TAILIEUCHUNG - Báo cáo Y học: S-Decyl-glutathione nonspecifically stimulates the ATPase activity of the nucleotide-binding domains of the human multidrug resistance-associated protein, MRP1 (ABCC1)

The human multidrug resistance-associated protein (MRP1) is an ATP-dependent efflux pump that transports anionic conjugates, and hydrophobic compounds in a glutathione dependent manner. Similar to the other, well-characterized multidrug transporter P-gp, MRP1 comprises two nucleotide-binding domains (NBDs) in addition to transmembrane domains. However, whereas the NBDs of P-gp have been shown to be functionally equivalent, those of MRP1 differ significantly. | Eur. J. Biochem. 269 3470-3478 2002 FEBS 2002 doi 5-Decyl-glutathione nonspecifically stimulates the ATPase activity of the nucleotide-binding domains of the human multidrug resistance-associated protein MRP1 ABCC1 Robbert H. Cool1 Marloes K. Veenstra1 Wim van Klompenburg1 Rene I. R. Heyne1 Michael Muller Elisabeth G. E. de Vries3 Hendrik W. van Veen1 f and Wil N. Konings1 1Department of Microbiology Groningen Biomolecular Sciences and Biotechnology Institute University of Groningen Haren the Netherlands department of Gasteroenterology and Hepatology University Hospital Groningen the Netherlands 3Department of Medical Oncology University Hospital Groningen the Netherlands The human multidrug resistance-associated protein MRP1 is an ATP-dependent efflux pump that transports anionic conjugates and hydrophobic compounds in a glutathione dependent manner. Similar to the other well-characterized multidrug transporter P-gp MRP1 comprises two nucleotide-binding domains NBDs in addition to transmembrane domains. However whereas the NBDs of P-gp have been shown to be functionally equivalent those of MRP1 differ significantly. The isolated NBDs of MRP1 have been characterized in Escherichia coli as fusions with either the glutathione-S-transferase GST or the maltose-binding domain MBP . The nonfused NBD1 was obtained bycleavage of the fusion protein with thrombin. The GST-fused forms of NBD1 and NBD2 hydrolyzed ATP with an apparent Km of 340 M and a Vmax of nmol PI-mg_1-min-1 and a Km of 910 M ATP and a Vmax of nmol PI-mg_1-min-1 respectively. Remarkably S-decyl-glutathione a conjugate specifically transported by MRP I and MRP 22. was able to tlim u aa le the ATPase activities of the isolated NBDs more than 2-fold in a concentration-dependent manner. However the stimulation of the ATPase activity wss Ho Lind to comcide with the formation of micelles by S-decyl-glutathione. Equivalent stimulation of ATPase activity co mid be obtained .

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