Abstract
Publisher Summary This chapter describes the multidrug resistance protein (MRP1) that has been cloned and sequenced from multidrug-resistant human lung cancer cells and identified as an integral membrane glycoprotein belonging to the superfamily of adenosine triphosphate-binding cassette (ABC) transporters. Primary active unidirectional adenosine triphosphate (ATP)-dependent transport of amphiphilic anions—in particular, of conjugates of lipophilic substances with glutathione, glucuronate, or sulfate, are the recognized functions of MRP1. An isoform of MRP1 with a related sequence and a similar function has been cloned from human and rat and localized predominantly to the hepatocyte canalicular membrane. This isoform is termed “MRP2” or “canalicular MRP” (cMRP) or “canalicular multispecific organic anion transporter” (cMOAT). Canalicular (apical) MRP is deficient in human Dubin–Johnson syndrome and in two mutant rat strains lacking the ATP-dependent transport of anionic conjugates across the hepatocyte canalicular membrane.
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