Molecular analysis of the massive GSH transport mechanism mediated by the human Multidrug Resistant Protein 1/ABCC1
The transporter Multidrug Resistance Protein 1 (MRP1, ABCC1) is implicated in multidrug resistant (MDR) phenotype of cancer cells. Glutathione (GSH) plays a key role in MRP1 transport activities. In addition, a ligand-stimulated GSH transport which triggers the death of cells overexpressing MRP1, by...
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| Veröffentlicht in: | Scientific reports 2020-05, Vol.10 (1), p.7616-7616, Article 7616 |
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| creator | Nasr, Rachad Lorendeau, Doriane Khonkarn, Ruttiros Dury, Lauriane Pérès, Basile Boumendjel, Ahcène Cortay, Jean-Claude Falson, Pierre Chaptal, Vincent Baubichon-Cortay, Hélène |
| description | The transporter Multidrug Resistance Protein 1 (MRP1, ABCC1) is implicated in multidrug resistant (MDR) phenotype of cancer cells. Glutathione (GSH) plays a key role in MRP1 transport activities. In addition, a ligand-stimulated GSH transport which triggers the death of cells overexpressing MRP1, by collateral sensitivity (CS), has been described. This CS could be a way to overcome the poor prognosis for patients suffering from a chemoresistant cancer. The molecular mechanism of such massive GSH transport and its connection to the other transport activities of MRP1 are unknown. In this context, we generated MRP1/MRP2 chimeras covering different regions, MRP2 being a close homolog that does not trigger CS. The one encompassing helices 16 and 17 led to the loss of CS and MDR phenotype without altering basal GSH transport. Within this region, the sole restoration of the original G1228 (D1236 in MRP2) close to the extracellular loop between the two helices fully rescued the CS (massive GSH efflux and cell death) but not the MDR phenotype. 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. |
| doi_str_mv | 10.1038/s41598-020-64400-x |
| format | Article |
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Glutathione (GSH) plays a key role in MRP1 transport activities. In addition, a ligand-stimulated GSH transport which triggers the death of cells overexpressing MRP1, by collateral sensitivity (CS), has been described. This CS could be a way to overcome the poor prognosis for patients suffering from a chemoresistant cancer. The molecular mechanism of such massive GSH transport and its connection to the other transport activities of MRP1 are unknown. In this context, we generated MRP1/MRP2 chimeras covering different regions, MRP2 being a close homolog that does not trigger CS. The one encompassing helices 16 and 17 led to the loss of CS and MDR phenotype without altering basal GSH transport. Within this region, the sole restoration of the original G1228 (D1236 in MRP2) close to the extracellular loop between the two helices fully rescued the CS (massive GSH efflux and cell death) but not the MDR phenotype. 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.</description><identifier>ISSN: 2045-2322</identifier><identifier>EISSN: 2045-2322</identifier><identifier>DOI: 10.1038/s41598-020-64400-x</identifier><identifier>PMID: 32377003</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>631/1647 ; 631/337 ; 631/45 ; Bile ; Biological Transport ; Cancer ; Cell death ; Cell Line ; Cell Membrane - metabolism ; Cellular Biology ; Chimeras ; Genotype & phenotype ; Glutathione ; Glutathione - metabolism ; Humanities and Social Sciences ; Humans ; Life Sciences ; Models, Molecular ; multidisciplinary ; Multidrug resistance ; Multidrug Resistance-Associated Proteins - chemistry ; Multidrug Resistance-Associated Proteins - metabolism ; Multidrug resistant organisms ; Phenotypes ; Protein Domains ; Protein transport ; Science ; Science (multidisciplinary) ; Subcellular Processes ; Verapamil</subject><ispartof>Scientific reports, 2020-05, Vol.10 (1), p.7616-7616, Article 7616</ispartof><rights>The Author(s) 2020</rights><rights>The Author(s) 2020. 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Glutathione (GSH) plays a key role in MRP1 transport activities. In addition, a ligand-stimulated GSH transport which triggers the death of cells overexpressing MRP1, by collateral sensitivity (CS), has been described. This CS could be a way to overcome the poor prognosis for patients suffering from a chemoresistant cancer. The molecular mechanism of such massive GSH transport and its connection to the other transport activities of MRP1 are unknown. In this context, we generated MRP1/MRP2 chimeras covering different regions, MRP2 being a close homolog that does not trigger CS. The one encompassing helices 16 and 17 led to the loss of CS and MDR phenotype without altering basal GSH transport. Within this region, the sole restoration of the original G1228 (D1236 in MRP2) close to the extracellular loop between the two helices fully rescued the CS (massive GSH efflux and cell death) but not the MDR phenotype. 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Glutathione (GSH) plays a key role in MRP1 transport activities. In addition, a ligand-stimulated GSH transport which triggers the death of cells overexpressing MRP1, by collateral sensitivity (CS), has been described. This CS could be a way to overcome the poor prognosis for patients suffering from a chemoresistant cancer. The molecular mechanism of such massive GSH transport and its connection to the other transport activities of MRP1 are unknown. In this context, we generated MRP1/MRP2 chimeras covering different regions, MRP2 being a close homolog that does not trigger CS. The one encompassing helices 16 and 17 led to the loss of CS and MDR phenotype without altering basal GSH transport. Within this region, the sole restoration of the original G1228 (D1236 in MRP2) close to the extracellular loop between the two helices fully rescued the CS (massive GSH efflux and cell death) but not the MDR phenotype. 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.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>32377003</pmid><doi>10.1038/s41598-020-64400-x</doi><tpages>1</tpages><orcidid>https://orcid.org/0000-0003-2647-4530</orcidid><orcidid>https://orcid.org/0000-0002-1830-6409</orcidid><orcidid>https://orcid.org/0000-0001-9921-0187</orcidid><orcidid>https://orcid.org/0000-0002-9760-4577</orcidid><orcidid>https://orcid.org/0000-0003-2603-0294</orcidid><oa>free_for_read</oa></addata></record> |
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| subjects | 631/1647 631/337 631/45 Bile Biological Transport Cancer Cell death Cell Line Cell Membrane - metabolism Cellular Biology Chimeras Genotype & phenotype Glutathione Glutathione - metabolism Humanities and Social Sciences Humans Life Sciences Models, Molecular multidisciplinary Multidrug resistance Multidrug Resistance-Associated Proteins - chemistry Multidrug Resistance-Associated Proteins - metabolism Multidrug resistant organisms Phenotypes Protein Domains Protein transport Science Science (multidisciplinary) Subcellular Processes Verapamil |
| title | Molecular analysis of the massive GSH transport mechanism mediated by the human Multidrug Resistant Protein 1/ABCC1 |
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