Back

Thioredoxin Reductase 1 inhibition triggers ferroptosis in KRAS-independent lung cancers

Andreani, C.; Bartolacci, C.; Melegari, M.; Sargentoni, N.; Luciani, L.; Marucci, A.; Galeazzi, R.; DeNicola, G. M.; Kilgore, J.; Williams, N. S.; Berto, S.; Gaetani, M.; Pattabhi, P.; Osman, S. S.; Mansour, A. T.; Pucciarelli, S.; Galassi, R.; Scaglioni, P. P.

2025-07-30 cancer biology
10.1101/2025.07.25.666783 bioRxiv
Show abstract

Lung cancers that harbor wild type KRAS (KRAS-WT) represent a molecularly diverse subset of tumors that often lack targeted therapeutic options. Using synthesized gold(I)-based inhibitors, a multi-omics approach, and functional validation, we identified Thioredoxin reductase 1 (TXNRD1), encoding as a selective vulnerability in KRAS-WT and oncogenic KRAS mutant (KM)-independent lung cancer (LC). Mechanistically, TRXR1 blockade induces ferroptosis through glutathione depletion, lipid reactive oxygen species (ROS) accumulation, and HMOX1-dependent iron overload in KRAS-WT LC both in vitro and in vivo. Furthermore, while KM LC cells are intrinsically resistant to TRXR1 inhibition, KMLC cells that acquire resistance to KRAS inhibitors (KRASi) undergo a redox shift that renders them sensitive to TRXR1 inhibition, uncovering a potential novel therapeutic vulnerability in KRASi-refractory tumors. These findings establish TRXR1 as a targetable redox checkpoint in KRAS-WT and KRASi-resistant lung cancers and support further development of TRXR1 inhibitors.

Matching journals

The top 6 journals account for 50% of the predicted probability mass.

50% of probability mass above

"Similar papers" are the closest papers from that journal in the model's embedding space. They show what the match is built on, but the ranking comes mostly from a classifier over the whole training set, not from these examples alone.