PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 32377003-2 2020 Glutathione (GSH) plays a key role in MRP1 transport activities. Glutathione 13-16 ATP binding cassette subfamily B member 1 Homo sapiens 38-42 32377003-2 2020 Glutathione (GSH) plays a key role in MRP1 transport activities. Glutathione 0-11 ATP binding cassette subfamily B member 1 Homo sapiens 38-42 32377003-3 2020 In addition, a ligand-stimulated GSH transport which triggers the death of cells overexpressing MRP1, by collateral sensitivity (CS), has been described. Glutathione 33-36 ATP binding cassette subfamily B member 1 Homo sapiens 96-100 32377003-5 2020 The molecular mechanism of such massive GSH transport and its connection to the other transport activities of MRP1 are unknown. Glutathione 40-43 ATP binding cassette subfamily B member 1 Homo sapiens 110-114 32377003-9 2020 The flexibility of that loop and the binding of a CS agent like verapamil could favor a particular conformation for the massive transport of GSH, not related to other transport activities of MRP1. Glutathione 141-144 ATP binding cassette subfamily B member 1 Homo sapiens 191-195 31268744-1 2019 The human multidrug resistance protein 1 (hMRP1) transporter is implicated in cancer multidrug resistance as well as immune responses involving its physiologic substrate, glutathione (GSH)-conjugated leukotriene C4 (LTC4). Glutathione 171-182 ATP binding cassette subfamily B member 1 Homo sapiens 10-40 31268744-2 2019 LTC4 binds a bipartite site on hMRP1, which a recent cryoelectron microscopy structure of LTC4-bound bovine Mrp1 depicts as composed of a positively charged pocket and a hydrophobic (H) pocket that binds the GSH moiety and surrounds the fatty acid moiety, respectively, of LTC4. Glutathione 208-211 ATP binding cassette subfamily B member 1 Homo sapiens 108-112 31302132-3 2019 We characterized a novel small molecule modulator that selectively enhanced MRP1-dependent efflux of reduced glutathione (GSH), an endogenous MRP1 substrate. Glutathione 109-120 ATP binding cassette subfamily B member 1 Homo sapiens 76-80 31302132-3 2019 We characterized a novel small molecule modulator that selectively enhanced MRP1-dependent efflux of reduced glutathione (GSH), an endogenous MRP1 substrate. Glutathione 109-120 ATP binding cassette subfamily B member 1 Homo sapiens 142-146 31302132-3 2019 We characterized a novel small molecule modulator that selectively enhanced MRP1-dependent efflux of reduced glutathione (GSH), an endogenous MRP1 substrate. Glutathione 122-125 ATP binding cassette subfamily B member 1 Homo sapiens 76-80 31302132-3 2019 We characterized a novel small molecule modulator that selectively enhanced MRP1-dependent efflux of reduced glutathione (GSH), an endogenous MRP1 substrate. Glutathione 122-125 ATP binding cassette subfamily B member 1 Homo sapiens 142-146 31302132-4 2019 Using cell lines expressing high levels of endogenous MRP1 from three difficult to treat cancer types-lung cancer, ovarian cancer and high-risk neuroblastoma-we showed that the MRP1 modulator substantially lowered intracellular GSH levels as a single agent. Glutathione 228-231 ATP binding cassette subfamily B member 1 Homo sapiens 54-58 31302132-4 2019 Using cell lines expressing high levels of endogenous MRP1 from three difficult to treat cancer types-lung cancer, ovarian cancer and high-risk neuroblastoma-we showed that the MRP1 modulator substantially lowered intracellular GSH levels as a single agent. Glutathione 228-231 ATP binding cassette subfamily B member 1 Homo sapiens 177-181 31302132-5 2019 The effect was on-target, as MRP1 knockdown abolished GSH depletion. Glutathione 54-57 ATP binding cassette subfamily B member 1 Homo sapiens 29-33 31302132-6 2019 The MRP1 modulator was synergistic with the GSH synthesis inhibitor buthionine sulfoximine (BSO), with the combination exhausting intracellular GSH, increasing intracellular reactive oxygen species (ROS) and abolishing clonogenic capacity. Glutathione 44-47 ATP binding cassette subfamily B member 1 Homo sapiens 4-8 31302132-6 2019 The MRP1 modulator was synergistic with the GSH synthesis inhibitor buthionine sulfoximine (BSO), with the combination exhausting intracellular GSH, increasing intracellular reactive oxygen species (ROS) and abolishing clonogenic capacity. Glutathione 144-147 ATP binding cassette subfamily B member 1 Homo sapiens 4-8 31302132-9 2019 GSH-depleting MRP1 modulators may therefore provide an enhanced therapeutic window to treat chemo-resistant MRP1-overexpressing pediatric and adult cancers. Glutathione 0-3 ATP binding cassette subfamily B member 1 Homo sapiens 14-18 31302132-9 2019 GSH-depleting MRP1 modulators may therefore provide an enhanced therapeutic window to treat chemo-resistant MRP1-overexpressing pediatric and adult cancers. Glutathione 0-3 ATP binding cassette subfamily B member 1 Homo sapiens 108-112 31268744-1 2019 The human multidrug resistance protein 1 (hMRP1) transporter is implicated in cancer multidrug resistance as well as immune responses involving its physiologic substrate, glutathione (GSH)-conjugated leukotriene C4 (LTC4). Glutathione 184-187 ATP binding cassette subfamily B member 1 Homo sapiens 10-40 27855620-0 2017 MRP1-dependent Collateral Sensitivity of Multidrug-resistant Cancer Cells: Identifying Selective Modulators Inducing Cellular Glutathione Depletion. Glutathione 126-137 ATP binding cassette subfamily B member 1 Homo sapiens 0-4 30806880-8 2019 Our study demonstrates that menadione rapidly depletes cultured astrocytes of GSH via ROS-induced oxidation to GSSG that is subsequently exported via Mrp1. Glutathione 78-81 ATP binding cassette subfamily B member 1 Homo sapiens 150-154 28303926-7 2017 Our results showed that MDR (P-gp overexpressing) cells have a different metabolic profile from their drug-sensitive counterparts, demonstrating decreases in the pentose phosphate pathway and oxidative phosphorylation rate; increases in glutathione metabolism and glycolysis; and alterations in the methionine/S-adenosylmethionine pathway. Glutathione 237-248 ATP binding cassette subfamily B member 1 Homo sapiens 29-33 30726737-4 2019 Disruption of the ATP binding cassette (ABC)-family transporter multidrug resistance protein 1 (MRP1) prevents glutathione efflux from the cell and strongly inhibits ferroptosis. Glutathione 111-122 ATP binding cassette subfamily B member 1 Homo sapiens 64-94 30726737-4 2019 Disruption of the ATP binding cassette (ABC)-family transporter multidrug resistance protein 1 (MRP1) prevents glutathione efflux from the cell and strongly inhibits ferroptosis. Glutathione 111-122 ATP binding cassette subfamily B member 1 Homo sapiens 96-100 24875445-0 2014 Collateral sensitivity of resistant MRP1-overexpressing cells to flavonoids and derivatives through GSH efflux. Glutathione 100-103 ATP binding cassette subfamily B member 1 Homo sapiens 36-40 27738951-5 2017 In addition, dual-drug loaded hybrid nanovesicles exhibit significantly stronger cell growth inhibition as compared with doxorubicin (DOX) mono-drug loaded nanovesicles due to the reduced intracellular glutathione (GSH) content by buthionine sulfoximine (BSO) or the P-glycoprotein (P-gp) inhibition by tariquidar (TQR). Glutathione 215-218 ATP binding cassette subfamily B member 1 Homo sapiens 267-281 27738951-5 2017 In addition, dual-drug loaded hybrid nanovesicles exhibit significantly stronger cell growth inhibition as compared with doxorubicin (DOX) mono-drug loaded nanovesicles due to the reduced intracellular glutathione (GSH) content by buthionine sulfoximine (BSO) or the P-glycoprotein (P-gp) inhibition by tariquidar (TQR). Glutathione 215-218 ATP binding cassette subfamily B member 1 Homo sapiens 283-287 27572418-10 2016 Incubation of HAEC with quercetin also led to the appearance of extracellular quercetin-glutathione conjugates, which was paralleled by upregulation of the multidrug resistance protein 1 (MRP1). Glutathione 88-99 ATP binding cassette subfamily B member 1 Homo sapiens 188-192 25281745-3 2014 The antioxidant GSH and the pro-inflammatory cysteinyl leukotriene C4 have been identified as key physiological organic anions effluxed by MRP1, and an ever growing body of evidence indicates that additional lipid-derived