Thioredoxin 1 (TXN) (TXN)

Thioredoxin 1 (TXN) is a small, 12-kDa oxidoreductase that plays a pivotal role in maintaining cellular redox homeostasis and protecting cells from oxidative stress-induced apoptosis [1, 3]. It functions by reducing protein disulfides through its conserved Cys-Gly-Pro-Cys active site, subsequently being regenerated by thioredoxin reductase (TrxR) and NADPH [2, 5]. In many human cancers, TXN is overexpressed at both the mRNA and protein levels, which correlates with increased cell proliferation, decreased apoptosis, and poor prognosis [3, 5]. This overexpression allows tumor cells to survive in high-ROS environments and resist chemotherapy [4]. Therapeutic targeting of the thioredoxin system has primarily focused on small molecule inhibitors like PX-12, which irreversibly binds to TXN, and Motexafin gadolinium, which acts as a redox mediator [4]. While mRNA-targeted approaches such as antisense oligonucleotides and siRNA have demonstrated efficacy in preclinical models by reducing TXN expression and inhibiting angiogenesis, they have not yet reached widespread clinical use [3].

Other names

ThioredoxinTRXTRX1Adult T-cell leukemia-derived factorADFSurface-associated sulphydryl-disulphide exchange proteinSASPThioredoxin 1 mRNA

Inhibition of the thioredoxin redox system, leading to increased reactive oxygen species (ROS) levels and induction of apoptosis.