Lysyl oxidase (LOX) is a copper-dependent extracellular enzyme responsible for post-translational oxidative deamination of peptidyl lysine residues in collagen and elastin precursors 1, catalyzing cross-linking of structural extracellular matrix (ECM) components essential for tissue integrity 2. Beyond its canonical ECM cross-linking role, LOX mediates ECM mechanical stiffness that activates the mechanosensitive Piezo1 ion channel, triggering ferroptotic neuronal death in hypoxic-ischemic brain damage 3. LOX contributes to multiple pathological processes: it promotes chemoresistance in triple-negative breast cancer by facilitating collagen cross-linking and fibronectin assembly, thereby reducing drug penetration and activating FAK/Src signaling 4, and enhances chondrosarcoma metastasis through miR-26b-5p suppression 5. LOX expression is elevated during fibrosis progression across cardiac, renal, pulmonary, and liver tissues, and LOX inhibition has shown promise in preclinical fibrosis models 2. Disease associations include familial thoracic aortic aneurysm. Therapeutically, LOX inhibition represents a target for fibrosis reversal, chemoresistance overcome, and neuroprotection, with traumatic acid identified as a novel LOX inhibitor 3.