mediators are also substrates of this transporter. Glutathione 16-19 ATP binding cassette subfamily B member 1 Homo sapiens 139-143 24875445-1 2014 The multidrug resistance protein 1 (MRP1) is involved in multidrug resistance of cancer cells by mediating drug efflux out of cells, often in co-transport with glutathione (GSH). Glutathione 160-171 ATP binding cassette subfamily B member 1 Homo sapiens 4-34 24875445-1 2014 The multidrug resistance protein 1 (MRP1) is involved in multidrug resistance of cancer cells by mediating drug efflux out of cells, often in co-transport with glutathione (GSH). Glutathione 160-171 ATP binding cassette subfamily B member 1 Homo sapiens 36-40 24875445-1 2014 The multidrug resistance protein 1 (MRP1) is involved in multidrug resistance of cancer cells by mediating drug efflux out of cells, often in co-transport with glutathione (GSH). Glutathione 173-176 ATP binding cassette subfamily B member 1 Homo sapiens 4-34 24875445-1 2014 The multidrug resistance protein 1 (MRP1) is involved in multidrug resistance of cancer cells by mediating drug efflux out of cells, often in co-transport with glutathione (GSH). Glutathione 173-176 ATP binding cassette subfamily B member 1 Homo sapiens 36-40 24875445-2 2014 GSH efflux mediated by MRP1 can be stimulated by verapamil. Glutathione 0-3 ATP binding cassette subfamily B member 1 Homo sapiens 23-27 24875445-3 2014 In cells overexpressing MRP1, we have previously shown that verapamil induced a huge intracellular GSH depletion which triggered apoptosis of the cells. Glutathione 99-102 ATP binding cassette subfamily B member 1 Homo sapiens 24-28 24875445-6 2014 A large number of these compounds stimulate MRP1-mediated GSH efflux and the most active ones have been evaluated for their cytotoxic effect on MRP1-overexpressing cells versus parental cells. Glutathione 58-61 ATP binding cassette subfamily B member 1 Homo sapiens 44-48 24146141-4 2014 We sought to determine the role of multidrug resistance protein 1 (MRP1) in GSH depletion and its regulatory role on extrinsic and intrinsic pathways of apoptosis. Glutathione 76-79 ATP binding cassette subfamily B member 1 Homo sapiens 35-65 24146141-4 2014 We sought to determine the role of multidrug resistance protein 1 (MRP1) in GSH depletion and its regulatory role on extrinsic and intrinsic pathways of apoptosis. Glutathione 76-79 ATP binding cassette subfamily B member 1 Homo sapiens 67-71 23800365-7 2013 Although moderate concentrations of formaldehyde are not acutely toxic for brain cells, exposure to formaldehyde severely affects their metabolism as demonstrated by the formaldehyde-induced acceleration of glycolytic flux and by the rapid multidrug resistance protein 1-mediated export of glutathione from both astrocytes and neurons. Glutathione 290-301 ATP binding cassette subfamily B member 1 Homo sapiens 240-270 24050699-4 2014 MRP1 also plays a role in the cellular efflux of the reduced and oxidized forms of GSH and thus contributes to the many physiological and pathophysiological processes influenced by these small peptides, including oxidative stress. Glutathione 83-86 ATP binding cassette subfamily B member 1 Homo sapiens 0-4 19398503-2 2009 MRP1 also transports glutathione (GSH); furthermore, this tripeptide stimulates transport of several substrates, including estrone 3-sulfate. Glutathione 21-32 ATP binding cassette subfamily B member 1 Homo sapiens 0-4 23341120-6 2013 The ritonavir-induced stimulated GSH export from astrocytes was completely prevented by MK571, an inhibitor of the multidrug resistance protein 1. Glutathione 33-36 ATP binding cassette subfamily B member 1 Homo sapiens 115-145 22464990-0 2012 Glutathione-mediated neuroprotection against methylmercury neurotoxicity in cortical culture is dependent on MRP1. Glutathione 0-11 ATP binding cassette subfamily B member 1 Homo sapiens 109-113 22464990-11 2012 Taken together, these data suggest glutathione offers neuroprotection against MeHg toxicity in a manner dependent on MRP1-mediated efflux. Glutathione 35-46 ATP binding cassette subfamily B member 1 Homo sapiens 117-121 22197475-6 2012 The ATP-binding cassette (ABC) transporter proteins, multidrug resistance protein 1 (MRP1/ABCC1) and the related protein MRP2 (ABCC2), are thought to play an important role in arsenic detoxification through the cellular efflux of arsenic-GSH conjugates. Glutathione 238-241 ATP binding cassette subfamily B member 1 Homo sapiens 53-83 22017299-6 2012 The stimulation of the GSH export from viable astrocytes by indinavir or nelfinavir was completely prevented by the application of MK571, an inhibitor of the multidrug resistance protein 1. Glutathione 23-26 ATP binding cassette subfamily B member 1 Homo sapiens 158-188 22017299-7 2012 These data demonstrate that indinavir and nelfinavir stimulate multidrug resistance protein 1-mediated GSH export from viable astrocytes and suggest that treatment of patients with such inhibitors may affect the GSH homeostasis in brain. Glutathione 103-106 ATP binding cassette subfamily B member 1 Homo sapiens 63-93 22017299-7 2012 These data demonstrate that indinavir and nelfinavir stimulate multidrug resistance protein 1-mediated GSH export from viable astrocytes and suggest that treatment of patients with such inhibitors may affect the GSH homeostasis in brain. Glutathione 212-215 ATP binding cassette subfamily B member 1 Homo sapiens 63-93 21925487-0 2011 Enhanced glutathione depletion, protein adduct formation, and cytotoxicity following exposure to 4-hydroxy-2-nonenal (HNE) in cells expressing human multidrug resistance protein-1 (MRP1) together with human glutathione S-transferase-M1 (GSTM1). Glutathione 9-20 ATP binding cassette subfamily B member 1 Homo sapiens 181-185 21925487-10 2011 However, HNE induced >80% depletion of GSH in cells expressing MRP1 alone. Glutathione 42-45 ATP binding cassette subfamily B member 1 Homo sapiens 66-70 21925487-11 2011 Co-expression of both MRP1 and GSTM1 caused slightly greater GSH depletion, consistent with the greater protein adduct formation and cytotoxicity in this cell line. Glutathione 61-64 ATP binding cassette subfamily B member 1 Homo sapiens 22-26 21925487-12 2011 Since expression of GSTM1 or MRP1 alone did not strongly sensitize cells to HNE, or result in greater HNE-protein adducts than in the control cell line, these results indicate that MRP1 and GSTM1 collaborate to enhance HNE-protein adduct formation and HNE cytotoxicity, facilitated by GSH depletion mediated by both MRP1 and GSTM1. Glutathione 285-288 ATP binding cassette subfamily B member 1 Homo sapiens 181-185 21925487-12 2011 Since expression of GSTM1 or MRP1 alone did not strongly sensitize cells to HNE, or result in greater HNE-protein adducts than in the control cell line, these results indicate that MRP1 and GSTM1 collaborate to enhance HNE-protein adduct formation and HNE cytotoxicity, facilitated by GSH depletion mediated by both MRP1 and GSTM1. Glutathione 285-288 ATP binding cassette subfamily B member 1 Homo sapiens 181-185 21634011-2 2011 MRP1 mediates MDR (multidrug resistance) by causing drug efflux either by conjugation to glutathione (GSH) or by co-transport with free GSH (without covalent bonding between the drug and GSH). Glutathione 89-100 ATP binding cassette subfamily B member 1 Homo sapiens 0-4 21634011-2 2011 MRP1 mediates MDR (multidrug resistance) by causing drug efflux either by conjugation to glutathione (GSH) or by co-transport with free GSH (without covalent bonding between the drug and GSH). Glutathione 102-105 ATP binding cassette subfamily B member 1 Homo sapiens 0-4 21634011-2 2011 MRP1 mediates MDR (multidrug resistance) by causing drug efflux either by conjugation to glutathione (GSH) or by co-transport with free GSH (without covalent bonding between the drug and GSH). Glutathione 136-139 ATP binding cassette subfamily B member 1 Homo sapiens 0-4 21634011-2 2011 MRP1 mediates MDR (multidrug resistance) by causing drug efflux either by conjugation to glutathione (GSH) or by co-transport with free GSH (without covalent bonding between the drug and GSH). Glutathione 136-139 ATP binding cassette subfamily B member 1 Homo sapiens 0-4 21634011-3 2011 We recently reported that the calcium channel blocker