PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 16004972-1 2005 Human erythrocyte membranes express the multidrug resistance-associated proteins, MRP1, MRP4 and 5, that collectively can efflux oxidised glutathione, glutathione conjugates and cyclic nucleotides. Glutathione 138-149 ATP binding cassette subfamily C member 4 Homo sapiens 88-98 32472168-0 2020 Human multidrug resistance protein 4 (MRP4) is a cellular efflux transporter for paracetamol glutathione and cysteine conjugates. Glutathione 93-104 ATP binding cassette subfamily C member 4 Homo sapiens 6-36 32472168-0 2020 Human multidrug resistance protein 4 (MRP4) is a cellular efflux transporter for paracetamol glutathione and cysteine conjugates. Glutathione 93-104 ATP binding cassette subfamily C member 4 Homo sapiens 38-42 28885828-10 2017 Furthermore, it was found that MRP4-mediated detoxication of the HBQs was GSH dependent, as the cytotoxicity of the HBQs was increased in GSH-depleted HEK-MRP4 cells in comparison to HEK-MRP4 cells. Glutathione 74-77 ATP binding cassette subfamily C member 4 Homo sapiens 31-35 28885828-10 2017 Furthermore, it was found that MRP4-mediated detoxication of the HBQs was GSH dependent, as the cytotoxicity of the HBQs was increased in GSH-depleted HEK-MRP4 cells in comparison to HEK-MRP4 cells. Glutathione 74-77 ATP binding cassette subfamily C member 4 Homo sapiens 155-159 28885828-10 2017 Furthermore, it was found that MRP4-mediated detoxication of the HBQs was GSH dependent, as the cytotoxicity of the HBQs was increased in GSH-depleted HEK-MRP4 cells in comparison to HEK-MRP4 cells. Glutathione 74-77 ATP binding cassette subfamily C member 4 Homo sapiens 155-159 28885828-10 2017 Furthermore, it was found that MRP4-mediated detoxication of the HBQs was GSH dependent, as the cytotoxicity of the HBQs was increased in GSH-depleted HEK-MRP4 cells in comparison to HEK-MRP4 cells. Glutathione 138-141 ATP binding cassette subfamily C member 4 Homo sapiens 31-35 28885828-10 2017 Furthermore, it was found that MRP4-mediated detoxication of the HBQs was GSH dependent, as the cytotoxicity of the HBQs was increased in GSH-depleted HEK-MRP4 cells in comparison to HEK-MRP4 cells. Glutathione 138-141 ATP binding cassette subfamily C member 4 Homo sapiens 155-159 28885828-10 2017 Furthermore, it was found that MRP4-mediated detoxication of the HBQs was GSH dependent, as the cytotoxicity of the HBQs was increased in GSH-depleted HEK-MRP4 cells in comparison to HEK-MRP4 cells. Glutathione 138-141 ATP binding cassette subfamily C member 4 Homo sapiens 155-159 28885828-11 2017 The GSH-dependent protection of cells from HBQs supports the possibility of HBQ-GSH conjugate efflux by MRP4. Glutathione 4-7 ATP binding cassette subfamily C member 4 Homo sapiens 104-108 28885828-11 2017 The GSH-dependent protection of cells from HBQs supports the possibility of HBQ-GSH conjugate efflux by MRP4. Glutathione 80-83 ATP binding cassette subfamily C member 4 Homo sapiens 104-108 28249282-7 2017 Bile acids are substrates for human MRP4 in the presence of physiological concentrations of reduced glutathione, which undergoes co-transport. Glutathione 100-111 ATP binding cassette subfamily C member 4 Homo sapiens 36-40 23462933-10 2013 The glucuronide, sulfate, and GSH conjugates are excreted by transporters in the canalicular (Mrp2 and Bcrp) and basolateral (Mrp3 and Mrp4) hepatocyte membranes. Glutathione 30-33 ATP binding cassette subfamily C member 4 Homo sapiens 135-139 17959747-4 2008 Here, we demonstrate that human ABCC4 mediates the ATP-dependent efflux of LTB(4) in the presence of reduced glutathione (GSH), whereby the latter can be replaced by S-methyl GSH. Glutathione 109-120 ATP binding cassette subfamily C member 4 Homo sapiens 32-37 17959747-4 2008 Here, we demonstrate that human ABCC4 mediates the ATP-dependent efflux of LTB(4) in the presence of reduced glutathione (GSH), whereby the latter can be replaced by S-methyl GSH. Glutathione 122-125 ATP binding cassette subfamily C member 4 Homo sapiens 32-37 17959747-4 2008 Here, we demonstrate that human ABCC4 mediates the ATP-dependent efflux of LTB(4) in the presence of reduced glutathione (GSH), whereby the latter can be replaced by S-methyl GSH. Glutathione 175-178 ATP binding cassette subfamily C member 4 Homo sapiens 32-37 17518506-4 2007 While erythrocytes mainly express multidrug resistance protein (MRP) 1, MRP4 and