Abstract:
: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 H(2)O(2) 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 H(2)O(2) damage. Transfection of mouse WEHI7.2 lymphoma cells with human TrxP-1 or TrxP-2, but not TrxP-4, protects the cells against H(2)O(2) 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 H(2)O(2) induced apoptosis caused by Trx-1, but does not protect against apoptosis induced by other agents.
journal_name
Arch Biochem Biophysjournal_title
Archives of biochemistry and biophysicsauthors
Berggren MI,Husbeck B,Samulitis B,Baker AF,Gallegos A,Powis Gdoi
10.1006/abbi.2001.2435subject
Has Abstractpub_date
2001-08-01 00:00:00pages
103-9issue
1eissn
0003-9861issn
1096-0384pii
S0003-9861(01)92435-Xjournal_volume
392pub_type
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journal_title:Archives of biochemistry and biophysics
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