verapamil can activate massive GSH efflux in MRP1-overexpressing cells, leading to cell death through apoptosis. Glutathione 85-88 ATP binding cassette subfamily B member 1 Homo sapiens 99-103 20487633-1 2010 Multidrug resistance (MDR) in cancer cells is often caused by the high expression of the plasma membrane drug transporter P-glycoprotein (Pgp) associated with an elevated intracellular glutathione (GSH) content in various human tumors. Glutathione 185-196 ATP binding cassette subfamily B member 1 Homo sapiens 122-136 20487633-1 2010 Multidrug resistance (MDR) in cancer cells is often caused by the high expression of the plasma membrane drug transporter P-glycoprotein (Pgp) associated with an elevated intracellular glutathione (GSH) content in various human tumors. Glutathione 185-196 ATP binding cassette subfamily B member 1 Homo sapiens 138-141 20487633-1 2010 Multidrug resistance (MDR) in cancer cells is often caused by the high expression of the plasma membrane drug transporter P-glycoprotein (Pgp) associated with an elevated intracellular glutathione (GSH) content in various human tumors. Glutathione 198-201 ATP binding cassette subfamily B member 1 Homo sapiens 122-136 20487633-1 2010 Multidrug resistance (MDR) in cancer cells is often caused by the high expression of the plasma membrane drug transporter P-glycoprotein (Pgp) associated with an elevated intracellular glutathione (GSH) content in various human tumors. Glutathione 198-201 ATP binding cassette subfamily B member 1 Homo sapiens 138-141 24382184-1 2013 Multidrug resistance (MDR) in cancer cells is often caused by the high expression of the plasma membrane drug transporter P-glycoprotein (Pgp) associated with an elevated intracellular glutathione (GSH) content in various human tumors. Glutathione 185-196 ATP binding cassette subfamily B member 1 Homo sapiens 122-136 24382184-1 2013 Multidrug resistance (MDR) in cancer cells is often caused by the high expression of the plasma membrane drug transporter P-glycoprotein (Pgp) associated with an elevated intracellular glutathione (GSH) content in various human tumors. Glutathione 185-196 ATP binding cassette subfamily B member 1 Homo sapiens 138-141 24382184-1 2013 Multidrug resistance (MDR) in cancer cells is often caused by the high expression of the plasma membrane drug transporter P-glycoprotein (Pgp) associated with an elevated intracellular glutathione (GSH) content in various human tumors. Glutathione 198-201 ATP binding cassette subfamily B member 1 Homo sapiens 122-136 24382184-1 2013 Multidrug resistance (MDR) in cancer cells is often caused by the high expression of the plasma membrane drug transporter P-glycoprotein (Pgp) associated with an elevated intracellular glutathione (GSH) content in various human tumors. Glutathione 198-201 ATP binding cassette subfamily B member 1 Homo sapiens 138-141 24013781-2 2013 In contrast to MDR1, MRP1 also transports glutathione (GSH) and drugs conjugated to GSH. Glutathione 84-87 ATP binding cassette subfamily B member 1 Homo sapiens 15-19 23542460-6 2013 The arsenate-induced stimulated GSH export from astrocytes was prevented by MK571, an inhibitor of the multidrug resistance protein 1. Glutathione 32-35 ATP binding cassette subfamily B member 1 Homo sapiens 103-133 21166805-7 2011 The Fal-stimulated GSH loss from viable astrocytes was completely prevented by semicarbazide-mediated chemical removal of Fal or by the application of MK571, an inhibitor of the multidrug resistance protein 1. Glutathione 19-22 ATP binding cassette subfamily B member 1 Homo sapiens 178-208 21166805-8 2011 These data demonstrate that Fal deprives astrocytes of cellular GSH by a multidrug resistance protein 1-mediated process. Glutathione 64-67 ATP binding cassette subfamily B member 1 Homo sapiens 73-103 20691599-0 2010 Iodination of verapamil for a stronger induction of death, through GSH efflux, of cancer cells overexpressing MRP1. Glutathione 67-70 ATP binding cassette subfamily B member 1 Homo sapiens 110-114 20691599-1 2010 The multidrug resistance protein 1 (MRP1), involved in multidrug resistance (MDR) of cancer cells, was found to be modulated by verapamil, through stimulation of GSH transport, leading to apoptosis of MRP1-overexpressing cells. Glutathione 162-165 ATP binding cassette subfamily B member 1 Homo sapiens 4-34 20691599-1 2010 The multidrug resistance protein 1 (MRP1), involved in multidrug resistance (MDR) of cancer cells, was found to be modulated by verapamil, through stimulation of GSH transport, leading to apoptosis of MRP1-overexpressing cells. Glutathione 162-165 ATP binding cassette subfamily B member 1 Homo sapiens 36-40 20691599-1 2010 The multidrug resistance protein 1 (MRP1), involved in multidrug resistance (MDR) of cancer cells, was found to be modulated by verapamil, through stimulation of GSH transport, leading to apoptosis of MRP1-overexpressing cells. Glutathione 162-165 ATP binding cassette subfamily B member 1 Homo sapiens 201-205 20691599-2 2010 In this study, various iodinated derivatives of verapamil were synthesized, including iodination on the B ring, known to be involved in verapamil cardiotoxicity, and assayed for the stimulation of GSH efflux by MRP1. Glutathione 197-200 ATP binding cassette subfamily B member 1 Homo sapiens 211-215 19398503-2 2009 MRP1 also transports glutathione (GSH); furthermore, this tripeptide stimulates transport of several substrates, including estrone 3-sulfate. Glutathione 34-37 ATP binding cassette subfamily B member 1 Homo sapiens 0-4 19398503-6 2009 In contrast, TM6-Lys(332) is important for enabling GSH and GSH-containing compounds to serve as substrates (e.g., leukotriene C(4)) or modulators (e.g., S-decyl-GSH, GSH disulfide) of MRP1 and, further, for enabling GSH (or S-methyl-GSH) to enhance the transport of estrone 3-sulfate and increase the inhibitory potency of LY465803. Glutathione 52-55 ATP binding cassette subfamily B member 1 Homo sapiens 185-189 19398503-6 2009 In contrast, TM6-Lys(332) is important for enabling GSH and GSH-containing compounds to serve as substrates (e.g., leukotriene C(4)) or modulators (e.g., S-decyl-GSH, GSH disulfide) of MRP1 and, further, for enabling GSH (or S-methyl-GSH) to enhance the transport of estrone 3-sulfate and increase the inhibitory potency of LY465803. Glutathione 60-63 ATP binding cassette subfamily B member 1 Homo sapiens 185-189 19398503-6 2009 In contrast, TM6-Lys(332) is important for enabling GSH and GSH-containing compounds to serve as substrates (e.g., leukotriene C(4)) or modulators (e.g., S-decyl-GSH, GSH disulfide) of MRP1 and, further, for enabling GSH (or S-methyl-GSH) to enhance the transport of estrone 3-sulfate and increase the inhibitory potency of LY465803. Glutathione 60-63 ATP binding cassette subfamily B member 1 Homo sapiens 185-189 18768387-0 2008 Mechanistic differences between GSH transport by multidrug resistance protein 1 (MRP1/ABCC1) and GSH modulation of MRP1-mediated transport. Glutathione 32-35 ATP binding cassette subfamily B member 1 Homo sapiens 49-79 19409044-11 2009 Outward transport of radiotracers by MRP1 was dependent on the intracellular glutathione levels. Glutathione 77-88 ATP binding cassette subfamily B member 1 Homo sapiens 37-41 18556457-3 2008 Glutathione (GSH) has been reported to play a role in cadmium resistance by serving as a cofactor for multidrug resistance protein 1/GS-X pump-mediated cadmium elimination. Glutathione 0-11 ATP binding cassette subfamily B member 1 Homo sapiens 102-132 18556457-3 2008 Glutathione (GSH) has been reported to play a role in cadmium resistance by serving as a cofactor for multidrug resistance protein 1/GS-X pump-mediated cadmium elimination. Glutathione 13-16 ATP binding cassette subfamily B member 1 Homo sapiens 102-132 16861249-6 2006 GSH-dependent photolabeling of MRP1 with an 125I-labeled photoaffinity analog of azido agosterol A (azido AG-A) was abolished by the mutations in ICL5 and ICL7. Glutathione 0-3 ATP binding cassette subfamily B member 1 Homo sapiens 31-35 18059532-9 2007 Taken together, our findings suggest that downregulating CIAPIN1 could sensitize leukemia cells to chemotherapeutic drugs by downregulating MDR-1 and Bcl-2 and by upregulating Bax, yet not altering either glutathione-S-transferase