Thioredoxin and thioredoxin reductase: current research with special reference to human disease

A Holmgren, J Lu - Biochemical and biophysical research communications, 2010 - Elsevier
Biochemical and biophysical research communications, 2010Elsevier
Thioredoxin (Trx) and thioredoxin reductase (TrxR) plus NADPH, comprising the thioredoxin
system, has a large number of functions in DNA synthesis, defense against oxidative stress
and apoptosis or redox signaling with reference to many diseases. All three isoenzymes of
mammalian TrxR contain an essential selenocysteine residue, which is the target of several
drugs in cancer treatment or mercury intoxication. The cytosolic Trx1 acting as the cells'
protein disulfide reductase is itself reversibly redox regulated via three structural Cys …
Thioredoxin (Trx) and thioredoxin reductase (TrxR) plus NADPH, comprising the thioredoxin system, has a large number of functions in DNA synthesis, defense against oxidative stress and apoptosis or redox signaling with reference to many diseases. All three isoenzymes of mammalian TrxR contain an essential selenocysteine residue, which is the target of several drugs in cancer treatment or mercury intoxication. The cytosolic Trx1 acting as the cells’ protein disulfide reductase is itself reversibly redox regulated via three structural Cys residues. The evolution of mammalian Trx system compared to its prokaryotic counterparts may be an adaptation to the use of hydrogen peroxide and nitric oxide in redox regulation and signal transduction.
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