Structural, mechanistic and clinical aspects of MRP1

被引:339
作者
Hipfner, DR [1 ]
Deeley, RG [1 ]
Cole, SPC [1 ]
机构
[1] Queens Univ, Canc Res Labs, Kingston, ON K7L 3N6, Canada
来源
BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES | 1999年 / 1461卷 / 02期
基金
英国医学研究理事会;
关键词
multidrug resistance; organic anion transport; ATP-binding cassette transporter; glutathione; topology; epitope mapping;
D O I
10.1016/S0005-2736(99)00168-6
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The cDNA encoding ATP-binding cassette (ABC) multidrug resistance protein MRP1 was originally cloned from a drug-selected lung cancer cell line resistant to multiple natural product chemotherapeutic agents. MRP1 is the founder of a branch of the ABC superfamily whose members (from species as diverse as plants and yeast to mammals) share several distinguishing structural features that may contribute to functional and mechanistic similarities among this subgroup of transport proteins. In addition to its role in resistance to natural product drugs, MRP1 land related proteins) functions as a primary active transporter of structurally diverse organic anions, many of which are formed by the biotransformation of various endo- and xenobiotics by Phase II conjugating enzymes, such as the glutathione S-transferases. MRP1 is involved in a number of glutathione-related cellular processes. Glutathione also appears to play a key role in MRP1-mediated drug resistance. This article reviews the discovery of MRP1 and its relationships with other ABC superfamily members, and summarizes current knowledge of the structure, transport functions and relevance of this protein to in vitro and clinical multidrug resistance. (C) 1999 Elsevier Science B.V. All rights reserved.
引用
收藏
页码:359 / 376
页数:18
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