activity or intracellular glutathione content in leukemia cells. Glutathione 205-216 ATP binding cassette subfamily B member 1 Homo sapiens 140-145 17187268-2 2007 This protein has an unusually broad substrate specificity and is capable of transporting not only a wide variety of neutral hydrophobic compounds, like the MDR1/P-glycoprotein, but also facilitating the extrusion of numerous glutathione, glucuronate, and sulfate conjugates. Glutathione 225-236 ATP binding cassette subfamily B member 1 Homo sapiens 156-160 17187268-2 2007 This protein has an unusually broad substrate specificity and is capable of transporting not only a wide variety of neutral hydrophobic compounds, like the MDR1/P-glycoprotein, but also facilitating the extrusion of numerous glutathione, glucuronate, and sulfate conjugates. Glutathione 225-236 ATP binding cassette subfamily B member 1 Homo sapiens 161-175 16105987-3 2005 The intrinsically photoreactive glutathione-conjugated cysteinyl leukotriene C4 (LTC4) is a high-affinity physiological substrate of MRP1 and is widely regarded as a model compound for evaluating the substrate binding and transport properties of wild-type and mutant forms of the transporter. Glutathione 32-43 ATP binding cassette subfamily B member 1 Homo sapiens 133-137 16769721-0 2006 A strong glutathione S-transferase inhibitor overcomes the P-glycoprotein-mediated resistance in tumor cells. Glutathione 9-20 ATP binding cassette subfamily B member 1 Homo sapiens 59-73 16769721-2 2006 The new glutathione S-transferase inhibitor 6-(7-nitro-2,1,3-benzoxadiazol-4-ylthio)hexanol (NBDHEX) is cytotoxic toward P-glycoprotein-overexpressing tumor cell lines, i.e. CEM-VBL10, CEM-VBL100, and U-2 OS/DX580. Glutathione 8-19 ATP binding cassette subfamily B member 1 Homo sapiens 121-135 16820223-0 2006 Transport of glutathione and glutathione conjugates by MRP1. Glutathione 13-24 ATP binding cassette subfamily B member 1 Homo sapiens 55-59 16820223-0 2006 Transport of glutathione and glutathione conjugates by MRP1. Glutathione 29-40 ATP binding cassette subfamily B member 1 Homo sapiens 55-59 16820223-3 2006 In addition to drugs and GSH conjugates, MRP1 exports GSH and GSH disulfide, and might thus have a role in cellular responses to oxidative stress. Glutathione 54-57 ATP binding cassette subfamily B member 1 Homo sapiens 41-45 16820223-4 2006 The transport of several drugs and conjugated organic anions by MRP1 requires the presence of GSH, but it is not well understood how GSH (and its analogues) enhances transport. Glutathione 94-97 ATP binding cassette subfamily B member 1 Homo sapiens 64-68 16820223-5 2006 Site-directed mutagenesis studies and biophysical analyses have provided important insights into the structural determinants of MRP1 that influence GSH and GSH conjugate binding and transport. Glutathione 148-151 ATP binding cassette subfamily B member 1 Homo sapiens 128-132 16820223-5 2006 Site-directed mutagenesis studies and biophysical analyses have provided important insights into the structural determinants of MRP1 that influence GSH and GSH conjugate binding and transport. Glutathione 156-159 ATP binding cassette subfamily B member 1 Homo sapiens 128-132 16784241-0 2006 Modulation of nitrated lipid signaling by multidrug resistance protein 1 (MRP1): glutathione conjugation and MRP1-mediated efflux inhibit nitrolinoleic acid-induced, PPARgamma-dependent transcription activation. Glutathione 81-92 ATP binding cassette subfamily B member 1 Homo sapiens 42-72 16784241-0 2006 Modulation of nitrated lipid signaling by multidrug resistance protein 1 (MRP1): glutathione conjugation and MRP1-mediated efflux inhibit nitrolinoleic acid-induced, PPARgamma-dependent transcription activation. Glutathione 81-92 ATP binding cassette subfamily B member 1 Homo sapiens 74-78 16415113-6 2006 Although mutation of Asn(1208) was without effect, two of six mutations in TM10, T550A and T556A, modulated the drug resistance profile of MRP1 without affecting transport of leukotriene C4, 17beta-estradiol 17-(beta-d-glucuronide) (E(2)17betaG), and glutathione. Glutathione 251-262 ATP binding cassette subfamily B member 1 Homo sapiens 139-143 16565074-0 2006 Role of GSH in estrone sulfate binding and translocation by the multidrug resistance protein 1 (MRP1/ABCC1). Glutathione 8-11 ATP binding cassette subfamily B member 1 Homo sapiens 64-94 16434618-0 2006 Multidrug resistance protein 1 (MRP1, ABCC1) mediates resistance to mitoxantrone via glutathione-dependent drug efflux. Glutathione 85-96 ATP binding cassette subfamily B member 1 Homo sapiens 0-30 16434618-0 2006 Multidrug resistance protein 1 (MRP1, ABCC1) mediates resistance to mitoxantrone via glutathione-dependent drug efflux. Glutathione 85-96 ATP binding cassette subfamily B member 1 Homo sapiens 32-36 16434618-5 2006 Unlike ABCG2 (breast cancer resistance protein, mitoxantrone-resistant protein), MRP1-mediated MX transport is dependent upon the presence of glutathione or its S-methyl analog. Glutathione 142-153 ATP binding cassette subfamily B member 1 Homo sapiens 81-85 16434618-7 2006 Together, these data are consistent with the interpretation that MX efflux by MRP1 involves cotransport of MX and glutathione. Glutathione 114-125 ATP binding cassette subfamily B member 1 Homo sapiens 78-82 16399362-0 2005 Multidrug resistance protein 1-mediated export of glutathione and glutathione disulfide from brain astrocytes. Glutathione 50-61 ATP binding cassette subfamily B member 1 Homo sapiens 0-30 16098482-2 2005 Much convincing evidence has accumulated that MRP1 transports most substances in a GSH-dependent manner. Glutathione 83-86 ATP binding cassette subfamily B member 1 Homo sapiens 46-50 16098482-3 2005 On the other hand, several reports have revealed that MRP1 can transport some substrates independently of GSH; however, the importance of GSH-independent transport activity is not well established and the mechanistic differences between GSH-dependent and -independent transport by MRP1 are unclear. Glutathione 106-109 ATP binding cassette subfamily B member 1 Homo sapiens 54-58 16098482-3 2005 On the other hand, several reports have revealed that MRP1 can transport some substrates independently of GSH; however, the importance of GSH-independent transport activity is not well established and the mechanistic differences between GSH-dependent and -independent transport by MRP1 are unclear. Glutathione 138-141 ATP binding cassette subfamily B member 1 Homo sapiens 54-58 16098482-3 2005 On the other hand, several reports have revealed that MRP1 can transport some substrates independently of GSH; however, the importance of GSH-independent transport activity is not well established and the mechanistic differences between GSH-dependent and -independent transport by MRP1 are unclear. Glutathione 138-141 ATP binding cassette subfamily B member 1 Homo sapiens 54-58 16098482-4 2005 We previously demonstrated that the amino acids W261 and K267 in the L0 region of MRP1 were important for leukotriene C4 (LTC4) transport activity of MRP1 and for GSH-dependent photolabeling of MRP1 with azidophenyl agosterol-A (azidoAG-A). Glutathione 163-166 ATP binding cassette subfamily B member 1 Homo sapiens 82-86 16098482-9 2005 Understanding the GSH-independent transport mechanism of MRP1, and identification of drugs that are transported by this mechanism, will be critical for combating MRP1-mediated drug resistance. Glutathione 18-21 ATP binding cassette subfamily B member 1 Homo sapiens 57-61 16098482-9 2005 Understanding the GSH-independent transport mechanism of MRP1, and identification of drugs that are transported by this mechanism, will be critical for combating MRP1-mediated drug resistance. Glutathione 18-21 ATP binding cassette subfamily B member 1 Homo sapiens 162-166 16098482-10 2005 We performed a pairwise comparison of compounds that are transported by MRP1 in a GSH-dependent or -independent manner. Glutathione 82-85 ATP binding cassette subfamily B member 1 Homo sapiens 72-76 16098482-11 2005 These data indicated that it may be possible to predict compounds that are transported by MRP1 in a GSH-independent manner. Glutathione 100-103 ATP binding cassette subfamily B member 1 Homo sapiens 90-94 15617835-2 2005 MRP1 