Alteration of thioredoxin reductase 1 levels in elucidating cancer etiology.

Abstract

Thioredoxin reductase 1 (TR1) is a major antioxidant and redox regulator in mammalian cells and appears to function as a double-edged sword in that it has roles in preventing and promoting/sustaining cancer. TR1 is overexpressed in many cancer cells and targeting its removal often leads to a reversal in numerous malignant characteristics which has marked this selenoenzyme as a prime target for cancer therapy. Since alterations in TR1 activity may lead to a better understanding of the etiology of cancer and new avenues for providing better therapeutic procedures, we have described herein techniques for removing and reexpressing TR1 employing RNAi technology and for assessing the catalytic activity of this enzyme.

• Authors: Min-Hyuk Yoo, Bradley A Carlson, Petra Tsuji, Robert Irons, Vadim N Gladyshev, Dolph L Hatfield
• Journal: Methods in enzymology (Methods Enzymol) Vol. 474 Pg. 255-75 ( 2010) ISSN: 1557-7988 [Electronic] United States
• PMID: 20609915 (Publication Type: Journal Article, Research Support, N.I.H., Extramural, Research Support, N.I.H., Intramural)
• Copyright: Copyright (c) 2010 Elsevier Inc. All rights reserved.

Chemical References

• Thioredoxin-Disulfide Reductase

Topics

• Animals
• Blotting, Northern
• Blotting, Western
• Cell Line, Tumor
• Gene Knockdown Techniques
• Humans
• Mice
• Neoplasms (enzymology, etiology, genetics)
• Thioredoxin-Disulfide Reductase (analysis, genetics, metabolism)