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Mutagenesis of the putative nucleotide-binding domains of the multidrug resistance associated protein (MRP). Analysis of the effect of these mutations on MRP mediated drug resistance and transport

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Mutagenesis of the putative nucleotide-binding domains of the multidrug resistance associated protein (MRP). Analysis of the effect of these mutations on MRP mediated drug resistance and transport

Content Provider	Springer Nature Link
Author	Center, Melvin S. Zhu, Qichao Sun, Hongwei
Copyright Year	1998
Abstract	Studies were conducted to examine the functional role of the nucleotide-binding domains of MRP in drug resistance and drug transport in isolated membrane vesicles. In vivo studies were conducted by preparing stable transfectants of HeLa cells with wild-type MRP cDNA or MRP cDNAs which had been mutated at certain nucleotide binding domains (NBD). Stable transfectants producing equivalent amounts of the MRP encoded protein P190 were used in this study. The results demonstrated that deletions in the C-motif of NBD1 or the A-motif of NBD2 have a pronounced effect in reducing resistance levels to chemotherapeutic agents. Certain single-site mutations in lysines in these same motifs also reduce IC50 values. It has also been observed that mutation of the MRP NBDs results in an increase in drug accumulation and a reduction in drug efflux. Additional studies have been carried out in which recombinant baculovirus containing either wild-type MRP or MRP containing mutated NBDs was prepared and used to infect SF21 insect cells. Using this system we have analyzed the effects of these mutations on in vitro transport of leukotriene C4 (LTC4) 17 β-estradiol 17 (β-D-glucuronide)(E217βG) and daunomycin in membrane vesicles prepared from baculovirus infected cells. The results demonstrate that deletions and site-specific mutations in MRP NBDs greatly reduce the ATP dependent transport of all three substrates. The results of these studies conducted both in vivo and in vitro demonstrate that the NBDs of MRP function in a cooperative manner and are critical for the transport activity of the MRP encoded protein P190. These studies also identify specific lysines in NBD1 and NBD2 which are important for optimal MRP activity.
Starting Page	61
Ending Page	69
Page Count	9
File Format	PDF
ISSN	09209069
Journal	Cytotechnology
Volume Number	27
Issue Number	1-3
e-ISSN	15730778
Language	English
Publisher	Kluwer Academic Publishers
Publisher Date	1998-01-01
Publisher Place	Dordrecht
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Biomedicine general Biotechnology Biochemistry
Content Type	Text
Resource Type	Article
Subject	Cell Biology Clinical Biochemistry Bioengineering Biomedical Engineering Biotechnology

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Mutagenesis of the putative nucleotide-binding domains of the multidrug resistance associated protein (MRP). Analysis of the effect of these mutations on MRP mediated drug resistance and transport.

Mutagenesis of the putative nucleotide-binding domains of the multidrug resistance associated protein (MRP). Analysis of the effect of these mutations on MRP mediated drug resistance and transport

Membrane topology of the human multidrug resistance-associated protein (MRP) and its homologs

Membrane topology of the human multidrug resistance-associated protein (MRP) and its homologs.

Cytokine-mediated reversal of multidrug resistance

Protein kinases and multidrug resistance

Membrane topology of the human multidrug resistance-associated protein (MRP) and its homologs

Multidrug resistance mediated by the ATP‐binding cassette transporter protein MRP

Acceleration of mrp-associated efflux of rhodamine 123 by genistein and related compounds.

Mutagenesis of the putative nucleotide-binding domains of the multidrug resistance associated protein (MRP). Analysis of the effect of these mutations on MRP mediated drug resistance and transport

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Mutagenesis of the putative nucleotide-binding domains of the multidrug resistance associated protein (MRP). Analysis of the effect of these mutations on MRP mediated drug resistance and transport.

Mutagenesis of the putative nucleotide-binding domains of the multidrug resistance associated protein (MRP). Analysis of the effect of these mutations on MRP mediated drug resistance and transport

Membrane topology of the human multidrug resistance-associated protein (MRP) and its homologs

Membrane topology of the human multidrug resistance-associated protein (MRP) and its homologs.

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Mutagenesis of the putative nucleotide-binding domains of the multidrug resistance associated protein (MRP). Analysis of the effect of these mutations on MRP mediated drug resistance and transport