependent As(III)-glutathione transport system in membrane vesicles of Leishmania tarentolaeQ37713114
A naturally occurring mutation in MRP1 results in a selective decrease in organic anion transport and in increased doxorubicin resistanceQ38288677
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.Q38297880
Membrane association of glutathione S-transferase mGSTA4-4, an enzyme that metabolizes lipid peroxidation productsQ39586133
Glutathione S-transferase M1 and multidrug resistance protein 1 act in synergy to protect melanoma cells from vincristine effects.Q40573414
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 analogQ40803174
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 transportQ40816606
New mechanisms of drug resistance in parasitic protozoaQ40945183
ATP- and glutathione-dependent transport of chemotherapeutic drugs by the multidrug resistance protein MRP1.Q40962980
ATP-dependent 17 beta-estradiol 17-(beta-D-glucuronide) transport by multidrug resistance protein (MRP). Inhibition by cholestatic steroidsQ41204983
Multidrug resistance protein (MRP)-mediated transport of leukotriene C4 and chemotherapeutic agents in membrane vesicles. Demonstration of glutathione-dependent vincristine transportQ41204990
Glutathione S-transferase pi facilitates the excretion of arsenic from arsenic-resistant Chinese hamster ovary cellsQ41553883
Glutathione S-transferase pi in an arsenic-resistant Chinese hamster ovary cell lineQ41589397
Arsenate Reduction in Human Erythrocytes and Rats--Testing the Role of Purine Nucleoside PhosphorylaseQ42440733
Co-amplification of the gamma-glutamylcysteine synthetase gene gsh1 and of the ABC transporter gene pgpA in arsenite-resistant Leishmania tarentolae.Q42619754
ATP-dependent glutathione disulphide transport mediated by the MRP gene-encoded conjugate export pumpQ42981150
Steroid and bile acid conjugates are substrates of human multidrug-resistance protein (MRP) 4 (ATP-binding cassette C4).Q43002793
The Leishmania ATP-binding cassette protein PGPA is an intracellular metal-thiol transporter ATPase.Q43578165
Arsenate reductase II. Purine nucleoside phosphorylase in the presence of dihydrolipoic acid is a route for reduction of arsenate to arsenite in mammalian systemsQ43998876
Charged amino acids in the sixth transmembrane helix of multidrug resistance protein 1 (MRP1/ABCC1) are critical determinants of transport activityQ44108486
Purine nucleoside phosphorylase as a cytosolic arsenate reductaseQ44186169
Structural requirements for functional interaction of glutathione tripeptide analogs with the human multidrug resistance protein 1 (MRP1).Q44285538
Functional and structural consequences of cysteine substitutions in the NH2 proximal region of the human multidrug resistance protein 1 (MRP1/ABCC1).Q44430387
Oxidation and detoxification of trivalent arsenic speciesQ44652900
Polymorphisms in the human monomethylarsonic acid (MMA V) reductase/hGSTO1 gene and changes in urinary arsenic profilesQ44696763
Formation and urinary excretion of arsenic triglutathione and methylarsenic diglutathioneQ44766396
Mutations of charged amino acids in or near the transmembrane helices of the second membrane spanning domain differentially affect the substrate specificity and transport activity of the multidrug resistance protein MRP1 (ABCC1).Q44904900
Role of the Multidrug Resistance Protein 1 in protection from heavy metal oxyanions: investigations in vitro and in MRP1-deficient miceQ45713478
Glutathione-dependent biliary excretion of arsenicQ45777659
Molecular cloning, characterization, and expression in Escherichia coli of full-length cDNAs of three human glutathione S-transferase Pi gene variants. Evidence for differential catalytic activity of the encoded proteinsQ48051232
In vitro inhibition of glutathione reductase by arsenotriglutathioneQ49271013
Monoclonal antibodies that inhibit the transport function of the 190-kDa multidrug resistance protein, MRP. Localization of their epitopes to the nucleotide-binding domains of the protein.Q54095422
P433issue31
P407language of work or nameEnglishQ1860
P921main subjectmultiple drug resistanceQ643839
P304page(s)32700-32708
P577publication date2004-05-25
P1433published inJournal of Biological ChemistryQ867727
P1476titleArsenic transport by the human multidrug resistance protein 1 (MRP1/ABCC1). Evidence that a tri-glutathione conjugate is required
P478volume279

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