MRP5, which are discussed with regard to their involvement in glutathione homeostasis (MRP1) and in the efflux of cyclic nucleotides (MRP4 and MRP5), leukocytes also express P-glycoprotein and breast cancer resistance protein. Glutathione 143-154 ATP binding cassette subfamily C member 4 Homo sapiens 72-76 17518506-4 2007 While erythrocytes mainly express multidrug resistance protein (MRP) 1, MRP4 and MRP5, which are discussed with regard to their involvement in glutathione homeostasis (MRP1) and in the efflux of cyclic nucleotides (MRP4 and MRP5), leukocytes also express P-glycoprotein and breast cancer resistance protein. Glutathione 143-154 ATP binding cassette subfamily C member 4 Homo sapiens 215-219 16282361-0 2006 Substrate specificity of human ABCC4 (MRP4)-mediated cotransport of bile acids and reduced glutathione. Glutathione 91-102 ATP binding cassette subfamily C member 4 Homo sapiens 31-36 16282361-0 2006 Substrate specificity of human ABCC4 (MRP4)-mediated cotransport of bile acids and reduced glutathione. Glutathione 91-102 ATP binding cassette subfamily C member 4 Homo sapiens 38-42 16282361-2 2006 Previous studies showed that human ABCC4 is localized to the sinusoidal membrane of hepatocytes and mediates, among other substrates, the cotransport of reduced glutathione (GSH) with bile acids. Glutathione 161-172 ATP binding cassette subfamily C member 4 Homo sapiens 35-40 16282361-2 2006 Previous studies showed that human ABCC4 is localized to the sinusoidal membrane of hepatocytes and mediates, among other substrates, the cotransport of reduced glutathione (GSH) with bile acids. Glutathione 174-177 ATP binding cassette subfamily C member 4 Homo sapiens 35-40 16282361-3 2006 In the present study, using inside-out membrane vesicles, we demonstrated that human ABCC4 in the presence of physiological concentrations of GSH has a high affinity for the taurine and glycine conjugates of the common natural bile acids as well as the unconjugated bile acid cholate. Glutathione 142-145 ATP binding cassette subfamily C member 4 Homo sapiens 85-90 16282361-4 2006 Chenodeoxycholyltaurine and chenodeoxycholylglycine were the GSH cosubstrates with the highest affinities for ABCC4, with K(m) values of 3.6 and 5.9 microM, respectively. Glutathione 61-64 ATP binding cassette subfamily C member 4 Homo sapiens 110-115 16282361-5 2006 Ursodeoxycholyltaurine and ursodeoxycholylglycine were cotransported together with GSH by ABCC4 with K(m) values of 7.8 and 12.5 microM, respectively, but no transport of ursodeoxycholate and deoxycholate was observed. Glutathione 83-86 ATP binding cassette subfamily C member 4 Homo sapiens 90-95 32855883-5 2020 Screening of GSH/GSSG efflux transporters revealed Mrp1, Mrp4, and Mrp5 to be present at the transcript level, but only Mrp5 was expressed at the protein level. Glutathione 13-16 ATP binding cassette subfamily C member 4 Homo sapiens 57-61 16004972-1 2005 Human erythrocyte membranes express the multidrug resistance-associated proteins, MRP1, MRP4 and 5, that collectively can efflux oxidised glutathione, glutathione conjugates and cyclic nucleotides. Glutathione 151-162 ATP binding cassette subfamily C member 4 Homo sapiens 88-98 15747503-6 2005 MRP4 also seems to be able to mediate the transport of conjugated steroids, prostaglandins, and glutathione. Glutathione 96-107 ATP binding cassette subfamily C member 4 Homo sapiens 0-4 14643890-6 2004 Using cells stably overexpressing ABCC4, this study shows that ABCC4 can facilitate the efflux of the glutathione conjugate, bimane-glutathione. Glutathione 102-113 ATP binding cassette subfamily C member 4 Homo sapiens 34-39 14643890-6 2004 Using cells stably overexpressing ABCC4, this study shows that ABCC4 can facilitate the efflux of the glutathione conjugate, bimane-glutathione. Glutathione 102-113 ATP binding cassette subfamily C member 4 Homo sapiens 63-68 14643890-12 2004 The determination that ABCC4 can mediate the transport of glucuronide and glutathione conjugates indicates that ABCC4 may play a role in the cellular extrusion of Phase II detoxification metabolites. Glutathione 74-85 ATP binding cassette subfamily C member 4 Homo sapiens 23-28 14643890-12 2004 The determination that ABCC4 can mediate the transport of glucuronide and glutathione conjugates indicates that ABCC4 may play a role in the cellular extrusion of Phase II detoxification metabolites. Glutathione 