Drug export activity of the human canalicular multispecific organic anion transporter in polarized kidney MDCK cells expressing cMOAT (MRP2) cDNA.

@article{Evers1998DrugEA,
  title={Drug export activity of the human canalicular multispecific organic anion transporter in polarized kidney MDCK cells expressing cMOAT (MRP2) cDNA.},
  author={Raymond Evers and Mirjam Kool and Liesbeth Van Deemter and Hans W R M Janssen and Jero Calafat and Lauran C. J. M. Oomen and Coen C. Paulusma and Ronald P. J. Oude Elferink and Frank Baas and Alfred H Schinkel and Piet Borst},
  journal={The Journal of clinical investigation},
  year={1998},
  volume={101 7},
  pages={1310-9}
}
The canalicular (apical) membrane of the hepatocyte contains an ATP-dependent transport system for organic anions, known as the multispecific organic anion transporter (cMOAT). The deduced amino acid sequence of cMOAT is 49% identical to that of the human multidrug resistance- associated protein (MRP) MRP1, and cMOAT and MRP1 are members of the same sub-family of adenine nucleotide binding cassette transporters. In contrast to MRP1, cMOAT was predominantly found intracellularly in nonpolarized… CONTINUE READING
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