Thiol antioxidant system
Thioredoxin and thioredoxin reductase
Also searched as Thioredoxin and thioredoxin reductase.
Redundancy that is not redundant: it handles protein disulphides and supplies ribonucleotide reductase, which glutathione does not do. Thioredoxin reductase is a selenoprotein, so selenium status governs both systems.
In depth
Thioredoxin and thioredoxin reductase — a redox network parallel to glutathione.
What drives it
Antioxidant defense increases it.
NRF2 induces the thioredoxin system. Carried by the intermediary-metabolism, micronutrient and redox reviews. doi 10.3390/nu18132141 · PMC9967593
Selenium proteins increases it.
Thioredoxin reductase is a selenoprotein - selenium governs both reducing systems. Carried by the intermediary-metabolism, micronutrient and redox reviews. doi 10.3390/nu18132141 · PMC9967593
Reducing power supply increases it.
NADPH-dependent, like glutathione regeneration. Carried by the intermediary-metabolism, micronutrient and redox reviews. doi 10.3390/nu18132141 · PMC9967593
What it drives
It reduces Oxidative stress.
Redundancy that is not redundant - it handles protein disulphides and supplies ribonucleotide reductase, which glutathione does not do. Carried by the intermediary-metabolism, micronutrient and redox reviews. doi 10.3390/nu18132141 · PMC9967593
Blends that modulate it
Each blend page names this pathway and carries the study behind its claim.
See it on the map
Open the causal map to follow this pathway upstream and downstream, arrow by arrow, each with its study.