Role of Rat Multidrug Resistance Protein 2 in Plasma and Biliary Disposition of Dibromosulfophthalein after Microsomal Enzyme Induction

2002 ◽  
Vol 180 (1) ◽  
pp. 56-63 ◽  
Author(s):  
David R. Johnson ◽  
Curtis D. Klaassen
Keyword(s):  
Multidrug Resistance ◽  
Enzyme Induction ◽  
Multidrug Resistance Protein ◽  
Microsomal Enzyme ◽  
Multidrug Resistance Protein 2 ◽  
Resistance Protein ◽  
Microsomal Enzyme Induction

scholarly journals Role of Glutathione in the Regulation of Cisplatin Resistance in Cancer Chemotherapy

2010 ◽  
Vol 2010 ◽  
pp. 1-7 ◽  
Author(s):  
Helen H. W. Chen ◽  
Macus Tien Kuo
Keyword(s):  
Multidrug Resistance ◽  
Mammalian Cells ◽  
Cisplatin Resistance ◽  
Multidrug Resistance Protein ◽  
Transfected Cells ◽  
High Affinity ◽  
Multidrug Resistance Protein 2 ◽  
Resistance Protein ◽  
Rate Limiting

Three mechanisms have been proposed for the role of glutathione (GSH) in regulating cisplatin (CDDP) sensitivities that affects its ultimate cell-killing ability: (i) GSH may serve as a cofactor in facilitating multidrug resistance protein 2- (MRP2-) mediated CDDP efflux in mammalian cells, since MRP2-transfected cells were shown to confer CDDP resistance; (ii) GSH may serve as a redox-regulating cytoprotector based on the observations that many CDDP-resistant cells overexpress GSH and γ-glutamylcysteine synthesis (γ-GCS), the rate-limiting enzyme for GSH biosynthesis; (iii) GSH may function as a copper (Cu) chelator. Elevated GSH expression depletes the cellular bioavailable Cu pool, resulting in upregulation of the high-affinity Cu transporter (hCtr1) which is also a CDDP transporter. This has been demonstrated that overexpression of GSH by transfection with γ-GCS conferred sensitization to CDDP toxicity. This review describes how these three models were developed and critically reviews their importance to overall CDDP cytotoxicity in cancer cell treatments.

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