High affinity selenium uptake in a keratinocyte model
Abbreviated Journal Title
selenium; anion transport; selenite; selenide; keratinocyte; SELENOPROTEIN-P; SACCHAROMYCES-CEREVISIAE; THIOREDOXIN REDUCTASE; SELENOTRISULFIDE; SELENOMETHIONINE; TRANSPORT; TOXICITY; SELENATE; BINDING; SYSTEM; Biochemistry & Molecular Biology; Biophysics; Cell Biology
The distribution of selenium in mammals has been recently shown to be mediated primarily by selenoprotein P. Even in the absence of selenoprotein P, selenium is distributed from the liver into all organs and tissues when supplemented in the diet. The form of selenium that is actively taken up by mammalian cells at trace concentrations has yet to be determined. We used a human keratinocyte model to determine whether reduction of the oxyanion selenite (SeO(3)(2-)) to the more reduced form of selenide (HSe(-)) would affect uptake. Indeed a reduced form of selenium, presumably selenide, was actively transported into keratinocytes and displayed saturation kinetics with an apparent K(m) of 279 nM. ATPase inhibitors blocked the uptake of selenide, as did the competing anions molybdate and chromate, but not sulfate. These results suggest that the small molecule form of selenium that is distributed in tissues is hydrogen selenide, despite its sensitivity to oxygen and reactivity to thiols. (C) 2007 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
"High affinity selenium uptake in a keratinocyte model" (2008). Faculty Bibliography 2000s. 347.