GLRX encodes glutaredoxin, a small thiol-oxidoreductase enzyme that catalyzes glutathione-dependent disulfide reduction reactions in partnership with glutathione reductase and NADPH. The protein removes S-glutathionyl adducts from cysteine residues on target proteins, thereby regulating reversible redox signaling without direct antioxidant activity. GLRX modulates diverse cellular processes through protein deglutathionylation. It regulates hepatic lipid metabolism by controlling sirtuin-1 activity, with GLRX-deficient mice developing spontaneous fatty liver disease and dyslipidemia 1. In vascular biology, GLRX overexpression inhibits endothelial cell migration and neovascularization via the Wnt5a/sFlt-1 pathway 2. Recent studies identify GLRX as a negative regulator in lymphangioleiomyomatosis, where it promotes cell proliferation through COX2/PGE2/ERK signaling by reducing S-glutathionylation of NF-κB 3. In pulmonary fibrosis, increased collagen S-glutathionylation and GLRX expression correlate with disease severity and fibroblast activation 4. GLRX variants are prioritized at genome-wide association loci for aortic aneurysm, showing differential expression in vascular smooth muscle cells of diseased tissue 5. GLRX is highly enriched in high-grade gliomas and associated with adverse prognosis and tumor immune microenvironment characteristics 6. Given its tissue-specific roles in pathological conditions including liver disease, lung fibrosis, and vascular dysfunction, GLRX represents a potential therapeutic target through redox-modulating interventions.