Antioxidant function of thioredoxin and glutaredoxin systems

Antioxidants and Redox Signaling

Volumn 2, Issue 4, 2000, Pages 811-820

  Holmgren, A ^a  

^a KAROLINSKA INSTITUTE   (Sweden)

Author keywords

[No Author keywords available]

Indexed keywords

ANTIOXIDANT; CYSTEINE; DEOXYRIBONUCLEOTIDE; EBSELEN; GLUTAREDOXIN DERIVATIVE; GLUTATHIONE PEROXIDASE; GLYCINE; HYDROGEN PEROXIDE; MUTANT PROTEIN; QUERCETIN; RIBONUCLEOTIDE REDUCTASE; SELENIUM; SELENOCYSTEINE; THIOREDOXIN; THIOREDOXIN REDUCTASE; TRACE ELEMENT; TRANSCRIPTION FACTOR; UNCLASSIFIED DRUG;

AMINO ACID SUBSTITUTION; ANTIOXIDANT ACTIVITY; CARBOXY TERMINAL SEQUENCE; CATALYSIS; CELL PROLIFERATION; CYTOSOL; ENZYME ACTIVE SITE; ENZYME SUBSTRATE; ESCHERICHIA COLI; GENE EXPRESSION; HUMAN; MAMMAL; NONHUMAN; OXIDATION REDUCTION REACTION; OXIDATIVE STRESS; PRIORITY JOURNAL; REVIEW; SELENIUM DEFICIENCY; SEQUENCE ANALYSIS; SIGNAL TRANSDUCTION; SITE DIRECTED MUTAGENESIS; STOP CODON;

EID: 0034534165     PISSN: 15230864     EISSN: None     Source Type: Journal    
DOI: 10.1089/ars.2000.2.4-811     Document Type: Review

References (58)

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3. The mechanism of thioredoxin reductase from human placenta is similar to the mechanisms of lipoamide dehydrogenase and glutathione reductase and is distinct from the mechanism of thioredoxin reductase from Escherichia coli
4. Regulation of PTP1B via glutathionylation of the active site cysteine 215
5. Cellular thioredoxin reductase activity is regulated by selenium
6. Selenodiglutathione is a highly efficient oxidant of reduced thioredoxin and a substrate for mammalian thioredoxin reductase
7. The thioredoxin and glutaredoxin systems are efficient electron donors to human plasma glutathione peroxidase
8. Human thioredoxin reductase directly reduces lipid hydroperoxides by NADPH and selenocystine strongly stimulates the reaction via catalytically generated selenols
9. Selenium and the thioredoxin and glutaredoxin systems
10. Selenocysteine: The 21st amino acid
11. Isoforms of mammalian peroxiredoxin that reduce peroxides in presence of thioredoxin
12. Identification of an abundant S-thiolated rat liver protein as carbonic anhydrase III; characterization of S-thiolation and dethiolation reactions
13. Isolation and characterization of calf liver thioredoxin
14. The protein disulphide-isomerase family: Unravelling a string of folds
15. Functional expression of rat thioredoxin reductase: Selenocysteine insertion sequence element is essential for the active enzyme
16. Mechanisms of the regulation of thioredoxin reductase activity in cancer cells by the chemopreventive agent selenium
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18. Cloning and sequencing of a human thioredoxin reductase
19. Selenocysteine, identified as the penultimate C-terminal residue in human T-cell thioredoxin reductase, corresponds to TGA in the human placental gene
20. Human placenta thioredoxin reductase: Isolation of the selenoenzyme, steady state kinetics, and inhibition by therapeutic gold compounds
21. Thioredoxin reductase activity is decreased by selenium deficiency
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23. Reduction of disulfides by thioredoxin. Exceptional reactivity of insulin and suggested functions of thioredoxin in mechanism of hormone action
24. Thioredoxin catalyzes the reduction of insulin disulfides by dithiothreitol and dihydrolipoamide
25. Thioredoxin
26. Thioredoxin and glutaredoxin systems
27. Glutaredoxin
28. Thioredoxin and thioredoxin reductase
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32. Selenite is a substrate for calf thymus thioredoxin reductase and thioredoxin and elicits a large non-stoichiometric oxidation of NADPH in the presence of oxygen
33. Reversible inactivation of protein-tyrosine phosphatase 1B in A431 cells stimulated with epidermal growth factor
34. Molecular cloning and characterization of a mitochondrial selenocysteine-containing thioredoxin reductase from rat liver
35. Knowing when not to stop: Selenocysteine incorporation in eukaryotes
36. Protein disulfide-isomerase is a substrate for thioredoxin reductase and has thioredoxin-like activity
37. Two resident ER proteins CaBP1 and CaBP2 with thioredoxin domains, are substrates for thioredoxin reductase. Comparison with protein disulfide isomerase
38. Rat liver thioredoxin and thioredoxin reductase: Purification and characterization
39. Thioredoxin - A fold for all reasons
40. Human mitochondrial thioredoxin reductase cDNA cloning, expression and genomic organization
41. Redox regulation of cardiac muscle calcium signaling
42. Methionine sulfoxide reductase in antioxidant defense
43. S-nitrosoglutathione is cleaved by the thioredoxin system with liberation of glutathione and redox regulating nitric oxide
44. Mammalian thioredoxin reductase is irreversibly inhibited by dinitrohalobenzenes by alkylation of both the redox active selenocysteine and its neighboring cysteine residue
45. Ebselen in acute middle cerebral artery occlusion: A placebo-controlled, double-blind clinical trial
46. Mutagenesis of structural half-cystine residues in human thioredoxin and effects on the regulation of activity by selenodiglutathione
47. Purification of mitochondrial thioredoxin reductase and its involvement in the redox regulation of membrane permeability
48. Prominent expression of the selenoprotein thioredoxin reductase in the medullary rays of the rat kidney and thioredoxin reductase mRNA variants differing at the 5′ untranslated region
49. Active oxygen generation as a possible mechanism of selenium toxicity
50. Ebselen
51. Redox regulation of cell signaling by selenocysteine in mammalian thioredoxin reductases
52. A new selenoprotein from human lung adenocarcinoma cells: Purification, properties, and thioredoxin reductase activity
53. Crystal structures of reduced, oxidized and mutated human thioredoxins: Evidence for a regulatory homodimer
54. Unscheduled DNA synthesis and chromosome aberrations induced by inorganic and organic selenium compounds in the presence of glutathione
55. Essential role of selenium in the catalytic activities of mammalian thioredoxin reductase revealed by characterization of recombinant enzymes with selenocysteine mutations
56. Rat and calf thioredoxin reductases are homologous to glutathione reductase with a carboxyterminal elongation containing a conserved catalytically active penultimate selenocysteine residue
57. Structure and mechanism of mammalian thioredoxin reductase: The active site is a redox-active selenolthiol/selenenylsulfide formed from the conserved cysteine-selenocysteine sequence