Five amino acids in the innermost cavity of the substrate binding cleft of organic cation transporter 1 interact with extracellular and intracellular corticosterone.

@article{Volk2009FiveAA,
  title={Five amino acids in the innermost cavity of the substrate binding cleft of organic cation transporter 1 interact with extracellular and intracellular corticosterone.},
  author={Christopher Volk and Valentin Gorboulev and Alexander Kotzsch and Thomas D Mueller and Hermann Koepsell},
  journal={Molecular pharmacology},
  year={2009},
  volume={76 2},
  pages={275-89}
}
We have shown previously that Leu447 and Gln448 in the transmembrane helix (TMH) 10 of rat organic cation transporter rOCT1 are critical for inhibition of cation uptake by corticosterone. Here, we tested whether the affinity of corticosterone is different when applied from the extracellular or intracellular side. The affinity of corticosterone was determined by measuring the inhibition of currents induced by tetraethylammonium(+) (TEA(+)) in Xenopus laevis oocytes expressing rOCT1. Either… CONTINUE READING
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