Involvements of mitochondrial thioredoxin reductase (TrxR2) in cell proliferation

Mammalian cells contain two forms of thioredoxin reductase (TrxR), cytosolic TrxR1 and mitochondrial TrxR2. To investigate the biological roles of TrxR2, we generated stable HeLa cell lines expressing a dominant negative form of TrxR2 (TrxR2DN) under the control of the tetracycline-off system. We ob...

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Bibliographic Details
Published in:Biochemical and biophysical research communications 2003-04, Vol.304 (1), p.119-124
Main Authors: Kim, Mi-Ra, Chang, Ho-Sung, Kim, Byung-Hak, Kim, Seongyong, Baek, Suk-Hwan, Hye Kim, Jung, Lee, Seung-Rock, Kim, Jae-Ryong
Format: Article
Language:English
Subjects:
Cell Cycle
Cell Division
Epidermal Growth Factor - pharmacology
Gene Expression Regulation
HeLa Cells
Humans
Hydrogen peroxide
Hydrogen Peroxide - analysis
Mitochondria - enzymology
Mitochondrial thioredoxin reductase
Mutation
Phosphoproteins - chemistry
Phosphoproteins - metabolism
Phosphorylation
Proliferation
Signal transduction
Tetracycline - pharmacology
Thioredoxin Reductase 2
Thioredoxin-Disulfide Reductase - genetics
Thioredoxin-Disulfide Reductase - physiology
Tyrosine - metabolism
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Summary:Mammalian cells contain two forms of thioredoxin reductase (TrxR), cytosolic TrxR1 and mitochondrial TrxR2. To investigate the biological roles of TrxR2, we generated stable HeLa cell lines expressing a dominant negative form of TrxR2 (TrxR2DN) under the control of the tetracycline-off system. We observed that TrxR2DN-induced cells, following stimulation with EGF, produced more hydrogen peroxide than uninduced cells. The extent of protein tyrosine phosphorylation of many proteins including ERK was higher in TrxR2DN-induced cells than in uninduced cells when stimulated with fetal bovine serum or EGF. Induction of TrxR2DN also resulted in the increased rate of progression of G 1 to S phase in cell cycle and cell proliferation and affected the expression of many proteins involved in cell cycle. These results suggest that TrxR2 participates in the regulation of protein tyrosine phosphorylation and cell growth as a component of the mitochondria specific H 2O 2-eliminating system that includes peroxiredoxin III and thioredoxin 2.
ISSN:0006-291X
1090-2104
DOI:10.1016/S0006-291X(03)00547-3