functions as an efflux pump of drugs, primarily those conjugated to glutathione (GSH). Glutathione 73-84 ATP binding cassette subfamily B member 1 Homo sapiens 0-4 15617835-2 2005 MRP1 functions as an efflux pump of drugs, primarily those conjugated to glutathione (GSH). Glutathione 86-89 ATP binding cassette subfamily B member 1 Homo sapiens 0-4 15617835-3 2005 Decreases in the intracellular concentration of GSH have been shown to enhance the response of MRP1-overexpressing cells to MRP1-substrate drugs by limiting the available drug-GSH conjugates. Glutathione 48-51 ATP binding cassette subfamily B member 1 Homo sapiens 95-99 15617835-3 2005 Decreases in the intracellular concentration of GSH have been shown to enhance the response of MRP1-overexpressing cells to MRP1-substrate drugs by limiting the available drug-GSH conjugates. Glutathione 48-51 ATP binding cassette subfamily B member 1 Homo sapiens 124-128 15617835-3 2005 Decreases in the intracellular concentration of GSH have been shown to enhance the response of MRP1-overexpressing cells to MRP1-substrate drugs by limiting the available drug-GSH conjugates. Glutathione 176-179 ATP binding cassette subfamily B member 1 Homo sapiens 95-99 15617835-3 2005 Decreases in the intracellular concentration of GSH have been shown to enhance the response of MRP1-overexpressing cells to MRP1-substrate drugs by limiting the available drug-GSH conjugates. Glutathione 176-179 ATP binding cassette subfamily B member 1 Homo sapiens 124-128 16041243-1 2005 The 190-kDa ATP-binding cassette (ABC) multidrug resistance protein 1 (MRP1) encoded by the MRP1/ABCC1 gene mediates the active cellular efflux of glucuronide, glutathione and sulfate conjugates. Glutathione 160-171 ATP binding cassette subfamily B member 1 Homo sapiens 39-69 16041243-1 2005 The 190-kDa ATP-binding cassette (ABC) multidrug resistance protein 1 (MRP1) encoded by the MRP1/ABCC1 gene mediates the active cellular efflux of glucuronide, glutathione and sulfate conjugates. Glutathione 160-171 ATP binding cassette subfamily B member 1 Homo sapiens 71-75 16041243-1 2005 The 190-kDa ATP-binding cassette (ABC) multidrug resistance protein 1 (MRP1) encoded by the MRP1/ABCC1 gene mediates the active cellular efflux of glucuronide, glutathione and sulfate conjugates. Glutathione 160-171 ATP binding cassette subfamily B member 1 Homo sapiens 92-96 12716947-6 2003 Microarray and biochemical analyses indicate a coordinated upregulation of enzymes involved in GSH biosynthesis (xCT cystine antiporter, gamma-glutamylcysteine synthetase, and GSH synthase), use (glutathione S-transferase and glutathione reductase), and export (multidrug resistance protein 1) with Nrf2 overexpression, leading to an increase in both media and intracellular GSH. Glutathione 95-98 ATP binding cassette subfamily B member 1 Homo sapiens 262-292 14629827-1 2003 The main causes of multidrug resistance (MDR) are overexpression of P-glycoprotein (P-gp) and multidrug resistance-associated protein isoform 1 (MRP1) often associated with high levels of glutathione (GSH). Glutathione 188-199 ATP binding cassette subfamily B member 1 Homo sapiens 68-82 14629827-1 2003 The main causes of multidrug resistance (MDR) are overexpression of P-glycoprotein (P-gp) and multidrug resistance-associated protein isoform 1 (MRP1) often associated with high levels of glutathione (GSH). Glutathione 188-199 ATP binding cassette subfamily B member 1 Homo sapiens 84-88 14629827-1 2003 The main causes of multidrug resistance (MDR) are overexpression of P-glycoprotein (P-gp) and multidrug resistance-associated protein isoform 1 (MRP1) often associated with high levels of glutathione (GSH). Glutathione 201-204 ATP binding cassette subfamily B member 1 Homo sapiens 68-82 14629827-1 2003 The main causes of multidrug resistance (MDR) are overexpression of P-glycoprotein (P-gp) and multidrug resistance-associated protein isoform 1 (MRP1) often associated with high levels of glutathione (GSH). Glutathione 201-204 ATP binding cassette subfamily B member 1 Homo sapiens 84-88 12721111-0 2003 Localization of the GSH-dependent photolabelling site of an agosterol A analog on human MRP1. Glutathione 20-23 ATP binding cassette subfamily B member 1 Homo sapiens 88-92 12721111-3 2003 We recently demonstrated that glutathione (GSH) is required for the labelling of the C-terminal half of MRP1 with a photoanalog of agosterol A (azido AG-A). Glutathione 30-41 ATP binding cassette subfamily B member 1 Homo sapiens 104-108 12721111-3 2003 We recently demonstrated that glutathione (GSH) is required for the labelling of the C-terminal half of MRP1 with a photoanalog of agosterol A (azido AG-A). Glutathione 43-46 ATP binding cassette subfamily B member 1 Homo sapiens 104-108 12721111-14 2003 In summary, this study demonstrated that the GSH-dependent azido AG-A photolabelling site on MRP1 resides in the region within TM14-17 and the cytoplasmic region proximate to the C-terminus of TM17. Glutathione 45-48 ATP binding cassette subfamily B member 1 Homo sapiens 93-97 12721111-15 2003 The charged amino acid Arg(1202) proximate to TM helix 16 is of critical importance for the GSH-dependent photolabelling of MRP1 with azido AG-A. Glutathione 92-95 ATP binding cassette subfamily B member 1 Homo sapiens 124-128 12721111-4 2003 In this study, we further characterized the GSH-dependent photolabelling site of azido AG-A on MRP1. Glutathione 44-47 ATP binding cassette subfamily B member 1 Homo sapiens 95-99 12721111-6 2003 An epitope-inserted MRP1, MRP1 1222HA, which has two hemagglutinin A (HA) epitopes in the extracellular loop between transmembrane segment (TM) 16 and TM17 of the transporter, could bind azido AG-A in a GSH-dependent manner. Glutathione 203-206 ATP binding cassette subfamily B member 1 Homo sapiens 20-24 12721111-6 2003 An epitope-inserted MRP1, MRP1 1222HA, which has two hemagglutinin A (HA) epitopes in the extracellular loop between transmembrane segment (TM) 16 and TM17 of the transporter, could bind azido AG-A in a GSH-dependent manner. Glutathione 203-206 ATP binding cassette subfamily B member 1 Homo sapiens 26-30 12721111-8 2003 Protease digestion of the photolabelled MRP1 1222HA, followed by immunoprecipitation with an anti-HA antibody suggested that the GSH-dependent azido AG-A photolabelling site on MRP1 resides in the region within TM14-17 and the cytoplasmic region proximate to the C-terminus of TM17. Glutathione 129-132 ATP binding cassette subfamily B member 1 Homo sapiens 40-44 12721111-8 2003 Protease digestion of the photolabelled MRP1 1222HA, followed by immunoprecipitation with an anti-HA antibody suggested that the GSH-dependent azido AG-A photolabelling site on MRP1 resides in the region within TM14-17 and the cytoplasmic region proximate to the C-terminus of TM17. Glutathione 129-132 ATP binding cassette subfamily B member 1 Homo sapiens 177-181 12485947-0 2003 Bioflavonoid stimulation of glutathione transport by the 190-kDa multidrug resistance protein 1 (MRP1). Glutathione 28-39 ATP binding cassette subfamily B member 1 Homo sapiens 65-95 12623128-2 2003 A clear distinction in the mechanism of translocation of substrates by MRP1 or P-gp is indicated by the finding that, in most of cases, the MRP1-mediated transport of substrates is inhibited by depletion of intracellular glutathione (GSH), which has no effect on their P-gp-mediated transport. Glutathione 221-232 ATP binding cassette subfamily B member 1 Homo sapiens 79-83 12623128-2 2003 A clear distinction in the mechanism of translocation of substrates by MRP1 or P-gp is indicated by the finding that, in most of cases, the MRP1-mediated transport of substrates is inhibited by depletion of intracellular glutathione (GSH), which has no effect on their P-gp-mediated transport. Glutathione 221-232 ATP binding cassette subfamily B member 1 Homo sapiens 269-273 12623128-2 2003 A clear distinction in the mechanism of translocation of substrates by MRP1 or P-gp is indicated by the finding that, in most of cases, the MRP1-mediated transport of substrates is inhibited by depletion of intracellular glutathione (GSH), which has no effect on their P-gp-mediated transport. Glutathione 234-237 ATP binding cassette subfamily B member 1 Homo sapiens 79-83 12623128-2 