Disease relevance of MRP

• Most of these proteins are known to, or can be inferred to participate in a transport process, such as in the case of the multidrug resistance protein (MDR), the STE6 gene product of yeast, and possibly the cystic fibrosis protein [1].

High impact information on MRP

• The N-terminal portion aligned with the HisP family of membrane-associated ATP-binding proteins, most of which are subunits of active transport complexes in bacteria, and to two regions of the multidrug resistance P-glycoprotein [2].
• This 19 exon insect gene, dMRP (FBgn0032456), spans slightly more than 22 kb [3].
• The gene contains two sets of transmembrane domains and two ATP-binding domains and shows a high degree of similarity to the mammalian P-glycoprotein/multidrug resistance (MDR) genes [4].
• Conservation in the position of intervening sequences between Mdr50 and the human MDR genes provides further evidence for their common origin [4].
• In situ expression of 2 multidrug resistance genes, mdr49 and mdr65, of Drosophila melanogaster was examined in wild-type third instar larval tissues under physiological conditions and after heat shock or colchicine feeding [5].

Biological context of MRP

• Data from mapping crosses of chromosome III support a role for a naturally occurring polymorphism in a multidrug resistance gene (Mdr65A) in alpha-amanitin resistance [6].

Anatomical context of MRP

• We now report that MDR in this cell line is partially reversed by the type I cAMP-dependent protein kinase (PKA) inhibitor, 8-Cl-cAMP [7].

Analytical, diagnostic and therapeutic context of MRP

• In situ hybridization and Northern analysis indicate that dMRP is expressed throughout development and appears to be head enriched in adults [8].

References