74-85 ATP binding cassette subfamily C member 4 Homo sapiens 112-117 12883481-0 2003 Cotransport of reduced glutathione with bile salts by MRP4 (ABCC4) localized to the basolateral hepatocyte membrane. Glutathione 23-34 ATP binding cassette subfamily C member 4 Homo sapiens 54-58 12883481-0 2003 Cotransport of reduced glutathione with bile salts by MRP4 (ABCC4) localized to the basolateral hepatocyte membrane. Glutathione 23-34 ATP binding cassette subfamily C member 4 Homo sapiens 60-65 12883481-4 2003 Recombinant human MRP4, expressed in V79 hamster fibroblasts and studied in membrane vesicles, mediated ATP-dependent cotransport of GSH or S-methyl-glutathione together with cholyltaurine, cholylglycine, or cholate. Glutathione 133-136 ATP binding cassette subfamily C member 4 Homo sapiens 18-22 12883481-10 2003 In conclusion, MRP4 can mediate the efflux of GSH from hepatocytes into blood by cotransport with monoanionic bile salts. Glutathione 46-49 ATP binding cassette subfamily C member 4 Homo sapiens 15-19 11802779-0 2002 Role of glutathione in the multidrug resistance protein 4 (MRP4/ABCC4)-mediated efflux of cAMP and resistance to purine analogues. Glutathione 8-19 ATP binding cassette subfamily C member 4 Homo sapiens 59-63 11802779-0 2002 Role of glutathione in the multidrug resistance protein 4 (MRP4/ABCC4)-mediated efflux of cAMP and resistance to purine analogues. Glutathione 8-19 ATP binding cassette subfamily C member 4 Homo sapiens 64-69 11802779-4 2002 Using cells stably overexpressing ABCC4, this study shows that ABCC4 exports GSH. Glutathione 77-80 ATP binding cassette subfamily C member 4 Homo sapiens 34-39 11802779-4 2002 Using cells stably overexpressing ABCC4, this study shows that ABCC4 exports GSH. Glutathione 77-80 ATP binding cassette subfamily C member 4 Homo sapiens 63-68 11802779-9 2002 We conclude that as well as nucleotide and nucleoside analogues, ABCC4 can mediate the export of GSH. Glutathione 97-100 ATP binding cassette subfamily C member 4 Homo sapiens 65-70 11802779-10 2002 In addition, GSH plays an important role in the function of ABCC4. Glutathione 13-16 ATP binding cassette subfamily C member 4 Homo sapiens 60-65 11802779-11 2002 Depletion of intracellular GSH adversely affects the export of cAMP by ABCC4. Glutathione 27-30 ATP binding cassette subfamily C member 4 Homo sapiens 71-76 15845416-4 2005 In particular, five of the 12 members of the MRP/CFTR family appear to mediate GSH export from cells namely, MRP1, MRP2, MRP4, MRP5, and CFTR. Glutathione 79-82 ATP binding cassette subfamily C member 4 Homo sapiens 121-125 15501592-8 2004 MRP proteins may, thus, contribute to the cellular efflux of endogenous anionic glutathione or glucuronate conjugates (substrates for MRP1), cyclic nucleotides (substrates for MRP4 and MRP5), or glutathione (co-substrate for MRP1 and MRP4); in addition, they may play an important role in the resistance of the brain to several cytotoxic and antiviral drugs. Glutathione 80-91 ATP binding cassette subfamily C member 4 Homo sapiens 176-180 15501592-8 2004 MRP proteins may, thus, contribute to the cellular efflux of endogenous anionic glutathione or glucuronate conjugates (substrates for MRP1), cyclic nucleotides (substrates for MRP4 and MRP5), or glutathione (co-substrate for MRP1 and MRP4); in addition, they may play an important role in the resistance of the brain to several cytotoxic and antiviral drugs. Glutathione 80-91 ATP binding cassette subfamily C member 4 Homo sapiens 234-238 15501592-8 2004 MRP proteins may, thus, contribute to the cellular efflux of endogenous anionic glutathione or glucuronate conjugates (substrates for MRP1), cyclic nucleotides (substrates for MRP4 and MRP5), or glutathione (co-substrate for MRP1 and MRP4); in addition, they may play an important role in the resistance of the brain to several cytotoxic and antiviral drugs. Glutathione 195-206 ATP binding cassette subfamily C member 4 Homo sapiens 176-180 15501592-8 2004 MRP proteins may, thus, contribute to the cellular efflux of endogenous anionic glutathione or glucuronate conjugates (substrates for MRP1), cyclic nucleotides (substrates for MRP4 and MRP5), or glutathione (co-substrate for MRP1 and MRP4); in addition, they may play an important role in the resistance of the brain to several cytotoxic and antiviral drugs. Glutathione 195-206 ATP binding cassette subfamily C member 4 Homo sapiens 234-238