ARS | Publication request: Chemical forms of selenium affect glutatione peroxidase activity in human Caco-2 cell model

Submitted to: Journal of Federation of American Societies for Experimental Biology
Publication Type: Abstract Only
Publication Acceptance Date: November 7, 2006
Publication Date: April 1, 2007
Repository URL: http://www.fasebj.org
Citation: Zeng, H., Botnen, J.H. 2007. Chemical forms of selenium affect glutatione peroxidase activity in human Caco-2 cell model [abstract]. Journal of Federation of American Societies for Experimental Biology. 21(5):A105.

Technical Abstract: The bioavailability of selenium (Se) is complicated because there are multiple naturally occurring chemical forms of this element in nature. Assessing the ability of a Se source to restore GPX1 activity in laboratory animals and humans is the most commonly used method. To search for an alternative (in vitro) bioassay method in addition to current in vivo models, we established a unique serum-free Caco-2 cell culture system, in which Se was seriously depleted. After 6 days of serum-free cell culture, the endogenous glutathione peroxidase (GPX1) activity in Caco-2 was extremely low. We then added various Se chemical forms with 15.6, 31.3, 62.5, or 125 nM concentrations for 8, 24, 48, or 72 hours. Our data suggest that selenite and se-(methyl)selenocysteine have stronger potential to restore GPX1 activity compared with that of selenomethionine at nmol/L levels in Caco-2 cells. Thus, this Caco-2 cell culture system may be useful in evaluating biological potential of different Se chemical forms.