title: Thioredoxin and thioredoxin reductase: current research with special reference to human disease.
abstract: 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.
authors.affiliation: Division of Biochemistry, Department of Medical Biochemistry and Biophysics, Karolinska Institutet, SE17177 Stockholm, Sweden. arne.holmgren@ki.se
authors.forename: Arne
authors.initials: A
authors.lastname: Holmgren
authors.forename: Jun
authors.initials: J
authors.lastname: Lu
mesh_terms: D000375:Aging / Q000378:metabolism; D001172:Arthritis, Rheumatoid / Q000378:metabolism; D002318:Cardiovascular Diseases / Q000378:metabolism; D003920:Diabetes Mellitus / Q000378:metabolism; D006801:Humans; D009369:Neoplasms / Q000378:metabolism; D019636:Neurodegenerative Diseases / Q000378:metabolism; D013880:Thioredoxin-Disulfide Reductase / Q000378:metabolism*; D013879:Thioredoxins / Q000378:metabolism*
chemical_list: D013879:Thioredoxins; D013880:Thioredoxin-Disulfide Reductase