Literature summary for 1.8.1.9 extracted from

Lemarechal, H.; Anract, P.; Beaudeux, J.L.; Bonnefont-Rousselot, D.; Ekindjian, O.G.; Borderie, D.
Impairment of thioredoxin reductase activity by oxidative stress in human rheumatoid synoviocytes (2007), Free Radic. Res., 41, 688-698.

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Inhibitors

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

Organism	UniProt	Comment	Textmining
Homo sapiens	-	-	-

Source Tissue

Source Tissue	Comment	Organism	Textmining
synoviocyte	thioredoxin reductase activity in rheumatoid arthritis cells is significantly higher than in osteoarthritis cells	Homo sapiens	-

Synonyms

Synonyms	Comment	Organism
thioredoxin reductase	-	Homo sapiens

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Release 2023.1 (January 2023)