Inhibitors | Comment | Organism | Structure |
---|---|---|---|
additional information | hypoxanthine/xanthine oxidase system and H2O2 in rheumatoid arthritis cells decrease thioredoxin reductase activity, which is found to be unchanged in osteoarthritis cells. H2O2 and superoxide anion cause a time-dependent accumulation of oxidized thioredoxin reductase and induces the formation of carbonyl groups in thioredoxin reductase protein in rheumatoid arthritis cells rather than osteoarthritis cells, and oxidizes the selenocysteine of the active site. The oxidation in thioredoxin reductase protein is irreversible in rheumatoid arthritis cells but not in osteoarthritis cells | Homo sapiens |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | - |
- |
- |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
synoviocyte | thioredoxin reductase activity in rheumatoid arthritis cells is significantly higher than in osteoarthritis cells | Homo sapiens | - |
Synonyms | Comment | Organism |
---|---|---|
thioredoxin reductase | - |
Homo sapiens |