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1 Institute of Anatomy and Cell Biology, University of Wuerzburg, Wuerzburg, Bavaria, Germany
* To whom correspondence should be addressed. E-mail: hermann{at}koepsell.de.
The product of gene RSC1A1, named RS1, participates in transcriptional and posttranscriptional regulation of sodium-D-glucose cotransporter SGLT1. Using co-expression in oocytes of Xenopus laevis, posttranscriptional inhibition of human SGLT1 (hSGLT1) and some other transporters by human RS1 (hRS1) was demonstrated previously. In the present study histidine tagged hRS1 was expressed in oocytes or Sf9 cells and purified using nickel(II)-charged nitrilotriacetic acid-agarose. hRS1 protein was injected into oocytes expressing hSGLT1 or the human organic cation transporter hOCT2, and the effect on hSGLT1 mediated uptake of methyl-
-D-[14C]glucopyranoside (AMG) or hOCT2 mediated uptake of [14C]tetraethylammonium (TEA) was measured. Within 30 min after the injection of hRS1 protein, hSGLT1 expressed AMG uptake or OCT2 expressed TEA uptake was inhibited by about 50%. Inhibition of AMG uptake was decreased when a dominant negative mutant of dynamin I was co-expressed and increased after stimulation of PKC. Inhibition remained unaltered when endocytosis was inhibited by chlorpromazine, imipramine or filipin but was prevented when exocytosis was inhibited by botulinum toxin B or when the release of vesicles from the TGN and endosomes was inhibited by brefeldin A. Inhibition of hSGLT1 mediated AMG uptake and hOCT2 mediated TEA uptake by hRS1 protein were decreased at enhanced intracellular AMG concentration. The data suggest that hRS1 protein exhibits glucose dependent short term inhibition of hSGLT1 and hOCT2 by inhibiting the release of vesicles from the TGN.
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