ACSL4 is a long-chain fatty acyl-CoA synthetase that catalyzes conversion of long-chain polyunsaturated fatty acids (PUFAs), particularly arachidonate and eicosapentaenoate, to their active acyl-CoA forms 1. This activation is critical for both lipid biosynthesis and beta-oxidation 12. ACSL4's primary pathophysiological role centers on ferroptosis regulation: it generates lipid-peroxidation substrates by activating PUFAs, particularly arachidonate, thereby promoting ferroptosis execution 34. ACSL4 remodels cellular membrane composition by enriching membranes with polyunsaturated omega-6 fatty acids, determining ferroptosis sensitivity 3. Beyond ferroptosis, ACSL4 modulates glucose-stimulated insulin secretion and prostaglandin E2 secretion 1. Clinically, ACSL4 has emerged as significant in multiple pathologies: it promotes metastatic extravasation in cancer by enhancing membrane fluidity and invasiveness 5, drives ferroptotic cardiomyocyte injury in doxorubicin cardiotoxicity 6, mediates sepsis-associated lung injury through lactate-induced ferroptosis 7, and contributes to ischemic stroke neuronal death 8 and hypertension-associated chrX kidney disease 9. ACSL4 inhibition represents a therapeutic target for ferroptosis-related diseases and cancer progression.