Thioredoxin peroxidase-1 (peroxiredoxin-1) is increased in thioredoxin-1 transfected cells and results in enhanced protection against apoptosis caused by hydrogen …

MI Berggren, B Husbeck, B Samulitis, AF Baker… - Archives of Biochemistry …, 2001 - Elsevier
MI Berggren, B Husbeck, B Samulitis, AF Baker, A Gallegos, G Powis
Archives of Biochemistry and Biophysics, 2001Elsevier
Thioredoxin-1 (Trx-1) is a small redox oncoprotein whose expression is increased in a
number of human primary cancers where it is associated with aggressive tumor growth,
inhibition of apoptosis and decreased patient survival. We report that Trx-1-transfected MCF-
7 human breast cancer cells have increased expression of thioredoxin peroxidase-1 (TrxP-
1) a peroxiredoxin family member that scavenges H2O2 using Trx-1 as a source of reducing
equivalents. Our work shows that TrxP-1 is more effective than selenium-dependent …
Thioredoxin-1 (Trx-1) is a small redox oncoprotein whose expression is increased in a number of human primary cancers where it is associated with aggressive tumor growth, inhibition of apoptosis and decreased patient survival. We report that Trx-1-transfected MCF-7 human breast cancer cells have increased expression of thioredoxin peroxidase-1 (TrxP-1) a peroxiredoxin family member that scavenges H2O2 using Trx-1 as a source of reducing equivalents. Our work shows that TrxP-1 is more effective than selenium-dependent glutathione peroxidase in protecting cells against H2O2 damage. Transfection of mouse WEHI7.2 lymphoma cells with human TrxP-1 or TrxP-2, but not TrxP-4, protects the cells against H2O2 induced apoptosis but does not protect against apoptosis induced by dexamethasone, etoposide, or doxorubicin. The results show that an increase in TrxP-1 expression contributes to the protection against H2O2 induced apoptosis caused by Trx-1, but does not protect against apoptosis induced by other agents.
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