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A reevaluation of substrate specificity of the rat cation transporter rOCT1

G Nagel1, C Volk, T Friedrich

  • 1Max-Planck-Insitiut für Biophysik, Kennedy-Allee 70, D-60596 Frankfurt, Germany. anat010@rzbox.uni-wuerzburg.de

Insights

The rat cation transporter rOCT1 does not transport type 2 cations like quinine. Inward currents observed were due to inhibition of other cation transport, not direct transport by rOCT1.

Area of Science:

  • Molecular biology
  • Physiology
  • Biochemistry

Background:

  • The rat cation transporter rOCT1 (organic cation transporter 1) is expressed in the kidney, liver, and small intestine.
  • rOCT1 is the first identified member of a protein family that transports hydrophilic cations.
  • Previous studies suggested rOCT1 transported type 2 cations, such as quinine and quinidine.

Purpose of the Study:

  • To reevaluate the substrate specificity of the rat cation transporter rOCT1.
  • To determine if rOCT1 transports type 2 cations previously suggested by electrical measurements.

Main Methods:

  • Tracer flux measurements were performed using oocytes and stably transfected human embryonic kidney cells.
  • Electrical measurements, including voltage dependence, were analyzed.
  • Tracer efflux measurements were conducted.

Main Results:

  • Tracer flux assays demonstrated that [3H]quinine and [3H]quinidine are not transported by rOCT1.
  • Observed inward currents induced by type 2 cations in rOCT1-expressing oocytes were not due to direct transport.
  • These currents result from the inhibition of electrogenic efflux of transported type 1 cations.

Conclusions:

  • rOCT1 does not transport type 2 cations, including quinine and quinidine.
  • The previously observed electrical effects were indirect, caused by inhibition of other transporter activities.
  • The specific hepatic transporter responsible for type 2 cation transport remains unidentified.

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