2003 A clear distinction in the mechanism of translocation of substrates by MRP1 or P-gp is indicated by the finding that, in most of cases, the MRP1-mediated transport of substrates is inhibited by depletion of intracellular glutathione (GSH), which has no effect on their P-gp-mediated transport. Glutathione 234-237 ATP binding cassette subfamily B member 1 Homo sapiens 269-273 12538817-0 2003 Structural requirements for functional interaction of glutathione tripeptide analogs with the human multidrug resistance protein 1 (MRP1). Glutathione 54-65 ATP binding cassette subfamily B member 1 Homo sapiens 100-130 12538817-0 2003 Structural requirements for functional interaction of glutathione tripeptide analogs with the human multidrug resistance protein 1 (MRP1). Glutathione 54-65 ATP binding cassette subfamily B member 1 Homo sapiens 132-136 12538817-1 2003 The human multidrug resistance protein 1 (MRP1) is a primary active transporter of reduced (GSH) and oxidized glutathione, as well as GSH-, glucuronate-, and sulfate-conjugated organic anions. Glutathione 92-95 ATP binding cassette subfamily B member 1 Homo sapiens 10-40 12538817-1 2003 The human multidrug resistance protein 1 (MRP1) is a primary active transporter of reduced (GSH) and oxidized glutathione, as well as GSH-, glucuronate-, and sulfate-conjugated organic anions. Glutathione 92-95 ATP binding cassette subfamily B member 1 Homo sapiens 42-46 12538817-1 2003 The human multidrug resistance protein 1 (MRP1) is a primary active transporter of reduced (GSH) and oxidized glutathione, as well as GSH-, glucuronate-, and sulfate-conjugated organic anions. Glutathione 110-121 ATP binding cassette subfamily B member 1 Homo sapiens 10-40 12538817-1 2003 The human multidrug resistance protein 1 (MRP1) is a primary active transporter of reduced (GSH) and oxidized glutathione, as well as GSH-, glucuronate-, and sulfate-conjugated organic anions. Glutathione 110-121 ATP binding cassette subfamily B member 1 Homo sapiens 42-46 12538817-1 2003 The human multidrug resistance protein 1 (MRP1) is a primary active transporter of reduced (GSH) and oxidized glutathione, as well as GSH-, glucuronate-, and sulfate-conjugated organic anions. Glutathione 134-137 ATP binding cassette subfamily B member 1 Homo sapiens 10-40 12538817-1 2003 The human multidrug resistance protein 1 (MRP1) is a primary active transporter of reduced (GSH) and oxidized glutathione, as well as GSH-, glucuronate-, and sulfate-conjugated organic anions. Glutathione 134-137 ATP binding cassette subfamily B member 1 Homo sapiens 42-46 12538817-2 2003 In addition, the transport of certain MRP1 substrates is stimulated by the presence of GSH. Glutathione 87-90 ATP binding cassette subfamily B member 1 Homo sapiens 38-42 12538817-10 2003 These data provide insight into the architecture of the GSH binding domain of MRP1. Glutathione 56-59 ATP binding cassette subfamily B member 1 Homo sapiens 78-82 12485947-10 2003 Our results suggest that flavonoids stimulate MRP1-mediated GSH transport by increasing the apparent affinity of the transporter for GSH but provide no evidence that a cotransport mechanism is involved. Glutathione 60-63 ATP binding cassette subfamily B member 1 Homo sapiens 46-50 12485947-10 2003 Our results suggest that flavonoids stimulate MRP1-mediated GSH transport by increasing the apparent affinity of the transporter for GSH but provide no evidence that a cotransport mechanism is involved. Glutathione 133-136 ATP binding cassette subfamily B member 1 Homo sapiens 46-50 12424247-7 2003 Our results show that during GSH-dependent drug transport, MRP1 does not undergo secondary structure changes but only modifications in its accessibility toward the external environment. Glutathione 29-32 ATP binding cassette subfamily B member 1 Homo sapiens 59-63 12485947-0 2003 Bioflavonoid stimulation of glutathione transport by the 190-kDa multidrug resistance protein 1 (MRP1). Glutathione 28-39 ATP binding cassette subfamily B member 1 Homo sapiens 97-101 12485947-3 2003 Reduced glutathione (GSH) is transported by MRP1 with very low affinity, and certain MRP1 substrates are transported in association with this tripeptide. Glutathione 8-19 ATP binding cassette subfamily B member 1 Homo sapiens 44-48 12485947-3 2003 Reduced glutathione (GSH) is transported by MRP1 with very low affinity, and certain MRP1 substrates are transported in association with this tripeptide. Glutathione 8-19 ATP binding cassette subfamily B member 1 Homo sapiens 85-89 12485947-3 2003 Reduced glutathione (GSH) is transported by MRP1 with very low affinity, and certain MRP1 substrates are transported in association with this tripeptide. Glutathione 21-24 ATP binding cassette subfamily B member 1 Homo sapiens 44-48 12485947-5 2003 In contrast, many of the same flavonoids markedly stimulate GSH transport by MRP1. Glutathione 60-63 ATP binding cassette subfamily B member 1 Homo sapiens 77-81 12485947-6 2003 In the present study, we found that stimulation of GSH transport in inside-out MRP1-enriched membrane vesicles by apigenin, naringenin, genistein, and quercetin was maximum at a concentration of 30 microM. Glutathione 51-54 ATP binding cassette subfamily B member 1 Homo sapiens 79-83 14552590-6 2003 The binding of [125I]azidoAG-A to P-gp differs from the binding of other photolabeled probes such as iodoaryl-azidoprazosin (IAAP) to P-gp and from the binding of [125I]azidoAG-A to MRP1 based on the differing effects of flupentixol and glutathione (GSH) on their binding. Glutathione 237-248 ATP binding cassette subfamily B member 1 Homo sapiens 34-38 14552590-6 2003 The binding of [125I]azidoAG-A to P-gp differs from the binding of other photolabeled probes such as iodoaryl-azidoprazosin (IAAP) to P-gp and from the binding of [125I]azidoAG-A to MRP1 based on the differing effects of flupentixol and glutathione (GSH) on their binding. Glutathione 250-253 ATP binding cassette subfamily B member 1 Homo sapiens 34-38 12034727-0 2002 GSH-dependent photolabeling of multidrug resistance protein MRP1 (ABCC1) by [125I]LY475776. Glutathione 0-3 ATP binding cassette subfamily B member 1 Homo sapiens 60-64 12387749-10 2002 Our results indicate that this tolerance in human cells involves increases in GSH levels and GST activity that allow for more efficient arsenic efflux by MRP1 and MDR1. Glutathione 78-81 ATP binding cassette subfamily B member 1 Homo sapiens 163-167 12034727-3 2002 In addition, MRP1 confers resistance against various anticancer drugs by reducing intracellular accumulation by co-export of drug with reduced GSH. Glutathione 143-146 ATP binding cassette subfamily B member 1 Homo sapiens 13-17 12034727-5 2002 We show that [125I]LY475776 photolabeling of MRP1 requires GSH but is also supported by several non-reducing GSH derivatives and peptide analogs. Glutathione 59-62 ATP binding cassette subfamily B member 1 Homo sapiens 45-49 12034727-5 2002 We show that [125I]LY475776 photolabeling of MRP1 requires GSH but is also supported by several non-reducing GSH derivatives and peptide analogs. Glutathione 109-112 ATP binding cassette subfamily B member 1 Homo sapiens 45-49 11898391-4 2002 Besides LTC4, which is a high-affinity substrate, a variety of conjugates of hydrophobic endogenous or xenobiotic substances with glutathione, glucuronate, or sulfate are transported by MRP1. Glutathione 130-141 ATP binding cassette subfamily B member 1 Homo sapiens 186-190 11306701-1 2001 The 190-kDa phosphoglycoprotein multidrug resistance protein 1 (MRP1) (ABCC1) confers resistance to a broad spectrum of anticancer drugs and also actively transports certain xenobiotics with reduced glutathione (GSH) (cotransport) as well as conjugated organic anions such as leukotriene C(4) (LTC(4)). Glutathione 199-210 ATP binding cassette subfamily B member 1 Homo sapiens 32-62 11279018-3 2001 Maximum Pgp expression occurred in tumor spheroids with a high percentage of quiescent, Ki-67-negative cells, elevated glutathione levels, increased expression of the cyclin-dependent kinase inhibitors p27Kip1 and p21WAF-1 as well as reduced ROS levels and minor activity of the mitogen-activated kinase (MAPK) members c-Jun amino-terminal kinase (JNK), extracellular signal-regulated kinase ERK1,2, and p38 