Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | - |
- |
- |
Source Tissue | Comment | Organism | Textmining |
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lens | glutathione reductase plays a key role in maintaining thiol groups in the lens, and its activity decreases with aging and cataract formation. The glutathione reductase activity in the cortex and nucleus of the cataractous lenses is significantly lower than that of the aged clear lenses. The highest activity in the cortex is observed in the clear aged lenses. The combination of thioredoxin and thioredoxin reductase revives the activity of glutathione reductase from both the cortex and nucleus of aged clear lenses. In cataract lenses (grade II and grade IV), there is a statistically significant recovery of glutathione reductase activity in the cortex, but not in the nucleus. No recovery is observed when thioredoxin or thioredoxin reductase are used separately. alpha-Crystallin successfully revives glutathione reductase activity in the cortex of cataract grade II lenses, but not in the nucleus. The combination of alpha-crystallin and thioredoxin/thioredoxin reductase gives a further increase of activity. Thioltransferase alone revives some of the glutathione reductase activity but together with the thioredoxin/thioredoxin reductase system gives no statistically significant enhancement of glutathione reductase activity | Homo sapiens | - |
lens | the combination of thioredioxin and thioredoxin reductase revives the activity of glutathione reductase from both the cortex and nucleus of aged clear lenses. In cataract lenses (grade II and grade IV) there is a statistically significant recovery of glutathione reductase activity in the cortex, but not in the nucleus. alpha-Crystallin successfully revives glutathione reductase activity in the cortex of cataract grade II lenses, but not in the nucleus. the combination of alpha-crystallin and thioredoxin/thioredoxin reductase gives a further increase in activity. Both disulfide bond formation and protein unfolding are responsible for glutathione inactivation | Homo sapiens | - |
Synonyms | Comment | Organism |
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glutathione reductase | - |
Homo sapiens |