Thioredoxiinijärjestelmät

Thioredoxin is a small, redox-active protein found in all living organisms. It plays a crucial role in cellular metabolism and defense against oxidative stress. Thioredoxin functions by reducing disulfide bonds, which are covalent bonds between sulfur atoms in cysteine residues. This reduction is essential for the proper functioning of many enzymes and proteins that contain disulfide bonds.

The thioredoxin system consists of thioredoxin itself, thioredoxin reductase, and NADPH. Thioredoxin reductase, a flavoprotein, uses NADPH as a reducing agent to regenerate the reduced form of thioredoxin. This cyclical process allows thioredoxin to continuously participate in redox reactions.

In addition to its role in protein disulfide reduction, thioredoxin is involved in a variety of cellular processes. These include DNA synthesis, cell proliferation, apoptosis, and immune responses. It can also act as a signaling molecule, interacting with transcription factors and other regulatory proteins. Due to its involvement in such fundamental cellular activities, dysregulation of the thioredoxin system has been implicated in various diseases, including cancer, neurodegenerative disorders, and inflammatory conditions. Research continues to explore the multifaceted roles of thioredoxin and its potential as a therapeutic target.