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Chemical forms of selenium affect glutathione peroxidase activity in human Caco‐2 cell model
Author(s) -
Zeng Huawei,
Botnen James H.
Publication year - 2007
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.21.5.a105-c
Subject(s) - selenium , bioavailability , gpx1 , glutathione peroxidase , selenocysteine , chemistry , caco 2 , peroxidase , in vitro , biochemistry , glutathione , bioassay , in vivo , cell culture , enzyme , biology , pharmacology , organic chemistry , cysteine , genetics
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 selenomeththionine 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.