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Mammalian glucose permease GLUT1 facilitates transport of arsenic trioxide and methylarsonous acid.

Authors: Liu, Z  Sanchez, MA  Jiang, X  Boles, E  Landfear, SM  Rosen, BP 
Citation: Liu Z, etal., Biochem Biophys Res Commun. 2006 Dec 15;351(2):424-30. Epub 2006 Oct 17.
Pubmed: (View Article at PubMed) PMID:17064664
DOI: Full-text: DOI:10.1016/j.bbrc.2006.10.054

Arsenic exposure is associated with hypertension, diabetes, and cancer. Some mammals methylate arsenic. Saccharomyces cerevisiae hexose permeases catalyze As(OH)(3) uptake. Here, we report that mammalian glucose transporter GLUT1 catalyzes As(OH)(3) and CH(3)As(OH)(2) uptake in yeast or in Xenopus laevis oocytes. Expression of GLUT1 in a yeast lacking other glucose transporters allows for growth on glucose. Yeast expressing yeast HXT1 or rat GLUT1 transport As(OH)(3) and CH(3)As(OH)(2). The K(m) of GLUT1 is to 1.2mM for CH(3)As(OH)(2), compared to a K(m) of 3mM for glucose. Inhibition between glucose and CH(3)As(OH)(2) is noncompetitive, suggesting differences between the translocation pathways of hexoses and arsenicals. Both human and rat GLUT1 catalyze uptake of both As(OH)(3) and CH(3)As(OH)(2) in oocytes. Thus GLUT1 may be a major pathway uptake of both inorganic and methylated arsenicals in erythrocytes or the epithelial cells of the blood-brain barrier, contributing to arsenic-related cardiovascular problems and neurotoxicity.


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RGD Object Information
RGD ID: 1624248
Created: 2007-05-07
Species: All species
Last Modified: 2007-05-07
Status: ACTIVE


RGD is funded by grant HL64541 from the National Heart, Lung, and Blood Institute on behalf of the NIH.