Transport of organic anions by multidrug resistance-associated protein in the erythrocyte. | Zendy

Błażej Rychlik | Zendy; Łukasz Pułaski | Zendy; Adam Sokal | Zendy; Mirosław Soszyński | Zendy; Grzegorz Bartosz | Zendy

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Transport of organic anions by multidrug resistance-associated protein in the erythrocyte.

Author(s) -

Błażej Rychlik,

Łukasz Pułaski,

Adam Sokal,

Mirosław Soszyński,

Grzegorz Bartosz

Publication year - 2000

Publication title -

acta biochimica polonica

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.452

H-Index - 78

eISSN - 1734-154X

pISSN - 0001-527X

DOI - 10.18388/abp.2000_3994

Subject(s) - glutathione , conjugate , chemistry , multiple drug resistance , biochemistry , atpase , transport protein , multidrug resistance associated proteins , substrate (aquarium) , enzyme , transporter , biology , atp binding cassette transporter , mathematical analysis , ecology , mathematics , gene , antibiotics

The active transport of oxidized glutathione and glutathione S-conjugates has been demonstrated for the first time in erythrocytes and this cell remained the main subject of research on the "glutathione S-conjugate pump" for years. Further studies identified the "glutathione S-conjugate pump" as multidrug resistance-associated protein (MRP). Even though cells overexpressing MRP and isolated MRP provide useful information on MRP structure and function, the erythrocyte remains an interesting model cell for studies of MRP1 in its natural environment, including the substrate specificity and ATPase activity of the protein.

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