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Thioredoxin reductase 1: Role in oxidative stress within cancer cells
Author(s) -
Yoo Min-Hyuk,
Carlson Bradley A,
Tsuji Petra A,
Gladyshev Vadim N,
Hatfield Dolph L
Publication year - 2012
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.26.1_supplement.253.2
Subject(s) - thioredoxin , thioredoxin reductase , oxidative stress , cancer cell , cancer , intracellular , chemistry , glutathione reductase , oxidative phosphorylation , microbiology and biotechnology , biochemistry , cancer research , biology , glutathione peroxidase , superoxide dismutase , genetics
Many selenoproteins (SPs) have roles in intracellular redox regulation due to the presence of selenocysteine at its catalytic core; e.g., thioredoxin reductase 1 (TR1) is a major antioxidant enzyme in mammals that functions in regulating thioredoxin redox status. This oxidoreductase is enriched in many malignant cells and has been proposed as a target for cancer therapy. We previously assessed the role of TR1 in the malignant process by knocking down its expression in cancer cells resulting in reversing of many of the malignant phenotypes. Cancer cells are proposed to have a more efficient anti‐oxidative system than normal cells and thioredoxin and glutathione comprise two of the major enzymatic, anti‐oxidative systems in mammals. To further elucidate TR1's role in anti‐oxidative systems in cancer cells, we targeted the removal of TR1 and Trx1 expression in NIH3T3 and DT cells (DT cells were derived from NIH 3T3 cells by over‐expressing oncogenic k‐ras). Our data have provided new insights into the expanded role of TR1 in cancer cells and the interrelationships between anti‐oxidative systems which will be presented. This research was supported by the Intramural Research Program of the NIH, NCI, CCR.