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  A Reevaluation of Substrate Specificity of the Rat Cation Transporter rOCT1

Nagel, G., Volk, C., Friedrich, T., Ulzheimer, J. C., Bamberg, E., & Koepsell, H. (1997). A Reevaluation of Substrate Specificity of the Rat Cation Transporter rOCT1. The Journal of Biological Chemistry, 272(51), 31953-31956. doi:10.1074/jbc.272.51.31953.

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 Creators:
Nagel, Georg1, 2, Author           
Volk, Christopher3, Author
Friedrich, Thomas1, Author           
Ulzheimer, Jochen C. 3, Author
Bamberg, Ernst1, 2, Author           
Koepsell, Hermann 3, Author
Affiliations:
1Department of Biophysical Chemistry, Max Planck Institute of Biophysics, Max Planck Society, ou_2068289              
2Johann-Wolfgang-Goethe-Universität, Biozentrum, FB 15, 60439 Frankfurt am Main, Germany, ou_persistent22              
3Anatomisches Institut der Bayerischen Julius-Maximilians-Universität, 97070 Würzburg, Germany, ou_persistent22              

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 Abstract: The substrate specificity of the previously cloned rat cation transporter rOCT1, which is expressed in kidney, liver, and small intestine, was reevaluated. rOCT1 is the first member of a new protein family comprising electrogenic and polyspecific cation transporters that transport hydrophilic cations like tetraethylammonium, choline, and monoamine neurotransmitters. Previous electrical measurements suggested that cations like quinine, quinidine, and cyanine 863, which have been classified as type 2 cations in the liver, are also transported by rOCT1, since they may induce inward currents in rOCT1 expressingXenopus oocytes (Busch, A. E., Quester, S., Ulzheimer, J. C., Waldegger, S., Gorboulev, V., Arndt, P., Lang, F., and Koepsell, H. (1996) J. Biol. Chem. 271, 32599–32604). Tracer flux measurements with oocytes and with stably transfected human embryonic kidney cells showed that [3H]quinine and [3H]quinidine are not transported by rOCT1. The voltage dependence observed for the quinine- or quinidine-induced inward currents in rOCT1-expressing oocytes, and tracer efflux measurements indicate that the inward currents by type 2 cations are generated by the inhibition of electrogenic efflux of transported type 1 cations. Therefore, rOCT1 cannot contribute to transport of type 2 cations in the liver and the hepatic transporter for type 2 cations remains to be identified.

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Language(s): eng - English
 Dates: 1997-10-311997-09-221997-12-011997-12-19
 Publication Status: Issued
 Pages: 5
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1074/jbc.272.51.31953
PMID: 9405386
 Degree: -

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Title: The Journal of Biological Chemistry
  Other : JBC
Source Genre: Journal
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Publ. Info: Baltimore, etc. : American Society for Biochemistry and Molecular Biology [etc.]
Pages: - Volume / Issue: 272 (51) Sequence Number: - Start / End Page: 31953 - 31956 Identifier: ISSN: 0021-9258
CoNE: https://pure.mpg.de/cone/journals/resource/954925410826_1