MAPK. Glutathione 119-130 ATP binding cassette subfamily B member 1 Homo sapiens 8-11 11279018-4 2001 Raising intracellular ROS by depletion of glutathione with buthionine sulfoximine (BSO) or glutamine starvation resulted in down-regulation of Pgp and p27Kip1, whereas ERK1,2 and JNK were activated. Glutathione 42-53 ATP binding cassette subfamily B member 1 Homo sapiens 143-146 11306701-11 2001 We conclude that dietary flavonoids may modulate the organic anion and GSH transport, ATPase, and/or drug resistance-conferring properties of MRP1. Glutathione 71-74 ATP binding cassette subfamily B member 1 Homo sapiens 142-146 11306701-1 2001 The 190-kDa phosphoglycoprotein multidrug resistance protein 1 (MRP1) (ABCC1) confers resistance to a broad spectrum of anticancer drugs and also actively transports certain xenobiotics with reduced glutathione (GSH) (cotransport) as well as conjugated organic anions such as leukotriene C(4) (LTC(4)). Glutathione 199-210 ATP binding cassette subfamily B member 1 Homo sapiens 64-68 11306701-1 2001 The 190-kDa phosphoglycoprotein multidrug resistance protein 1 (MRP1) (ABCC1) confers resistance to a broad spectrum of anticancer drugs and also actively transports certain xenobiotics with reduced glutathione (GSH) (cotransport) as well as conjugated organic anions such as leukotriene C(4) (LTC(4)). Glutathione 212-215 ATP binding cassette subfamily B member 1 Homo sapiens 32-62 11306701-1 2001 The 190-kDa phosphoglycoprotein multidrug resistance protein 1 (MRP1) (ABCC1) confers resistance to a broad spectrum of anticancer drugs and also actively transports certain xenobiotics with reduced glutathione (GSH) (cotransport) as well as conjugated organic anions such as leukotriene C(4) (LTC(4)). Glutathione 212-215 ATP binding cassette subfamily B member 1 Homo sapiens 64-68 11306701-3 2001 Most flavonoids inhibited MRP1-mediated LTC(4) transport in membrane vesicles and inhibition by several flavonoids was enhanced by GSH. Glutathione 131-134 ATP binding cassette subfamily B member 1 Homo sapiens 26-30 11306701-7 2001 Several flavonoids, especially naringenin and apigenin, markedly stimulated GSH transport by MRP1, suggesting they may be cotransported with this tripeptide. Glutathione 76-79 ATP binding cassette subfamily B member 1 Homo sapiens 93-97 11115505-7 2001 To explain this selectivity of MRP1/GST-mediated resistance, we report results of side-by-side experiments comparing the kinetics of MLP- versus CHB-glutathione conjugate: formation, product inhibition of GSTA1-1 catalysis, and transport by MRP1. Glutathione 149-160 ATP binding cassette subfamily B member 1 Homo sapiens 31-35 11102445-0 2001 Glutathione stimulates sulfated estrogen transport by multidrug resistance protein 1. Glutathione 0-11 ATP binding cassette subfamily B member 1 Homo sapiens 54-84 11102445-13 2001 These results provide the first example of GSH-stimulated, MRP1-mediated transport of a potential endogenous substrate and expand the range of MRP1 substrates whose transport is stimulated by GSH to include certain hydrophilic conjugated endobiotics, in addition to previously identified hydrophobic xenobiotics. Glutathione 43-46 ATP binding cassette subfamily B member 1 Homo sapiens 59-63 11102445-13 2001 These results provide the first example of GSH-stimulated, MRP1-mediated transport of a potential endogenous substrate and expand the range of MRP1 substrates whose transport is stimulated by GSH to include certain hydrophilic conjugated endobiotics, in addition to previously identified hydrophobic xenobiotics. Glutathione 43-46 ATP binding cassette subfamily B member 1 Homo sapiens 143-147 11102445-13 2001 These results provide the first example of GSH-stimulated, MRP1-mediated transport of a potential endogenous substrate and expand the range of MRP1 substrates whose transport is stimulated by GSH to include certain hydrophilic conjugated endobiotics, in addition to previously identified hydrophobic xenobiotics. Glutathione 192-195 ATP binding cassette subfamily B member 1 Homo sapiens 59-63 11102445-13 2001 These results provide the first example of GSH-stimulated, MRP1-mediated transport of a potential endogenous substrate and expand the range of MRP1 substrates whose transport is stimulated by GSH to include certain hydrophilic conjugated endobiotics, in addition to previously identified hydrophobic xenobiotics. Glutathione 192-195 ATP binding cassette subfamily B member 1 Homo sapiens 143-147 10950878-1 2000 CFTR (cystic fibrosis transmembrane conductance regulator), MDR1 (multidrug resistance), and MRP1 (multidrug resistance-associated protein), members of the ABC transporter superfamily, possess multiple functions, particularly Cl(-), anion, and glutathione conjugate transport and cell detoxification. Glutathione 244-255 ATP binding cassette subfamily B member 1 Homo sapiens 60-64 11721885-2 2001 In addition, MRP1 is expressed in normal tissues acting as an efflux pump for glutathione, glucuronate, and sulfate conjugates and may thus influence the pharmacokinetic properties of many drugs. Glutathione 78-89 ATP binding cassette subfamily B member 1 Homo sapiens 13-17 10773025-0 2000 Verapamil stimulates glutathione transport by the 190-kDa multidrug resistance protein 1 (MRP1). Glutathione 21-32 ATP binding cassette subfamily B member 1 Homo sapiens 58-88 10747957-4 2000 Vanadate-induced nucleotide trapping in MRP1 was found to be stimulated by reduced glutathione, glutathione disulfide, and etoposide and to be synergistically stimulated by the presence of etoposide and either glutathione. Glutathione 83-94 ATP binding cassette subfamily B member 1 Homo sapiens 40-44 10747957-4 2000 Vanadate-induced nucleotide trapping in MRP1 was found to be stimulated by reduced glutathione, glutathione disulfide, and etoposide and to be synergistically stimulated by the presence of etoposide and either glutathione. Glutathione 96-107 ATP binding cassette subfamily B member 1 Homo sapiens 40-44 10747957-5 2000 These results suggest that glutathione and etoposide interact with MRP1 at different sites and that those bindings cooperatively stimulate the nucleotide trapping. Glutathione 27-38 ATP binding cassette subfamily B member 1 Homo sapiens 67-71 10773025-0 2000 Verapamil stimulates glutathione transport by the 190-kDa multidrug resistance protein 1 (MRP1). Glutathione 21-32 ATP binding cassette subfamily B member 1 Homo sapiens 90-94 10773025-8 2000 However, verapamil strongly stimulated MRP1-mediated GSH uptake by membrane vesicles in a concentration-dependent and osmotically sensitive manner that was inhibitable by MRP1-specific monoclonal antibodies. Glutathione 53-56 ATP binding cassette subfamily B member 1 Homo sapiens 39-43 10773025-8 2000 However, verapamil strongly stimulated MRP1-mediated GSH uptake by membrane vesicles in a concentration-dependent and osmotically sensitive manner that was inhibitable by MRP1-specific monoclonal antibodies. Glutathione 53-56 ATP binding cassette subfamily B member 1 Homo sapiens 171-175 10773025-10 2000 It is proposed that the variable ability of verapamil to modulate MRP1-mediated resistance in different cell lines may be more closely linked to its effect on the GSH status of the cells than on its ability to inhibit the MRP1 transporter itself. Glutathione 163-166 ATP binding cassette subfamily B member 1 Homo sapiens 66-70 28481204-3 1997 The unique functional features of this transporter include its ability to mediate ATP-dependent transmembrane movement of organic anions such as glutathione conjugates, as well as weakly cationic amphiphilic compounds such as doxorubicin and other substrates of P-glycoprotein. Glutathione 145-156 ATP binding cassette subfamily B member 1 Homo sapiens 262-276 10024515-7 1999 Similarly, MDCKII cells expressing the human multidrug resistance protein 1 showed a 4-fold increase in GSH excretion across the basolateral membrane. Glutathione 104-107 ATP binding cassette subfamily B member 1 Homo sapiens 45-75 10500793-3 1999 Known mechanisms of MDR are overexpression of the ATP-dependent membrane proteins P-glycoprotein (P-gp) and multidrug resistance protein (MRP1), or an increased detoxification of compounds mediated by glutathione (GSH) or GSH related enzymes. Glutathione 