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Originally published In Press as doi:10.1074/jbc.M314006200 on February 14, 2004

J. Biol. Chem., Vol. 279, Issue 17, 17312-17318, April 23, 2004
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Arsenic Trioxide Uptake by Hexose Permeases in Saccharomyces cerevisiae*

Zijuan Liu{ddagger}, Eckhard Boles§, and Barry P. Rosen{ddagger}

From the {ddagger}Department of Biochemistry and Molecular Biology, Wayne State University, School of Medicine, Detroit, Michigan 48201 and §Institut für Mikrobiologie, Goethe-Universität, Frankfurt D-60439, Germany

Arsenic trioxide is a toxic metalloid and carcinogen that is also used as an anticancer drug, and for this reason it is important to identify the routes of arsenite uptake by cells. In this study the ability of hexose transporters to facilitate arsenic trioxide uptake in Saccharomyces cerevisiae was examined. In the absence of glucose, strains with disruption of the arsenite efflux gene ACR3 accumulated high levels of 73As(OH)3. The addition of glucose inhibited uptake by ~80%. Disruption of FPS1, the aquaglyceroporin gene, reduced glucose-independent uptake by only about 25%, and the residual uptake was nearly completely inhibited by hexoses, including glucose, galactose, mannose, and fructose but not pentoses or disaccharides. A strain lacking FPS1, ACR3, and all genes for hexose permeases except for HXT3, HXT6, HXT7, and GAL2 exhibited hexose-inhibitable 73As(OH)3 uptake, whereas a strain lacking all 18 hexose transport-related genes (HXT1 to HXT17 and GAL2), FPS1 and ACR3, exhibited <10% of wild type 73As(OH)3 transport. When HXT1, HXT3, HXT4, HXT5, HXT7, or HXT9 was individually expressed in that strain, hexose-inhibitable 73As(OH)3 uptake was restored. In addition, the transport of [14C]glucose was inhibited by As(OH)3. These results clearly demonstrate that hexose permeases catalyze the majority of the transport of the trivalent metalloid arsenic trioxide.

Received for publication, December 22, 2003 , and in revised form, February 13, 2004.

* This work was supported by National Institutes of Health Grants ES10344 and GM55425 and by a pilot project grant from the Wayne State University Environmental Health Sciences Center in Molecular and Cellular Toxicology with Human Applications. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

To whom correspondence should be addressed: Dept. of Biochemistry and Molecular Biology, Wayne State University, School of Medicine, 540 E. Canfield Ave., Detroit, MI 48201. Tel.: 313-577-0618; Fax: 313-577-2765; E-mail: brosen{at}med.wayne.edu.


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