Cellular thioredoxin reductase activity is regulated by selenium.

M Berggren; A Gallegos; J Gasdaska; G Powis

PubMed · 9413175

Cellular thioredoxin reductase activity is regulated by selenium.

M Berggren·A Gallegos·J Gasdaska·G Powis

Abstract

Selenium (Se) is an essential trace element and has been reported to decrease the incidence of some human cancers. We have investigated the effects of Se on thioredoxin reductase, a selenocysteine containing flavoenzyme, in HT-29 human colon cancer cells grown in serum-free medium. Sodium selenite and other Se containing compounds produced a time and concentration dependent increase in intracellular thioredoxin reductase activity and protein levels. Selenite was the most active of the Se compounds examined: 1 microM selenite produced a 28-fold increase in thioredoxin reductase activity by 1 day and 10 microM selenite over a 60-fold increase by 5 days. The activity of a related non-selenocysteine containing flavoenzyme glutathione reductase was not increased by selenite. Selenite, but not the other Se containing compounds inhibited cell growth at concentrations above 2 microM. The results show that Se can produce large increases in cell thioredoxin reductase activity.

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Blotting, Western Cell Division Colonic Neoplasms Cysteine Humans Organoselenium Compounds Selenium Selenocysteine Selenomethionine Thioredoxin-Disulfide Reductase Tumor Cells, Cultured Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

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M Berggren, A Gallegos, J Gasdaska, G Powis. Cellular thioredoxin reductase activity is regulated by selenium.. https://pubmed.ncbi.nlm.nih.gov/9413175/

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