222-225 ATP binding cassette subfamily B member 1 Homo sapiens 82-96 10500793-3 1999 Known mechanisms of MDR are overexpression of the ATP-dependent membrane proteins P-glycoprotein (P-gp) and multidrug resistance protein (MRP1), or an increased detoxification of compounds mediated by glutathione (GSH) or GSH related enzymes. Glutathione 222-225 ATP binding cassette subfamily B member 1 Homo sapiens 98-102 9533762-0 1998 Transport of glutathione conjugates into secretory vesicles is mediated by the multidrug-resistance protein 1. Glutathione 13-24 ATP binding cassette subfamily B member 1 Homo sapiens 79-109 10708754-0 2000 The effect of glutathione on the ATPase activity of MRP1 in its natural membranes. Glutathione 14-25 ATP binding cassette subfamily B member 1 Homo sapiens 52-56 10708754-2 2000 However, the cellular antioxidant glutathione (GSH) has been shown to have an important role in MRP1-mediated drug transport. Glutathione 34-45 ATP binding cassette subfamily B member 1 Homo sapiens 96-100 10708754-2 2000 However, the cellular antioxidant glutathione (GSH) has been shown to have an important role in MRP1-mediated drug transport. Glutathione 47-50 ATP binding cassette subfamily B member 1 Homo sapiens 96-100 10708754-3 2000 In this study we show that GSH stimulates the ATPase activity of MRP1 in a natural plasma membrane environment. Glutathione 27-30 ATP binding cassette subfamily B member 1 Homo sapiens 65-69 10708754-6 2000 In addition, the effect of GSH on the MRP1 ATPase activity is not increased by daunorubicin or by vincristine. Glutathione 27-30 ATP binding cassette subfamily B member 1 Homo sapiens 38-42 10708754-7 2000 In contrast, a GSH conjugate of daunorubicin (WP811) does induce the ATPase activity of MRP1. Glutathione 15-18 ATP binding cassette subfamily B member 1 Homo sapiens 88-92 9184795-19 1997 Unlike Pgp, MRP is able to transport metallic oxyanions and glutathione and other conjugates, including peptidyl leukotrienes. Glutathione 60-71 ATP binding cassette subfamily B member 1 Homo sapiens 7-10 9187270-3 1997 Two possible candidates for this GSH conjugate pump are the 190-kDa multidrug resistance protein (MRP) and the 170-kDa P-glycoprotein. Glutathione 33-36 ATP binding cassette subfamily B member 1 Homo sapiens 119-133 7578013-3 1995 We used the glutathione S-transferase gene fusion system to express and purify a series of fusion proteins containing the relevant portion (residues 644-689) of the linker region of the human MDR1 gene product. Glutathione 12-23 ATP binding cassette subfamily B member 1 Homo sapiens 192-196 8831715-9 1996 P-glycoprotein-enriched membrane vesicles have been shown to directly transport several chemotherapeutic drugs, whereas vincristine transport by MRP-enriched membrane vesicles is demonstrable only in the presence of reduced glutathione. Glutathione 224-235 ATP binding cassette subfamily B member 1 Homo sapiens 0-14 34842266-6 2021 In addition, the presence of copper ions could allow glutathione (GHS) to be consumed and oxygen to be produced, likely suppressing the expression of P-glycoprotein (P-gp) and overcoming the issue of MDR relating to LT. More importantly, synergistic chemo-photothermal therapy with LT and Cu2-xS NCs was more effective than any single therapy or theoretical combination. Glutathione 53-64 ATP binding cassette subfamily B member 1 Homo sapiens 150-164 7644478-3 1995 Glutathione depletion had less effect on MDR in cells transfected with MDR1 cDNA encoding P-glycoprotein and did not increase the passive uptake of daunorubicin by cells, indicating that the decrease of MRP-mediated MDR was not due to nonspecific membrane damage. Glutathione 0-11 ATP binding cassette subfamily B member 1 Homo sapiens 71-75 8093688-2 1993 Oxidize glutathione and glutathione thioethers are transported out of cells by ATP dependent systems that are distinct from the P glycoprotein pathway. Glutathione 8-19 ATP binding cassette subfamily B member 1 Homo sapiens 128-142 2200165-0 1990 Is the glutathione S-conjugate carrier an mdr1 gene product? Glutathione 7-18 ATP binding cassette subfamily B member 1 Homo sapiens 42-46 34842266-6 2021 In addition, the presence of copper ions could allow glutathione (GHS) to be consumed and oxygen to be produced, likely suppressing the expression of P-glycoprotein (P-gp) and overcoming the issue of MDR relating to LT. More importantly, synergistic chemo-photothermal therapy with LT and Cu2-xS NCs was more effective than any single therapy or theoretical combination. Glutathione 53-64 ATP binding cassette subfamily B member 1 Homo sapiens 166-170 35080351-0 2022 GSH facilitates the binding and inhibitory activity of novel Multidrug resistance protein 1 (MRP1) modulators. Glutathione 0-3 ATP binding cassette subfamily B member 1 Homo sapiens 61-91 35080351-0 2022 GSH facilitates the binding and inhibitory activity of novel Multidrug resistance protein 1 (MRP1) modulators. Glutathione 0-3 ATP binding cassette subfamily B member 1 Homo sapiens 93-97 35080351-1 2022 MRP1 (ABCC1) is a membrane transporter that confers multidrug resistance in cancer cells by exporting chemotherapeutic agents, often in a glutathione (GSH) dependent manner. Glutathione 138-149 ATP binding cassette subfamily B member 1 Homo sapiens 0-4 35080351-1 2022 MRP1 (ABCC1) is a membrane transporter that confers multidrug resistance in cancer cells by exporting chemotherapeutic agents, often in a glutathione (GSH) dependent manner. Glutathione 151-154 ATP binding cassette subfamily B member 1 Homo sapiens 0-4 35080351-2 2022 This transport activity can be altered by compounds (modulators) that block drug transport while simultaneously stimulating GSH efflux by MRP1. Glutathione 124-127 ATP binding cassette subfamily B member 1 Homo sapiens 138-142 35080351-3 2022 In MRP1-expressing cells, modulator-stimulated GSH efflux can be sufficient to deplete GSH and increase sensitivity to chemotherapy, enhancing cancer cell death. Glutathione 47-50 ATP binding cassette subfamily B member 1 Homo sapiens 3-7 35080351-3 2022 In MRP1-expressing cells, modulator-stimulated GSH efflux can be sufficient to deplete GSH and increase sensitivity to chemotherapy, enhancing cancer cell death. Glutathione 87-90 ATP binding cassette subfamily B member 1 Homo sapiens 3-7 35080351-4 2022 Further development of clinically useful MRP1 modulators requires a better mechanistic understanding of modulator binding and its relationship to GSH binding and transport. Glutathione 146-149 ATP binding cassette subfamily B member 1 Homo sapiens 41-45 35080351-6 2022 Binding of these modulators to MRP1 was dependent on the presence of GSH but not its reducing capacity. Glutathione 69-72 ATP binding cassette subfamily B member 1 Homo sapiens 31-35 35080351-7 2022 Accordingly, the modulators poorly inhibited organic anion transport by K332L-mutant MRP1 where GSH binding and transport is limited. Glutathione 96-99 ATP binding cassette subfamily B member 1 Homo sapiens 85-89 35080351-9 2022 Immunoblots of limited trypsin digests of MRP1 suggest that binding of GSH, but not the modulators, induces a conformation change in MRP1. Glutathione 71-74 ATP binding cassette subfamily B member 1 Homo sapiens 42-46 35080351-9 2022 Immunoblots of limited trypsin digests of MRP1 suggest that binding of GSH, but not the modulators, induces a conformation change in MRP1. Glutathione 71-74 ATP binding cassette subfamily B member 1 Homo sapiens 133-137 35080351-10 2022 Together, these findings support the model in which GSH binding induces a conformation change that facilitates binding of MRP1 modulators, possibly in a proposed hydrophobic binding pocket of MRP1. Glutathione 52-55 ATP binding cassette subfamily B member 1 Homo sapiens 122-126 35080351-10 2022 Together, these findings support the model in which GSH binding induces a conformation change that facilitates binding of MRP1 modulators, possibly in a proposed hydrophobic binding pocket of MRP1. Glutathione 52-55 ATP binding cassette subfamily B member 1 Homo sapiens 192-196 35173543-0 2022 High Expression of G6PD Increases Doxorubicin Resistance in Triple Negative Breast Cancer Cells by Maintaining GSH Level. Glutathione 111-114 ATP binding cassette subfamily B member 1 Homo sapiens 34-56