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

Zijuan Liu, Marco A. Sanchez, Xuan Jiang, Eckhard Boles, Scott M. Landfear, Barry P. Rosen

Research output: Contribution to journalArticlepeer-review

115 Scopus citations


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 CH3As(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 CH3As(OH)2. The Km of GLUT1 is to 1.2 mM for CH3As(OH)2, compared to a Km of 3 mM for glucose. Inhibition between glucose and CH3As(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 CH3As(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.

Original languageEnglish (US)
Pages (from-to)424-430
Number of pages7
JournalBiochemical and Biophysical Research Communications
Issue number2
StatePublished - Dec 15 2006


  • Arsenic trioxide
  • Arsenite
  • GLUT1
  • Glucose permease
  • Methylarsenous acid

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


Dive into the research topics of 'Mammalian glucose permease GLUT1 facilitates transport of arsenic trioxide and methylarsonous acid'. Together they form a unique fingerprint.

Cite this