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Am J Physiol Renal Physiol (February 19, 2002). doi:10.1152/ajprenal.00274.2001
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Articles in PresS, published online ahead of print February 19, 2002
Am J Physiol Renal Physiol, 10.1152/ajprenal.00274.2001
Submitted on September 4, 2001
Accepted on February 12, 2002

Electrophysiological analysis of the substrate specificity of human and rat purine-selective nucleoside transporters

Karin M Gerstin1, Mark J Dresser1, and Kathleen M Giacomini1*

1 Department of Biopharmaceutical Sciences, UCSF, San Francisco, CA, USA

* To whom correspondence should be addressed. E-mail: karing{at}itsa.ucsf.edu.

To understand the roles that nucleoside transporters play in the in vivo distribution of clinically important nucleoside analogs, the substrate specificity of each transporter isoform should be determined. In the present work, we studied the substrate specificities of the human and rat orthologs of the purine-selective, Na+-dependent nucleoside transporter, SPNT (CNT2), for nucleosides, nucleobases, and base- and ribose-modified nucleoside analogs. The two-electrode voltage clamp technique in Xenopus laevis oocytes expressing these transporters was used. Purine nucleosides and uridine induced currents in oocytes expressing rSPNT or hSPNT1. The rank order of magnitude of nucleoside-induced currents was guanosine > uridine > adenosine > inosine and guanosine > uridine > inosine > adenosine for rSPNT- and hSPNT1-expressing oocytes, respectively. Uridine analogs (modified at the 5-position of the base) induced little or no current suggesting that these compounds are only poorly transported by either transporter. Cladribine (2-chloro-2'-deoxyadenosine) induced currents in oocytes expressing rSPNT (K0.5 = 57 ±12 µM) but not hSPNT1. The ribose-modified nucleoside analogs, adenine arabinoside and 2',3'-dideoxyadenosine induced currents in rSPNT- but not hSPNT1-expressing oocytes. These data suggest that there are notable species differences in the specificity of SPNT for synthetic nucleoside analogs.




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