Title

High affinity selenium uptake in a keratinocyte model

Authors

Authors

D. Ganyc;W. T. Self

Comments

Authors: contact us about adding a copy of your work at STARS@ucf.edu

Abbreviated Journal Title

FEBS Lett.

Keywords

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

Abstract

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.

Journal Title

Febs Letters

Volume

582

Issue/Number

2

Publication Date

1-1-2008

Document Type

Article

Language

English

First Page

299

Last Page

304

WOS Identifier

WOS:000257271700026

ISSN

0014-5793

Share

COinS